Ticket #9113: 2bbv.cif

data_2BBV
# 
_entry.id   2BBV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2BBV         
RCSB  PRV004       
WWPDB D_1000177816 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2BBV 
_pdbx_database_status.recvd_initial_deposition_date   1994-06-06 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    NDB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Wery, J.-P.'   1 
'Reddy, V.S.'   2 
'Hosur, M.V.'   3 
'Johnson, J.E.' 4 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'The refined three-dimensional structure of an insect virus at 2.8 A resolution.'               J.Mol.Biol. 235 565 586 
1994 JMOBAK UK 0022-2836 0070 ? 8289282 10.1006/jmbi.1994.1014 
1       'Ordered Duplex RNA Controls Capsid Architecture in an Icosahedral Animal Virus'                Nature      361 176 ?   
1993 NATUAS UK 0028-0836 0006 ? ?       ?                      
2       'Structural Homology Among Four Nodaviruses as Deduced by Sequencing and X-Ray Crystallography' J.Mol.Biol. 214 423 ?   
1990 JMOBAK UK 0022-2836 0070 ? ?       ?                      
3       'Structure of an Insect Virus at 3.0 Angstroms Resolution'                                      Proteins    2   167 ?   
1987 PSFGEY US 0887-3585 0867 ? ?       ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Wery, J.P.'      1  
primary 'Reddy, V.S.'     2  
primary 'Hosur, M.V.'     3  
primary 'Johnson, J.E.'   4  
1       'Fisher, A.J.'    5  
1       'Johnson, J.E.'   6  
2       'Kaesberg, P.'    7  
2       'Dasgupta, R.'    8  
2       'Sgro, J.-Y.'     9  
2       'Wery, J.-P.'     10 
2       'Selling, B.H.'   11 
2       'Hosur, M.V.'     12 
2       'Johnson, J.E.'   13 
3       'Hosur, M.V.'     14 
3       'Schmidt, T.'     15 
3       'Tucker, R.C.'    16 
3       'Johnson, J.E.'   17 
3       'Gallagher, T.M.' 18 
3       'Selling, B.H.'   19 
3       'Rueckert, R.R.'  20 
# 
_cell.entry_id           2BBV 
_cell.length_a           362.000 
_cell.length_b           362.000 
_cell.length_c           362.000 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              360 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2BBV 
_symmetry.space_group_name_H-M             'P 42 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                208 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     syn 
;RNA (5'-R(*UP*CP*UP*UP*AP*UP*AP*UP*CP*U)-3')
;
3060.812  1   ? ? ? ? 
2 polymer     nat 'PROTEIN (BLACK BEETLE VIRUS CAPSID PROTEIN)'  39436.656 3   ? ? ? ? 
3 polymer     nat 'PROTEIN (BLACK BEETLE VIRUS CAPSID PROTEIN)'  4459.174  3   ? ? ? ? 
4 non-polymer syn 'CALCIUM ION'                                  40.078    5   ? ? ? ? 
5 water       nat water                                          18.015    208 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 polyribonucleotide no no UCUUAUAUCU UCUUAUAUCU N     ? 
2 'polypeptide(L)'   no no 
;MVRNNNRRRQRTQRIVTTTTQTAPVPQQNVPKQPRRRRNRARRNRRQGRAMNMGALTRLSQPGLAFLKCAFAPPDFNTDP
GKGIPDRFEGKVVTRKDVLNQSINFTANRDTFILIAPTPGVAYWVADVPAGTFPISTTTFNAVNFPGFNSMFGNAAASRS
DQVSSFRYASMNVGIYPTSNLMQFAGSITVWKCPVKLSNVQFPVATTPATSALVHTLVGLDGVLAVGPDNFSESFIKGVF
SQSVCNEPDFEFSDILEGIQTLPPANVTVATSGQPFNLAAGAEAVSGIVGWGNMDTIVIRVSAPTGAVNSAILKTWACLE
YRPNPNAMLYQFGHDSPPCDEVALQEYRTVARSLPVAVIAAQN
;
;MVRNNNRRRQRTQRIVTTTTQTAPVPQQNVPKQPRRRRNRARRNRRQGRAMNMGALTRLSQPGLAFLKCAFAPPDFNTDP
GKGIPDRFEGKVVTRKDVLNQSINFTANRDTFILIAPTPGVAYWVADVPAGTFPISTTTFNAVNFPGFNSMFGNAAASRS
DQVSSFRYASMNVGIYPTSNLMQFAGSITVWKCPVKLSNVQFPVATTPATSALVHTLVGLDGVLAVGPDNFSESFIKGVF
SQSVCNEPDFEFSDILEGIQTLPPANVTVATSGQPFNLAAGAEAVSGIVGWGNMDTIVIRVSAPTGAVNSAILKTWACLE
YRPNPNAMLYQFGHDSPPCDEVALQEYRTVARSLPVAVIAAQN
;
A,B,C ? 
3 'polypeptide(L)'   no no ASMWERVKSIIKSSLAMASNVPGPIGIAASGLSGLSALFEGFGF ASMWERVKSIIKSSLAMASNVPGPIGIAASGLSGLSALFEGFGF D,E,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   U   n 
1 2   C   n 
1 3   U   n 
1 4   U   n 
1 5   A   n 
1 6   U   n 
1 7   A   n 
1 8   U   n 
1 9   C   n 
1 10  U   n 
2 1   MET n 
2 2   VAL n 
2 3   ARG n 
2 4   ASN n 
2 5   ASN n 
2 6   ASN n 
2 7   ARG n 
2 8   ARG n 
2 9   ARG n 
2 10  GLN n 
2 11  ARG n 
2 12  THR n 
2 13  GLN n 
2 14  ARG n 
2 15  ILE n 
2 16  VAL n 
2 17  THR n 
2 18  THR n 
2 19  THR n 
2 20  THR n 
2 21  GLN n 
2 22  THR n 
2 23  ALA n 
2 24  PRO n 
2 25  VAL n 
2 26  PRO n 
2 27  GLN n 
2 28  GLN n 
2 29  ASN n 
2 30  VAL n 
2 31  PRO n 
2 32  LYS n 
2 33  GLN n 
2 34  PRO n 
2 35  ARG n 
2 36  ARG n 
2 37  ARG n 
2 38  ARG n 
2 39  ASN n 
2 40  ARG n 
2 41  ALA n 
2 42  ARG n 
2 43  ARG n 
2 44  ASN n 
2 45  ARG n 
2 46  ARG n 
2 47  GLN n 
2 48  GLY n 
2 49  ARG n 
2 50  ALA n 
2 51  MET n 
2 52  ASN n 
2 53  MET n 
2 54  GLY n 
2 55  ALA n 
2 56  LEU n 
2 57  THR n 
2 58  ARG n 
2 59  LEU n 
2 60  SER n 
2 61  GLN n 
2 62  PRO n 
2 63  GLY n 
2 64  LEU n 
2 65  ALA n 
2 66  PHE n 
2 67  LEU n 
2 68  LYS n 
2 69  CYS n 
2 70  ALA n 
2 71  PHE n 
2 72  ALA n 
2 73  PRO n 
2 74  PRO n 
2 75  ASP n 
2 76  PHE n 
2 77  ASN n 
2 78  THR n 
2 79  ASP n 
2 80  PRO n 
2 81  GLY n 
2 82  LYS n 
2 83  GLY n 
2 84  ILE n 
2 85  PRO n 
2 86  ASP n 
2 87  ARG n 
2 88  PHE n 
2 89  GLU n 
2 90  GLY n 
2 91  LYS n 
2 92  VAL n 
2 93  VAL n 
2 94  THR n 
2 95  ARG n 
2 96  LYS n 
2 97  ASP n 
2 98  VAL n 
2 99  LEU n 
2 100 ASN n 
2 101 GLN n 
2 102 SER n 
2 103 ILE n 
2 104 ASN n 
2 105 PHE n 
2 106 THR n 
2 107 ALA n 
2 108 ASN n 
2 109 ARG n 
2 110 ASP n 
2 111 THR n 
2 112 PHE n 
2 113 ILE n 
2 114 LEU n 
2 115 ILE n 
2 116 ALA n 
2 117 PRO n 
2 118 THR n 
2 119 PRO n 
2 120 GLY n 
2 121 VAL n 
2 122 ALA n 
2 123 TYR n 
2 124 TRP n 
2 125 VAL n 
2 126 ALA n 
2 127 ASP n 
2 128 VAL n 
2 129 PRO n 
2 130 ALA n 
2 131 GLY n 
2 132 THR n 
2 133 PHE n 
2 134 PRO n 
2 135 ILE n 
2 136 SER n 
2 137 THR n 
2 138 THR n 
2 139 THR n 
2 140 PHE n 
2 141 ASN n 
2 142 ALA n 
2 143 VAL n 
2 144 ASN n 
2 145 PHE n 
2 146 PRO n 
2 147 GLY n 
2 148 PHE n 
2 149 ASN n 
2 150 SER n 
2 151 MET n 
2 152 PHE n 
2 153 GLY n 
2 154 ASN n 
2 155 ALA n 
2 156 ALA n 
2 157 ALA n 
2 158 SER n 
2 159 ARG n 
2 160 SER n 
2 161 ASP n 
2 162 GLN n 
2 163 VAL n 
2 164 SER n 
2 165 SER n 
2 166 PHE n 
2 167 ARG n 
2 168 TYR n 
2 169 ALA n 
2 170 SER n 
2 171 MET n 
2 172 ASN n 
2 173 VAL n 
2 174 GLY n 
2 175 ILE n 
2 176 TYR n 
2 177 PRO n 
2 178 THR n 
2 179 SER n 
2 180 ASN n 
2 181 LEU n 
2 182 MET n 
2 183 GLN n 
2 184 PHE n 
2 185 ALA n 
2 186 GLY n 
2 187 SER n 
2 188 ILE n 
2 189 THR n 
2 190 VAL n 
2 191 TRP n 
2 192 LYS n 
2 193 CYS n 
2 194 PRO n 
2 195 VAL n 
2 196 LYS n 
2 197 LEU n 
2 198 SER n 
2 199 ASN n 
2 200 VAL n 
2 201 GLN n 
2 202 PHE n 
2 203 PRO n 
2 204 VAL n 
2 205 ALA n 
2 206 THR n 
2 207 THR n 
2 208 PRO n 
2 209 ALA n 
2 210 THR n 
2 211 SER n 
2 212 ALA n 
2 213 LEU n 
2 214 VAL n 
2 215 HIS n 
2 216 THR n 
2 217 LEU n 
2 218 VAL n 
2 219 GLY n 
2 220 LEU n 
2 221 ASP n 
2 222 GLY n 
2 223 VAL n 
2 224 LEU n 
2 225 ALA n 
2 226 VAL n 
2 227 GLY n 
2 228 PRO n 
2 229 ASP n 
2 230 ASN n 
2 231 PHE n 
2 232 SER n 
2 233 GLU n 
2 234 SER n 
2 235 PHE n 
2 236 ILE n 
2 237 LYS n 
2 238 GLY n 
2 239 VAL n 
2 240 PHE n 
2 241 SER n 
2 242 GLN n 
2 243 SER n 
2 244 VAL n 
2 245 CYS n 
2 246 ASN n 
2 247 GLU n 
2 248 PRO n 
2 249 ASP n 
2 250 PHE n 
2 251 GLU n 
2 252 PHE n 
2 253 SER n 
2 254 ASP n 
2 255 ILE n 
2 256 LEU n 
2 257 GLU n 
2 258 GLY n 
2 259 ILE n 
2 260 GLN n 
2 261 THR n 
2 262 LEU n 
2 263 PRO n 
2 264 PRO n 
2 265 ALA n 
2 266 ASN n 
2 267 VAL n 
2 268 THR n 
2 269 VAL n 
2 270 ALA n 
2 271 THR n 
2 272 SER n 
2 273 GLY n 
2 274 GLN n 
2 275 PRO n 
2 276 PHE n 
2 277 ASN n 
2 278 LEU n 
2 279 ALA n 
2 280 ALA n 
2 281 GLY n 
2 282 ALA n 
2 283 GLU n 
2 284 ALA n 
2 285 VAL n 
2 286 SER n 
2 287 GLY n 
2 288 ILE n 
2 289 VAL n 
2 290 GLY n 
2 291 TRP n 
2 292 GLY n 
2 293 ASN n 
2 294 MET n 
2 295 ASP n 
2 296 THR n 
2 297 ILE n 
2 298 VAL n 
2 299 ILE n 
2 300 ARG n 
2 301 VAL n 
2 302 SER n 
2 303 ALA n 
2 304 PRO n 
2 305 THR n 
2 306 GLY n 
2 307 ALA n 
2 308 VAL n 
2 309 ASN n 
2 310 SER n 
2 311 ALA n 
2 312 ILE n 
2 313 LEU n 
2 314 LYS n 
2 315 THR n 
2 316 TRP n 
2 317 ALA n 
2 318 CYS n 
2 319 LEU n 
2 320 GLU n 
2 321 TYR n 
2 322 ARG n 
2 323 PRO n 
2 324 ASN n 
2 325 PRO n 
2 326 ASN n 
2 327 ALA n 
2 328 MET n 
2 329 LEU n 
2 330 TYR n 
2 331 GLN n 
2 332 PHE n 
2 333 GLY n 
2 334 HIS n 
2 335 ASP n 
2 336 SER n 
2 337 PRO n 
2 338 PRO n 
2 339 CYS n 
2 340 ASP n 
2 341 GLU n 
2 342 VAL n 
2 343 ALA n 
2 344 LEU n 
2 345 GLN n 
2 346 GLU n 
2 347 TYR n 
2 348 ARG n 
2 349 THR n 
2 350 VAL n 
2 351 ALA n 
2 352 ARG n 
2 353 SER n 
2 354 LEU n 
2 355 PRO n 
2 356 VAL n 
2 357 ALA n 
2 358 VAL n 
2 359 ILE n 
2 360 ALA n 
2 361 ALA n 
2 362 GLN n 
2 363 ASN n 
3 1   ALA n 
3 2   SER n 
3 3   MET n 
3 4   TRP n 
3 5   GLU n 
3 6   ARG n 
3 7   VAL n 
3 8   LYS n 
3 9   SER n 
3 10  ILE n 
3 11  ILE n 
3 12  LYS n 
3 13  SER n 
3 14  SER n 
3 15  LEU n 
3 16  ALA n 
3 17  MET n 
3 18  ALA n 
3 19  SER n 
3 20  ASN n 
3 21  VAL n 
3 22  PRO n 
3 23  GLY n 
3 24  PRO n 
3 25  ILE n 
3 26  GLY n 
3 27  ILE n 
3 28  ALA n 
3 29  ALA n 
3 30  SER n 
3 31  GLY n 
3 32  LEU n 
3 33  SER n 
3 34  GLY n 
3 35  LEU n 
3 36  SER n 
3 37  ALA n 
3 38  LEU n 
3 39  PHE n 
3 40  GLU n 
3 41  GLY n 
3 42  PHE n 
3 43  GLY n 
3 44  PHE n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
2 1 sample ? ? ? 'Black beetle virus' 12285 Alphanodavirus ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 'GROWN IN DROSOPHILA MELANOGASTER' 
3 1 sample ? ? ? 'Black beetle virus' 12285 Alphanodavirus ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 'GROWN IN DROSOPHILA MELANOGASTER' 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
_struct_ref.pdbx_seq_one_letter_code 
1 UNP COAT_BBV P04329 2 1   ? ? 
2 UNP COAT_BBV P04329 3 364 ? ? 
3 PDB 2BBV     2BBV   1 ?   ? ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2BBV A 1 ? 363 ? P04329 1   ? 363 ? 1   363 
2 2 2BBV D 1 ? 44  ? P04329 364 ? 407 ? 364 407 
3 1 2BBV B 1 ? 363 ? P04329 1   ? 363 ? 1   363 
4 2 2BBV E 1 ? 44  ? P04329 364 ? 407 ? 364 407 
5 1 2BBV C 1 ? 363 ? P04329 1   ? 363 ? 1   363 
6 2 2BBV F 1 ? 44  ? P04329 364 ? 407 ? 364 407 
7 3 2BBV N 1 ? 10  ? 2BBV   1   ? 10  ? 1   10  
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A   'RNA linking'       y "ADENOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O7 P' 347.221 
ALA 'L-peptide linking' y ALANINE                      ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                     ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                   ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'              ? 'C4 H7 N O4'      133.103 
C   'RNA linking'       y "CYTIDINE-5'-MONOPHOSPHATE"  ? 'C9 H14 N3 O8 P'  323.197 
CA  non-polymer         . 'CALCIUM ION'                ? 'Ca 2'            40.078  
CYS 'L-peptide linking' y CYSTEINE                     ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                    ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'              ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                      ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                    ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                        ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                   ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                      ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                       ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                   ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                      ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                       ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                    ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                   ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                     ? 'C9 H11 N O3'     181.189 
U   'RNA linking'       y "URIDINE-5'-MONOPHOSPHATE"   ? 'C9 H13 N2 O9 P'  324.181 
VAL 'L-peptide linking' y VALINE                       ? 'C5 H11 N O2'     117.146 
# 
_exptl.entry_id          2BBV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   ? 
_exptl_crystal.density_Matthews      ? 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 2BBV 
_refine.ls_number_reflns_obs                     112000 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          4.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             6.000 
_refine.ls_d_res_high                            2.800 
_refine.ls_percent_reflns_obs                    67.500 
_refine.ls_R_factor_obs                          0.221 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.221 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;THE ENDS OF THE THREE SUBUNITS (A, B AND C) AND ENDS OF
THEIR CLEAVED PRODUCTS (BETA AND GAMMA) AND THE ORDERED
PEPTIDE_ARM MIGHT HAVE UNACCEPTABLE STEREOCHEMISTRY.  THESE
RESIDUES ARE A 56, A 363, D 364, D 379, B 56, B 363, E 364,
E 379, C 20, C 31, C 55, C 363, F 364, AND F 379.
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7403 
_refine_hist.pdbx_number_atoms_nucleic_acid   201 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.number_atoms_solvent             208 
_refine_hist.number_atoms_total               7817 
_refine_hist.d_res_high                       2.800 
_refine_hist.d_res_low                        6.000 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d                ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             0.800 1.000 ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            1.300 1.500 ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             1.900 1.500 ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            2.700 2.000 ? ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given    ? 1.00000000  0.00000000  0.00000000  0.00000000  1.00000000  0.00000000 0.00000000  0.00000000 1.00000000 0.00000 
0.00000 0.00000 
2 generate ? 0.30901699  -0.80901699 0.50000000  0.80901699  0.50000000  0.30901699 -0.50000000 0.30901699 0.80901699 0.00000 
0.00000 0.00000 
3 generate ? -0.80901699 -0.50000000 0.30901699  0.50000000  -0.30901699 0.80901699 -0.30901699 0.80901699 0.50000000 0.00000 
0.00000 0.00000 
4 generate ? -0.80901699 0.50000000  -0.30901699 -0.50000000 -0.30901699 0.80901699 0.30901699  0.80901699 0.50000000 0.00000 
0.00000 0.00000 
5 generate ? 0.30901699  0.80901699  -0.50000000 -0.80901699 0.50000000  0.30901699 0.50000000  0.30901699 0.80901699 0.00000 
0.00000 0.00000 
# 
_struct.entry_id                  2BBV 
_struct.title                     'THE REFINED THREE-DIMENSIONAL STRUCTURE OF AN INSECT VIRUS AT 2.8 ANGSTROMS RESOLUTION' 
_struct.pdbx_descriptor           'BLACK BEETLE VIRUS CAPSID PROTEIN/RNA COMPLEX' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2BBV 
_struct_keywords.pdbx_keywords   Virus/RNA 
_struct_keywords.text            'PROTEIN-RNA COMPLEX, DOUBLE HELIX, Icosahedral virus, Virus-RNA COMPLEX' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               
;BBV HAS AN ICOSAHEDRAL PENTAMER IN THE CRYSTALLOGRAPHIC
ASYMMETRIC UNIT.  THIS FIVE-FOLD NON-CRYSTALLOGRAPHIC
SYMMETRY WAS USED TO AVERAGE THE ELECTRON DENSITY MAP IN
THE PHASE REFINEMENT PROCEDURE.  THE FOUR TRANSFORMATIONS
PRESENTED ON *MTRIX* RECORDS BELOW WILL GENERATE THE
ADDITIONAL 12 OF THE 15 SUBUNITS COMPRISING THE PENTAMERIC
UNIT WHEN APPLIED TO THE THREE SUBUNITS PRESENTED IN THIS
ENTRY.
;
_struct_biol.pdbx_parent_biol_id   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  A1  GLN B 61  ? PRO B 73  ? GLN A 61  PRO A 73  1 ? 13 
HELX_P HELX_P2  SA1 GLY B 147 ? MET B 151 ? GLY A 147 MET A 151 5 ? 5  
HELX_P HELX_P3  SA2 GLY B 219 ? VAL B 223 ? GLY A 219 VAL A 223 5 ? 5  
HELX_P HELX_P4  SA3 LEU B 329 ? GLY B 333 ? LEU A 329 GLY A 333 5 ? 5  
HELX_P HELX_P5  A2  GLU B 341 ? SER B 353 ? GLU A 341 SER A 353 1 ? 13 
HELX_P HELX_P6  A3  SER C 2   ? ALA C 16  ? SER D 365 ALA D 379 1 ? 15 
HELX_P HELX_P7  B1  GLN D 61  ? PRO D 73  ? GLN B 61  PRO B 73  1 ? 13 
HELX_P HELX_P8  SB1 GLY D 147 ? MET D 151 ? GLY B 147 MET B 151 5 ? 5  
HELX_P HELX_P9  SB2 GLY D 219 ? VAL D 223 ? GLY B 219 VAL B 223 5 ? 5  
HELX_P HELX_P10 SB3 LEU D 329 ? GLY D 333 ? LEU B 329 GLY B 333 5 ? 5  
HELX_P HELX_P11 B2  GLU D 341 ? SER D 353 ? GLU B 341 SER B 353 1 ? 13 
HELX_P HELX_P12 B3  SER E 2   ? ALA E 16  ? SER E 365 ALA E 379 1 ? 15 
HELX_P HELX_P13 C1  GLN F 61  ? PRO F 73  ? GLN C 61  PRO C 73  1 ? 13 
HELX_P HELX_P14 SC1 GLY F 147 ? MET F 151 ? GLY C 147 MET C 151 5 ? 5  
HELX_P HELX_P15 SC2 GLY F 219 ? VAL F 223 ? GLY C 219 VAL C 223 5 ? 5  
HELX_P HELX_P16 SC3 LEU F 329 ? GLY F 333 ? LEU C 329 GLY C 333 5 ? 5  
HELX_P HELX_P17 C2  GLU F 341 ? SER F 353 ? GLU C 341 SER C 353 1 ? 13 
HELX_P HELX_P18 C3  SER G 2   ? ALA G 16  ? SER F 365 ALA F 379 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ? ? H CA . CA ? ? ? 1_555 B GLY 273 O   ? ? A CA 364 A GLY 273 1_555 ? ? ? ? ? ? ?             2.298 ? 
metalc2  metalc ? ? H CA . CA ? ? ? 1_555 B ASP 221 OD2 ? ? A CA 364 A ASP 221 1_555 ? ? ? ? ? ? ?             2.413 ? 
metalc3  metalc ? ? H CA . CA ? ? ? 1_555 D ASP 161 OD1 ? ? A CA 364 B ASP 161 1_555 ? ? ? ? ? ? ?             2.699 ? 
metalc4  metalc ? ? I CA . CA ? ? ? 1_555 F GLU 251 OE1 ? ? A CA 365 C GLU 251 1_555 ? ? ? ? ? ? ?             2.709 ? 
metalc5  metalc ? ? I CA . CA ? ? ? 1_555 B GLU 251 OE1 ? ? A CA 365 A GLU 251 1_555 ? ? ? ? ? ? ?             2.593 ? 
metalc6  metalc ? ? I CA . CA ? ? ? 1_555 D GLU 251 OE1 ? ? A CA 365 B GLU 251 1_555 ? ? ? ? ? ? ?             3.114 ? 
metalc7  metalc ? ? J CA . CA ? ? ? 1_555 D ASP 221 OD2 ? ? B CA 364 B ASP 221 1_555 ? ? ? ? ? ? ?             2.284 ? 
metalc8  metalc ? ? J CA . CA ? ? ? 1_555 F ASP 161 OD1 ? ? B CA 364 C ASP 161 1_555 ? ? ? ? ? ? ?             2.455 ? 
metalc9  metalc ? ? J CA . CA ? ? ? 1_555 D GLY 273 O   ? ? B CA 364 B GLY 273 1_555 ? ? ? ? ? ? ?             2.610 ? 
metalc10 metalc ? ? K CA . CA ? ? ? 1_555 F GLY 273 O   ? ? C CA 364 C GLY 273 1_555 ? ? ? ? ? ? ?             2.166 ? 
metalc11 metalc ? ? K CA . CA ? ? ? 1_555 F ASP 221 OD1 ? ? C CA 364 C ASP 221 1_555 ? ? ? ? ? ? ?             2.992 ? 
metalc12 metalc ? ? L CA . CA ? ? ? 1_555 F ASP 249 OD1 ? ? C CA 365 C ASP 249 1_555 ? ? ? ? ? ? ?             3.004 ? 
metalc13 metalc ? ? L CA . CA ? ? ? 1_555 F ASP 249 OD2 ? ? C CA 365 C ASP 249 1_555 ? ? ? ? ? ? ?             2.914 ? 
metalc14 metalc ? ? L CA . CA ? ? ? 1_555 F GLU 251 OE2 ? ? C CA 365 C GLU 251 1_555 ? ? ? ? ? ? ?             2.750 ? 
metalc15 metalc ? ? L CA . CA ? ? ? 1_555 B ASP 249 OD2 ? ? C CA 365 A ASP 249 1_555 ? ? ? ? ? ? ?             2.288 ? 
metalc16 metalc ? ? L CA . CA ? ? ? 1_555 D ASP 249 OD2 ? ? C CA 365 B ASP 249 1_555 ? ? ? ? ? ? ?             2.781 ? 
hydrog1  hydrog ? ? A U  3 O4 ? ? ? 1_555 A U   8   N3  ? ? N U  3   N U   8   2_555 ? ? ? ? ? ? 'U-U MISPAIR' ?     ? 
hydrog2  hydrog ? ? A U  4 N3 ? ? ? 1_555 A A   7   N1  ? ? N U  4   N A   7   2_555 ? ? ? ? ? ? WATSON-CRICK  ?     ? 
hydrog3  hydrog ? ? A U  4 O4 ? ? ? 1_555 A A   7   N6  ? ? N U  4   N A   7   2_555 ? ? ? ? ? ? WATSON-CRICK  ?     ? 
hydrog4  hydrog ? ? A A  5 N6 ? ? ? 1_555 A U   6   O4  ? ? N A  5   N U   6   2_555 ? ? ? ? ? ? 'A-U PAIR'    ?     ? 
hydrog5  hydrog ? ? A U  6 O4 ? ? ? 1_555 A A   5   N6  ? ? N U  6   N A   5   2_555 ? ? ? ? ? ? 'U-A PAIR'    ?     ? 
hydrog6  hydrog ? ? A A  7 N1 ? ? ? 1_555 A U   4   N3  ? ? N A  7   N U   4   2_555 ? ? ? ? ? ? WATSON-CRICK  ?     ? 
hydrog7  hydrog ? ? A A  7 N6 ? ? ? 1_555 A U   4   O4  ? ? N A  7   N U   4   2_555 ? ? ? ? ? ? WATSON-CRICK  ?     ? 
hydrog8  hydrog ? ? A U  8 N3 ? ? ? 1_555 A U   3   O4  ? ? N U  8   N U   3   2_555 ? ? ? ? ? ? 'U-U MISPAIR' ?     ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 262 B . ? LEU 262 A PRO 263 B ? PRO 263 A 1 6.46 
2 LEU 262 D . ? LEU 262 B PRO 263 D ? PRO 263 B 1 1.39 
3 LEU 262 F . ? LEU 262 C PRO 263 F ? PRO 263 C 1 1.82 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
ABG ? 4 ? 
ACF ? 4 ? 
AEX ? 4 ? 
APR ? 2 ? 
BBG ? 4 ? 
BCF ? 4 ? 
BEX ? 4 ? 
BPR ? 2 ? 
CBG ? 4 ? 
CCF ? 4 ? 
CEX ? 4 ? 
CPR ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
ABG 1 2 ? anti-parallel 
ABG 2 3 ? anti-parallel 
ABG 3 4 ? anti-parallel 
ACF 1 2 ? anti-parallel 
ACF 2 3 ? anti-parallel 
ACF 3 4 ? anti-parallel 
AEX 1 2 ? anti-parallel 
AEX 2 3 ? parallel      
AEX 3 4 ? anti-parallel 
APR 1 2 ? anti-parallel 
BBG 1 2 ? anti-parallel 
BBG 2 3 ? anti-parallel 
BBG 3 4 ? anti-parallel 
BCF 1 2 ? anti-parallel 
BCF 2 3 ? anti-parallel 
BCF 3 4 ? anti-parallel 
BEX 1 2 ? anti-parallel 
BEX 2 3 ? parallel      
BEX 3 4 ? anti-parallel 
BPR 1 2 ? anti-parallel 
CBG 1 2 ? anti-parallel 
CBG 2 3 ? anti-parallel 
CBG 3 4 ? anti-parallel 
CCF 1 2 ? anti-parallel 
CCF 2 3 ? anti-parallel 
CCF 3 4 ? anti-parallel 
CEX 1 2 ? anti-parallel 
CEX 2 3 ? parallel      
CEX 3 4 ? anti-parallel 
CPR 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
ABG 1 VAL B 92  ? PHE B 105 ? VAL A 92  PHE A 105 
ABG 2 ASN B 309 ? LEU B 319 ? ASN A 309 LEU A 319 
ABG 3 ALA B 169 ? THR B 178 ? ALA A 169 THR A 178 
ABG 4 VAL B 239 ? SER B 243 ? VAL A 239 SER A 243 
ACF 1 ASN B 108 ? THR B 118 ? ASN A 108 THR A 118 
ACF 2 THR B 296 ? SER B 302 ? THR A 296 SER A 302 
ACF 3 SER B 187 ? CYS B 193 ? SER A 187 CYS A 193 
ACF 4 PHE B 231 ? PHE B 235 ? PHE A 231 PHE A 235 
AEX 1 VAL B 121 ? PRO B 129 ? VAL A 121 PRO A 129 
AEX 2 THR B 137 ? PHE B 145 ? THR A 137 PHE A 145 
AEX 3 ASN B 277 ? ALA B 279 ? ASN A 277 ALA A 279 
AEX 4 GLN B 260 ? LEU B 262 ? GLN A 260 LEU A 262 
APR 1 LYS B 196 ? VAL B 204 ? LYS A 196 VAL A 204 
APR 2 ALA B 209 ? VAL B 218 ? ALA A 209 VAL A 218 
BBG 1 VAL D 92  ? PHE D 105 ? VAL B 92  PHE B 105 
BBG 2 ASN D 309 ? LEU D 319 ? ASN B 309 LEU B 319 
BBG 3 ALA D 169 ? THR D 178 ? ALA B 169 THR B 178 
BBG 4 VAL D 239 ? SER D 243 ? VAL B 239 SER B 243 
BCF 1 ASN D 108 ? THR D 118 ? ASN B 108 THR B 118 
BCF 2 THR D 296 ? SER D 302 ? THR B 296 SER B 302 
BCF 3 SER D 187 ? CYS D 193 ? SER B 187 CYS B 193 
BCF 4 PHE D 231 ? PHE D 235 ? PHE B 231 PHE B 235 
BEX 1 VAL D 121 ? PRO D 129 ? VAL B 121 PRO B 129 
BEX 2 THR D 137 ? PHE D 145 ? THR B 137 PHE B 145 
BEX 3 ASN D 277 ? ALA D 279 ? ASN B 277 ALA B 279 
BEX 4 GLN D 260 ? LEU D 262 ? GLN B 260 LEU B 262 
BPR 1 LYS D 196 ? VAL D 204 ? LYS B 196 VAL B 204 
BPR 2 ALA D 209 ? VAL D 218 ? ALA B 209 VAL B 218 
CBG 1 VAL F 92  ? PHE F 105 ? VAL C 92  PHE C 105 
CBG 2 ASN F 309 ? LEU F 319 ? ASN C 309 LEU C 319 
CBG 3 ALA F 169 ? THR F 178 ? ALA C 169 THR C 178 
CBG 4 VAL F 239 ? SER F 243 ? VAL C 239 SER C 243 
CCF 1 ASN F 108 ? THR F 118 ? ASN C 108 THR C 118 
CCF 2 THR F 296 ? SER F 302 ? THR C 296 SER C 302 
CCF 3 SER F 187 ? CYS F 193 ? SER C 187 CYS C 193 
CCF 4 PHE F 231 ? PHE F 235 ? PHE C 231 PHE C 235 
CEX 1 VAL F 121 ? PRO F 129 ? VAL C 121 PRO C 129 
CEX 2 THR F 137 ? PHE F 145 ? THR C 137 PHE C 145 
CEX 3 ASN F 277 ? ALA F 279 ? ASN C 277 ALA C 279 
CEX 4 GLN F 260 ? LEU F 262 ? GLN C 260 LEU C 262 
CPR 1 LYS F 196 ? VAL F 204 ? LYS C 196 VAL C 204 
CPR 2 ALA F 209 ? VAL F 218 ? ALA C 209 VAL C 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CA A 364' 
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CA B 364' 
AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CA C 364' 
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA C 365' 
AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CA A 365' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 3 ASP B 221 ? ASP A 221 . ? 1_555 ? 
2  AC1 3 GLY B 273 ? GLY A 273 . ? 1_555 ? 
3  AC1 3 ASP D 161 ? ASP B 161 . ? 1_555 ? 
4  AC2 3 ASP D 221 ? ASP B 221 . ? 1_555 ? 
5  AC2 3 GLY D 273 ? GLY B 273 . ? 1_555 ? 
6  AC2 3 ASP F 161 ? ASP C 161 . ? 1_555 ? 
7  AC3 2 ASP F 221 ? ASP C 221 . ? 1_555 ? 
8  AC3 2 GLY F 273 ? GLY C 273 . ? 1_555 ? 
9  AC4 6 ASP B 249 ? ASP A 249 . ? 1_555 ? 
10 AC4 6 GLU B 251 ? GLU A 251 . ? 1_555 ? 
11 AC4 6 ASP D 249 ? ASP B 249 . ? 1_555 ? 
12 AC4 6 GLU D 251 ? GLU B 251 . ? 1_555 ? 
13 AC4 6 ASP F 249 ? ASP C 249 . ? 1_555 ? 
14 AC4 6 GLU F 251 ? GLU C 251 . ? 1_555 ? 
15 AC5 3 GLU B 251 ? GLU A 251 . ? 1_555 ? 
16 AC5 3 GLU D 251 ? GLU B 251 . ? 1_555 ? 
17 AC5 3 GLU F 251 ? GLU C 251 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2BBV 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2BBV 
_atom_sites.fract_transf_matrix[1][1]   0.002762 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.002762 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.002762 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    O  "O5'" . U   A 1 1   ? 12.003  4.744  94.642  1.00 27.06 ? 1   U   N "O5'" 1 
ATOM   2    C  "C5'" . U   A 1 1   ? 11.034  4.634  93.577  1.00 34.01 ? 1   U   N "C5'" 1 
ATOM   3    C  "C4'" . U   A 1 1   ? 11.171  3.265  92.907  1.00 37.53 ? 1   U   N "C4'" 1 
ATOM   4    O  "O4'" . U   A 1 1   ? 12.465  2.721  93.294  1.00 39.37 ? 1   U   N "O4'" 1 
ATOM   5    C  "C3'" . U   A 1 1   ? 10.156  2.200  93.317  1.00 36.77 ? 1   U   N "C3'" 1 
ATOM   6    O  "O3'" . U   A 1 1   ? 8.937   2.309  92.570  1.00 39.27 ? 1   U   N "O3'" 1 
ATOM   7    C  "C2'" . U   A 1 1   ? 10.940  0.920  93.058  1.00 36.15 ? 1   U   N "C2'" 1 
ATOM   8    O  "O2'" . U   A 1 1   ? 10.832  0.525  91.699  1.00 37.41 ? 1   U   N "O2'" 1 
ATOM   9    C  "C1'" . U   A 1 1   ? 12.363  1.313  93.487  1.00 39.52 ? 1   U   N "C1'" 1 
ATOM   10   N  N1    . U   A 1 1   ? 12.724  1.057  94.906  1.00 44.02 ? 1   U   N N1    1 
ATOM   11   C  C2    . U   A 1 1   ? 12.315  -0.125 95.464  1.00 38.81 ? 1   U   N C2    1 
ATOM   12   O  O2    . U   A 1 1   ? 11.682  -0.965 94.847  1.00 34.40 ? 1   U   N O2    1 
ATOM   13   N  N3    . U   A 1 1   ? 12.661  -0.324 96.785  1.00 44.14 ? 1   U   N N3    1 
ATOM   14   C  C4    . U   A 1 1   ? 13.381  0.556  97.583  1.00 45.56 ? 1   U   N C4    1 
ATOM   15   O  O4    . U   A 1 1   ? 13.626  0.266  98.753  1.00 45.64 ? 1   U   N O4    1 
ATOM   16   C  C5    . U   A 1 1   ? 13.773  1.768  96.912  1.00 42.89 ? 1   U   N C5    1 
ATOM   17   C  C6    . U   A 1 1   ? 13.447  1.986  95.630  1.00 41.95 ? 1   U   N C6    1 
ATOM   18   P  P     . C   A 1 2   ? 7.563   1.747  93.176  1.00 47.90 ? 2   C   N P     1 
ATOM   19   O  OP1   . C   A 1 2   ? 6.426   2.568  92.699  1.00 45.51 ? 2   C   N OP1   1 
ATOM   20   O  OP2   . C   A 1 2   ? 7.662   1.642  94.650  1.00 40.11 ? 2   C   N OP2   1 
ATOM   21   O  "O5'" . C   A 1 2   ? 7.478   0.271  92.540  1.00 44.42 ? 2   C   N "O5'" 1 
ATOM   22   C  "C5'" . C   A 1 2   ? 6.170   -0.292 92.242  1.00 40.62 ? 2   C   N "C5'" 1 
ATOM   23   C  "C4'" . C   A 1 2   ? 6.285   -1.817 92.082  1.00 39.59 ? 2   C   N "C4'" 1 
ATOM   24   O  "O4'" . C   A 1 2   ? 7.628   -2.192 92.501  1.00 38.97 ? 2   C   N "O4'" 1 
ATOM   25   C  "C3'" . C   A 1 2   ? 5.370   -2.683 92.960  1.00 41.66 ? 2   C   N "C3'" 1 
ATOM   26   O  "O3'" . C   A 1 2   ? 4.064   -2.870 92.417  1.00 46.16 ? 2   C   N "O3'" 1 
ATOM   27   C  "C2'" . C   A 1 2   ? 6.162   -3.973 93.061  1.00 37.98 ? 2   C   N "C2'" 1 
ATOM   28   O  "O2'" . C   A 1 2   ? 5.930   -4.802 91.931  1.00 26.07 ? 2   C   N "O2'" 1 
ATOM   29   C  "C1'" . C   A 1 2   ? 7.592   -3.448 93.174  1.00 39.13 ? 2   C   N "C1'" 1 
ATOM   30   N  N1    . C   A 1 2   ? 8.054   -3.213 94.555  1.00 41.24 ? 2   C   N N1    1 
ATOM   31   C  C2    . C   A 1 2   ? 7.904   -4.239 95.478  1.00 45.32 ? 2   C   N C2    1 
ATOM   32   O  O2    . C   A 1 2   ? 7.401   -5.311 95.110  1.00 44.19 ? 2   C   N O2    1 
ATOM   33   N  N3    . C   A 1 2   ? 8.316   -4.038 96.759  1.00 47.45 ? 2   C   N N3    1 
ATOM   34   C  C4    . C   A 1 2   ? 8.856   -2.863 97.113  1.00 48.12 ? 2   C   N C4    1 
ATOM   35   N  N4    . C   A 1 2   ? 9.241   -2.710 98.365  1.00 49.72 ? 2   C   N N4    1 
ATOM   36   C  C5    . C   A 1 2   ? 9.022   -1.787 96.173  1.00 45.61 ? 2   C   N C5    1 
ATOM   37   C  C6    . C   A 1 2   ? 8.606   -2.011 94.911  1.00 42.27 ? 2   C   N C6    1 
ATOM   38   P  P     . U   A 1 3   ? 2.882   -3.372 93.380  1.00 55.94 ? 3   U   N P     1 
ATOM   39   O  OP1   . U   A 1 3   ? 1.589   -3.324 92.663  1.00 52.28 ? 3   U   N OP1   1 
ATOM   40   O  OP2   . U   A 1 3   ? 2.909   -2.609 94.649  1.00 47.93 ? 3   U   N OP2   1 
ATOM   41   O  "O5'" . U   A 1 3   ? 3.280   -4.907 93.682  1.00 50.46 ? 3   U   N "O5'" 1 
ATOM   42   C  "C5'" . U   A 1 3   ? 2.268   -5.798 94.241  1.00 46.15 ? 3   U   N "C5'" 1 
ATOM   43   C  "C4'" . U   A 1 3   ? 2.942   -7.059 94.818  1.00 43.56 ? 3   U   N "C4'" 1 
ATOM   44   O  "O4'" . U   A 1 3   ? 4.362   -6.779 94.909  1.00 42.64 ? 3   U   N "O4'" 1 
ATOM   45   C  "C3'" . U   A 1 3   ? 2.537   -7.493 96.241  1.00 45.87 ? 3   U   N "C3'" 1 
ATOM   46   O  "O3'" . U   A 1 3   ? 1.355   -8.299 96.241  1.00 44.85 ? 3   U   N "O3'" 1 
ATOM   47   C  "C2'" . U   A 1 3   ? 3.785   -8.230 96.698  1.00 42.15 ? 3   U   N "C2'" 1 
ATOM   48   O  "O2'" . U   A 1 3   ? 3.768   -9.580 96.256  1.00 40.77 ? 3   U   N "O2'" 1 
ATOM   49   C  "C1'" . U   A 1 3   ? 4.900   -7.379 96.079  1.00 39.65 ? 3   U   N "C1'" 1 
ATOM   50   N  N1    . U   A 1 3   ? 5.397   -6.269 96.911  1.00 41.28 ? 3   U   N N1    1 
ATOM   51   C  C2    . U   A 1 3   ? 5.473   -6.482 98.257  1.00 42.11 ? 3   U   N C2    1 
ATOM   52   O  O2    . U   A 1 3   ? 5.170   -7.540 98.784  1.00 41.04 ? 3   U   N O2    1 
ATOM   53   N  N3    . U   A 1 3   ? 5.923   -5.418 99.007  1.00 41.92 ? 3   U   N N3    1 
ATOM   54   C  C4    . U   A 1 3   ? 6.300   -4.173 98.513  1.00 37.19 ? 3   U   N C4    1 
ATOM   55   O  O4    . U   A 1 3   ? 6.683   -3.299 99.286  1.00 33.22 ? 3   U   N O4    1 
ATOM   56   C  C5    . U   A 1 3   ? 6.190   -4.049 97.084  1.00 40.22 ? 3   U   N C5    1 
ATOM   57   C  C6    . U   A 1 3   ? 5.754   -5.068 96.336  1.00 39.82 ? 3   U   N C6    1 
ATOM   58   P  P     . U   A 1 4   ? 0.562   -8.650 97.602  1.00 49.09 ? 4   U   N P     1 
ATOM   59   O  OP1   . U   A 1 4   ? -0.094  -9.974 97.475  1.00 44.88 ? 4   U   N OP1   1 
ATOM   60   O  OP2   . U   A 1 4   ? -0.345  -7.545 97.969  1.00 43.61 ? 4   U   N OP2   1 
ATOM   61   O  "O5'" . U   A 1 4   ? 1.690   -8.758 98.745  1.00 44.70 ? 4   U   N "O5'" 1 
ATOM   62   C  "C5'" . U   A 1 4   ? 1.625   -9.913 99.623  1.00 45.20 ? 4   U   N "C5'" 1 
ATOM   63   C  "C4'" . U   A 1 4   ? 1.512   -9.525 101.120 1.00 43.57 ? 4   U   N "C4'" 1 
ATOM   64   O  "O4'" . U   A 1 4   ? 2.789   -8.960 101.559 1.00 41.91 ? 4   U   N "O4'" 1 
ATOM   65   C  "C3'" . U   A 1 4   ? 0.518   -8.412 101.494 1.00 42.31 ? 4   U   N "C3'" 1 
ATOM   66   O  "O3'" . U   A 1 4   ? -0.826  -8.832 101.650 1.00 42.14 ? 4   U   N "O3'" 1 
ATOM   67   C  "C2'" . U   A 1 4   ? 1.058   -7.905 102.811 1.00 43.09 ? 4   U   N "C2'" 1 
ATOM   68   O  "O2'" . U   A 1 4   ? 0.611   -8.714 103.890 1.00 44.11 ? 4   U   N "O2'" 1 
ATOM   69   C  "C1'" . U   A 1 4   ? 2.547   -7.965 102.560 1.00 40.57 ? 4   U   N "C1'" 1 
ATOM   70   N  N1    . U   A 1 4   ? 3.020   -6.658 102.113 1.00 35.22 ? 4   U   N N1    1 
ATOM   71   C  C2    . U   A 1 4   ? 3.097   -5.696 103.078 1.00 35.63 ? 4   U   N C2    1 
ATOM   72   O  O2    . U   A 1 4   ? 2.836   -5.896 104.253 1.00 34.82 ? 4   U   N O2    1 
ATOM   73   N  N3    . U   A 1 4   ? 3.501   -4.456 102.641 1.00 37.95 ? 4   U   N N3    1 
ATOM   74   C  C4    . U   A 1 4   ? 3.836   -4.123 101.332 1.00 36.98 ? 4   U   N C4    1 
ATOM   75   O  O4    . U   A 1 4   ? 4.177   -2.974 101.065 1.00 37.14 ? 4   U   N O4    1 
ATOM   76   C  C5    . U   A 1 4   ? 3.736   -5.217 100.397 1.00 35.17 ? 4   U   N C5    1 
ATOM   77   C  C6    . U   A 1 4   ? 3.339   -6.429 100.797 1.00 33.82 ? 4   U   N C6    1 
ATOM   78   P  P     . A   A 1 5   ? -1.914  -7.712 102.006 1.00 49.31 ? 5   A   N P     1 
ATOM   79   O  OP1   . A   A 1 5   ? -3.276  -8.239 101.778 1.00 49.43 ? 5   A   N OP1   1 
ATOM   80   O  OP2   . A   A 1 5   ? -1.607  -6.463 101.270 1.00 45.81 ? 5   A   N OP2   1 
ATOM   81   O  "O5'" . A   A 1 5   ? -1.682  -7.453 103.585 1.00 46.08 ? 5   A   N "O5'" 1 
ATOM   82   C  "C5'" . A   A 1 5   ? -1.188  -8.545 104.381 1.00 47.74 ? 5   A   N "C5'" 1 
ATOM   83   C  "C4'" . A   A 1 5   ? -1.286  -8.266 105.901 1.00 46.76 ? 5   A   N "C4'" 1 
ATOM   84   O  "O4'" . A   A 1 5   ? -0.006  -7.671 106.349 1.00 48.02 ? 5   A   N "O4'" 1 
ATOM   85   C  "C3'" . A   A 1 5   ? -2.339  -7.269 106.365 1.00 50.55 ? 5   A   N "C3'" 1 
ATOM   86   O  "O3'" . A   A 1 5   ? -3.630  -7.864 106.487 1.00 48.39 ? 5   A   N "O3'" 1 
ATOM   87   C  "C2'" . A   A 1 5   ? -1.802  -6.799 107.706 1.00 48.70 ? 5   A   N "C2'" 1 
ATOM   88   O  "O2'" . A   A 1 5   ? -2.188  -7.680 108.751 1.00 44.89 ? 5   A   N "O2'" 1 
ATOM   89   C  "C1'" . A   A 1 5   ? -0.297  -6.763 107.443 1.00 44.79 ? 5   A   N "C1'" 1 
ATOM   90   N  N9    . A   A 1 5   ? 0.187   -5.367 107.165 1.00 38.45 ? 5   A   N N9    1 
ATOM   91   C  C8    . A   A 1 5   ? 0.514   -4.414 108.083 1.00 37.69 ? 5   A   N C8    1 
ATOM   92   N  N7    . A   A 1 5   ? 0.902   -3.284 107.576 1.00 35.51 ? 5   A   N N7    1 
ATOM   93   C  C5    . A   A 1 5   ? 0.834   -3.488 106.220 1.00 32.10 ? 5   A   N C5    1 
ATOM   94   C  C6    . A   A 1 5   ? 1.115   -2.663 105.113 1.00 32.23 ? 5   A   N C6    1 
ATOM   95   N  N6    . A   A 1 5   ? 1.544   -1.388 105.238 1.00 30.24 ? 5   A   N N6    1 
ATOM   96   N  N1    . A   A 1 5   ? 0.943   -3.181 103.892 1.00 31.10 ? 5   A   N N1    1 
ATOM   97   C  C2    . A   A 1 5   ? 0.516   -4.448 103.782 1.00 30.06 ? 5   A   N C2    1 
ATOM   98   N  N3    . A   A 1 5   ? 0.219   -5.316 104.737 1.00 31.55 ? 5   A   N N3    1 
ATOM   99   C  C4    . A   A 1 5   ? 0.402   -4.757 105.944 1.00 34.60 ? 5   A   N C4    1 
ATOM   100  P  P     . U   A 1 6   ? -4.918  -7.036 106.037 1.00 54.16 ? 6   U   N P     1 
ATOM   101  O  OP1   . U   A 1 6   ? -6.143  -7.837 106.277 1.00 49.61 ? 6   U   N OP1   1 
ATOM   102  O  OP2   . U   A 1 6   ? -4.758  -6.576 104.640 1.00 50.05 ? 6   U   N OP2   1 
ATOM   103  O  "O5'" . U   A 1 6   ? -4.870  -5.776 107.029 1.00 47.95 ? 6   U   N "O5'" 1 
ATOM   104  C  "C5'" . U   A 1 6   ? -4.403  -6.010 108.369 1.00 40.54 ? 6   U   N "C5'" 1 
ATOM   105  C  "C4'" . U   A 1 6   ? -4.199  -4.695 109.140 1.00 38.71 ? 6   U   N "C4'" 1 
ATOM   106  O  "O4'" . U   A 1 6   ? -2.902  -4.131 108.772 1.00 38.16 ? 6   U   N "O4'" 1 
ATOM   107  C  "C3'" . U   A 1 6   ? -5.200  -3.576 108.869 1.00 41.68 ? 6   U   N "C3'" 1 
ATOM   108  O  "O3'" . U   A 1 6   ? -6.377  -3.760 109.658 1.00 43.86 ? 6   U   N "O3'" 1 
ATOM   109  C  "C2'" . U   A 1 6   ? -4.392  -2.337 109.241 1.00 38.50 ? 6   U   N "C2'" 1 
ATOM   110  O  "O2'" . U   A 1 6   ? -4.493  -2.062 110.627 1.00 36.42 ? 6   U   N "O2'" 1 
ATOM   111  C  "C1'" . U   A 1 6   ? -2.974  -2.703 108.781 1.00 36.31 ? 6   U   N "C1'" 1 
ATOM   112  N  N1    . U   A 1 6   ? -2.604  -2.185 107.436 1.00 33.70 ? 6   U   N N1    1 
ATOM   113  C  C2    . U   A 1 6   ? -1.607  -1.245 107.400 1.00 36.74 ? 6   U   N C2    1 
ATOM   114  O  O2    . U   A 1 6   ? -1.034  -0.856 108.404 1.00 35.18 ? 6   U   N O2    1 
ATOM   115  N  N3    . U   A 1 6   ? -1.273  -0.752 106.154 1.00 37.24 ? 6   U   N N3    1 
ATOM   116  C  C4    . U   A 1 6   ? -1.848  -1.127 104.946 1.00 39.85 ? 6   U   N C4    1 
ATOM   117  O  O4    . U   A 1 6   ? -1.465  -0.608 103.896 1.00 40.52 ? 6   U   N O4    1 
ATOM   118  C  C5    . U   A 1 6   ? -2.879  -2.130 105.074 1.00 38.62 ? 6   U   N C5    1 
ATOM   119  C  C6    . U   A 1 6   ? -3.227  -2.624 106.280 1.00 36.57 ? 6   U   N C6    1 
ATOM   120  P  P     . A   A 1 7   ? -7.526  -2.646 109.719 1.00 52.92 ? 7   A   N P     1 
ATOM   121  O  OP1   . A   A 1 7   ? -8.541  -3.025 110.728 1.00 47.06 ? 7   A   N OP1   1 
ATOM   122  O  OP2   . A   A 1 7   ? -8.061  -2.385 108.368 1.00 46.05 ? 7   A   N OP2   1 
ATOM   123  O  "O5'" . A   A 1 7   ? -6.762  -1.333 110.230 1.00 50.70 ? 7   A   N "O5'" 1 
ATOM   124  C  "C5'" . A   A 1 7   ? -7.567  -0.269 110.804 1.00 49.60 ? 7   A   N "C5'" 1 
ATOM   125  C  "C4'" . A   A 1 7   ? -6.799  1.044  110.731 1.00 47.10 ? 7   A   N "C4'" 1 
ATOM   126  O  "O4'" . A   A 1 7   ? -5.559  0.722  110.058 1.00 46.71 ? 7   A   N "O4'" 1 
ATOM   127  C  "C3'" . A   A 1 7   ? -7.410  2.143  109.856 1.00 49.31 ? 7   A   N "C3'" 1 
ATOM   128  O  "O3'" . A   A 1 7   ? -8.420  2.903  110.474 1.00 49.26 ? 7   A   N "O3'" 1 
ATOM   129  C  "C2'" . A   A 1 7   ? -6.225  2.971  109.481 1.00 47.68 ? 7   A   N "C2'" 1 
ATOM   130  O  "O2'" . A   A 1 7   ? -5.909  3.902  110.512 1.00 48.07 ? 7   A   N "O2'" 1 
ATOM   131  C  "C1'" . A   A 1 7   ? -5.234  1.848  109.277 1.00 44.21 ? 7   A   N "C1'" 1 
ATOM   132  N  N9    . A   A 1 7   ? -5.288  1.521  107.887 1.00 36.08 ? 7   A   N N9    1 
ATOM   133  C  C8    . A   A 1 7   ? -5.764  0.397  107.265 1.00 35.43 ? 7   A   N C8    1 
ATOM   134  N  N7    . A   A 1 7   ? -5.707  0.490  105.966 1.00 31.69 ? 7   A   N N7    1 
ATOM   135  C  C5    . A   A 1 7   ? -5.156  1.749  105.776 1.00 29.73 ? 7   A   N C5    1 
ATOM   136  C  C6    . A   A 1 7   ? -4.834  2.524  104.645 1.00 27.42 ? 7   A   N C6    1 
ATOM   137  N  N6    . A   A 1 7   ? -5.084  2.132  103.382 1.00 23.30 ? 7   A   N N6    1 
ATOM   138  N  N1    . A   A 1 7   ? -4.256  3.721  104.843 1.00 29.11 ? 7   A   N N1    1 
ATOM   139  C  C2    . A   A 1 7   ? -4.013  4.130  106.091 1.00 27.80 ? 7   A   N C2    1 
ATOM   140  N  N3    . A   A 1 7   ? -4.278  3.524  107.214 1.00 30.06 ? 7   A   N N3    1 
ATOM   141  C  C4    . A   A 1 7   ? -4.866  2.359  106.971 1.00 33.43 ? 7   A   N C4    1 
ATOM   142  P  P     . U   A 1 8   ? -9.630  3.374  109.555 1.00 50.50 ? 8   U   N P     1 
ATOM   143  O  OP1   . U   A 1 8   ? -10.561 4.213  110.335 1.00 46.62 ? 8   U   N OP1   1 
ATOM   144  O  OP2   . U   A 1 8   ? -10.250 2.194  108.908 1.00 45.50 ? 8   U   N OP2   1 
ATOM   145  O  "O5'" . U   A 1 8   ? -8.898  4.263  108.423 1.00 42.94 ? 8   U   N "O5'" 1 
ATOM   146  C  "C5'" . U   A 1 8   ? -8.121  5.406  108.844 1.00 40.82 ? 8   U   N "C5'" 1 
ATOM   147  C  "C4'" . U   A 1 8   ? -8.091  6.503  107.756 1.00 40.29 ? 8   U   N "C4'" 1 
ATOM   148  O  "O4'" . U   A 1 8   ? -7.091  6.143  106.750 1.00 41.85 ? 8   U   N "O4'" 1 
ATOM   149  C  "C3'" . U   A 1 8   ? -9.373  6.717  106.962 1.00 37.28 ? 8   U   N "C3'" 1 
ATOM   150  O  "O3'" . U   A 1 8   ? -10.276 7.570  107.666 1.00 38.06 ? 8   U   N "O3'" 1 
ATOM   151  C  "C2'" . U   A 1 8   ? -8.844  7.321  105.661 1.00 38.05 ? 8   U   N "C2'" 1 
ATOM   152  O  "O2'" . U   A 1 8   ? -8.687  8.726  105.777 1.00 33.48 ? 8   U   N "O2'" 1 
ATOM   153  C  "C1'" . U   A 1 8   ? -7.525  6.560  105.449 1.00 40.28 ? 8   U   N "C1'" 1 
ATOM   154  N  N1    . U   A 1 8   ? -7.599  5.348  104.581 1.00 39.56 ? 8   U   N N1    1 
ATOM   155  C  C2    . U   A 1 8   ? -7.410  5.524  103.230 1.00 38.63 ? 8   U   N C2    1 
ATOM   156  O  O2    . U   A 1 8   ? -7.212  6.617  102.726 1.00 36.91 ? 8   U   N O2    1 
ATOM   157  N  N3    . U   A 1 8   ? -7.459  4.383  102.452 1.00 37.79 ? 8   U   N N3    1 
ATOM   158  C  C4    . U   A 1 8   ? -7.685  3.091  102.909 1.00 41.43 ? 8   U   N C4    1 
ATOM   159  O  O4    . U   A 1 8   ? -7.701  2.150  102.115 1.00 39.65 ? 8   U   N O4    1 
ATOM   160  C  C5    . U   A 1 8   ? -7.882  3.001  104.334 1.00 40.98 ? 8   U   N C5    1 
ATOM   161  C  C6    . U   A 1 8   ? -7.835  4.095  105.115 1.00 38.91 ? 8   U   N C6    1 
ATOM   162  P  P     . C   A 1 9   ? -11.805 7.655  107.229 1.00 42.52 ? 9   C   N P     1 
ATOM   163  O  OP1   . C   A 1 9   ? -12.551 8.532  108.160 1.00 41.72 ? 9   C   N OP1   1 
ATOM   164  O  OP2   . C   A 1 9   ? -12.370 6.296  107.080 1.00 41.54 ? 9   C   N OP2   1 
ATOM   165  O  "O5'" . C   A 1 9   ? -11.709 8.342  105.791 1.00 39.91 ? 9   C   N "O5'" 1 
ATOM   166  C  "C5'" . C   A 1 9   ? -11.141 9.660  105.699 1.00 37.99 ? 9   C   N "C5'" 1 
ATOM   167  C  "C4'" . C   A 1 9   ? -11.079 10.072 104.232 1.00 39.29 ? 9   C   N "C4'" 1 
ATOM   168  O  "O4'" . C   A 1 9   ? -10.133 9.183  103.563 1.00 38.66 ? 9   C   N "O4'" 1 
ATOM   169  C  "C3'" . C   A 1 9   ? -12.360 9.856  103.437 1.00 36.22 ? 9   C   N "C3'" 1 
ATOM   170  O  "O3'" . C   A 1 9   ? -13.318 10.876 103.590 1.00 43.58 ? 9   C   N "O3'" 1 
ATOM   171  C  "C2'" . C   A 1 9   ? -11.849 9.744  102.020 1.00 33.77 ? 9   C   N "C2'" 1 
ATOM   172  O  "O2'" . C   A 1 9   ? -11.632 11.029 101.453 1.00 33.83 ? 9   C   N "O2'" 1 
ATOM   173  C  "C1'" . C   A 1 9   ? -10.589 8.931  102.234 1.00 36.76 ? 9   C   N "C1'" 1 
ATOM   174  N  N1    . C   A 1 9   ? -10.864 7.499  102.074 1.00 35.01 ? 9   C   N N1    1 
ATOM   175  C  C2    . C   A 1 9   ? -10.682 6.950  100.816 1.00 37.89 ? 9   C   N C2    1 
ATOM   176  O  O2    . C   A 1 9   ? -10.261 7.668  99.896  1.00 38.53 ? 9   C   N O2    1 
ATOM   177  N  N3    . C   A 1 9   ? -10.969 5.635  100.631 1.00 40.81 ? 9   C   N N3    1 
ATOM   178  C  C4    . C   A 1 9   ? -11.409 4.895  101.659 1.00 40.31 ? 9   C   N C4    1 
ATOM   179  N  N4    . C   A 1 9   ? -11.682 3.625  101.434 1.00 39.51 ? 9   C   N N4    1 
ATOM   180  C  C5    . C   A 1 9   ? -11.589 5.447  102.977 1.00 39.29 ? 9   C   N C5    1 
ATOM   181  C  C6    . C   A 1 9   ? -11.304 6.752  103.131 1.00 37.20 ? 9   C   N C6    1 
ATOM   182  P  P     . U   A 1 10  ? -14.827 10.489 103.282 1.00 49.98 ? 10  U   N P     1 
ATOM   183  O  OP1   . U   A 1 10  ? -15.733 11.236 104.177 1.00 47.19 ? 10  U   N OP1   1 
ATOM   184  O  OP2   . U   A 1 10  ? -14.985 9.016  103.335 1.00 48.62 ? 10  U   N OP2   1 
ATOM   185  O  "O5'" . U   A 1 10  ? -14.997 10.981 101.769 1.00 47.31 ? 10  U   N "O5'" 1 
ATOM   186  C  "C5'" . U   A 1 10  ? -14.507 12.291 101.436 1.00 46.19 ? 10  U   N "C5'" 1 
ATOM   187  C  "C4'" . U   A 1 10  ? -14.529 12.504 99.919  1.00 48.56 ? 10  U   N "C4'" 1 
ATOM   188  O  "O4'" . U   A 1 10  ? -13.593 11.563 99.306  1.00 47.88 ? 10  U   N "O4'" 1 
ATOM   189  C  "C3'" . U   A 1 10  ? -15.850 12.214 99.222  1.00 49.22 ? 10  U   N "C3'" 1 
ATOM   190  O  "O3'" . U   A 1 10  ? -16.749 13.309 99.306  1.00 45.44 ? 10  U   N "O3'" 1 
ATOM   191  C  "C2'" . U   A 1 10  ? -15.400 11.909 97.802  1.00 47.42 ? 10  U   N "C2'" 1 
ATOM   192  O  "O2'" . U   A 1 10  ? -15.241 13.104 97.051  1.00 45.18 ? 10  U   N "O2'" 1 
ATOM   193  C  "C1'" . U   A 1 10  ? -14.099 11.142 98.035  1.00 47.43 ? 10  U   N "C1'" 1 
ATOM   194  N  N1    . U   A 1 10  ? -14.275 9.671  98.048  1.00 46.44 ? 10  U   N N1    1 
ATOM   195  C  C2    . U   A 1 10  ? -14.292 9.043  96.830  1.00 47.34 ? 10  U   N C2    1 
ATOM   196  O  O2    . U   A 1 10  ? -14.168 9.639  95.774  1.00 47.14 ? 10  U   N O2    1 
ATOM   197  N  N3    . U   A 1 10  ? -14.460 7.673  96.858  1.00 45.01 ? 10  U   N N3    1 
ATOM   198  C  C4    . U   A 1 10  ? -14.610 6.892  97.997  1.00 44.40 ? 10  U   N C4    1 
ATOM   199  O  O4    . U   A 1 10  ? -14.754 5.674  97.892  1.00 41.69 ? 10  U   N O4    1 
ATOM   200  C  C5    . U   A 1 10  ? -14.577 7.639  99.231  1.00 46.97 ? 10  U   N C5    1 
ATOM   201  C  C6    . U   A 1 10  ? -14.416 8.972  99.231  1.00 45.28 ? 10  U   N C6    1 
ATOM   202  N  N     . LEU B 2 56  ? -7.949  48.466 105.739 1.00 20.88 ? 56  LEU A N     1 
ATOM   203  C  CA    . LEU B 2 56  ? -7.180  47.354 106.324 1.00 19.48 ? 56  LEU A CA    1 
ATOM   204  C  C     . LEU B 2 56  ? -7.865  46.010 106.025 1.00 19.19 ? 56  LEU A C     1 
ATOM   205  O  O     . LEU B 2 56  ? -7.426  44.951 106.501 1.00 20.35 ? 56  LEU A O     1 
ATOM   206  C  CB    . LEU B 2 56  ? -7.062  47.567 107.833 1.00 20.81 ? 56  LEU A CB    1 
ATOM   207  C  CG    . LEU B 2 56  ? -6.535  48.963 108.185 1.00 19.62 ? 56  LEU A CG    1 
ATOM   208  C  CD1   . LEU B 2 56  ? -7.367  50.091 107.567 1.00 18.29 ? 56  LEU A CD1   1 
ATOM   209  C  CD2   . LEU B 2 56  ? -6.517  49.240 109.688 1.00 18.76 ? 56  LEU A CD2   1 
ATOM   210  N  N     . THR B 2 57  ? -8.913  46.115 105.226 1.00 18.68 ? 57  THR A N     1 
ATOM   211  C  CA    . THR B 2 57  ? -9.767  44.978 104.827 1.00 24.01 ? 57  THR A CA    1 
ATOM   212  C  C     . THR B 2 57  ? -8.945  43.742 104.417 1.00 21.54 ? 57  THR A C     1 
ATOM   213  O  O     . THR B 2 57  ? -9.133  43.184 103.325 1.00 19.30 ? 57  THR A O     1 
ATOM   214  C  CB    . THR B 2 57  ? -10.670 45.380 103.663 1.00 25.13 ? 57  THR A CB    1 
ATOM   215  O  OG1   . THR B 2 57  ? -11.999 44.940 103.910 1.00 25.79 ? 57  THR A OG1   1 
ATOM   216  C  CG2   . THR B 2 57  ? -10.228 44.782 102.329 1.00 24.03 ? 57  THR A CG2   1 
ATOM   217  N  N     . ARG B 2 58  ? -8.068  43.384 105.325 1.00 18.68 ? 58  ARG A N     1 
ATOM   218  C  CA    . ARG B 2 58  ? -7.236  42.167 105.269 1.00 15.39 ? 58  ARG A CA    1 
ATOM   219  C  C     . ARG B 2 58  ? -7.326  41.589 106.662 1.00 15.65 ? 58  ARG A C     1 
ATOM   220  O  O     . ARG B 2 58  ? -6.936  40.434 106.901 1.00 14.71 ? 58  ARG A O     1 
ATOM   221  C  CB    . ARG B 2 58  ? -5.784  42.504 104.914 1.00 14.65 ? 58  ARG A CB    1 
ATOM   222  C  CG    . ARG B 2 58  ? -4.783  41.484 105.478 1.00 16.20 ? 58  ARG A CG    1 
ATOM   223  C  CD    . ARG B 2 58  ? -3.479  41.400 104.674 1.00 17.71 ? 58  ARG A CD    1 
ATOM   224  N  NE    . ARG B 2 58  ? -2.702  40.180 104.957 1.00 17.45 ? 58  ARG A NE    1 
ATOM   225  C  CZ    . ARG B 2 58  ? -1.384  40.056 104.731 1.00 25.09 ? 58  ARG A CZ    1 
ATOM   226  N  NH1   . ARG B 2 58  ? -0.672  41.070 104.220 1.00 25.13 ? 58  ARG A NH1   1 
ATOM   227  N  NH2   . ARG B 2 58  ? -0.679  38.944 104.987 1.00 24.03 ? 58  ARG A NH2   1 
ATOM   228  N  N     . LEU B 2 59  ? -7.855  42.497 107.457 1.00 16.65 ? 59  LEU A N     1 
ATOM   229  C  CA    . LEU B 2 59  ? -8.147  42.331 108.869 1.00 14.65 ? 59  LEU A CA    1 
ATOM   230  C  C     . LEU B 2 59  ? -9.625  42.017 109.025 1.00 13.28 ? 59  LEU A C     1 
ATOM   231  O  O     . LEU B 2 59  ? -10.440 42.320 108.139 1.00 13.62 ? 59  LEU A O     1 
ATOM   232  C  CB    . LEU B 2 59  ? -7.877  43.649 109.602 1.00 14.71 ? 59  LEU A CB    1 
ATOM   233  C  CG    . LEU B 2 59  ? -6.501  43.715 110.256 1.00 15.60 ? 59  LEU A CG    1 
ATOM   234  C  CD1   . LEU B 2 59  ? -6.169  45.107 110.800 1.00 14.62 ? 59  LEU A CD1   1 
ATOM   235  C  CD2   . LEU B 2 59  ? -6.362  42.760 111.441 1.00 15.28 ? 59  LEU A CD2   1 
ATOM   236  N  N     . SER B 2 60  ? -9.929  41.421 110.147 1.00 11.51 ? 60  SER A N     1 
ATOM   237  C  CA    . SER B 2 60  ? -11.301 41.061 110.487 1.00 11.21 ? 60  SER A CA    1 
ATOM   238  C  C     . SER B 2 60  ? -11.901 42.150 111.369 1.00 11.79 ? 60  SER A C     1 
ATOM   239  O  O     . SER B 2 60  ? -11.195 42.781 112.172 1.00 11.59 ? 60  SER A O     1 
ATOM   240  C  CB    . SER B 2 60  ? -11.324 39.728 111.230 1.00 10.66 ? 60  SER A CB    1 
ATOM   241  O  OG    . SER B 2 60  ? -11.422 39.954 112.627 1.00 10.34 ? 60  SER A OG    1 
ATOM   242  N  N     . GLN B 2 61  ? -13.185 42.327 111.175 1.00 12.24 ? 61  GLN A N     1 
ATOM   243  C  CA    . GLN B 2 61  ? -13.980 43.306 111.913 1.00 12.86 ? 61  GLN A CA    1 
ATOM   244  C  C     . GLN B 2 61  ? -13.650 43.218 113.405 1.00 11.45 ? 61  GLN A C     1 
ATOM   245  O  O     . GLN B 2 61  ? -13.151 44.183 114.007 1.00 11.50 ? 61  GLN A O     1 
ATOM   246  C  CB    . GLN B 2 61  ? -15.464 43.005 111.697 1.00 18.88 ? 61  GLN A CB    1 
ATOM   247  C  CG    . GLN B 2 61  ? -15.732 42.258 110.384 1.00 26.12 ? 61  GLN A CG    1 
ATOM   248  C  CD    . GLN B 2 61  ? -15.906 40.745 110.568 1.00 29.96 ? 61  GLN A CD    1 
ATOM   249  O  OE1   . GLN B 2 61  ? -15.623 39.975 109.650 1.00 30.35 ? 61  GLN A OE1   1 
ATOM   250  N  NE2   . GLN B 2 61  ? -16.362 40.266 111.710 1.00 31.18 ? 61  GLN A NE2   1 
ATOM   251  N  N     . PRO B 2 62  ? -13.912 42.071 114.046 1.00 11.13 ? 62  PRO A N     1 
ATOM   252  C  CA    . PRO B 2 62  ? -13.647 41.903 115.466 1.00 11.35 ? 62  PRO A CA    1 
ATOM   253  C  C     . PRO B 2 62  ? -12.182 42.091 115.786 1.00 11.95 ? 62  PRO A C     1 
ATOM   254  O  O     . PRO B 2 62  ? -11.847 42.486 116.947 1.00 12.65 ? 62  PRO A O     1 
ATOM   255  C  CB    . PRO B 2 62  ? -14.094 40.491 115.757 1.00 10.30 ? 62  PRO A CB    1 
ATOM   256  C  CG    . PRO B 2 62  ? -14.613 39.890 114.460 1.00 10.22 ? 62  PRO A CG    1 
ATOM   257  C  CD    . PRO B 2 62  ? -14.489 40.909 113.372 1.00 10.92 ? 62  PRO A CD    1 
ATOM   258  N  N     . GLY B 2 63  ? -11.353 41.817 114.797 1.00 11.44 ? 63  GLY A N     1 
ATOM   259  C  CA    . GLY B 2 63  ? -9.888  41.915 114.932 1.00 10.45 ? 63  GLY A CA    1 
ATOM   260  C  C     . GLY B 2 63  ? -9.444  43.378 115.057 1.00 10.13 ? 63  GLY A C     1 
ATOM   261  O  O     . GLY B 2 63  ? -8.513  43.701 115.812 1.00 8.64  ? 63  GLY A O     1 
ATOM   262  N  N     . LEU B 2 64  ? -10.132 44.218 114.306 1.00 9.60  ? 64  LEU A N     1 
ATOM   263  C  CA    . LEU B 2 64  ? -9.853  45.664 114.248 1.00 9.61  ? 64  LEU A CA    1 
ATOM   264  C  C     . LEU B 2 64  ? -10.225 46.354 115.565 1.00 8.70  ? 64  LEU A C     1 
ATOM   265  O  O     . LEU B 2 64  ? -9.506  47.239 116.050 1.00 9.00  ? 64  LEU A O     1 
ATOM   266  C  CB    . LEU B 2 64  ? -10.656 46.308 113.119 1.00 11.49 ? 64  LEU A CB    1 
ATOM   267  C  CG    . LEU B 2 64  ? -10.339 47.793 112.936 1.00 8.67  ? 64  LEU A CG    1 
ATOM   268  C  CD1   . LEU B 2 64  ? -8.893  48.049 112.506 1.00 13.06 ? 64  LEU A CD1   1 
ATOM   269  C  CD2   . LEU B 2 64  ? -11.212 48.464 111.874 1.00 12.00 ? 64  LEU A CD2   1 
ATOM   270  N  N     . ALA B 2 65  ? -11.351 45.939 116.115 1.00 7.81  ? 65  ALA A N     1 
ATOM   271  C  CA    . ALA B 2 65  ? -11.853 46.490 117.384 1.00 6.91  ? 65  ALA A CA    1 
ATOM   272  C  C     . ALA B 2 65  ? -10.853 46.191 118.499 1.00 6.18  ? 65  ALA A C     1 
ATOM   273  O  O     . ALA B 2 65  ? -10.485 47.077 119.284 1.00 4.91  ? 65  ALA A O     1 
ATOM   274  C  CB    . ALA B 2 65  ? -13.201 45.860 117.735 1.00 3.32  ? 65  ALA A CB    1 
ATOM   275  N  N     . PHE B 2 66  ? -10.451 44.938 118.517 1.00 11.98 ? 66  PHE A N     1 
ATOM   276  C  CA    . PHE B 2 66  ? -9.486  44.418 119.488 1.00 11.62 ? 66  PHE A CA    1 
ATOM   277  C  C     . PHE B 2 66  ? -8.312  45.393 119.625 1.00 11.82 ? 66  PHE A C     1 
ATOM   278  O  O     . PHE B 2 66  ? -7.853  45.687 120.738 1.00 12.88 ? 66  PHE A O     1 
ATOM   279  C  CB    . PHE B 2 66  ? -8.972  43.058 119.009 1.00 10.72 ? 66  PHE A CB    1 
ATOM   280  C  CG    . PHE B 2 66  ? -7.693  42.614 119.714 1.00 10.99 ? 66  PHE A CG    1 
ATOM   281  C  CD1   . PHE B 2 66  ? -7.701  42.386 121.094 1.00 11.51 ? 66  PHE A CD1   1 
ATOM   282  C  CD2   . PHE B 2 66  ? -6.516  42.434 118.978 1.00 11.66 ? 66  PHE A CD2   1 
ATOM   283  C  CE1   . PHE B 2 66  ? -6.529  41.977 121.741 1.00 10.88 ? 66  PHE A CE1   1 
ATOM   284  C  CE2   . PHE B 2 66  ? -5.344  42.025 119.625 1.00 10.38 ? 66  PHE A CE2   1 
ATOM   285  C  CZ    . PHE B 2 66  ? -5.351  41.797 121.007 1.00 10.32 ? 66  PHE A CZ    1 
ATOM   286  N  N     . LEU B 2 67  ? -7.871  45.867 118.475 1.00 11.45 ? 67  LEU A N     1 
ATOM   287  C  CA    . LEU B 2 67  ? -6.742  46.806 118.370 1.00 11.82 ? 67  LEU A CA    1 
ATOM   288  C  C     . LEU B 2 67  ? -7.131  48.191 118.901 1.00 12.79 ? 67  LEU A C     1 
ATOM   289  O  O     . LEU B 2 67  ? -6.324  48.877 119.546 1.00 13.16 ? 67  LEU A O     1 
ATOM   290  C  CB    . LEU B 2 67  ? -6.324  46.965 116.904 1.00 9.53  ? 67  LEU A CB    1 
ATOM   291  C  CG    . LEU B 2 67  ? -5.533  45.770 116.367 1.00 7.45  ? 67  LEU A CG    1 
ATOM   292  C  CD1   . LEU B 2 67  ? -5.150  45.922 114.892 1.00 5.52  ? 67  LEU A CD1   1 
ATOM   293  C  CD2   . LEU B 2 67  ? -4.219  45.539 117.114 1.00 4.04  ? 67  LEU A CD2   1 
ATOM   294  N  N     . LYS B 2 68  ? -8.366  48.556 118.611 1.00 13.07 ? 68  LYS A N     1 
ATOM   295  C  CA    . LYS B 2 68  ? -8.926  49.866 118.981 1.00 13.23 ? 68  LYS A CA    1 
ATOM   296  C  C     . LYS B 2 68  ? -9.047  50.018 120.501 1.00 13.62 ? 68  LYS A C     1 
ATOM   297  O  O     . LYS B 2 68  ? -8.660  51.044 121.078 1.00 13.86 ? 68  LYS A O     1 
ATOM   298  C  CB    . LYS B 2 68  ? -10.306 50.040 118.352 1.00 11.63 ? 68  LYS A CB    1 
ATOM   299  C  CG    . LYS B 2 68  ? -10.248 50.123 116.825 1.00 11.24 ? 68  LYS A CG    1 
ATOM   300  C  CD    . LYS B 2 68  ? -11.175 51.191 116.246 1.00 11.00 ? 68  LYS A CD    1 
ATOM   301  C  CE    . LYS B 2 68  ? -12.387 50.597 115.527 1.00 10.57 ? 68  LYS A CE    1 
ATOM   302  N  NZ    . LYS B 2 68  ? -12.851 51.422 114.403 1.00 9.68  ? 68  LYS A NZ    1 
ATOM   303  N  N     . CYS B 2 69  ? -9.587  49.003 121.146 1.00 14.02 ? 69  CYS A N     1 
ATOM   304  C  CA    . CYS B 2 69  ? -9.758  49.048 122.602 1.00 13.85 ? 69  CYS A CA    1 
ATOM   305  C  C     . CYS B 2 69  ? -8.413  48.925 123.304 1.00 12.92 ? 69  CYS A C     1 
ATOM   306  O  O     . CYS B 2 69  ? -8.174  49.557 124.343 1.00 14.08 ? 69  CYS A O     1 
ATOM   307  C  CB    . CYS B 2 69  ? -10.632 47.908 123.117 1.00 16.97 ? 69  CYS A CB    1 
ATOM   308  S  SG    . CYS B 2 69  ? -10.958 48.107 124.933 1.00 23.87 ? 69  CYS A SG    1 
ATOM   309  N  N     . ALA B 2 70  ? -7.582  48.117 122.699 1.00 11.30 ? 70  ALA A N     1 
ATOM   310  C  CA    . ALA B 2 70  ? -6.254  47.816 123.218 1.00 11.06 ? 70  ALA A CA    1 
ATOM   311  C  C     . ALA B 2 70  ? -5.353  49.057 123.262 1.00 12.10 ? 70  ALA A C     1 
ATOM   312  O  O     . ALA B 2 70  ? -4.525  49.212 124.168 1.00 12.77 ? 70  ALA A O     1 
ATOM   313  C  CB    . ALA B 2 70  ? -5.569  46.775 122.329 1.00 9.06  ? 70  ALA A CB    1 
ATOM   314  N  N     . PHE B 2 71  ? -5.514  49.961 122.298 1.00 11.82 ? 71  PHE A N     1 
ATOM   315  C  CA    . PHE B 2 71  ? -4.581  51.103 122.201 1.00 11.51 ? 71  PHE A CA    1 
ATOM   316  C  C     . PHE B 2 71  ? -5.227  52.505 122.196 1.00 11.82 ? 71  PHE A C     1 
ATOM   317  O  O     . PHE B 2 71  ? -4.651  53.476 122.702 1.00 12.34 ? 71  PHE A O     1 
ATOM   318  C  CB    . PHE B 2 71  ? -3.751  50.981 120.928 1.00 11.92 ? 71  PHE A CB    1 
ATOM   319  C  CG    . PHE B 2 71  ? -2.869  49.733 120.940 1.00 11.52 ? 71  PHE A CG    1 
ATOM   320  C  CD1   . PHE B 2 71  ? -1.794  49.647 121.833 1.00 11.09 ? 71  PHE A CD1   1 
ATOM   321  C  CD2   . PHE B 2 71  ? -3.142  48.676 120.066 1.00 11.58 ? 71  PHE A CD2   1 
ATOM   322  C  CE1   . PHE B 2 71  ? -0.989  48.502 121.849 1.00 12.91 ? 71  PHE A CE1   1 
ATOM   323  C  CE2   . PHE B 2 71  ? -2.338  47.531 120.082 1.00 11.78 ? 71  PHE A CE2   1 
ATOM   324  C  CZ    . PHE B 2 71  ? -1.261  47.444 120.974 1.00 12.62 ? 71  PHE A CZ    1 
ATOM   325  N  N     . ALA B 2 72  ? -6.407  52.665 121.631 1.00 11.76 ? 72  ALA A N     1 
ATOM   326  C  CA    . ALA B 2 72  ? -7.019  54.015 121.572 1.00 11.75 ? 72  ALA A CA    1 
ATOM   327  C  C     . ALA B 2 72  ? -8.433  54.023 122.144 1.00 12.52 ? 72  ALA A C     1 
ATOM   328  O  O     . ALA B 2 72  ? -9.406  54.322 121.433 1.00 12.81 ? 72  ALA A O     1 
ATOM   329  C  CB    . ALA B 2 72  ? -7.078  54.509 120.129 1.00 10.81 ? 72  ALA A CB    1 
ATOM   330  N  N     . PRO B 2 73  ? -8.607  53.709 123.429 1.00 13.08 ? 73  PRO A N     1 
ATOM   331  C  CA    . PRO B 2 73  ? -9.923  53.697 124.036 1.00 12.76 ? 73  PRO A CA    1 
ATOM   332  C  C     . PRO B 2 73  ? -10.575 55.062 123.969 1.00 12.52 ? 73  PRO A C     1 
ATOM   333  O  O     . PRO B 2 73  ? -11.742 55.166 123.478 1.00 13.03 ? 73  PRO A O     1 
ATOM   334  C  CB    . PRO B 2 73  ? -9.659  53.281 125.465 1.00 12.71 ? 73  PRO A CB    1 
ATOM   335  C  CG    . PRO B 2 73  ? -8.160  53.067 125.620 1.00 13.29 ? 73  PRO A CG    1 
ATOM   336  C  CD    . PRO B 2 73  ? -7.496  53.348 124.310 1.00 13.25 ? 73  PRO A CD    1 
ATOM   337  N  N     . PRO B 2 74  ? -9.910  56.127 124.440 1.00 12.60 ? 74  PRO A N     1 
ATOM   338  C  CA    . PRO B 2 74  ? -10.492 57.474 124.476 1.00 12.78 ? 74  PRO A CA    1 
ATOM   339  C  C     . PRO B 2 74  ? -10.819 58.099 123.116 1.00 13.55 ? 74  PRO A C     1 
ATOM   340  O  O     . PRO B 2 74  ? -11.372 59.243 123.078 1.00 14.53 ? 74  PRO A O     1 
ATOM   341  C  CB    . PRO B 2 74  ? -9.421  58.318 125.129 1.00 12.18 ? 74  PRO A CB    1 
ATOM   342  C  CG    . PRO B 2 74  ? -8.231  57.417 125.430 1.00 12.44 ? 74  PRO A CG    1 
ATOM   343  C  CD    . PRO B 2 74  ? -8.547  56.027 124.974 1.00 12.78 ? 74  PRO A CD    1 
ATOM   344  N  N     . ASP B 2 75  ? -10.531 57.419 122.011 1.00 13.00 ? 75  ASP A N     1 
ATOM   345  C  CA    . ASP B 2 75  ? -10.703 58.031 120.656 1.00 13.00 ? 75  ASP A CA    1 
ATOM   346  C  C     . ASP B 2 75  ? -12.073 57.760 119.980 1.00 13.00 ? 75  ASP A C     1 
ATOM   347  O  O     . ASP B 2 75  ? -12.467 58.454 119.030 1.00 14.00 ? 75  ASP A O     1 
ATOM   348  C  CB    . ASP B 2 75  ? -9.627  57.516 119.701 1.00 15.00 ? 75  ASP A CB    1 
ATOM   349  C  CG    . ASP B 2 75  ? -8.209  57.822 120.188 1.00 19.00 ? 75  ASP A CG    1 
ATOM   350  O  OD1   . ASP B 2 75  ? -8.031  58.497 121.273 1.00 20.00 ? 75  ASP A OD1   1 
ATOM   351  O  OD2   . ASP B 2 75  ? -7.191  57.401 119.517 1.00 20.00 ? 75  ASP A OD2   1 
ATOM   352  N  N     . PHE B 2 76  ? -12.796 56.761 120.453 1.00 12.35 ? 76  PHE A N     1 
ATOM   353  C  CA    . PHE B 2 76  ? -14.117 56.396 119.873 1.00 13.49 ? 76  PHE A CA    1 
ATOM   354  C  C     . PHE B 2 76  ? -15.194 56.846 120.824 1.00 14.70 ? 76  PHE A C     1 
ATOM   355  O  O     . PHE B 2 76  ? -14.990 56.808 122.050 1.00 16.35 ? 76  PHE A O     1 
ATOM   356  C  CB    . PHE B 2 76  ? -14.104 54.904 119.594 1.00 11.47 ? 76  PHE A CB    1 
ATOM   357  C  CG    . PHE B 2 76  ? -12.829 54.521 118.844 1.00 10.05 ? 76  PHE A CG    1 
ATOM   358  C  CD1   . PHE B 2 76  ? -12.729 54.770 117.469 1.00 10.53 ? 76  PHE A CD1   1 
ATOM   359  C  CD2   . PHE B 2 76  ? -11.755 53.945 119.532 1.00 10.75 ? 76  PHE A CD2   1 
ATOM   360  C  CE1   . PHE B 2 76  ? -11.554 54.442 116.783 1.00 11.12 ? 76  PHE A CE1   1 
ATOM   361  C  CE2   . PHE B 2 76  ? -10.580 53.617 118.845 1.00 11.42 ? 76  PHE A CE2   1 
ATOM   362  C  CZ    . PHE B 2 76  ? -10.480 53.866 117.470 1.00 11.22 ? 76  PHE A CZ    1 
ATOM   363  N  N     . ASN B 2 77  ? -16.323 57.261 120.267 1.00 14.50 ? 77  ASN A N     1 
ATOM   364  C  CA    . ASN B 2 77  ? -17.481 57.754 121.035 1.00 14.24 ? 77  ASN A CA    1 
ATOM   365  C  C     . ASN B 2 77  ? -18.156 56.606 121.765 1.00 15.44 ? 77  ASN A C     1 
ATOM   366  O  O     . ASN B 2 77  ? -19.172 56.802 122.454 1.00 16.02 ? 77  ASN A O     1 
ATOM   367  C  CB    . ASN B 2 77  ? -18.376 58.631 120.171 1.00 11.70 ? 77  ASN A CB    1 
ATOM   368  C  CG    . ASN B 2 77  ? -19.863 58.475 120.421 1.00 12.58 ? 77  ASN A CG    1 
ATOM   369  O  OD1   . ASN B 2 77  ? -20.486 59.246 121.176 1.00 11.90 ? 77  ASN A OD1   1 
ATOM   370  N  ND2   . ASN B 2 77  ? -20.445 57.443 119.805 1.00 14.18 ? 77  ASN A ND2   1 
ATOM   371  N  N     . THR B 2 78  ? -17.565 55.435 121.634 1.00 16.08 ? 78  THR A N     1 
ATOM   372  C  CA    . THR B 2 78  ? -18.080 54.197 122.267 1.00 16.01 ? 78  THR A CA    1 
ATOM   373  C  C     . THR B 2 78  ? -17.113 53.035 122.041 1.00 16.56 ? 78  THR A C     1 
ATOM   374  O  O     . THR B 2 78  ? -16.682 52.738 120.908 1.00 17.54 ? 78  THR A O     1 
ATOM   375  C  CB    . THR B 2 78  ? -19.532 53.935 121.717 1.00 16.92 ? 78  THR A CB    1 
ATOM   376  O  OG1   . THR B 2 78  ? -20.400 53.893 122.891 1.00 19.01 ? 78  THR A OG1   1 
ATOM   377  C  CG2   . THR B 2 78  ? -19.600 52.694 120.832 1.00 16.65 ? 78  THR A CG2   1 
ATOM   378  N  N     . ASP B 2 79  ? -16.727 52.403 123.141 1.00 15.70 ? 79  ASP A N     1 
ATOM   379  C  CA    . ASP B 2 79  ? -15.813 51.292 123.233 1.00 15.77 ? 79  ASP A CA    1 
ATOM   380  C  C     . ASP B 2 79  ? -16.170 50.211 122.196 1.00 15.30 ? 79  ASP A C     1 
ATOM   381  O  O     . ASP B 2 79  ? -17.123 49.466 122.432 1.00 16.33 ? 79  ASP A O     1 
ATOM   382  C  CB    . ASP B 2 79  ? -15.781 50.644 124.628 1.00 19.83 ? 79  ASP A CB    1 
ATOM   383  C  CG    . ASP B 2 79  ? -14.495 49.823 124.736 1.00 24.37 ? 79  ASP A CG    1 
ATOM   384  O  OD1   . ASP B 2 79  ? -14.155 49.053 123.813 1.00 24.21 ? 79  ASP A OD1   1 
ATOM   385  O  OD2   . ASP B 2 79  ? -13.842 50.041 125.780 1.00 26.16 ? 79  ASP A OD2   1 
ATOM   386  N  N     . PRO B 2 80  ? -15.365 50.198 121.147 1.00 14.56 ? 80  PRO A N     1 
ATOM   387  C  CA    . PRO B 2 80  ? -15.535 49.254 120.035 1.00 14.34 ? 80  PRO A CA    1 
ATOM   388  C  C     . PRO B 2 80  ? -15.139 47.842 120.401 1.00 14.96 ? 80  PRO A C     1 
ATOM   389  O  O     . PRO B 2 80  ? -15.606 46.868 119.793 1.00 15.11 ? 80  PRO A O     1 
ATOM   390  C  CB    . PRO B 2 80  ? -14.617 49.816 118.944 1.00 13.97 ? 80  PRO A CB    1 
ATOM   391  C  CG    . PRO B 2 80  ? -13.489 50.430 119.764 1.00 13.99 ? 80  PRO A CG    1 
ATOM   392  C  CD    . PRO B 2 80  ? -14.214 51.108 120.931 1.00 14.15 ? 80  PRO A CD    1 
ATOM   393  N  N     . GLY B 2 81  ? -14.253 47.749 121.392 1.00 15.09 ? 81  GLY A N     1 
ATOM   394  C  CA    . GLY B 2 81  ? -13.760 46.435 121.861 1.00 14.48 ? 81  GLY A CA    1 
ATOM   395  C  C     . GLY B 2 81  ? -14.914 45.440 121.997 1.00 14.58 ? 81  GLY A C     1 
ATOM   396  O  O     . GLY B 2 81  ? -15.944 45.763 122.587 1.00 15.76 ? 81  GLY A O     1 
ATOM   397  N  N     . LYS B 2 82  ? -14.701 44.254 121.449 1.00 14.76 ? 82  LYS A N     1 
ATOM   398  C  CA    . LYS B 2 82  ? -15.660 43.158 121.509 1.00 15.38 ? 82  LYS A CA    1 
ATOM   399  C  C     . LYS B 2 82  ? -15.039 41.779 121.732 1.00 15.55 ? 82  LYS A C     1 
ATOM   400  O  O     . LYS B 2 82  ? -15.609 40.816 121.142 1.00 17.08 ? 82  LYS A O     1 
ATOM   401  C  CB    . LYS B 2 82  ? -16.562 43.041 120.275 1.00 17.41 ? 82  LYS A CB    1 
ATOM   402  C  CG    . LYS B 2 82  ? -15.814 43.300 118.963 1.00 17.68 ? 82  LYS A CG    1 
ATOM   403  C  CD    . LYS B 2 82  ? -16.677 44.252 118.117 1.00 17.54 ? 82  LYS A CD    1 
ATOM   404  C  CE    . LYS B 2 82  ? -17.715 43.454 117.344 1.00 18.91 ? 82  LYS A CE    1 
ATOM   405  N  NZ    . LYS B 2 82  ? -17.348 43.435 115.864 1.00 19.30 ? 82  LYS A NZ    1 
ATOM   406  N  N     . GLY B 2 83  ? -13.994 41.666 122.531 1.00 14.45 ? 83  GLY A N     1 
ATOM   407  C  CA    . GLY B 2 83  ? -13.358 40.372 122.836 1.00 13.06 ? 83  GLY A CA    1 
ATOM   408  C  C     . GLY B 2 83  ? -12.028 40.191 122.120 1.00 12.55 ? 83  GLY A C     1 
ATOM   409  O  O     . GLY B 2 83  ? -11.639 41.002 121.239 1.00 12.64 ? 83  GLY A O     1 
ATOM   410  N  N     . ILE B 2 84  ? -11.328 39.133 122.499 1.00 11.49 ? 84  ILE A N     1 
ATOM   411  C  CA    . ILE B 2 84  ? -10.023 38.788 121.929 1.00 10.53 ? 84  ILE A CA    1 
ATOM   412  C  C     . ILE B 2 84  ? -10.138 37.830 120.762 1.00 12.01 ? 84  ILE A C     1 
ATOM   413  O  O     . ILE B 2 84  ? -10.742 36.744 120.935 1.00 12.86 ? 84  ILE A O     1 
ATOM   414  C  CB    . ILE B 2 84  ? -9.154  38.170 123.088 1.00 6.56  ? 84  ILE A CB    1 
ATOM   415  C  CG1   . ILE B 2 84  ? -9.086  39.174 124.258 1.00 4.20  ? 84  ILE A CG1   1 
ATOM   416  C  CG2   . ILE B 2 84  ? -7.762  37.692 122.622 1.00 7.06  ? 84  ILE A CG2   1 
ATOM   417  C  CD1   . ILE B 2 84  ? -8.566  38.561 125.582 1.00 3.77  ? 84  ILE A CD1   1 
ATOM   418  N  N     . PRO B 2 85  ? -9.539  38.182 119.628 1.00 13.00 ? 85  PRO A N     1 
ATOM   419  C  CA    . PRO B 2 85  ? -9.558  37.375 118.403 1.00 14.35 ? 85  PRO A CA    1 
ATOM   420  C  C     . PRO B 2 85  ? -8.512  36.290 118.286 1.00 16.87 ? 85  PRO A C     1 
ATOM   421  O  O     . PRO B 2 85  ? -7.683  36.284 117.355 1.00 19.78 ? 85  PRO A O     1 
ATOM   422  C  CB    . PRO B 2 85  ? -9.377  38.447 117.317 1.00 13.49 ? 85  PRO A CB    1 
ATOM   423  C  CG    . PRO B 2 85  ? -8.349  39.350 117.950 1.00 13.46 ? 85  PRO A CG    1 
ATOM   424  C  CD    . PRO B 2 85  ? -8.825  39.458 119.402 1.00 13.23 ? 85  PRO A CD    1 
ATOM   425  N  N     . ASP B 2 86  ? -8.527  35.349 119.202 1.00 16.85 ? 86  ASP A N     1 
ATOM   426  C  CA    . ASP B 2 86  ? -7.586  34.227 119.275 1.00 16.07 ? 86  ASP A CA    1 
ATOM   427  C  C     . ASP B 2 86  ? -8.367  32.928 119.163 1.00 16.50 ? 86  ASP A C     1 
ATOM   428  O  O     . ASP B 2 86  ? -9.606  32.978 119.061 1.00 17.92 ? 86  ASP A O     1 
ATOM   429  C  CB    . ASP B 2 86  ? -6.744  34.304 120.527 1.00 15.96 ? 86  ASP A CB    1 
ATOM   430  C  CG    . ASP B 2 86  ? -7.270  33.743 121.818 1.00 16.17 ? 86  ASP A CG    1 
ATOM   431  O  OD1   . ASP B 2 86  ? -8.491  33.575 121.948 1.00 17.11 ? 86  ASP A OD1   1 
ATOM   432  O  OD2   . ASP B 2 86  ? -6.468  33.469 122.751 1.00 17.01 ? 86  ASP A OD2   1 
ATOM   433  N  N     . ARG B 2 87  ? -7.677  31.814 119.225 1.00 15.15 ? 87  ARG A N     1 
ATOM   434  C  CA    . ARG B 2 87  ? -8.328  30.507 119.093 1.00 13.65 ? 87  ARG A CA    1 
ATOM   435  C  C     . ARG B 2 87  ? -9.504  30.236 119.990 1.00 12.70 ? 87  ARG A C     1 
ATOM   436  O  O     . ARG B 2 87  ? -10.504 29.606 119.553 1.00 13.76 ? 87  ARG A O     1 
ATOM   437  C  CB    . ARG B 2 87  ? -7.237  29.429 119.182 1.00 12.99 ? 87  ARG A CB    1 
ATOM   438  C  CG    . ARG B 2 87  ? -7.518  28.208 118.326 1.00 13.39 ? 87  ARG A CG    1 
ATOM   439  C  CD    . ARG B 2 87  ? -6.973  28.313 116.954 1.00 13.99 ? 87  ARG A CD    1 
ATOM   440  N  NE    . ARG B 2 87  ? -5.500  28.101 116.952 1.00 14.38 ? 87  ARG A NE    1 
ATOM   441  C  CZ    . ARG B 2 87  ? -4.974  27.740 115.759 1.00 15.37 ? 87  ARG A CZ    1 
ATOM   442  N  NH1   . ARG B 2 87  ? -5.845  27.551 114.753 1.00 15.50 ? 87  ARG A NH1   1 
ATOM   443  N  NH2   . ARG B 2 87  ? -3.686  27.551 115.600 1.00 16.45 ? 87  ARG A NH2   1 
ATOM   444  N  N     . PHE B 2 88  ? -9.489  30.609 121.242 1.00 11.24 ? 88  PHE A N     1 
ATOM   445  C  CA    . PHE B 2 88  ? -10.606 30.368 122.168 1.00 10.29 ? 88  PHE A CA    1 
ATOM   446  C  C     . PHE B 2 88  ? -11.844 31.053 121.582 1.00 10.54 ? 88  PHE A C     1 
ATOM   447  O  O     . PHE B 2 88  ? -11.766 32.232 121.173 1.00 11.37 ? 88  PHE A O     1 
ATOM   448  C  CB    . PHE B 2 88  ? -10.343 30.857 123.586 1.00 8.19  ? 88  PHE A CB    1 
ATOM   449  C  CG    . PHE B 2 88  ? -11.499 30.778 124.531 1.00 8.45  ? 88  PHE A CG    1 
ATOM   450  C  CD1   . PHE B 2 88  ? -11.806 29.590 125.186 1.00 8.77  ? 88  PHE A CD1   1 
ATOM   451  C  CD2   . PHE B 2 88  ? -12.302 31.879 124.778 1.00 9.78  ? 88  PHE A CD2   1 
ATOM   452  C  CE1   . PHE B 2 88  ? -12.903 29.514 126.059 1.00 8.25  ? 88  PHE A CE1   1 
ATOM   453  C  CE2   . PHE B 2 88  ? -13.391 31.825 125.629 1.00 9.33  ? 88  PHE A CE2   1 
ATOM   454  C  CZ    . PHE B 2 88  ? -13.703 30.648 126.280 1.00 7.67  ? 88  PHE A CZ    1 
ATOM   455  N  N     . GLU B 2 89  ? -12.940 30.321 121.603 1.00 9.96  ? 89  GLU A N     1 
ATOM   456  C  CA    . GLU B 2 89  ? -14.218 30.827 121.113 1.00 10.13 ? 89  GLU A CA    1 
ATOM   457  C  C     . GLU B 2 89  ? -15.405 30.455 121.980 1.00 10.70 ? 89  GLU A C     1 
ATOM   458  O  O     . GLU B 2 89  ? -16.539 30.428 121.417 1.00 12.62 ? 89  GLU A O     1 
ATOM   459  C  CB    . GLU B 2 89  ? -14.521 30.254 119.732 1.00 9.92  ? 89  GLU A CB    1 
ATOM   460  C  CG    . GLU B 2 89  ? -13.564 30.649 118.602 1.00 10.80 ? 89  GLU A CG    1 
ATOM   461  C  CD    . GLU B 2 89  ? -14.207 30.460 117.245 1.00 11.38 ? 89  GLU A CD    1 
ATOM   462  O  OE1   . GLU B 2 89  ? -15.350 30.998 117.235 1.00 12.71 ? 89  GLU A OE1   1 
ATOM   463  O  OE2   . GLU B 2 89  ? -13.669 29.839 116.347 1.00 11.08 ? 89  GLU A OE2   1 
ATOM   464  N  N     . GLY B 2 90  ? -15.200 30.204 123.253 1.00 10.71 ? 90  GLY A N     1 
ATOM   465  C  CA    . GLY B 2 90  ? -16.241 29.804 124.197 1.00 10.07 ? 90  GLY A CA    1 
ATOM   466  C  C     . GLY B 2 90  ? -17.029 30.973 124.746 1.00 10.65 ? 90  GLY A C     1 
ATOM   467  O  O     . GLY B 2 90  ? -16.789 32.120 124.348 1.00 10.54 ? 90  GLY A O     1 
ATOM   468  N  N     . LYS B 2 91  ? -17.950 30.660 125.647 1.00 10.48 ? 91  LYS A N     1 
ATOM   469  C  CA    . LYS B 2 91  ? -18.805 31.669 126.282 1.00 10.78 ? 91  LYS A CA    1 
ATOM   470  C  C     . LYS B 2 91  ? -17.941 32.658 127.062 1.00 12.06 ? 91  LYS A C     1 
ATOM   471  O  O     . LYS B 2 91  ? -16.913 32.309 127.659 1.00 12.96 ? 91  LYS A O     1 
ATOM   472  C  CB    . LYS B 2 91  ? -19.898 31.139 127.172 1.00 7.92  ? 91  LYS A CB    1 
ATOM   473  C  CG    . LYS B 2 91  ? -21.298 31.247 126.587 1.00 5.38  ? 91  LYS A CG    1 
ATOM   474  C  CD    . LYS B 2 91  ? -22.038 32.469 127.110 1.00 2.77  ? 91  LYS A CD    1 
ATOM   475  C  CE    . LYS B 2 91  ? -23.041 32.979 126.089 1.00 5.45  ? 91  LYS A CE    1 
ATOM   476  N  NZ    . LYS B 2 91  ? -24.309 32.209 126.050 1.00 9.57  ? 91  LYS A NZ    1 
ATOM   477  N  N     . VAL B 2 92  ? -18.447 33.883 127.053 1.00 12.56 ? 92  VAL A N     1 
ATOM   478  C  CA    . VAL B 2 92  ? -17.722 35.003 127.689 1.00 12.17 ? 92  VAL A CA    1 
ATOM   479  C  C     . VAL B 2 92  ? -18.605 36.242 127.745 1.00 12.51 ? 92  VAL A C     1 
ATOM   480  O  O     . VAL B 2 92  ? -19.426 36.455 126.816 1.00 12.98 ? 92  VAL A O     1 
ATOM   481  C  CB    . VAL B 2 92  ? -16.545 35.215 126.662 1.00 10.07 ? 92  VAL A CB    1 
ATOM   482  C  CG1   . VAL B 2 92  ? -16.734 36.519 125.889 1.00 7.88  ? 92  VAL A CG1   1 
ATOM   483  C  CG2   . VAL B 2 92  ? -15.161 35.041 127.177 1.00 13.24 ? 92  VAL A CG2   1 
ATOM   484  N  N     . VAL B 2 93  ? -18.455 37.035 128.786 1.00 12.32 ? 93  VAL A N     1 
ATOM   485  C  CA    . VAL B 2 93  ? -19.146 38.327 128.880 1.00 12.41 ? 93  VAL A CA    1 
ATOM   486  C  C     . VAL B 2 93  ? -17.932 39.291 128.868 1.00 12.47 ? 93  VAL A C     1 
ATOM   487  O  O     . VAL B 2 93  ? -16.898 38.885 129.423 1.00 12.26 ? 93  VAL A O     1 
ATOM   488  C  CB    . VAL B 2 93  ? -20.095 38.573 130.018 1.00 11.81 ? 93  VAL A CB    1 
ATOM   489  C  CG1   . VAL B 2 93  ? -20.990 37.390 130.343 1.00 9.11  ? 93  VAL A CG1   1 
ATOM   490  C  CG2   . VAL B 2 93  ? -19.381 39.119 131.249 1.00 10.56 ? 93  VAL A CG2   1 
ATOM   491  N  N     . THR B 2 94  ? -18.057 40.400 128.182 1.00 12.58 ? 94  THR A N     1 
ATOM   492  C  CA    . THR B 2 94  ? -16.921 41.356 128.136 1.00 13.18 ? 94  THR A CA    1 
ATOM   493  C  C     . THR B 2 94  ? -17.315 42.491 129.081 1.00 14.11 ? 94  THR A C     1 
ATOM   494  O  O     . THR B 2 94  ? -18.503 42.848 129.170 1.00 15.73 ? 94  THR A O     1 
ATOM   495  C  CB    . THR B 2 94  ? -16.487 41.812 126.723 1.00 11.05 ? 94  THR A CB    1 
ATOM   496  O  OG1   . THR B 2 94  ? -16.892 40.808 125.741 1.00 13.62 ? 94  THR A OG1   1 
ATOM   497  C  CG2   . THR B 2 94  ? -14.957 42.056 126.604 1.00 9.85  ? 94  THR A CG2   1 
ATOM   498  N  N     . ARG B 2 95  ? -16.349 42.970 129.821 1.00 13.89 ? 95  ARG A N     1 
ATOM   499  C  CA    . ARG B 2 95  ? -16.581 44.052 130.802 1.00 13.44 ? 95  ARG A CA    1 
ATOM   500  C  C     . ARG B 2 95  ? -15.674 45.190 130.344 1.00 12.93 ? 95  ARG A C     1 
ATOM   501  O  O     . ARG B 2 95  ? -14.500 44.936 130.048 1.00 13.32 ? 95  ARG A O     1 
ATOM   502  C  CB    . ARG B 2 95  ? -16.149 43.648 132.190 1.00 14.94 ? 95  ARG A CB    1 
ATOM   503  C  CG    . ARG B 2 95  ? -17.123 43.833 133.306 1.00 15.34 ? 95  ARG A CG    1 
ATOM   504  C  CD    . ARG B 2 95  ? -17.687 45.200 133.399 1.00 13.79 ? 95  ARG A CD    1 
ATOM   505  N  NE    . ARG B 2 95  ? -18.946 45.148 134.140 1.00 13.64 ? 95  ARG A NE    1 
ATOM   506  C  CZ    . ARG B 2 95  ? -19.187 45.673 135.344 1.00 13.41 ? 95  ARG A CZ    1 
ATOM   507  N  NH1   . ARG B 2 95  ? -18.214 46.355 135.968 1.00 12.30 ? 95  ARG A NH1   1 
ATOM   508  N  NH2   . ARG B 2 95  ? -20.409 45.556 135.905 1.00 13.75 ? 95  ARG A NH2   1 
ATOM   509  N  N     . LYS B 2 96  ? -16.273 46.344 130.303 1.00 12.11 ? 96  LYS A N     1 
ATOM   510  C  CA    . LYS B 2 96  ? -15.459 47.526 129.878 1.00 12.04 ? 96  LYS A CA    1 
ATOM   511  C  C     . LYS B 2 96  ? -15.500 48.478 131.072 1.00 11.61 ? 96  LYS A C     1 
ATOM   512  O  O     . LYS B 2 96  ? -16.430 49.270 131.261 1.00 11.78 ? 96  LYS A O     1 
ATOM   513  C  CB    . LYS B 2 96  ? -15.933 48.068 128.566 1.00 13.37 ? 96  LYS A CB    1 
ATOM   514  C  CG    . LYS B 2 96  ? -16.300 46.993 127.539 1.00 14.95 ? 96  LYS A CG    1 
ATOM   515  C  CD    . LYS B 2 96  ? -15.193 46.844 126.473 1.00 15.20 ? 96  LYS A CD    1 
ATOM   516  C  CE    . LYS B 2 96  ? -15.899 46.893 125.102 1.00 14.87 ? 96  LYS A CE    1 
ATOM   517  N  NZ    . LYS B 2 96  ? -17.347 47.244 125.403 1.00 16.74 ? 96  LYS A NZ    1 
ATOM   518  N  N     . ASP B 2 97  ? -14.500 48.297 131.901 1.00 10.71 ? 97  ASP A N     1 
ATOM   519  C  CA    . ASP B 2 97  ? -14.299 49.031 133.130 1.00 11.10 ? 97  ASP A CA    1 
ATOM   520  C  C     . ASP B 2 97  ? -13.725 50.415 132.860 1.00 10.57 ? 97  ASP A C     1 
ATOM   521  O  O     . ASP B 2 97  ? -12.660 50.504 132.236 1.00 12.15 ? 97  ASP A O     1 
ATOM   522  C  CB    . ASP B 2 97  ? -13.355 48.240 134.068 1.00 14.46 ? 97  ASP A CB    1 
ATOM   523  C  CG    . ASP B 2 97  ? -14.003 46.965 134.594 1.00 17.17 ? 97  ASP A CG    1 
ATOM   524  O  OD1   . ASP B 2 97  ? -15.242 46.911 134.746 1.00 17.65 ? 97  ASP A OD1   1 
ATOM   525  O  OD2   . ASP B 2 97  ? -13.204 46.014 134.866 1.00 20.48 ? 97  ASP A OD2   1 
ATOM   526  N  N     . VAL B 2 98  ? -14.393 51.428 133.338 1.00 9.37  ? 98  VAL A N     1 
ATOM   527  C  CA    . VAL B 2 98  ? -13.917 52.812 133.196 1.00 8.39  ? 98  VAL A CA    1 
ATOM   528  C  C     . VAL B 2 98  ? -14.144 53.498 134.560 1.00 8.20  ? 98  VAL A C     1 
ATOM   529  O  O     . VAL B 2 98  ? -15.234 53.327 135.145 1.00 7.92  ? 98  VAL A O     1 
ATOM   530  C  CB    . VAL B 2 98  ? -14.562 53.554 132.020 1.00 7.61  ? 98  VAL A CB    1 
ATOM   531  C  CG1   . VAL B 2 98  ? -14.002 54.949 131.755 1.00 8.20  ? 98  VAL A CG1   1 
ATOM   532  C  CG2   . VAL B 2 98  ? -14.496 52.717 130.762 1.00 8.36  ? 98  VAL A CG2   1 
ATOM   533  N  N     . LEU B 2 99  ? -13.119 54.185 134.989 1.00 7.64  ? 99  LEU A N     1 
ATOM   534  C  CA    . LEU B 2 99  ? -13.056 54.970 136.185 1.00 7.52  ? 99  LEU A CA    1 
ATOM   535  C  C     . LEU B 2 99  ? -12.583 56.388 135.800 1.00 7.99  ? 99  LEU A C     1 
ATOM   536  O  O     . LEU B 2 99  ? -11.610 56.557 135.051 1.00 8.51  ? 99  LEU A O     1 
ATOM   537  C  CB    . LEU B 2 99  ? -12.116 54.368 137.247 1.00 6.43  ? 99  LEU A CB    1 
ATOM   538  C  CG    . LEU B 2 99  ? -12.122 55.241 138.497 1.00 5.97  ? 99  LEU A CG    1 
ATOM   539  C  CD1   . LEU B 2 99  ? -13.454 55.171 139.246 1.00 5.45  ? 99  LEU A CD1   1 
ATOM   540  C  CD2   . LEU B 2 99  ? -11.036 54.872 139.494 1.00 5.09  ? 99  LEU A CD2   1 
ATOM   541  N  N     . ASN B 2 100 ? -13.323 57.359 136.300 1.00 8.48  ? 100 ASN A N     1 
ATOM   542  C  CA    . ASN B 2 100 ? -13.028 58.802 136.146 1.00 8.82  ? 100 ASN A CA    1 
ATOM   543  C  C     . ASN B 2 100 ? -12.899 59.359 137.548 1.00 9.11  ? 100 ASN A C     1 
ATOM   544  O  O     . ASN B 2 100 ? -13.789 59.193 138.387 1.00 8.65  ? 100 ASN A O     1 
ATOM   545  C  CB    . ASN B 2 100 ? -14.213 59.546 135.511 1.00 9.30  ? 100 ASN A CB    1 
ATOM   546  C  CG    . ASN B 2 100 ? -14.142 59.664 133.988 1.00 12.03 ? 100 ASN A CG    1 
ATOM   547  O  OD1   . ASN B 2 100 ? -14.353 58.679 133.285 1.00 15.13 ? 100 ASN A OD1   1 
ATOM   548  N  ND2   . ASN B 2 100 ? -13.867 60.829 133.430 1.00 12.34 ? 100 ASN A ND2   1 
ATOM   549  N  N     . GLN B 2 101 ? -11.816 60.019 137.858 1.00 10.18 ? 101 GLN A N     1 
ATOM   550  C  CA    . GLN B 2 101 ? -11.697 60.511 139.224 1.00 11.54 ? 101 GLN A CA    1 
ATOM   551  C  C     . GLN B 2 101 ? -10.824 61.739 139.364 1.00 12.09 ? 101 GLN A C     1 
ATOM   552  O  O     . GLN B 2 101 ? -9.623  61.707 139.055 1.00 13.28 ? 101 GLN A O     1 
ATOM   553  C  CB    . GLN B 2 101 ? -11.099 59.441 140.130 1.00 12.15 ? 101 GLN A CB    1 
ATOM   554  C  CG    . GLN B 2 101 ? -11.263 59.780 141.611 1.00 13.90 ? 101 GLN A CG    1 
ATOM   555  C  CD    . GLN B 2 101 ? -11.151 58.561 142.522 1.00 16.50 ? 101 GLN A CD    1 
ATOM   556  O  OE1   . GLN B 2 101 ? -10.048 58.199 142.926 1.00 17.82 ? 101 GLN A OE1   1 
ATOM   557  N  NE2   . GLN B 2 101 ? -12.236 57.899 142.876 1.00 16.87 ? 101 GLN A NE2   1 
ATOM   558  N  N     . SER B 2 102 ? -11.488 62.771 139.844 1.00 11.74 ? 102 SER A N     1 
ATOM   559  C  CA    . SER B 2 102 ? -10.838 64.023 140.190 1.00 11.47 ? 102 SER A CA    1 
ATOM   560  C  C     . SER B 2 102 ? -9.847  63.670 141.281 1.00 11.86 ? 102 SER A C     1 
ATOM   561  O  O     . SER B 2 102 ? -10.134 62.874 142.180 1.00 12.58 ? 102 SER A O     1 
ATOM   562  C  CB    . SER B 2 102 ? -11.883 65.024 140.685 1.00 9.55  ? 102 SER A CB    1 
ATOM   563  O  OG    . SER B 2 102 ? -13.171 64.421 140.677 1.00 13.39 ? 102 SER A OG    1 
ATOM   564  N  N     . ILE B 2 103 ? -8.681  64.233 141.218 1.00 11.65 ? 103 ILE A N     1 
ATOM   565  C  CA    . ILE B 2 103 ? -7.661  63.877 142.192 1.00 11.62 ? 103 ILE A CA    1 
ATOM   566  C  C     . ILE B 2 103 ? -6.796  65.079 142.455 1.00 12.16 ? 103 ILE A C     1 
ATOM   567  O  O     . ILE B 2 103 ? -6.392  65.784 141.506 1.00 12.66 ? 103 ILE A O     1 
ATOM   568  C  CB    . ILE B 2 103 ? -6.923  62.651 141.626 1.00 11.33 ? 103 ILE A CB    1 
ATOM   569  C  CG1   . ILE B 2 103 ? -5.755  62.161 142.475 1.00 13.29 ? 103 ILE A CG1   1 
ATOM   570  C  CG2   . ILE B 2 103 ? -6.347  62.884 140.231 1.00 11.62 ? 103 ILE A CG2   1 
ATOM   571  C  CD1   . ILE B 2 103 ? -5.310  60.739 142.104 1.00 15.35 ? 103 ILE A CD1   1 
ATOM   572  N  N     . ASN B 2 104 ? -6.563  65.354 143.738 1.00 11.28 ? 104 ASN A N     1 
ATOM   573  C  CA    . ASN B 2 104 ? -5.717  66.499 144.113 1.00 10.74 ? 104 ASN A CA    1 
ATOM   574  C  C     . ASN B 2 104 ? -4.389  65.944 144.633 1.00 11.19 ? 104 ASN A C     1 
ATOM   575  O  O     . ASN B 2 104 ? -4.445  65.450 145.781 1.00 12.14 ? 104 ASN A O     1 
ATOM   576  C  CB    . ASN B 2 104 ? -6.364  67.297 145.227 1.00 12.78 ? 104 ASN A CB    1 
ATOM   577  C  CG    . ASN B 2 104 ? -7.460  68.174 144.654 1.00 17.18 ? 104 ASN A CG    1 
ATOM   578  O  OD1   . ASN B 2 104 ? -8.495  68.221 145.345 1.00 16.90 ? 104 ASN A OD1   1 
ATOM   579  N  ND2   . ASN B 2 104 ? -7.192  68.772 143.494 1.00 19.18 ? 104 ASN A ND2   1 
ATOM   580  N  N     . PHE B 2 105 ? -3.337  66.054 143.875 1.00 10.94 ? 105 PHE A N     1 
ATOM   581  C  CA    . PHE B 2 105 ? -2.058  65.518 144.385 1.00 11.57 ? 105 PHE A CA    1 
ATOM   582  C  C     . PHE B 2 105 ? -1.557  66.422 145.515 1.00 12.80 ? 105 PHE A C     1 
ATOM   583  O  O     . PHE B 2 105 ? -1.449  67.655 145.393 1.00 13.38 ? 105 PHE A O     1 
ATOM   584  C  CB    . PHE B 2 105 ? -1.061  65.227 143.276 1.00 9.02  ? 105 PHE A CB    1 
ATOM   585  C  CG    . PHE B 2 105 ? -1.575  64.258 142.240 1.00 7.31  ? 105 PHE A CG    1 
ATOM   586  C  CD1   . PHE B 2 105 ? -2.328  64.727 141.155 1.00 6.62  ? 105 PHE A CD1   1 
ATOM   587  C  CD2   . PHE B 2 105 ? -1.305  62.898 142.346 1.00 6.47  ? 105 PHE A CD2   1 
ATOM   588  C  CE1   . PHE B 2 105 ? -2.819  63.856 140.205 1.00 6.13  ? 105 PHE A CE1   1 
ATOM   589  C  CE2   . PHE B 2 105 ? -1.778  61.998 141.386 1.00 7.29  ? 105 PHE A CE2   1 
ATOM   590  C  CZ    . PHE B 2 105 ? -2.544  62.495 140.326 1.00 7.47  ? 105 PHE A CZ    1 
ATOM   591  N  N     . THR B 2 106 ? -1.273  65.729 146.640 1.00 12.87 ? 106 THR A N     1 
ATOM   592  C  CA    . THR B 2 106 ? -0.748  66.432 147.816 1.00 12.48 ? 106 THR A CA    1 
ATOM   593  C  C     . THR B 2 106 ? 0.623   67.011 147.452 1.00 11.86 ? 106 THR A C     1 
ATOM   594  O  O     . THR B 2 106 ? 1.427   66.295 146.826 1.00 12.25 ? 106 THR A O     1 
ATOM   595  C  CB    . THR B 2 106 ? -0.584  65.532 149.090 1.00 12.54 ? 106 THR A CB    1 
ATOM   596  O  OG1   . THR B 2 106 ? -1.885  65.519 149.745 1.00 14.08 ? 106 THR A OG1   1 
ATOM   597  C  CG2   . THR B 2 106 ? 0.500   66.049 150.023 1.00 12.64 ? 106 THR A CG2   1 
ATOM   598  N  N     . ALA B 2 107 ? 0.818   68.237 147.881 1.00 11.57 ? 107 ALA A N     1 
ATOM   599  C  CA    . ALA B 2 107 ? 2.081   68.942 147.614 1.00 11.05 ? 107 ALA A CA    1 
ATOM   600  C  C     . ALA B 2 107 ? 3.203   68.425 148.497 1.00 11.17 ? 107 ALA A C     1 
ATOM   601  O  O     . ALA B 2 107 ? 2.980   67.892 149.592 1.00 11.64 ? 107 ALA A O     1 
ATOM   602  C  CB    . ALA B 2 107 ? 1.875   70.443 147.777 1.00 9.63  ? 107 ALA A CB    1 
ATOM   603  N  N     . ASN B 2 108 ? 4.417   68.598 148.000 1.00 11.51 ? 108 ASN A N     1 
ATOM   604  C  CA    . ASN B 2 108 ? 5.602   68.175 148.741 1.00 12.43 ? 108 ASN A CA    1 
ATOM   605  C  C     . ASN B 2 108 ? 5.604   66.668 149.010 1.00 12.27 ? 108 ASN A C     1 
ATOM   606  O  O     . ASN B 2 108 ? 6.167   66.205 150.014 1.00 13.11 ? 108 ASN A O     1 
ATOM   607  C  CB    . ASN B 2 108 ? 5.631   68.913 150.099 1.00 14.54 ? 108 ASN A CB    1 
ATOM   608  C  CG    . ASN B 2 108 ? 7.026   68.873 150.715 1.00 18.29 ? 108 ASN A CG    1 
ATOM   609  O  OD1   . ASN B 2 108 ? 7.949   68.333 150.099 1.00 19.53 ? 108 ASN A OD1   1 
ATOM   610  N  ND2   . ASN B 2 108 ? 7.238   69.412 151.897 1.00 22.08 ? 108 ASN A ND2   1 
ATOM   611  N  N     . ARG B 2 109 ? 4.976   65.945 148.104 1.00 11.94 ? 109 ARG A N     1 
ATOM   612  C  CA    . ARG B 2 109 ? 4.901   64.474 148.166 1.00 11.67 ? 109 ARG A CA    1 
ATOM   613  C  C     . ARG B 2 109 ? 4.949   63.880 146.760 1.00 11.44 ? 109 ARG A C     1 
ATOM   614  O  O     . ARG B 2 109 ? 4.498   64.501 145.789 1.00 10.94 ? 109 ARG A O     1 
ATOM   615  C  CB    . ARG B 2 109 ? 3.574   64.001 148.784 1.00 9.88  ? 109 ARG A CB    1 
ATOM   616  C  CG    . ARG B 2 109 ? 3.168   64.754 150.045 1.00 8.99  ? 109 ARG A CG    1 
ATOM   617  C  CD    . ARG B 2 109 ? 3.831   64.232 151.319 1.00 11.52 ? 109 ARG A CD    1 
ATOM   618  N  NE    . ARG B 2 109 ? 4.177   62.805 151.308 1.00 12.38 ? 109 ARG A NE    1 
ATOM   619  C  CZ    . ARG B 2 109 ? 3.776   61.928 152.240 1.00 11.39 ? 109 ARG A CZ    1 
ATOM   620  N  NH1   . ARG B 2 109 ? 2.915   62.277 153.211 1.00 11.66 ? 109 ARG A NH1   1 
ATOM   621  N  NH2   . ARG B 2 109 ? 4.248   60.686 152.330 1.00 9.76  ? 109 ARG A NH2   1 
ATOM   622  N  N     . ASP B 2 110 ? 5.514   62.689 146.683 1.00 10.89 ? 110 ASP A N     1 
ATOM   623  C  CA    . ASP B 2 110 ? 5.538   61.913 145.433 1.00 10.73 ? 110 ASP A CA    1 
ATOM   624  C  C     . ASP B 2 110 ? 4.407   60.863 145.581 1.00 9.76  ? 110 ASP A C     1 
ATOM   625  O  O     . ASP B 2 110 ? 4.411   60.090 146.523 1.00 8.74  ? 110 ASP A O     1 
ATOM   626  C  CB    . ASP B 2 110 ? 6.913   61.292 145.210 1.00 13.11 ? 110 ASP A CB    1 
ATOM   627  C  CG    . ASP B 2 110 ? 7.936   62.322 144.731 1.00 15.36 ? 110 ASP A CG    1 
ATOM   628  O  OD1   . ASP B 2 110 ? 7.676   63.580 144.849 1.00 15.27 ? 110 ASP A OD1   1 
ATOM   629  O  OD2   . ASP B 2 110 ? 9.052   61.939 144.215 1.00 15.65 ? 110 ASP A OD2   1 
ATOM   630  N  N     . THR B 2 111 ? 3.457   60.967 144.686 1.00 9.57  ? 111 THR A N     1 
ATOM   631  C  CA    . THR B 2 111 ? 2.289   60.079 144.651 1.00 8.80  ? 111 THR A CA    1 
ATOM   632  C  C     . THR B 2 111 ? 2.581   58.990 143.610 1.00 8.42  ? 111 THR A C     1 
ATOM   633  O  O     . THR B 2 111 ? 2.925   59.346 142.474 1.00 8.13  ? 111 THR A O     1 
ATOM   634  C  CB    . THR B 2 111 ? 0.953   60.827 144.285 1.00 8.29  ? 111 THR A CB    1 
ATOM   635  O  OG1   . THR B 2 111 ? 0.767   61.858 145.304 1.00 6.93  ? 111 THR A OG1   1 
ATOM   636  C  CG2   . THR B 2 111 ? -0.270  59.920 144.161 1.00 8.00  ? 111 THR A CG2   1 
ATOM   637  N  N     . PHE B 2 112 ? 2.439   57.765 144.065 1.00 8.00  ? 112 PHE A N     1 
ATOM   638  C  CA    . PHE B 2 112 ? 2.663   56.621 143.181 1.00 7.82  ? 112 PHE A CA    1 
ATOM   639  C  C     . PHE B 2 112 ? 1.338   55.927 142.871 1.00 9.33  ? 112 PHE A C     1 
ATOM   640  O  O     . PHE B 2 112 ? 0.719   55.495 143.845 1.00 9.48  ? 112 PHE A O     1 
ATOM   641  C  CB    . PHE B 2 112 ? 3.619   55.602 143.766 1.00 5.50  ? 112 PHE A CB    1 
ATOM   642  C  CG    . PHE B 2 112 ? 5.051   56.047 143.730 1.00 7.71  ? 112 PHE A CG    1 
ATOM   643  C  CD1   . PHE B 2 112 ? 5.506   56.979 144.663 1.00 7.13  ? 112 PHE A CD1   1 
ATOM   644  C  CD2   . PHE B 2 112 ? 5.916   55.530 142.766 1.00 5.64  ? 112 PHE A CD2   1 
ATOM   645  C  CE1   . PHE B 2 112 ? 6.849   57.366 144.659 1.00 4.91  ? 112 PHE A CE1   1 
ATOM   646  C  CE2   . PHE B 2 112 ? 7.245   55.927 142.756 1.00 3.62  ? 112 PHE A CE2   1 
ATOM   647  C  CZ    . PHE B 2 112 ? 7.718   56.830 143.707 1.00 2.99  ? 112 PHE A CZ    1 
ATOM   648  N  N     . ILE B 2 113 ? 1.031   55.859 141.588 1.00 9.78  ? 113 ILE A N     1 
ATOM   649  C  CA    . ILE B 2 113 ? -0.186  55.161 141.130 1.00 9.93  ? 113 ILE A CA    1 
ATOM   650  C  C     . ILE B 2 113 ? 0.278   53.880 140.423 1.00 11.27 ? 113 ILE A C     1 
ATOM   651  O  O     . ILE B 2 113 ? 1.364   53.823 139.839 1.00 12.40 ? 113 ILE A O     1 
ATOM   652  C  CB    . ILE B 2 113 ? -1.165  56.021 140.305 1.00 6.98  ? 113 ILE A CB    1 
ATOM   653  C  CG1   . ILE B 2 113 ? -1.622  57.251 141.120 1.00 6.12  ? 113 ILE A CG1   1 
ATOM   654  C  CG2   . ILE B 2 113 ? -2.416  55.210 139.854 1.00 5.96  ? 113 ILE A CG2   1 
ATOM   655  C  CD1   . ILE B 2 113 ? -2.003  58.492 140.268 1.00 7.15  ? 113 ILE A CD1   1 
ATOM   656  N  N     . LEU B 2 114 ? -0.502  52.835 140.543 1.00 11.38 ? 114 LEU A N     1 
ATOM   657  C  CA    . LEU B 2 114 ? -0.184  51.560 139.926 1.00 10.76 ? 114 LEU A CA    1 
ATOM   658  C  C     . LEU B 2 114 ? -1.436  51.040 139.178 1.00 10.75 ? 114 LEU A C     1 
ATOM   659  O  O     . LEU B 2 114 ? -2.443  50.815 139.854 1.00 11.32 ? 114 LEU A O     1 
ATOM   660  C  CB    . LEU B 2 114 ? 0.211   50.513 140.947 1.00 9.80  ? 114 LEU A CB    1 
ATOM   661  C  CG    . LEU B 2 114 ? 1.301   50.634 141.934 1.00 9.89  ? 114 LEU A CG    1 
ATOM   662  C  CD1   . LEU B 2 114 ? 1.584   49.245 142.529 1.00 10.02 ? 114 LEU A CD1   1 
ATOM   663  C  CD2   . LEU B 2 114 ? 2.586   51.150 141.298 1.00 9.40  ? 114 LEU A CD2   1 
ATOM   664  N  N     . ILE B 2 115 ? -1.270  50.851 137.895 1.00 9.83  ? 115 ILE A N     1 
ATOM   665  C  CA    . ILE B 2 115 ? -2.404  50.280 137.125 1.00 8.41  ? 115 ILE A CA    1 
ATOM   666  C  C     . ILE B 2 115 ? -1.963  48.835 136.928 1.00 7.95  ? 115 ILE A C     1 
ATOM   667  O  O     . ILE B 2 115 ? -1.091  48.594 136.078 1.00 8.05  ? 115 ILE A O     1 
ATOM   668  C  CB    . ILE B 2 115 ? -2.680  51.163 135.892 1.00 6.42  ? 115 ILE A CB    1 
ATOM   669  C  CG1   . ILE B 2 115 ? -3.379  52.474 136.359 1.00 5.33  ? 115 ILE A CG1   1 
ATOM   670  C  CG2   . ILE B 2 115 ? -3.519  50.492 134.773 1.00 5.79  ? 115 ILE A CG2   1 
ATOM   671  C  CD1   . ILE B 2 115 ? -2.337  53.576 136.687 1.00 7.47  ? 115 ILE A CD1   1 
ATOM   672  N  N     . ALA B 2 116 ? -2.485  47.970 137.783 1.00 7.78  ? 116 ALA A N     1 
ATOM   673  C  CA    . ALA B 2 116 ? -2.134  46.526 137.762 1.00 8.63  ? 116 ALA A CA    1 
ATOM   674  C  C     . ALA B 2 116 ? -3.325  45.711 137.280 1.00 9.11  ? 116 ALA A C     1 
ATOM   675  O  O     . ALA B 2 116 ? -4.428  46.224 137.475 1.00 10.23 ? 116 ALA A O     1 
ATOM   676  C  CB    . ALA B 2 116 ? -1.694  46.116 139.165 1.00 9.05  ? 116 ALA A CB    1 
ATOM   677  N  N     . PRO B 2 117 ? -3.125  44.532 136.731 1.00 9.30  ? 117 PRO A N     1 
ATOM   678  C  CA    . PRO B 2 117 ? -4.195  43.664 136.245 1.00 9.88  ? 117 PRO A CA    1 
ATOM   679  C  C     . PRO B 2 117 ? -4.970  42.885 137.288 1.00 11.34 ? 117 PRO A C     1 
ATOM   680  O  O     . PRO B 2 117 ? -5.144  41.653 137.193 1.00 14.04 ? 117 PRO A O     1 
ATOM   681  C  CB    . PRO B 2 117 ? -3.488  42.704 135.275 1.00 9.26  ? 117 PRO A CB    1 
ATOM   682  C  CG    . PRO B 2 117 ? -2.139  42.549 135.910 1.00 9.25  ? 117 PRO A CG    1 
ATOM   683  C  CD    . PRO B 2 117 ? -1.799  43.918 136.501 1.00 8.70  ? 117 PRO A CD    1 
ATOM   684  N  N     . THR B 2 118 ? -5.467  43.597 138.276 1.00 10.20 ? 118 THR A N     1 
ATOM   685  C  CA    . THR B 2 118 ? -6.288  43.034 139.361 1.00 7.94  ? 118 THR A CA    1 
ATOM   686  C  C     . THR B 2 118 ? -7.737  43.369 139.046 1.00 7.16  ? 118 THR A C     1 
ATOM   687  O  O     . THR B 2 118 ? -8.102  44.561 139.238 1.00 7.52  ? 118 THR A O     1 
ATOM   688  C  CB    . THR B 2 118 ? -5.867  43.667 140.752 1.00 5.11  ? 118 THR A CB    1 
ATOM   689  O  OG1   . THR B 2 118 ? -5.732  45.098 140.514 1.00 5.49  ? 118 THR A OG1   1 
ATOM   690  C  CG2   . THR B 2 118 ? -4.623  43.056 141.371 1.00 4.86  ? 118 THR A CG2   1 
ATOM   691  N  N     . PRO B 2 119 ? -8.513  42.417 138.573 1.00 5.86  ? 119 PRO A N     1 
ATOM   692  C  CA    . PRO B 2 119 ? -9.917  42.672 138.213 1.00 5.78  ? 119 PRO A CA    1 
ATOM   693  C  C     . PRO B 2 119 ? -10.686 43.375 139.311 1.00 6.58  ? 119 PRO A C     1 
ATOM   694  O  O     . PRO B 2 119 ? -10.613 43.035 140.509 1.00 7.41  ? 119 PRO A O     1 
ATOM   695  C  CB    . PRO B 2 119 ? -10.496 41.298 137.908 1.00 5.44  ? 119 PRO A CB    1 
ATOM   696  C  CG    . PRO B 2 119 ? -9.294  40.481 137.497 1.00 5.12  ? 119 PRO A CG    1 
ATOM   697  C  CD    . PRO B 2 119 ? -8.129  41.031 138.319 1.00 5.37  ? 119 PRO A CD    1 
ATOM   698  N  N     . GLY B 2 120 ? -11.409 44.402 138.894 1.00 6.52  ? 120 GLY A N     1 
ATOM   699  C  CA    . GLY B 2 120 ? -12.268 45.173 139.761 1.00 6.61  ? 120 GLY A CA    1 
ATOM   700  C  C     . GLY B 2 120 ? -11.748 46.462 140.325 1.00 6.88  ? 120 GLY A C     1 
ATOM   701  O  O     . GLY B 2 120 ? -12.617 47.373 140.516 1.00 6.50  ? 120 GLY A O     1 
ATOM   702  N  N     . VAL B 2 121 ? -10.438 46.528 140.626 1.00 6.33  ? 121 VAL A N     1 
ATOM   703  C  CA    . VAL B 2 121 ? -9.934  47.804 141.202 1.00 7.41  ? 121 VAL A CA    1 
ATOM   704  C  C     . VAL B 2 121 ? -9.197  48.552 140.101 1.00 7.25  ? 121 VAL A C     1 
ATOM   705  O  O     . VAL B 2 121 ? -8.363  47.913 139.472 1.00 8.00  ? 121 VAL A O     1 
ATOM   706  C  CB    . VAL B 2 121 ? -9.167  47.622 142.498 1.00 8.47  ? 121 VAL A CB    1 
ATOM   707  C  CG1   . VAL B 2 121 ? -9.777  46.536 143.388 1.00 9.54  ? 121 VAL A CG1   1 
ATOM   708  C  CG2   . VAL B 2 121 ? -7.695  47.335 142.325 1.00 9.97  ? 121 VAL A CG2   1 
ATOM   709  N  N     . ALA B 2 122 ? -9.508  49.798 139.879 1.00 6.36  ? 122 ALA A N     1 
ATOM   710  C  CA    . ALA B 2 122 ? -8.912  50.670 138.888 1.00 5.66  ? 122 ALA A CA    1 
ATOM   711  C  C     . ALA B 2 122 ? -7.434  50.919 139.146 1.00 7.20  ? 122 ALA A C     1 
ATOM   712  O  O     . ALA B 2 122 ? -6.625  50.827 138.201 1.00 8.67  ? 122 ALA A O     1 
ATOM   713  C  CB    . ALA B 2 122 ? -9.615  52.034 138.866 1.00 2.98  ? 122 ALA A CB    1 
ATOM   714  N  N     . TYR B 2 123 ? -7.062  51.255 140.379 1.00 7.93  ? 123 TYR A N     1 
ATOM   715  C  CA    . TYR B 2 123 ? -5.622  51.516 140.624 1.00 8.29  ? 123 TYR A CA    1 
ATOM   716  C  C     . TYR B 2 123 ? -5.341  51.478 142.126 1.00 8.85  ? 123 TYR A C     1 
ATOM   717  O  O     . TYR B 2 123 ? -6.268  51.411 142.944 1.00 9.27  ? 123 TYR A O     1 
ATOM   718  C  CB    . TYR B 2 123 ? -5.212  52.861 140.013 1.00 6.05  ? 123 TYR A CB    1 
ATOM   719  C  CG    . TYR B 2 123 ? -5.885  54.039 140.711 1.00 7.51  ? 123 TYR A CG    1 
ATOM   720  C  CD1   . TYR B 2 123 ? -7.128  54.488 140.264 1.00 7.61  ? 123 TYR A CD1   1 
ATOM   721  C  CD2   . TYR B 2 123 ? -5.263  54.660 141.801 1.00 9.68  ? 123 TYR A CD2   1 
ATOM   722  C  CE1   . TYR B 2 123 ? -7.752  55.561 140.901 1.00 9.12  ? 123 TYR A CE1   1 
ATOM   723  C  CE2   . TYR B 2 123 ? -5.889  55.736 142.438 1.00 9.81  ? 123 TYR A CE2   1 
ATOM   724  C  CZ    . TYR B 2 123 ? -7.135  56.186 141.987 1.00 9.70  ? 123 TYR A CZ    1 
ATOM   725  O  OH    . TYR B 2 123 ? -7.748  57.232 142.601 1.00 10.23 ? 123 TYR A OH    1 
ATOM   726  N  N     . TRP B 2 124 ? -4.058  51.500 142.428 1.00 8.90  ? 124 TRP A N     1 
ATOM   727  C  CA    . TRP B 2 124 ? -3.549  51.502 143.810 1.00 9.18  ? 124 TRP A CA    1 
ATOM   728  C  C     . TRP B 2 124 ? -2.684  52.753 143.998 1.00 10.12 ? 124 TRP A C     1 
ATOM   729  O  O     . TRP B 2 124 ? -1.802  53.048 143.178 1.00 10.84 ? 124 TRP A O     1 
ATOM   730  C  CB    . TRP B 2 124 ? -2.712  50.237 144.064 1.00 7.66  ? 124 TRP A CB    1 
ATOM   731  C  CG    . TRP B 2 124 ? -3.413  48.938 143.636 1.00 6.61  ? 124 TRP A CG    1 
ATOM   732  C  CD1   . TRP B 2 124 ? -3.600  48.493 142.385 1.00 6.90  ? 124 TRP A CD1   1 
ATOM   733  C  CD2   . TRP B 2 124 ? -3.983  47.982 144.522 1.00 5.84  ? 124 TRP A CD2   1 
ATOM   734  N  NE1   . TRP B 2 124 ? -4.299  47.246 142.477 1.00 6.18  ? 124 TRP A NE1   1 
ATOM   735  C  CE2   . TRP B 2 124 ? -4.515  46.966 143.738 1.00 5.96  ? 124 TRP A CE2   1 
ATOM   736  C  CE3   . TRP B 2 124 ? -4.094  47.897 145.915 1.00 4.31  ? 124 TRP A CE3   1 
ATOM   737  C  CZ2   . TRP B 2 124 ? -5.170  45.849 144.272 1.00 5.86  ? 124 TRP A CZ2   1 
ATOM   738  C  CZ3   . TRP B 2 124 ? -4.753  46.768 146.444 1.00 4.46  ? 124 TRP A CZ3   1 
ATOM   739  C  CH2   . TRP B 2 124 ? -5.266  45.793 145.660 1.00 5.68  ? 124 TRP A CH2   1 
ATOM   740  N  N     . VAL B 2 125 ? -2.954  53.477 145.074 1.00 10.39 ? 125 VAL A N     1 
ATOM   741  C  CA    . VAL B 2 125 ? -2.232  54.729 145.370 1.00 10.23 ? 125 VAL A CA    1 
ATOM   742  C  C     . VAL B 2 125 ? -1.505  54.677 146.709 1.00 10.64 ? 125 VAL A C     1 
ATOM   743  O  O     . VAL B 2 125 ? -1.792  53.822 147.559 1.00 11.54 ? 125 VAL A O     1 
ATOM   744  C  CB    . VAL B 2 125 ? -3.191  55.916 145.455 1.00 8.19  ? 125 VAL A CB    1 
ATOM   745  C  CG1   . VAL B 2 125 ? -2.923  56.976 144.384 1.00 6.70  ? 125 VAL A CG1   1 
ATOM   746  C  CG2   . VAL B 2 125 ? -4.655  55.517 145.297 1.00 7.63  ? 125 VAL A CG2   1 
ATOM   747  N  N     . ALA B 2 126 ? -0.601  55.627 146.807 1.00 10.38 ? 126 ALA A N     1 
ATOM   748  C  CA    . ALA B 2 126 ? 0.250   55.848 147.974 1.00 10.46 ? 126 ALA A CA    1 
ATOM   749  C  C     . ALA B 2 126 ? 1.230   56.969 147.647 1.00 10.73 ? 126 ALA A C     1 
ATOM   750  O  O     . ALA B 2 126 ? 1.675   57.117 146.499 1.00 11.71 ? 126 ALA A O     1 
ATOM   751  C  CB    . ALA B 2 126 ? 1.028   54.572 148.309 1.00 8.79  ? 126 ALA A CB    1 
ATOM   752  N  N     . ASP B 2 127 ? 1.539   57.757 148.653 1.00 10.35 ? 127 ASP A N     1 
ATOM   753  C  CA    . ASP B 2 127 ? 2.501   58.846 148.490 1.00 9.83  ? 127 ASP A CA    1 
ATOM   754  C  C     . ASP B 2 127 ? 3.554   58.771 149.600 1.00 8.28  ? 127 ASP A C     1 
ATOM   755  O  O     . ASP B 2 127 ? 3.339   58.164 150.643 1.00 8.01  ? 127 ASP A O     1 
ATOM   756  C  CB    . ASP B 2 127 ? 1.814   60.198 148.475 1.00 12.79 ? 127 ASP A CB    1 
ATOM   757  C  CG    . ASP B 2 127 ? 1.046   60.462 149.741 1.00 15.18 ? 127 ASP A CG    1 
ATOM   758  O  OD1   . ASP B 2 127 ? -0.175  60.076 149.825 1.00 17.44 ? 127 ASP A OD1   1 
ATOM   759  O  OD2   . ASP B 2 127 ? 1.626   61.063 150.716 1.00 15.00 ? 127 ASP A OD2   1 
ATOM   760  N  N     . VAL B 2 128 ? 4.636   59.422 149.273 1.00 7.18  ? 128 VAL A N     1 
ATOM   761  C  CA    . VAL B 2 128 ? 5.805   59.447 150.142 1.00 6.87  ? 128 VAL A CA    1 
ATOM   762  C  C     . VAL B 2 128 ? 6.477   60.813 150.030 1.00 7.16  ? 128 VAL A C     1 
ATOM   763  O  O     . VAL B 2 128 ? 6.158   61.592 149.118 1.00 7.59  ? 128 VAL A O     1 
ATOM   764  C  CB    . VAL B 2 128 ? 6.758   58.345 149.579 1.00 5.28  ? 128 VAL A CB    1 
ATOM   765  C  CG1   . VAL B 2 128 ? 6.116   56.981 149.540 1.00 4.85  ? 128 VAL A CG1   1 
ATOM   766  C  CG2   . VAL B 2 128 ? 7.253   58.766 148.208 1.00 5.77  ? 128 VAL A CG2   1 
ATOM   767  N  N     . PRO B 2 129 ? 7.414   61.017 150.949 1.00 6.98  ? 129 PRO A N     1 
ATOM   768  C  CA    . PRO B 2 129 ? 8.218   62.238 150.952 1.00 6.78  ? 129 PRO A CA    1 
ATOM   769  C  C     . PRO B 2 129 ? 8.852   62.422 149.560 1.00 7.13  ? 129 PRO A C     1 
ATOM   770  O  O     . PRO B 2 129 ? 9.427   61.463 149.025 1.00 6.52  ? 129 PRO A O     1 
ATOM   771  C  CB    . PRO B 2 129 ? 9.322   61.906 151.970 1.00 5.65  ? 129 PRO A CB    1 
ATOM   772  C  CG    . PRO B 2 129 ? 8.729   60.905 152.893 1.00 4.77  ? 129 PRO A CG    1 
ATOM   773  C  CD    . PRO B 2 129 ? 7.781   60.101 152.038 1.00 5.94  ? 129 PRO A CD    1 
ATOM   774  N  N     . ALA B 2 130 ? 8.737   63.612 149.026 1.00 7.74  ? 130 ALA A N     1 
ATOM   775  C  CA    . ALA B 2 130 ? 9.277   63.989 147.723 1.00 8.50  ? 130 ALA A CA    1 
ATOM   776  C  C     . ALA B 2 130 ? 10.749  63.610 147.594 1.00 9.48  ? 130 ALA A C     1 
ATOM   777  O  O     . ALA B 2 130 ? 11.607  63.860 148.461 1.00 10.57 ? 130 ALA A O     1 
ATOM   778  C  CB    . ALA B 2 130 ? 9.056   65.462 147.477 1.00 7.67  ? 130 ALA A CB    1 
ATOM   779  N  N     . GLY B 2 131 ? 11.011  62.978 146.466 1.00 9.82  ? 131 GLY A N     1 
ATOM   780  C  CA    . GLY B 2 131 ? 12.369  62.486 146.173 1.00 10.24 ? 131 GLY A CA    1 
ATOM   781  C  C     . GLY B 2 131 ? 12.584  61.195 146.972 1.00 11.30 ? 131 GLY A C     1 
ATOM   782  O  O     . GLY B 2 131 ? 13.749  60.875 147.262 1.00 13.13 ? 131 GLY A O     1 
ATOM   783  N  N     . THR B 2 132 ? 11.501  60.524 147.311 1.00 10.91 ? 132 THR A N     1 
ATOM   784  C  CA    . THR B 2 132 ? 11.579  59.267 148.056 1.00 11.05 ? 132 THR A CA    1 
ATOM   785  C  C     . THR B 2 132 ? 10.674  58.246 147.360 1.00 11.76 ? 132 THR A C     1 
ATOM   786  O  O     . THR B 2 132 ? 9.728   58.659 146.686 1.00 13.41 ? 132 THR A O     1 
ATOM   787  C  CB    . THR B 2 132 ? 11.313  59.443 149.578 1.00 10.33 ? 132 THR A CB    1 
ATOM   788  O  OG1   . THR B 2 132 ? 10.158  58.608 149.955 1.00 10.78 ? 132 THR A OG1   1 
ATOM   789  C  CG2   . THR B 2 132 ? 11.090  60.867 150.038 1.00 9.45  ? 132 THR A CG2   1 
ATOM   790  N  N     . PHE B 2 133 ? 11.003  56.982 147.497 1.00 11.51 ? 133 PHE A N     1 
ATOM   791  C  CA    . PHE B 2 133 ? 10.266  55.843 146.926 1.00 11.20 ? 133 PHE A CA    1 
ATOM   792  C  C     . PHE B 2 133 ? 9.559   55.115 148.061 1.00 12.00 ? 133 PHE A C     1 
ATOM   793  O  O     . PHE B 2 133 ? 9.850   55.394 149.242 1.00 13.65 ? 133 PHE A O     1 
ATOM   794  C  CB    . PHE B 2 133 ? 11.244  54.920 146.173 1.00 7.29  ? 133 PHE A CB    1 
ATOM   795  C  CG    . PHE B 2 133 ? 11.498  55.430 144.782 1.00 5.84  ? 133 PHE A CG    1 
ATOM   796  C  CD1   . PHE B 2 133 ? 12.518  56.371 144.598 1.00 4.37  ? 133 PHE A CD1   1 
ATOM   797  C  CD2   . PHE B 2 133 ? 10.693  55.018 143.719 1.00 5.85  ? 133 PHE A CD2   1 
ATOM   798  C  CE1   . PHE B 2 133 ? 12.772  56.891 143.337 1.00 5.94  ? 133 PHE A CE1   1 
ATOM   799  C  CE2   . PHE B 2 133 ? 10.928  55.549 142.436 1.00 6.36  ? 133 PHE A CE2   1 
ATOM   800  C  CZ    . PHE B 2 133 ? 11.974  56.492 142.251 1.00 5.38  ? 133 PHE A CZ    1 
ATOM   801  N  N     . PRO B 2 134 ? 8.679   54.198 147.736 1.00 11.17 ? 134 PRO A N     1 
ATOM   802  C  CA    . PRO B 2 134 ? 7.945   53.472 148.785 1.00 10.49 ? 134 PRO A CA    1 
ATOM   803  C  C     . PRO B 2 134 ? 8.874   52.610 149.608 1.00 10.27 ? 134 PRO A C     1 
ATOM   804  O  O     . PRO B 2 134 ? 9.725   51.856 149.120 1.00 10.33 ? 134 PRO A O     1 
ATOM   805  C  CB    . PRO B 2 134 ? 6.865   52.714 148.032 1.00 10.24 ? 134 PRO A CB    1 
ATOM   806  C  CG    . PRO B 2 134 ? 6.831   53.299 146.644 1.00 10.80 ? 134 PRO A CG    1 
ATOM   807  C  CD    . PRO B 2 134 ? 8.244   53.818 146.389 1.00 11.08 ? 134 PRO A CD    1 
ATOM   808  N  N     . ILE B 2 135 ? 8.716   52.713 150.918 1.00 10.24 ? 135 ILE A N     1 
ATOM   809  C  CA    . ILE B 2 135 ? 9.489   51.912 151.875 1.00 10.68 ? 135 ILE A CA    1 
ATOM   810  C  C     . ILE B 2 135 ? 8.598   50.772 152.393 1.00 10.99 ? 135 ILE A C     1 
ATOM   811  O  O     . ILE B 2 135 ? 7.386   50.732 152.211 1.00 10.61 ? 135 ILE A O     1 
ATOM   812  C  CB    . ILE B 2 135 ? 10.107  52.742 153.027 1.00 10.62 ? 135 ILE A CB    1 
ATOM   813  C  CG1   . ILE B 2 135 ? 8.952   53.375 153.854 1.00 11.68 ? 135 ILE A CG1   1 
ATOM   814  C  CG2   . ILE B 2 135 ? 11.131  53.775 152.497 1.00 8.49  ? 135 ILE A CG2   1 
ATOM   815  C  CD1   . ILE B 2 135 ? 9.211   53.300 155.383 1.00 25.00 ? 135 ILE A CD1   1 
ATOM   816  N  N     . SER B 2 136 ? 9.292   49.842 153.014 1.00 11.06 ? 136 SER A N     1 
ATOM   817  C  CA    . SER B 2 136 ? 8.752   48.627 153.610 1.00 11.66 ? 136 SER A CA    1 
ATOM   818  C  C     . SER B 2 136 ? 7.456   48.873 154.379 1.00 11.90 ? 136 SER A C     1 
ATOM   819  O  O     . SER B 2 136 ? 6.660   47.928 154.458 1.00 12.73 ? 136 SER A O     1 
ATOM   820  C  CB    . SER B 2 136 ? 9.730   48.011 154.617 1.00 12.92 ? 136 SER A CB    1 
ATOM   821  O  OG    . SER B 2 136 ? 9.558   48.795 155.823 1.00 15.62 ? 136 SER A OG    1 
ATOM   822  N  N     . THR B 2 137 ? 7.312   50.049 154.953 1.00 12.23 ? 137 THR A N     1 
ATOM   823  C  CA    . THR B 2 137 ? 6.109   50.318 155.737 1.00 13.26 ? 137 THR A CA    1 
ATOM   824  C  C     . THR B 2 137 ? 5.002   50.980 154.952 1.00 14.34 ? 137 THR A C     1 
ATOM   825  O  O     . THR B 2 137 ? 3.955   51.262 155.577 1.00 16.01 ? 137 THR A O     1 
ATOM   826  C  CB    . THR B 2 137 ? 6.463   51.108 157.051 1.00 13.80 ? 137 THR A CB    1 
ATOM   827  O  OG1   . THR B 2 137 ? 6.733   52.489 156.656 1.00 16.35 ? 137 THR A OG1   1 
ATOM   828  C  CG2   . THR B 2 137 ? 7.642   50.482 157.771 1.00 15.23 ? 137 THR A CG2   1 
ATOM   829  N  N     . THR B 2 138 ? 5.194   51.196 153.670 1.00 13.99 ? 138 THR A N     1 
ATOM   830  C  CA    . THR B 2 138 ? 4.218   51.828 152.773 1.00 12.35 ? 138 THR A CA    1 
ATOM   831  C  C     . THR B 2 138 ? 3.033   50.901 152.525 1.00 12.67 ? 138 THR A C     1 
ATOM   832  O  O     . THR B 2 138 ? 3.223   49.665 152.605 1.00 13.41 ? 138 THR A O     1 
ATOM   833  C  CB    . THR B 2 138 ? 4.869   52.240 151.394 1.00 10.85 ? 138 THR A CB    1 
ATOM   834  O  OG1   . THR B 2 138 ? 6.049   53.038 151.735 1.00 9.82  ? 138 THR A OG1   1 
ATOM   835  C  CG2   . THR B 2 138 ? 3.933   53.018 150.471 1.00 11.04 ? 138 THR A CG2   1 
ATOM   836  N  N     . THR B 2 139 ? 1.891   51.527 152.224 1.00 11.83 ? 139 THR A N     1 
ATOM   837  C  CA    . THR B 2 139 ? 0.701   50.750 151.915 1.00 11.37 ? 139 THR A CA    1 
ATOM   838  C  C     . THR B 2 139 ? -0.117  51.320 150.764 1.00 11.07 ? 139 THR A C     1 
ATOM   839  O  O     . THR B 2 139 ? -0.815  52.344 150.917 1.00 11.59 ? 139 THR A O     1 
ATOM   840  C  CB    . THR B 2 139 ? -0.253  50.494 153.131 1.00 11.47 ? 139 THR A CB    1 
ATOM   841  O  OG1   . THR B 2 139 ? 0.441   49.532 153.987 1.00 13.20 ? 139 THR A OG1   1 
ATOM   842  C  CG2   . THR B 2 139 ? -1.646  50.030 152.674 1.00 8.43  ? 139 THR A CG2   1 
ATOM   843  N  N     . PHE B 2 140 ? -0.081  50.607 149.641 1.00 10.11 ? 140 PHE A N     1 
ATOM   844  C  CA    . PHE B 2 140 ? -0.875  51.027 148.465 1.00 9.33  ? 140 PHE A CA    1 
ATOM   845  C  C     . PHE B 2 140 ? -2.315  50.573 148.751 1.00 8.83  ? 140 PHE A C     1 
ATOM   846  O  O     . PHE B 2 140 ? -2.568  49.421 149.115 1.00 7.42  ? 140 PHE A O     1 
ATOM   847  C  CB    . PHE B 2 140 ? -0.350  50.535 147.133 1.00 9.75  ? 140 PHE A CB    1 
ATOM   848  C  CG    . PHE B 2 140 ? 0.905   51.197 146.633 1.00 9.15  ? 140 PHE A CG    1 
ATOM   849  C  CD1   . PHE B 2 140 ? 2.149   50.831 147.164 1.00 8.02  ? 140 PHE A CD1   1 
ATOM   850  C  CD2   . PHE B 2 140 ? 0.853   52.162 145.641 1.00 9.18  ? 140 PHE A CD2   1 
ATOM   851  C  CE1   . PHE B 2 140 ? 3.328   51.428 146.741 1.00 6.51  ? 140 PHE A CE1   1 
ATOM   852  C  CE2   . PHE B 2 140 ? 2.028   52.770 145.192 1.00 8.50  ? 140 PHE A CE2   1 
ATOM   853  C  CZ    . PHE B 2 140 ? 3.255   52.396 145.750 1.00 8.19  ? 140 PHE A CZ    1 
ATOM   854  N  N     . ASN B 2 141 ? -3.210  51.510 148.567 1.00 9.38  ? 141 ASN A N     1 
ATOM   855  C  CA    . ASN B 2 141 ? -4.644  51.329 148.781 1.00 9.69  ? 141 ASN A CA    1 
ATOM   856  C  C     . ASN B 2 141 ? -5.367  51.246 147.449 1.00 9.93  ? 141 ASN A C     1 
ATOM   857  O  O     . ASN B 2 141 ? -5.030  52.034 146.533 1.00 9.82  ? 141 ASN A O     1 
ATOM   858  C  CB    . ASN B 2 141 ? -5.153  52.501 149.657 1.00 10.77 ? 141 ASN A CB    1 
ATOM   859  C  CG    . ASN B 2 141 ? -4.809  52.192 151.106 1.00 15.32 ? 141 ASN A CG    1 
ATOM   860  O  OD1   . ASN B 2 141 ? -5.360  51.220 151.645 1.00 18.88 ? 141 ASN A OD1   1 
ATOM   861  N  ND2   . ASN B 2 141 ? -3.892  52.933 151.697 1.00 17.41 ? 141 ASN A ND2   1 
ATOM   862  N  N     . ALA B 2 142 ? -6.320  50.327 147.429 1.00 9.51  ? 142 ALA A N     1 
ATOM   863  C  CA    . ALA B 2 142 ? -7.141  50.068 146.239 1.00 9.25  ? 142 ALA A CA    1 
ATOM   864  C  C     . ALA B 2 142 ? -8.198  51.117 145.960 1.00 9.28  ? 142 ALA A C     1 
ATOM   865  O  O     . ALA B 2 142 ? -8.819  51.669 146.900 1.00 9.58  ? 142 ALA A O     1 
ATOM   866  C  CB    . ALA B 2 142 ? -7.778  48.687 146.422 1.00 6.90  ? 142 ALA A CB    1 
ATOM   867  N  N     . VAL B 2 143 ? -8.443  51.424 144.709 1.00 9.37  ? 143 VAL A N     1 
ATOM   868  C  CA    . VAL B 2 143 ? -9.496  52.354 144.258 1.00 9.40  ? 143 VAL A CA    1 
ATOM   869  C  C     . VAL B 2 143 ? -10.232 51.531 143.176 1.00 9.87  ? 143 VAL A C     1 
ATOM   870  O  O     . VAL B 2 143 ? -9.613  51.176 142.160 1.00 10.17 ? 143 VAL A O     1 
ATOM   871  C  CB    . VAL B 2 143 ? -8.992  53.700 143.792 1.00 7.67  ? 143 VAL A CB    1 
ATOM   872  C  CG1   . VAL B 2 143 ? -10.140 54.601 143.317 1.00 6.58  ? 143 VAL A CG1   1 
ATOM   873  C  CG2   . VAL B 2 143 ? -8.156  54.402 144.828 1.00 6.95  ? 143 VAL A CG2   1 
ATOM   874  N  N     . ASN B 2 144 ? -11.472 51.204 143.457 1.00 10.24 ? 144 ASN A N     1 
ATOM   875  C  CA    . ASN B 2 144 ? -12.251 50.361 142.572 1.00 10.29 ? 144 ASN A CA    1 
ATOM   876  C  C     . ASN B 2 144 ? -12.901 51.071 141.402 1.00 11.72 ? 144 ASN A C     1 
ATOM   877  O  O     . ASN B 2 144 ? -13.098 52.290 141.414 1.00 13.63 ? 144 ASN A O     1 
ATOM   878  C  CB    . ASN B 2 144 ? -13.411 49.619 143.269 1.00 6.45  ? 144 ASN A CB    1 
ATOM   879  C  CG    . ASN B 2 144 ? -13.063 48.931 144.586 1.00 7.35  ? 144 ASN A CG    1 
ATOM   880  O  OD1   . ASN B 2 144 ? -13.583 47.847 144.864 1.00 7.90  ? 144 ASN A OD1   1 
ATOM   881  N  ND2   . ASN B 2 144 ? -12.228 49.500 145.425 1.00 7.94  ? 144 ASN A ND2   1 
ATOM   882  N  N     . PHE B 2 145 ? -13.188 50.225 140.426 1.00 11.84 ? 145 PHE A N     1 
ATOM   883  C  CA    . PHE B 2 145 ? -13.951 50.602 139.245 1.00 10.73 ? 145 PHE A CA    1 
ATOM   884  C  C     . PHE B 2 145 ? -15.402 50.570 139.689 1.00 10.22 ? 145 PHE A C     1 
ATOM   885  O  O     . PHE B 2 145 ? -15.778 49.793 140.578 1.00 10.60 ? 145 PHE A O     1 
ATOM   886  C  CB    . PHE B 2 145 ? -13.752 49.571 138.126 1.00 10.52 ? 145 PHE A CB    1 
ATOM   887  C  CG    . PHE B 2 145 ? -12.639 49.897 137.119 1.00 10.79 ? 145 PHE A CG    1 
ATOM   888  C  CD1   . PHE B 2 145 ? -12.765 50.984 136.241 1.00 11.62 ? 145 PHE A CD1   1 
ATOM   889  C  CD2   . PHE B 2 145 ? -11.498 49.087 137.067 1.00 11.20 ? 145 PHE A CD2   1 
ATOM   890  C  CE1   . PHE B 2 145 ? -11.751 51.252 135.307 1.00 10.34 ? 145 PHE A CE1   1 
ATOM   891  C  CE2   . PHE B 2 145 ? -10.489 49.352 136.133 1.00 10.60 ? 145 PHE A CE2   1 
ATOM   892  C  CZ    . PHE B 2 145 ? -10.616 50.433 135.252 1.00 10.58 ? 145 PHE A CZ    1 
ATOM   893  N  N     . PRO B 2 146 ? -16.306 51.364 139.154 1.00 10.47 ? 146 PRO A N     1 
ATOM   894  C  CA    . PRO B 2 146 ? -17.679 51.323 139.619 1.00 10.53 ? 146 PRO A CA    1 
ATOM   895  C  C     . PRO B 2 146 ? -18.306 49.944 139.421 1.00 10.89 ? 146 PRO A C     1 
ATOM   896  O  O     . PRO B 2 146 ? -18.082 49.315 138.342 1.00 10.50 ? 146 PRO A O     1 
ATOM   897  C  CB    . PRO B 2 146 ? -18.365 52.366 138.771 1.00 9.91  ? 146 PRO A CB    1 
ATOM   898  C  CG    . PRO B 2 146 ? -17.323 52.969 137.834 1.00 10.17 ? 146 PRO A CG    1 
ATOM   899  C  CD    . PRO B 2 146 ? -16.002 52.318 138.092 1.00 10.35 ? 146 PRO A CD    1 
ATOM   900  N  N     . GLY B 2 147 ? -19.051 49.508 140.452 1.00 11.82 ? 147 GLY A N     1 
ATOM   901  C  CA    . GLY B 2 147 ? -19.873 48.253 140.431 1.00 13.54 ? 147 GLY A CA    1 
ATOM   902  C  C     . GLY B 2 147 ? -19.108 46.956 140.808 1.00 15.01 ? 147 GLY A C     1 
ATOM   903  O  O     . GLY B 2 147 ? -19.398 45.867 140.283 1.00 17.29 ? 147 GLY A O     1 
ATOM   904  N  N     . PHE B 2 148 ? -18.169 47.067 141.727 1.00 14.64 ? 148 PHE A N     1 
ATOM   905  C  CA    . PHE B 2 148 ? -17.346 45.917 142.180 1.00 14.09 ? 148 PHE A CA    1 
ATOM   906  C  C     . PHE B 2 148 ? -18.207 44.871 142.911 1.00 14.21 ? 148 PHE A C     1 
ATOM   907  O  O     . PHE B 2 148 ? -18.216 43.680 142.563 1.00 14.29 ? 148 PHE A O     1 
ATOM   908  C  CB    . PHE B 2 148 ? -16.251 46.414 143.128 1.00 11.25 ? 148 PHE A CB    1 
ATOM   909  C  CG    . PHE B 2 148 ? -15.390 45.303 143.746 1.00 9.72  ? 148 PHE A CG    1 
ATOM   910  C  CD1   . PHE B 2 148 ? -15.900 44.511 144.783 1.00 8.86  ? 148 PHE A CD1   1 
ATOM   911  C  CD2   . PHE B 2 148 ? -14.084 45.086 143.283 1.00 8.85  ? 148 PHE A CD2   1 
ATOM   912  C  CE1   . PHE B 2 148 ? -15.105 43.511 145.359 1.00 7.79  ? 148 PHE A CE1   1 
ATOM   913  C  CE2   . PHE B 2 148 ? -13.289 44.088 143.861 1.00 7.45  ? 148 PHE A CE2   1 
ATOM   914  C  CZ    . PHE B 2 148 ? -13.800 43.301 144.900 1.00 6.41  ? 148 PHE A CZ    1 
ATOM   915  N  N     . ASN B 2 149 ? -18.923 45.331 143.926 1.00 14.64 ? 149 ASN A N     1 
ATOM   916  C  CA    . ASN B 2 149 ? -19.772 44.443 144.737 1.00 15.02 ? 149 ASN A CA    1 
ATOM   917  C  C     . ASN B 2 149 ? -20.709 43.654 143.816 1.00 15.13 ? 149 ASN A C     1 
ATOM   918  O  O     . ASN B 2 149 ? -21.094 42.523 144.171 1.00 15.73 ? 149 ASN A O     1 
ATOM   919  C  CB    . ASN B 2 149 ? -20.530 45.241 145.790 1.00 16.34 ? 149 ASN A CB    1 
ATOM   920  C  CG    . ASN B 2 149 ? -19.688 45.460 147.052 1.00 18.89 ? 149 ASN A CG    1 
ATOM   921  O  OD1   . ASN B 2 149 ? -19.282 46.588 147.328 1.00 21.00 ? 149 ASN A OD1   1 
ATOM   922  N  ND2   . ASN B 2 149 ? -19.390 44.439 147.838 1.00 19.05 ? 149 ASN A ND2   1 
ATOM   923  N  N     . SER B 2 150 ? -21.068 44.249 142.697 1.00 14.60 ? 150 SER A N     1 
ATOM   924  C  CA    . SER B 2 150 ? -21.990 43.579 141.768 1.00 14.74 ? 150 SER A CA    1 
ATOM   925  C  C     . SER B 2 150 ? -21.278 42.478 141.006 1.00 14.26 ? 150 SER A C     1 
ATOM   926  O  O     . SER B 2 150 ? -21.890 41.527 140.494 1.00 15.15 ? 150 SER A O     1 
ATOM   927  C  CB    . SER B 2 150 ? -22.620 44.608 140.845 1.00 17.58 ? 150 SER A CB    1 
ATOM   928  O  OG    . SER B 2 150 ? -21.913 44.744 139.613 1.00 22.56 ? 150 SER A OG    1 
ATOM   929  N  N     . MET B 2 151 ? -19.969 42.589 140.897 1.00 12.82 ? 151 MET A N     1 
ATOM   930  C  CA    . MET B 2 151 ? -19.200 41.585 140.152 1.00 11.17 ? 151 MET A CA    1 
ATOM   931  C  C     . MET B 2 151 ? -18.577 40.609 141.134 1.00 10.90 ? 151 MET A C     1 
ATOM   932  O  O     . MET B 2 151 ? -18.483 39.449 140.747 1.00 12.30 ? 151 MET A O     1 
ATOM   933  C  CB    . MET B 2 151 ? -18.088 42.203 139.310 1.00 10.46 ? 151 MET A CB    1 
ATOM   934  C  CG    . MET B 2 151 ? -18.586 42.868 138.068 1.00 10.83 ? 151 MET A CG    1 
ATOM   935  S  SD    . MET B 2 151 ? -19.140 41.580 136.927 1.00 10.96 ? 151 MET A SD    1 
ATOM   936  C  CE    . MET B 2 151 ? -17.632 40.971 136.185 1.00 9.16  ? 151 MET A CE    1 
ATOM   937  N  N     . PHE B 2 152 ? -18.167 41.067 142.310 1.00 10.75 ? 152 PHE A N     1 
ATOM   938  C  CA    . PHE B 2 152 ? -17.458 40.147 143.237 1.00 10.95 ? 152 PHE A CA    1 
ATOM   939  C  C     . PHE B 2 152 ? -17.982 39.965 144.636 1.00 11.23 ? 152 PHE A C     1 
ATOM   940  O  O     . PHE B 2 152 ? -17.342 39.272 145.489 1.00 11.12 ? 152 PHE A O     1 
ATOM   941  C  CB    . PHE B 2 152 ? -15.940 40.513 143.211 1.00 10.06 ? 152 PHE A CB    1 
ATOM   942  C  CG    . PHE B 2 152 ? -15.403 40.617 141.807 1.00 8.12  ? 152 PHE A CG    1 
ATOM   943  C  CD1   . PHE B 2 152 ? -15.224 39.466 141.046 1.00 6.02  ? 152 PHE A CD1   1 
ATOM   944  C  CD2   . PHE B 2 152 ? -15.098 41.864 141.274 1.00 6.14  ? 152 PHE A CD2   1 
ATOM   945  C  CE1   . PHE B 2 152 ? -14.719 39.543 139.743 1.00 3.88  ? 152 PHE A CE1   1 
ATOM   946  C  CE2   . PHE B 2 152 ? -14.627 41.964 139.978 1.00 6.11  ? 152 PHE A CE2   1 
ATOM   947  C  CZ    . PHE B 2 152 ? -14.425 40.808 139.213 1.00 4.96  ? 152 PHE A CZ    1 
ATOM   948  N  N     . GLY B 2 153 ? -19.129 40.534 144.943 1.00 11.12 ? 153 GLY A N     1 
ATOM   949  C  CA    . GLY B 2 153 ? -19.720 40.319 146.273 1.00 12.79 ? 153 GLY A CA    1 
ATOM   950  C  C     . GLY B 2 153 ? -19.157 41.216 147.336 1.00 13.59 ? 153 GLY A C     1 
ATOM   951  O  O     . GLY B 2 153 ? -18.547 42.223 146.968 1.00 14.83 ? 153 GLY A O     1 
ATOM   952  N  N     . ASN B 2 154 ? -19.418 40.822 148.569 1.00 14.23 ? 154 ASN A N     1 
ATOM   953  C  CA    . ASN B 2 154 ? -18.947 41.593 149.731 1.00 15.79 ? 154 ASN A CA    1 
ATOM   954  C  C     . ASN B 2 154 ? -18.382 40.656 150.794 1.00 15.78 ? 154 ASN A C     1 
ATOM   955  O  O     . ASN B 2 154 ? -18.488 40.942 151.995 1.00 17.16 ? 154 ASN A O     1 
ATOM   956  C  CB    . ASN B 2 154 ? -20.093 42.448 150.282 1.00 18.78 ? 154 ASN A CB    1 
ATOM   957  C  CG    . ASN B 2 154 ? -21.347 41.565 150.277 1.00 22.86 ? 154 ASN A CG    1 
ATOM   958  O  OD1   . ASN B 2 154 ? -22.132 41.701 149.309 1.00 26.19 ? 154 ASN A OD1   1 
ATOM   959  N  ND2   . ASN B 2 154 ? -21.452 40.706 151.286 1.00 23.04 ? 154 ASN A ND2   1 
ATOM   960  N  N     . ALA B 2 155 ? -17.786 39.593 150.299 1.00 14.95 ? 155 ALA A N     1 
ATOM   961  C  CA    . ALA B 2 155 ? -17.166 38.584 151.172 1.00 13.99 ? 155 ALA A CA    1 
ATOM   962  C  C     . ALA B 2 155 ? -15.955 37.989 150.480 1.00 13.88 ? 155 ALA A C     1 
ATOM   963  O  O     . ALA B 2 155 ? -15.961 37.684 149.277 1.00 14.66 ? 155 ALA A O     1 
ATOM   964  C  CB    . ALA B 2 155 ? -18.241 37.586 151.526 1.00 13.86 ? 155 ALA A CB    1 
ATOM   965  N  N     . ALA B 2 156 ? -14.913 37.805 151.266 1.00 12.96 ? 156 ALA A N     1 
ATOM   966  C  CA    . ALA B 2 156 ? -13.650 37.268 150.774 1.00 11.95 ? 156 ALA A CA    1 
ATOM   967  C  C     . ALA B 2 156 ? -13.726 35.897 150.165 1.00 11.95 ? 156 ALA A C     1 
ATOM   968  O  O     . ALA B 2 156 ? -12.756 35.552 149.434 1.00 11.88 ? 156 ALA A O     1 
ATOM   969  C  CB    . ALA B 2 156 ? -12.575 37.366 151.859 1.00 11.34 ? 156 ALA A CB    1 
ATOM   970  N  N     . ALA B 2 157 ? -14.714 35.046 150.418 1.00 12.14 ? 157 ALA A N     1 
ATOM   971  C  CA    . ALA B 2 157 ? -14.669 33.728 149.741 1.00 11.59 ? 157 ALA A CA    1 
ATOM   972  C  C     . ALA B 2 157 ? -15.922 33.594 148.876 1.00 11.87 ? 157 ALA A C     1 
ATOM   973  O  O     . ALA B 2 157 ? -16.379 32.469 148.676 1.00 12.11 ? 157 ALA A O     1 
ATOM   974  C  CB    . ALA B 2 157 ? -14.463 32.525 150.587 1.00 9.32  ? 157 ALA A CB    1 
ATOM   975  N  N     . SER B 2 158 ? -16.379 34.714 148.377 1.00 11.46 ? 158 SER A N     1 
ATOM   976  C  CA    . SER B 2 158 ? -17.571 34.706 147.523 1.00 10.72 ? 158 SER A CA    1 
ATOM   977  C  C     . SER B 2 158 ? -17.289 35.499 146.265 1.00 9.75  ? 158 SER A C     1 
ATOM   978  O  O     . SER B 2 158 ? -18.146 36.213 145.731 1.00 8.66  ? 158 SER A O     1 
ATOM   979  C  CB    . SER B 2 158 ? -18.760 35.233 148.321 1.00 11.12 ? 158 SER A CB    1 
ATOM   980  O  OG    . SER B 2 158 ? -18.707 36.661 148.375 1.00 11.98 ? 158 SER A OG    1 
ATOM   981  N  N     . ARG B 2 159 ? -16.071 35.346 145.777 1.00 10.03 ? 159 ARG A N     1 
ATOM   982  C  CA    . ARG B 2 159 ? -15.642 36.076 144.571 1.00 9.52  ? 159 ARG A CA    1 
ATOM   983  C  C     . ARG B 2 159 ? -15.998 35.385 143.301 1.00 9.55  ? 159 ARG A C     1 
ATOM   984  O  O     . ARG B 2 159 ? -16.130 36.134 142.281 1.00 11.25 ? 159 ARG A O     1 
ATOM   985  C  CB    . ARG B 2 159 ? -14.173 36.470 144.682 1.00 9.34  ? 159 ARG A CB    1 
ATOM   986  C  CG    . ARG B 2 159 ? -13.882 36.923 146.125 1.00 10.12 ? 159 ARG A CG    1 
ATOM   987  C  CD    . ARG B 2 159 ? -13.648 38.367 146.229 1.00 12.99 ? 159 ARG A CD    1 
ATOM   988  N  NE    . ARG B 2 159 ? -14.734 39.210 146.665 1.00 14.83 ? 159 ARG A NE    1 
ATOM   989  C  CZ    . ARG B 2 159 ? -14.616 40.106 147.660 1.00 14.85 ? 159 ARG A CZ    1 
ATOM   990  N  NH1   . ARG B 2 159 ? -13.479 40.172 148.341 1.00 15.04 ? 159 ARG A NH1   1 
ATOM   991  N  NH2   . ARG B 2 159 ? -15.617 40.899 148.004 1.00 15.93 ? 159 ARG A NH2   1 
ATOM   992  N  N     . SER B 2 160 ? -16.234 34.087 143.271 1.00 8.20  ? 160 SER A N     1 
ATOM   993  C  CA    . SER B 2 160 ? -16.585 33.453 141.990 1.00 7.88  ? 160 SER A CA    1 
ATOM   994  C  C     . SER B 2 160 ? -18.033 33.114 141.825 1.00 8.72  ? 160 SER A C     1 
ATOM   995  O  O     . SER B 2 160 ? -18.325 32.252 140.935 1.00 10.19 ? 160 SER A O     1 
ATOM   996  C  CB    . SER B 2 160 ? -15.724 32.238 141.732 1.00 6.24  ? 160 SER A CB    1 
ATOM   997  O  OG    . SER B 2 160 ? -15.139 31.797 142.945 1.00 9.71  ? 160 SER A OG    1 
ATOM   998  N  N     . ASP B 2 161 ? -18.971 33.710 142.556 1.00 9.49  ? 161 ASP A N     1 
ATOM   999  C  CA    . ASP B 2 161 ? -20.378 33.318 142.326 1.00 9.77  ? 161 ASP A CA    1 
ATOM   1000 C  C     . ASP B 2 161 ? -20.797 33.762 140.925 1.00 9.86  ? 161 ASP A C     1 
ATOM   1001 O  O     . ASP B 2 161 ? -21.460 33.016 140.194 1.00 10.97 ? 161 ASP A O     1 
ATOM   1002 C  CB    . ASP B 2 161 ? -21.371 33.737 143.365 1.00 9.83  ? 161 ASP A CB    1 
ATOM   1003 C  CG    . ASP B 2 161 ? -20.793 33.688 144.772 1.00 12.11 ? 161 ASP A CG    1 
ATOM   1004 O  OD1   . ASP B 2 161 ? -19.518 33.743 144.934 1.00 12.13 ? 161 ASP A OD1   1 
ATOM   1005 O  OD2   . ASP B 2 161 ? -21.578 33.591 145.787 1.00 16.33 ? 161 ASP A OD2   1 
ATOM   1006 N  N     . GLN B 2 162 ? -20.365 34.947 140.556 1.00 9.58  ? 162 GLN A N     1 
ATOM   1007 C  CA    . GLN B 2 162 ? -20.716 35.535 139.253 1.00 9.79  ? 162 GLN A CA    1 
ATOM   1008 C  C     . GLN B 2 162 ? -19.802 35.054 138.119 1.00 10.52 ? 162 GLN A C     1 
ATOM   1009 O  O     . GLN B 2 162 ? -20.273 34.687 137.031 1.00 11.68 ? 162 GLN A O     1 
ATOM   1010 C  CB    . GLN B 2 162 ? -20.583 37.055 139.305 1.00 9.43  ? 162 GLN A CB    1 
ATOM   1011 C  CG    . GLN B 2 162 ? -21.931 37.767 139.240 1.00 9.26  ? 162 GLN A CG    1 
ATOM   1012 C  CD    . GLN B 2 162 ? -23.030 37.009 139.981 1.00 10.08 ? 162 GLN A CD    1 
ATOM   1013 O  OE1   . GLN B 2 162 ? -23.292 37.296 141.147 1.00 11.11 ? 162 GLN A OE1   1 
ATOM   1014 N  NE2   . GLN B 2 162 ? -23.692 36.045 139.371 1.00 10.87 ? 162 GLN A NE2   1 
ATOM   1015 N  N     . VAL B 2 163 ? -18.519 35.072 138.402 1.00 10.72 ? 163 VAL A N     1 
ATOM   1016 C  CA    . VAL B 2 163 ? -17.485 34.755 137.410 1.00 9.57  ? 163 VAL A CA    1 
ATOM   1017 C  C     . VAL B 2 163 ? -16.448 33.793 138.014 1.00 10.03 ? 163 VAL A C     1 
ATOM   1018 O  O     . VAL B 2 163 ? -16.144 33.847 139.211 1.00 10.10 ? 163 VAL A O     1 
ATOM   1019 C  CB    . VAL B 2 163 ? -16.849 36.085 137.003 1.00 7.29  ? 163 VAL A CB    1 
ATOM   1020 C  CG1   . VAL B 2 163 ? -15.363 35.981 136.693 1.00 7.12  ? 163 VAL A CG1   1 
ATOM   1021 C  CG2   . VAL B 2 163 ? -17.503 36.710 135.769 1.00 4.95  ? 163 VAL A CG2   1 
ATOM   1022 N  N     . SER B 2 164 ? -15.912 32.922 137.166 1.00 10.56 ? 164 SER A N     1 
ATOM   1023 C  CA    . SER B 2 164 ? -14.923 31.913 137.601 1.00 11.20 ? 164 SER A CA    1 
ATOM   1024 C  C     . SER B 2 164 ? -13.518 32.233 137.074 1.00 11.65 ? 164 SER A C     1 
ATOM   1025 O  O     . SER B 2 164 ? -12.506 31.961 137.742 1.00 12.43 ? 164 SER A O     1 
ATOM   1026 C  CB    . SER B 2 164 ? -15.316 30.524 137.087 1.00 11.35 ? 164 SER A CB    1 
ATOM   1027 O  OG    . SER B 2 164 ? -14.853 30.347 135.756 1.00 10.77 ? 164 SER A OG    1 
ATOM   1028 N  N     . SER B 2 165 ? -13.479 32.809 135.883 1.00 11.33 ? 165 SER A N     1 
ATOM   1029 C  CA    . SER B 2 165 ? -12.206 33.122 135.216 1.00 10.94 ? 165 SER A CA    1 
ATOM   1030 C  C     . SER B 2 165 ? -12.253 34.421 134.458 1.00 10.94 ? 165 SER A C     1 
ATOM   1031 O  O     . SER B 2 165 ? -13.365 34.969 134.266 1.00 11.87 ? 165 SER A O     1 
ATOM   1032 C  CB    . SER B 2 165 ? -11.868 32.013 134.222 1.00 11.34 ? 165 SER A CB    1 
ATOM   1033 O  OG    . SER B 2 165 ? -11.048 31.042 134.850 1.00 14.18 ? 165 SER A OG    1 
ATOM   1034 N  N     . PHE B 2 166 ? -11.106 34.873 133.979 1.00 9.94  ? 166 PHE A N     1 
ATOM   1035 C  CA    . PHE B 2 166 ? -11.055 36.142 133.214 1.00 9.43  ? 166 PHE A CA    1 
ATOM   1036 C  C     . PHE B 2 166 ? -9.726  36.255 132.491 1.00 9.40  ? 166 PHE A C     1 
ATOM   1037 O  O     . PHE B 2 166 ? -8.730  35.669 132.935 1.00 9.25  ? 166 PHE A O     1 
ATOM   1038 C  CB    . PHE B 2 166 ? -11.179 37.299 134.242 1.00 7.95  ? 166 PHE A CB    1 
ATOM   1039 C  CG    . PHE B 2 166 ? -9.903  37.450 135.057 1.00 6.40  ? 166 PHE A CG    1 
ATOM   1040 C  CD1   . PHE B 2 166 ? -9.700  36.681 136.209 1.00 4.24  ? 166 PHE A CD1   1 
ATOM   1041 C  CD2   . PHE B 2 166 ? -8.906  38.339 134.626 1.00 3.45  ? 166 PHE A CD2   1 
ATOM   1042 C  CE1   . PHE B 2 166 ? -8.508  36.777 136.923 1.00 3.23  ? 166 PHE A CE1   1 
ATOM   1043 C  CE2   . PHE B 2 166 ? -7.708  38.435 135.330 1.00 3.24  ? 166 PHE A CE2   1 
ATOM   1044 C  CZ    . PHE B 2 166 ? -7.508  37.656 136.464 1.00 3.37  ? 166 PHE A CZ    1 
ATOM   1045 N  N     . ARG B 2 167 ? -9.685  37.002 131.430 1.00 9.26  ? 167 ARG A N     1 
ATOM   1046 C  CA    . ARG B 2 167 ? -8.477  37.298 130.656 1.00 8.35  ? 167 ARG A CA    1 
ATOM   1047 C  C     . ARG B 2 167 ? -8.576  38.795 130.280 1.00 8.34  ? 167 ARG A C     1 
ATOM   1048 O  O     . ARG B 2 167 ? -9.695  39.212 129.944 1.00 9.12  ? 167 ARG A O     1 
ATOM   1049 C  CB    . ARG B 2 167 ? -8.182  36.507 129.413 1.00 5.47  ? 167 ARG A CB    1 
ATOM   1050 C  CG    . ARG B 2 167 ? -9.194  35.581 128.827 1.00 4.92  ? 167 ARG A CG    1 
ATOM   1051 C  CD    . ARG B 2 167 ? -9.463  35.802 127.384 1.00 4.87  ? 167 ARG A CD    1 
ATOM   1052 N  NE    . ARG B 2 167 ? -8.684  34.848 126.603 1.00 6.12  ? 167 ARG A NE    1 
ATOM   1053 C  CZ    . ARG B 2 167 ? -9.114  34.443 125.412 1.00 7.52  ? 167 ARG A CZ    1 
ATOM   1054 N  NH1   . ARG B 2 167 ? -10.346 34.754 125.040 1.00 5.79  ? 167 ARG A NH1   1 
ATOM   1055 N  NH2   . ARG B 2 167 ? -8.379  33.676 124.608 1.00 9.23  ? 167 ARG A NH2   1 
ATOM   1056 N  N     . TYR B 2 168 ? -7.484  39.497 130.363 1.00 7.88  ? 168 TYR A N     1 
ATOM   1057 C  CA    . TYR B 2 168 ? -7.391  40.921 130.041 1.00 8.31  ? 168 TYR A CA    1 
ATOM   1058 C  C     . TYR B 2 168 ? -7.179  41.161 128.540 1.00 8.56  ? 168 TYR A C     1 
ATOM   1059 O  O     . TYR B 2 168 ? -6.227  40.635 127.919 1.00 8.56  ? 168 TYR A O     1 
ATOM   1060 C  CB    . TYR B 2 168 ? -6.201  41.615 130.761 1.00 8.72  ? 168 TYR A CB    1 
ATOM   1061 C  CG    . TYR B 2 168 ? -6.556  42.144 132.121 1.00 7.68  ? 168 TYR A CG    1 
ATOM   1062 C  CD1   . TYR B 2 168 ? -6.508  41.277 133.217 1.00 9.50  ? 168 TYR A CD1   1 
ATOM   1063 C  CD2   . TYR B 2 168 ? -6.958  43.461 132.325 1.00 6.21  ? 168 TYR A CD2   1 
ATOM   1064 C  CE1   . TYR B 2 168 ? -6.845  41.687 134.496 1.00 9.05  ? 168 TYR A CE1   1 
ATOM   1065 C  CE2   . TYR B 2 168 ? -7.289  43.892 133.600 1.00 5.26  ? 168 TYR A CE2   1 
ATOM   1066 C  CZ    . TYR B 2 168 ? -7.222  43.001 134.677 1.00 6.40  ? 168 TYR A CZ    1 
ATOM   1067 O  OH    . TYR B 2 168 ? -7.516  43.387 135.957 1.00 5.98  ? 168 TYR A OH    1 
ATOM   1068 N  N     . ALA B 2 169 ? -8.034  42.012 128.030 1.00 9.17  ? 169 ALA A N     1 
ATOM   1069 C  CA    . ALA B 2 169 ? -7.929  42.382 126.615 1.00 9.57  ? 169 ALA A CA    1 
ATOM   1070 C  C     . ALA B 2 169 ? -7.150  43.703 126.522 1.00 10.67 ? 169 ALA A C     1 
ATOM   1071 O  O     . ALA B 2 169 ? -6.445  43.965 125.539 1.00 11.39 ? 169 ALA A O     1 
ATOM   1072 C  CB    . ALA B 2 169 ? -9.318  42.554 126.015 1.00 6.23  ? 169 ALA A CB    1 
ATOM   1073 N  N     . SER B 2 170 ? -7.348  44.522 127.554 1.00 11.54 ? 170 SER A N     1 
ATOM   1074 C  CA    . SER B 2 170 ? -6.691  45.835 127.644 1.00 12.44 ? 170 SER A CA    1 
ATOM   1075 C  C     . SER B 2 170 ? -6.688  46.436 129.052 1.00 12.73 ? 170 SER A C     1 
ATOM   1076 O  O     . SER B 2 170 ? -7.393  46.060 129.992 1.00 13.53 ? 170 SER A O     1 
ATOM   1077 C  CB    . SER B 2 170 ? -7.327  46.844 126.693 1.00 12.23 ? 170 SER A CB    1 
ATOM   1078 O  OG    . SER B 2 170 ? -8.589  47.232 127.212 1.00 13.86 ? 170 SER A OG    1 
ATOM   1079 N  N     . MET B 2 171 ? -5.851  47.460 129.128 1.00 12.30 ? 171 MET A N     1 
ATOM   1080 C  CA    . MET B 2 171 ? -5.613  48.218 130.374 1.00 12.24 ? 171 MET A CA    1 
ATOM   1081 C  C     . MET B 2 171 ? -4.833  49.481 130.002 1.00 12.70 ? 171 MET A C     1 
ATOM   1082 O  O     . MET B 2 171 ? -3.632  49.413 129.691 1.00 13.74 ? 171 MET A O     1 
ATOM   1083 C  CB    . MET B 2 171 ? -4.792  47.303 131.297 1.00 10.14 ? 171 MET A CB    1 
ATOM   1084 C  CG    . MET B 2 171 ? -4.627  47.898 132.663 1.00 10.14 ? 171 MET A CG    1 
ATOM   1085 S  SD    . MET B 2 171 ? -3.817  46.693 133.752 1.00 12.54 ? 171 MET A SD    1 
ATOM   1086 C  CE    . MET B 2 171 ? -2.081  46.896 133.324 1.00 9.04  ? 171 MET A CE    1 
ATOM   1087 N  N     . ASN B 2 172 ? -5.521  50.601 130.023 1.00 11.90 ? 172 ASN A N     1 
ATOM   1088 C  CA    . ASN B 2 172 ? -4.937  51.907 129.681 1.00 10.73 ? 172 ASN A CA    1 
ATOM   1089 C  C     . ASN B 2 172 ? -5.165  52.859 130.855 1.00 10.49 ? 172 ASN A C     1 
ATOM   1090 O  O     . ASN B 2 172 ? -6.103  52.633 131.619 1.00 9.79  ? 172 ASN A O     1 
ATOM   1091 C  CB    . ASN B 2 172 ? -5.623  52.471 128.436 1.00 10.74 ? 172 ASN A CB    1 
ATOM   1092 C  CG    . ASN B 2 172 ? -5.517  51.633 127.185 1.00 11.84 ? 172 ASN A CG    1 
ATOM   1093 O  OD1   . ASN B 2 172 ? -6.150  50.583 127.037 1.00 10.59 ? 172 ASN A OD1   1 
ATOM   1094 N  ND2   . ASN B 2 172 ? -4.703  52.118 126.226 1.00 12.34 ? 172 ASN A ND2   1 
ATOM   1095 N  N     . VAL B 2 173 ? -4.370  53.899 130.900 1.00 9.83  ? 173 VAL A N     1 
ATOM   1096 C  CA    . VAL B 2 173 ? -4.458  54.936 131.925 1.00 10.34 ? 173 VAL A CA    1 
ATOM   1097 C  C     . VAL B 2 173 ? -4.304  56.324 131.298 1.00 10.57 ? 173 VAL A C     1 
ATOM   1098 O  O     . VAL B 2 173 ? -3.581  56.450 130.294 1.00 11.83 ? 173 VAL A O     1 
ATOM   1099 C  CB    . VAL B 2 173 ? -3.373  54.736 133.006 1.00 11.06 ? 173 VAL A CB    1 
ATOM   1100 C  CG1   . VAL B 2 173 ? -1.975  55.055 132.481 1.00 10.28 ? 173 VAL A CG1   1 
ATOM   1101 C  CG2   . VAL B 2 173 ? -3.699  55.572 134.241 1.00 10.16 ? 173 VAL A CG2   1 
ATOM   1102 N  N     . GLY B 2 174 ? -4.944  57.279 131.952 1.00 10.31 ? 174 GLY A N     1 
ATOM   1103 C  CA    . GLY B 2 174 ? -4.881  58.664 131.510 1.00 10.30 ? 174 GLY A CA    1 
ATOM   1104 C  C     . GLY B 2 174 ? -4.999  59.688 132.615 1.00 10.15 ? 174 GLY A C     1 
ATOM   1105 O  O     . GLY B 2 174 ? -5.867  59.594 133.495 1.00 10.08 ? 174 GLY A O     1 
ATOM   1106 N  N     . ILE B 2 175 ? -4.139  60.695 132.592 1.00 10.06 ? 175 ILE A N     1 
ATOM   1107 C  CA    . ILE B 2 175 ? -4.097  61.816 133.517 1.00 9.21  ? 175 ILE A CA    1 
ATOM   1108 C  C     . ILE B 2 175 ? -4.286  63.110 132.712 1.00 9.22  ? 175 ILE A C     1 
ATOM   1109 O  O     . ILE B 2 175 ? -3.455  63.472 131.878 1.00 9.80  ? 175 ILE A O     1 
ATOM   1110 C  CB    . ILE B 2 175 ? -2.780  61.859 134.344 1.00 6.76  ? 175 ILE A CB    1 
ATOM   1111 C  CG1   . ILE B 2 175 ? -2.640  60.556 135.169 1.00 7.60  ? 175 ILE A CG1   1 
ATOM   1112 C  CG2   . ILE B 2 175 ? -2.708  63.099 135.274 1.00 3.81  ? 175 ILE A CG2   1 
ATOM   1113 C  CD1   . ILE B 2 175 ? -2.243  60.843 136.647 1.00 8.30  ? 175 ILE A CD1   1 
ATOM   1114 N  N     . TYR B 2 176 ? -5.379  63.778 132.971 1.00 8.88  ? 176 TYR A N     1 
ATOM   1115 C  CA    . TYR B 2 176 ? -5.765  65.037 132.325 1.00 8.99  ? 176 TYR A CA    1 
ATOM   1116 C  C     . TYR B 2 176 ? -5.829  66.169 133.341 1.00 9.02  ? 176 TYR A C     1 
ATOM   1117 O  O     . TYR B 2 176 ? -6.877  66.440 133.972 1.00 9.05  ? 176 TYR A O     1 
ATOM   1118 C  CB    . TYR B 2 176 ? -7.132  64.859 131.622 1.00 10.04 ? 176 TYR A CB    1 
ATOM   1119 C  CG    . TYR B 2 176 ? -7.192  63.650 130.730 1.00 10.89 ? 176 TYR A CG    1 
ATOM   1120 C  CD1   . TYR B 2 176 ? -7.509  62.390 131.244 1.00 11.91 ? 176 TYR A CD1   1 
ATOM   1121 C  CD2   . TYR B 2 176 ? -6.929  63.754 129.358 1.00 10.77 ? 176 TYR A CD2   1 
ATOM   1122 C  CE1   . TYR B 2 176 ? -7.536  61.256 130.436 1.00 12.09 ? 176 TYR A CE1   1 
ATOM   1123 C  CE2   . TYR B 2 176 ? -6.968  62.625 128.537 1.00 11.55 ? 176 TYR A CE2   1 
ATOM   1124 C  CZ    . TYR B 2 176 ? -7.267  61.377 129.082 1.00 13.22 ? 176 TYR A CZ    1 
ATOM   1125 O  OH    . TYR B 2 176 ? -7.299  60.255 128.309 1.00 13.46 ? 176 TYR A OH    1 
ATOM   1126 N  N     . PRO B 2 177 ? -4.695  66.836 133.506 1.00 9.06  ? 177 PRO A N     1 
ATOM   1127 C  CA    . PRO B 2 177 ? -4.602  67.943 134.474 1.00 9.08  ? 177 PRO A CA    1 
ATOM   1128 C  C     . PRO B 2 177 ? -5.689  68.993 134.241 1.00 9.87  ? 177 PRO A C     1 
ATOM   1129 O  O     . PRO B 2 177 ? -6.120  69.295 133.117 1.00 10.41 ? 177 PRO A O     1 
ATOM   1130 C  CB    . PRO B 2 177 ? -3.187  68.465 134.374 1.00 8.78  ? 177 PRO A CB    1 
ATOM   1131 C  CG    . PRO B 2 177 ? -2.421  67.430 133.625 1.00 9.56  ? 177 PRO A CG    1 
ATOM   1132 C  CD    . PRO B 2 177 ? -3.419  66.592 132.837 1.00 9.52  ? 177 PRO A CD    1 
ATOM   1133 N  N     . THR B 2 178 ? -6.099  69.530 135.391 1.00 9.94  ? 178 THR A N     1 
ATOM   1134 C  CA    . THR B 2 178 ? -7.111  70.579 135.443 1.00 11.03 ? 178 THR A CA    1 
ATOM   1135 C  C     . THR B 2 178 ? -6.656  71.786 136.253 1.00 12.85 ? 178 THR A C     1 
ATOM   1136 O  O     . THR B 2 178 ? -7.498  72.672 136.495 1.00 15.58 ? 178 THR A O     1 
ATOM   1137 C  CB    . THR B 2 178 ? -8.495  70.013 135.952 1.00 9.91  ? 178 THR A CB    1 
ATOM   1138 O  OG1   . THR B 2 178 ? -8.228  69.488 137.290 1.00 12.28 ? 178 THR A OG1   1 
ATOM   1139 C  CG2   . THR B 2 178 ? -9.103  68.975 135.003 1.00 9.55  ? 178 THR A CG2   1 
ATOM   1140 N  N     . SER B 2 179 ? -5.405  71.826 136.671 1.00 12.37 ? 179 SER A N     1 
ATOM   1141 C  CA    . SER B 2 179 ? -4.856  72.988 137.394 1.00 12.00 ? 179 SER A CA    1 
ATOM   1142 C  C     . SER B 2 179 ? -4.716  74.080 136.300 1.00 12.61 ? 179 SER A C     1 
ATOM   1143 O  O     . SER B 2 179 ? -4.816  73.726 135.108 1.00 13.26 ? 179 SER A O     1 
ATOM   1144 C  CB    . SER B 2 179 ? -3.483  72.777 137.987 1.00 9.99  ? 179 SER A CB    1 
ATOM   1145 O  OG    . SER B 2 179 ? -3.376  71.633 138.790 1.00 7.04  ? 179 SER A OG    1 
ATOM   1146 N  N     . ASN B 2 180 ? -4.500  75.279 136.768 1.00 12.16 ? 180 ASN A N     1 
ATOM   1147 C  CA    . ASN B 2 180 ? -4.266  76.429 135.866 1.00 12.84 ? 180 ASN A CA    1 
ATOM   1148 C  C     . ASN B 2 180 ? -2.731  76.605 135.727 1.00 12.89 ? 180 ASN A C     1 
ATOM   1149 O  O     . ASN B 2 180 ? -1.956  76.152 136.584 1.00 12.74 ? 180 ASN A O     1 
ATOM   1150 C  CB    . ASN B 2 180 ? -4.934  77.693 136.342 1.00 15.29 ? 180 ASN A CB    1 
ATOM   1151 C  CG    . ASN B 2 180 ? -4.340  78.232 137.645 1.00 17.04 ? 180 ASN A CG    1 
ATOM   1152 O  OD1   . ASN B 2 180 ? -3.134  78.461 137.724 1.00 18.02 ? 180 ASN A OD1   1 
ATOM   1153 N  ND2   . ASN B 2 180 ? -5.123  78.452 138.685 1.00 17.40 ? 180 ASN A ND2   1 
ATOM   1154 N  N     . LEU B 2 181 ? -2.337  77.261 134.643 1.00 13.49 ? 181 LEU A N     1 
ATOM   1155 C  CA    . LEU B 2 181 ? -0.913  77.432 134.246 1.00 14.73 ? 181 LEU A CA    1 
ATOM   1156 C  C     . LEU B 2 181 ? -0.101  78.394 135.142 1.00 15.78 ? 181 LEU A C     1 
ATOM   1157 O  O     . LEU B 2 181 ? 0.858   79.036 134.683 1.00 18.45 ? 181 LEU A O     1 
ATOM   1158 C  CB    . LEU B 2 181 ? -0.827  77.994 132.824 1.00 14.08 ? 181 LEU A CB    1 
ATOM   1159 C  CG    . LEU B 2 181 ? -0.599  76.915 131.762 1.00 12.46 ? 181 LEU A CG    1 
ATOM   1160 C  CD1   . LEU B 2 181 ? -1.219  75.567 132.136 1.00 10.54 ? 181 LEU A CD1   1 
ATOM   1161 C  CD2   . LEU B 2 181 ? -1.196  77.282 130.401 1.00 12.06 ? 181 LEU A CD2   1 
ATOM   1162 N  N     . MET B 2 182 ? -0.467  78.490 136.409 1.00 14.59 ? 182 MET A N     1 
ATOM   1163 C  CA    . MET B 2 182 ? 0.273   79.348 137.363 1.00 13.73 ? 182 MET A CA    1 
ATOM   1164 C  C     . MET B 2 182 ? 0.411   78.679 138.731 1.00 13.64 ? 182 MET A C     1 
ATOM   1165 O  O     . MET B 2 182 ? 1.308   79.014 139.518 1.00 14.72 ? 182 MET A O     1 
ATOM   1166 C  CB    . MET B 2 182 ? -0.425  80.686 137.601 1.00 16.28 ? 182 MET A CB    1 
ATOM   1167 C  CG    . MET B 2 182 ? -0.269  81.172 139.051 1.00 20.43 ? 182 MET A CG    1 
ATOM   1168 S  SD    . MET B 2 182 ? 0.596   82.724 139.198 1.00 27.32 ? 182 MET A SD    1 
ATOM   1169 C  CE    . MET B 2 182 ? 2.351   82.475 139.019 1.00 23.36 ? 182 MET A CE    1 
ATOM   1170 N  N     . GLN B 2 183 ? -0.486  77.742 139.015 1.00 12.58 ? 183 GLN A N     1 
ATOM   1171 C  CA    . GLN B 2 183 ? -0.444  77.028 140.301 1.00 11.97 ? 183 GLN A CA    1 
ATOM   1172 C  C     . GLN B 2 183 ? 0.339   75.699 140.186 1.00 12.63 ? 183 GLN A C     1 
ATOM   1173 O  O     . GLN B 2 183 ? 1.111   75.334 141.076 1.00 13.65 ? 183 GLN A O     1 
ATOM   1174 C  CB    . GLN B 2 183 ? -1.851  76.743 140.855 1.00 11.80 ? 183 GLN A CB    1 
ATOM   1175 C  CG    . GLN B 2 183 ? -2.855  76.236 139.821 1.00 12.70 ? 183 GLN A CG    1 
ATOM   1176 C  CD    . GLN B 2 183 ? -4.250  76.007 140.420 1.00 15.41 ? 183 GLN A CD    1 
ATOM   1177 O  OE1   . GLN B 2 183 ? -5.180  75.649 139.699 1.00 18.57 ? 183 GLN A OE1   1 
ATOM   1178 N  NE2   . GLN B 2 183 ? -4.457  76.195 141.712 1.00 14.08 ? 183 GLN A NE2   1 
ATOM   1179 N  N     . PHE B 2 184 ? 0.162   74.967 139.088 1.00 11.78 ? 184 PHE A N     1 
ATOM   1180 C  CA    . PHE B 2 184 ? 0.826   73.639 138.921 1.00 11.21 ? 184 PHE A CA    1 
ATOM   1181 C  C     . PHE B 2 184 ? 2.366   73.753 138.957 1.00 11.02 ? 184 PHE A C     1 
ATOM   1182 O  O     . PHE B 2 184 ? 2.932   74.838 138.763 1.00 11.13 ? 184 PHE A O     1 
ATOM   1183 C  CB    . PHE B 2 184 ? 0.437   72.986 137.596 1.00 9.98  ? 184 PHE A CB    1 
ATOM   1184 C  CG    . PHE B 2 184 ? 1.455   73.248 136.492 1.00 9.67  ? 184 PHE A CG    1 
ATOM   1185 C  CD1   . PHE B 2 184 ? 2.558   72.398 136.331 1.00 8.77  ? 184 PHE A CD1   1 
ATOM   1186 C  CD2   . PHE B 2 184 ? 1.280   74.343 135.647 1.00 11.12 ? 184 PHE A CD2   1 
ATOM   1187 C  CE1   . PHE B 2 184 ? 3.491   72.654 135.319 1.00 7.73  ? 184 PHE A CE1   1 
ATOM   1188 C  CE2   . PHE B 2 184 ? 2.212   74.600 134.637 1.00 11.89 ? 184 PHE A CE2   1 
ATOM   1189 C  CZ    . PHE B 2 184 ? 3.318   73.756 134.472 1.00 9.17  ? 184 PHE A CZ    1 
ATOM   1190 N  N     . ALA B 2 185 ? 2.979   72.595 139.209 1.00 10.99 ? 185 ALA A N     1 
ATOM   1191 C  CA    . ALA B 2 185 ? 4.451   72.425 139.297 1.00 10.99 ? 185 ALA A CA    1 
ATOM   1192 C  C     . ALA B 2 185 ? 4.777   70.949 139.484 1.00 11.59 ? 185 ALA A C     1 
ATOM   1193 O  O     . ALA B 2 185 ? 4.058   70.233 140.221 1.00 12.45 ? 185 ALA A O     1 
ATOM   1194 C  CB    . ALA B 2 185 ? 5.000   73.222 140.481 1.00 9.70  ? 185 ALA A CB    1 
ATOM   1195 N  N     . GLY B 2 186 ? 5.807   70.506 138.794 1.00 11.29 ? 186 GLY A N     1 
ATOM   1196 C  CA    . GLY B 2 186 ? 6.146   69.067 138.940 1.00 12.07 ? 186 GLY A CA    1 
ATOM   1197 C  C     . GLY B 2 186 ? 6.001   68.340 137.610 1.00 12.45 ? 186 GLY A C     1 
ATOM   1198 O  O     . GLY B 2 186 ? 5.833   68.948 136.548 1.00 12.61 ? 186 GLY A O     1 
ATOM   1199 N  N     . SER B 2 187 ? 6.054   67.022 137.755 1.00 12.35 ? 187 SER A N     1 
ATOM   1200 C  CA    . SER B 2 187 ? 5.995   66.149 136.576 1.00 12.94 ? 187 SER A CA    1 
ATOM   1201 C  C     . SER B 2 187 ? 5.305   64.811 136.774 1.00 13.58 ? 187 SER A C     1 
ATOM   1202 O  O     . SER B 2 187 ? 4.912   64.392 137.859 1.00 14.08 ? 187 SER A O     1 
ATOM   1203 C  CB    . SER B 2 187 ? 7.503   65.797 136.315 1.00 12.06 ? 187 SER A CB    1 
ATOM   1204 O  OG    . SER B 2 187 ? 8.013   65.401 137.600 1.00 10.74 ? 187 SER A OG    1 
ATOM   1205 N  N     . ILE B 2 188 ? 5.223   64.109 135.656 1.00 13.48 ? 188 ILE A N     1 
ATOM   1206 C  CA    . ILE B 2 188 ? 4.682   62.776 135.506 1.00 13.07 ? 188 ILE A CA    1 
ATOM   1207 C  C     . ILE B 2 188 ? 5.786   61.877 134.920 1.00 13.56 ? 188 ILE A C     1 
ATOM   1208 O  O     . ILE B 2 188 ? 6.531   62.300 134.022 1.00 14.74 ? 188 ILE A O     1 
ATOM   1209 C  CB    . ILE B 2 188 ? 3.383   62.710 134.644 1.00 9.05  ? 188 ILE A CB    1 
ATOM   1210 C  CG1   . ILE B 2 188 ? 2.276   63.558 135.309 1.00 8.04  ? 188 ILE A CG1   1 
ATOM   1211 C  CG2   . ILE B 2 188 ? 2.954   61.222 134.460 1.00 7.18  ? 188 ILE A CG2   1 
ATOM   1212 C  CD1   . ILE B 2 188 ? 0.843   63.271 134.796 1.00 8.81  ? 188 ILE A CD1   1 
ATOM   1213 N  N     . THR B 2 189 ? 5.859   60.701 135.525 1.00 12.40 ? 189 THR A N     1 
ATOM   1214 C  CA    . THR B 2 189 ? 6.852   59.707 135.117 1.00 11.65 ? 189 THR A CA    1 
ATOM   1215 C  C     . THR B 2 189 ? 6.220   58.319 135.068 1.00 11.53 ? 189 THR A C     1 
ATOM   1216 O  O     . THR B 2 189 ? 5.695   57.843 136.069 1.00 12.24 ? 189 THR A O     1 
ATOM   1217 C  CB    . THR B 2 189 ? 8.141   59.655 136.002 1.00 11.47 ? 189 THR A CB    1 
ATOM   1218 O  OG1   . THR B 2 189 ? 8.556   61.041 136.207 1.00 12.91 ? 189 THR A OG1   1 
ATOM   1219 C  CG2   . THR B 2 189 ? 9.241   58.774 135.384 1.00 10.93 ? 189 THR A CG2   1 
ATOM   1220 N  N     . VAL B 2 190 ? 6.321   57.737 133.879 1.00 11.04 ? 190 VAL A N     1 
ATOM   1221 C  CA    . VAL B 2 190 ? 5.730   56.411 133.688 1.00 10.09 ? 190 VAL A CA    1 
ATOM   1222 C  C     . VAL B 2 190 ? 6.770   55.387 133.301 1.00 9.93  ? 190 VAL A C     1 
ATOM   1223 O  O     . VAL B 2 190 ? 7.729   55.717 132.586 1.00 10.77 ? 190 VAL A O     1 
ATOM   1224 C  CB    . VAL B 2 190 ? 4.541   56.558 132.743 1.00 8.94  ? 190 VAL A CB    1 
ATOM   1225 C  CG1   . VAL B 2 190 ? 3.831   55.210 132.593 1.00 7.57  ? 190 VAL A CG1   1 
ATOM   1226 C  CG2   . VAL B 2 190 ? 3.616   57.658 133.252 1.00 8.31  ? 190 VAL A CG2   1 
ATOM   1227 N  N     . TRP B 2 191 ? 6.534   54.216 133.853 1.00 8.72  ? 191 TRP A N     1 
ATOM   1228 C  CA    . TRP B 2 191 ? 7.411   53.044 133.629 1.00 8.34  ? 191 TRP A CA    1 
ATOM   1229 C  C     . TRP B 2 191 ? 6.544   51.804 133.858 1.00 8.35  ? 191 TRP A C     1 
ATOM   1230 O  O     . TRP B 2 191 ? 5.624   51.880 134.691 1.00 9.19  ? 191 TRP A O     1 
ATOM   1231 C  CB    . TRP B 2 191 ? 8.693   53.140 134.370 1.00 7.51  ? 191 TRP A CB    1 
ATOM   1232 C  CG    . TRP B 2 191 ? 8.844   52.908 135.809 1.00 8.13  ? 191 TRP A CG    1 
ATOM   1233 C  CD1   . TRP B 2 191 ? 9.205   51.739 136.434 1.00 9.16  ? 191 TRP A CD1   1 
ATOM   1234 C  CD2   . TRP B 2 191 ? 8.742   53.889 136.858 1.00 8.85  ? 191 TRP A CD2   1 
ATOM   1235 N  NE1   . TRP B 2 191 ? 9.288   51.920 137.781 1.00 9.17  ? 191 TRP A NE1   1 
ATOM   1236 C  CE2   . TRP B 2 191 ? 9.013   53.228 138.077 1.00 9.58  ? 191 TRP A CE2   1 
ATOM   1237 C  CE3   . TRP B 2 191 ? 8.444   55.255 136.866 1.00 8.65  ? 191 TRP A CE3   1 
ATOM   1238 C  CZ2   . TRP B 2 191 ? 8.972   53.894 139.307 1.00 8.72  ? 191 TRP A CZ2   1 
ATOM   1239 C  CZ3   . TRP B 2 191 ? 8.402   55.925 138.085 1.00 8.13  ? 191 TRP A CZ3   1 
ATOM   1240 C  CH2   . TRP B 2 191 ? 8.653   55.252 139.291 1.00 8.22  ? 191 TRP A CH2   1 
ATOM   1241 N  N     . LYS B 2 192 ? 6.760   50.762 133.082 1.00 7.60  ? 192 LYS A N     1 
ATOM   1242 C  CA    . LYS B 2 192 ? 5.942   49.540 133.260 1.00 6.77  ? 192 LYS A CA    1 
ATOM   1243 C  C     . LYS B 2 192 ? 6.806   48.487 133.940 1.00 7.23  ? 192 LYS A C     1 
ATOM   1244 O  O     . LYS B 2 192 ? 8.034   48.461 133.778 1.00 7.26  ? 192 LYS A O     1 
ATOM   1245 C  CB    . LYS B 2 192 ? 5.335   49.083 131.956 1.00 3.83  ? 192 LYS A CB    1 
ATOM   1246 C  CG    . LYS B 2 192 ? 4.357   50.047 131.318 1.00 3.26  ? 192 LYS A CG    1 
ATOM   1247 C  CD    . LYS B 2 192 ? 4.772   50.612 129.969 1.00 3.93  ? 192 LYS A CD    1 
ATOM   1248 C  CE    . LYS B 2 192 ? 3.558   50.966 129.129 1.00 4.95  ? 192 LYS A CE    1 
ATOM   1249 N  NZ    . LYS B 2 192 ? 3.906   51.642 127.870 1.00 5.21  ? 192 LYS A NZ    1 
ATOM   1250 N  N     . CYS B 2 193 ? 6.208   47.641 134.751 1.00 7.43  ? 193 CYS A N     1 
ATOM   1251 C  CA    . CYS B 2 193 ? 6.956   46.594 135.464 1.00 9.06  ? 193 CYS A CA    1 
ATOM   1252 C  C     . CYS B 2 193 ? 6.232   45.264 135.261 1.00 9.97  ? 193 CYS A C     1 
ATOM   1253 O  O     . CYS B 2 193 ? 4.995   45.328 135.230 1.00 11.28 ? 193 CYS A O     1 
ATOM   1254 C  CB    . CYS B 2 193 ? 6.938   46.874 136.968 1.00 11.75 ? 193 CYS A CB    1 
ATOM   1255 S  SG    . CYS B 2 193 ? 7.796   48.348 137.495 1.00 15.65 ? 193 CYS A SG    1 
ATOM   1256 N  N     . PRO B 2 194 ? 6.971   44.187 135.202 1.00 9.81  ? 194 PRO A N     1 
ATOM   1257 C  CA    . PRO B 2 194 ? 6.400   42.846 135.071 1.00 9.60  ? 194 PRO A CA    1 
ATOM   1258 C  C     . PRO B 2 194 ? 6.231   42.161 136.420 1.00 10.38 ? 194 PRO A C     1 
ATOM   1259 O  O     . PRO B 2 194 ? 6.958   41.185 136.694 1.00 11.87 ? 194 PRO A O     1 
ATOM   1260 C  CB    . PRO B 2 194 ? 7.447   42.113 134.232 1.00 9.06  ? 194 PRO A CB    1 
ATOM   1261 C  CG    . PRO B 2 194 ? 8.736   42.700 134.728 1.00 9.16  ? 194 PRO A CG    1 
ATOM   1262 C  CD    . PRO B 2 194 ? 8.440   44.113 135.232 1.00 9.59  ? 194 PRO A CD    1 
ATOM   1263 N  N     . VAL B 2 195 ? 5.304   42.656 137.223 1.00 10.31 ? 195 VAL A N     1 
ATOM   1264 C  CA    . VAL B 2 195 ? 5.056   42.030 138.535 1.00 10.63 ? 195 VAL A CA    1 
ATOM   1265 C  C     . VAL B 2 195 ? 4.098   40.858 138.286 1.00 11.49 ? 195 VAL A C     1 
ATOM   1266 O  O     . VAL B 2 195 ? 3.140   41.058 137.508 1.00 12.65 ? 195 VAL A O     1 
ATOM   1267 C  CB    . VAL B 2 195 ? 4.568   42.973 139.638 1.00 7.97  ? 195 VAL A CB    1 
ATOM   1268 C  CG1   . VAL B 2 195 ? 4.656   44.457 139.340 1.00 6.48  ? 195 VAL A CG1   1 
ATOM   1269 C  CG2   . VAL B 2 195 ? 3.165   42.631 140.110 1.00 8.61  ? 195 VAL A CG2   1 
ATOM   1270 N  N     . LYS B 2 196 ? 4.375   39.758 138.931 1.00 10.79 ? 196 LYS A N     1 
ATOM   1271 C  CA    . LYS B 2 196 ? 3.539   38.557 138.829 1.00 11.10 ? 196 LYS A CA    1 
ATOM   1272 C  C     . LYS B 2 196 ? 3.211   38.055 140.230 1.00 11.33 ? 196 LYS A C     1 
ATOM   1273 O  O     . LYS B 2 196 ? 3.963   38.363 141.164 1.00 11.48 ? 196 LYS A O     1 
ATOM   1274 C  CB    . LYS B 2 196 ? 4.256   37.448 138.057 1.00 10.64 ? 196 LYS A CB    1 
ATOM   1275 C  CG    . LYS B 2 196 ? 5.622   37.907 137.526 1.00 8.74  ? 196 LYS A CG    1 
ATOM   1276 C  CD    . LYS B 2 196 ? 5.480   38.405 136.100 1.00 8.11  ? 196 LYS A CD    1 
ATOM   1277 C  CE    . LYS B 2 196 ? 4.752   37.385 135.280 1.00 9.10  ? 196 LYS A CE    1 
ATOM   1278 N  NZ    . LYS B 2 196 ? 5.388   37.187 133.939 1.00 11.83 ? 196 LYS A NZ    1 
ATOM   1279 N  N     . LEU B 2 197 ? 2.123   37.323 140.326 1.00 12.08 ? 197 LEU A N     1 
ATOM   1280 C  CA    . LEU B 2 197 ? 1.657   36.759 141.607 1.00 12.65 ? 197 LEU A CA    1 
ATOM   1281 C  C     . LEU B 2 197 ? 2.239   35.344 141.697 1.00 13.04 ? 197 LEU A C     1 
ATOM   1282 O  O     . LEU B 2 197 ? 1.817   34.486 140.919 1.00 14.05 ? 197 LEU A O     1 
ATOM   1283 C  CB    . LEU B 2 197 ? 0.141   36.804 141.655 1.00 10.00 ? 197 LEU A CB    1 
ATOM   1284 C  CG    . LEU B 2 197 ? -0.461  36.116 142.883 1.00 7.31  ? 197 LEU A CG    1 
ATOM   1285 C  CD1   . LEU B 2 197 ? -0.261  37.021 144.087 1.00 6.46  ? 197 LEU A CD1   1 
ATOM   1286 C  CD2   . LEU B 2 197 ? -1.943  35.878 142.585 1.00 5.70  ? 197 LEU A CD2   1 
ATOM   1287 N  N     . SER B 2 198 ? 3.188   35.199 142.575 1.00 13.26 ? 198 SER A N     1 
ATOM   1288 C  CA    . SER B 2 198 ? 3.970   34.002 142.875 1.00 12.95 ? 198 SER A CA    1 
ATOM   1289 C  C     . SER B 2 198 ? 3.679   33.563 144.304 1.00 12.24 ? 198 SER A C     1 
ATOM   1290 O  O     . SER B 2 198 ? 2.674   33.988 144.882 1.00 12.92 ? 198 SER A O     1 
ATOM   1291 C  CB    . SER B 2 198 ? 5.451   34.304 142.681 1.00 14.46 ? 198 SER A CB    1 
ATOM   1292 O  OG    . SER B 2 198 ? 6.245   33.153 142.723 1.00 18.01 ? 198 SER A OG    1 
ATOM   1293 N  N     . ASN B 2 199 ? 4.520   32.720 144.857 1.00 11.55 ? 199 ASN A N     1 
ATOM   1294 C  CA    . ASN B 2 199 ? 4.269   32.237 146.238 1.00 12.14 ? 199 ASN A CA    1 
ATOM   1295 C  C     . ASN B 2 199 ? 5.607   32.249 146.983 1.00 12.88 ? 199 ASN A C     1 
ATOM   1296 O  O     . ASN B 2 199 ? 6.683   32.293 146.350 1.00 13.70 ? 199 ASN A O     1 
ATOM   1297 C  CB    . ASN B 2 199 ? 3.547   30.900 146.208 1.00 12.82 ? 199 ASN A CB    1 
ATOM   1298 C  CG    . ASN B 2 199 ? 4.284   29.902 145.329 1.00 15.79 ? 199 ASN A CG    1 
ATOM   1299 O  OD1   . ASN B 2 199 ? 5.506   29.672 145.462 1.00 16.54 ? 199 ASN A OD1   1 
ATOM   1300 N  ND2   . ASN B 2 199 ? 3.547   29.318 144.389 1.00 17.80 ? 199 ASN A ND2   1 
ATOM   1301 N  N     . VAL B 2 200 ? 5.486   32.242 148.294 1.00 12.50 ? 200 VAL A N     1 
ATOM   1302 C  CA    . VAL B 2 200 ? 6.596   32.239 149.256 1.00 11.14 ? 200 VAL A CA    1 
ATOM   1303 C  C     . VAL B 2 200 ? 6.390   31.020 150.165 1.00 11.34 ? 200 VAL A C     1 
ATOM   1304 O  O     . VAL B 2 200 ? 5.245   30.773 150.571 1.00 10.44 ? 200 VAL A O     1 
ATOM   1305 C  CB    . VAL B 2 200 ? 6.596   33.548 150.081 1.00 8.13  ? 200 VAL A CB    1 
ATOM   1306 C  CG1   . VAL B 2 200 ? 5.422   33.607 151.054 1.00 6.25  ? 200 VAL A CG1   1 
ATOM   1307 C  CG2   . VAL B 2 200 ? 7.896   33.774 150.817 1.00 4.88  ? 200 VAL A CG2   1 
ATOM   1308 N  N     . GLN B 2 201 ? 7.460   30.321 150.437 1.00 11.87 ? 201 GLN A N     1 
ATOM   1309 C  CA    . GLN B 2 201 ? 7.419   29.136 151.318 1.00 12.32 ? 201 GLN A CA    1 
ATOM   1310 C  C     . GLN B 2 201 ? 8.340   29.427 152.502 1.00 12.30 ? 201 GLN A C     1 
ATOM   1311 O  O     . GLN B 2 201 ? 9.490   29.853 152.240 1.00 13.48 ? 201 GLN A O     1 
ATOM   1312 C  CB    . GLN B 2 201 ? 7.776   27.846 150.635 1.00 14.83 ? 201 GLN A CB    1 
ATOM   1313 C  CG    . GLN B 2 201 ? 9.139   27.227 150.855 1.00 18.64 ? 201 GLN A CG    1 
ATOM   1314 C  CD    . GLN B 2 201 ? 9.154   25.783 150.341 1.00 21.07 ? 201 GLN A CD    1 
ATOM   1315 O  OE1   . GLN B 2 201 ? 8.093   25.266 149.958 1.00 22.54 ? 201 GLN A OE1   1 
ATOM   1316 N  NE2   . GLN B 2 201 ? 10.338  25.178 150.336 1.00 20.41 ? 201 GLN A NE2   1 
ATOM   1317 N  N     . PHE B 2 202 ? 7.797   29.220 153.684 1.00 11.51 ? 202 PHE A N     1 
ATOM   1318 C  CA    . PHE B 2 202 ? 8.572   29.437 154.933 1.00 10.76 ? 202 PHE A CA    1 
ATOM   1319 C  C     . PHE B 2 202 ? 8.057   28.622 156.094 1.00 11.33 ? 202 PHE A C     1 
ATOM   1320 O  O     . PHE B 2 202 ? 6.851   28.616 156.384 1.00 11.41 ? 202 PHE A O     1 
ATOM   1321 C  CB    . PHE B 2 202 ? 8.544   30.895 155.356 1.00 8.89  ? 202 PHE A CB    1 
ATOM   1322 C  CG    . PHE B 2 202 ? 7.117   31.366 155.632 1.00 10.51 ? 202 PHE A CG    1 
ATOM   1323 C  CD1   . PHE B 2 202 ? 6.251   31.626 154.564 1.00 10.88 ? 202 PHE A CD1   1 
ATOM   1324 C  CD2   . PHE B 2 202 ? 6.673   31.524 156.950 1.00 11.69 ? 202 PHE A CD2   1 
ATOM   1325 C  CE1   . PHE B 2 202 ? 4.939   32.044 154.813 1.00 13.21 ? 202 PHE A CE1   1 
ATOM   1326 C  CE2   . PHE B 2 202 ? 5.361   31.943 157.200 1.00 12.85 ? 202 PHE A CE2   1 
ATOM   1327 C  CZ    . PHE B 2 202 ? 4.493   32.203 156.131 1.00 12.38 ? 202 PHE A CZ    1 
ATOM   1328 N  N     . PRO B 2 203 ? 8.957   27.914 156.768 1.00 11.50 ? 203 PRO A N     1 
ATOM   1329 C  CA    . PRO B 2 203 ? 8.599   27.140 157.926 1.00 12.45 ? 203 PRO A CA    1 
ATOM   1330 C  C     . PRO B 2 203 ? 8.168   28.044 159.045 1.00 13.94 ? 203 PRO A C     1 
ATOM   1331 O  O     . PRO B 2 203 ? 8.964   28.939 159.462 1.00 14.96 ? 203 PRO A O     1 
ATOM   1332 C  CB    . PRO B 2 203 ? 9.887   26.458 158.324 1.00 11.61 ? 203 PRO A CB    1 
ATOM   1333 C  CG    . PRO B 2 203 ? 10.972  26.920 157.366 1.00 11.61 ? 203 PRO A CG    1 
ATOM   1334 C  CD    . PRO B 2 203 ? 10.368  27.867 156.381 1.00 11.47 ? 203 PRO A CD    1 
ATOM   1335 N  N     . VAL B 2 204 ? 6.954   27.846 159.515 1.00 14.44 ? 204 VAL A N     1 
ATOM   1336 C  CA    . VAL B 2 204 ? 6.480   28.581 160.693 1.00 14.75 ? 204 VAL A CA    1 
ATOM   1337 C  C     . VAL B 2 204 ? 6.909   27.737 161.894 1.00 15.17 ? 204 VAL A C     1 
ATOM   1338 O  O     . VAL B 2 204 ? 7.672   26.770 161.754 1.00 15.41 ? 204 VAL A O     1 
ATOM   1339 C  CB    . VAL B 2 204 ? 4.969   28.823 160.614 1.00 14.37 ? 204 VAL A CB    1 
ATOM   1340 C  CG1   . VAL B 2 204 ? 4.162   27.549 160.382 1.00 13.22 ? 204 VAL A CG1   1 
ATOM   1341 C  CG2   . VAL B 2 204 ? 4.399   29.457 161.886 1.00 12.84 ? 204 VAL A CG2   1 
ATOM   1342 N  N     . ALA B 2 205 ? 6.443   28.069 163.073 1.00 16.41 ? 205 ALA A N     1 
ATOM   1343 C  CA    . ALA B 2 205 ? 6.873   27.323 164.265 1.00 18.21 ? 205 ALA A CA    1 
ATOM   1344 C  C     . ALA B 2 205 ? 5.703   26.681 165.008 1.00 19.67 ? 205 ALA A C     1 
ATOM   1345 O  O     . ALA B 2 205 ? 5.845   26.239 166.158 1.00 20.28 ? 205 ALA A O     1 
ATOM   1346 C  CB    . ALA B 2 205 ? 7.609   28.245 165.232 1.00 17.88 ? 205 ALA A CB    1 
ATOM   1347 N  N     . THR B 2 206 ? 4.550   26.633 164.364 1.00 19.42 ? 206 THR A N     1 
ATOM   1348 C  CA    . THR B 2 206 ? 3.386   25.980 164.976 1.00 17.73 ? 206 THR A CA    1 
ATOM   1349 C  C     . THR B 2 206 ? 3.917   24.648 165.597 1.00 17.21 ? 206 THR A C     1 
ATOM   1350 O  O     . THR B 2 206 ? 4.965   24.124 165.184 1.00 18.50 ? 206 THR A O     1 
ATOM   1351 C  CB    . THR B 2 206 ? 2.304   25.766 163.914 1.00 16.70 ? 206 THR A CB    1 
ATOM   1352 O  OG1   . THR B 2 206 ? 2.590   24.598 163.159 1.00 15.70 ? 206 THR A OG1   1 
ATOM   1353 C  CG2   . THR B 2 206 ? 2.194   26.932 162.930 1.00 18.11 ? 206 THR A CG2   1 
ATOM   1354 N  N     . THR B 2 207 ? 3.199   24.116 166.589 1.00 15.57 ? 207 THR A N     1 
ATOM   1355 C  CA    . THR B 2 207 ? 3.617   22.891 167.345 1.00 14.24 ? 207 THR A CA    1 
ATOM   1356 C  C     . THR B 2 207 ? 3.839   21.693 166.433 1.00 13.70 ? 207 THR A C     1 
ATOM   1357 O  O     . THR B 2 207 ? 4.970   21.204 166.286 1.00 14.58 ? 207 THR A O     1 
ATOM   1358 C  CB    . THR B 2 207 ? 2.555   22.482 168.363 1.00 13.82 ? 207 THR A CB    1 
ATOM   1359 O  OG1   . THR B 2 207 ? 1.904   23.635 168.876 1.00 15.51 ? 207 THR A OG1   1 
ATOM   1360 C  CG2   . THR B 2 207 ? 3.133   21.715 169.554 1.00 12.85 ? 207 THR A CG2   1 
ATOM   1361 N  N     . PRO B 2 208 ? 2.810   21.141 165.775 1.00 12.62 ? 208 PRO A N     1 
ATOM   1362 C  CA    . PRO B 2 208 ? 3.031   20.009 164.912 1.00 12.26 ? 208 PRO A CA    1 
ATOM   1363 C  C     . PRO B 2 208 ? 4.067   20.421 163.918 1.00 12.72 ? 208 PRO A C     1 
ATOM   1364 O  O     . PRO B 2 208 ? 4.565   19.540 163.151 1.00 13.06 ? 208 PRO A O     1 
ATOM   1365 C  CB    . PRO B 2 208 ? 1.668   19.724 164.331 1.00 12.21 ? 208 PRO A CB    1 
ATOM   1366 C  CG    . PRO B 2 208 ? 0.693   20.730 164.922 1.00 12.50 ? 208 PRO A CG    1 
ATOM   1367 C  CD    . PRO B 2 208 ? 1.437   21.628 165.863 1.00 12.33 ? 208 PRO A CD    1 
ATOM   1368 N  N     . ALA B 2 209 ? 4.330   21.721 163.998 1.00 13.34 ? 209 ALA A N     1 
ATOM   1369 C  CA    . ALA B 2 209 ? 5.322   22.431 163.171 1.00 13.30 ? 209 ALA A CA    1 
ATOM   1370 C  C     . ALA B 2 209 ? 5.036   22.194 161.680 1.00 13.45 ? 209 ALA A C     1 
ATOM   1371 O  O     . ALA B 2 209 ? 5.021   21.047 161.207 1.00 12.69 ? 209 ALA A O     1 
ATOM   1372 C  CB    . ALA B 2 209 ? 6.726   21.934 163.510 1.00 11.76 ? 209 ALA A CB    1 
ATOM   1373 N  N     . THR B 2 210 ? 4.823   23.300 160.972 1.00 14.36 ? 210 THR A N     1 
ATOM   1374 C  CA    . THR B 2 210 ? 4.484   23.274 159.534 1.00 14.07 ? 210 THR A CA    1 
ATOM   1375 C  C     . THR B 2 210 ? 5.350   24.225 158.694 1.00 13.24 ? 210 THR A C     1 
ATOM   1376 O  O     . THR B 2 210 ? 5.993   25.142 159.228 1.00 13.40 ? 210 THR A O     1 
ATOM   1377 C  CB    . THR B 2 210 ? 3.041   23.743 159.312 1.00 14.94 ? 210 THR A CB    1 
ATOM   1378 O  OG1   . THR B 2 210 ? 2.917   25.117 159.662 1.00 18.21 ? 210 THR A OG1   1 
ATOM   1379 C  CG2   . THR B 2 210 ? 2.018   22.968 160.140 1.00 12.96 ? 210 THR A CG2   1 
ATOM   1380 N  N     . SER B 2 211 ? 5.304   23.930 157.401 1.00 11.64 ? 211 SER A N     1 
ATOM   1381 C  CA    . SER B 2 211 ? 5.934   24.723 156.327 1.00 11.56 ? 211 SER A CA    1 
ATOM   1382 C  C     . SER B 2 211 ? 4.782   25.465 155.635 1.00 11.09 ? 211 SER A C     1 
ATOM   1383 O  O     . SER B 2 211 ? 3.770   24.858 155.259 1.00 12.17 ? 211 SER A O     1 
ATOM   1384 C  CB    . SER B 2 211 ? 6.657   23.793 155.351 1.00 13.14 ? 211 SER A CB    1 
ATOM   1385 O  OG    . SER B 2 211 ? 7.942   24.314 155.044 1.00 14.64 ? 211 SER A OG    1 
ATOM   1386 N  N     . ALA B 2 212 ? 4.926   26.769 155.482 1.00 10.28 ? 212 ALA A N     1 
ATOM   1387 C  CA    . ALA B 2 212 ? 3.834   27.608 154.939 1.00 10.00 ? 212 ALA A CA    1 
ATOM   1388 C  C     . ALA B 2 212 ? 4.079   28.076 153.508 1.00 9.84  ? 212 ALA A C     1 
ATOM   1389 O  O     . ALA B 2 212 ? 5.179   28.560 153.147 1.00 9.42  ? 212 ALA A O     1 
ATOM   1390 C  CB    . ALA B 2 212 ? 3.661   28.861 155.799 1.00 10.55 ? 212 ALA A CB    1 
ATOM   1391 N  N     . LEU B 2 213 ? 3.053   27.965 152.692 1.00 8.98  ? 213 LEU A N     1 
ATOM   1392 C  CA    . LEU B 2 213 ? 3.027   28.384 151.292 1.00 8.71  ? 213 LEU A CA    1 
ATOM   1393 C  C     . LEU B 2 213 ? 1.941   29.465 151.165 1.00 8.97  ? 213 LEU A C     1 
ATOM   1394 O  O     . LEU B 2 213 ? 0.765   29.186 151.439 1.00 9.36  ? 213 LEU A O     1 
ATOM   1395 C  CB    . LEU B 2 213 ? 2.740   27.175 150.397 1.00 7.68  ? 213 LEU A CB    1 
ATOM   1396 C  CG    . LEU B 2 213 ? 2.583   27.553 148.917 1.00 7.55  ? 213 LEU A CG    1 
ATOM   1397 C  CD1   . LEU B 2 213 ? 3.904   28.057 148.365 1.00 6.49  ? 213 LEU A CD1   1 
ATOM   1398 C  CD2   . LEU B 2 213 ? 2.042   26.352 148.158 1.00 5.14  ? 213 LEU A CD2   1 
ATOM   1399 N  N     . VAL B 2 214 ? 2.326   30.652 150.755 1.00 8.94  ? 214 VAL A N     1 
ATOM   1400 C  CA    . VAL B 2 214 ? 1.380   31.785 150.664 1.00 8.92  ? 214 VAL A CA    1 
ATOM   1401 C  C     . VAL B 2 214 ? 1.663   32.696 149.495 1.00 9.03  ? 214 VAL A C     1 
ATOM   1402 O  O     . VAL B 2 214 ? 2.812   32.800 149.025 1.00 8.43  ? 214 VAL A O     1 
ATOM   1403 C  CB    . VAL B 2 214 ? 1.542   32.490 152.041 1.00 9.75  ? 214 VAL A CB    1 
ATOM   1404 C  CG1   . VAL B 2 214 ? 2.282   33.800 151.902 1.00 8.18  ? 214 VAL A CG1   1 
ATOM   1405 C  CG2   . VAL B 2 214 ? 0.205   32.555 152.751 1.00 11.40 ? 214 VAL A CG2   1 
ATOM   1406 N  N     . HIS B 2 215 ? 0.628   33.368 149.028 1.00 9.25  ? 215 HIS A N     1 
ATOM   1407 C  CA    . HIS B 2 215 ? 0.718   34.255 147.863 1.00 10.33 ? 215 HIS A CA    1 
ATOM   1408 C  C     . HIS B 2 215 ? 1.698   35.395 148.100 1.00 12.38 ? 215 HIS A C     1 
ATOM   1409 O  O     . HIS B 2 215 ? 1.808   35.994 149.179 1.00 13.11 ? 215 HIS A O     1 
ATOM   1410 C  CB    . HIS B 2 215 ? -0.589  34.880 147.379 1.00 10.55 ? 215 HIS A CB    1 
ATOM   1411 C  CG    . HIS B 2 215 ? -1.657  34.007 146.840 1.00 12.16 ? 215 HIS A CG    1 
ATOM   1412 N  ND1   . HIS B 2 215 ? -1.512  33.120 145.796 1.00 13.55 ? 215 HIS A ND1   1 
ATOM   1413 C  CD2   . HIS B 2 215 ? -2.952  33.913 147.224 1.00 12.26 ? 215 HIS A CD2   1 
ATOM   1414 C  CE1   . HIS B 2 215 ? -2.668  32.508 145.574 1.00 14.74 ? 215 HIS A CE1   1 
ATOM   1415 N  NE2   . HIS B 2 215 ? -3.561  32.995 146.418 1.00 13.26 ? 215 HIS A NE2   1 
ATOM   1416 N  N     . THR B 2 216 ? 2.368   35.701 147.002 1.00 13.40 ? 216 THR A N     1 
ATOM   1417 C  CA    . THR B 2 216 ? 3.357   36.778 147.013 1.00 13.97 ? 216 THR A CA    1 
ATOM   1418 C  C     . THR B 2 216 ? 3.535   37.384 145.635 1.00 14.11 ? 216 THR A C     1 
ATOM   1419 O  O     . THR B 2 216 ? 3.524   36.678 144.624 1.00 15.04 ? 216 THR A O     1 
ATOM   1420 C  CB    . THR B 2 216 ? 4.729   36.239 147.576 1.00 15.38 ? 216 THR A CB    1 
ATOM   1421 O  OG1   . THR B 2 216 ? 5.395   37.426 148.107 1.00 16.91 ? 216 THR A OG1   1 
ATOM   1422 C  CG2   . THR B 2 216 ? 5.551   35.505 146.529 1.00 16.87 ? 216 THR A CG2   1 
ATOM   1423 N  N     . LEU B 2 217 ? 3.678   38.691 145.639 1.00 12.93 ? 217 LEU A N     1 
ATOM   1424 C  CA    . LEU B 2 217 ? 3.876   39.466 144.406 1.00 11.58 ? 217 LEU A CA    1 
ATOM   1425 C  C     . LEU B 2 217 ? 5.379   39.471 144.133 1.00 11.16 ? 217 LEU A C     1 
ATOM   1426 O  O     . LEU B 2 217 ? 6.112   39.824 145.104 1.00 11.90 ? 217 LEU A O     1 
ATOM   1427 C  CB    . LEU B 2 217 ? 3.298   40.838 144.707 1.00 12.07 ? 217 LEU A CB    1 
ATOM   1428 C  CG    . LEU B 2 217 ? 1.984   41.323 144.165 1.00 13.75 ? 217 LEU A CG    1 
ATOM   1429 C  CD1   . LEU B 2 217 ? 1.159   40.250 143.467 1.00 14.70 ? 217 LEU A CD1   1 
ATOM   1430 C  CD2   . LEU B 2 217 ? 1.180   41.898 145.333 1.00 12.88 ? 217 LEU A CD2   1 
ATOM   1431 N  N     . VAL B 2 218 ? 5.797   39.099 142.926 1.00 10.24 ? 218 VAL A N     1 
ATOM   1432 C  CA    . VAL B 2 218 ? 7.247   39.121 142.587 1.00 9.05  ? 218 VAL A CA    1 
ATOM   1433 C  C     . VAL B 2 218 ? 7.446   40.198 141.515 1.00 9.87  ? 218 VAL A C     1 
ATOM   1434 O  O     . VAL B 2 218 ? 6.676   40.206 140.536 1.00 10.70 ? 218 VAL A O     1 
ATOM   1435 C  CB    . VAL B 2 218 ? 7.754   37.750 142.184 1.00 6.15  ? 218 VAL A CB    1 
ATOM   1436 C  CG1   . VAL B 2 218 ? 7.800   36.726 143.285 1.00 4.45  ? 218 VAL A CG1   1 
ATOM   1437 C  CG2   . VAL B 2 218 ? 6.942   37.226 140.995 1.00 6.16  ? 218 VAL A CG2   1 
ATOM   1438 N  N     . GLY B 2 219 ? 8.394   41.102 141.726 1.00 10.25 ? 219 GLY A N     1 
ATOM   1439 C  CA    . GLY B 2 219 ? 8.620   42.148 140.735 1.00 10.63 ? 219 GLY A CA    1 
ATOM   1440 C  C     . GLY B 2 219 ? 8.166   43.534 141.155 1.00 11.41 ? 219 GLY A C     1 
ATOM   1441 O  O     . GLY B 2 219 ? 8.200   44.477 140.318 1.00 11.92 ? 219 GLY A O     1 
ATOM   1442 N  N     . LEU B 2 220 ? 7.776   43.676 142.400 1.00 11.25 ? 220 LEU A N     1 
ATOM   1443 C  CA    . LEU B 2 220 ? 7.352   44.970 142.956 1.00 10.61 ? 220 LEU A CA    1 
ATOM   1444 C  C     . LEU B 2 220 ? 8.550   45.841 143.327 1.00 10.34 ? 220 LEU A C     1 
ATOM   1445 O  O     . LEU B 2 220 ? 8.393   47.006 143.721 1.00 11.26 ? 220 LEU A O     1 
ATOM   1446 C  CB    . LEU B 2 220 ? 6.487   44.621 144.192 1.00 9.61  ? 220 LEU A CB    1 
ATOM   1447 C  CG    . LEU B 2 220 ? 5.071   45.142 144.189 1.00 10.88 ? 220 LEU A CG    1 
ATOM   1448 C  CD1   . LEU B 2 220 ? 4.530   45.172 142.749 1.00 9.48  ? 220 LEU A CD1   1 
ATOM   1449 C  CD2   . LEU B 2 220 ? 4.228   44.217 145.043 1.00 11.32 ? 220 LEU A CD2   1 
ATOM   1450 N  N     . ASP B 2 221 ? 9.740   45.274 143.244 1.00 10.03 ? 221 ASP A N     1 
ATOM   1451 C  CA    . ASP B 2 221 ? 10.987  45.991 143.596 1.00 10.15 ? 221 ASP A CA    1 
ATOM   1452 C  C     . ASP B 2 221 ? 11.319  46.983 142.473 1.00 10.08 ? 221 ASP A C     1 
ATOM   1453 O  O     . ASP B 2 221 ? 12.228  47.810 142.558 1.00 9.81  ? 221 ASP A O     1 
ATOM   1454 C  CB    . ASP B 2 221 ? 12.099  44.975 143.868 1.00 11.06 ? 221 ASP A CB    1 
ATOM   1455 C  CG    . ASP B 2 221 ? 12.130  44.465 145.297 1.00 13.53 ? 221 ASP A CG    1 
ATOM   1456 O  OD1   . ASP B 2 221 ? 12.144  45.262 146.262 1.00 14.41 ? 221 ASP A OD1   1 
ATOM   1457 O  OD2   . ASP B 2 221 ? 12.148  43.211 145.481 1.00 13.51 ? 221 ASP A OD2   1 
ATOM   1458 N  N     . GLY B 2 222 ? 10.537  46.826 141.419 1.00 10.98 ? 222 GLY A N     1 
ATOM   1459 C  CA    . GLY B 2 222 ? 10.644  47.620 140.207 1.00 12.38 ? 222 GLY A CA    1 
ATOM   1460 C  C     . GLY B 2 222 ? 10.019  48.984 140.459 1.00 13.45 ? 222 GLY A C     1 
ATOM   1461 O  O     . GLY B 2 222 ? 10.342  49.942 139.728 1.00 15.21 ? 222 GLY A O     1 
ATOM   1462 N  N     . VAL B 2 223 ? 9.151   49.041 141.461 1.00 12.77 ? 223 VAL A N     1 
ATOM   1463 C  CA    . VAL B 2 223 ? 8.528   50.353 141.744 1.00 11.94 ? 223 VAL A CA    1 
ATOM   1464 C  C     . VAL B 2 223 ? 9.500   51.294 142.472 1.00 11.96 ? 223 VAL A C     1 
ATOM   1465 O  O     . VAL B 2 223 ? 9.216   52.500 142.627 1.00 12.56 ? 223 VAL A O     1 
ATOM   1466 C  CB    . VAL B 2 223 ? 7.234   50.169 142.576 1.00 9.25  ? 223 VAL A CB    1 
ATOM   1467 C  CG1   . VAL B 2 223 ? 6.645   51.529 142.936 1.00 8.53  ? 223 VAL A CG1   1 
ATOM   1468 C  CG2   . VAL B 2 223 ? 6.241   49.249 141.925 1.00 7.93  ? 223 VAL A CG2   1 
ATOM   1469 N  N     . LEU B 2 224 ? 10.603  50.763 142.935 1.00 11.58 ? 224 LEU A N     1 
ATOM   1470 C  CA    . LEU B 2 224 ? 11.615  51.437 143.719 1.00 11.26 ? 224 LEU A CA    1 
ATOM   1471 C  C     . LEU B 2 224 ? 12.610  52.291 142.990 1.00 11.55 ? 224 LEU A C     1 
ATOM   1472 O  O     . LEU B 2 224 ? 13.506  52.886 143.657 1.00 12.75 ? 224 LEU A O     1 
ATOM   1473 C  CB    . LEU B 2 224 ? 12.293  50.331 144.574 1.00 9.60  ? 224 LEU A CB    1 
ATOM   1474 C  CG    . LEU B 2 224 ? 11.318  49.658 145.539 1.00 8.54  ? 224 LEU A CG    1 
ATOM   1475 C  CD1   . LEU B 2 224 ? 11.996  48.690 146.460 1.00 8.29  ? 224 LEU A CD1   1 
ATOM   1476 C  CD2   . LEU B 2 224 ? 10.626  50.774 146.312 1.00 6.42  ? 224 LEU A CD2   1 
ATOM   1477 N  N     . ALA B 2 225 ? 12.534  52.388 141.687 1.00 11.03 ? 225 ALA A N     1 
ATOM   1478 C  CA    . ALA B 2 225 ? 13.451  53.248 140.916 1.00 9.80  ? 225 ALA A CA    1 
ATOM   1479 C  C     . ALA B 2 225 ? 12.680  53.609 139.641 1.00 9.66  ? 225 ALA A C     1 
ATOM   1480 O  O     . ALA B 2 225 ? 11.720  52.905 139.308 1.00 10.08 ? 225 ALA A O     1 
ATOM   1481 C  CB    . ALA B 2 225 ? 14.708  52.562 140.518 1.00 7.04  ? 225 ALA A CB    1 
ATOM   1482 N  N     . VAL B 2 226 ? 13.135  54.690 139.037 1.00 9.82  ? 226 VAL A N     1 
ATOM   1483 C  CA    . VAL B 2 226 ? 12.455  55.070 137.760 1.00 9.84  ? 226 VAL A CA    1 
ATOM   1484 C  C     . VAL B 2 226 ? 13.012  54.073 136.751 1.00 10.32 ? 226 VAL A C     1 
ATOM   1485 O  O     . VAL B 2 226 ? 14.263  53.892 136.702 1.00 11.31 ? 226 VAL A O     1 
ATOM   1486 C  CB    . VAL B 2 226 ? 12.709  56.554 137.503 1.00 7.27  ? 226 VAL A CB    1 
ATOM   1487 C  CG1   . VAL B 2 226 ? 12.722  56.881 136.013 1.00 7.66  ? 226 VAL A CG1   1 
ATOM   1488 C  CG2   . VAL B 2 226 ? 11.689  57.425 138.236 1.00 6.49  ? 226 VAL A CG2   1 
ATOM   1489 N  N     . GLY B 2 227 ? 12.168  53.402 135.992 1.00 9.89  ? 227 GLY A N     1 
ATOM   1490 C  CA    . GLY B 2 227 ? 12.759  52.428 135.028 1.00 9.83  ? 227 GLY A CA    1 
ATOM   1491 C  C     . GLY B 2 227 ? 13.537  53.182 133.941 1.00 9.54  ? 227 GLY A C     1 
ATOM   1492 O  O     . GLY B 2 227 ? 13.147  54.304 133.572 1.00 9.28  ? 227 GLY A O     1 
ATOM   1493 N  N     . PRO B 2 228 ? 14.617  52.547 133.480 1.00 8.40  ? 228 PRO A N     1 
ATOM   1494 C  CA    . PRO B 2 228 ? 15.424  53.125 132.402 1.00 8.28  ? 228 PRO A CA    1 
ATOM   1495 C  C     . PRO B 2 228 ? 14.503  53.482 131.233 1.00 8.94  ? 228 PRO A C     1 
ATOM   1496 O  O     . PRO B 2 228 ? 14.681  54.566 130.635 1.00 9.12  ? 228 PRO A O     1 
ATOM   1497 C  CB    . PRO B 2 228 ? 16.461  52.077 132.055 1.00 7.68  ? 228 PRO A CB    1 
ATOM   1498 C  CG    . PRO B 2 228 ? 16.437  51.068 133.141 1.00 6.97  ? 228 PRO A CG    1 
ATOM   1499 C  CD    . PRO B 2 228 ? 15.145  51.251 133.920 1.00 7.53  ? 228 PRO A CD    1 
ATOM   1500 N  N     . ASP B 2 229 ? 13.541  52.616 130.935 1.00 9.18  ? 229 ASP A N     1 
ATOM   1501 C  CA    . ASP B 2 229 ? 12.593  52.891 129.804 1.00 9.51  ? 229 ASP A CA    1 
ATOM   1502 C  C     . ASP B 2 229 ? 11.458  53.707 130.410 1.00 10.29 ? 229 ASP A C     1 
ATOM   1503 O  O     . ASP B 2 229 ? 10.568  52.983 130.955 1.00 12.47 ? 229 ASP A O     1 
ATOM   1504 C  CB    . ASP B 2 229 ? 12.029  51.622 129.174 1.00 8.01  ? 229 ASP A CB    1 
ATOM   1505 C  CG    . ASP B 2 229 ? 12.945  50.666 128.490 1.00 7.86  ? 229 ASP A CG    1 
ATOM   1506 O  OD1   . ASP B 2 229 ? 13.801  51.188 127.735 1.00 8.10  ? 229 ASP A OD1   1 
ATOM   1507 O  OD2   . ASP B 2 229 ? 12.931  49.420 128.604 1.00 5.39  ? 229 ASP A OD2   1 
ATOM   1508 N  N     . ASN B 2 230 ? 11.418  55.006 130.347 1.00 9.72  ? 230 ASN A N     1 
ATOM   1509 C  CA    . ASN B 2 230 ? 10.259  55.687 131.012 1.00 9.50  ? 230 ASN A CA    1 
ATOM   1510 C  C     . ASN B 2 230 ? 9.828   56.922 130.253 1.00 9.83  ? 230 ASN A C     1 
ATOM   1511 O  O     . ASN B 2 230 ? 10.464  57.296 129.276 1.00 10.09 ? 230 ASN A O     1 
ATOM   1512 C  CB    . ASN B 2 230 ? 10.740  56.055 132.430 1.00 8.61  ? 230 ASN A CB    1 
ATOM   1513 C  CG    . ASN B 2 230 ? 11.948  56.983 132.300 1.00 7.02  ? 230 ASN A CG    1 
ATOM   1514 O  OD1   . ASN B 2 230 ? 11.748  58.186 132.123 1.00 7.31  ? 230 ASN A OD1   1 
ATOM   1515 N  ND2   . ASN B 2 230 ? 13.154  56.460 132.364 1.00 5.98  ? 230 ASN A ND2   1 
ATOM   1516 N  N     . PHE B 2 231 ? 8.782   57.536 130.753 1.00 10.29 ? 231 PHE A N     1 
ATOM   1517 C  CA    . PHE B 2 231 ? 8.232   58.782 130.168 1.00 10.51 ? 231 PHE A CA    1 
ATOM   1518 C  C     . PHE B 2 231 ? 8.250   59.783 131.333 1.00 12.01 ? 231 PHE A C     1 
ATOM   1519 O  O     . PHE B 2 231 ? 7.774   59.404 132.408 1.00 13.58 ? 231 PHE A O     1 
ATOM   1520 C  CB    . PHE B 2 231 ? 6.870   58.607 129.543 1.00 6.42  ? 231 PHE A CB    1 
ATOM   1521 C  CG    . PHE B 2 231 ? 6.104   59.856 129.251 1.00 5.82  ? 231 PHE A CG    1 
ATOM   1522 C  CD1   . PHE B 2 231 ? 5.374   60.503 130.238 1.00 5.78  ? 231 PHE A CD1   1 
ATOM   1523 C  CD2   . PHE B 2 231 ? 6.096   60.379 127.957 1.00 5.02  ? 231 PHE A CD2   1 
ATOM   1524 C  CE1   . PHE B 2 231 ? 4.674   61.682 129.941 1.00 6.10  ? 231 PHE A CE1   1 
ATOM   1525 C  CE2   . PHE B 2 231 ? 5.415   61.539 127.638 1.00 4.09  ? 231 PHE A CE2   1 
ATOM   1526 C  CZ    . PHE B 2 231 ? 4.698   62.205 128.626 1.00 3.98  ? 231 PHE A CZ    1 
ATOM   1527 N  N     . SER B 2 232 ? 8.815   60.934 131.137 1.00 12.24 ? 232 SER A N     1 
ATOM   1528 C  CA    . SER B 2 232 ? 8.918   61.977 132.167 1.00 11.81 ? 232 SER A CA    1 
ATOM   1529 C  C     . SER B 2 232 ? 8.584   63.300 131.504 1.00 11.14 ? 232 SER A C     1 
ATOM   1530 O  O     . SER B 2 232 ? 9.023   63.471 130.340 1.00 11.93 ? 232 SER A O     1 
ATOM   1531 C  CB    . SER B 2 232 ? 10.311  61.986 132.757 1.00 12.06 ? 232 SER A CB    1 
ATOM   1532 O  OG    . SER B 2 232 ? 10.220  62.229 134.174 1.00 15.07 ? 232 SER A OG    1 
ATOM   1533 N  N     . GLU B 2 233 ? 7.844   64.154 132.177 1.00 10.45 ? 233 GLU A N     1 
ATOM   1534 C  CA    . GLU B 2 233 ? 7.502   65.453 131.498 1.00 9.60  ? 233 GLU A CA    1 
ATOM   1535 C  C     . GLU B 2 233 ? 6.717   66.311 132.460 1.00 9.35  ? 233 GLU A C     1 
ATOM   1536 O  O     . GLU B 2 233 ? 6.380   65.849 133.564 1.00 9.50  ? 233 GLU A O     1 
ATOM   1537 C  CB    . GLU B 2 233 ? 6.823   65.119 130.195 1.00 8.19  ? 233 GLU A CB    1 
ATOM   1538 C  CG    . GLU B 2 233 ? 6.357   66.119 129.189 1.00 9.80  ? 233 GLU A CG    1 
ATOM   1539 C  CD    . GLU B 2 233 ? 7.239   67.195 128.685 1.00 10.42 ? 233 GLU A CD    1 
ATOM   1540 O  OE1   . GLU B 2 233 ? 7.536   68.181 129.335 1.00 13.14 ? 233 GLU A OE1   1 
ATOM   1541 O  OE2   . GLU B 2 233 ? 7.627   67.014 127.515 1.00 10.12 ? 233 GLU A OE2   1 
ATOM   1542 N  N     . SER B 2 234 ? 6.453   67.555 132.119 1.00 9.19  ? 234 SER A N     1 
ATOM   1543 C  CA    . SER B 2 234 ? 5.697   68.515 132.938 1.00 10.41 ? 234 SER A CA    1 
ATOM   1544 C  C     . SER B 2 234 ? 4.312   67.912 133.279 1.00 11.44 ? 234 SER A C     1 
ATOM   1545 O  O     . SER B 2 234 ? 3.715   67.182 132.473 1.00 12.39 ? 234 SER A O     1 
ATOM   1546 C  CB    . SER B 2 234 ? 5.451   69.822 132.206 1.00 10.50 ? 234 SER A CB    1 
ATOM   1547 O  OG    . SER B 2 234 ? 5.637   70.917 133.091 1.00 9.44  ? 234 SER A OG    1 
ATOM   1548 N  N     . PHE B 2 235 ? 3.837   68.245 134.471 1.00 11.57 ? 235 PHE A N     1 
ATOM   1549 C  CA    . PHE B 2 235 ? 2.542   67.760 135.012 1.00 11.06 ? 235 PHE A CA    1 
ATOM   1550 C  C     . PHE B 2 235 ? 1.355   68.223 134.150 1.00 11.38 ? 235 PHE A C     1 
ATOM   1551 O  O     . PHE B 2 235 ? 0.415   67.454 133.892 1.00 12.75 ? 235 PHE A O     1 
ATOM   1552 C  CB    . PHE B 2 235 ? 2.323   68.332 136.420 1.00 9.09  ? 235 PHE A CB    1 
ATOM   1553 C  CG    . PHE B 2 235 ? 0.978   67.945 137.040 1.00 8.45  ? 235 PHE A CG    1 
ATOM   1554 C  CD1   . PHE B 2 235 ? 0.763   66.637 137.489 1.00 7.76  ? 235 PHE A CD1   1 
ATOM   1555 C  CD2   . PHE B 2 235 ? -0.036  68.903 137.164 1.00 8.92  ? 235 PHE A CD2   1 
ATOM   1556 C  CE1   . PHE B 2 235 ? -0.466  66.286 138.062 1.00 6.89  ? 235 PHE A CE1   1 
ATOM   1557 C  CE2   . PHE B 2 235 ? -1.265  68.552 137.736 1.00 6.77  ? 235 PHE A CE2   1 
ATOM   1558 C  CZ    . PHE B 2 235 ? -1.480  67.244 138.185 1.00 6.47  ? 235 PHE A CZ    1 
ATOM   1559 N  N     . ILE B 2 236 ? 1.438   69.475 133.734 1.00 11.75 ? 236 ILE A N     1 
ATOM   1560 C  CA    . ILE B 2 236 ? 0.375   70.149 132.960 1.00 10.79 ? 236 ILE A CA    1 
ATOM   1561 C  C     . ILE B 2 236 ? 0.282   69.646 131.512 1.00 11.48 ? 236 ILE A C     1 
ATOM   1562 O  O     . ILE B 2 236 ? -0.494  70.172 130.701 1.00 12.00 ? 236 ILE A O     1 
ATOM   1563 C  CB    . ILE B 2 236 ? 0.640   71.654 132.897 1.00 7.59  ? 236 ILE A CB    1 
ATOM   1564 C  CG1   . ILE B 2 236 ? -0.635  72.476 132.701 1.00 6.44  ? 236 ILE A CG1   1 
ATOM   1565 C  CG2   . ILE B 2 236 ? 1.569   72.049 131.747 1.00 5.68  ? 236 ILE A CG2   1 
ATOM   1566 C  CD1   . ILE B 2 236 ? -1.809  71.966 133.540 1.00 5.98  ? 236 ILE A CD1   1 
ATOM   1567 N  N     . LYS B 2 237 ? 1.064   68.637 131.193 1.00 12.08 ? 237 LYS A N     1 
ATOM   1568 C  CA    . LYS B 2 237 ? 1.066   68.065 129.836 1.00 11.79 ? 237 LYS A CA    1 
ATOM   1569 C  C     . LYS B 2 237 ? 0.243   66.773 129.811 1.00 11.98 ? 237 LYS A C     1 
ATOM   1570 O  O     . LYS B 2 237 ? -0.095  66.252 128.738 1.00 12.75 ? 237 LYS A O     1 
ATOM   1571 C  CB    . LYS B 2 237 ? 2.499   67.782 129.387 1.00 8.94  ? 237 LYS A CB    1 
ATOM   1572 C  CG    . LYS B 2 237 ? 2.994   68.783 128.339 1.00 6.42  ? 237 LYS A CG    1 
ATOM   1573 C  CD    . LYS B 2 237 ? 4.489   69.081 128.452 1.00 7.94  ? 237 LYS A CD    1 
ATOM   1574 C  CE    . LYS B 2 237 ? 5.198   69.075 127.096 1.00 9.29  ? 237 LYS A CE    1 
ATOM   1575 N  NZ    . LYS B 2 237 ? 6.456   69.834 127.101 1.00 10.87 ? 237 LYS A NZ    1 
ATOM   1576 N  N     . GLY B 2 238 ? -0.062  66.298 131.006 1.00 11.04 ? 238 GLY A N     1 
ATOM   1577 C  CA    . GLY B 2 238 ? -0.862  65.076 131.206 1.00 10.86 ? 238 GLY A CA    1 
ATOM   1578 C  C     . GLY B 2 238 ? -0.116  63.854 130.664 1.00 10.90 ? 238 GLY A C     1 
ATOM   1579 O  O     . GLY B 2 238 ? 1.074   63.930 130.323 1.00 11.47 ? 238 GLY A O     1 
ATOM   1580 N  N     . VAL B 2 239 ? -0.848  62.752 130.607 1.00 10.21 ? 239 VAL A N     1 
ATOM   1581 C  CA    . VAL B 2 239 ? -0.315  61.478 130.110 1.00 10.08 ? 239 VAL A CA    1 
ATOM   1582 C  C     . VAL B 2 239 ? -1.456  60.519 129.767 1.00 10.21 ? 239 VAL A C     1 
ATOM   1583 O  O     . VAL B 2 239 ? -2.553  60.602 130.295 1.00 11.06 ? 239 VAL A O     1 
ATOM   1584 C  CB    . VAL B 2 239 ? 0.638   60.878 131.143 1.00 9.14  ? 239 VAL A CB    1 
ATOM   1585 C  CG1   . VAL B 2 239 ? -0.056  59.965 132.149 1.00 8.29  ? 239 VAL A CG1   1 
ATOM   1586 C  CG2   . VAL B 2 239 ? 1.750   60.044 130.502 1.00 9.33  ? 239 VAL A CG2   1 
ATOM   1587 N  N     . PHE B 2 240 ? -1.143  59.618 128.880 1.00 10.26 ? 240 PHE A N     1 
ATOM   1588 C  CA    . PHE B 2 240 ? -1.965  58.530 128.361 1.00 10.07 ? 240 PHE A CA    1 
ATOM   1589 C  C     . PHE B 2 240 ? -0.964  57.374 128.104 1.00 9.67  ? 240 PHE A C     1 
ATOM   1590 O  O     . PHE B 2 240 ? 0.007   57.574 127.350 1.00 9.57  ? 240 PHE A O     1 
ATOM   1591 C  CB    . PHE B 2 240 ? -2.768  58.855 127.082 1.00 10.88 ? 240 PHE A CB    1 
ATOM   1592 C  CG    . PHE B 2 240 ? -3.503  57.646 126.560 1.00 11.98 ? 240 PHE A CG    1 
ATOM   1593 C  CD1   . PHE B 2 240 ? -4.716  57.272 127.139 1.00 12.61 ? 240 PHE A CD1   1 
ATOM   1594 C  CD2   . PHE B 2 240 ? -2.953  56.844 125.582 1.00 12.42 ? 240 PHE A CD2   1 
ATOM   1595 C  CE1   . PHE B 2 240 ? -5.403  56.143 126.726 1.00 11.56 ? 240 PHE A CE1   1 
ATOM   1596 C  CE2   . PHE B 2 240 ? -3.619  55.691 125.156 1.00 11.34 ? 240 PHE A CE2   1 
ATOM   1597 C  CZ    . PHE B 2 240 ? -4.851  55.351 125.725 1.00 11.65 ? 240 PHE A CZ    1 
ATOM   1598 N  N     . SER B 2 241 ? -1.214  56.272 128.771 1.00 9.31  ? 241 SER A N     1 
ATOM   1599 C  CA    . SER B 2 241 ? -0.331  55.099 128.607 1.00 9.25  ? 241 SER A CA    1 
ATOM   1600 C  C     . SER B 2 241 ? -1.192  53.844 128.492 1.00 9.63  ? 241 SER A C     1 
ATOM   1601 O  O     . SER B 2 241 ? -2.387  53.812 128.842 1.00 9.54  ? 241 SER A O     1 
ATOM   1602 C  CB    . SER B 2 241 ? 0.702   54.993 129.693 1.00 8.79  ? 241 SER A CB    1 
ATOM   1603 O  OG    . SER B 2 241 ? 1.626   53.943 129.446 1.00 10.86 ? 241 SER A OG    1 
ATOM   1604 N  N     . GLN B 2 242 ? -0.556  52.821 127.928 1.00 10.40 ? 242 GLN A N     1 
ATOM   1605 C  CA    . GLN B 2 242 ? -1.284  51.544 127.748 1.00 10.77 ? 242 GLN A CA    1 
ATOM   1606 C  C     . GLN B 2 242 ? -0.301  50.420 128.065 1.00 11.15 ? 242 GLN A C     1 
ATOM   1607 O  O     . GLN B 2 242 ? 0.921   50.603 127.943 1.00 10.96 ? 242 GLN A O     1 
ATOM   1608 C  CB    . GLN B 2 242 ? -1.991  51.402 126.421 1.00 10.27 ? 242 GLN A CB    1 
ATOM   1609 C  CG    . GLN B 2 242 ? -1.193  51.514 125.180 1.00 13.14 ? 242 GLN A CG    1 
ATOM   1610 C  CD    . GLN B 2 242 ? -1.072  52.854 124.522 1.00 15.88 ? 242 GLN A CD    1 
ATOM   1611 O  OE1   . GLN B 2 242 ? -0.001  53.467 124.532 1.00 18.62 ? 242 GLN A OE1   1 
ATOM   1612 N  NE2   . GLN B 2 242 ? -2.144  53.340 123.896 1.00 14.02 ? 242 GLN A NE2   1 
ATOM   1613 N  N     . SER B 2 243 ? -0.902  49.346 128.537 1.00 11.24 ? 243 SER A N     1 
ATOM   1614 C  CA    . SER B 2 243 ? -0.161  48.120 128.871 1.00 11.62 ? 243 SER A CA    1 
ATOM   1615 C  C     . SER B 2 243 ? -0.521  47.073 127.797 1.00 12.67 ? 243 SER A C     1 
ATOM   1616 O  O     . SER B 2 243 ? -1.511  47.263 127.039 1.00 14.77 ? 243 SER A O     1 
ATOM   1617 C  CB    . SER B 2 243 ? -0.393  47.648 130.271 1.00 9.40  ? 243 SER A CB    1 
ATOM   1618 O  OG    . SER B 2 243 ? 0.387   46.477 130.458 1.00 8.01  ? 243 SER A OG    1 
ATOM   1619 N  N     . VAL B 2 244 ? 0.279   46.034 127.690 1.00 11.91 ? 244 VAL A N     1 
ATOM   1620 C  CA    . VAL B 2 244 ? 0.042   44.977 126.687 1.00 10.55 ? 244 VAL A CA    1 
ATOM   1621 C  C     . VAL B 2 244 ? 0.237   43.605 127.348 1.00 10.78 ? 244 VAL A C     1 
ATOM   1622 O  O     . VAL B 2 244 ? 1.029   43.462 128.311 1.00 11.66 ? 244 VAL A O     1 
ATOM   1623 C  CB    . VAL B 2 244 ? 0.953   45.196 125.466 1.00 8.40  ? 244 VAL A CB    1 
ATOM   1624 C  CG1   . VAL B 2 244 ? 1.410   43.851 124.894 1.00 6.64  ? 244 VAL A CG1   1 
ATOM   1625 C  CG2   . VAL B 2 244 ? 0.323   46.006 124.334 1.00 7.72  ? 244 VAL A CG2   1 
ATOM   1626 N  N     . CYS B 2 245 ? -0.474  42.627 126.835 1.00 10.02 ? 245 CYS A N     1 
ATOM   1627 C  CA    . CYS B 2 245 ? -0.364  41.262 127.375 1.00 9.69  ? 245 CYS A CA    1 
ATOM   1628 C  C     . CYS B 2 245 ? 1.110   40.900 127.531 1.00 10.08 ? 245 CYS A C     1 
ATOM   1629 O  O     . CYS B 2 245 ? 1.874   41.205 126.599 1.00 11.70 ? 245 CYS A O     1 
ATOM   1630 C  CB    . CYS B 2 245 ? -1.007  40.268 126.425 1.00 9.21  ? 245 CYS A CB    1 
ATOM   1631 S  SG    . CYS B 2 245 ? -0.782  38.590 127.002 1.00 8.60  ? 245 CYS A SG    1 
ATOM   1632 N  N     . ASN B 2 246 ? 1.493   40.234 128.606 1.00 9.36  ? 246 ASN A N     1 
ATOM   1633 C  CA    . ASN B 2 246 ? 2.907   39.945 128.852 1.00 9.50  ? 246 ASN A CA    1 
ATOM   1634 C  C     . ASN B 2 246 ? 3.251   38.479 128.711 1.00 9.99  ? 246 ASN A C     1 
ATOM   1635 O  O     . ASN B 2 246 ? 4.157   37.968 129.384 1.00 9.84  ? 246 ASN A O     1 
ATOM   1636 C  CB    . ASN B 2 246 ? 3.322   40.481 130.224 1.00 11.21 ? 246 ASN A CB    1 
ATOM   1637 C  CG    . ASN B 2 246 ? 2.598   39.767 131.362 1.00 12.74 ? 246 ASN A CG    1 
ATOM   1638 O  OD1   . ASN B 2 246 ? 2.524   40.295 132.469 1.00 12.69 ? 246 ASN A OD1   1 
ATOM   1639 N  ND2   . ASN B 2 246 ? 2.052   38.583 131.149 1.00 15.77 ? 246 ASN A ND2   1 
ATOM   1640 N  N     . GLU B 2 247 ? 2.541   37.853 127.816 1.00 9.67  ? 247 GLU A N     1 
ATOM   1641 C  CA    . GLU B 2 247 ? 2.765   36.452 127.507 1.00 9.36  ? 247 GLU A CA    1 
ATOM   1642 C  C     . GLU B 2 247 ? 2.606   36.223 126.017 1.00 10.07 ? 247 GLU A C     1 
ATOM   1643 O  O     . GLU B 2 247 ? 2.003   37.043 125.308 1.00 10.75 ? 247 GLU A O     1 
ATOM   1644 C  CB    . GLU B 2 247 ? 1.807   35.579 128.308 1.00 8.32  ? 247 GLU A CB    1 
ATOM   1645 C  CG    . GLU B 2 247 ? 2.044   35.659 129.817 1.00 12.05 ? 247 GLU A CG    1 
ATOM   1646 C  CD    . GLU B 2 247 ? 3.160   34.729 130.298 1.00 15.88 ? 247 GLU A CD    1 
ATOM   1647 O  OE1   . GLU B 2 247 ? 3.902   34.114 129.440 1.00 16.37 ? 247 GLU A OE1   1 
ATOM   1648 O  OE2   . GLU B 2 247 ? 3.358   34.559 131.561 1.00 18.94 ? 247 GLU A OE2   1 
ATOM   1649 N  N     . PRO B 2 248 ? 3.134   35.119 125.495 1.00 10.16 ? 248 PRO A N     1 
ATOM   1650 C  CA    . PRO B 2 248 ? 3.079   34.850 124.078 1.00 11.00 ? 248 PRO A CA    1 
ATOM   1651 C  C     . PRO B 2 248 ? 1.660   34.795 123.575 1.00 11.96 ? 248 PRO A C     1 
ATOM   1652 O  O     . PRO B 2 248 ? 1.431   35.033 122.349 1.00 13.40 ? 248 PRO A O     1 
ATOM   1653 C  CB    . PRO B 2 248 ? 3.774   33.521 123.930 1.00 11.40 ? 248 PRO A CB    1 
ATOM   1654 C  CG    . PRO B 2 248 ? 4.218   33.071 125.312 1.00 10.52 ? 248 PRO A CG    1 
ATOM   1655 C  CD    . PRO B 2 248 ? 3.804   34.105 126.309 1.00 10.29 ? 248 PRO A CD    1 
ATOM   1656 N  N     . ASP B 2 249 ? 0.734   34.498 124.474 1.00 16.43 ? 249 ASP A N     1 
ATOM   1657 C  CA    . ASP B 2 249 ? -0.688  34.360 124.099 1.00 18.10 ? 249 ASP A CA    1 
ATOM   1658 C  C     . ASP B 2 249 ? -1.621  34.977 125.148 1.00 20.15 ? 249 ASP A C     1 
ATOM   1659 O  O     . ASP B 2 249 ? -1.208  35.812 125.964 1.00 21.66 ? 249 ASP A O     1 
ATOM   1660 C  CB    . ASP B 2 249 ? -1.040  32.885 123.956 1.00 19.55 ? 249 ASP A CB    1 
ATOM   1661 C  CG    . ASP B 2 249 ? -0.753  32.091 125.226 1.00 21.67 ? 249 ASP A CG    1 
ATOM   1662 O  OD1   . ASP B 2 249 ? -0.622  32.707 126.352 1.00 18.28 ? 249 ASP A OD1   1 
ATOM   1663 O  OD2   . ASP B 2 249 ? -0.642  30.809 125.172 1.00 23.66 ? 249 ASP A OD2   1 
ATOM   1664 N  N     . PHE B 2 250 ? -2.871  34.528 125.087 1.00 10.75 ? 250 PHE A N     1 
ATOM   1665 C  CA    . PHE B 2 250 ? -3.942  35.033 125.962 1.00 9.40  ? 250 PHE A CA    1 
ATOM   1666 C  C     . PHE B 2 250 ? -4.719  33.912 126.648 1.00 8.93  ? 250 PHE A C     1 
ATOM   1667 O  O     . PHE B 2 250 ? -5.810  33.522 126.205 1.00 7.60  ? 250 PHE A O     1 
ATOM   1668 C  CB    . PHE B 2 250 ? -4.959  35.821 125.143 1.00 8.62  ? 250 PHE A CB    1 
ATOM   1669 C  CG    . PHE B 2 250 ? -4.384  37.113 124.584 1.00 8.92  ? 250 PHE A CG    1 
ATOM   1670 C  CD1   . PHE B 2 250 ? -3.675  37.096 123.379 1.00 9.48  ? 250 PHE A CD1   1 
ATOM   1671 C  CD2   . PHE B 2 250 ? -4.565  38.309 125.282 1.00 8.45  ? 250 PHE A CD2   1 
ATOM   1672 C  CE1   . PHE B 2 250 ? -3.143  38.284 122.868 1.00 11.00 ? 250 PHE A CE1   1 
ATOM   1673 C  CE2   . PHE B 2 250 ? -4.033  39.497 124.772 1.00 8.67  ? 250 PHE A CE2   1 
ATOM   1674 C  CZ    . PHE B 2 250 ? -3.321  39.485 123.565 1.00 11.11 ? 250 PHE A CZ    1 
ATOM   1675 N  N     . GLU B 2 251 ? -4.149  33.426 127.726 1.00 15.07 ? 251 GLU A N     1 
ATOM   1676 C  CA    . GLU B 2 251 ? -4.791  32.389 128.527 1.00 16.49 ? 251 GLU A CA    1 
ATOM   1677 C  C     . GLU B 2 251 ? -5.618  33.006 129.627 1.00 14.91 ? 251 GLU A C     1 
ATOM   1678 O  O     . GLU B 2 251 ? -5.331  34.118 130.085 1.00 15.01 ? 251 GLU A O     1 
ATOM   1679 C  CB    . GLU B 2 251 ? -3.786  31.516 129.225 1.00 19.80 ? 251 GLU A CB    1 
ATOM   1680 C  CG    . GLU B 2 251 ? -4.160  30.055 129.118 1.00 26.19 ? 251 GLU A CG    1 
ATOM   1681 C  CD    . GLU B 2 251 ? -2.949  29.162 129.239 1.00 32.89 ? 251 GLU A CD    1 
ATOM   1682 O  OE1   . GLU B 2 251 ? -2.280  29.155 130.337 1.00 33.23 ? 251 GLU A OE1   1 
ATOM   1683 O  OE2   . GLU B 2 251 ? -2.599  28.427 128.244 1.00 36.65 ? 251 GLU A OE2   1 
ATOM   1684 N  N     . PHE B 2 252 ? -6.613  32.252 130.019 1.00 10.01 ? 252 PHE A N     1 
ATOM   1685 C  CA    . PHE B 2 252 ? -7.521  32.662 131.081 1.00 9.50  ? 252 PHE A CA    1 
ATOM   1686 C  C     . PHE B 2 252 ? -6.862  32.432 132.437 1.00 9.06  ? 252 PHE A C     1 
ATOM   1687 O  O     . PHE B 2 252 ? -6.090  31.478 132.619 1.00 7.74  ? 252 PHE A O     1 
ATOM   1688 C  CB    . PHE B 2 252 ? -8.814  31.855 131.000 1.00 9.92  ? 252 PHE A CB    1 
ATOM   1689 C  CG    . PHE B 2 252 ? -9.801  32.423 129.981 1.00 8.82  ? 252 PHE A CG    1 
ATOM   1690 C  CD1   . PHE B 2 252 ? -9.756  31.993 128.650 1.00 8.56  ? 252 PHE A CD1   1 
ATOM   1691 C  CD2   . PHE B 2 252 ? -10.747 33.374 130.379 1.00 6.96  ? 252 PHE A CD2   1 
ATOM   1692 C  CE1   . PHE B 2 252 ? -10.659 32.513 127.716 1.00 10.17 ? 252 PHE A CE1   1 
ATOM   1693 C  CE2   . PHE B 2 252 ? -11.650 33.895 129.445 1.00 6.07  ? 252 PHE A CE2   1 
ATOM   1694 C  CZ    . PHE B 2 252 ? -11.607 33.464 128.114 1.00 8.88  ? 252 PHE A CZ    1 
ATOM   1695 N  N     . SER B 2 253 ? -7.191  33.331 133.336 1.00 9.62  ? 253 SER A N     1 
ATOM   1696 C  CA    . SER B 2 253 ? -6.707  33.299 134.718 1.00 9.72  ? 253 SER A CA    1 
ATOM   1697 C  C     . SER B 2 253 ? -7.901  33.095 135.642 1.00 9.38  ? 253 SER A C     1 
ATOM   1698 O  O     . SER B 2 253 ? -9.020  33.538 135.347 1.00 9.32  ? 253 SER A O     1 
ATOM   1699 C  CB    . SER B 2 253 ? -6.007  34.617 135.054 1.00 10.15 ? 253 SER A CB    1 
ATOM   1700 O  OG    . SER B 2 253 ? -5.191  35.023 133.965 1.00 11.93 ? 253 SER A OG    1 
ATOM   1701 N  N     . ASP B 2 254 ? -7.648  32.424 136.741 1.00 9.43  ? 254 ASP A N     1 
ATOM   1702 C  CA    . ASP B 2 254 ? -8.707  32.103 137.697 1.00 9.51  ? 254 ASP A CA    1 
ATOM   1703 C  C     . ASP B 2 254 ? -8.914  33.239 138.702 1.00 9.25  ? 254 ASP A C     1 
ATOM   1704 O  O     . ASP B 2 254 ? -8.026  34.050 138.924 1.00 8.62  ? 254 ASP A O     1 
ATOM   1705 C  CB    . ASP B 2 254 ? -8.377  30.816 138.437 1.00 12.40 ? 254 ASP A CB    1 
ATOM   1706 C  CG    . ASP B 2 254 ? -7.890  29.720 137.497 1.00 17.16 ? 254 ASP A CG    1 
ATOM   1707 O  OD1   . ASP B 2 254 ? -8.471  29.543 136.357 1.00 17.28 ? 254 ASP A OD1   1 
ATOM   1708 O  OD2   . ASP B 2 254 ? -6.896  28.983 137.846 1.00 18.81 ? 254 ASP A OD2   1 
ATOM   1709 N  N     . ILE B 2 255 ? -10.134 33.189 139.247 1.00 9.43  ? 255 ILE A N     1 
ATOM   1710 C  CA    . ILE B 2 255 ? -10.560 34.133 140.297 1.00 9.81  ? 255 ILE A CA    1 
ATOM   1711 C  C     . ILE B 2 255 ? -9.993  33.518 141.584 1.00 10.75 ? 255 ILE A C     1 
ATOM   1712 O  O     . ILE B 2 255 ? -10.089 32.268 141.706 1.00 10.64 ? 255 ILE A O     1 
ATOM   1713 C  CB    . ILE B 2 255 ? -12.109 34.244 140.334 1.00 9.33  ? 255 ILE A CB    1 
ATOM   1714 C  CG1   . ILE B 2 255 ? -12.602 35.247 139.276 1.00 9.30  ? 255 ILE A CG1   1 
ATOM   1715 C  CG2   . ILE B 2 255 ? -12.638 34.568 141.746 1.00 8.39  ? 255 ILE A CG2   1 
ATOM   1716 C  CD1   . ILE B 2 255 ? -12.160 36.705 139.424 1.00 8.97  ? 255 ILE A CD1   1 
ATOM   1717 N  N     . LEU B 2 256 ? -9.425  34.339 142.431 1.00 10.92 ? 256 LEU A N     1 
ATOM   1718 C  CA    . LEU B 2 256 ? -8.844  33.835 143.699 1.00 10.79 ? 256 LEU A CA    1 
ATOM   1719 C  C     . LEU B 2 256 ? -9.716  34.157 144.903 1.00 10.64 ? 256 LEU A C     1 
ATOM   1720 O  O     . LEU B 2 256 ? -10.217 35.296 145.024 1.00 11.57 ? 256 LEU A O     1 
ATOM   1721 C  CB    . LEU B 2 256 ? -7.483  34.520 143.811 1.00 9.84  ? 256 LEU A CB    1 
ATOM   1722 C  CG    . LEU B 2 256 ? -6.492  34.405 142.691 1.00 9.23  ? 256 LEU A CG    1 
ATOM   1723 C  CD1   . LEU B 2 256 ? -5.337  35.384 142.881 1.00 8.56  ? 256 LEU A CD1   1 
ATOM   1724 C  CD2   . LEU B 2 256 ? -5.992  32.961 142.718 1.00 9.27  ? 256 LEU A CD2   1 
ATOM   1725 N  N     . GLU B 2 257 ? -9.854  33.243 145.840 1.00 10.03 ? 257 GLU A N     1 
ATOM   1726 C  CA    . GLU B 2 257 ? -10.676 33.551 147.036 1.00 9.29  ? 257 GLU A CA    1 
ATOM   1727 C  C     . GLU B 2 257 ? -9.901  33.950 148.266 1.00 9.66  ? 257 GLU A C     1 
ATOM   1728 O  O     . GLU B 2 257 ? -8.735  33.544 148.501 1.00 9.46  ? 257 GLU A O     1 
ATOM   1729 C  CB    . GLU B 2 257 ? -11.536 32.310 147.344 1.00 6.82  ? 257 GLU A CB    1 
ATOM   1730 C  CG    . GLU B 2 257 ? -12.577 32.041 146.204 1.00 6.47  ? 257 GLU A CG    1 
ATOM   1731 C  CD    . GLU B 2 257 ? -13.631 33.137 146.266 1.00 8.37  ? 257 GLU A CD    1 
ATOM   1732 O  OE1   . GLU B 2 257 ? -13.533 34.044 147.075 1.00 10.41 ? 257 GLU A OE1   1 
ATOM   1733 O  OE2   . GLU B 2 257 ? -14.556 33.039 145.455 1.00 7.26  ? 257 GLU A OE2   1 
ATOM   1734 N  N     . GLY B 2 258 ? -10.540 34.745 149.090 1.00 10.18 ? 258 GLY A N     1 
ATOM   1735 C  CA    . GLY B 2 258 ? -10.113 35.274 150.345 1.00 11.09 ? 258 GLY A CA    1 
ATOM   1736 C  C     . GLY B 2 258 ? -8.879  36.124 150.409 1.00 11.23 ? 258 GLY A C     1 
ATOM   1737 O  O     . GLY B 2 258 ? -8.122  35.993 151.410 1.00 13.27 ? 258 GLY A O     1 
ATOM   1738 N  N     . ILE B 2 259 ? -8.651  37.001 149.443 1.00 10.53 ? 259 ILE A N     1 
ATOM   1739 C  CA    . ILE B 2 259 ? -7.453  37.859 149.453 1.00 11.06 ? 259 ILE A CA    1 
ATOM   1740 C  C     . ILE B 2 259 ? -7.826  39.345 149.569 1.00 12.44 ? 259 ILE A C     1 
ATOM   1741 O  O     . ILE B 2 259 ? -8.438  39.889 148.604 1.00 14.04 ? 259 ILE A O     1 
ATOM   1742 C  CB    . ILE B 2 259 ? -6.618  37.672 148.143 1.00 9.97  ? 259 ILE A CB    1 
ATOM   1743 C  CG1   . ILE B 2 259 ? -6.016  36.268 147.969 1.00 11.50 ? 259 ILE A CG1   1 
ATOM   1744 C  CG2   . ILE B 2 259 ? -5.503  38.763 147.980 1.00 5.23  ? 259 ILE A CG2   1 
ATOM   1745 C  CD1   . ILE B 2 259 ? -5.339  36.155 146.554 1.00 9.01  ? 259 ILE A CD1   1 
ATOM   1746 N  N     . GLN B 2 260 ? -7.378  39.932 150.680 1.00 12.12 ? 260 GLN A N     1 
ATOM   1747 C  CA    . GLN B 2 260 ? -7.624  41.342 150.955 1.00 11.45 ? 260 GLN A CA    1 
ATOM   1748 C  C     . GLN B 2 260 ? -6.336  42.146 151.008 1.00 12.09 ? 260 GLN A C     1 
ATOM   1749 O  O     . GLN B 2 260 ? -6.308  43.327 150.622 1.00 11.91 ? 260 GLN A O     1 
ATOM   1750 C  CB    . GLN B 2 260 ? -8.458  41.574 152.204 1.00 8.18  ? 260 GLN A CB    1 
ATOM   1751 C  CG    . GLN B 2 260 ? -9.829  40.897 152.141 1.00 7.93  ? 260 GLN A CG    1 
ATOM   1752 C  CD    . GLN B 2 260 ? -10.720 41.454 151.030 1.00 10.97 ? 260 GLN A CD    1 
ATOM   1753 O  OE1   . GLN B 2 260 ? -10.847 42.670 150.894 1.00 10.89 ? 260 GLN A OE1   1 
ATOM   1754 N  NE2   . GLN B 2 260 ? -11.353 40.630 150.216 1.00 12.93 ? 260 GLN A NE2   1 
ATOM   1755 N  N     . THR B 2 261 ? -5.302  41.505 151.474 1.00 12.84 ? 261 THR A N     1 
ATOM   1756 C  CA    . THR B 2 261 ? -3.985  42.125 151.521 1.00 13.85 ? 261 THR A CA    1 
ATOM   1757 C  C     . THR B 2 261 ? -2.908  41.091 151.222 1.00 14.93 ? 261 THR A C     1 
ATOM   1758 O  O     . THR B 2 261 ? -2.954  39.964 151.734 1.00 16.99 ? 261 THR A O     1 
ATOM   1759 C  CB    . THR B 2 261 ? -3.708  42.769 152.881 1.00 14.55 ? 261 THR A CB    1 
ATOM   1760 O  OG1   . THR B 2 261 ? -3.461  41.768 153.852 1.00 20.12 ? 261 THR A OG1   1 
ATOM   1761 C  CG2   . THR B 2 261 ? -4.864  43.634 153.386 1.00 14.65 ? 261 THR A CG2   1 
ATOM   1762 N  N     . LEU B 2 262 ? -2.036  41.576 150.393 1.00 13.83 ? 262 LEU A N     1 
ATOM   1763 C  CA    . LEU B 2 262 ? -0.820  40.929 149.905 1.00 14.14 ? 262 LEU A CA    1 
ATOM   1764 C  C     . LEU B 2 262 ? 0.297   41.895 150.383 1.00 14.97 ? 262 LEU A C     1 
ATOM   1765 O  O     . LEU B 2 262 ? 0.468   42.993 149.837 1.00 18.22 ? 262 LEU A O     1 
ATOM   1766 C  CB    . LEU B 2 262 ? -0.869  41.017 148.367 1.00 11.23 ? 262 LEU A CB    1 
ATOM   1767 C  CG    . LEU B 2 262 ? -0.626  39.684 147.658 1.00 10.04 ? 262 LEU A CG    1 
ATOM   1768 C  CD1   . LEU B 2 262 ? -1.629  38.600 148.055 1.00 11.77 ? 262 LEU A CD1   1 
ATOM   1769 C  CD2   . LEU B 2 262 ? -0.725  39.798 146.133 1.00 6.41  ? 262 LEU A CD2   1 
ATOM   1770 N  N     . PRO B 2 263 ? 1.175   41.675 151.399 1.00 12.55 ? 263 PRO A N     1 
ATOM   1771 C  CA    . PRO B 2 263 ? 1.312   40.421 152.146 1.00 10.94 ? 263 PRO A CA    1 
ATOM   1772 C  C     . PRO B 2 263 ? 0.045   39.982 152.822 1.00 10.33 ? 263 PRO A C     1 
ATOM   1773 O  O     . PRO B 2 263 ? -0.738  40.859 153.303 1.00 10.04 ? 263 PRO A O     1 
ATOM   1774 C  CB    . PRO B 2 263 ? 2.372   40.723 153.188 1.00 10.01 ? 263 PRO A CB    1 
ATOM   1775 C  CG    . PRO B 2 263 ? 2.827   42.162 152.996 1.00 10.97 ? 263 PRO A CG    1 
ATOM   1776 C  CD    . PRO B 2 263 ? 2.073   42.749 151.852 1.00 10.44 ? 263 PRO A CD    1 
ATOM   1777 N  N     . PRO B 2 264 ? -0.212  38.657 152.908 1.00 10.24 ? 264 PRO A N     1 
ATOM   1778 C  CA    . PRO B 2 264 ? -1.403  38.158 153.566 1.00 10.35 ? 264 PRO A CA    1 
ATOM   1779 C  C     . PRO B 2 264 ? -1.396  38.613 154.992 1.00 11.11 ? 264 PRO A C     1 
ATOM   1780 O  O     . PRO B 2 264 ? -0.406  39.280 155.425 1.00 11.74 ? 264 PRO A O     1 
ATOM   1781 C  CB    . PRO B 2 264 ? -1.289  36.654 153.442 1.00 10.02 ? 264 PRO A CB    1 
ATOM   1782 C  CG    . PRO B 2 264 ? -0.003  36.344 152.692 1.00 10.30 ? 264 PRO A CG    1 
ATOM   1783 C  CD    . PRO B 2 264 ? 0.678   37.634 152.352 1.00 10.91 ? 264 PRO A CD    1 
ATOM   1784 N  N     . ALA B 2 265 ? -2.459  38.285 155.695 1.00 11.32 ? 265 ALA A N     1 
ATOM   1785 C  CA    . ALA B 2 265 ? -2.553  38.617 157.114 1.00 11.00 ? 265 ALA A CA    1 
ATOM   1786 C  C     . ALA B 2 265 ? -1.761  37.592 157.905 1.00 10.44 ? 265 ALA A C     1 
ATOM   1787 O  O     . ALA B 2 265 ? -1.695  36.410 157.527 1.00 9.89  ? 265 ALA A O     1 
ATOM   1788 C  CB    . ALA B 2 265 ? -4.004  38.595 157.591 1.00 11.23 ? 265 ALA A CB    1 
ATOM   1789 N  N     . ASN B 2 266 ? -1.195  38.097 158.961 1.00 10.69 ? 266 ASN A N     1 
ATOM   1790 C  CA    . ASN B 2 266 ? -0.412  37.310 159.897 1.00 11.81 ? 266 ASN A CA    1 
ATOM   1791 C  C     . ASN B 2 266 ? 0.863   36.814 159.205 1.00 12.12 ? 266 ASN A C     1 
ATOM   1792 O  O     . ASN B 2 266 ? 1.334   35.692 159.483 1.00 13.51 ? 266 ASN A O     1 
ATOM   1793 C  CB    . ASN B 2 266 ? -1.306  36.203 160.459 1.00 14.66 ? 266 ASN A CB    1 
ATOM   1794 C  CG    . ASN B 2 266 ? -2.387  36.787 161.383 1.00 17.84 ? 266 ASN A CG    1 
ATOM   1795 O  OD1   . ASN B 2 266 ? -2.279  37.945 161.795 1.00 19.49 ? 266 ASN A OD1   1 
ATOM   1796 N  ND2   . ASN B 2 266 ? -3.430  36.063 161.738 1.00 18.02 ? 266 ASN A ND2   1 
ATOM   1797 N  N     . VAL B 2 267 ? 1.358   37.722 158.335 1.00 10.43 ? 267 VAL A N     1 
ATOM   1798 C  CA    . VAL B 2 267 ? 2.636   37.554 157.604 1.00 9.86  ? 267 VAL A CA    1 
ATOM   1799 C  C     . VAL B 2 267 ? 3.377   38.872 157.427 1.00 10.91 ? 267 VAL A C     1 
ATOM   1800 O  O     . VAL B 2 267 ? 2.839   39.820 156.828 1.00 11.63 ? 267 VAL A O     1 
ATOM   1801 C  CB    . VAL B 2 267 ? 2.466   36.874 156.242 1.00 8.46  ? 267 VAL A CB    1 
ATOM   1802 C  CG1   . VAL B 2 267 ? 1.015   36.734 155.804 1.00 9.45  ? 267 VAL A CG1   1 
ATOM   1803 C  CG2   . VAL B 2 267 ? 3.190   37.609 155.112 1.00 7.11  ? 267 VAL A CG2   1 
ATOM   1804 N  N     . THR B 2 268 ? 4.618   38.871 157.974 1.00 11.90 ? 268 THR A N     1 
ATOM   1805 C  CA    . THR B 2 268 ? 5.494   40.056 157.891 1.00 13.07 ? 268 THR A CA    1 
ATOM   1806 C  C     . THR B 2 268 ? 5.848   40.332 156.446 1.00 14.07 ? 268 THR A C     1 
ATOM   1807 O  O     . THR B 2 268 ? 6.041   39.406 155.639 1.00 15.38 ? 268 THR A O     1 
ATOM   1808 C  CB    . THR B 2 268 ? 6.879   39.997 158.655 1.00 14.89 ? 268 THR A CB    1 
ATOM   1809 O  OG1   . THR B 2 268 ? 7.165   38.777 159.321 1.00 18.51 ? 268 THR A OG1   1 
ATOM   1810 C  CG2   . THR B 2 268 ? 6.982   41.075 159.733 1.00 15.55 ? 268 THR A CG2   1 
ATOM   1811 N  N     . VAL B 2 269 ? 5.900   41.608 156.160 1.00 13.98 ? 269 VAL A N     1 
ATOM   1812 C  CA    . VAL B 2 269 ? 6.297   42.075 154.848 1.00 13.87 ? 269 VAL A CA    1 
ATOM   1813 C  C     . VAL B 2 269 ? 7.679   41.494 154.527 1.00 14.32 ? 269 VAL A C     1 
ATOM   1814 O  O     . VAL B 2 269 ? 8.054   41.330 153.363 1.00 16.11 ? 269 VAL A O     1 
ATOM   1815 C  CB    . VAL B 2 269 ? 6.378   43.603 154.841 1.00 12.02 ? 269 VAL A CB    1 
ATOM   1816 C  CG1   . VAL B 2 269 ? 7.435   44.141 153.874 1.00 9.99  ? 269 VAL A CG1   1 
ATOM   1817 C  CG2   . VAL B 2 269 ? 5.063   44.270 154.431 1.00 12.93 ? 269 VAL A CG2   1 
ATOM   1818 N  N     . ALA B 2 270 ? 8.409   41.176 155.588 1.00 14.31 ? 270 ALA A N     1 
ATOM   1819 C  CA    . ALA B 2 270 ? 9.786   40.662 155.472 1.00 14.63 ? 270 ALA A CA    1 
ATOM   1820 C  C     . ALA B 2 270 ? 9.836   39.195 155.013 1.00 15.52 ? 270 ALA A C     1 
ATOM   1821 O  O     . ALA B 2 270 ? 10.760  38.770 154.313 1.00 16.96 ? 270 ALA A O     1 
ATOM   1822 C  CB    . ALA B 2 270 ? 10.515  40.750 156.810 1.00 10.78 ? 270 ALA A CB    1 
ATOM   1823 N  N     . THR B 2 271 ? 8.859   38.398 155.402 1.00 15.27 ? 271 THR A N     1 
ATOM   1824 C  CA    . THR B 2 271 ? 8.875   36.975 155.013 1.00 15.96 ? 271 THR A CA    1 
ATOM   1825 C  C     . THR B 2 271 ? 8.258   36.791 153.615 1.00 16.06 ? 271 THR A C     1 
ATOM   1826 O  O     . THR B 2 271 ? 8.536   35.807 152.916 1.00 16.50 ? 271 THR A O     1 
ATOM   1827 C  CB    . THR B 2 271 ? 8.146   36.114 156.046 1.00 15.47 ? 271 THR A CB    1 
ATOM   1828 O  OG1   . THR B 2 271 ? 7.107   35.378 155.424 1.00 14.41 ? 271 THR A OG1   1 
ATOM   1829 C  CG2   . THR B 2 271 ? 7.529   36.926 157.182 1.00 16.40 ? 271 THR A CG2   1 
ATOM   1830 N  N     . SER B 2 272 ? 7.434   37.748 153.224 1.00 15.92 ? 272 SER A N     1 
ATOM   1831 C  CA    . SER B 2 272 ? 6.781   37.735 151.900 1.00 16.11 ? 272 SER A CA    1 
ATOM   1832 C  C     . SER B 2 272 ? 7.813   38.041 150.816 1.00 16.64 ? 272 SER A C     1 
ATOM   1833 O  O     . SER B 2 272 ? 7.728   37.552 149.681 1.00 17.96 ? 272 SER A O     1 
ATOM   1834 C  CB    . SER B 2 272 ? 5.690   38.804 151.836 1.00 16.35 ? 272 SER A CB    1 
ATOM   1835 O  OG    . SER B 2 272 ? 6.280   40.086 151.657 1.00 15.72 ? 272 SER A OG    1 
ATOM   1836 N  N     . GLY B 2 273 ? 8.767   38.854 151.211 1.00 16.62 ? 273 GLY A N     1 
ATOM   1837 C  CA    . GLY B 2 273 ? 9.843   39.286 150.325 1.00 16.34 ? 273 GLY A CA    1 
ATOM   1838 C  C     . GLY B 2 273 ? 9.352   40.426 149.423 1.00 16.19 ? 273 GLY A C     1 
ATOM   1839 O  O     . GLY B 2 273 ? 9.943   40.701 148.373 1.00 17.38 ? 273 GLY A O     1 
ATOM   1840 N  N     . GLN B 2 274 ? 8.269   41.067 149.855 1.00 14.25 ? 274 GLN A N     1 
ATOM   1841 C  CA    . GLN B 2 274 ? 7.679   42.223 149.134 1.00 12.36 ? 274 GLN A CA    1 
ATOM   1842 C  C     . GLN B 2 274 ? 8.211   43.534 149.703 1.00 11.06 ? 274 GLN A C     1 
ATOM   1843 O  O     . GLN B 2 274 ? 8.357   43.675 150.931 1.00 10.96 ? 274 GLN A O     1 
ATOM   1844 C  CB    . GLN B 2 274 ? 6.157   42.229 149.276 1.00 12.81 ? 274 GLN A CB    1 
ATOM   1845 C  CG    . GLN B 2 274 ? 5.479   41.128 148.460 1.00 13.71 ? 274 GLN A CG    1 
ATOM   1846 C  CD    . GLN B 2 274 ? 3.961   41.290 148.381 1.00 14.75 ? 274 GLN A CD    1 
ATOM   1847 O  OE1   . GLN B 2 274 ? 3.461   42.413 148.381 1.00 13.90 ? 274 GLN A OE1   1 
ATOM   1848 N  NE2   . GLN B 2 274 ? 3.187   40.223 148.311 1.00 16.06 ? 274 GLN A NE2   1 
ATOM   1849 N  N     . PRO B 2 275 ? 8.522   44.523 148.846 1.00 10.42 ? 275 PRO A N     1 
ATOM   1850 C  CA    . PRO B 2 275 ? 9.036   45.801 149.294 1.00 10.24 ? 275 PRO A CA    1 
ATOM   1851 C  C     . PRO B 2 275 ? 7.992   46.560 150.048 1.00 10.72 ? 275 PRO A C     1 
ATOM   1852 O  O     . PRO B 2 275 ? 8.338   47.442 150.885 1.00 11.43 ? 275 PRO A O     1 
ATOM   1853 C  CB    . PRO B 2 275 ? 9.329   46.567 148.038 1.00 9.41  ? 275 PRO A CB    1 
ATOM   1854 C  CG    . PRO B 2 275 ? 8.884   45.717 146.872 1.00 9.28  ? 275 PRO A CG    1 
ATOM   1855 C  CD    . PRO B 2 275 ? 8.371   44.406 147.395 1.00 9.82  ? 275 PRO A CD    1 
ATOM   1856 N  N     . PHE B 2 276 ? 6.734   46.273 149.743 1.00 10.17 ? 276 PHE A N     1 
ATOM   1857 C  CA    . PHE B 2 276 ? 5.635   46.951 150.439 1.00 10.11 ? 276 PHE A CA    1 
ATOM   1858 C  C     . PHE B 2 276 ? 4.373   46.086 150.497 1.00 11.16 ? 276 PHE A C     1 
ATOM   1859 O  O     . PHE B 2 276 ? 4.419   44.869 150.260 1.00 10.94 ? 276 PHE A O     1 
ATOM   1860 C  CB    . PHE B 2 276 ? 5.330   48.326 149.830 1.00 8.33  ? 276 PHE A CB    1 
ATOM   1861 C  CG    . PHE B 2 276 ? 5.479   48.423 148.315 1.00 7.13  ? 276 PHE A CG    1 
ATOM   1862 C  CD1   . PHE B 2 276 ? 6.713   48.767 147.748 1.00 7.46  ? 276 PHE A CD1   1 
ATOM   1863 C  CD2   . PHE B 2 276 ? 4.371   48.188 147.501 1.00 7.53  ? 276 PHE A CD2   1 
ATOM   1864 C  CE1   . PHE B 2 276 ? 6.831   48.876 146.358 1.00 8.66  ? 276 PHE A CE1   1 
ATOM   1865 C  CE2   . PHE B 2 276 ? 4.488   48.295 146.115 1.00 6.92  ? 276 PHE A CE2   1 
ATOM   1866 C  CZ    . PHE B 2 276 ? 5.718   48.640 145.542 1.00 8.01  ? 276 PHE A CZ    1 
ATOM   1867 N  N     . ASN B 2 277 ? 3.287   46.775 150.808 1.00 12.42 ? 277 ASN A N     1 
ATOM   1868 C  CA    . ASN B 2 277 ? 1.996   46.148 151.138 1.00 13.36 ? 277 ASN A CA    1 
ATOM   1869 C  C     . ASN B 2 277 ? 0.799   46.732 150.350 1.00 14.91 ? 277 ASN A C     1 
ATOM   1870 O  O     . ASN B 2 277 ? 0.492   47.928 150.450 1.00 17.29 ? 277 ASN A O     1 
ATOM   1871 C  CB    . ASN B 2 277 ? 1.761   46.447 152.621 1.00 11.19 ? 277 ASN A CB    1 
ATOM   1872 C  CG    . ASN B 2 277 ? 0.974   45.390 153.371 1.00 14.70 ? 277 ASN A CG    1 
ATOM   1873 O  OD1   . ASN B 2 277 ? 0.014   44.858 152.831 1.00 14.64 ? 277 ASN A OD1   1 
ATOM   1874 N  ND2   . ASN B 2 277 ? 1.316   45.068 154.605 1.00 16.76 ? 277 ASN A ND2   1 
ATOM   1875 N  N     . LEU B 2 278 ? 0.133   45.849 149.602 1.00 13.98 ? 278 LEU A N     1 
ATOM   1876 C  CA    . LEU B 2 278 ? -1.092  46.178 148.819 1.00 12.25 ? 278 LEU A CA    1 
ATOM   1877 C  C     . LEU B 2 278 ? -2.334  45.785 149.646 1.00 11.00 ? 278 LEU A C     1 
ATOM   1878 O  O     . LEU B 2 278 ? -2.546  44.605 149.946 1.00 9.67  ? 278 LEU A O     1 
ATOM   1879 C  CB    . LEU B 2 278 ? -1.127  45.356 147.514 1.00 11.18 ? 278 LEU A CB    1 
ATOM   1880 C  CG    . LEU B 2 278 ? -0.609  46.104 146.280 1.00 12.00 ? 278 LEU A CG    1 
ATOM   1881 C  CD1   . LEU B 2 278 ? 0.913   46.252 146.268 1.00 11.56 ? 278 LEU A CD1   1 
ATOM   1882 C  CD2   . LEU B 2 278 ? -0.963  45.404 144.961 1.00 12.79 ? 278 LEU A CD2   1 
ATOM   1883 N  N     . ALA B 2 279 ? -3.147  46.775 150.019 1.00 10.81 ? 279 ALA A N     1 
ATOM   1884 C  CA    . ALA B 2 279 ? -4.370  46.522 150.833 1.00 11.44 ? 279 ALA A CA    1 
ATOM   1885 C  C     . ALA B 2 279 ? -5.640  46.893 150.056 1.00 12.31 ? 279 ALA A C     1 
ATOM   1886 O  O     . ALA B 2 279 ? -5.832  48.044 149.660 1.00 14.68 ? 279 ALA A O     1 
ATOM   1887 C  CB    . ALA B 2 279 ? -4.342  47.335 152.128 1.00 8.81  ? 279 ALA A CB    1 
ATOM   1888 N  N     . ALA B 2 280 ? -6.465  45.892 149.869 1.00 11.70 ? 280 ALA A N     1 
ATOM   1889 C  CA    . ALA B 2 280 ? -7.769  45.990 149.217 1.00 10.98 ? 280 ALA A CA    1 
ATOM   1890 C  C     . ALA B 2 280 ? -8.718  46.607 150.273 1.00 11.67 ? 280 ALA A C     1 
ATOM   1891 O  O     . ALA B 2 280 ? -9.701  47.276 149.921 1.00 12.31 ? 280 ALA A O     1 
ATOM   1892 C  CB    . ALA B 2 280 ? -8.355  44.629 148.858 1.00 6.24  ? 280 ALA A CB    1 
ATOM   1893 N  N     . GLY B 2 281 ? -8.413  46.312 151.533 1.00 11.11 ? 281 GLY A N     1 
ATOM   1894 C  CA    . GLY B 2 281 ? -9.236  46.864 152.615 1.00 10.31 ? 281 GLY A CA    1 
ATOM   1895 C  C     . GLY B 2 281 ? -10.309 45.910 153.066 1.00 10.38 ? 281 GLY A C     1 
ATOM   1896 O  O     . GLY B 2 281 ? -10.103 44.687 153.008 1.00 10.51 ? 281 GLY A O     1 
ATOM   1897 N  N     . ALA B 2 282 ? -11.416 46.464 153.514 1.00 10.39 ? 282 ALA A N     1 
ATOM   1898 C  CA    . ALA B 2 282 ? -12.533 45.684 154.035 1.00 10.57 ? 282 ALA A CA    1 
ATOM   1899 C  C     . ALA B 2 282 ? -13.194 44.859 152.939 1.00 11.11 ? 282 ALA A C     1 
ATOM   1900 O  O     . ALA B 2 282 ? -13.611 45.419 151.921 1.00 11.45 ? 282 ALA A O     1 
ATOM   1901 C  CB    . ALA B 2 282 ? -13.596 46.578 154.652 1.00 10.24 ? 282 ALA A CB    1 
ATOM   1902 N  N     . GLU B 2 283 ? -13.360 43.597 153.282 1.00 11.14 ? 283 GLU A N     1 
ATOM   1903 C  CA    . GLU B 2 283 ? -13.963 42.601 152.395 1.00 11.86 ? 283 GLU A CA    1 
ATOM   1904 C  C     . GLU B 2 283 ? -15.288 42.984 151.785 1.00 12.39 ? 283 GLU A C     1 
ATOM   1905 O  O     . GLU B 2 283 ? -15.628 42.488 150.674 1.00 14.50 ? 283 GLU A O     1 
ATOM   1906 C  CB    . GLU B 2 283 ? -14.020 41.242 153.046 1.00 11.99 ? 283 GLU A CB    1 
ATOM   1907 C  CG    . GLU B 2 283 ? -15.342 40.586 153.390 1.00 15.01 ? 283 GLU A CG    1 
ATOM   1908 C  CD    . GLU B 2 283 ? -15.152 39.406 154.309 1.00 17.86 ? 283 GLU A CD    1 
ATOM   1909 O  OE1   . GLU B 2 283 ? -14.263 38.643 153.877 1.00 21.27 ? 283 GLU A OE1   1 
ATOM   1910 O  OE2   . GLU B 2 283 ? -15.744 39.215 155.340 1.00 19.95 ? 283 GLU A OE2   1 
ATOM   1911 N  N     . ALA B 2 284 ? -16.046 43.872 152.401 1.00 11.59 ? 284 ALA A N     1 
ATOM   1912 C  CA    . ALA B 2 284 ? -17.330 44.241 151.761 1.00 10.63 ? 284 ALA A CA    1 
ATOM   1913 C  C     . ALA B 2 284 ? -17.103 45.412 150.808 1.00 9.75  ? 284 ALA A C     1 
ATOM   1914 O  O     . ALA B 2 284 ? -18.051 45.851 150.128 1.00 9.73  ? 284 ALA A O     1 
ATOM   1915 C  CB    . ALA B 2 284 ? -18.361 44.585 152.808 1.00 10.32 ? 284 ALA A CB    1 
ATOM   1916 N  N     . VAL B 2 285 ? -15.880 45.891 150.769 1.00 8.99  ? 285 VAL A N     1 
ATOM   1917 C  CA    . VAL B 2 285 ? -15.552 47.049 149.923 1.00 8.79  ? 285 VAL A CA    1 
ATOM   1918 C  C     . VAL B 2 285 ? -14.795 46.757 148.652 1.00 8.20  ? 285 VAL A C     1 
ATOM   1919 O  O     . VAL B 2 285 ? -15.176 47.270 147.572 1.00 7.74  ? 285 VAL A O     1 
ATOM   1920 C  CB    . VAL B 2 285 ? -14.853 48.059 150.867 1.00 8.57  ? 285 VAL A CB    1 
ATOM   1921 C  CG1   . VAL B 2 285 ? -14.231 49.220 150.140 1.00 9.29  ? 285 VAL A CG1   1 
ATOM   1922 C  CG2   . VAL B 2 285 ? -15.834 48.532 151.922 1.00 7.67  ? 285 VAL A CG2   1 
ATOM   1923 N  N     . SER B 2 286 ? -13.740 45.989 148.721 1.00 8.20  ? 286 SER A N     1 
ATOM   1924 C  CA    . SER B 2 286 ? -12.869 45.592 147.609 1.00 7.84  ? 286 SER A CA    1 
ATOM   1925 C  C     . SER B 2 286 ? -12.202 44.252 147.954 1.00 8.65  ? 286 SER A C     1 
ATOM   1926 O  O     . SER B 2 286 ? -12.550 43.621 148.974 1.00 9.32  ? 286 SER A O     1 
ATOM   1927 C  CB    . SER B 2 286 ? -11.825 46.663 147.360 1.00 4.79  ? 286 SER A CB    1 
ATOM   1928 O  OG    . SER B 2 286 ? -11.346 46.657 146.046 1.00 3.33  ? 286 SER A OG    1 
ATOM   1929 N  N     . GLY B 2 287 ? -11.269 43.842 147.102 1.00 8.64  ? 287 GLY A N     1 
ATOM   1930 C  CA    . GLY B 2 287 ? -10.553 42.554 147.331 1.00 8.51  ? 287 GLY A CA    1 
ATOM   1931 C  C     . GLY B 2 287 ? -9.631  42.306 146.138 1.00 8.62  ? 287 GLY A C     1 
ATOM   1932 O  O     . GLY B 2 287 ? -9.883  42.887 145.050 1.00 9.15  ? 287 GLY A O     1 
ATOM   1933 N  N     . ILE B 2 288 ? -8.591  41.500 146.366 1.00 8.85  ? 288 ILE A N     1 
ATOM   1934 C  CA    . ILE B 2 288 ? -7.667  41.188 145.225 1.00 10.30 ? 288 ILE A CA    1 
ATOM   1935 C  C     . ILE B 2 288 ? -8.176  39.876 144.634 1.00 11.97 ? 288 ILE A C     1 
ATOM   1936 O  O     . ILE B 2 288 ? -7.826  38.802 145.172 1.00 12.38 ? 288 ILE A O     1 
ATOM   1937 C  CB    . ILE B 2 288 ? -6.189  41.188 145.689 1.00 7.66  ? 288 ILE A CB    1 
ATOM   1938 C  CG1   . ILE B 2 288 ? -5.847  42.580 146.300 1.00 7.19  ? 288 ILE A CG1   1 
ATOM   1939 C  CG2   . ILE B 2 288 ? -5.160  40.823 144.600 1.00 3.71  ? 288 ILE A CG2   1 
ATOM   1940 C  CD1   . ILE B 2 288 ? -4.704  42.460 147.335 1.00 5.57  ? 288 ILE A CD1   1 
ATOM   1941 N  N     . VAL B 2 289 ? -9.020  39.967 143.603 1.00 12.78 ? 289 VAL A N     1 
ATOM   1942 C  CA    . VAL B 2 289 ? -9.626  38.751 143.058 1.00 13.20 ? 289 VAL A CA    1 
ATOM   1943 C  C     . VAL B 2 289 ? -8.832  38.016 142.014 1.00 14.55 ? 289 VAL A C     1 
ATOM   1944 O  O     . VAL B 2 289 ? -9.361  36.953 141.598 1.00 17.21 ? 289 VAL A O     1 
ATOM   1945 C  CB    . VAL B 2 289 ? -11.080 38.999 142.625 1.00 11.07 ? 289 VAL A CB    1 
ATOM   1946 C  CG1   . VAL B 2 289 ? -11.951 39.709 143.651 1.00 10.09 ? 289 VAL A CG1   1 
ATOM   1947 C  CG2   . VAL B 2 289 ? -11.128 39.707 141.274 1.00 8.19  ? 289 VAL A CG2   1 
ATOM   1948 N  N     . GLY B 2 290 ? -7.665  38.512 141.626 1.00 13.69 ? 290 GLY A N     1 
ATOM   1949 C  CA    . GLY B 2 290 ? -6.834  37.816 140.607 1.00 11.93 ? 290 GLY A CA    1 
ATOM   1950 C  C     . GLY B 2 290 ? -5.699  38.690 140.106 1.00 11.33 ? 290 GLY A C     1 
ATOM   1951 O  O     . GLY B 2 290 ? -5.716  39.909 140.317 1.00 10.43 ? 290 GLY A O     1 
ATOM   1952 N  N     . TRP B 2 291 ? -4.721  38.079 139.461 1.00 10.82 ? 291 TRP A N     1 
ATOM   1953 C  CA    . TRP B 2 291 ? -3.572  38.794 138.887 1.00 10.28 ? 291 TRP A CA    1 
ATOM   1954 C  C     . TRP B 2 291 ? -3.422  38.477 137.400 1.00 10.17 ? 291 TRP A C     1 
ATOM   1955 O  O     . TRP B 2 291 ? -3.043  37.374 136.956 1.00 11.36 ? 291 TRP A O     1 
ATOM   1956 C  CB    . TRP B 2 291 ? -2.314  38.645 139.752 1.00 6.59  ? 291 TRP A CB    1 
ATOM   1957 C  CG    . TRP B 2 291 ? -1.424  39.845 139.557 1.00 6.97  ? 291 TRP A CG    1 
ATOM   1958 C  CD1   . TRP B 2 291 ? -0.607  40.072 138.489 1.00 6.21  ? 291 TRP A CD1   1 
ATOM   1959 C  CD2   . TRP B 2 291 ? -1.351  41.022 140.377 1.00 8.46  ? 291 TRP A CD2   1 
ATOM   1960 N  NE1   . TRP B 2 291 ? 0.007   41.290 138.618 1.00 7.77  ? 291 TRP A NE1   1 
ATOM   1961 C  CE2   . TRP B 2 291 ? -0.432  41.902 139.754 1.00 8.85  ? 291 TRP A CE2   1 
ATOM   1962 C  CE3   . TRP B 2 291 ? -1.958  41.411 141.572 1.00 9.58  ? 291 TRP A CE3   1 
ATOM   1963 C  CZ2   . TRP B 2 291 ? -0.107  43.139 140.290 1.00 9.40  ? 291 TRP A CZ2   1 
ATOM   1964 C  CZ3   . TRP B 2 291 ? -1.618  42.631 142.117 1.00 9.91  ? 291 TRP A CZ3   1 
ATOM   1965 C  CH2   . TRP B 2 291 ? -0.724  43.493 141.480 1.00 10.08 ? 291 TRP A CH2   1 
ATOM   1966 N  N     . GLY B 2 292 ? -3.734  39.446 136.541 1.00 8.85  ? 292 GLY A N     1 
ATOM   1967 C  CA    . GLY B 2 292 ? -3.699  39.272 135.091 1.00 8.58  ? 292 GLY A CA    1 
ATOM   1968 C  C     . GLY B 2 292 ? -2.310  39.223 134.498 1.00 9.16  ? 292 GLY A C     1 
ATOM   1969 O  O     . GLY B 2 292 ? -1.299  39.352 135.204 1.00 9.56  ? 292 GLY A O     1 
ATOM   1970 N  N     . ASN B 2 293 ? -2.259  39.061 133.181 1.00 8.68  ? 293 ASN A N     1 
ATOM   1971 C  CA    . ASN B 2 293 ? -0.985  38.986 132.468 1.00 8.19  ? 293 ASN A CA    1 
ATOM   1972 C  C     . ASN B 2 293 ? -0.631  40.257 131.717 1.00 8.60  ? 293 ASN A C     1 
ATOM   1973 O  O     . ASN B 2 293 ? -0.375  40.149 130.489 1.00 10.38 ? 293 ASN A O     1 
ATOM   1974 C  CB    . ASN B 2 293 ? -1.015  37.752 131.539 1.00 5.94  ? 293 ASN A CB    1 
ATOM   1975 C  CG    . ASN B 2 293 ? -1.135  36.501 132.392 1.00 6.09  ? 293 ASN A CG    1 
ATOM   1976 O  OD1   . ASN B 2 293 ? -1.995  35.640 132.199 1.00 5.34  ? 293 ASN A OD1   1 
ATOM   1977 N  ND2   . ASN B 2 293 ? -0.258  36.441 133.402 1.00 9.47  ? 293 ASN A ND2   1 
ATOM   1978 N  N     . MET B 2 294 ? -0.612  41.378 132.406 1.00 7.69  ? 294 MET A N     1 
ATOM   1979 C  CA    . MET B 2 294 ? -0.284  42.684 131.772 1.00 7.41  ? 294 MET A CA    1 
ATOM   1980 C  C     . MET B 2 294 ? 0.783   43.306 132.662 1.00 7.95  ? 294 MET A C     1 
ATOM   1981 O  O     . MET B 2 294 ? 0.856   42.930 133.850 1.00 8.76  ? 294 MET A O     1 
ATOM   1982 C  CB    . MET B 2 294 ? -1.541  43.515 131.642 1.00 8.23  ? 294 MET A CB    1 
ATOM   1983 C  CG    . MET B 2 294 ? -2.738  42.711 131.252 1.00 9.81  ? 294 MET A CG    1 
ATOM   1984 S  SD    . MET B 2 294 ? -3.187  43.034 129.505 1.00 13.79 ? 294 MET A SD    1 
ATOM   1985 C  CE    . MET B 2 294 ? -2.027  44.329 129.090 1.00 10.09 ? 294 MET A CE    1 
ATOM   1986 N  N     . ASP B 2 295 ? 1.613   44.173 132.147 1.00 8.85  ? 295 ASP A N     1 
ATOM   1987 C  CA    . ASP B 2 295 ? 2.665   44.794 133.015 1.00 9.68  ? 295 ASP A CA    1 
ATOM   1988 C  C     . ASP B 2 295 ? 1.933   45.872 133.814 1.00 10.37 ? 295 ASP A C     1 
ATOM   1989 O  O     . ASP B 2 295 ? 0.937   46.434 133.300 1.00 11.14 ? 295 ASP A O     1 
ATOM   1990 C  CB    . ASP B 2 295 ? 3.888   45.253 132.241 1.00 9.11  ? 295 ASP A CB    1 
ATOM   1991 C  CG    . ASP B 2 295 ? 4.871   44.114 131.982 1.00 10.74 ? 295 ASP A CG    1 
ATOM   1992 O  OD1   . ASP B 2 295 ? 4.499   42.965 132.327 1.00 9.91  ? 295 ASP A OD1   1 
ATOM   1993 O  OD2   . ASP B 2 295 ? 5.978   44.318 131.452 1.00 12.88 ? 295 ASP A OD2   1 
ATOM   1994 N  N     . THR B 2 296 ? 2.385   46.078 135.031 1.00 10.39 ? 296 THR A N     1 
ATOM   1995 C  CA    . THR B 2 296 ? 1.721   47.094 135.885 1.00 10.60 ? 296 THR A CA    1 
ATOM   1996 C  C     . THR B 2 296 ? 2.242   48.418 135.363 1.00 11.68 ? 296 THR A C     1 
ATOM   1997 O  O     . THR B 2 296 ? 3.458   48.446 135.100 1.00 12.47 ? 296 THR A O     1 
ATOM   1998 C  CB    . THR B 2 296 ? 2.053   46.859 137.399 1.00 8.59  ? 296 THR A CB    1 
ATOM   1999 O  OG1   . THR B 2 296 ? 1.858   45.431 137.645 1.00 10.03 ? 296 THR A OG1   1 
ATOM   2000 C  CG2   . THR B 2 296 ? 1.268   47.735 138.377 1.00 7.41  ? 296 THR A CG2   1 
ATOM   2001 N  N     . ILE B 2 297 ? 1.357   49.364 135.157 1.00 12.25 ? 297 ILE A N     1 
ATOM   2002 C  CA    . ILE B 2 297 ? 1.838   50.690 134.687 1.00 12.09 ? 297 ILE A CA    1 
ATOM   2003 C  C     . ILE B 2 297 ? 2.048   51.446 136.019 1.00 12.05 ? 297 ILE A C     1 
ATOM   2004 O  O     . ILE B 2 297 ? 1.093   51.430 136.816 1.00 12.40 ? 297 ILE A O     1 
ATOM   2005 C  CB    . ILE B 2 297 ? 0.904   51.445 133.718 1.00 9.91  ? 297 ILE A CB    1 
ATOM   2006 C  CG1   . ILE B 2 297 ? 0.322   50.526 132.625 1.00 8.33  ? 297 ILE A CG1   1 
ATOM   2007 C  CG2   . ILE B 2 297 ? 1.642   52.676 133.087 1.00 10.75 ? 297 ILE A CG2   1 
ATOM   2008 C  CD1   . ILE B 2 297 ? -0.454  51.281 131.505 1.00 6.51  ? 297 ILE A CD1   1 
ATOM   2009 N  N     . VAL B 2 298 ? 3.226   51.968 136.211 1.00 10.90 ? 298 VAL A N     1 
ATOM   2010 C  CA    . VAL B 2 298 ? 3.602   52.717 137.407 1.00 10.15 ? 298 VAL A CA    1 
ATOM   2011 C  C     . VAL B 2 298 ? 3.663   54.205 137.021 1.00 10.81 ? 298 VAL A C     1 
ATOM   2012 O  O     . VAL B 2 298 ? 4.392   54.547 136.086 1.00 11.64 ? 298 VAL A O     1 
ATOM   2013 C  CB    . VAL B 2 298 ? 5.000   52.315 137.927 1.00 8.23  ? 298 VAL A CB    1 
ATOM   2014 C  CG1   . VAL B 2 298 ? 5.397   53.157 139.127 1.00 8.05  ? 298 VAL A CG1   1 
ATOM   2015 C  CG2   . VAL B 2 298 ? 5.168   50.828 138.152 1.00 7.32  ? 298 VAL A CG2   1 
ATOM   2016 N  N     . ILE B 2 299 ? 2.926   55.010 137.710 1.00 11.38 ? 299 ILE A N     1 
ATOM   2017 C  CA    . ILE B 2 299 ? 2.900   56.450 137.527 1.00 11.18 ? 299 ILE A CA    1 
ATOM   2018 C  C     . ILE B 2 299 ? 3.341   57.069 138.865 1.00 11.97 ? 299 ILE A C     1 
ATOM   2019 O  O     . ILE B 2 299 ? 2.857   56.631 139.928 1.00 13.53 ? 299 ILE A O     1 
ATOM   2020 C  CB    . ILE B 2 299 ? 1.490   56.990 137.125 1.00 10.59 ? 299 ILE A CB    1 
ATOM   2021 C  CG1   . ILE B 2 299 ? 0.800   55.980 136.186 1.00 10.44 ? 299 ILE A CG1   1 
ATOM   2022 C  CG2   . ILE B 2 299 ? 1.566   58.419 136.509 1.00 10.16 ? 299 ILE A CG2   1 
ATOM   2023 C  CD1   . ILE B 2 299 ? -0.323  56.560 135.279 1.00 9.93  ? 299 ILE A CD1   1 
ATOM   2024 N  N     . ARG B 2 300 ? 4.232   58.017 138.774 1.00 11.48 ? 300 ARG A N     1 
ATOM   2025 C  CA    . ARG B 2 300 ? 4.736   58.777 139.901 1.00 10.43 ? 300 ARG A CA    1 
ATOM   2026 C  C     . ARG B 2 300 ? 4.505   60.266 139.589 1.00 10.52 ? 300 ARG A C     1 
ATOM   2027 O  O     . ARG B 2 300 ? 5.220   60.809 138.725 1.00 11.17 ? 300 ARG A O     1 
ATOM   2028 C  CB    . ARG B 2 300 ? 6.209   58.580 140.206 1.00 9.63  ? 300 ARG A CB    1 
ATOM   2029 C  CG    . ARG B 2 300 ? 6.647   59.507 141.364 1.00 10.45 ? 300 ARG A CG    1 
ATOM   2030 C  CD    . ARG B 2 300 ? 8.125   59.507 141.484 1.00 8.73  ? 300 ARG A CD    1 
ATOM   2031 N  NE    . ARG B 2 300 ? 8.713   60.093 140.262 1.00 10.63 ? 300 ARG A NE    1 
ATOM   2032 C  CZ    . ARG B 2 300 ? 10.049  60.262 140.195 1.00 11.24 ? 300 ARG A CZ    1 
ATOM   2033 N  NH1   . ARG B 2 300 ? 10.781  59.898 141.273 1.00 13.11 ? 300 ARG A NH1   1 
ATOM   2034 N  NH2   . ARG B 2 300 ? 10.669  60.781 139.139 1.00 11.24 ? 300 ARG A NH2   1 
ATOM   2035 N  N     . VAL B 2 301 ? 3.511   60.844 140.201 1.00 10.00 ? 301 VAL A N     1 
ATOM   2036 C  CA    . VAL B 2 301 ? 3.170   62.278 140.046 1.00 9.80  ? 301 VAL A CA    1 
ATOM   2037 C  C     . VAL B 2 301 ? 4.066   62.940 141.110 1.00 10.58 ? 301 VAL A C     1 
ATOM   2038 O  O     . VAL B 2 301 ? 4.275   62.275 142.146 1.00 11.24 ? 301 VAL A O     1 
ATOM   2039 C  CB    . VAL B 2 301 ? 1.683   62.546 140.308 1.00 7.12  ? 301 VAL A CB    1 
ATOM   2040 C  CG1   . VAL B 2 301 ? 1.300   63.999 140.046 1.00 5.33  ? 301 VAL A CG1   1 
ATOM   2041 C  CG2   . VAL B 2 301 ? 0.730   61.582 139.636 1.00 5.52  ? 301 VAL A CG2   1 
ATOM   2042 N  N     . SER B 2 302 ? 4.535   64.136 140.891 1.00 10.98 ? 302 SER A N     1 
ATOM   2043 C  CA    . SER B 2 302 ? 5.455   64.725 141.905 1.00 12.39 ? 302 SER A CA    1 
ATOM   2044 C  C     . SER B 2 302 ? 5.359   66.228 142.051 1.00 13.45 ? 302 SER A C     1 
ATOM   2045 O  O     . SER B 2 302 ? 5.987   67.005 141.299 1.00 14.64 ? 302 SER A O     1 
ATOM   2046 C  CB    . SER B 2 302 ? 6.860   64.272 141.514 1.00 12.19 ? 302 SER A CB    1 
ATOM   2047 O  OG    . SER B 2 302 ? 7.745   64.675 142.527 1.00 14.44 ? 302 SER A OG    1 
ATOM   2048 N  N     . ALA B 2 303 ? 4.562   66.637 143.036 1.00 13.90 ? 303 ALA A N     1 
ATOM   2049 C  CA    . ALA B 2 303 ? 4.298   68.028 143.325 1.00 13.86 ? 303 ALA A CA    1 
ATOM   2050 C  C     . ALA B 2 303 ? 5.241   68.605 144.371 1.00 14.31 ? 303 ALA A C     1 
ATOM   2051 O  O     . ALA B 2 303 ? 5.256   68.213 145.552 1.00 13.97 ? 303 ALA A O     1 
ATOM   2052 C  CB    . ALA B 2 303 ? 2.846   68.222 143.797 1.00 12.17 ? 303 ALA A CB    1 
ATOM   2053 N  N     . PRO B 2 304 ? 6.004   69.596 143.924 1.00 14.34 ? 304 PRO A N     1 
ATOM   2054 C  CA    . PRO B 2 304 ? 6.912   70.333 144.820 1.00 14.42 ? 304 PRO A CA    1 
ATOM   2055 C  C     . PRO B 2 304 ? 6.061   71.091 145.843 1.00 15.41 ? 304 PRO A C     1 
ATOM   2056 O  O     . PRO B 2 304 ? 4.812   71.068 145.802 1.00 15.39 ? 304 PRO A O     1 
ATOM   2057 C  CB    . PRO B 2 304 ? 7.677   71.247 143.878 1.00 13.68 ? 304 PRO A CB    1 
ATOM   2058 C  CG    . PRO B 2 304 ? 6.712   71.485 142.753 1.00 13.90 ? 304 PRO A CG    1 
ATOM   2059 C  CD    . PRO B 2 304 ? 6.041   70.119 142.546 1.00 13.74 ? 304 PRO A CD    1 
ATOM   2060 N  N     . THR B 2 305 ? 6.725   71.767 146.779 1.00 16.32 ? 305 THR A N     1 
ATOM   2061 C  CA    . THR B 2 305 ? 5.947   72.511 147.788 1.00 15.94 ? 305 THR A CA    1 
ATOM   2062 C  C     . THR B 2 305 ? 5.225   73.678 147.141 1.00 14.86 ? 305 THR A C     1 
ATOM   2063 O  O     . THR B 2 305 ? 5.838   74.354 146.296 1.00 14.98 ? 305 THR A O     1 
ATOM   2064 C  CB    . THR B 2 305 ? 6.841   73.018 148.973 1.00 17.22 ? 305 THR A CB    1 
ATOM   2065 O  OG1   . THR B 2 305 ? 6.376   72.267 150.144 1.00 20.46 ? 305 THR A OG1   1 
ATOM   2066 C  CG2   . THR B 2 305 ? 6.734   74.534 149.208 1.00 15.57 ? 305 THR A CG2   1 
ATOM   2067 N  N     . GLY B 2 306 ? 3.988   73.888 147.548 1.00 14.27 ? 306 GLY A N     1 
ATOM   2068 C  CA    . GLY B 2 306 ? 3.210   74.997 146.968 1.00 14.04 ? 306 GLY A CA    1 
ATOM   2069 C  C     . GLY B 2 306 ? 2.586   74.654 145.624 1.00 14.35 ? 306 GLY A C     1 
ATOM   2070 O  O     . GLY B 2 306 ? 1.948   75.500 144.951 1.00 15.41 ? 306 GLY A O     1 
ATOM   2071 N  N     . ALA B 2 307 ? 2.714   73.411 145.184 1.00 13.36 ? 307 ALA A N     1 
ATOM   2072 C  CA    . ALA B 2 307 ? 2.131   73.021 143.890 1.00 13.14 ? 307 ALA A CA    1 
ATOM   2073 C  C     . ALA B 2 307 ? 0.642   72.750 144.028 1.00 12.55 ? 307 ALA A C     1 
ATOM   2074 O  O     . ALA B 2 307 ? 0.195   72.076 144.973 1.00 12.92 ? 307 ALA A O     1 
ATOM   2075 C  CB    . ALA B 2 307 ? 2.907   71.827 143.323 1.00 13.87 ? 307 ALA A CB    1 
ATOM   2076 N  N     . VAL B 2 308 ? -0.120  73.244 143.065 1.00 11.81 ? 308 VAL A N     1 
ATOM   2077 C  CA    . VAL B 2 308 ? -1.573  73.000 143.026 1.00 11.07 ? 308 VAL A CA    1 
ATOM   2078 C  C     . VAL B 2 308 ? -1.882  72.200 141.749 1.00 11.58 ? 308 VAL A C     1 
ATOM   2079 O  O     . VAL B 2 308 ? -2.330  72.708 140.724 1.00 11.80 ? 308 VAL A O     1 
ATOM   2080 C  CB    . VAL B 2 308 ? -2.405  74.248 143.259 1.00 8.96  ? 308 VAL A CB    1 
ATOM   2081 C  CG1   . VAL B 2 308 ? -3.904  73.955 143.350 1.00 6.32  ? 308 VAL A CG1   1 
ATOM   2082 C  CG2   . VAL B 2 308 ? -1.977  74.956 144.536 1.00 7.78  ? 308 VAL A CG2   1 
ATOM   2083 N  N     . ASN B 2 309 ? -1.585  70.915 141.899 1.00 11.80 ? 309 ASN A N     1 
ATOM   2084 C  CA    . ASN B 2 309 ? -1.702  69.844 140.934 1.00 10.74 ? 309 ASN A CA    1 
ATOM   2085 C  C     . ASN B 2 309 ? -3.010  69.063 141.148 1.00 10.55 ? 309 ASN A C     1 
ATOM   2086 O  O     . ASN B 2 309 ? -3.246  68.389 142.152 1.00 11.54 ? 309 ASN A O     1 
ATOM   2087 C  CB    . ASN B 2 309 ? -0.503  68.898 140.936 1.00 10.77 ? 309 ASN A CB    1 
ATOM   2088 C  CG    . ASN B 2 309 ? 0.853   69.510 140.700 1.00 11.84 ? 309 ASN A CG    1 
ATOM   2089 O  OD1   . ASN B 2 309 ? 1.908   68.807 140.728 1.00 13.15 ? 309 ASN A OD1   1 
ATOM   2090 N  ND2   . ASN B 2 309 ? 0.920   70.811 140.440 1.00 9.63  ? 309 ASN A ND2   1 
ATOM   2091 N  N     . SER B 2 310 ? -3.820  69.160 140.112 1.00 10.13 ? 310 SER A N     1 
ATOM   2092 C  CA    . SER B 2 310 ? -5.116  68.465 140.102 1.00 9.49  ? 310 SER A CA    1 
ATOM   2093 C  C     . SER B 2 310 ? -5.378  68.013 138.669 1.00 9.75  ? 310 SER A C     1 
ATOM   2094 O  O     . SER B 2 310 ? -5.088  68.744 137.714 1.00 9.90  ? 310 SER A O     1 
ATOM   2095 C  CB    . SER B 2 310 ? -6.205  69.375 140.635 1.00 8.14  ? 310 SER A CB    1 
ATOM   2096 O  OG    . SER B 2 310 ? -5.581  70.634 140.853 1.00 8.39  ? 310 SER A OG    1 
ATOM   2097 N  N     . ALA B 2 311 ? -5.936  66.815 138.663 1.00 9.76  ? 311 ALA A N     1 
ATOM   2098 C  CA    . ALA B 2 311 ? -6.272  66.085 137.450 1.00 10.60 ? 311 ALA A CA    1 
ATOM   2099 C  C     . ALA B 2 311 ? -7.508  65.209 137.627 1.00 11.66 ? 311 ALA A C     1 
ATOM   2100 O  O     . ALA B 2 311 ? -8.077  65.013 138.706 1.00 11.96 ? 311 ALA A O     1 
ATOM   2101 C  CB    . ALA B 2 311 ? -5.054  65.176 137.155 1.00 8.33  ? 311 ALA A CB    1 
ATOM   2102 N  N     . ILE B 2 312 ? -7.912  64.709 136.482 1.00 11.67 ? 312 ILE A N     1 
ATOM   2103 C  CA    . ILE B 2 312 ? -8.999  63.746 136.326 1.00 11.41 ? 312 ILE A CA    1 
ATOM   2104 C  C     . ILE B 2 312 ? -8.197  62.469 136.009 1.00 12.10 ? 312 ILE A C     1 
ATOM   2105 O  O     . ILE B 2 312 ? -7.346  62.533 135.098 1.00 13.49 ? 312 ILE A O     1 
ATOM   2106 C  CB    . ILE B 2 312 ? -9.985  64.104 135.184 1.00 9.68  ? 312 ILE A CB    1 
ATOM   2107 C  CG1   . ILE B 2 312 ? -10.953 65.223 135.620 1.00 10.18 ? 312 ILE A CG1   1 
ATOM   2108 C  CG2   . ILE B 2 312 ? -10.789 62.862 134.723 1.00 10.36 ? 312 ILE A CG2   1 
ATOM   2109 C  CD1   . ILE B 2 312 ? -11.473 66.113 134.464 1.00 10.97 ? 312 ILE A CD1   1 
ATOM   2110 N  N     . LEU B 2 313 ? -8.388  61.442 136.779 1.00 12.26 ? 313 LEU A N     1 
ATOM   2111 C  CA    . LEU B 2 313 ? -7.641  60.190 136.492 1.00 11.97 ? 313 LEU A CA    1 
ATOM   2112 C  C     . LEU B 2 313 ? -8.623  59.212 135.856 1.00 12.40 ? 313 LEU A C     1 
ATOM   2113 O  O     . LEU B 2 313 ? -9.526  58.671 136.538 1.00 14.13 ? 313 LEU A O     1 
ATOM   2114 C  CB    . LEU B 2 313 ? -6.923  59.732 137.754 1.00 10.47 ? 313 LEU A CB    1 
ATOM   2115 C  CG    . LEU B 2 313 ? -5.863  58.651 137.528 1.00 10.08 ? 313 LEU A CG    1 
ATOM   2116 C  CD1   . LEU B 2 313 ? -5.141  58.280 138.797 1.00 10.82 ? 313 LEU A CD1   1 
ATOM   2117 C  CD2   . LEU B 2 313 ? -6.589  57.445 136.919 1.00 9.45  ? 313 LEU A CD2   1 
ATOM   2118 N  N     . LYS B 2 314 ? -8.503  59.043 134.561 1.00 11.72 ? 314 LYS A N     1 
ATOM   2119 C  CA    . LYS B 2 314 ? -9.377  58.098 133.820 1.00 11.68 ? 314 LYS A CA    1 
ATOM   2120 C  C     . LYS B 2 314 ? -8.594  56.782 133.789 1.00 12.97 ? 314 LYS A C     1 
ATOM   2121 O  O     . LYS B 2 314 ? -7.345  56.814 133.764 1.00 14.59 ? 314 LYS A O     1 
ATOM   2122 C  CB    . LYS B 2 314 ? -9.617  58.557 132.404 1.00 9.93  ? 314 LYS A CB    1 
ATOM   2123 C  CG    . LYS B 2 314 ? -10.986 59.147 132.132 1.00 11.76 ? 314 LYS A CG    1 
ATOM   2124 C  CD    . LYS B 2 314 ? -11.821 58.108 131.382 1.00 11.38 ? 314 LYS A CD    1 
ATOM   2125 C  CE    . LYS B 2 314 ? -12.172 58.612 129.994 1.00 11.79 ? 314 LYS A CE    1 
ATOM   2126 N  NZ    . LYS B 2 314 ? -13.603 59.012 129.933 1.00 14.41 ? 314 LYS A NZ    1 
ATOM   2127 N  N     . THR B 2 315 ? -9.281  55.670 133.805 1.00 12.44 ? 315 THR A N     1 
ATOM   2128 C  CA    . THR B 2 315 ? -8.606  54.352 133.749 1.00 11.80 ? 315 THR A CA    1 
ATOM   2129 C  C     . THR B 2 315 ? -9.576  53.322 133.154 1.00 11.36 ? 315 THR A C     1 
ATOM   2130 O  O     . THR B 2 315 ? -10.673 53.097 133.693 1.00 11.68 ? 315 THR A O     1 
ATOM   2131 C  CB    . THR B 2 315 ? -8.033  53.910 135.125 1.00 10.87 ? 315 THR A CB    1 
ATOM   2132 O  OG1   . THR B 2 315 ? -7.214  52.762 134.964 1.00 13.71 ? 315 THR A OG1   1 
ATOM   2133 C  CG2   . THR B 2 315 ? -9.122  53.556 136.140 1.00 8.70  ? 315 THR A CG2   1 
ATOM   2134 N  N     . TRP B 2 316 ? -9.110  52.766 132.038 1.00 11.64 ? 316 TRP A N     1 
ATOM   2135 C  CA    . TRP B 2 316 ? -9.828  51.747 131.242 1.00 10.94 ? 316 TRP A CA    1 
ATOM   2136 C  C     . TRP B 2 316 ? -9.183  50.351 131.419 1.00 10.67 ? 316 TRP A C     1 
ATOM   2137 O  O     . TRP B 2 316 ? -7.966  50.228 131.611 1.00 10.25 ? 316 TRP A O     1 
ATOM   2138 C  CB    . TRP B 2 316 ? -9.715  52.033 129.726 1.00 9.56  ? 316 TRP A CB    1 
ATOM   2139 C  CG    . TRP B 2 316 ? -10.266 53.387 129.211 1.00 10.59 ? 316 TRP A CG    1 
ATOM   2140 C  CD1   . TRP B 2 316 ? -11.473 53.620 128.664 1.00 11.94 ? 316 TRP A CD1   1 
ATOM   2141 C  CD2   . TRP B 2 316 ? -9.560  54.627 129.210 1.00 10.84 ? 316 TRP A CD2   1 
ATOM   2142 N  NE1   . TRP B 2 316 ? -11.510 55.000 128.272 1.00 12.54 ? 316 TRP A NE1   1 
ATOM   2143 C  CE2   . TRP B 2 316 ? -10.373 55.567 128.585 1.00 11.80 ? 316 TRP A CE2   1 
ATOM   2144 C  CE3   . TRP B 2 316 ? -8.297  55.019 129.668 1.00 9.38  ? 316 TRP A CE3   1 
ATOM   2145 C  CZ2   . TRP B 2 316 ? -9.973  56.890 128.346 1.00 10.20 ? 316 TRP A CZ2   1 
ATOM   2146 C  CZ3   . TRP B 2 316 ? -7.913  56.359 129.445 1.00 9.65  ? 316 TRP A CZ3   1 
ATOM   2147 C  CH2   . TRP B 2 316 ? -8.711  57.248 128.811 1.00 9.28  ? 316 TRP A CH2   1 
ATOM   2148 N  N     . ALA B 2 317 ? -10.031 49.337 131.330 1.00 10.72 ? 317 ALA A N     1 
ATOM   2149 C  CA    . ALA B 2 317 ? -9.640  47.905 131.420 1.00 10.79 ? 317 ALA A CA    1 
ATOM   2150 C  C     . ALA B 2 317 ? -10.787 47.080 130.822 1.00 11.17 ? 317 ALA A C     1 
ATOM   2151 O  O     . ALA B 2 317 ? -11.863 47.091 131.423 1.00 11.25 ? 317 ALA A O     1 
ATOM   2152 C  CB    . ALA B 2 317 ? -9.408  47.512 132.880 1.00 9.20  ? 317 ALA A CB    1 
ATOM   2153 N  N     . CYS B 2 318 ? -10.491 46.479 129.688 1.00 10.77 ? 318 CYS A N     1 
ATOM   2154 C  CA    . CYS B 2 318 ? -11.492 45.668 128.982 1.00 10.25 ? 318 CYS A CA    1 
ATOM   2155 C  C     . CYS B 2 318 ? -11.128 44.200 129.222 1.00 10.45 ? 318 CYS A C     1 
ATOM   2156 O  O     . CYS B 2 318 ? -9.944  43.873 128.992 1.00 10.28 ? 318 CYS A O     1 
ATOM   2157 C  CB    . CYS B 2 318 ? -11.624 45.931 127.486 1.00 11.09 ? 318 CYS A CB    1 
ATOM   2158 S  SG    . CYS B 2 318 ? -12.657 44.626 126.684 1.00 15.04 ? 318 CYS A SG    1 
ATOM   2159 N  N     . LEU B 2 319 ? -12.118 43.450 129.645 1.00 10.43 ? 319 LEU A N     1 
ATOM   2160 C  CA    . LEU B 2 319 ? -11.894 42.045 129.942 1.00 11.62 ? 319 LEU A CA    1 
ATOM   2161 C  C     . LEU B 2 319 ? -12.929 41.102 129.333 1.00 13.87 ? 319 LEU A C     1 
ATOM   2162 O  O     . LEU B 2 319 ? -14.077 41.456 129.014 1.00 15.83 ? 319 LEU A O     1 
ATOM   2163 C  CB    . LEU B 2 319 ? -12.008 41.881 131.478 1.00 7.55  ? 319 LEU A CB    1 
ATOM   2164 C  CG    . LEU B 2 319 ? -10.969 42.488 132.378 1.00 5.62  ? 319 LEU A CG    1 
ATOM   2165 C  CD1   . LEU B 2 319 ? -11.331 43.930 132.703 1.00 3.48  ? 319 LEU A CD1   1 
ATOM   2166 C  CD2   . LEU B 2 319 ? -10.918 41.676 133.689 1.00 5.99  ? 319 LEU A CD2   1 
ATOM   2167 N  N     . GLU B 2 320 ? -12.449 39.861 129.313 1.00 14.54 ? 320 GLU A N     1 
ATOM   2168 C  CA    . GLU B 2 320 ? -13.343 38.758 128.881 1.00 13.47 ? 320 GLU A CA    1 
ATOM   2169 C  C     . GLU B 2 320 ? -13.423 37.854 130.118 1.00 13.36 ? 320 GLU A C     1 
ATOM   2170 O  O     . GLU B 2 320 ? -12.301 37.496 130.534 1.00 15.85 ? 320 GLU A O     1 
ATOM   2171 C  CB    . GLU B 2 320 ? -12.767 37.944 127.787 1.00 9.76  ? 320 GLU A CB    1 
ATOM   2172 C  CG    . GLU B 2 320 ? -13.155 38.330 126.341 1.00 8.52  ? 320 GLU A CG    1 
ATOM   2173 C  CD    . GLU B 2 320 ? -12.572 37.241 125.454 1.00 8.33  ? 320 GLU A CD    1 
ATOM   2174 O  OE1   . GLU B 2 320 ? -11.821 36.424 126.003 1.00 7.71  ? 320 GLU A OE1   1 
ATOM   2175 O  OE2   . GLU B 2 320 ? -12.941 37.273 124.291 1.00 8.06  ? 320 GLU A OE2   1 
ATOM   2176 N  N     . TYR B 2 321 ? -14.603 37.646 130.640 1.00 11.67 ? 321 TYR A N     1 
ATOM   2177 C  CA    . TYR B 2 321 ? -14.783 36.790 131.817 1.00 10.33 ? 321 TYR A CA    1 
ATOM   2178 C  C     . TYR B 2 321 ? -15.514 35.514 131.372 1.00 10.38 ? 321 TYR A C     1 
ATOM   2179 O  O     . TYR B 2 321 ? -16.103 35.463 130.309 1.00 9.63  ? 321 TYR A O     1 
ATOM   2180 C  CB    . TYR B 2 321 ? -15.663 37.405 132.887 1.00 9.69  ? 321 TYR A CB    1 
ATOM   2181 C  CG    . TYR B 2 321 ? -15.108 38.510 133.713 1.00 8.63  ? 321 TYR A CG    1 
ATOM   2182 C  CD1   . TYR B 2 321 ? -14.307 38.267 134.820 1.00 7.15  ? 321 TYR A CD1   1 
ATOM   2183 C  CD2   . TYR B 2 321 ? -15.430 39.842 133.386 1.00 7.34  ? 321 TYR A CD2   1 
ATOM   2184 C  CE1   . TYR B 2 321 ? -13.798 39.320 135.585 1.00 7.33  ? 321 TYR A CE1   1 
ATOM   2185 C  CE2   . TYR B 2 321 ? -14.926 40.890 134.139 1.00 9.38  ? 321 TYR A CE2   1 
ATOM   2186 C  CZ    . TYR B 2 321 ? -14.101 40.621 135.233 1.00 9.49  ? 321 TYR A CZ    1 
ATOM   2187 O  OH    . TYR B 2 321 ? -13.623 41.660 135.993 1.00 10.35 ? 321 TYR A OH    1 
ATOM   2188 N  N     . ARG B 2 322 ? -15.498 34.547 132.250 1.00 11.02 ? 322 ARG A N     1 
ATOM   2189 C  CA    . ARG B 2 322 ? -16.258 33.289 132.001 1.00 11.56 ? 322 ARG A CA    1 
ATOM   2190 C  C     . ARG B 2 322 ? -17.444 33.371 132.961 1.00 11.46 ? 322 ARG A C     1 
ATOM   2191 O  O     . ARG B 2 322 ? -17.225 33.264 134.174 1.00 12.61 ? 322 ARG A O     1 
ATOM   2192 C  CB    . ARG B 2 322 ? -15.409 32.052 132.236 1.00 11.55 ? 322 ARG A CB    1 
ATOM   2193 C  CG    . ARG B 2 322 ? -14.407 31.864 131.110 1.00 10.72 ? 322 ARG A CG    1 
ATOM   2194 C  CD    . ARG B 2 322 ? -15.073 31.333 129.857 1.00 8.07  ? 322 ARG A CD    1 
ATOM   2195 N  NE    . ARG B 2 322 ? -14.805 29.886 129.800 1.00 6.01  ? 322 ARG A NE    1 
ATOM   2196 C  CZ    . ARG B 2 322 ? -15.757 28.978 129.614 1.00 7.11  ? 322 ARG A CZ    1 
ATOM   2197 N  NH1   . ARG B 2 322 ? -16.978 29.392 129.313 1.00 8.39  ? 322 ARG A NH1   1 
ATOM   2198 N  NH2   . ARG B 2 322 ? -15.466 27.698 129.704 1.00 7.67  ? 322 ARG A NH2   1 
ATOM   2199 N  N     . PRO B 2 323 ? -18.598 33.664 132.422 1.00 11.01 ? 323 PRO A N     1 
ATOM   2200 C  CA    . PRO B 2 323 ? -19.812 33.809 133.229 1.00 10.74 ? 323 PRO A CA    1 
ATOM   2201 C  C     . PRO B 2 323 ? -20.311 32.445 133.664 1.00 10.60 ? 323 PRO A C     1 
ATOM   2202 O  O     . PRO B 2 323 ? -20.266 31.503 132.849 1.00 11.59 ? 323 PRO A O     1 
ATOM   2203 C  CB    . PRO B 2 323 ? -20.776 34.501 132.272 1.00 11.06 ? 323 PRO A CB    1 
ATOM   2204 C  CG    . PRO B 2 323 ? -20.383 33.968 130.922 1.00 11.19 ? 323 PRO A CG    1 
ATOM   2205 C  CD    . PRO B 2 323 ? -18.868 33.831 130.991 1.00 11.04 ? 323 PRO A CD    1 
ATOM   2206 N  N     . ASN B 2 324 ? -20.726 32.343 134.890 1.00 10.00 ? 324 ASN A N     1 
ATOM   2207 C  CA    . ASN B 2 324 ? -21.289 31.124 135.503 1.00 9.68  ? 324 ASN A CA    1 
ATOM   2208 C  C     . ASN B 2 324 ? -22.789 31.102 135.180 1.00 9.45  ? 324 ASN A C     1 
ATOM   2209 O  O     . ASN B 2 324 ? -23.516 32.106 135.314 1.00 8.72  ? 324 ASN A O     1 
ATOM   2210 C  CB    . ASN B 2 324 ? -20.993 31.220 137.003 1.00 11.26 ? 324 ASN A CB    1 
ATOM   2211 C  CG    . ASN B 2 324 ? -19.702 30.533 137.410 1.00 12.82 ? 324 ASN A CG    1 
ATOM   2212 O  OD1   . ASN B 2 324 ? -18.900 31.131 138.151 1.00 12.53 ? 324 ASN A OD1   1 
ATOM   2213 N  ND2   . ASN B 2 324 ? -19.527 29.282 136.948 1.00 14.07 ? 324 ASN A ND2   1 
ATOM   2214 N  N     . PRO B 2 325 ? -23.269 29.956 134.742 1.00 9.26  ? 325 PRO A N     1 
ATOM   2215 C  CA    . PRO B 2 325 ? -24.682 29.776 134.354 1.00 9.12  ? 325 PRO A CA    1 
ATOM   2216 C  C     . PRO B 2 325 ? -25.694 30.297 135.355 1.00 9.62  ? 325 PRO A C     1 
ATOM   2217 O  O     . PRO B 2 325 ? -26.830 30.669 134.958 1.00 8.88  ? 325 PRO A O     1 
ATOM   2218 C  CB    . PRO B 2 325 ? -24.847 28.297 134.024 1.00 9.18  ? 325 PRO A CB    1 
ATOM   2219 C  CG    . PRO B 2 325 ? -23.470 27.747 133.887 1.00 9.03  ? 325 PRO A CG    1 
ATOM   2220 C  CD    . PRO B 2 325 ? -22.488 28.721 134.537 1.00 9.22  ? 325 PRO A CD    1 
ATOM   2221 N  N     . ASN B 2 326 ? -25.338 30.368 136.626 1.00 10.01 ? 326 ASN A N     1 
ATOM   2222 C  CA    . ASN B 2 326 ? -26.240 30.871 137.666 1.00 10.84 ? 326 ASN A CA    1 
ATOM   2223 C  C     . ASN B 2 326 ? -26.180 32.394 137.752 1.00 11.90 ? 326 ASN A C     1 
ATOM   2224 O  O     . ASN B 2 326 ? -27.090 33.002 138.358 1.00 13.47 ? 326 ASN A O     1 
ATOM   2225 C  CB    . ASN B 2 326 ? -25.839 30.274 139.034 1.00 11.73 ? 326 ASN A CB    1 
ATOM   2226 C  CG    . ASN B 2 326 ? -24.439 30.755 139.396 1.00 14.80 ? 326 ASN A CG    1 
ATOM   2227 O  OD1   . ASN B 2 326 ? -24.208 31.448 140.383 1.00 19.00 ? 326 ASN A OD1   1 
ATOM   2228 N  ND2   . ASN B 2 326 ? -23.472 30.411 138.548 1.00 14.19 ? 326 ASN A ND2   1 
ATOM   2229 N  N     . ALA B 2 327 ? -25.126 32.995 137.226 1.00 11.22 ? 327 ALA A N     1 
ATOM   2230 C  CA    . ALA B 2 327 ? -24.989 34.477 137.305 1.00 11.67 ? 327 ALA A CA    1 
ATOM   2231 C  C     . ALA B 2 327 ? -26.030 35.191 136.473 1.00 13.06 ? 327 ALA A C     1 
ATOM   2232 O  O     . ALA B 2 327 ? -26.532 34.603 135.496 1.00 14.68 ? 327 ALA A O     1 
ATOM   2233 C  CB    . ALA B 2 327 ? -23.569 34.851 136.951 1.00 8.39  ? 327 ALA A CB    1 
ATOM   2234 N  N     . MET B 2 328 ? -26.381 36.423 136.805 1.00 12.50 ? 328 MET A N     1 
ATOM   2235 C  CA    . MET B 2 328 ? -27.389 37.212 136.082 1.00 13.32 ? 328 MET A CA    1 
ATOM   2236 C  C     . MET B 2 328 ? -26.816 38.032 134.932 1.00 13.55 ? 328 MET A C     1 
ATOM   2237 O  O     . MET B 2 328 ? -27.619 38.572 134.152 1.00 14.49 ? 328 MET A O     1 
ATOM   2238 C  CB    . MET B 2 328 ? -28.211 38.110 137.003 1.00 14.12 ? 328 MET A CB    1 
ATOM   2239 C  CG    . MET B 2 328 ? -29.154 37.250 137.830 1.00 18.45 ? 328 MET A CG    1 
ATOM   2240 S  SD    . MET B 2 328 ? -30.455 36.608 136.674 1.00 24.29 ? 328 MET A SD    1 
ATOM   2241 C  CE    . MET B 2 328 ? -30.410 34.884 137.273 1.00 20.05 ? 328 MET A CE    1 
ATOM   2242 N  N     . LEU B 2 329 ? -25.513 38.104 134.862 1.00 12.62 ? 329 LEU A N     1 
ATOM   2243 C  CA    . LEU B 2 329 ? -24.755 38.819 133.823 1.00 11.96 ? 329 LEU A CA    1 
ATOM   2244 C  C     . LEU B 2 329 ? -24.558 37.864 132.630 1.00 12.29 ? 329 LEU A C     1 
ATOM   2245 O  O     . LEU B 2 329 ? -24.150 38.232 131.525 1.00 13.87 ? 329 LEU A O     1 
ATOM   2246 C  CB    . LEU B 2 329 ? -23.490 39.403 134.416 1.00 10.83 ? 329 LEU A CB    1 
ATOM   2247 C  CG    . LEU B 2 329 ? -22.172 38.697 134.581 1.00 10.45 ? 329 LEU A CG    1 
ATOM   2248 C  CD1   . LEU B 2 329 ? -21.579 38.932 135.971 1.00 9.09  ? 329 LEU A CD1   1 
ATOM   2249 C  CD2   . LEU B 2 329 ? -22.291 37.200 134.341 1.00 11.45 ? 329 LEU A CD2   1 
ATOM   2250 N  N     . TYR B 2 330 ? -24.897 36.618 132.862 1.00 11.27 ? 330 TYR A N     1 
ATOM   2251 C  CA    . TYR B 2 330 ? -24.781 35.572 131.880 1.00 10.58 ? 330 TYR A CA    1 
ATOM   2252 C  C     . TYR B 2 330 ? -25.481 35.853 130.572 1.00 10.84 ? 330 TYR A C     1 
ATOM   2253 O  O     . TYR B 2 330 ? -24.930 35.590 129.474 1.00 12.40 ? 330 TYR A O     1 
ATOM   2254 C  CB    . TYR B 2 330 ? -25.327 34.239 132.498 1.00 10.93 ? 330 TYR A CB    1 
ATOM   2255 C  CG    . TYR B 2 330 ? -24.939 33.095 131.573 1.00 8.89  ? 330 TYR A CG    1 
ATOM   2256 C  CD1   . TYR B 2 330 ? -25.752 32.788 130.487 1.00 6.21  ? 330 TYR A CD1   1 
ATOM   2257 C  CD2   . TYR B 2 330 ? -23.750 32.402 131.753 1.00 8.34  ? 330 TYR A CD2   1 
ATOM   2258 C  CE1   . TYR B 2 330 ? -25.405 31.782 129.596 1.00 8.85  ? 330 TYR A CE1   1 
ATOM   2259 C  CE2   . TYR B 2 330 ? -23.406 31.389 130.848 1.00 9.45  ? 330 TYR A CE2   1 
ATOM   2260 C  CZ    . TYR B 2 330 ? -24.232 31.081 129.767 1.00 10.28 ? 330 TYR A CZ    1 
ATOM   2261 O  OH    . TYR B 2 330 ? -23.917 30.093 128.891 1.00 8.96  ? 330 TYR A OH    1 
ATOM   2262 N  N     . GLN B 2 331 ? -26.705 36.328 130.638 1.00 10.34 ? 331 GLN A N     1 
ATOM   2263 C  CA    . GLN B 2 331 ? -27.546 36.639 129.467 1.00 10.44 ? 331 GLN A CA    1 
ATOM   2264 C  C     . GLN B 2 331 ? -26.990 37.788 128.642 1.00 9.96  ? 331 GLN A C     1 
ATOM   2265 O  O     . GLN B 2 331 ? -27.584 38.196 127.620 1.00 9.74  ? 331 GLN A O     1 
ATOM   2266 C  CB    . GLN B 2 331 ? -29.001 37.005 129.826 1.00 10.98 ? 331 GLN A CB    1 
ATOM   2267 C  CG    . GLN B 2 331 ? -29.146 37.382 131.294 1.00 12.08 ? 331 GLN A CG    1 
ATOM   2268 C  CD    . GLN B 2 331 ? -29.277 36.094 132.087 1.00 12.83 ? 331 GLN A CD    1 
ATOM   2269 O  OE1   . GLN B 2 331 ? -29.850 35.964 133.157 1.00 10.51 ? 331 GLN A OE1   1 
ATOM   2270 N  NE2   . GLN B 2 331 ? -28.707 35.065 131.451 1.00 16.10 ? 331 GLN A NE2   1 
ATOM   2271 N  N     . PHE B 2 332 ? -25.882 38.342 129.055 1.00 10.05 ? 332 PHE A N     1 
ATOM   2272 C  CA    . PHE B 2 332 ? -25.307 39.467 128.281 1.00 11.07 ? 332 PHE A CA    1 
ATOM   2273 C  C     . PHE B 2 332 ? -24.100 38.918 127.522 1.00 12.56 ? 332 PHE A C     1 
ATOM   2274 O  O     . PHE B 2 332 ? -23.571 39.650 126.690 1.00 14.13 ? 332 PHE A O     1 
ATOM   2275 C  CB    . PHE B 2 332 ? -24.929 40.627 129.156 1.00 9.06  ? 332 PHE A CB    1 
ATOM   2276 C  CG    . PHE B 2 332 ? -25.915 41.280 130.050 1.00 9.38  ? 332 PHE A CG    1 
ATOM   2277 C  CD1   . PHE B 2 332 ? -27.074 41.853 129.538 1.00 10.85 ? 332 PHE A CD1   1 
ATOM   2278 C  CD2   . PHE B 2 332 ? -25.653 41.373 131.413 1.00 9.72  ? 332 PHE A CD2   1 
ATOM   2279 C  CE1   . PHE B 2 332 ? -27.982 42.509 130.380 1.00 11.30 ? 332 PHE A CE1   1 
ATOM   2280 C  CE2   . PHE B 2 332 ? -26.534 42.011 132.270 1.00 9.84  ? 332 PHE A CE2   1 
ATOM   2281 C  CZ    . PHE B 2 332 ? -27.706 42.573 131.762 1.00 10.17 ? 332 PHE A CZ    1 
ATOM   2282 N  N     . GLY B 2 333 ? -23.689 37.713 127.819 1.00 12.50 ? 333 GLY A N     1 
ATOM   2283 C  CA    . GLY B 2 333 ? -22.508 37.085 127.223 1.00 13.87 ? 333 GLY A CA    1 
ATOM   2284 C  C     . GLY B 2 333 ? -22.694 36.850 125.688 1.00 14.64 ? 333 GLY A C     1 
ATOM   2285 O  O     . GLY B 2 333 ? -23.799 36.992 125.150 1.00 17.40 ? 333 GLY A O     1 
ATOM   2286 N  N     . HIS B 2 334 ? -21.568 36.510 125.040 1.00 13.53 ? 334 HIS A N     1 
ATOM   2287 C  CA    . HIS B 2 334 ? -21.461 36.152 123.582 1.00 12.35 ? 334 HIS A CA    1 
ATOM   2288 C  C     . HIS B 2 334 ? -20.261 35.171 123.450 1.00 11.07 ? 334 HIS A C     1 
ATOM   2289 O  O     . HIS B 2 334 ? -19.694 34.717 124.442 1.00 10.76 ? 334 HIS A O     1 
ATOM   2290 C  CB    . HIS B 2 334 ? -21.264 37.415 122.723 1.00 13.33 ? 334 HIS A CB    1 
ATOM   2291 C  CG    . HIS B 2 334 ? -20.134 38.295 123.234 1.00 11.77 ? 334 HIS A CG    1 
ATOM   2292 N  ND1   . HIS B 2 334 ? -18.836 38.167 122.758 1.00 12.75 ? 334 HIS A ND1   1 
ATOM   2293 C  CD2   . HIS B 2 334 ? -20.112 39.284 124.161 1.00 10.53 ? 334 HIS A CD2   1 
ATOM   2294 C  CE1   . HIS B 2 334 ? -18.082 39.044 123.392 1.00 13.96 ? 334 HIS A CE1   1 
ATOM   2295 N  NE2   . HIS B 2 334 ? -18.827 39.717 124.235 1.00 13.75 ? 334 HIS A NE2   1 
ATOM   2296 N  N     . ASP B 2 335 ? -19.842 34.799 122.244 1.00 9.91  ? 335 ASP A N     1 
ATOM   2297 C  CA    . ASP B 2 335 ? -18.678 33.859 122.075 1.00 10.02 ? 335 ASP A CA    1 
ATOM   2298 C  C     . ASP B 2 335 ? -17.424 34.672 121.869 1.00 9.88  ? 335 ASP A C     1 
ATOM   2299 O  O     . ASP B 2 335 ? -17.640 35.774 121.304 1.00 10.56 ? 335 ASP A O     1 
ATOM   2300 C  CB    . ASP B 2 335 ? -18.923 32.948 120.874 1.00 11.42 ? 335 ASP A CB    1 
ATOM   2301 C  CG    . ASP B 2 335 ? -20.259 32.207 120.957 1.00 12.05 ? 335 ASP A CG    1 
ATOM   2302 O  OD1   . ASP B 2 335 ? -20.749 31.887 122.107 1.00 11.94 ? 335 ASP A OD1   1 
ATOM   2303 O  OD2   . ASP B 2 335 ? -20.893 31.905 119.877 1.00 13.16 ? 335 ASP A OD2   1 
ATOM   2304 N  N     . SER B 2 336 ? -16.264 34.168 122.271 1.00 9.66  ? 336 SER A N     1 
ATOM   2305 C  CA    . SER B 2 336 ? -15.040 35.009 121.999 1.00 10.52 ? 336 SER A CA    1 
ATOM   2306 C  C     . SER B 2 336 ? -14.933 34.996 120.458 1.00 11.48 ? 336 SER A C     1 
ATOM   2307 O  O     . SER B 2 336 ? -15.293 33.954 119.853 1.00 13.27 ? 336 SER A O     1 
ATOM   2308 C  CB    . SER B 2 336 ? -13.763 34.525 122.635 1.00 8.02  ? 336 SER A CB    1 
ATOM   2309 N  N     . PRO B 2 337 ? -14.526 36.105 119.890 1.00 10.75 ? 337 PRO A N     1 
ATOM   2310 C  CA    . PRO B 2 337 ? -14.353 36.188 118.428 1.00 10.31 ? 337 PRO A CA    1 
ATOM   2311 C  C     . PRO B 2 337 ? -13.245 35.202 118.044 1.00 9.76  ? 337 PRO A C     1 
ATOM   2312 O  O     . PRO B 2 337 ? -12.337 34.925 118.857 1.00 10.08 ? 337 PRO A O     1 
ATOM   2313 C  CB    . PRO B 2 337 ? -13.989 37.642 118.191 1.00 10.64 ? 337 PRO A CB    1 
ATOM   2314 C  CG    . PRO B 2 337 ? -13.315 38.063 119.472 1.00 10.42 ? 337 PRO A CG    1 
ATOM   2315 C  CD    . PRO B 2 337 ? -14.103 37.344 120.570 1.00 10.70 ? 337 PRO A CD    1 
ATOM   2316 N  N     . PRO B 2 338 ? -13.349 34.665 116.848 1.00 8.88  ? 338 PRO A N     1 
ATOM   2317 C  CA    . PRO B 2 338 ? -12.432 33.671 116.283 1.00 8.09  ? 338 PRO A CA    1 
ATOM   2318 C  C     . PRO B 2 338 ? -11.070 34.225 115.888 1.00 7.66  ? 338 PRO A C     1 
ATOM   2319 O  O     . PRO B 2 338 ? -10.971 35.440 115.649 1.00 7.73  ? 338 PRO A O     1 
ATOM   2320 C  CB    . PRO B 2 338 ? -13.184 33.181 115.038 1.00 7.99  ? 338 PRO A CB    1 
ATOM   2321 C  CG    . PRO B 2 338 ? -13.863 34.477 114.592 1.00 8.42  ? 338 PRO A CG    1 
ATOM   2322 C  CD    . PRO B 2 338 ? -14.454 34.975 115.904 1.00 8.37  ? 338 PRO A CD    1 
ATOM   2323 N  N     . CYS B 2 339 ? -10.090 33.337 115.798 1.00 7.83  ? 339 CYS A N     1 
ATOM   2324 C  CA    . CYS B 2 339 ? -8.708  33.662 115.462 1.00 7.95  ? 339 CYS A CA    1 
ATOM   2325 C  C     . CYS B 2 339 ? -8.618  34.659 114.313 1.00 7.72  ? 339 CYS A C     1 
ATOM   2326 O  O     . CYS B 2 339 ? -9.294  34.458 113.293 1.00 8.60  ? 339 CYS A O     1 
ATOM   2327 C  CB    . CYS B 2 339 ? -7.845  32.446 115.090 1.00 8.36  ? 339 CYS A CB    1 
ATOM   2328 S  SG    . CYS B 2 339 ? -6.047  32.677 115.371 1.00 12.33 ? 339 CYS A SG    1 
ATOM   2329 N  N     . ASP B 2 340 ? -7.783  35.653 114.527 1.00 7.83  ? 340 ASP A N     1 
ATOM   2330 C  CA    . ASP B 2 340 ? -7.494  36.730 113.573 1.00 8.59  ? 340 ASP A CA    1 
ATOM   2331 C  C     . ASP B 2 340 ? -5.960  36.882 113.607 1.00 9.85  ? 340 ASP A C     1 
ATOM   2332 O  O     . ASP B 2 340 ? -5.487  37.809 114.278 1.00 11.26 ? 340 ASP A O     1 
ATOM   2333 C  CB    . ASP B 2 340 ? -8.216  38.041 113.854 1.00 8.10  ? 340 ASP A CB    1 
ATOM   2334 C  CG    . ASP B 2 340 ? -8.020  39.109 112.800 1.00 10.10 ? 340 ASP A CG    1 
ATOM   2335 O  OD1   . ASP B 2 340 ? -6.965  39.059 112.107 1.00 8.38  ? 340 ASP A OD1   1 
ATOM   2336 O  OD2   . ASP B 2 340 ? -8.853  40.005 112.577 1.00 12.03 ? 340 ASP A OD2   1 
ATOM   2337 N  N     . GLU B 2 341 ? -5.287  35.996 112.909 1.00 9.66  ? 341 GLU A N     1 
ATOM   2338 C  CA    . GLU B 2 341 ? -3.832  35.993 112.863 1.00 9.77  ? 341 GLU A CA    1 
ATOM   2339 C  C     . GLU B 2 341 ? -3.234  37.377 112.671 1.00 9.34  ? 341 GLU A C     1 
ATOM   2340 O  O     . GLU B 2 341 ? -2.224  37.628 113.363 1.00 9.19  ? 341 GLU A O     1 
ATOM   2341 C  CB    . GLU B 2 341 ? -3.240  35.137 111.750 1.00 14.04 ? 341 GLU A CB    1 
ATOM   2342 C  CG    . GLU B 2 341 ? -2.551  33.838 112.137 1.00 19.33 ? 341 GLU A CG    1 
ATOM   2343 C  CD    . GLU B 2 341 ? -1.428  33.907 113.126 1.00 23.83 ? 341 GLU A CD    1 
ATOM   2344 O  OE1   . GLU B 2 341 ? -0.387  34.428 112.633 1.00 26.03 ? 341 GLU A OE1   1 
ATOM   2345 O  OE2   . GLU B 2 341 ? -1.496  33.472 114.270 1.00 26.06 ? 341 GLU A OE2   1 
ATOM   2346 N  N     . VAL B 2 342 ? -3.816  38.153 111.784 1.00 8.24  ? 342 VAL A N     1 
ATOM   2347 C  CA    . VAL B 2 342 ? -3.313  39.503 111.503 1.00 7.84  ? 342 VAL A CA    1 
ATOM   2348 C  C     . VAL B 2 342 ? -3.473  40.384 112.735 1.00 8.11  ? 342 VAL A C     1 
ATOM   2349 O  O     . VAL B 2 342 ? -2.550  41.085 113.170 1.00 7.89  ? 342 VAL A O     1 
ATOM   2350 C  CB    . VAL B 2 342 ? -3.976  40.118 110.257 1.00 8.06  ? 342 VAL A CB    1 
ATOM   2351 C  CG1   . VAL B 2 342 ? -3.666  41.612 110.138 1.00 6.91  ? 342 VAL A CG1   1 
ATOM   2352 C  CG2   . VAL B 2 342 ? -3.577  39.401 108.987 1.00 8.87  ? 342 VAL A CG2   1 
ATOM   2353 N  N     . ALA B 2 343 ? -4.682  40.355 113.287 1.00 9.11  ? 343 ALA A N     1 
ATOM   2354 C  CA    . ALA B 2 343 ? -4.923  41.222 114.481 1.00 9.78  ? 343 ALA A CA    1 
ATOM   2355 C  C     . ALA B 2 343 ? -3.899  40.882 115.548 1.00 10.79 ? 343 ALA A C     1 
ATOM   2356 O  O     . ALA B 2 343 ? -3.213  41.752 116.111 1.00 11.94 ? 343 ALA A O     1 
ATOM   2357 C  CB    . ALA B 2 343 ? -6.374  41.191 114.848 1.00 7.03  ? 343 ALA A CB    1 
ATOM   2358 N  N     . LEU B 2 344 ? -3.705  39.609 115.829 1.00 10.37 ? 344 LEU A N     1 
ATOM   2359 C  CA    . LEU B 2 344 ? -2.750  39.103 116.800 1.00 10.38 ? 344 LEU A CA    1 
ATOM   2360 C  C     . LEU B 2 344 ? -1.311  39.536 116.524 1.00 11.28 ? 344 LEU A C     1 
ATOM   2361 O  O     . LEU B 2 344 ? -0.549  39.905 117.457 1.00 12.28 ? 344 LEU A O     1 
ATOM   2362 C  CB    . LEU B 2 344 ? -2.968  37.570 116.840 1.00 9.45  ? 344 LEU A CB    1 
ATOM   2363 C  CG    . LEU B 2 344 ? -4.181  37.073 117.610 1.00 8.17  ? 344 LEU A CG    1 
ATOM   2364 C  CD1   . LEU B 2 344 ? -4.269  35.560 117.532 1.00 7.54  ? 344 LEU A CD1   1 
ATOM   2365 C  CD2   . LEU B 2 344 ? -4.077  37.513 119.067 1.00 5.02  ? 344 LEU A CD2   1 
ATOM   2366 N  N     . GLN B 2 345 ? -0.882  39.459 115.281 1.00 11.04 ? 345 GLN A N     1 
ATOM   2367 C  CA    . GLN B 2 345 ? 0.475   39.798 114.865 1.00 10.28 ? 345 GLN A CA    1 
ATOM   2368 C  C     . GLN B 2 345 ? 0.771   41.277 115.041 1.00 10.20 ? 345 GLN A C     1 
ATOM   2369 O  O     . GLN B 2 345 ? 1.769   41.643 115.660 1.00 10.08 ? 345 GLN A O     1 
ATOM   2370 C  CB    . GLN B 2 345 ? 0.731   39.413 113.408 1.00 12.13 ? 345 GLN A CB    1 
ATOM   2371 C  CG    . GLN B 2 345 ? 2.203   39.180 113.127 1.00 15.88 ? 345 GLN A CG    1 
ATOM   2372 C  CD    . GLN B 2 345 ? 3.016   38.721 114.328 1.00 17.47 ? 345 GLN A CD    1 
ATOM   2373 O  OE1   . GLN B 2 345 ? 2.935   37.571 114.807 1.00 18.91 ? 345 GLN A OE1   1 
ATOM   2374 N  NE2   . GLN B 2 345 ? 3.849   39.663 114.801 1.00 17.57 ? 345 GLN A NE2   1 
ATOM   2375 N  N     . GLU B 2 346 ? -0.095  42.092 114.491 1.00 10.03 ? 346 GLU A N     1 
ATOM   2376 C  CA    . GLU B 2 346 ? -0.028  43.544 114.538 1.00 9.96  ? 346 GLU A CA    1 
ATOM   2377 C  C     . GLU B 2 346 ? -0.163  44.067 115.952 1.00 9.89  ? 346 GLU A C     1 
ATOM   2378 O  O     . GLU B 2 346 ? 0.315   45.181 116.245 1.00 11.14 ? 346 GLU A O     1 
ATOM   2379 C  CB    . GLU B 2 346 ? -1.126  44.214 113.699 1.00 10.69 ? 346 GLU A CB    1 
ATOM   2380 C  CG    . GLU B 2 346 ? -1.157  43.847 112.219 1.00 14.81 ? 346 GLU A CG    1 
ATOM   2381 C  CD    . GLU B 2 346 ? 0.029   44.268 111.390 1.00 20.13 ? 346 GLU A CD    1 
ATOM   2382 O  OE1   . GLU B 2 346 ? 0.541   45.347 111.836 1.00 20.68 ? 346 GLU A OE1   1 
ATOM   2383 O  OE2   . GLU B 2 346 ? 0.475   43.677 110.396 1.00 22.09 ? 346 GLU A OE2   1 
ATOM   2384 N  N     . TYR B 2 347 ? -0.798  43.288 116.816 1.00 9.05  ? 347 TYR A N     1 
ATOM   2385 C  CA    . TYR B 2 347 ? -1.022  43.681 118.222 1.00 8.77  ? 347 TYR A CA    1 
ATOM   2386 C  C     . TYR B 2 347 ? 0.345   43.837 118.885 1.00 9.65  ? 347 TYR A C     1 
ATOM   2387 O  O     . TYR B 2 347 ? 0.566   44.806 119.611 1.00 9.47  ? 347 TYR A O     1 
ATOM   2388 C  CB    . TYR B 2 347 ? -1.925  42.718 118.979 1.00 6.44  ? 347 TYR A CB    1 
ATOM   2389 C  CG    . TYR B 2 347 ? -1.942  42.862 120.478 1.00 6.95  ? 347 TYR A CG    1 
ATOM   2390 C  CD1   . TYR B 2 347 ? -2.851  43.723 121.101 1.00 7.39  ? 347 TYR A CD1   1 
ATOM   2391 C  CD2   . TYR B 2 347 ? -1.065  42.168 121.304 1.00 8.88  ? 347 TYR A CD2   1 
ATOM   2392 C  CE1   . TYR B 2 347 ? -2.903  43.870 122.485 1.00 8.31  ? 347 TYR A CE1   1 
ATOM   2393 C  CE2   . TYR B 2 347 ? -1.084  42.305 122.692 1.00 8.99  ? 347 TYR A CE2   1 
ATOM   2394 C  CZ    . TYR B 2 347 ? -2.012  43.148 123.277 1.00 9.03  ? 347 TYR A CZ    1 
ATOM   2395 O  OH    . TYR B 2 347 ? -2.039  43.279 124.643 1.00 10.16 ? 347 TYR A OH    1 
ATOM   2396 N  N     . ARG B 2 348 ? 1.202   42.882 118.553 1.00 10.25 ? 348 ARG A N     1 
ATOM   2397 C  CA    . ARG B 2 348 ? 2.566   42.818 119.054 1.00 10.50 ? 348 ARG A CA    1 
ATOM   2398 C  C     . ARG B 2 348 ? 3.474   43.898 118.475 1.00 11.83 ? 348 ARG A C     1 
ATOM   2399 O  O     . ARG B 2 348 ? 4.339   44.456 119.191 1.00 12.78 ? 348 ARG A O     1 
ATOM   2400 C  CB    . ARG B 2 348 ? 3.172   41.454 118.696 1.00 8.09  ? 348 ARG A CB    1 
ATOM   2401 C  CG    . ARG B 2 348 ? 3.122   40.367 119.722 1.00 7.97  ? 348 ARG A CG    1 
ATOM   2402 C  CD    . ARG B 2 348 ? 2.038   40.474 120.730 1.00 9.46  ? 348 ARG A CD    1 
ATOM   2403 N  NE    . ARG B 2 348 ? 2.524   40.218 122.088 1.00 9.94  ? 348 ARG A NE    1 
ATOM   2404 C  CZ    . ARG B 2 348 ? 1.872   39.434 122.944 1.00 8.98  ? 348 ARG A CZ    1 
ATOM   2405 N  NH1   . ARG B 2 348 ? 0.757   38.807 122.593 1.00 9.67  ? 348 ARG A NH1   1 
ATOM   2406 N  NH2   . ARG B 2 348 ? 2.330   39.221 124.173 1.00 8.33  ? 348 ARG A NH2   1 
ATOM   2407 N  N     . THR B 2 349 ? 3.305   44.173 117.173 1.00 11.50 ? 349 THR A N     1 
ATOM   2408 C  CA    . THR B 2 349 ? 4.234   45.146 116.553 1.00 11.23 ? 349 THR A CA    1 
ATOM   2409 C  C     . THR B 2 349 ? 3.818   46.568 116.844 1.00 10.95 ? 349 THR A C     1 
ATOM   2410 O  O     . THR B 2 349 ? 4.717   47.435 116.973 1.00 11.39 ? 349 THR A O     1 
ATOM   2411 C  CB    . THR B 2 349 ? 4.588   44.840 115.059 1.00 10.69 ? 349 THR A CB    1 
ATOM   2412 O  OG1   . THR B 2 349 ? 3.948   45.850 114.244 1.00 10.92 ? 349 THR A OG1   1 
ATOM   2413 C  CG2   . THR B 2 349 ? 4.156   43.448 114.602 1.00 9.98  ? 349 THR A CG2   1 
ATOM   2414 N  N     . VAL B 2 350 ? 2.510   46.739 116.965 1.00 9.80  ? 350 VAL A N     1 
ATOM   2415 C  CA    . VAL B 2 350 ? 1.954   48.082 117.259 1.00 9.62  ? 350 VAL A CA    1 
ATOM   2416 C  C     . VAL B 2 350 ? 2.510   48.531 118.611 1.00 9.54  ? 350 VAL A C     1 
ATOM   2417 O  O     . VAL B 2 350 ? 3.042   49.630 118.737 1.00 9.12  ? 350 VAL A O     1 
ATOM   2418 C  CB    . VAL B 2 350 ? 0.427   48.053 117.231 1.00 9.85  ? 350 VAL A CB    1 
ATOM   2419 C  CG1   . VAL B 2 350 ? -0.160  49.069 118.208 1.00 10.26 ? 350 VAL A CG1   1 
ATOM   2420 C  CG2   . VAL B 2 350 ? -0.148  48.237 115.852 1.00 10.04 ? 350 VAL A CG2   1 
ATOM   2421 N  N     . ALA B 2 351 ? 2.386   47.600 119.542 1.00 9.44  ? 351 ALA A N     1 
ATOM   2422 C  CA    . ALA B 2 351 ? 2.805   47.691 120.938 1.00 8.99  ? 351 ALA A CA    1 
ATOM   2423 C  C     . ALA B 2 351 ? 4.274   48.122 121.014 1.00 8.58  ? 351 ALA A C     1 
ATOM   2424 O  O     . ALA B 2 351 ? 4.661   48.967 121.823 1.00 8.73  ? 351 ALA A O     1 
ATOM   2425 C  CB    . ALA B 2 351 ? 2.606   46.381 121.700 1.00 7.97  ? 351 ALA A CB    1 
ATOM   2426 N  N     . ARG B 2 352 ? 4.997   47.477 120.136 1.00 9.45  ? 352 ARG A N     1 
ATOM   2427 C  CA    . ARG B 2 352 ? 6.430   47.660 119.956 1.00 10.88 ? 352 ARG A CA    1 
ATOM   2428 C  C     . ARG B 2 352 ? 6.733   49.030 119.361 1.00 11.48 ? 352 ARG A C     1 
ATOM   2429 O  O     . ARG B 2 352 ? 7.705   49.619 119.867 1.00 12.08 ? 352 ARG A O     1 
ATOM   2430 C  CB    . ARG B 2 352 ? 7.084   46.567 119.087 1.00 11.46 ? 352 ARG A CB    1 
ATOM   2431 C  CG    . ARG B 2 352 ? 8.504   46.218 119.537 1.00 11.90 ? 352 ARG A CG    1 
ATOM   2432 C  CD    . ARG B 2 352 ? 9.059   45.120 118.681 1.00 12.51 ? 352 ARG A CD    1 
ATOM   2433 N  NE    . ARG B 2 352 ? 9.072   45.472 117.298 1.00 14.33 ? 352 ARG A NE    1 
ATOM   2434 C  CZ    . ARG B 2 352 ? 8.488   45.018 116.208 1.00 18.27 ? 352 ARG A CZ    1 
ATOM   2435 N  NH1   . ARG B 2 352 ? 7.657   43.966 116.132 1.00 18.01 ? 352 ARG A NH1   1 
ATOM   2436 N  NH2   . ARG B 2 352 ? 8.735   45.625 115.021 1.00 20.76 ? 352 ARG A NH2   1 
ATOM   2437 N  N     . SER B 2 353 ? 5.973   49.532 118.407 1.00 11.66 ? 353 SER A N     1 
ATOM   2438 C  CA    . SER B 2 353 ? 6.286   50.835 117.816 1.00 10.94 ? 353 SER A CA    1 
ATOM   2439 C  C     . SER B 2 353 ? 5.702   52.002 118.561 1.00 10.27 ? 353 SER A C     1 
ATOM   2440 O  O     . SER B 2 353 ? 5.792   53.136 118.035 1.00 10.54 ? 353 SER A O     1 
ATOM   2441 C  CB    . SER B 2 353 ? 5.945   50.917 116.344 1.00 12.59 ? 353 SER A CB    1 
ATOM   2442 O  OG    . SER B 2 353 ? 6.009   49.655 115.695 1.00 16.41 ? 353 SER A OG    1 
ATOM   2443 N  N     . LEU B 2 354 ? 5.141   51.828 119.725 1.00 10.17 ? 354 LEU A N     1 
ATOM   2444 C  CA    . LEU B 2 354 ? 4.573   52.953 120.499 1.00 9.81  ? 354 LEU A CA    1 
ATOM   2445 C  C     . LEU B 2 354 ? 5.541   53.357 121.610 1.00 10.86 ? 354 LEU A C     1 
ATOM   2446 O  O     . LEU B 2 354 ? 6.295   52.510 122.116 1.00 11.17 ? 354 LEU A O     1 
ATOM   2447 C  CB    . LEU B 2 354 ? 3.208   52.461 120.985 1.00 6.41  ? 354 LEU A CB    1 
ATOM   2448 C  CG    . LEU B 2 354 ? 2.024   52.505 120.043 1.00 5.36  ? 354 LEU A CG    1 
ATOM   2449 C  CD1   . LEU B 2 354 ? 0.862   51.669 120.545 1.00 4.50  ? 354 LEU A CD1   1 
ATOM   2450 C  CD2   . LEU B 2 354 ? 1.584   53.957 119.881 1.00 6.29  ? 354 LEU A CD2   1 
ATOM   2451 N  N     . PRO B 2 355 ? 5.475   54.636 121.979 1.00 11.44 ? 355 PRO A N     1 
ATOM   2452 C  CA    . PRO B 2 355 ? 6.306   55.223 123.057 1.00 11.14 ? 355 PRO A CA    1 
ATOM   2453 C  C     . PRO B 2 355 ? 5.834   54.682 124.390 1.00 10.76 ? 355 PRO A C     1 
ATOM   2454 O  O     . PRO B 2 355 ? 4.698   54.157 124.380 1.00 10.23 ? 355 PRO A O     1 
ATOM   2455 C  CB    . PRO B 2 355 ? 6.104   56.715 122.932 1.00 11.38 ? 355 PRO A CB    1 
ATOM   2456 C  CG    . PRO B 2 355 ? 4.926   56.955 122.035 1.00 12.03 ? 355 PRO A CG    1 
ATOM   2457 C  CD    . PRO B 2 355 ? 4.565   55.631 121.390 1.00 11.96 ? 355 PRO A CD    1 
ATOM   2458 N  N     . VAL B 2 356 ? 6.587   54.776 125.481 1.00 10.84 ? 356 VAL A N     1 
ATOM   2459 C  CA    . VAL B 2 356 ? 6.046   54.179 126.723 1.00 10.97 ? 356 VAL A CA    1 
ATOM   2460 C  C     . VAL B 2 356 ? 4.761   54.899 127.153 1.00 11.46 ? 356 VAL A C     1 
ATOM   2461 O  O     . VAL B 2 356 ? 3.952   54.283 127.860 1.00 11.82 ? 356 VAL A O     1 
ATOM   2462 C  CB    . VAL B 2 356 ? 6.999   54.067 127.903 1.00 10.11 ? 356 VAL A CB    1 
ATOM   2463 C  CG1   . VAL B 2 356 ? 8.437   53.741 127.561 1.00 10.57 ? 356 VAL A CG1   1 
ATOM   2464 C  CG2   . VAL B 2 356 ? 6.894   55.280 128.814 1.00 8.95  ? 356 VAL A CG2   1 
ATOM   2465 N  N     . ALA B 2 357 ? 4.683   56.152 126.771 1.00 11.60 ? 357 ALA A N     1 
ATOM   2466 C  CA    . ALA B 2 357 ? 3.537   57.002 127.102 1.00 12.68 ? 357 ALA A CA    1 
ATOM   2467 C  C     . ALA B 2 357 ? 3.574   58.243 126.209 1.00 13.63 ? 357 ALA A C     1 
ATOM   2468 O  O     . ALA B 2 357 ? 4.576   58.578 125.583 1.00 14.71 ? 357 ALA A O     1 
ATOM   2469 C  CB    . ALA B 2 357 ? 3.473   57.400 128.568 1.00 10.78 ? 357 ALA A CB    1 
ATOM   2470 N  N     . VAL B 2 358 ? 2.439   58.910 126.220 1.00 13.12 ? 358 VAL A N     1 
ATOM   2471 C  CA    . VAL B 2 358 ? 2.274   60.112 125.376 1.00 12.69 ? 358 VAL A CA    1 
ATOM   2472 C  C     . VAL B 2 358 ? 1.566   61.174 126.213 1.00 13.23 ? 358 VAL A C     1 
ATOM   2473 O  O     . VAL B 2 358 ? 0.840   60.761 127.141 1.00 13.27 ? 358 VAL A O     1 
ATOM   2474 C  CB    . VAL B 2 358 ? 1.470   59.622 124.156 1.00 11.93 ? 358 VAL A CB    1 
ATOM   2475 C  CG1   . VAL B 2 358 ? 0.002   60.022 124.242 1.00 9.96  ? 358 VAL A CG1   1 
ATOM   2476 C  CG2   . VAL B 2 358 ? 2.147   59.989 122.862 1.00 12.41 ? 358 VAL A CG2   1 
ATOM   2477 N  N     . ILE B 2 359 ? 1.846   62.429 125.856 1.00 12.84 ? 359 ILE A N     1 
ATOM   2478 C  CA    . ILE B 2 359 ? 1.197   63.538 126.583 1.00 12.15 ? 359 ILE A CA    1 
ATOM   2479 C  C     . ILE B 2 359 ? -0.297  63.442 126.181 1.00 12.37 ? 359 ILE A C     1 
ATOM   2480 O  O     . ILE B 2 359 ? -0.637  62.910 125.114 1.00 12.53 ? 359 ILE A O     1 
ATOM   2481 C  CB    . ILE B 2 359 ? 1.831   64.913 126.291 1.00 10.04 ? 359 ILE A CB    1 
ATOM   2482 C  CG1   . ILE B 2 359 ? 2.009   65.182 124.796 1.00 8.04  ? 359 ILE A CG1   1 
ATOM   2483 C  CG2   . ILE B 2 359 ? 3.218   65.077 126.915 1.00 10.56 ? 359 ILE A CG2   1 
ATOM   2484 C  CD1   . ILE B 2 359 ? 0.740   65.718 124.130 1.00 6.90  ? 359 ILE A CD1   1 
ATOM   2485 N  N     . ALA B 2 360 ? -1.140  63.958 127.048 1.00 12.46 ? 360 ALA A N     1 
ATOM   2486 C  CA    . ALA B 2 360 ? -2.621  63.853 126.952 1.00 11.67 ? 360 ALA A CA    1 
ATOM   2487 C  C     . ALA B 2 360 ? -3.248  64.320 125.614 1.00 12.21 ? 360 ALA A C     1 
ATOM   2488 O  O     . ALA B 2 360 ? -4.211  63.717 125.114 1.00 13.35 ? 360 ALA A O     1 
ATOM   2489 C  CB    . ALA B 2 360 ? -3.276  64.689 128.053 1.00 7.30  ? 360 ALA A CB    1 
ATOM   2490 N  N     . ALA B 2 361 ? -2.727  65.387 125.039 1.00 12.19 ? 361 ALA A N     1 
ATOM   2491 C  CA    . ALA B 2 361 ? -3.302  65.976 123.801 1.00 13.31 ? 361 ALA A CA    1 
ATOM   2492 C  C     . ALA B 2 361 ? -3.042  65.108 122.556 1.00 14.03 ? 361 ALA A C     1 
ATOM   2493 O  O     . ALA B 2 361 ? -3.407  65.483 121.428 1.00 15.38 ? 361 ALA A O     1 
ATOM   2494 C  CB    . ALA B 2 361 ? -2.703  67.356 123.540 1.00 7.37  ? 361 ALA A CB    1 
ATOM   2495 N  N     . GLN B 2 362 ? -2.419  63.969 122.785 1.00 14.02 ? 362 GLN A N     1 
ATOM   2496 C  CA    . GLN B 2 362 ? -2.078  63.021 121.709 1.00 14.65 ? 362 GLN A CA    1 
ATOM   2497 C  C     . GLN B 2 362 ? -2.685  61.655 121.945 1.00 15.72 ? 362 GLN A C     1 
ATOM   2498 O  O     . GLN B 2 362 ? -2.053  60.621 121.685 1.00 17.79 ? 362 GLN A O     1 
ATOM   2499 C  CB    . GLN B 2 362 ? -0.588  62.724 121.671 1.00 12.64 ? 362 GLN A CB    1 
ATOM   2500 C  CG    . GLN B 2 362 ? 0.289   63.929 121.392 1.00 14.36 ? 362 GLN A CG    1 
ATOM   2501 C  CD    . GLN B 2 362 ? 1.754   63.525 121.248 1.00 19.61 ? 362 GLN A CD    1 
ATOM   2502 O  OE1   . GLN B 2 362 ? 2.289   62.841 122.120 1.00 22.82 ? 362 GLN A OE1   1 
ATOM   2503 N  NE2   . GLN B 2 362 ? 2.438   63.899 120.186 1.00 22.41 ? 362 GLN A NE2   1 
ATOM   2504 N  N     . ASN B 2 363 ? -3.888  61.637 122.438 1.00 15.00 ? 363 ASN A N     1 
ATOM   2505 C  CA    . ASN B 2 363 ? -4.526  60.365 122.708 1.00 14.00 ? 363 ASN A CA    1 
ATOM   2506 C  C     . ASN B 2 363 ? -5.730  60.150 121.799 1.00 14.00 ? 363 ASN A C     1 
ATOM   2507 O  O     . ASN B 2 363 ? -6.016  60.995 120.938 1.00 14.00 ? 363 ASN A O     1 
ATOM   2508 C  CB    . ASN B 2 363 ? -4.939  60.263 124.183 1.00 15.00 ? 363 ASN A CB    1 
ATOM   2509 C  CG    . ASN B 2 363 ? -6.179  61.078 124.541 1.00 17.00 ? 363 ASN A CG    1 
ATOM   2510 O  OD1   . ASN B 2 363 ? -7.235  60.505 124.808 1.00 16.00 ? 363 ASN A OD1   1 
ATOM   2511 N  ND2   . ASN B 2 363 ? -6.113  62.394 124.572 1.00 19.00 ? 363 ASN A ND2   1 
ATOM   2512 O  OXT   . ASN B 2 363 ? -6.424  59.130 121.921 1.00 14.00 ? 363 ASN A OXT   1 
ATOM   2513 N  N     . ALA C 3 1   ? -2.159  65.387 115.636 1.00 19.24 ? 364 ALA D N     1 
ATOM   2514 C  CA    . ALA C 3 1   ? -2.517  64.000 116.072 1.00 19.11 ? 364 ALA D CA    1 
ATOM   2515 C  C     . ALA C 3 1   ? -3.055  63.626 117.437 1.00 18.75 ? 364 ALA D C     1 
ATOM   2516 O  O     . ALA C 3 1   ? -2.855  64.348 118.423 1.00 19.84 ? 364 ALA D O     1 
ATOM   2517 C  CB    . ALA C 3 1   ? -1.319  63.110 115.770 1.00 18.34 ? 364 ALA D CB    1 
ATOM   2518 N  N     . SER C 3 2   ? -3.695  62.447 117.222 1.00 17.11 ? 365 SER D N     1 
ATOM   2519 C  CA    . SER C 3 2   ? -4.396  61.560 118.169 1.00 15.51 ? 365 SER D CA    1 
ATOM   2520 C  C     . SER C 3 2   ? -3.744  60.156 118.092 1.00 15.12 ? 365 SER D C     1 
ATOM   2521 O  O     . SER C 3 2   ? -2.841  59.915 117.273 1.00 14.63 ? 365 SER D O     1 
ATOM   2522 C  CB    . SER C 3 2   ? -5.878  61.439 117.766 1.00 13.80 ? 365 SER D CB    1 
ATOM   2523 O  OG    . SER C 3 2   ? -6.080  60.269 116.978 1.00 14.75 ? 365 SER D OG    1 
ATOM   2524 N  N     . MET C 3 3   ? -4.223  59.250 118.938 1.00 14.28 ? 366 MET D N     1 
ATOM   2525 C  CA    . MET C 3 3   ? -3.663  57.878 119.061 1.00 13.22 ? 366 MET D CA    1 
ATOM   2526 C  C     . MET C 3 3   ? -3.948  57.008 117.822 1.00 12.48 ? 366 MET D C     1 
ATOM   2527 O  O     . MET C 3 3   ? -3.027  56.587 117.107 1.00 11.64 ? 366 MET D O     1 
ATOM   2528 C  CB    . MET C 3 3   ? -4.235  57.169 120.288 1.00 13.07 ? 366 MET D CB    1 
ATOM   2529 C  CG    . MET C 3 3   ? -3.150  56.505 121.144 1.00 13.11 ? 366 MET D CG    1 
ATOM   2530 S  SD    . MET C 3 3   ? -1.895  55.696 120.171 1.00 15.07 ? 366 MET D SD    1 
ATOM   2531 C  CE    . MET C 3 3   ? -0.303  55.875 120.948 1.00 13.20 ? 366 MET D CE    1 
ATOM   2532 N  N     . TRP C 3 4   ? -5.217  56.723 117.581 1.00 11.68 ? 367 TRP D N     1 
ATOM   2533 C  CA    . TRP C 3 4   ? -5.611  55.899 116.422 1.00 11.96 ? 367 TRP D CA    1 
ATOM   2534 C  C     . TRP C 3 4   ? -4.800  56.333 115.201 1.00 12.68 ? 367 TRP D C     1 
ATOM   2535 O  O     . TRP C 3 4   ? -4.223  55.499 114.486 1.00 12.17 ? 367 TRP D O     1 
ATOM   2536 C  CB    . TRP C 3 4   ? -7.101  56.069 116.117 1.00 10.70 ? 367 TRP D CB    1 
ATOM   2537 C  CG    . TRP C 3 4   ? -7.638  55.026 115.127 1.00 13.31 ? 367 TRP D CG    1 
ATOM   2538 C  CD1   . TRP C 3 4   ? -8.377  55.255 114.031 1.00 14.52 ? 367 TRP D CD1   1 
ATOM   2539 C  CD2   . TRP C 3 4   ? -7.431  53.624 115.222 1.00 14.67 ? 367 TRP D CD2   1 
ATOM   2540 N  NE1   . TRP C 3 4   ? -8.648  53.983 113.430 1.00 14.94 ? 367 TRP D NE1   1 
ATOM   2541 C  CE2   . TRP C 3 4   ? -8.088  53.041 114.146 1.00 14.88 ? 367 TRP D CE2   1 
ATOM   2542 C  CE3   . TRP C 3 4   ? -6.749  52.807 116.130 1.00 15.30 ? 367 TRP D CE3   1 
ATOM   2543 C  CZ2   . TRP C 3 4   ? -8.111  51.659 113.922 1.00 15.27 ? 367 TRP D CZ2   1 
ATOM   2544 C  CZ3   . TRP C 3 4   ? -6.776  51.416 115.894 1.00 16.35 ? 367 TRP D CZ3   1 
ATOM   2545 C  CH2   . TRP C 3 4   ? -7.426  50.871 114.842 1.00 15.94 ? 367 TRP D CH2   1 
ATOM   2546 N  N     . GLU C 3 5   ? -4.788  57.639 115.018 1.00 13.88 ? 368 GLU D N     1 
ATOM   2547 C  CA    . GLU C 3 5   ? -4.068  58.289 113.918 1.00 15.21 ? 368 GLU D CA    1 
ATOM   2548 C  C     . GLU C 3 5   ? -2.611  57.826 113.910 1.00 15.16 ? 368 GLU D C     1 
ATOM   2549 O  O     . GLU C 3 5   ? -1.950  57.816 112.862 1.00 14.66 ? 368 GLU D O     1 
ATOM   2550 C  CB    . GLU C 3 5   ? -4.106  59.808 114.094 1.00 17.53 ? 368 GLU D CB    1 
ATOM   2551 C  CG    . GLU C 3 5   ? -5.175  60.484 113.234 1.00 21.66 ? 368 GLU D CG    1 
ATOM   2552 C  CD    . GLU C 3 5   ? -4.817  61.924 112.860 1.00 24.91 ? 368 GLU D CD    1 
ATOM   2553 O  OE1   . GLU C 3 5   ? -3.589  62.244 112.630 1.00 24.83 ? 368 GLU D OE1   1 
ATOM   2554 O  OE2   . GLU C 3 5   ? -5.743  62.818 112.776 1.00 25.84 ? 368 GLU D OE2   1 
ATOM   2555 N  N     . ARG C 3 6   ? -2.150  57.447 115.091 1.00 14.85 ? 369 ARG D N     1 
ATOM   2556 C  CA    . ARG C 3 6   ? -0.766  56.991 115.287 1.00 14.51 ? 369 ARG D CA    1 
ATOM   2557 C  C     . ARG C 3 6   ? -0.630  55.487 115.034 1.00 15.09 ? 369 ARG D C     1 
ATOM   2558 O  O     . ARG C 3 6   ? 0.347   55.023 114.435 1.00 16.30 ? 369 ARG D O     1 
ATOM   2559 C  CB    . ARG C 3 6   ? -0.292  57.258 116.719 1.00 13.49 ? 369 ARG D CB    1 
ATOM   2560 C  CG    . ARG C 3 6   ? 0.921   56.402 117.106 1.00 13.18 ? 369 ARG D CG    1 
ATOM   2561 C  CD    . ARG C 3 6   ? 1.907   57.119 118.036 1.00 13.69 ? 369 ARG D CD    1 
ATOM   2562 N  NE    . ARG C 3 6   ? 1.437   58.440 118.474 1.00 17.82 ? 369 ARG D NE    1 
ATOM   2563 C  CZ    . ARG C 3 6   ? 2.217   59.350 119.076 1.00 19.78 ? 369 ARG D CZ    1 
ATOM   2564 N  NH1   . ARG C 3 6   ? 3.510   59.097 119.321 1.00 20.13 ? 369 ARG D NH1   1 
ATOM   2565 N  NH2   . ARG C 3 6   ? 1.791   60.556 119.476 1.00 18.22 ? 369 ARG D NH2   1 
ATOM   2566 N  N     . VAL C 3 7   ? -1.609  54.732 115.494 1.00 14.44 ? 370 VAL D N     1 
ATOM   2567 C  CA    . VAL C 3 7   ? -1.566  53.270 115.349 1.00 14.39 ? 370 VAL D CA    1 
ATOM   2568 C  C     . VAL C 3 7   ? -1.981  52.827 113.944 1.00 13.73 ? 370 VAL D C     1 
ATOM   2569 O  O     . VAL C 3 7   ? -1.565  51.765 113.459 1.00 12.89 ? 370 VAL D O     1 
ATOM   2570 C  CB    . VAL C 3 7   ? -2.452  52.592 116.399 1.00 14.23 ? 370 VAL D CB    1 
ATOM   2571 C  CG1   . VAL C 3 7   ? -3.547  53.512 116.941 1.00 12.85 ? 370 VAL D CG1   1 
ATOM   2572 C  CG2   . VAL C 3 7   ? -3.176  51.356 115.862 1.00 13.76 ? 370 VAL D CG2   1 
ATOM   2573 N  N     . LYS C 3 8   ? -2.792  53.640 113.302 1.00 13.47 ? 371 LYS D N     1 
ATOM   2574 C  CA    . LYS C 3 8   ? -3.251  53.343 111.938 1.00 13.79 ? 371 LYS D CA    1 
ATOM   2575 C  C     . LYS C 3 8   ? -2.054  53.382 110.983 1.00 14.21 ? 371 LYS D C     1 
ATOM   2576 O  O     . LYS C 3 8   ? -1.842  52.458 110.184 1.00 13.81 ? 371 LYS D O     1 
ATOM   2577 C  CB    . LYS C 3 8   ? -4.302  54.359 111.494 1.00 12.40 ? 371 LYS D CB    1 
ATOM   2578 C  CG    . LYS C 3 8   ? -5.562  53.697 110.931 1.00 12.41 ? 371 LYS D CG    1 
ATOM   2579 C  CD    . LYS C 3 8   ? -6.854  54.298 111.489 1.00 13.82 ? 371 LYS D CD    1 
ATOM   2580 C  CE    . LYS C 3 8   ? -7.913  54.537 110.411 1.00 16.22 ? 371 LYS D CE    1 
ATOM   2581 N  NZ    . LYS C 3 8   ? -9.254  54.092 110.815 1.00 18.13 ? 371 LYS D NZ    1 
ATOM   2582 N  N     . SER C 3 9   ? -1.302  54.461 111.103 1.00 14.26 ? 372 SER D N     1 
ATOM   2583 C  CA    . SER C 3 9   ? -0.097  54.684 110.291 1.00 14.82 ? 372 SER D CA    1 
ATOM   2584 C  C     . SER C 3 9   ? 0.804   53.451 110.362 1.00 15.02 ? 372 SER D C     1 
ATOM   2585 O  O     . SER C 3 9   ? 1.135   52.842 109.335 1.00 15.72 ? 372 SER D O     1 
ATOM   2586 C  CB    . SER C 3 9   ? 0.676   55.895 110.819 1.00 16.52 ? 372 SER D CB    1 
ATOM   2587 O  OG    . SER C 3 9   ? -0.191  56.742 111.558 1.00 19.84 ? 372 SER D OG    1 
ATOM   2588 N  N     . ILE C 3 10  ? 1.167   53.128 111.588 1.00 14.83 ? 373 ILE D N     1 
ATOM   2589 C  CA    . ILE C 3 10  ? 2.027   51.978 111.891 1.00 15.30 ? 373 ILE D CA    1 
ATOM   2590 C  C     . ILE C 3 10  ? 1.538   50.732 111.153 1.00 16.30 ? 373 ILE D C     1 
ATOM   2591 O  O     . ILE C 3 10  ? 2.242   50.180 110.296 1.00 16.31 ? 373 ILE D O     1 
ATOM   2592 C  CB    . ILE C 3 10  ? 1.984   51.663 113.390 1.00 12.69 ? 373 ILE D CB    1 
ATOM   2593 C  CG1   . ILE C 3 10  ? 2.580   52.768 114.260 1.00 12.51 ? 373 ILE D CG1   1 
ATOM   2594 C  CG2   . ILE C 3 10  ? 2.753   50.391 113.756 1.00 9.93  ? 373 ILE D CG2   1 
ATOM   2595 C  CD1   . ILE C 3 10  ? 3.049   52.263 115.627 1.00 25.00 ? 373 ILE D CD1   1 
ATOM   2596 N  N     . ILE C 3 11  ? 0.336   50.352 111.527 1.00 16.71 ? 374 ILE D N     1 
ATOM   2597 C  CA    . ILE C 3 11  ? -0.340  49.151 111.020 1.00 17.55 ? 374 ILE D CA    1 
ATOM   2598 C  C     . ILE C 3 11  ? -0.416  49.111 109.486 1.00 17.78 ? 374 ILE D C     1 
ATOM   2599 O  O     . ILE C 3 11  ? -0.396  48.038 108.871 1.00 18.14 ? 374 ILE D O     1 
ATOM   2600 C  CB    . ILE C 3 11  ? -1.768  49.093 111.556 1.00 17.78 ? 374 ILE D CB    1 
ATOM   2601 C  CG1   . ILE C 3 11  ? -1.907  48.182 112.777 1.00 17.54 ? 374 ILE D CG1   1 
ATOM   2602 C  CG2   . ILE C 3 11  ? -2.769  48.569 110.526 1.00 17.97 ? 374 ILE D CG2   1 
ATOM   2603 C  CD1   . ILE C 3 11  ? -3.184  48.444 113.576 1.00 25.00 ? 374 ILE D CD1   1 
ATOM   2604 N  N     . LYS C 3 12  ? -0.509  50.271 108.870 1.00 18.09 ? 375 LYS D N     1 
ATOM   2605 C  CA    . LYS C 3 12  ? -0.638  50.354 107.401 1.00 18.30 ? 375 LYS D CA    1 
ATOM   2606 C  C     . LYS C 3 12  ? 0.692   50.050 106.705 1.00 18.63 ? 375 LYS D C     1 
ATOM   2607 O  O     . LYS C 3 12  ? 0.716   49.523 105.581 1.00 19.09 ? 375 LYS D O     1 
ATOM   2608 C  CB    . LYS C 3 12  ? -1.083  51.756 106.981 1.00 16.97 ? 375 LYS D CB    1 
ATOM   2609 C  CG    . LYS C 3 12  ? -2.291  51.737 106.041 1.00 59.15 ? 375 LYS D CG    1 
ATOM   2610 C  CD    . LYS C 3 12  ? -3.068  53.054 106.039 1.00 52.12 ? 375 LYS D CD    1 
ATOM   2611 C  CE    . LYS C 3 12  ? -2.322  54.186 105.330 1.00 55.19 ? 375 LYS D CE    1 
ATOM   2612 N  NZ    . LYS C 3 12  ? -3.054  54.722 104.173 1.00 54.29 ? 375 LYS D NZ    1 
ATOM   2613 N  N     . SER C 3 13  ? 1.753   50.387 107.407 1.00 18.01 ? 376 SER D N     1 
ATOM   2614 C  CA    . SER C 3 13  ? 3.126   50.253 106.903 1.00 17.99 ? 376 SER D CA    1 
ATOM   2615 C  C     . SER C 3 13  ? 3.654   48.808 107.047 1.00 17.97 ? 376 SER D C     1 
ATOM   2616 O  O     . SER C 3 13  ? 4.472   48.341 106.243 1.00 17.63 ? 376 SER D O     1 
ATOM   2617 C  CB    . SER C 3 13  ? 4.032   51.235 107.654 1.00 18.75 ? 376 SER D CB    1 
ATOM   2618 O  OG    . SER C 3 13  ? 5.069   50.542 108.320 1.00 24.39 ? 376 SER D OG    1 
ATOM   2619 N  N     . SER C 3 14  ? 3.187   48.099 108.066 1.00 17.98 ? 377 SER D N     1 
ATOM   2620 C  CA    . SER C 3 14  ? 3.624   46.703 108.310 1.00 18.01 ? 377 SER D CA    1 
ATOM   2621 C  C     . SER C 3 14  ? 2.785   45.725 107.493 1.00 18.03 ? 377 SER D C     1 
ATOM   2622 O  O     . SER C 3 14  ? 2.893   44.499 107.639 1.00 17.88 ? 377 SER D O     1 
ATOM   2623 C  CB    . SER C 3 14  ? 3.475   46.335 109.781 1.00 19.31 ? 377 SER D CB    1 
ATOM   2624 O  OG    . SER C 3 14  ? 4.573   46.845 110.517 1.00 19.60 ? 377 SER D OG    1 
ATOM   2625 N  N     . LEU C 3 15  ? 1.960   46.295 106.661 1.00 18.54 ? 378 LEU D N     1 
ATOM   2626 C  CA    . LEU C 3 15  ? 1.102   45.525 105.775 1.00 19.42 ? 378 LEU D CA    1 
ATOM   2627 C  C     . LEU C 3 15  ? 1.349   45.998 104.365 1.00 21.23 ? 378 LEU D C     1 
ATOM   2628 O  O     . LEU C 3 15  ? 0.433   46.026 103.529 1.00 22.84 ? 378 LEU D O     1 
ATOM   2629 C  CB    . LEU C 3 15  ? -0.354  45.706 106.181 1.00 17.28 ? 378 LEU D CB    1 
ATOM   2630 C  CG    . LEU C 3 15  ? -0.814  44.600 107.126 1.00 16.51 ? 378 LEU D CG    1 
ATOM   2631 C  CD1   . LEU C 3 15  ? -2.024  43.830 106.601 1.00 16.11 ? 378 LEU D CD1   1 
ATOM   2632 C  CD2   . LEU C 3 15  ? 0.273   43.549 107.374 1.00 15.05 ? 378 LEU D CD2   1 
ATOM   2633 N  N     . ALA C 3 16  ? 2.601   46.355 104.160 1.00 21.70 ? 379 ALA D N     1 
ATOM   2634 C  CA    . ALA C 3 16  ? 3.034   46.862 102.879 1.00 22.28 ? 379 ALA D CA    1 
ATOM   2635 C  C     . ALA C 3 16  ? 4.561   46.788 102.670 1.00 22.60 ? 379 ALA D C     1 
ATOM   2636 O  O     . ALA C 3 16  ? 5.289   47.592 103.323 1.00 22.45 ? 379 ALA D O     1 
ATOM   2637 C  CB    . ALA C 3 16  ? 2.631   48.331 102.731 1.00 21.32 ? 379 ALA D CB    1 
ATOM   2638 N  N     . LEU D 2 56  ? 19.702  28.584 104.410 1.00 20.88 ? 56  LEU B N     1 
ATOM   2639 C  CA    . LEU D 2 56  ? 18.369  28.406 105.036 1.00 20.97 ? 56  LEU B CA    1 
ATOM   2640 C  C     . LEU D 2 56  ? 17.812  29.779 105.115 1.00 21.32 ? 56  LEU B C     1 
ATOM   2641 O  O     . LEU D 2 56  ? 17.972  30.474 106.129 1.00 21.60 ? 56  LEU B O     1 
ATOM   2642 C  CB    . LEU D 2 56  ? 18.605  27.832 106.421 1.00 20.32 ? 56  LEU B CB    1 
ATOM   2643 C  CG    . LEU D 2 56  ? 19.123  26.393 106.417 1.00 19.62 ? 56  LEU B CG    1 
ATOM   2644 C  CD1   . LEU D 2 56  ? 20.651  26.308 106.446 1.00 18.76 ? 56  LEU B CD1   1 
ATOM   2645 C  CD2   . LEU D 2 56  ? 18.641  25.582 107.621 1.00 18.29 ? 56  LEU B CD2   1 
ATOM   2646 N  N     . THR D 2 57  ? 17.198  30.104 104.037 1.00 20.48 ? 57  THR B N     1 
ATOM   2647 C  CA    . THR D 2 57  ? 16.727  31.436 103.809 1.00 19.48 ? 57  THR B CA    1 
ATOM   2648 C  C     . THR D 2 57  ? 15.213  31.524 103.923 1.00 19.19 ? 57  THR B C     1 
ATOM   2649 O  O     . THR D 2 57  ? 14.541  32.097 103.053 1.00 20.35 ? 57  THR B O     1 
ATOM   2650 C  CB    . THR D 2 57  ? 17.242  31.839 102.444 1.00 19.81 ? 57  THR B CB    1 
ATOM   2651 O  OG1   . THR D 2 57  ? 18.498  32.488 102.580 1.00 20.79 ? 57  THR B OG1   1 
ATOM   2652 C  CG2   . THR D 2 57  ? 16.303  32.789 101.706 1.00 18.31 ? 57  THR B CG2   1 
ATOM   2653 N  N     . ARG D 2 58  ? 14.747  30.951 105.006 1.00 18.68 ? 58  ARG B N     1 
ATOM   2654 C  CA    . ARG D 2 58  ? 13.338  30.972 105.395 1.00 17.92 ? 58  ARG B CA    1 
ATOM   2655 C  C     . ARG D 2 58  ? 13.298  31.374 106.855 1.00 17.45 ? 58  ARG B C     1 
ATOM   2656 O  O     . ARG D 2 58  ? 12.361  32.046 107.309 1.00 17.71 ? 58  ARG B O     1 
ATOM   2657 C  CB    . ARG D 2 58  ? 12.706  29.607 105.136 1.00 17.95 ? 58  ARG B CB    1 
ATOM   2658 C  CG    . ARG D 2 58  ? 12.919  29.202 103.678 1.00 19.35 ? 58  ARG B CG    1 
ATOM   2659 C  CD    . ARG D 2 58  ? 12.248  27.890 103.264 1.00 21.54 ? 58  ARG B CD    1 
ATOM   2660 N  NE    . ARG D 2 58  ? 10.957  28.193 102.681 1.00 24.01 ? 58  ARG B NE    1 
ATOM   2661 C  CZ    . ARG D 2 58  ? 9.768   27.917 103.190 1.00 25.13 ? 58  ARG B CZ    1 
ATOM   2662 N  NH1   . ARG D 2 58  ? 8.785   28.815 103.260 1.00 25.09 ? 58  ARG B NH1   1 
ATOM   2663 N  NH2   . ARG D 2 58  ? 9.498   26.733 103.752 1.00 24.03 ? 58  ARG B NH2   1 
ATOM   2664 N  N     . LEU D 2 59  ? 14.341  30.942 107.534 1.00 16.20 ? 59  LEU B N     1 
ATOM   2665 C  CA    . LEU D 2 59  ? 14.544  31.274 108.936 1.00 14.65 ? 59  LEU B CA    1 
ATOM   2666 C  C     . LEU D 2 59  ? 15.013  32.737 109.012 1.00 13.28 ? 59  LEU B C     1 
ATOM   2667 O  O     . LEU D 2 59  ? 15.754  33.274 108.175 1.00 13.62 ? 59  LEU B O     1 
ATOM   2668 C  CB    . LEU D 2 59  ? 15.588  30.349 109.563 1.00 14.71 ? 59  LEU B CB    1 
ATOM   2669 C  CG    . LEU D 2 59  ? 15.103  28.907 109.727 1.00 15.65 ? 59  LEU B CG    1 
ATOM   2670 C  CD1   . LEU D 2 59  ? 16.237  27.886 109.608 1.00 15.39 ? 59  LEU B CD1   1 
ATOM   2671 C  CD2   . LEU D 2 59  ? 14.444  28.651 111.084 1.00 14.66 ? 59  LEU B CD2   1 
ATOM   2672 N  N     . SER D 2 60  ? 14.532  33.350 110.072 1.00 11.51 ? 60  SER B N     1 
ATOM   2673 C  CA    . SER D 2 60  ? 14.895  34.747 110.374 1.00 11.21 ? 60  SER B CA    1 
ATOM   2674 C  C     . SER D 2 60  ? 16.281  34.665 111.036 1.00 11.79 ? 60  SER B C     1 
ATOM   2675 O  O     . SER D 2 60  ? 16.631  33.602 111.569 1.00 11.59 ? 60  SER B O     1 
ATOM   2676 C  CB    . SER D 2 60  ? 13.886  35.226 111.428 1.00 10.66 ? 60  SER B CB    1 
ATOM   2677 O  OG    . SER D 2 60  ? 13.465  34.027 112.102 1.00 10.34 ? 60  SER B OG    1 
ATOM   2678 N  N     . GLN D 2 61  ? 16.961  35.790 111.002 1.00 12.24 ? 61  GLN B N     1 
ATOM   2679 C  CA    . GLN D 2 61  ? 18.296  35.871 111.596 1.00 12.86 ? 61  GLN B CA    1 
ATOM   2680 C  C     . GLN D 2 61  ? 18.328  35.270 112.981 1.00 11.45 ? 61  GLN B C     1 
ATOM   2681 O  O     . GLN D 2 61  ? 19.269  34.514 113.281 1.00 11.50 ? 61  GLN B O     1 
ATOM   2682 C  CB    . GLN D 2 61  ? 18.912  37.245 111.499 1.00 18.88 ? 61  GLN B CB    1 
ATOM   2683 C  CG    . GLN D 2 61  ? 20.053  37.233 110.482 1.00 26.12 ? 61  GLN B CG    1 
ATOM   2684 C  CD    . GLN D 2 61  ? 20.746  35.882 110.443 1.00 29.96 ? 61  GLN B CD    1 
ATOM   2685 O  OE1   . GLN D 2 61  ? 21.729  35.583 111.143 1.00 30.35 ? 61  GLN B OE1   1 
ATOM   2686 N  NE2   . GLN D 2 61  ? 20.213  35.009 109.566 1.00 31.18 ? 61  GLN B NE2   1 
ATOM   2687 N  N     . PRO D 2 62  ? 17.334  35.555 113.788 1.00 11.13 ? 62  PRO B N     1 
ATOM   2688 C  CA    . PRO D 2 62  ? 17.201  35.055 115.163 1.00 11.35 ? 62  PRO B CA    1 
ATOM   2689 C  C     . PRO D 2 62  ? 16.483  33.718 115.230 1.00 11.95 ? 62  PRO B C     1 
ATOM   2690 O  O     . PRO D 2 62  ? 16.697  32.913 116.169 1.00 12.65 ? 62  PRO B O     1 
ATOM   2691 C  CB    . PRO D 2 62  ? 16.427  36.152 115.895 1.00 10.30 ? 62  PRO B CB    1 
ATOM   2692 C  CG    . PRO D 2 62  ? 16.149  37.206 114.864 1.00 10.22 ? 62  PRO B CG    1 
ATOM   2693 C  CD    . PRO D 2 62  ? 16.198  36.465 113.514 1.00 10.92 ? 62  PRO B CD    1 
ATOM   2694 N  N     . GLY D 2 63  ? 15.615  33.497 114.250 1.00 11.44 ? 63  GLY B N     1 
ATOM   2695 C  CA    . GLY D 2 63  ? 14.896  32.190 114.267 1.00 10.45 ? 63  GLY B CA    1 
ATOM   2696 C  C     . GLY D 2 63  ? 16.015  31.130 114.217 1.00 10.13 ? 63  GLY B C     1 
ATOM   2697 O  O     . GLY D 2 63  ? 15.970  30.124 114.922 1.00 8.64  ? 63  GLY B O     1 
ATOM   2698 N  N     . LEU D 2 64  ? 16.997  31.455 113.370 1.00 10.20 ? 64  LEU B N     1 
ATOM   2699 C  CA    . LEU D 2 64  ? 18.145  30.598 113.127 1.00 9.61  ? 64  LEU B CA    1 
ATOM   2700 C  C     . LEU D 2 64  ? 19.170  30.581 114.247 1.00 8.67  ? 64  LEU B C     1 
ATOM   2701 O  O     . LEU D 2 64  ? 19.808  29.529 114.488 1.00 8.98  ? 64  LEU B O     1 
ATOM   2702 C  CB    . LEU D 2 64  ? 18.737  30.901 111.741 1.00 11.49 ? 64  LEU B CB    1 
ATOM   2703 C  CG    . LEU D 2 64  ? 20.136  30.254 111.588 1.00 13.11 ? 64  LEU B CG    1 
ATOM   2704 C  CD1   . LEU D 2 64  ? 20.013  28.932 110.859 1.00 13.06 ? 64  LEU B CD1   1 
ATOM   2705 C  CD2   . LEU D 2 64  ? 21.009  31.284 110.886 1.00 12.00 ? 64  LEU B CD2   1 
ATOM   2706 N  N     . ALA D 2 65  ? 19.343  31.714 114.923 1.00 7.81  ? 65  ALA B N     1 
ATOM   2707 C  CA    . ALA D 2 65  ? 20.285  31.713 116.066 1.00 6.91  ? 65  ALA B CA    1 
ATOM   2708 C  C     . ALA D 2 65  ? 19.672  30.847 117.190 1.00 6.18  ? 65  ALA B C     1 
ATOM   2709 O  O     . ALA D 2 65  ? 20.459  30.277 117.938 1.00 4.91  ? 65  ALA B O     1 
ATOM   2710 C  CB    . ALA D 2 65  ? 20.615  33.095 116.576 1.00 3.32  ? 65  ALA B CB    1 
ATOM   2711 N  N     . PHE D 2 66  ? 18.359  30.818 117.272 1.00 6.90  ? 66  PHE B N     1 
ATOM   2712 C  CA    . PHE D 2 66  ? 17.570  30.077 118.246 1.00 7.75  ? 66  PHE B CA    1 
ATOM   2713 C  C     . PHE D 2 66  ? 17.893  28.571 118.168 1.00 8.66  ? 66  PHE B C     1 
ATOM   2714 O  O     . PHE D 2 66  ? 18.145  27.847 119.142 1.00 8.69  ? 66  PHE B O     1 
ATOM   2715 C  CB    . PHE D 2 66  ? 16.061  30.234 118.013 1.00 7.23  ? 66  PHE B CB    1 
ATOM   2716 C  CG    . PHE D 2 66  ? 15.086  29.413 118.797 1.00 7.15  ? 66  PHE B CG    1 
ATOM   2717 C  CD1   . PHE D 2 66  ? 15.092  29.391 120.192 1.00 9.18  ? 66  PHE B CD1   1 
ATOM   2718 C  CD2   . PHE D 2 66  ? 14.070  28.705 118.170 1.00 6.78  ? 66  PHE B CD2   1 
ATOM   2719 C  CE1   . PHE D 2 66  ? 14.167  28.706 120.949 1.00 8.08  ? 66  PHE B CE1   1 
ATOM   2720 C  CE2   . PHE D 2 66  ? 13.139  27.954 118.901 1.00 7.14  ? 66  PHE B CE2   1 
ATOM   2721 C  CZ    . PHE D 2 66  ? 13.179  27.958 120.312 1.00 7.63  ? 66  PHE B CZ    1 
ATOM   2722 N  N     . LEU D 2 67  ? 17.782  28.149 116.904 1.00 8.99  ? 67  LEU B N     1 
ATOM   2723 C  CA    . LEU D 2 67  ? 18.004  26.730 116.600 1.00 9.98  ? 67  LEU B CA    1 
ATOM   2724 C  C     . LEU D 2 67  ? 19.432  26.370 116.992 1.00 11.09 ? 67  LEU B C     1 
ATOM   2725 O  O     . LEU D 2 67  ? 19.667  25.254 117.465 1.00 12.06 ? 67  LEU B O     1 
ATOM   2726 C  CB    . LEU D 2 67  ? 17.689  26.523 115.109 1.00 10.22 ? 67  LEU B CB    1 
ATOM   2727 C  CG    . LEU D 2 67  ? 16.192  26.494 114.774 1.00 10.03 ? 67  LEU B CG    1 
ATOM   2728 C  CD1   . LEU D 2 67  ? 16.014  26.088 113.326 1.00 9.10  ? 67  LEU B CD1   1 
ATOM   2729 C  CD2   . LEU D 2 67  ? 15.532  25.508 115.743 1.00 9.36  ? 67  LEU B CD2   1 
ATOM   2730 N  N     . LYS D 2 68  ? 20.316  27.315 116.754 1.00 11.52 ? 68  LYS B N     1 
ATOM   2731 C  CA    . LYS D 2 68  ? 21.734  27.102 117.033 1.00 12.35 ? 68  LYS B CA    1 
ATOM   2732 C  C     . LYS D 2 68  ? 22.039  26.932 118.503 1.00 12.89 ? 68  LYS B C     1 
ATOM   2733 O  O     . LYS D 2 68  ? 22.696  25.934 118.929 1.00 13.66 ? 68  LYS B O     1 
ATOM   2734 C  CB    . LYS D 2 68  ? 22.553  28.229 116.405 1.00 11.92 ? 68  LYS B CB    1 
ATOM   2735 C  CG    . LYS D 2 68  ? 22.859  27.876 114.938 1.00 12.59 ? 68  LYS B CG    1 
ATOM   2736 C  CD    . LYS D 2 68  ? 23.195  29.104 114.124 1.00 14.30 ? 68  LYS B CD    1 
ATOM   2737 C  CE    . LYS D 2 68  ? 24.580  28.994 113.496 1.00 16.14 ? 68  LYS B CE    1 
ATOM   2738 N  NZ    . LYS D 2 68  ? 24.854  30.261 112.734 1.00 19.10 ? 68  LYS B NZ    1 
ATOM   2739 N  N     . CYS D 2 69  ? 21.585  27.896 119.294 1.00 12.63 ? 69  CYS B N     1 
ATOM   2740 C  CA    . CYS D 2 69  ? 21.807  27.880 120.754 1.00 11.59 ? 69  CYS B CA    1 
ATOM   2741 C  C     . CYS D 2 69  ? 21.106  26.629 121.314 1.00 10.96 ? 69  CYS B C     1 
ATOM   2742 O  O     . CYS D 2 69  ? 21.653  25.915 122.160 1.00 9.74  ? 69  CYS B O     1 
ATOM   2743 C  CB    . CYS D 2 69  ? 21.350  29.159 121.414 1.00 11.25 ? 69  CYS B CB    1 
ATOM   2744 S  SG    . CYS D 2 69  ? 21.574  29.224 123.229 1.00 15.23 ? 69  CYS B SG    1 
ATOM   2745 N  N     . ALA D 2 70  ? 19.932  26.404 120.765 1.00 10.83 ? 70  ALA B N     1 
ATOM   2746 C  CA    . ALA D 2 70  ? 19.074  25.299 121.123 1.00 11.36 ? 70  ALA B CA    1 
ATOM   2747 C  C     . ALA D 2 70  ? 19.746  23.945 121.025 1.00 11.87 ? 70  ALA B C     1 
ATOM   2748 O  O     . ALA D 2 70  ? 19.701  23.224 122.053 1.00 12.57 ? 70  ALA B O     1 
ATOM   2749 C  CB    . ALA D 2 70  ? 17.785  25.328 120.278 1.00 11.54 ? 70  ALA B CB    1 
ATOM   2750 N  N     . PHE D 2 71  ? 20.346  23.611 119.900 1.00 12.18 ? 71  PHE B N     1 
ATOM   2751 C  CA    . PHE D 2 71  ? 20.939  22.297 119.698 1.00 12.32 ? 71  PHE B CA    1 
ATOM   2752 C  C     . PHE D 2 71  ? 22.468  22.155 119.560 1.00 12.59 ? 71  PHE B C     1 
ATOM   2753 O  O     . PHE D 2 71  ? 23.034  21.081 119.816 1.00 13.93 ? 71  PHE B O     1 
ATOM   2754 C  CB    . PHE D 2 71  ? 20.277  21.656 118.435 1.00 11.34 ? 71  PHE B CB    1 
ATOM   2755 C  CG    . PHE D 2 71  ? 18.752  21.678 118.506 1.00 11.92 ? 71  PHE B CG    1 
ATOM   2756 C  CD1   . PHE D 2 71  ? 18.080  20.788 119.351 1.00 12.51 ? 71  PHE B CD1   1 
ATOM   2757 C  CD2   . PHE D 2 71  ? 18.031  22.592 117.731 1.00 11.94 ? 71  PHE B CD2   1 
ATOM   2758 C  CE1   . PHE D 2 71  ? 16.684  20.811 119.420 1.00 13.77 ? 71  PHE B CE1   1 
ATOM   2759 C  CE2   . PHE D 2 71  ? 16.634  22.616 117.800 1.00 13.66 ? 71  PHE B CE2   1 
ATOM   2760 C  CZ    . PHE D 2 71  ? 15.960  21.725 118.645 1.00 14.03 ? 71  PHE B CZ    1 
ATOM   2761 N  N     . ALA D 2 72  ? 23.200  23.161 119.163 1.00 11.46 ? 72  ALA B N     1 
ATOM   2762 C  CA    . ALA D 2 72  ? 24.659  22.957 119.003 1.00 10.53 ? 72  ALA B CA    1 
ATOM   2763 C  C     . ALA D 2 72  ? 25.458  24.114 119.591 1.00 11.17 ? 72  ALA B C     1 
ATOM   2764 O  O     . ALA D 2 72  ? 26.183  24.818 118.874 1.00 10.97 ? 72  ALA B O     1 
ATOM   2765 C  CB    . ALA D 2 72  ? 25.016  22.839 117.523 1.00 7.46  ? 72  ALA B CB    1 
ATOM   2766 N  N     . PRO D 2 73  ? 25.378  24.365 120.898 1.00 12.27 ? 73  PRO B N     1 
ATOM   2767 C  CA    . PRO D 2 73  ? 26.122  25.452 121.501 1.00 13.01 ? 73  PRO B CA    1 
ATOM   2768 C  C     . PRO D 2 73  ? 27.617  25.275 121.310 1.00 13.86 ? 73  PRO B C     1 
ATOM   2769 O  O     . PRO D 2 73  ? 28.304  26.252 120.873 1.00 15.07 ? 73  PRO B O     1 
ATOM   2770 C  CB    . PRO D 2 73  ? 25.737  25.391 122.960 1.00 12.37 ? 73  PRO B CB    1 
ATOM   2771 C  CG    . PRO D 2 73  ? 24.761  24.238 123.138 1.00 12.06 ? 73  PRO B CG    1 
ATOM   2772 C  CD    . PRO D 2 73  ? 24.540  23.584 121.810 1.00 12.21 ? 73  PRO B CD    1 
ATOM   2773 N  N     . PRO D 2 74  ? 28.190  24.095 121.612 1.00 13.57 ? 74  PRO B N     1 
ATOM   2774 C  CA    . PRO D 2 74  ? 29.639  23.873 121.523 1.00 13.71 ? 74  PRO B CA    1 
ATOM   2775 C  C     . PRO D 2 74  ? 30.235  24.008 120.123 1.00 14.52 ? 74  PRO B C     1 
ATOM   2776 O  O     . PRO D 2 74  ? 31.496  23.921 119.976 1.00 15.57 ? 74  PRO B O     1 
ATOM   2777 C  CB    . PRO D 2 74  ? 29.824  22.447 121.985 1.00 12.93 ? 74  PRO B CB    1 
ATOM   2778 C  CG    . PRO D 2 74  ? 28.451  21.881 122.318 1.00 12.70 ? 74  PRO B CG    1 
ATOM   2779 C  CD    . PRO D 2 74  ? 27.417  22.936 122.068 1.00 13.15 ? 74  PRO B CD    1 
ATOM   2780 N  N     . ASP D 2 75  ? 29.406  24.222 119.113 1.00 14.00 ? 75  ASP B N     1 
ATOM   2781 C  CA    . ASP D 2 75  ? 29.889  24.272 117.705 1.00 15.00 ? 75  ASP B CA    1 
ATOM   2782 C  C     . ASP D 2 75  ? 30.161  25.692 117.185 1.00 16.00 ? 75  ASP B C     1 
ATOM   2783 O  O     . ASP D 2 75  ? 30.365  25.906 115.980 1.00 18.00 ? 75  ASP B O     1 
ATOM   2784 C  CB    . ASP D 2 75  ? 28.848  23.687 116.752 1.00 16.00 ? 75  ASP B CB    1 
ATOM   2785 C  CG    . ASP D 2 75  ? 28.590  22.200 116.980 1.00 21.00 ? 75  ASP B CG    1 
ATOM   2786 O  OD1   . ASP D 2 75  ? 29.030  21.628 118.047 1.00 24.40 ? 75  ASP B OD1   1 
ATOM   2787 O  OD2   . ASP D 2 75  ? 27.930  21.521 116.105 1.00 21.00 ? 75  ASP B OD2   1 
ATOM   2788 N  N     . PHE D 2 76  ? 30.176  26.665 118.069 1.00 15.39 ? 76  PHE B N     1 
ATOM   2789 C  CA    . PHE D 2 76  ? 30.385  28.058 117.643 1.00 15.37 ? 76  PHE B CA    1 
ATOM   2790 C  C     . PHE D 2 76  ? 31.321  28.798 118.599 1.00 15.95 ? 76  PHE B C     1 
ATOM   2791 O  O     . PHE D 2 76  ? 31.289  28.577 119.819 1.00 17.94 ? 76  PHE B O     1 
ATOM   2792 C  CB    . PHE D 2 76  ? 29.035  28.764 117.565 1.00 12.49 ? 76  PHE B CB    1 
ATOM   2793 C  CG    . PHE D 2 76  ? 28.074  28.052 116.610 1.00 13.35 ? 76  PHE B CG    1 
ATOM   2794 C  CD1   . PHE D 2 76  ? 28.182  28.256 115.229 1.00 13.43 ? 76  PHE B CD1   1 
ATOM   2795 C  CD2   . PHE D 2 76  ? 27.092  27.189 117.114 1.00 14.84 ? 76  PHE B CD2   1 
ATOM   2796 C  CE1   . PHE D 2 76  ? 27.310  27.600 114.353 1.00 14.44 ? 76  PHE B CE1   1 
ATOM   2797 C  CE2   . PHE D 2 76  ? 26.219  26.533 116.237 1.00 14.98 ? 76  PHE B CE2   1 
ATOM   2798 C  CZ    . PHE D 2 76  ? 26.328  26.738 114.857 1.00 14.78 ? 76  PHE B CZ    1 
ATOM   2799 N  N     . ASN D 2 77  ? 32.117  29.654 117.973 1.00 14.84 ? 77  ASN B N     1 
ATOM   2800 C  CA    . ASN D 2 77  ? 33.122  30.489 118.649 1.00 13.08 ? 77  ASN B CA    1 
ATOM   2801 C  C     . ASN D 2 77  ? 32.499  31.210 119.844 1.00 12.88 ? 77  ASN B C     1 
ATOM   2802 O  O     . ASN D 2 77  ? 33.102  31.298 120.923 1.00 11.97 ? 77  ASN B O     1 
ATOM   2803 C  CB    . ASN D 2 77  ? 33.684  31.525 117.681 1.00 9.83  ? 77  ASN B CB    1 
ATOM   2804 C  CG    . ASN D 2 77  ? 34.809  32.351 118.299 1.00 11.04 ? 77  ASN B CG    1 
ATOM   2805 O  OD1   . ASN D 2 77  ? 35.563  31.841 119.126 1.00 10.15 ? 77  ASN B OD1   1 
ATOM   2806 N  ND2   . ASN D 2 77  ? 34.966  33.612 117.947 1.00 12.51 ? 77  ASN B ND2   1 
ATOM   2807 N  N     . THR D 2 78  ? 31.306  31.726 119.620 1.00 13.49 ? 78  THR B N     1 
ATOM   2808 C  CA    . THR D 2 78  ? 30.533  32.385 120.681 1.00 14.56 ? 78  THR B CA    1 
ATOM   2809 C  C     . THR D 2 78  ? 29.049  32.162 120.435 1.00 15.72 ? 78  THR B C     1 
ATOM   2810 O  O     . THR D 2 78  ? 28.627  32.215 119.253 1.00 17.39 ? 78  THR B O     1 
ATOM   2811 C  CB    . THR D 2 78  ? 30.886  33.872 120.801 1.00 14.92 ? 78  THR B CB    1 
ATOM   2812 O  OG1   . THR D 2 78  ? 29.985  34.659 120.048 1.00 14.04 ? 78  THR B OG1   1 
ATOM   2813 C  CG2   . THR D 2 78  ? 32.304  34.193 120.327 1.00 15.15 ? 78  THR B CG2   1 
ATOM   2814 N  N     . ASP D 2 79  ? 28.294  31.895 121.475 1.00 15.79 ? 79  ASP B N     1 
ATOM   2815 C  CA    . ASP D 2 79  ? 26.878  31.633 121.468 1.00 16.89 ? 79  ASP B CA    1 
ATOM   2816 C  C     . ASP D 2 79  ? 25.989  32.639 120.716 1.00 16.68 ? 79  ASP B C     1 
ATOM   2817 O  O     . ASP D 2 79  ? 25.870  33.809 121.117 1.00 17.24 ? 79  ASP B O     1 
ATOM   2818 C  CB    . ASP D 2 79  ? 26.352  31.502 122.933 1.00 21.02 ? 79  ASP B CB    1 
ATOM   2819 C  CG    . ASP D 2 79  ? 25.171  30.533 123.013 1.00 24.31 ? 79  ASP B CG    1 
ATOM   2820 O  OD1   . ASP D 2 79  ? 24.167  30.678 122.213 1.00 24.73 ? 79  ASP B OD1   1 
ATOM   2821 O  OD2   . ASP D 2 79  ? 25.182  29.568 123.866 1.00 26.55 ? 79  ASP B OD2   1 
ATOM   2822 N  N     . PRO D 2 80  ? 25.353  32.156 119.616 1.00 15.56 ? 80  PRO B N     1 
ATOM   2823 C  CA    . PRO D 2 80  ? 24.426  32.942 118.789 1.00 14.86 ? 80  PRO B CA    1 
ATOM   2824 C  C     . PRO D 2 80  ? 23.162  33.350 119.529 1.00 14.85 ? 80  PRO B C     1 
ATOM   2825 O  O     . PRO D 2 80  ? 22.737  34.545 119.422 1.00 14.49 ? 80  PRO B O     1 
ATOM   2826 C  CB    . PRO D 2 80  ? 24.048  32.009 117.661 1.00 14.94 ? 80  PRO B CB    1 
ATOM   2827 C  CG    . PRO D 2 80  ? 24.759  30.686 117.890 1.00 15.10 ? 80  PRO B CG    1 
ATOM   2828 C  CD    . PRO D 2 80  ? 25.566  30.782 119.145 1.00 15.17 ? 80  PRO B CD    1 
ATOM   2829 N  N     . GLY D 2 81  ? 22.574  32.390 120.227 1.00 14.26 ? 81  GLY B N     1 
ATOM   2830 C  CA    . GLY D 2 81  ? 21.325  32.601 120.991 1.00 14.01 ? 81  GLY B CA    1 
ATOM   2831 C  C     . GLY D 2 81  ? 21.019  34.098 121.094 1.00 13.95 ? 81  GLY B C     1 
ATOM   2832 O  O     . GLY D 2 81  ? 21.900  34.914 121.402 1.00 14.52 ? 81  GLY B O     1 
ATOM   2833 N  N     . LYS D 2 82  ? 19.768  34.434 120.832 1.00 13.30 ? 82  LYS B N     1 
ATOM   2834 C  CA    . LYS D 2 82  ? 19.318  35.829 120.887 1.00 13.24 ? 82  LYS B CA    1 
ATOM   2835 C  C     . LYS D 2 82  ? 17.832  35.927 121.229 1.00 14.16 ? 82  LYS B C     1 
ATOM   2836 O  O     . LYS D 2 82  ? 17.160  36.909 120.893 1.00 14.97 ? 82  LYS B O     1 
ATOM   2837 C  CB    . LYS D 2 82  ? 19.548  36.523 119.546 1.00 11.04 ? 82  LYS B CB    1 
ATOM   2838 C  CG    . LYS D 2 82  ? 19.530  35.563 118.359 1.00 0.00  ? 82  LYS B CG    1 
ATOM   2839 C  CD    . LYS D 2 82  ? 20.558  35.925 117.287 1.00 0.00  ? 82  LYS B CD    1 
ATOM   2840 C  CE    . LYS D 2 82  ? 20.536  37.408 116.912 1.00 0.00  ? 82  LYS B CE    1 
ATOM   2841 N  NZ    . LYS D 2 82  ? 20.732  37.639 115.473 1.00 0.00  ? 82  LYS B NZ    1 
ATOM   2842 N  N     . GLY D 2 83  ? 17.330  34.909 121.890 1.00 13.92 ? 83  GLY B N     1 
ATOM   2843 C  CA    . GLY D 2 83  ? 15.934  34.912 122.341 1.00 13.31 ? 83  GLY B CA    1 
ATOM   2844 C  C     . GLY D 2 83  ? 15.069  33.939 121.546 1.00 12.80 ? 83  GLY B C     1 
ATOM   2845 O  O     . GLY D 2 83  ? 15.490  33.413 120.501 1.00 13.80 ? 83  GLY B O     1 
ATOM   2846 N  N     . ILE D 2 84  ? 13.882  33.775 122.102 1.00 10.91 ? 84  ILE B N     1 
ATOM   2847 C  CA    . ILE D 2 84  ? 12.860  32.863 121.597 1.00 10.34 ? 84  ILE B CA    1 
ATOM   2848 C  C     . ILE D 2 84  ? 11.951  33.539 120.589 1.00 10.59 ? 84  ILE B C     1 
ATOM   2849 O  O     . ILE D 2 84  ? 11.136  34.402 120.983 1.00 11.25 ? 84  ILE B O     1 
ATOM   2850 C  CB    . ILE D 2 84  ? 12.032  32.329 122.766 1.00 9.46  ? 84  ILE B CB    1 
ATOM   2851 C  CG1   . ILE D 2 84  ? 12.866  31.486 123.736 1.00 9.77  ? 84  ILE B CG1   1 
ATOM   2852 C  CG2   . ILE D 2 84  ? 10.875  31.433 122.322 1.00 7.36  ? 84  ILE B CG2   1 
ATOM   2853 C  CD1   . ILE D 2 84  ? 12.235  31.362 125.123 1.00 25.00 ? 84  ILE B CD1   1 
ATOM   2854 N  N     . PRO D 2 85  ? 12.043  33.132 119.334 1.00 10.91 ? 85  PRO B N     1 
ATOM   2855 C  CA    . PRO D 2 85  ? 11.269  33.681 118.230 1.00 12.05 ? 85  PRO B CA    1 
ATOM   2856 C  C     . PRO D 2 85  ? 9.799   33.321 118.151 1.00 13.93 ? 85  PRO B C     1 
ATOM   2857 O  O     . PRO D 2 85  ? 9.288   32.939 117.074 1.00 16.00 ? 85  PRO B O     1 
ATOM   2858 C  CB    . PRO D 2 85  ? 12.033  33.208 116.982 1.00 11.59 ? 85  PRO B CB    1 
ATOM   2859 C  CG    . PRO D 2 85  ? 12.601  31.873 117.431 1.00 11.10 ? 85  PRO B CG    1 
ATOM   2860 C  CD    . PRO D 2 85  ? 13.018  32.122 118.872 1.00 10.71 ? 85  PRO B CD    1 
ATOM   2861 N  N     . ASP D 2 86  ? 9.115   33.489 119.272 1.00 14.09 ? 86  ASP B N     1 
ATOM   2862 C  CA    . ASP D 2 86  ? 7.669   33.264 119.401 1.00 12.89 ? 86  ASP B CA    1 
ATOM   2863 C  C     . ASP D 2 86  ? 7.004   34.662 119.379 1.00 13.40 ? 86  ASP B C     1 
ATOM   2864 O  O     . ASP D 2 86  ? 7.699   35.639 119.068 1.00 15.04 ? 86  ASP B O     1 
ATOM   2865 C  CB    . ASP D 2 86  ? 7.200   32.441 120.558 1.00 12.06 ? 86  ASP B CB    1 
ATOM   2866 C  CG    . ASP D 2 86  ? 7.543   32.996 121.927 1.00 15.46 ? 86  ASP B CG    1 
ATOM   2867 O  OD1   . ASP D 2 86  ? 8.305   33.979 121.985 1.00 18.35 ? 86  ASP B OD1   1 
ATOM   2868 O  OD2   . ASP D 2 86  ? 7.052   32.370 122.915 1.00 16.67 ? 86  ASP B OD2   1 
ATOM   2869 N  N     . ARG D 2 87  ? 5.740   34.696 119.702 1.00 12.38 ? 87  ARG B N     1 
ATOM   2870 C  CA    . ARG D 2 87  ? 4.902   35.880 119.706 1.00 11.44 ? 87  ARG B CA    1 
ATOM   2871 C  C     . ARG D 2 87  ? 5.289   36.977 120.667 1.00 11.55 ? 87  ARG B C     1 
ATOM   2872 O  O     . ARG D 2 87  ? 5.206   38.150 120.257 1.00 13.01 ? 87  ARG B O     1 
ATOM   2873 C  CB    . ARG D 2 87  ? 3.428   35.509 119.976 1.00 12.66 ? 87  ARG B CB    1 
ATOM   2874 C  CG    . ARG D 2 87  ? 2.438   36.442 119.325 1.00 16.11 ? 87  ARG B CG    1 
ATOM   2875 C  CD    . ARG D 2 87  ? 2.148   36.119 117.899 1.00 17.19 ? 87  ARG B CD    1 
ATOM   2876 N  NE    . ARG D 2 87  ? 0.943   35.311 117.734 1.00 16.52 ? 87  ARG B NE    1 
ATOM   2877 C  CZ    . ARG D 2 87  ? 0.364   34.975 116.575 1.00 15.94 ? 87  ARG B CZ    1 
ATOM   2878 N  NH1   . ARG D 2 87  ? 0.804   35.328 115.368 1.00 12.64 ? 87  ARG B NH1   1 
ATOM   2879 N  NH2   . ARG D 2 87  ? -0.756  34.241 116.644 1.00 15.81 ? 87  ARG B NH2   1 
ATOM   2880 N  N     . PHE D 2 88  ? 5.661   36.695 121.882 1.00 11.53 ? 88  PHE B N     1 
ATOM   2881 C  CA    . PHE D 2 88  ? 6.040   37.742 122.881 1.00 11.05 ? 88  PHE B CA    1 
ATOM   2882 C  C     . PHE D 2 88  ? 7.251   38.533 122.396 1.00 11.44 ? 88  PHE B C     1 
ATOM   2883 O  O     . PHE D 2 88  ? 8.229   37.997 121.796 1.00 12.99 ? 88  PHE B O     1 
ATOM   2884 C  CB    . PHE D 2 88  ? 6.173   37.065 124.251 1.00 6.97  ? 88  PHE B CB    1 
ATOM   2885 C  CG    . PHE D 2 88  ? 6.871   37.889 125.291 1.00 3.72  ? 88  PHE B CG    1 
ATOM   2886 C  CD1   . PHE D 2 88  ? 8.253   37.928 125.357 1.00 3.76  ? 88  PHE B CD1   1 
ATOM   2887 C  CD2   . PHE D 2 88  ? 6.118   38.634 126.191 1.00 3.70  ? 88  PHE B CD2   1 
ATOM   2888 C  CE1   . PHE D 2 88  ? 8.893   38.720 126.322 1.00 3.99  ? 88  PHE B CE1   1 
ATOM   2889 C  CE2   . PHE D 2 88  ? 6.729   39.432 127.130 1.00 4.10  ? 88  PHE B CE2   1 
ATOM   2890 C  CZ    . PHE D 2 88  ? 8.123   39.469 127.208 1.00 3.13  ? 88  PHE B CZ    1 
ATOM   2891 N  N     . GLU D 2 89  ? 7.221   39.851 122.603 1.00 11.31 ? 89  GLU B N     1 
ATOM   2892 C  CA    . GLU D 2 89  ? 8.334   40.733 122.202 1.00 11.23 ? 89  GLU B CA    1 
ATOM   2893 C  C     . GLU D 2 89  ? 8.591   41.805 123.273 1.00 11.25 ? 89  GLU B C     1 
ATOM   2894 O  O     . GLU D 2 89  ? 9.004   42.947 122.999 1.00 11.78 ? 89  GLU B O     1 
ATOM   2895 C  CB    . GLU D 2 89  ? 8.218   41.399 120.857 1.00 11.11 ? 89  GLU B CB    1 
ATOM   2896 C  CG    . GLU D 2 89  ? 7.720   40.573 119.681 1.00 12.17 ? 89  GLU B CG    1 
ATOM   2897 C  CD    . GLU D 2 89  ? 7.652   41.313 118.369 1.00 14.04 ? 89  GLU B CD    1 
ATOM   2898 O  OE1   . GLU D 2 89  ? 8.582   42.162 118.260 1.00 13.83 ? 89  GLU B OE1   1 
ATOM   2899 O  OE2   . GLU D 2 89  ? 6.774   41.065 117.543 1.00 17.12 ? 89  GLU B OE2   1 
ATOM   2900 N  N     . GLY D 2 90  ? 8.371   41.367 124.511 1.00 10.57 ? 90  GLY B N     1 
ATOM   2901 C  CA    . GLY D 2 90  ? 8.556   42.191 125.698 1.00 11.04 ? 90  GLY B CA    1 
ATOM   2902 C  C     . GLY D 2 90  ? 10.046  42.365 125.983 1.00 10.76 ? 90  GLY B C     1 
ATOM   2903 O  O     . GLY D 2 90  ? 10.858  41.779 125.262 1.00 11.52 ? 90  GLY B O     1 
ATOM   2904 N  N     . LYS D 2 91  ? 10.283  43.184 127.001 1.00 9.84  ? 91  LYS B N     1 
ATOM   2905 C  CA    . LYS D 2 91  ? 11.631  43.484 127.486 1.00 9.19  ? 91  LYS B CA    1 
ATOM   2906 C  C     . LYS D 2 91  ? 12.152  42.241 128.214 1.00 10.28 ? 91  LYS B C     1 
ATOM   2907 O  O     . LYS D 2 91  ? 11.436  41.650 129.052 1.00 11.10 ? 91  LYS B O     1 
ATOM   2908 C  CB    . LYS D 2 91  ? 11.748  44.606 128.494 1.00 6.91  ? 91  LYS B CB    1 
ATOM   2909 C  CG    . LYS D 2 91  ? 12.569  45.804 127.995 1.00 7.02  ? 91  LYS B CG    1 
ATOM   2910 C  CD    . LYS D 2 91  ? 14.057  45.577 128.182 1.00 7.08  ? 91  LYS B CD    1 
ATOM   2911 C  CE    . LYS D 2 91  ? 14.799  46.893 128.209 1.00 7.96  ? 91  LYS B CE    1 
ATOM   2912 N  NZ    . LYS D 2 91  ? 14.808  47.561 126.890 1.00 11.15 ? 91  LYS B NZ    1 
ATOM   2913 N  N     . VAL D 2 92  ? 13.364  41.886 127.845 1.00 10.83 ? 92  VAL B N     1 
ATOM   2914 C  CA    . VAL D 2 92  ? 14.007  40.720 128.456 1.00 11.50 ? 92  VAL B CA    1 
ATOM   2915 C  C     . VAL D 2 92  ? 15.529  40.944 128.412 1.00 12.56 ? 92  VAL B C     1 
ATOM   2916 O  O     . VAL D 2 92  ? 16.051  41.845 127.771 1.00 12.93 ? 92  VAL B O     1 
ATOM   2917 C  CB    . VAL D 2 92  ? 13.698  39.403 127.699 1.00 9.57  ? 92  VAL B CB    1 
ATOM   2918 C  CG1   . VAL D 2 92  ? 12.243  39.161 127.379 1.00 9.29  ? 92  VAL B CG1   1 
ATOM   2919 C  CG2   . VAL D 2 92  ? 14.600  39.325 126.461 1.00 7.71  ? 92  VAL B CG2   1 
ATOM   2920 N  N     . VAL D 2 93  ? 16.122  40.002 129.106 1.00 12.53 ? 93  VAL B N     1 
ATOM   2921 C  CA    . VAL D 2 93  ? 17.579  39.850 129.187 1.00 12.46 ? 93  VAL B CA    1 
ATOM   2922 C  C     . VAL D 2 93  ? 17.810  38.341 128.971 1.00 11.89 ? 93  VAL B C     1 
ATOM   2923 O  O     . VAL D 2 93  ? 17.277  37.512 129.742 1.00 12.40 ? 93  VAL B O     1 
ATOM   2924 C  CB    . VAL D 2 93  ? 18.212  40.425 130.446 1.00 12.08 ? 93  VAL B CB    1 
ATOM   2925 C  CG1   . VAL D 2 93  ? 18.052  41.937 130.529 1.00 10.46 ? 93  VAL B CG1   1 
ATOM   2926 C  CG2   . VAL D 2 93  ? 17.726  39.721 131.697 1.00 10.82 ? 93  VAL B CG2   1 
ATOM   2927 N  N     . THR D 2 94  ? 18.508  38.089 127.875 1.00 10.91 ? 94  THR B N     1 
ATOM   2928 C  CA    . THR D 2 94  ? 18.818  36.661 127.561 1.00 10.47 ? 94  THR B CA    1 
ATOM   2929 C  C     . THR D 2 94  ? 20.136  36.386 128.281 1.00 9.66  ? 94  THR B C     1 
ATOM   2930 O  O     . THR D 2 94  ? 21.111  37.153 128.156 1.00 9.64  ? 94  THR B O     1 
ATOM   2931 C  CB    . THR D 2 94  ? 18.783  36.374 126.031 1.00 12.32 ? 94  THR B CB    1 
ATOM   2932 O  OG1   . THR D 2 94  ? 19.758  37.278 125.410 1.00 13.75 ? 94  THR B OG1   1 
ATOM   2933 C  CG2   . THR D 2 94  ? 17.425  36.546 125.331 1.00 13.49 ? 94  THR B CG2   1 
ATOM   2934 N  N     . ARG D 2 95  ? 20.169  35.354 129.101 1.00 9.81  ? 95  ARG B N     1 
ATOM   2935 C  CA    . ARG D 2 95  ? 21.381  34.990 129.850 1.00 9.35  ? 95  ARG B CA    1 
ATOM   2936 C  C     . ARG D 2 95  ? 21.811  33.593 129.396 1.00 10.10 ? 95  ARG B C     1 
ATOM   2937 O  O     . ARG D 2 95  ? 20.977  32.683 129.254 1.00 10.97 ? 95  ARG B O     1 
ATOM   2938 C  CB    . ARG D 2 95  ? 21.229  35.036 131.354 1.00 6.89  ? 95  ARG B CB    1 
ATOM   2939 C  CG    . ARG D 2 95  ? 22.447  34.514 132.111 1.00 6.75  ? 95  ARG B CG    1 
ATOM   2940 C  CD    . ARG D 2 95  ? 22.898  35.465 133.166 1.00 5.05  ? 95  ARG B CD    1 
ATOM   2941 N  NE    . ARG D 2 95  ? 23.945  34.934 134.003 1.00 6.66  ? 95  ARG B NE    1 
ATOM   2942 C  CZ    . ARG D 2 95  ? 24.868  35.665 134.615 1.00 9.52  ? 95  ARG B CZ    1 
ATOM   2943 N  NH1   . ARG D 2 95  ? 24.859  36.991 134.486 1.00 8.36  ? 95  ARG B NH1   1 
ATOM   2944 N  NH2   . ARG D 2 95  ? 25.848  35.137 135.365 1.00 13.63 ? 95  ARG B NH2   1 
ATOM   2945 N  N     . LYS D 2 96  ? 23.097  33.502 129.168 1.00 9.72  ? 96  LYS B N     1 
ATOM   2946 C  CA    . LYS D 2 96  ? 23.717  32.240 128.728 1.00 10.26 ? 96  LYS B CA    1 
ATOM   2947 C  C     . LYS D 2 96  ? 24.712  31.787 129.785 1.00 10.22 ? 96  LYS B C     1 
ATOM   2948 O  O     . LYS D 2 96  ? 25.869  32.228 129.934 1.00 10.41 ? 96  LYS B O     1 
ATOM   2949 C  CB    . LYS D 2 96  ? 24.292  32.381 127.333 1.00 10.73 ? 96  LYS B CB    1 
ATOM   2950 C  CG    . LYS D 2 96  ? 23.377  33.228 126.439 1.00 12.28 ? 96  LYS B CG    1 
ATOM   2951 C  CD    . LYS D 2 96  ? 23.405  32.736 124.988 1.00 14.12 ? 96  LYS B CD    1 
ATOM   2952 C  CE    . LYS D 2 96  ? 23.640  33.932 124.052 1.00 15.78 ? 96  LYS B CE    1 
ATOM   2953 N  NZ    . LYS D 2 96  ? 23.393  35.207 124.803 1.00 16.68 ? 96  LYS B NZ    1 
ATOM   2954 N  N     . ASP D 2 97  ? 24.176  30.888 130.590 1.00 9.42  ? 97  ASP B N     1 
ATOM   2955 C  CA    . ASP D 2 97  ? 24.909  30.284 131.697 1.00 8.70  ? 97  ASP B CA    1 
ATOM   2956 C  C     . ASP D 2 97  ? 25.744  29.119 131.153 1.00 8.80  ? 97  ASP B C     1 
ATOM   2957 O  O     . ASP D 2 97  ? 25.206  28.294 130.410 1.00 9.41  ? 97  ASP B O     1 
ATOM   2958 C  CB    . ASP D 2 97  ? 23.895  29.798 132.733 1.00 9.22  ? 97  ASP B CB    1 
ATOM   2959 C  CG    . ASP D 2 97  ? 23.029  30.882 133.321 1.00 12.17 ? 97  ASP B CG    1 
ATOM   2960 O  OD1   . ASP D 2 97  ? 23.683  31.860 133.741 1.00 13.86 ? 97  ASP B OD1   1 
ATOM   2961 O  OD2   . ASP D 2 97  ? 21.784  30.761 133.430 1.00 13.03 ? 97  ASP B OD2   1 
ATOM   2962 N  N     . VAL D 2 98  ? 27.001  29.070 131.530 1.00 8.41  ? 98  VAL B N     1 
ATOM   2963 C  CA    . VAL D 2 98  ? 27.880  27.968 131.150 1.00 9.26  ? 98  VAL B CA    1 
ATOM   2964 C  C     . VAL D 2 98  ? 28.615  27.557 132.445 1.00 9.68  ? 98  VAL B C     1 
ATOM   2965 O  O     . VAL D 2 98  ? 28.966  28.496 133.175 1.00 10.06 ? 98  VAL B O     1 
ATOM   2966 C  CB    . VAL D 2 98  ? 28.900  28.291 130.043 1.00 10.09 ? 98  VAL B CB    1 
ATOM   2967 C  CG1   . VAL D 2 98  ? 29.820  27.111 129.709 1.00 10.27 ? 98  VAL B CG1   1 
ATOM   2968 C  CG2   . VAL D 2 98  ? 28.226  28.760 128.769 1.00 9.78  ? 98  VAL B CG2   1 
ATOM   2969 N  N     . LEU D 2 99  ? 28.795  26.266 132.621 1.00 9.72  ? 99  LEU B N     1 
ATOM   2970 C  CA    . LEU D 2 99  ? 29.563  25.733 133.733 1.00 9.54  ? 99  LEU B CA    1 
ATOM   2971 C  C     . LEU D 2 99  ? 30.582  24.741 133.136 1.00 9.71  ? 99  LEU B C     1 
ATOM   2972 O  O     . LEU D 2 99  ? 30.201  23.863 132.352 1.00 11.02 ? 99  LEU B O     1 
ATOM   2973 C  CB    . LEU D 2 99  ? 28.733  25.119 134.849 1.00 9.86  ? 99  LEU B CB    1 
ATOM   2974 C  CG    . LEU D 2 99  ? 29.612  24.601 136.003 1.00 9.71  ? 99  LEU B CG    1 
ATOM   2975 C  CD1   . LEU D 2 99  ? 30.506  25.709 136.547 1.00 9.88  ? 99  LEU B CD1   1 
ATOM   2976 C  CD2   . LEU D 2 99  ? 28.709  24.065 137.108 1.00 9.95  ? 99  LEU B CD2   1 
ATOM   2977 N  N     . ASN D 2 100 ? 31.832  24.910 133.456 1.00 8.99  ? 100 ASN B N     1 
ATOM   2978 C  CA    . ASN D 2 100 ? 32.945  24.054 133.037 1.00 7.91  ? 100 ASN B CA    1 
ATOM   2979 C  C     . ASN D 2 100 ? 33.472  23.490 134.371 1.00 8.48  ? 100 ASN B C     1 
ATOM   2980 O  O     . ASN D 2 100 ? 33.777  24.291 135.277 1.00 8.97  ? 100 ASN B O     1 
ATOM   2981 C  CB    . ASN D 2 100 ? 34.056  24.797 132.337 1.00 7.76  ? 100 ASN B CB    1 
ATOM   2982 C  CG    . ASN D 2 100 ? 33.931  24.914 130.840 1.00 9.08  ? 100 ASN B CG    1 
ATOM   2983 O  OD1   . ASN D 2 100 ? 33.025  25.633 130.384 1.00 9.68  ? 100 ASN B OD1   1 
ATOM   2984 N  ND2   . ASN D 2 100 ? 34.820  24.232 130.121 1.00 8.35  ? 100 ASN B ND2   1 
ATOM   2985 N  N     . GLN D 2 101 ? 33.588  22.193 134.425 1.00 9.07  ? 101 GLN B N     1 
ATOM   2986 C  CA    . GLN D 2 101 ? 34.083  21.598 135.687 1.00 10.04 ? 101 GLN B CA    1 
ATOM   2987 C  C     . GLN D 2 101 ? 34.886  20.335 135.511 1.00 10.77 ? 101 GLN B C     1 
ATOM   2988 O  O     . GLN D 2 101 ? 34.490  19.380 134.843 1.00 10.69 ? 101 GLN B O     1 
ATOM   2989 C  CB    . GLN D 2 101 ? 32.856  21.403 136.589 1.00 9.07  ? 101 GLN B CB    1 
ATOM   2990 C  CG    . GLN D 2 101 ? 33.325  21.518 138.037 1.00 11.98 ? 101 GLN B CG    1 
ATOM   2991 C  CD    . GLN D 2 101 ? 32.058  21.448 138.879 1.00 15.27 ? 101 GLN B CD    1 
ATOM   2992 O  OE1   . GLN D 2 101 ? 31.451  20.365 138.841 1.00 15.12 ? 101 GLN B OE1   1 
ATOM   2993 N  NE2   . GLN D 2 101 ? 31.785  22.590 139.490 1.00 14.77 ? 101 GLN B NE2   1 
ATOM   2994 N  N     . SER D 2 102 ? 36.060  20.339 136.102 1.00 11.34 ? 102 SER B N     1 
ATOM   2995 C  CA    . SER D 2 102 ? 36.969  19.161 136.077 1.00 12.04 ? 102 SER B CA    1 
ATOM   2996 C  C     . SER D 2 102 ? 36.401  18.303 137.203 1.00 13.87 ? 102 SER B C     1 
ATOM   2997 O  O     . SER D 2 102 ? 36.199  18.885 138.296 1.00 16.13 ? 102 SER B O     1 
ATOM   2998 C  CB    . SER D 2 102 ? 38.370  19.606 136.395 1.00 9.42  ? 102 SER B CB    1 
ATOM   2999 O  OG    . SER D 2 102 ? 38.837  20.410 135.283 1.00 9.92  ? 102 SER B OG    1 
ATOM   3000 N  N     . ILE D 2 103 ? 36.123  17.053 136.919 1.00 13.12 ? 103 ILE B N     1 
ATOM   3001 C  CA    . ILE D 2 103 ? 35.519  16.181 137.955 1.00 12.53 ? 103 ILE B CA    1 
ATOM   3002 C  C     . ILE D 2 103 ? 35.965  14.741 137.814 1.00 12.99 ? 103 ILE B C     1 
ATOM   3003 O  O     . ILE D 2 103 ? 36.008  14.222 136.691 1.00 14.31 ? 103 ILE B O     1 
ATOM   3004 C  CB    . ILE D 2 103 ? 33.969  16.364 137.842 1.00 10.90 ? 103 ILE B CB    1 
ATOM   3005 C  CG1   . ILE D 2 103 ? 33.184  15.248 138.577 1.00 12.18 ? 103 ILE B CG1   1 
ATOM   3006 C  CG2   . ILE D 2 103 ? 33.492  16.440 136.358 1.00 9.28  ? 103 ILE B CG2   1 
ATOM   3007 C  CD1   . ILE D 2 103 ? 31.657  15.350 138.217 1.00 14.89 ? 103 ILE B CD1   1 
ATOM   3008 N  N     . ASN D 2 104 ? 36.280  14.155 138.962 1.00 12.43 ? 104 ASN B N     1 
ATOM   3009 C  CA    . ASN D 2 104 ? 36.689  12.745 139.034 1.00 11.60 ? 104 ASN B CA    1 
ATOM   3010 C  C     . ASN D 2 104 ? 35.540  11.964 139.695 1.00 10.19 ? 104 ASN B C     1 
ATOM   3011 O  O     . ASN D 2 104 ? 35.224  12.114 140.888 1.00 11.20 ? 104 ASN B O     1 
ATOM   3012 C  CB    . ASN D 2 104 ? 37.972  12.536 139.806 1.00 13.71 ? 104 ASN B CB    1 
ATOM   3013 C  CG    . ASN D 2 104 ? 39.149  13.324 139.307 1.00 16.29 ? 104 ASN B CG    1 
ATOM   3014 O  OD1   . ASN D 2 104 ? 39.783  12.882 138.335 1.00 17.05 ? 104 ASN B OD1   1 
ATOM   3015 N  ND2   . ASN D 2 104 ? 39.443  14.456 139.934 1.00 16.92 ? 104 ASN B ND2   1 
ATOM   3016 N  N     . PHE D 2 105 ? 34.949  11.118 138.882 1.00 8.56  ? 105 PHE B N     1 
ATOM   3017 C  CA    . PHE D 2 105 ? 33.818  10.297 139.440 1.00 8.16  ? 105 PHE B CA    1 
ATOM   3018 C  C     . PHE D 2 105 ? 34.411  9.343  140.466 1.00 8.45  ? 105 PHE B C     1 
ATOM   3019 O  O     . PHE D 2 105 ? 35.403  8.651  140.205 1.00 8.69  ? 105 PHE B O     1 
ATOM   3020 C  CB    . PHE D 2 105 ? 33.097  9.677  138.252 1.00 6.57  ? 105 PHE B CB    1 
ATOM   3021 C  CG    . PHE D 2 105 ? 32.431  10.744 137.392 1.00 6.35  ? 105 PHE B CG    1 
ATOM   3022 C  CD1   . PHE D 2 105 ? 31.252  11.351 137.835 1.00 6.06  ? 105 PHE B CD1   1 
ATOM   3023 C  CD2   . PHE D 2 105 ? 33.005  11.120 136.175 1.00 7.70  ? 105 PHE B CD2   1 
ATOM   3024 C  CE1   . PHE D 2 105 ? 30.645  12.341 137.056 1.00 7.14  ? 105 PHE B CE1   1 
ATOM   3025 C  CE2   . PHE D 2 105 ? 32.398  12.109 135.395 1.00 8.27  ? 105 PHE B CE2   1 
ATOM   3026 C  CZ    . PHE D 2 105 ? 31.218  12.720 135.836 1.00 7.92  ? 105 PHE B CZ    1 
ATOM   3027 N  N     . THR D 2 106 ? 33.797  9.367  141.627 1.00 8.25  ? 106 THR B N     1 
ATOM   3028 C  CA    . THR D 2 106 ? 34.224  8.547  142.755 1.00 9.08  ? 106 THR B CA    1 
ATOM   3029 C  C     . THR D 2 106 ? 34.083  7.061  142.349 1.00 9.21  ? 106 THR B C     1 
ATOM   3030 O  O     . THR D 2 106 ? 33.048  6.634  141.822 1.00 9.56  ? 106 THR B O     1 
ATOM   3031 C  CB    . THR D 2 106 ? 33.397  8.956  143.981 1.00 10.03 ? 106 THR B CB    1 
ATOM   3032 O  OG1   . THR D 2 106 ? 33.443  10.379 144.160 1.00 13.78 ? 106 THR B OG1   1 
ATOM   3033 C  CG2   . THR D 2 106 ? 33.914  8.326  145.267 1.00 9.13  ? 106 THR B CG2   1 
ATOM   3034 N  N     . ALA D 2 107 ? 35.149  6.305  142.598 1.00 8.46  ? 107 ALA B N     1 
ATOM   3035 C  CA    . ALA D 2 107 ? 35.246  4.877  142.206 1.00 8.42  ? 107 ALA B CA    1 
ATOM   3036 C  C     . ALA D 2 107 ? 34.345  3.971  143.059 1.00 8.84  ? 107 ALA B C     1 
ATOM   3037 O  O     . ALA D 2 107 ? 34.180  4.186  144.268 1.00 9.49  ? 107 ALA B O     1 
ATOM   3038 C  CB    . ALA D 2 107 ? 36.686  4.384  142.356 1.00 7.41  ? 107 ALA B CB    1 
ATOM   3039 N  N     . ASN D 2 108 ? 33.810  2.979  142.362 1.00 8.83  ? 108 ASN B N     1 
ATOM   3040 C  CA    . ASN D 2 108 ? 32.916  1.953  142.926 1.00 8.45  ? 108 ASN B CA    1 
ATOM   3041 C  C     . ASN D 2 108 ? 31.602  2.570  143.410 1.00 8.71  ? 108 ASN B C     1 
ATOM   3042 O  O     . ASN D 2 108 ? 30.964  2.066  144.344 1.00 9.83  ? 108 ASN B O     1 
ATOM   3043 C  CB    . ASN D 2 108 ? 33.575  1.248  144.111 1.00 8.15  ? 108 ASN B CB    1 
ATOM   3044 C  CG    . ASN D 2 108 ? 32.762  0.048  144.608 1.00 10.36 ? 108 ASN B CG    1 
ATOM   3045 O  OD1   . ASN D 2 108 ? 32.157  -0.661 143.803 1.00 11.63 ? 108 ASN B OD1   1 
ATOM   3046 N  ND2   . ASN D 2 108 ? 32.706  -0.226 145.898 1.00 9.58  ? 108 ASN B ND2   1 
ATOM   3047 N  N     . ARG D 2 109 ? 31.219  3.653  142.763 1.00 8.77  ? 109 ARG B N     1 
ATOM   3048 C  CA    . ARG D 2 109 ? 29.964  4.355  143.084 1.00 10.39 ? 109 ARG B CA    1 
ATOM   3049 C  C     . ARG D 2 109 ? 29.219  4.704  141.789 1.00 10.54 ? 109 ARG B C     1 
ATOM   3050 O  O     . ARG D 2 109 ? 29.799  4.689  140.691 1.00 11.22 ? 109 ARG B O     1 
ATOM   3051 C  CB    . ARG D 2 109 ? 30.248  5.657  143.858 1.00 12.38 ? 109 ARG B CB    1 
ATOM   3052 C  CG    . ARG D 2 109 ? 30.426  5.461  145.378 1.00 12.76 ? 109 ARG B CG    1 
ATOM   3053 C  CD    . ARG D 2 109 ? 29.105  5.263  146.143 1.00 14.70 ? 109 ARG B CD    1 
ATOM   3054 N  NE    . ARG D 2 109 ? 28.715  6.411  146.991 1.00 17.95 ? 109 ARG B NE    1 
ATOM   3055 C  CZ    . ARG D 2 109 ? 28.257  6.307  148.258 1.00 18.55 ? 109 ARG B CZ    1 
ATOM   3056 N  NH1   . ARG D 2 109 ? 28.164  5.119  148.876 1.00 21.57 ? 109 ARG B NH1   1 
ATOM   3057 N  NH2   . ARG D 2 109 ? 27.829  7.347  148.990 1.00 16.47 ? 109 ARG B NH2   1 
ATOM   3058 N  N     . ASP D 2 110 ? 27.941  4.993  141.965 1.00 9.73  ? 110 ASP B N     1 
ATOM   3059 C  CA    . ASP D 2 110 ? 27.052  5.417  140.872 1.00 9.27  ? 110 ASP B CA    1 
ATOM   3060 C  C     . ASP D 2 110 ? 26.675  6.887  141.132 1.00 9.40  ? 110 ASP B C     1 
ATOM   3061 O  O     . ASP D 2 110 ? 25.944  7.184  142.082 1.00 10.24 ? 110 ASP B O     1 
ATOM   3062 C  CB    . ASP D 2 110 ? 25.830  4.515  140.804 1.00 10.23 ? 110 ASP B CB    1 
ATOM   3063 C  CG    . ASP D 2 110 ? 26.092  3.287  139.940 1.00 12.78 ? 110 ASP B CG    1 
ATOM   3064 O  OD1   . ASP D 2 110 ? 27.302  2.866  139.788 1.00 13.54 ? 110 ASP B OD1   1 
ATOM   3065 O  OD2   . ASP D 2 110 ? 25.114  2.681  139.367 1.00 15.63 ? 110 ASP B OD2   1 
ATOM   3066 N  N     . THR D 2 111 ? 27.202  7.744  140.293 1.00 8.85  ? 111 THR B N     1 
ATOM   3067 C  CA    . THR D 2 111 ? 26.947  9.185  140.419 1.00 8.62  ? 111 THR B CA    1 
ATOM   3068 C  C     . THR D 2 111 ? 25.720  9.482  139.550 1.00 9.42  ? 111 THR B C     1 
ATOM   3069 O  O     . THR D 2 111 ? 25.701  9.058  138.393 1.00 9.93  ? 111 THR B O     1 
ATOM   3070 C  CB    . THR D 2 111 ? 28.175  10.069 140.033 1.00 8.42  ? 111 THR B CB    1 
ATOM   3071 O  OG1   . THR D 2 111 ? 29.295  9.618  140.839 1.00 8.22  ? 111 THR B OG1   1 
ATOM   3072 C  CG2   . THR D 2 111 ? 27.980  11.581 140.224 1.00 9.20  ? 111 THR B CG2   1 
ATOM   3073 N  N     . PHE D 2 112 ? 24.809  10.160 140.209 1.00 8.97  ? 112 PHE B N     1 
ATOM   3074 C  CA    . PHE D 2 112 ? 23.564  10.555 139.538 1.00 8.64  ? 112 PHE B CA    1 
ATOM   3075 C  C     . PHE D 2 112 ? 23.604  12.074 139.361 1.00 9.36  ? 112 PHE B C     1 
ATOM   3076 O  O     . PHE D 2 112 ? 23.786  12.773 140.374 1.00 10.22 ? 112 PHE B O     1 
ATOM   3077 C  CB    . PHE D 2 112 ? 22.357  10.044 140.292 1.00 6.61  ? 112 PHE B CB    1 
ATOM   3078 C  CG    . PHE D 2 112 ? 22.029  8.610  139.987 1.00 7.83  ? 112 PHE B CG    1 
ATOM   3079 C  CD1   . PHE D 2 112 ? 22.770  7.586  140.580 1.00 7.77  ? 112 PHE B CD1   1 
ATOM   3080 C  CD2   . PHE D 2 112 ? 20.990  8.294  139.109 1.00 6.72  ? 112 PHE B CD2   1 
ATOM   3081 C  CE1   . PHE D 2 112 ? 22.468  6.256  140.349 1.00 7.70  ? 112 PHE B CE1   1 
ATOM   3082 C  CE2   . PHE D 2 112 ? 20.693  6.955  138.846 1.00 6.82  ? 112 PHE B CE2   1 
ATOM   3083 C  CZ    . PHE D 2 112 ? 21.431  5.938  139.480 1.00 7.26  ? 112 PHE B CZ    1 
ATOM   3084 N  N     . ILE D 2 113 ? 23.496  12.529 138.127 1.00 8.97  ? 113 ILE B N     1 
ATOM   3085 C  CA    . ILE D 2 113 ? 23.510  13.966 137.828 1.00 9.35  ? 113 ILE B CA    1 
ATOM   3086 C  C     . ILE D 2 113 ? 22.165  14.275 137.180 1.00 10.07 ? 113 ILE B C     1 
ATOM   3087 O  O     . ILE D 2 113 ? 21.705  13.507 136.326 1.00 10.89 ? 113 ILE B O     1 
ATOM   3088 C  CB    . ILE D 2 113 ? 24.726  14.390 136.953 1.00 9.48  ? 113 ILE B CB    1 
ATOM   3089 C  CG1   . ILE D 2 113 ? 26.048  14.211 137.721 1.00 8.73  ? 113 ILE B CG1   1 
ATOM   3090 C  CG2   . ILE D 2 113 ? 24.610  15.856 136.466 1.00 9.59  ? 113 ILE B CG2   1 
ATOM   3091 C  CD1   . ILE D 2 113 ? 27.285  13.995 136.807 1.00 9.22  ? 113 ILE B CD1   1 
ATOM   3092 N  N     . LEU D 2 114 ? 21.566  15.366 137.611 1.00 9.20  ? 114 LEU B N     1 
ATOM   3093 C  CA    . LEU D 2 114 ? 20.264  15.791 137.074 1.00 8.33  ? 114 LEU B CA    1 
ATOM   3094 C  C     . LEU D 2 114 ? 20.428  17.173 136.432 1.00 7.76  ? 114 LEU B C     1 
ATOM   3095 O  O     . LEU D 2 114 ? 20.883  18.077 137.146 1.00 8.42  ? 114 LEU B O     1 
ATOM   3096 C  CB    . LEU D 2 114 ? 19.253  15.855 138.209 1.00 8.33  ? 114 LEU B CB    1 
ATOM   3097 C  CG    . LEU D 2 114 ? 19.088  14.729 139.189 1.00 9.11  ? 114 LEU B CG    1 
ATOM   3098 C  CD1   . LEU D 2 114 ? 17.930  15.023 140.148 1.00 8.75  ? 114 LEU B CD1   1 
ATOM   3099 C  CD2   . LEU D 2 114 ? 18.741  13.451 138.396 1.00 8.75  ? 114 LEU B CD2   1 
ATOM   3100 N  N     . ILE D 2 115 ? 20.043  17.298 135.195 1.00 6.84  ? 115 ILE B N     1 
ATOM   3101 C  CA    . ILE D 2 115 ? 20.113  18.643 134.549 1.00 6.99  ? 115 ILE B CA    1 
ATOM   3102 C  C     . ILE D 2 115 ? 18.657  19.111 134.504 1.00 7.49  ? 115 ILE B C     1 
ATOM   3103 O  O     . ILE D 2 115 ? 17.875  18.745 133.614 1.00 7.66  ? 115 ILE B O     1 
ATOM   3104 C  CB    . ILE D 2 115 ? 20.897  18.504 133.226 1.00 6.34  ? 115 ILE B CB    1 
ATOM   3105 C  CG1   . ILE D 2 115 ? 22.188  17.679 133.494 1.00 6.85  ? 115 ILE B CG1   1 
ATOM   3106 C  CG2   . ILE D 2 115 ? 21.195  19.844 132.519 1.00 5.42  ? 115 ILE B CG2   1 
ATOM   3107 C  CD1   . ILE D 2 115 ? 23.487  18.519 133.651 1.00 7.90  ? 115 ILE B CD1   1 
ATOM   3108 N  N     . ALA D 2 116 ? 18.281  19.853 135.535 1.00 7.67  ? 116 ALA B N     1 
ATOM   3109 C  CA    . ALA D 2 116 ? 16.927  20.371 135.739 1.00 8.78  ? 116 ALA B CA    1 
ATOM   3110 C  C     . ALA D 2 116 ? 16.800  21.851 135.388 1.00 9.54  ? 116 ALA B C     1 
ATOM   3111 O  O     . ALA D 2 116 ? 17.814  22.549 135.571 1.00 9.79  ? 116 ALA B O     1 
ATOM   3112 C  CB    . ALA D 2 116 ? 16.618  20.219 137.250 1.00 6.47  ? 116 ALA B CB    1 
ATOM   3113 N  N     . PRO D 2 117 ? 15.608  22.289 134.991 1.00 9.73  ? 117 PRO B N     1 
ATOM   3114 C  CA    . PRO D 2 117 ? 15.328  23.679 134.631 1.00 10.18 ? 117 PRO B CA    1 
ATOM   3115 C  C     . PRO D 2 117 ? 15.061  24.598 135.814 1.00 10.93 ? 117 PRO B C     1 
ATOM   3116 O  O     . PRO D 2 117 ? 14.031  25.305 135.890 1.00 12.64 ? 117 PRO B O     1 
ATOM   3117 C  CB    . PRO D 2 117 ? 14.087  23.572 133.730 1.00 10.29 ? 117 PRO B CB    1 
ATOM   3118 C  CG    . PRO D 2 117 ? 13.330  22.445 134.392 1.00 9.88  ? 117 PRO B CG    1 
ATOM   3119 C  CD    . PRO D 2 117 ? 14.407  21.450 134.805 1.00 9.34  ? 117 PRO B CD    1 
ATOM   3120 N  N     . THR D 2 118 ? 16.001  24.582 136.728 1.00 10.61 ? 118 THR B N     1 
ATOM   3121 C  CA    . THR D 2 118 ? 16.083  25.375 137.961 1.00 9.19  ? 118 THR B CA    1 
ATOM   3122 C  C     . THR D 2 118 ? 17.082  26.501 137.683 1.00 8.90  ? 118 THR B C     1 
ATOM   3123 O  O     . THR D 2 118 ? 18.298  26.207 137.679 1.00 8.29  ? 118 THR B O     1 
ATOM   3124 C  CB    . THR D 2 118 ? 16.597  24.447 139.136 1.00 8.57  ? 118 THR B CB    1 
ATOM   3125 O  OG1   . THR D 2 118 ? 17.889  23.908 138.703 1.00 9.16  ? 118 THR B OG1   1 
ATOM   3126 C  CG2   . THR D 2 118 ? 15.619  23.328 139.552 1.00 6.00  ? 118 THR B CG2   1 
ATOM   3127 N  N     . PRO D 2 119 ? 16.622  27.711 137.398 1.00 9.52  ? 119 PRO B N     1 
ATOM   3128 C  CA    . PRO D 2 119 ? 17.521  28.836 137.086 1.00 9.16  ? 119 PRO B CA    1 
ATOM   3129 C  C     . PRO D 2 119 ? 18.565  29.044 138.166 1.00 9.46  ? 119 PRO B C     1 
ATOM   3130 O  O     . PRO D 2 119 ? 18.217  28.915 139.357 1.00 11.07 ? 119 PRO B O     1 
ATOM   3131 C  CB    . PRO D 2 119 ? 16.601  30.051 136.973 1.00 8.02  ? 119 PRO B CB    1 
ATOM   3132 C  CG    . PRO D 2 119 ? 15.247  29.472 136.678 1.00 8.44  ? 119 PRO B CG    1 
ATOM   3133 C  CD    . PRO D 2 119 ? 15.214  28.120 137.375 1.00 9.07  ? 119 PRO B CD    1 
ATOM   3134 N  N     . GLY D 2 120 ? 19.789  29.326 137.787 1.00 8.52  ? 120 GLY B N     1 
ATOM   3135 C  CA    . GLY D 2 120 ? 20.921  29.571 138.655 1.00 8.13  ? 120 GLY B CA    1 
ATOM   3136 C  C     . GLY D 2 120 ? 21.787  28.367 138.994 1.00 8.19  ? 120 GLY B C     1 
ATOM   3137 O  O     . GLY D 2 120 ? 23.004  28.512 139.328 1.00 7.68  ? 120 GLY B O     1 
ATOM   3138 N  N     . VAL D 2 121 ? 21.215  27.174 138.937 1.00 8.74  ? 121 VAL B N     1 
ATOM   3139 C  CA    . VAL D 2 121 ? 21.977  25.960 139.266 1.00 10.60 ? 121 VAL B CA    1 
ATOM   3140 C  C     . VAL D 2 121 ? 22.094  25.047 138.050 1.00 11.20 ? 121 VAL B C     1 
ATOM   3141 O  O     . VAL D 2 121 ? 21.127  24.626 137.418 1.00 11.70 ? 121 VAL B O     1 
ATOM   3142 C  CB    . VAL D 2 121 ? 21.510  25.299 140.569 1.00 10.99 ? 121 VAL B CB    1 
ATOM   3143 C  CG1   . VAL D 2 121 ? 20.647  26.204 141.435 1.00 9.61  ? 121 VAL B CG1   1 
ATOM   3144 C  CG2   . VAL D 2 121 ? 20.855  23.964 140.366 1.00 10.30 ? 121 VAL B CG2   1 
ATOM   3145 N  N     . ALA D 2 122 ? 23.352  24.755 137.749 1.00 11.13 ? 122 ALA B N     1 
ATOM   3146 C  CA    . ALA D 2 122 ? 23.800  23.937 136.639 1.00 10.77 ? 122 ALA B CA    1 
ATOM   3147 C  C     . ALA D 2 122 ? 23.300  22.510 136.739 1.00 10.96 ? 122 ALA B C     1 
ATOM   3148 O  O     . ALA D 2 122 ? 22.660  22.011 135.787 1.00 11.82 ? 122 ALA B O     1 
ATOM   3149 C  CB    . ALA D 2 122 ? 25.333  23.976 136.516 1.00 11.26 ? 122 ALA B CB    1 
ATOM   3150 N  N     . TYR D 2 123 ? 23.611  21.843 137.839 1.00 9.72  ? 123 TYR B N     1 
ATOM   3151 C  CA    . TYR D 2 123 ? 23.131  20.434 137.917 1.00 9.43  ? 123 TYR B CA    1 
ATOM   3152 C  C     . TYR D 2 123 ? 22.992  20.070 139.377 1.00 10.78 ? 123 TYR B C     1 
ATOM   3153 O  O     . TYR D 2 123 ? 23.370  20.868 140.256 1.00 12.02 ? 123 TYR B O     1 
ATOM   3154 C  CB    . TYR D 2 123 ? 24.074  19.521 137.124 1.00 7.81  ? 123 TYR B CB    1 
ATOM   3155 C  CG    . TYR D 2 123 ? 25.459  19.456 137.722 1.00 8.67  ? 123 TYR B CG    1 
ATOM   3156 C  CD1   . TYR D 2 123 ? 26.460  20.371 137.387 1.00 8.18  ? 123 TYR B CD1   1 
ATOM   3157 C  CD2   . TYR D 2 123 ? 25.752  18.468 138.676 1.00 8.74  ? 123 TYR B CD2   1 
ATOM   3158 C  CE1   . TYR D 2 123 ? 27.717  20.310 137.978 1.00 9.19  ? 123 TYR B CE1   1 
ATOM   3159 C  CE2   . TYR D 2 123 ? 27.014  18.387 139.269 1.00 9.85  ? 123 TYR B CE2   1 
ATOM   3160 C  CZ    . TYR D 2 123 ? 27.986  19.323 138.914 1.00 11.52 ? 123 TYR B CZ    1 
ATOM   3161 O  OH    . TYR D 2 123 ? 29.233  19.252 139.491 1.00 11.91 ? 123 TYR B OH    1 
ATOM   3162 N  N     . TRP D 2 124 ? 22.425  18.918 139.611 1.00 10.40 ? 124 TRP B N     1 
ATOM   3163 C  CA    . TRP D 2 124 ? 22.170  18.380 140.959 1.00 10.22 ? 124 TRP B CA    1 
ATOM   3164 C  C     . TRP D 2 124 ? 22.831  17.007 140.991 1.00 10.63 ? 124 TRP B C     1 
ATOM   3165 O  O     . TRP D 2 124 ? 22.479  16.179 140.114 1.00 11.87 ? 124 TRP B O     1 
ATOM   3166 C  CB    . TRP D 2 124 ? 20.664  18.289 141.183 1.00 9.76  ? 124 TRP B CB    1 
ATOM   3167 C  CG    . TRP D 2 124 ? 19.955  19.596 141.089 1.00 8.40  ? 124 TRP B CG    1 
ATOM   3168 C  CD1   . TRP D 2 124 ? 19.558  20.240 139.943 1.00 7.02  ? 124 TRP B CD1   1 
ATOM   3169 C  CD2   . TRP D 2 124 ? 19.560  20.434 142.179 1.00 7.37  ? 124 TRP B CD2   1 
ATOM   3170 N  NE1   . TRP D 2 124 ? 18.926  21.414 140.266 1.00 6.63  ? 124 TRP B NE1   1 
ATOM   3171 C  CE2   . TRP D 2 124 ? 18.924  21.565 141.627 1.00 7.44  ? 124 TRP B CE2   1 
ATOM   3172 C  CE3   . TRP D 2 124 ? 19.679  20.331 143.554 1.00 6.79  ? 124 TRP B CE3   1 
ATOM   3173 C  CZ2   . TRP D 2 124 ? 18.413  22.594 142.403 1.00 7.99  ? 124 TRP B CZ2   1 
ATOM   3174 C  CZ3   . TRP D 2 124 ? 19.167  21.348 144.337 1.00 6.54  ? 124 TRP B CZ3   1 
ATOM   3175 C  CH2   . TRP D 2 124 ? 18.538  22.463 143.775 1.00 7.60  ? 124 TRP B CH2   1 
ATOM   3176 N  N     . VAL D 2 125 ? 23.728  16.794 141.939 1.00 9.89  ? 125 VAL B N     1 
ATOM   3177 C  CA    . VAL D 2 125 ? 24.381  15.488 141.957 1.00 8.55  ? 125 VAL B CA    1 
ATOM   3178 C  C     . VAL D 2 125 ? 24.309  14.810 143.313 1.00 9.22  ? 125 VAL B C     1 
ATOM   3179 O  O     . VAL D 2 125 ? 24.199  15.451 144.363 1.00 9.14  ? 125 VAL B O     1 
ATOM   3180 C  CB    . VAL D 2 125 ? 25.862  15.651 141.556 1.00 4.70  ? 125 VAL B CB    1 
ATOM   3181 C  CG1   . VAL D 2 125 ? 26.573  16.571 142.540 1.00 2.71  ? 125 VAL B CG1   1 
ATOM   3182 C  CG2   . VAL D 2 125 ? 26.539  14.291 141.455 1.00 2.97  ? 125 VAL B CG2   1 
ATOM   3183 N  N     . ALA D 2 126 ? 24.480  13.511 143.190 1.00 9.04  ? 126 ALA B N     1 
ATOM   3184 C  CA    . ALA D 2 126 ? 24.479  12.578 144.301 1.00 9.44  ? 126 ALA B CA    1 
ATOM   3185 C  C     . ALA D 2 126 ? 25.070  11.256 143.821 1.00 10.10 ? 126 ALA B C     1 
ATOM   3186 O  O     . ALA D 2 126 ? 25.018  10.917 142.620 1.00 10.95 ? 126 ALA B O     1 
ATOM   3187 C  CB    . ALA D 2 126 ? 23.048  12.395 144.811 1.00 9.04  ? 126 ALA B CB    1 
ATOM   3188 N  N     . ASP D 2 127 ? 25.639  10.572 144.798 1.00 10.19 ? 127 ASP B N     1 
ATOM   3189 C  CA    . ASP D 2 127 ? 26.232  9.262  144.477 1.00 10.23 ? 127 ASP B CA    1 
ATOM   3190 C  C     . ASP D 2 127 ? 25.713  8.238  145.493 1.00 9.92  ? 127 ASP B C     1 
ATOM   3191 O  O     . ASP D 2 127 ? 25.352  8.521  146.643 1.00 10.22 ? 127 ASP B O     1 
ATOM   3192 C  CB    . ASP D 2 127 ? 27.725  9.344  144.271 1.00 11.30 ? 127 ASP B CB    1 
ATOM   3193 C  CG    . ASP D 2 127 ? 28.442  9.691  145.574 1.00 13.16 ? 127 ASP B CG    1 
ATOM   3194 O  OD1   . ASP D 2 127 ? 28.716  8.780  146.385 1.00 10.18 ? 127 ASP B OD1   1 
ATOM   3195 O  OD2   . ASP D 2 127 ? 28.680  10.910 145.735 1.00 17.69 ? 127 ASP B OD2   1 
ATOM   3196 N  N     . VAL D 2 128 ? 25.691  7.034  144.951 1.00 9.39  ? 128 VAL B N     1 
ATOM   3197 C  CA    . VAL D 2 128 ? 25.187  5.870  145.658 1.00 9.07  ? 128 VAL B CA    1 
ATOM   3198 C  C     . VAL D 2 128 ? 26.020  4.647  145.309 1.00 8.85  ? 128 VAL B C     1 
ATOM   3199 O  O     . VAL D 2 128 ? 26.770  4.666  144.321 1.00 9.11  ? 128 VAL B O     1 
ATOM   3200 C  CB    . VAL D 2 128 ? 23.693  5.754  145.235 1.00 8.92  ? 128 VAL B CB    1 
ATOM   3201 C  CG1   . VAL D 2 128 ? 22.956  7.051  145.536 1.00 9.25  ? 128 VAL B CG1   1 
ATOM   3202 C  CG2   . VAL D 2 128 ? 23.516  5.358  143.788 1.00 7.82  ? 128 VAL B CG2   1 
ATOM   3203 N  N     . PRO D 2 129 ? 25.847  3.626  146.139 1.00 8.20  ? 129 PRO B N     1 
ATOM   3204 C  CA    . PRO D 2 129 ? 26.486  2.333  145.944 1.00 8.85  ? 129 PRO B CA    1 
ATOM   3205 C  C     . PRO D 2 129 ? 26.146  1.799  144.536 1.00 9.38  ? 129 PRO B C     1 
ATOM   3206 O  O     . PRO D 2 129 ? 24.999  1.670  144.062 1.00 9.10  ? 129 PRO B O     1 
ATOM   3207 C  CB    . PRO D 2 129 ? 25.879  1.428  146.994 1.00 8.92  ? 129 PRO B CB    1 
ATOM   3208 C  CG    . PRO D 2 129 ? 25.309  2.347  148.022 1.00 8.50  ? 129 PRO B CG    1 
ATOM   3209 C  CD    . PRO D 2 129 ? 24.950  3.620  147.293 1.00 8.32  ? 129 PRO B CD    1 
ATOM   3210 N  N     . ALA D 2 130 ? 27.254  1.471  143.878 1.00 9.46  ? 130 ALA B N     1 
ATOM   3211 C  CA    . ALA D 2 130 ? 27.178  0.946  142.517 1.00 9.99  ? 130 ALA B CA    1 
ATOM   3212 C  C     . ALA D 2 130 ? 26.064  -0.097 142.449 1.00 10.55 ? 130 ALA B C     1 
ATOM   3213 O  O     . ALA D 2 130 ? 25.904  -0.969 143.337 1.00 11.88 ? 130 ALA B O     1 
ATOM   3214 C  CB    . ALA D 2 130 ? 28.539  0.377  142.145 1.00 11.28 ? 130 ALA B CB    1 
ATOM   3215 N  N     . GLY D 2 131 ? 25.300  0.004  141.358 1.00 9.82  ? 131 GLY B N     1 
ATOM   3216 C  CA    . GLY D 2 131 ? 24.226  -0.975 141.112 1.00 9.50  ? 131 GLY B CA    1 
ATOM   3217 C  C     . GLY D 2 131 ? 22.939  -0.577 141.799 1.00 9.17  ? 131 GLY B C     1 
ATOM   3218 O  O     . GLY D 2 131 ? 21.923  -1.303 141.661 1.00 9.65  ? 131 GLY B O     1 
ATOM   3219 N  N     . THR D 2 132 ? 22.991  0.550  142.493 1.00 8.30  ? 132 THR B N     1 
ATOM   3220 C  CA    . THR D 2 132 ? 21.756  0.994  143.187 1.00 8.71  ? 132 THR B CA    1 
ATOM   3221 C  C     . THR D 2 132 ? 21.283  2.323  142.665 1.00 10.08 ? 132 THR B C     1 
ATOM   3222 O  O     . THR D 2 132 ? 22.011  2.948  141.887 1.00 11.45 ? 132 THR B O     1 
ATOM   3223 C  CB    . THR D 2 132 ? 22.061  0.958  144.732 1.00 5.44  ? 132 THR B CB    1 
ATOM   3224 O  OG1   . THR D 2 132 ? 22.756  2.213  145.003 1.00 4.62  ? 132 THR B OG1   1 
ATOM   3225 C  CG2   . THR D 2 132 ? 22.892  -0.284 145.060 1.00 4.58  ? 132 THR B CG2   1 
ATOM   3226 N  N     . PHE D 2 133 ? 20.095  2.733  143.043 1.00 10.31 ? 133 PHE B N     1 
ATOM   3227 C  CA    . PHE D 2 133 ? 19.452  3.989  142.664 1.00 10.21 ? 133 PHE B CA    1 
ATOM   3228 C  C     . PHE D 2 133 ? 19.189  4.790  143.946 1.00 10.43 ? 133 PHE B C     1 
ATOM   3229 O  O     . PHE D 2 133 ? 19.130  4.220  145.047 1.00 11.12 ? 133 PHE B O     1 
ATOM   3230 C  CB    . PHE D 2 133 ? 18.114  3.757  141.961 1.00 10.60 ? 133 PHE B CB    1 
ATOM   3231 C  CG    . PHE D 2 133 ? 18.203  3.446  140.502 1.00 10.62 ? 133 PHE B CG    1 
ATOM   3232 C  CD1   . PHE D 2 133 ? 18.204  4.466  139.554 1.00 10.62 ? 133 PHE B CD1   1 
ATOM   3233 C  CD2   . PHE D 2 133 ? 18.294  2.114  140.094 1.00 9.81  ? 133 PHE B CD2   1 
ATOM   3234 C  CE1   . PHE D 2 133 ? 18.299  4.180  138.193 1.00 10.72 ? 133 PHE B CE1   1 
ATOM   3235 C  CE2   . PHE D 2 133 ? 18.373  1.791  138.754 1.00 10.01 ? 133 PHE B CE2   1 
ATOM   3236 C  CZ    . PHE D 2 133 ? 18.379  2.832  137.809 1.00 11.40 ? 133 PHE B CZ    1 
ATOM   3237 N  N     . PRO D 2 134 ? 18.979  6.081  143.767 1.00 10.16 ? 134 PRO B N     1 
ATOM   3238 C  CA    . PRO D 2 134 ? 18.683  6.947  144.906 1.00 9.50  ? 134 PRO B CA    1 
ATOM   3239 C  C     . PRO D 2 134 ? 17.510  6.384  145.718 1.00 8.98  ? 134 PRO B C     1 
ATOM   3240 O  O     . PRO D 2 134 ? 16.400  6.095  145.248 1.00 7.88  ? 134 PRO B O     1 
ATOM   3241 C  CB    . PRO D 2 134 ? 18.330  8.287  144.260 1.00 9.40  ? 134 PRO B CB    1 
ATOM   3242 C  CG    . PRO D 2 134 ? 19.007  8.276  142.919 1.00 10.02 ? 134 PRO B CG    1 
ATOM   3243 C  CD    . PRO D 2 134 ? 19.015  6.819  142.491 1.00 10.42 ? 134 PRO B CD    1 
ATOM   3244 N  N     . ILE D 2 135 ? 17.744  6.268  147.009 1.00 8.85  ? 135 ILE B N     1 
ATOM   3245 C  CA    . ILE D 2 135 ? 16.718  5.820  147.973 1.00 8.84  ? 135 ILE B CA    1 
ATOM   3246 C  C     . ILE D 2 135 ? 16.171  7.078  148.675 1.00 9.27  ? 135 ILE B C     1 
ATOM   3247 O  O     . ILE D 2 135 ? 16.743  8.172  148.558 1.00 9.73  ? 135 ILE B O     1 
ATOM   3248 C  CB    . ILE D 2 135 ? 17.356  4.783  148.912 1.00 8.53  ? 135 ILE B CB    1 
ATOM   3249 C  CG1   . ILE D 2 135 ? 18.247  5.433  149.973 1.00 12.43 ? 135 ILE B CG1   1 
ATOM   3250 C  CG2   . ILE D 2 135 ? 18.237  3.772  148.174 1.00 5.77  ? 135 ILE B CG2   1 
ATOM   3251 C  CD1   . ILE D 2 135 ? 19.133  4.431  150.711 1.00 13.00 ? 135 ILE B CD1   1 
ATOM   3252 N  N     . SER D 2 136 ? 15.070  6.882  149.369 1.00 9.43  ? 136 SER B N     1 
ATOM   3253 C  CA    . SER D 2 136 ? 14.332  7.957  150.066 1.00 10.43 ? 136 SER B CA    1 
ATOM   3254 C  C     . SER D 2 136 ? 15.230  8.815  150.971 1.00 9.83  ? 136 SER B C     1 
ATOM   3255 O  O     . SER D 2 136 ? 14.900  9.970  151.284 1.00 9.99  ? 136 SER B O     1 
ATOM   3256 C  CB    . SER D 2 136 ? 13.259  7.346  150.970 1.00 12.94 ? 136 SER B CB    1 
ATOM   3257 O  OG    . SER D 2 136 ? 13.868  6.738  152.102 1.00 16.36 ? 136 SER B OG    1 
ATOM   3258 N  N     . THR D 2 137 ? 16.338  8.230  151.361 1.00 9.03  ? 137 THR B N     1 
ATOM   3259 C  CA    . THR D 2 137 ? 17.281  8.843  152.312 1.00 8.49  ? 137 THR B CA    1 
ATOM   3260 C  C     . THR D 2 137 ? 18.363  9.701  151.619 1.00 9.41  ? 137 THR B C     1 
ATOM   3261 O  O     . THR D 2 137 ? 19.177  10.357 152.286 1.00 11.23 ? 137 THR B O     1 
ATOM   3262 C  CB    . THR D 2 137 ? 17.979  7.726  153.088 1.00 5.18  ? 137 THR B CB    1 
ATOM   3263 O  OG1   . THR D 2 137 ? 17.965  8.013  154.474 1.00 6.12  ? 137 THR B OG1   1 
ATOM   3264 C  CG2   . THR D 2 137 ? 19.434  7.525  152.666 1.00 5.73  ? 137 THR B CG2   1 
ATOM   3265 N  N     . THR D 2 138 ? 18.337  9.686  150.301 1.00 9.34  ? 138 THR B N     1 
ATOM   3266 C  CA    . THR D 2 138 ? 19.333  10.383 149.446 1.00 9.25  ? 138 THR B CA    1 
ATOM   3267 C  C     . THR D 2 138 ? 19.024  11.857 149.289 1.00 10.00 ? 138 THR B C     1 
ATOM   3268 O  O     . THR D 2 138 ? 17.822  12.199 149.311 1.00 10.16 ? 138 THR B O     1 
ATOM   3269 C  CB    . THR D 2 138 ? 19.309  9.730  148.062 1.00 9.60  ? 138 THR B CB    1 
ATOM   3270 O  OG1   . THR D 2 138 ? 19.239  8.315  148.199 1.00 12.18 ? 138 THR B OG1   1 
ATOM   3271 C  CG2   . THR D 2 138 ? 20.540  10.049 147.220 1.00 7.42  ? 138 THR B CG2   1 
ATOM   3272 N  N     . THR D 2 139 ? 20.058  12.688 149.150 1.00 10.96 ? 139 THR B N     1 
ATOM   3273 C  CA    . THR D 2 139 ? 19.830  14.135 148.966 1.00 11.19 ? 139 THR B CA    1 
ATOM   3274 C  C     . THR D 2 139 ? 20.636  14.590 147.747 1.00 11.61 ? 139 THR B C     1 
ATOM   3275 O  O     . THR D 2 139 ? 21.846  14.304 147.741 1.00 12.30 ? 139 THR B O     1 
ATOM   3276 C  CB    . THR D 2 139 ? 20.249  15.031 150.185 1.00 10.47 ? 139 THR B CB    1 
ATOM   3277 O  OG1   . THR D 2 139 ? 19.300  14.815 151.265 1.00 10.66 ? 139 THR B OG1   1 
ATOM   3278 C  CG2   . THR D 2 139 ? 20.366  16.510 149.793 1.00 9.61  ? 139 THR B CG2   1 
ATOM   3279 N  N     . PHE D 2 140 ? 19.989  15.237 146.802 1.00 11.60 ? 140 PHE B N     1 
ATOM   3280 C  CA    . PHE D 2 140 ? 20.742  15.741 145.613 1.00 11.51 ? 140 PHE B CA    1 
ATOM   3281 C  C     . PHE D 2 140 ? 21.248  17.119 146.018 1.00 11.59 ? 140 PHE B C     1 
ATOM   3282 O  O     . PHE D 2 140 ? 20.475  17.864 146.657 1.00 12.55 ? 140 PHE B O     1 
ATOM   3283 C  CB    . PHE D 2 140 ? 19.915  15.778 144.339 1.00 10.93 ? 140 PHE B CB    1 
ATOM   3284 C  CG    . PHE D 2 140 ? 19.809  14.418 143.707 1.00 10.67 ? 140 PHE B CG    1 
ATOM   3285 C  CD1   . PHE D 2 140 ? 18.988  13.459 144.292 1.00 10.50 ? 140 PHE B CD1   1 
ATOM   3286 C  CD2   . PHE D 2 140 ? 20.593  14.096 142.600 1.00 11.49 ? 140 PHE B CD2   1 
ATOM   3287 C  CE1   . PHE D 2 140 ? 18.907  12.182 143.758 1.00 10.97 ? 140 PHE B CE1   1 
ATOM   3288 C  CE2   . PHE D 2 140 ? 20.524  12.805 142.058 1.00 11.74 ? 140 PHE B CE2   1 
ATOM   3289 C  CZ    . PHE D 2 140 ? 19.668  11.852 142.641 1.00 12.24 ? 140 PHE B CZ    1 
ATOM   3290 N  N     . ASN D 2 141 ? 22.475  17.424 145.726 1.00 11.23 ? 141 ASN B N     1 
ATOM   3291 C  CA    . ASN D 2 141 ? 23.005  18.768 146.102 1.00 10.44 ? 141 ASN B CA    1 
ATOM   3292 C  C     . ASN D 2 141 ? 23.083  19.575 144.814 1.00 10.72 ? 141 ASN B C     1 
ATOM   3293 O  O     . ASN D 2 141 ? 23.277  18.965 143.738 1.00 11.54 ? 141 ASN B O     1 
ATOM   3294 C  CB    . ASN D 2 141 ? 24.304  18.596 146.855 1.00 10.90 ? 141 ASN B CB    1 
ATOM   3295 C  CG    . ASN D 2 141 ? 24.070  18.173 148.298 1.00 13.61 ? 141 ASN B CG    1 
ATOM   3296 O  OD1   . ASN D 2 141 ? 24.262  16.982 148.605 1.00 15.65 ? 141 ASN B OD1   1 
ATOM   3297 N  ND2   . ASN D 2 141 ? 23.661  19.138 149.115 1.00 15.29 ? 141 ASN B ND2   1 
ATOM   3298 N  N     . ALA D 2 142 ? 22.967  20.878 144.955 1.00 10.06 ? 142 ALA B N     1 
ATOM   3299 C  CA    . ALA D 2 142 ? 22.992  21.745 143.760 1.00 10.03 ? 142 ALA B CA    1 
ATOM   3300 C  C     . ALA D 2 142 ? 24.362  22.240 143.389 1.00 10.09 ? 142 ALA B C     1 
ATOM   3301 O  O     . ALA D 2 142 ? 25.133  22.558 144.310 1.00 11.51 ? 142 ALA B O     1 
ATOM   3302 C  CB    . ALA D 2 142 ? 22.051  22.929 144.032 1.00 10.70 ? 142 ALA B CB    1 
ATOM   3303 N  N     . VAL D 2 143 ? 24.683  22.321 142.118 1.00 10.08 ? 143 VAL B N     1 
ATOM   3304 C  CA    . VAL D 2 143 ? 25.973  22.894 141.650 1.00 9.80  ? 143 VAL B CA    1 
ATOM   3305 C  C     . VAL D 2 143 ? 25.575  24.098 140.770 1.00 10.95 ? 143 VAL B C     1 
ATOM   3306 O  O     . VAL D 2 143 ? 24.969  23.900 139.704 1.00 11.28 ? 143 VAL B O     1 
ATOM   3307 C  CB    . VAL D 2 143 ? 26.880  21.897 140.974 1.00 8.31  ? 143 VAL B CB    1 
ATOM   3308 C  CG1   . VAL D 2 143 ? 28.176  22.548 140.489 1.00 6.67  ? 143 VAL B CG1   1 
ATOM   3309 C  CG2   . VAL D 2 143 ? 27.142  20.710 141.870 1.00 7.42  ? 143 VAL B CG2   1 
ATOM   3310 N  N     . ASN D 2 144 ? 25.853  25.263 141.292 1.00 11.58 ? 144 ASN B N     1 
ATOM   3311 C  CA    . ASN D 2 144 ? 25.509  26.542 140.694 1.00 11.48 ? 144 ASN B CA    1 
ATOM   3312 C  C     . ASN D 2 144 ? 26.364  26.883 139.468 1.00 11.57 ? 144 ASN B C     1 
ATOM   3313 O  O     . ASN D 2 144 ? 27.518  26.513 139.370 1.00 13.05 ? 144 ASN B O     1 
ATOM   3314 C  CB    . ASN D 2 144 ? 25.735  27.715 141.646 1.00 12.15 ? 144 ASN B CB    1 
ATOM   3315 C  CG    . ASN D 2 144 ? 24.855  28.009 142.795 1.00 14.21 ? 144 ASN B CG    1 
ATOM   3316 O  OD1   . ASN D 2 144 ? 23.790  27.447 143.040 1.00 15.87 ? 144 ASN B OD1   1 
ATOM   3317 N  ND2   . ASN D 2 144 ? 25.336  28.997 143.550 1.00 16.81 ? 144 ASN B ND2   1 
ATOM   3318 N  N     . PHE D 2 145 ? 25.749  27.696 138.645 1.00 10.48 ? 145 PHE B N     1 
ATOM   3319 C  CA    . PHE D 2 145 ? 26.478  28.244 137.449 1.00 9.29  ? 145 PHE B CA    1 
ATOM   3320 C  C     . PHE D 2 145 ? 27.126  29.508 138.067 1.00 8.44  ? 145 PHE B C     1 
ATOM   3321 O  O     . PHE D 2 145 ? 26.568  30.030 139.063 1.00 8.93  ? 145 PHE B O     1 
ATOM   3322 C  CB    . PHE D 2 145 ? 25.482  28.655 136.404 1.00 8.29  ? 145 PHE B CB    1 
ATOM   3323 C  CG    . PHE D 2 145 ? 25.031  27.752 135.335 1.00 7.05  ? 145 PHE B CG    1 
ATOM   3324 C  CD1   . PHE D 2 145 ? 25.934  27.236 134.410 1.00 7.15  ? 145 PHE B CD1   1 
ATOM   3325 C  CD2   . PHE D 2 145 ? 23.665  27.466 135.212 1.00 5.69  ? 145 PHE B CD2   1 
ATOM   3326 C  CE1   . PHE D 2 145 ? 25.501  26.430 133.368 1.00 6.04  ? 145 PHE B CE1   1 
ATOM   3327 C  CE2   . PHE D 2 145 ? 23.208  26.668 134.189 1.00 5.41  ? 145 PHE B CE2   1 
ATOM   3328 C  CZ    . PHE D 2 145 ? 24.122  26.151 133.289 1.00 5.04  ? 145 PHE B CZ    1 
ATOM   3329 N  N     . PRO D 2 146 ? 28.179  29.988 137.495 1.00 8.06  ? 146 PRO B N     1 
ATOM   3330 C  CA    . PRO D 2 146 ? 28.822  31.212 138.041 1.00 8.81  ? 146 PRO B CA    1 
ATOM   3331 C  C     . PRO D 2 146 ? 27.809  32.349 138.029 1.00 9.54  ? 146 PRO B C     1 
ATOM   3332 O  O     . PRO D 2 146 ? 26.924  32.331 137.149 1.00 10.60 ? 146 PRO B O     1 
ATOM   3333 C  CB    . PRO D 2 146 ? 29.964  31.464 137.085 1.00 7.95  ? 146 PRO B CB    1 
ATOM   3334 C  CG    . PRO D 2 146 ? 29.565  30.727 135.830 1.00 7.72  ? 146 PRO B CG    1 
ATOM   3335 C  CD    . PRO D 2 146 ? 28.888  29.452 136.341 1.00 8.18  ? 146 PRO B CD    1 
ATOM   3336 N  N     . GLY D 2 147 ? 27.921  33.271 138.949 1.00 10.57 ? 147 GLY B N     1 
ATOM   3337 C  CA    . GLY D 2 147 ? 27.122  34.450 139.139 1.00 12.76 ? 147 GLY B CA    1 
ATOM   3338 C  C     . GLY D 2 147 ? 25.814  34.397 139.874 1.00 14.17 ? 147 GLY B C     1 
ATOM   3339 O  O     . GLY D 2 147 ? 25.097  35.437 139.907 1.00 15.83 ? 147 GLY B O     1 
ATOM   3340 N  N     . PHE D 2 148 ? 25.441  33.296 140.498 1.00 13.56 ? 148 PHE B N     1 
ATOM   3341 C  CA    . PHE D 2 148 ? 24.187  33.080 141.215 1.00 12.91 ? 148 PHE B CA    1 
ATOM   3342 C  C     . PHE D 2 148 ? 23.720  34.227 142.099 1.00 12.72 ? 148 PHE B C     1 
ATOM   3343 O  O     . PHE D 2 148 ? 22.596  34.712 141.885 1.00 13.62 ? 148 PHE B O     1 
ATOM   3344 C  CB    . PHE D 2 148 ? 24.124  31.774 142.016 1.00 11.34 ? 148 PHE B CB    1 
ATOM   3345 C  CG    . PHE D 2 148 ? 22.811  31.477 142.681 1.00 10.85 ? 148 PHE B CG    1 
ATOM   3346 C  CD1   . PHE D 2 148 ? 22.502  32.044 143.917 1.00 11.01 ? 148 PHE B CD1   1 
ATOM   3347 C  CD2   . PHE D 2 148 ? 21.888  30.608 142.091 1.00 11.09 ? 148 PHE B CD2   1 
ATOM   3348 C  CE1   . PHE D 2 148 ? 21.280  31.774 144.555 1.00 10.44 ? 148 PHE B CE1   1 
ATOM   3349 C  CE2   . PHE D 2 148 ? 20.676  30.325 142.692 1.00 10.00 ? 148 PHE B CE2   1 
ATOM   3350 C  CZ    . PHE D 2 148 ? 20.362  30.909 143.930 1.00 9.84  ? 148 PHE B CZ    1 
ATOM   3351 N  N     . ASN D 2 149 ? 24.518  34.598 143.077 1.00 12.78 ? 149 ASN B N     1 
ATOM   3352 C  CA    . ASN D 2 149 ? 24.131  35.685 144.002 1.00 12.96 ? 149 ASN B CA    1 
ATOM   3353 C  C     . ASN D 2 149 ? 23.918  36.985 143.223 1.00 13.81 ? 149 ASN B C     1 
ATOM   3354 O  O     . ASN D 2 149 ? 23.009  37.758 143.553 1.00 15.38 ? 149 ASN B O     1 
ATOM   3355 C  CB    . ASN D 2 149 ? 25.119  35.895 145.138 1.00 11.73 ? 149 ASN B CB    1 
ATOM   3356 C  CG    . ASN D 2 149 ? 25.296  34.710 146.046 1.00 15.01 ? 149 ASN B CG    1 
ATOM   3357 O  OD1   . ASN D 2 149 ? 26.383  34.109 146.068 1.00 18.25 ? 149 ASN B OD1   1 
ATOM   3358 N  ND2   . ASN D 2 149 ? 24.264  34.342 146.816 1.00 15.26 ? 149 ASN B ND2   1 
ATOM   3359 N  N     . SER D 2 150 ? 24.792  37.193 142.243 1.00 13.81 ? 150 SER B N     1 
ATOM   3360 C  CA    . SER D 2 150 ? 24.669  38.462 141.493 1.00 14.20 ? 150 SER B CA    1 
ATOM   3361 C  C     . SER D 2 150 ? 23.320  38.502 140.797 1.00 13.85 ? 150 SER B C     1 
ATOM   3362 O  O     . SER D 2 150 ? 22.813  39.567 140.378 1.00 15.56 ? 150 SER B O     1 
ATOM   3363 C  CB    . SER D 2 150 ? 25.831  38.633 140.537 1.00 14.47 ? 150 SER B CB    1 
ATOM   3364 O  OG    . SER D 2 150 ? 25.544  37.973 139.300 1.00 17.35 ? 150 SER B OG    1 
ATOM   3365 N  N     . MET D 2 151 ? 22.728  37.332 140.703 1.00 12.90 ? 151 MET B N     1 
ATOM   3366 C  CA    . MET D 2 151 ? 21.451  37.180 140.005 1.00 12.74 ? 151 MET B CA    1 
ATOM   3367 C  C     . MET D 2 151 ? 20.245  36.975 140.889 1.00 13.59 ? 151 MET B C     1 
ATOM   3368 O  O     . MET D 2 151 ? 19.179  37.549 140.563 1.00 14.76 ? 151 MET B O     1 
ATOM   3369 C  CB    . MET D 2 151 ? 21.621  35.959 139.079 1.00 11.71 ? 151 MET B CB    1 
ATOM   3370 C  CG    . MET D 2 151 ? 20.551  35.912 138.045 1.00 11.71 ? 151 MET B CG    1 
ATOM   3371 S  SD    . MET D 2 151 ? 21.067  37.039 136.695 1.00 11.77 ? 151 MET B SD    1 
ATOM   3372 C  CE    . MET D 2 151 ? 19.446  37.445 136.033 1.00 10.82 ? 151 MET B CE    1 
ATOM   3373 N  N     . PHE D 2 152 ? 20.427  36.167 141.936 1.00 13.21 ? 152 PHE B N     1 
ATOM   3374 C  CA    . PHE D 2 152 ? 19.339  35.810 142.842 1.00 13.38 ? 152 PHE B CA    1 
ATOM   3375 C  C     . PHE D 2 152 ? 19.473  36.170 144.297 1.00 14.02 ? 152 PHE B C     1 
ATOM   3376 O  O     . PHE D 2 152 ? 18.601  35.699 145.091 1.00 14.54 ? 152 PHE B O     1 
ATOM   3377 C  CB    . PHE D 2 152 ? 18.987  34.304 142.691 1.00 13.34 ? 152 PHE B CB    1 
ATOM   3378 C  CG    . PHE D 2 152 ? 18.639  34.012 141.259 1.00 13.12 ? 152 PHE B CG    1 
ATOM   3379 C  CD1   . PHE D 2 152 ? 17.460  34.504 140.723 1.00 12.91 ? 152 PHE B CD1   1 
ATOM   3380 C  CD2   . PHE D 2 152 ? 19.496  33.279 140.463 1.00 11.38 ? 152 PHE B CD2   1 
ATOM   3381 C  CE1   . PHE D 2 152 ? 17.122  34.263 139.389 1.00 11.96 ? 152 PHE B CE1   1 
ATOM   3382 C  CE2   . PHE D 2 152 ? 19.167  33.034 139.153 1.00 9.66  ? 152 PHE B CE2   1 
ATOM   3383 C  CZ    . PHE D 2 152 ? 17.994  33.528 138.594 1.00 9.83  ? 152 PHE B CZ    1 
ATOM   3384 N  N     . GLY D 2 153 ? 20.482  36.939 144.646 1.00 14.19 ? 153 GLY B N     1 
ATOM   3385 C  CA    . GLY D 2 153 ? 20.661  37.377 146.044 1.00 14.45 ? 153 GLY B CA    1 
ATOM   3386 C  C     . GLY D 2 153 ? 21.255  36.286 146.914 1.00 15.64 ? 153 GLY B C     1 
ATOM   3387 O  O     . GLY D 2 153 ? 21.778  35.289 146.393 1.00 16.77 ? 153 GLY B O     1 
ATOM   3388 N  N     . ASN D 2 154 ? 21.134  36.519 148.218 1.00 15.91 ? 154 ASN B N     1 
ATOM   3389 C  CA    . ASN D 2 154 ? 21.677  35.617 149.237 1.00 15.46 ? 154 ASN B CA    1 
ATOM   3390 C  C     . ASN D 2 154 ? 20.776  35.520 150.457 1.00 15.26 ? 154 ASN B C     1 
ATOM   3391 O  O     . ASN D 2 154 ? 21.259  35.426 151.603 1.00 16.49 ? 154 ASN B O     1 
ATOM   3392 C  CB    . ASN D 2 154 ? 23.101  36.086 149.638 1.00 17.19 ? 154 ASN B CB    1 
ATOM   3393 C  CG    . ASN D 2 154 ? 23.089  37.619 149.478 1.00 23.53 ? 154 ASN B CG    1 
ATOM   3394 O  OD1   . ASN D 2 154 ? 23.962  38.123 148.743 1.00 28.17 ? 154 ASN B OD1   1 
ATOM   3395 N  ND2   . ASN D 2 154 ? 22.077  38.234 150.098 1.00 21.59 ? 154 ASN B ND2   1 
ATOM   3396 N  N     . ALA D 2 155 ? 19.502  35.528 150.190 1.00 13.73 ? 155 ALA B N     1 
ATOM   3397 C  CA    . ALA D 2 155 ? 18.476  35.384 151.240 1.00 13.12 ? 155 ALA B CA    1 
ATOM   3398 C  C     . ALA D 2 155 ? 17.335  34.626 150.564 1.00 12.91 ? 155 ALA B C     1 
ATOM   3399 O  O     . ALA D 2 155 ? 17.058  34.970 149.401 1.00 12.83 ? 155 ALA B O     1 
ATOM   3400 C  CB    . ALA D 2 155 ? 18.015  36.741 151.711 1.00 16.41 ? 155 ALA B CB    1 
ATOM   3401 N  N     . ALA D 2 156 ? 16.749  33.704 151.272 1.00 12.18 ? 156 ALA B N     1 
ATOM   3402 C  CA    . ALA D 2 156 ? 15.661  32.907 150.703 1.00 11.06 ? 156 ALA B CA    1 
ATOM   3403 C  C     . ALA D 2 156 ? 14.516  33.737 150.183 1.00 10.57 ? 156 ALA B C     1 
ATOM   3404 O  O     . ALA D 2 156 ? 13.756  33.239 149.303 1.00 9.40  ? 156 ALA B O     1 
ATOM   3405 C  CB    . ALA D 2 156 ? 15.216  31.861 151.708 1.00 9.46  ? 156 ALA B CB    1 
ATOM   3406 N  N     . ALA D 2 157 ? 14.294  34.962 150.629 1.00 10.78 ? 157 ALA B N     1 
ATOM   3407 C  CA    . ALA D 2 157 ? 13.131  35.683 150.060 1.00 11.47 ? 157 ALA B CA    1 
ATOM   3408 C  C     . ALA D 2 157 ? 13.543  36.870 149.231 1.00 12.28 ? 157 ALA B C     1 
ATOM   3409 O  O     . ALA D 2 157 ? 12.761  37.846 149.121 1.00 13.27 ? 157 ALA B O     1 
ATOM   3410 C  CB    . ALA D 2 157 ? 12.111  35.954 151.130 1.00 9.46  ? 157 ALA B CB    1 
ATOM   3411 N  N     . SER D 2 158 ? 14.711  36.820 148.598 1.00 12.70 ? 158 SER B N     1 
ATOM   3412 C  CA    . SER D 2 158 ? 15.126  37.959 147.747 1.00 12.95 ? 158 SER B CA    1 
ATOM   3413 C  C     . SER D 2 158 ? 15.392  37.467 146.327 1.00 11.77 ? 158 SER B C     1 
ATOM   3414 O  O     . SER D 2 158 ? 16.224  38.080 145.625 1.00 11.25 ? 158 SER B O     1 
ATOM   3415 C  CB    . SER D 2 158 ? 16.385  38.620 148.272 1.00 17.33 ? 158 SER B CB    1 
ATOM   3416 O  OG    . SER D 2 158 ? 16.278  39.003 149.623 1.00 21.83 ? 158 SER B OG    1 
ATOM   3417 N  N     . ARG D 2 159 ? 14.702  36.382 145.987 1.00 10.63 ? 159 ARG B N     1 
ATOM   3418 C  CA    . ARG D 2 159 ? 14.919  35.772 144.677 1.00 8.84  ? 159 ARG B CA    1 
ATOM   3419 C  C     . ARG D 2 159 ? 14.548  36.663 143.522 1.00 8.83  ? 159 ARG B C     1 
ATOM   3420 O  O     . ARG D 2 159 ? 15.268  36.640 142.482 1.00 9.98  ? 159 ARG B O     1 
ATOM   3421 C  CB    . ARG D 2 159 ? 14.321  34.389 144.589 1.00 7.26  ? 159 ARG B CB    1 
ATOM   3422 C  CG    . ARG D 2 159 ? 15.124  33.316 145.294 1.00 7.11  ? 159 ARG B CG    1 
ATOM   3423 C  CD    . ARG D 2 159 ? 16.450  33.746 145.827 1.00 7.91  ? 159 ARG B CD    1 
ATOM   3424 N  NE    . ARG D 2 159 ? 17.048  32.690 146.653 1.00 10.22 ? 159 ARG B NE    1 
ATOM   3425 C  CZ    . ARG D 2 159 ? 18.227  32.806 147.272 1.00 11.06 ? 159 ARG B CZ    1 
ATOM   3426 N  NH1   . ARG D 2 159 ? 18.959  33.924 147.119 1.00 7.03  ? 159 ARG B NH1   1 
ATOM   3427 N  NH2   . ARG D 2 159 ? 18.751  31.843 148.037 1.00 12.82 ? 159 ARG B NH2   1 
ATOM   3428 N  N     . SER D 2 160 ? 13.518  37.483 143.662 1.00 8.27  ? 160 SER B N     1 
ATOM   3429 C  CA    . SER D 2 160 ? 13.084  38.349 142.567 1.00 8.12  ? 160 SER B CA    1 
ATOM   3430 C  C     . SER D 2 160 ? 13.449  39.799 142.653 1.00 9.09  ? 160 SER B C     1 
ATOM   3431 O  O     . SER D 2 160 ? 12.659  40.619 142.109 1.00 9.92  ? 160 SER B O     1 
ATOM   3432 C  CB    . SER D 2 160 ? 11.578  38.218 142.364 1.00 5.97  ? 160 SER B CB    1 
ATOM   3433 O  OG    . SER D 2 160 ? 10.930  37.802 143.541 1.00 3.60  ? 160 SER B OG    1 
ATOM   3434 N  N     . ASP D 2 161 ? 14.565  40.144 143.262 1.00 10.08 ? 161 ASP B N     1 
ATOM   3435 C  CA    . ASP D 2 161 ? 14.930  41.588 143.342 1.00 10.27 ? 161 ASP B CA    1 
ATOM   3436 C  C     . ASP D 2 161 ? 15.297  42.072 141.946 1.00 10.52 ? 161 ASP B C     1 
ATOM   3437 O  O     . ASP D 2 161 ? 14.732  43.096 141.521 1.00 11.44 ? 161 ASP B O     1 
ATOM   3438 C  CB    . ASP D 2 161 ? 15.933  41.843 144.437 1.00 11.79 ? 161 ASP B CB    1 
ATOM   3439 C  CG    . ASP D 2 161 ? 15.336  41.850 145.833 1.00 13.54 ? 161 ASP B CG    1 
ATOM   3440 O  OD1   . ASP D 2 161 ? 14.138  41.483 145.976 1.00 15.16 ? 161 ASP B OD1   1 
ATOM   3441 O  OD2   . ASP D 2 161 ? 15.993  42.205 146.830 1.00 14.25 ? 161 ASP B OD2   1 
ATOM   3442 N  N     . GLN D 2 162 ? 16.161  41.339 141.264 1.00 9.55  ? 162 GLN B N     1 
ATOM   3443 C  CA    . GLN D 2 162 ? 16.652  41.625 139.932 1.00 9.24  ? 162 GLN B CA    1 
ATOM   3444 C  C     . GLN D 2 162 ? 15.665  41.292 138.793 1.00 9.94  ? 162 GLN B C     1 
ATOM   3445 O  O     . GLN D 2 162 ? 15.398  42.103 137.867 1.00 10.51 ? 162 GLN B O     1 
ATOM   3446 C  CB    . GLN D 2 162 ? 17.932  40.865 139.584 1.00 10.21 ? 162 GLN B CB    1 
ATOM   3447 C  CG    . GLN D 2 162 ? 19.210  41.209 140.306 1.00 10.97 ? 162 GLN B CG    1 
ATOM   3448 C  CD    . GLN D 2 162 ? 19.261  42.688 140.591 1.00 11.98 ? 162 GLN B CD    1 
ATOM   3449 O  OE1   . GLN D 2 162 ? 19.501  43.492 139.696 1.00 15.33 ? 162 GLN B OE1   1 
ATOM   3450 N  NE2   . GLN D 2 162 ? 18.996  43.017 141.844 1.00 12.79 ? 162 GLN B NE2   1 
ATOM   3451 N  N     . VAL D 2 163 ? 15.189  40.060 138.831 1.00 9.73  ? 163 VAL B N     1 
ATOM   3452 C  CA    . VAL D 2 163 ? 14.298  39.494 137.798 1.00 8.78  ? 163 VAL B CA    1 
ATOM   3453 C  C     . VAL D 2 163 ? 13.014  38.965 138.401 1.00 9.13  ? 163 VAL B C     1 
ATOM   3454 O  O     . VAL D 2 163 ? 12.959  38.583 139.574 1.00 8.99  ? 163 VAL B O     1 
ATOM   3455 C  CB    . VAL D 2 163 ? 15.132  38.367 137.120 1.00 7.93  ? 163 VAL B CB    1 
ATOM   3456 C  CG1   . VAL D 2 163 ? 14.331  37.106 137.037 1.00 6.79  ? 163 VAL B CG1   1 
ATOM   3457 C  CG2   . VAL D 2 163 ? 15.759  38.796 135.824 1.00 7.02  ? 163 VAL B CG2   1 
ATOM   3458 N  N     . SER D 2 164 ? 11.964  38.882 137.601 1.00 10.02 ? 164 SER B N     1 
ATOM   3459 C  CA    . SER D 2 164 ? 10.665  38.407 138.086 1.00 10.69 ? 164 SER B CA    1 
ATOM   3460 C  C     . SER D 2 164 ? 10.201  37.101 137.487 1.00 10.94 ? 164 SER B C     1 
ATOM   3461 O  O     . SER D 2 164 ? 9.541   36.288 138.175 1.00 13.22 ? 164 SER B O     1 
ATOM   3462 C  CB    . SER D 2 164 ? 9.613   39.487 137.868 1.00 10.74 ? 164 SER B CB    1 
ATOM   3463 O  OG    . SER D 2 164 ? 8.870   39.208 136.712 1.00 10.25 ? 164 SER B OG    1 
ATOM   3464 N  N     . SER D 2 165 ? 10.435  36.860 136.225 1.00 9.89  ? 165 SER B N     1 
ATOM   3465 C  CA    . SER D 2 165 ? 9.983   35.583 135.605 1.00 9.63  ? 165 SER B CA    1 
ATOM   3466 C  C     . SER D 2 165 ? 11.046  35.149 134.612 1.00 8.59  ? 165 SER B C     1 
ATOM   3467 O  O     . SER D 2 165 ? 12.048  35.859 134.414 1.00 8.06  ? 165 SER B O     1 
ATOM   3468 C  CB    . SER D 2 165 ? 8.596   35.675 135.033 1.00 10.63 ? 165 SER B CB    1 
ATOM   3469 O  OG    . SER D 2 165 ? 8.227   37.030 134.872 1.00 13.40 ? 165 SER B OG    1 
ATOM   3470 N  N     . PHE D 2 166 ? 10.820  33.984 134.034 1.00 8.06  ? 166 PHE B N     1 
ATOM   3471 C  CA    . PHE D 2 166 ? 11.858  33.518 133.076 1.00 8.56  ? 166 PHE B CA    1 
ATOM   3472 C  C     . PHE D 2 166 ? 11.289  32.413 132.219 1.00 8.15  ? 166 PHE B C     1 
ATOM   3473 O  O     . PHE D 2 166 ? 10.293  31.799 132.609 1.00 8.44  ? 166 PHE B O     1 
ATOM   3474 C  CB    . PHE D 2 166 ? 13.076  32.997 133.885 1.00 7.91  ? 166 PHE B CB    1 
ATOM   3475 C  CG    . PHE D 2 166 ? 12.699  31.713 134.573 1.00 7.96  ? 166 PHE B CG    1 
ATOM   3476 C  CD1   . PHE D 2 166 ? 12.056  31.760 135.811 1.00 7.04  ? 166 PHE B CD1   1 
ATOM   3477 C  CD2   . PHE D 2 166 ? 12.958  30.492 133.958 1.00 7.89  ? 166 PHE B CD2   1 
ATOM   3478 C  CE1   . PHE D 2 166 ? 11.714  30.569 136.461 1.00 8.42  ? 166 PHE B CE1   1 
ATOM   3479 C  CE2   . PHE D 2 166 ? 12.614  29.298 134.588 1.00 9.39  ? 166 PHE B CE2   1 
ATOM   3480 C  CZ    . PHE D 2 166 ? 11.979  29.339 135.827 1.00 9.72  ? 166 PHE B CZ    1 
ATOM   3481 N  N     . ARG D 2 167 ? 11.949  32.194 131.108 1.00 7.62  ? 167 ARG B N     1 
ATOM   3482 C  CA    . ARG D 2 167 ? 11.534  31.097 130.214 1.00 7.40  ? 167 ARG B CA    1 
ATOM   3483 C  C     . ARG D 2 167 ? 12.830  30.518 129.661 1.00 8.07  ? 167 ARG B C     1 
ATOM   3484 O  O     . ARG D 2 167 ? 13.765  31.285 129.387 1.00 8.91  ? 167 ARG B O     1 
ATOM   3485 C  CB    . ARG D 2 167 ? 10.603  31.553 129.132 1.00 7.56  ? 167 ARG B CB    1 
ATOM   3486 C  CG    . ARG D 2 167 ? 11.280  32.266 127.964 1.00 9.07  ? 167 ARG B CG    1 
ATOM   3487 C  CD    . ARG D 2 167 ? 10.453  33.474 127.638 1.00 7.97  ? 167 ARG B CD    1 
ATOM   3488 N  NE    . ARG D 2 167 ? 9.217   33.106 126.976 1.00 6.36  ? 167 ARG B NE    1 
ATOM   3489 C  CZ    . ARG D 2 167 ? 8.945   33.566 125.751 1.00 7.06  ? 167 ARG B CZ    1 
ATOM   3490 N  NH1   . ARG D 2 167 ? 9.813   34.341 125.106 1.00 6.11  ? 167 ARG B NH1   1 
ATOM   3491 N  NH2   . ARG D 2 167 ? 7.783   33.226 125.195 1.00 7.69  ? 167 ARG B NH2   1 
ATOM   3492 N  N     . TYR D 2 168 ? 12.853  29.197 129.567 1.00 8.80  ? 168 TYR B N     1 
ATOM   3493 C  CA    . TYR D 2 168 ? 14.018  28.501 129.037 1.00 8.75  ? 168 TYR B CA    1 
ATOM   3494 C  C     . TYR D 2 168 ? 13.876  28.427 127.500 1.00 9.45  ? 168 TYR B C     1 
ATOM   3495 O  O     . TYR D 2 168 ? 12.803  28.118 126.978 1.00 9.81  ? 168 TYR B O     1 
ATOM   3496 C  CB    . TYR D 2 168 ? 14.202  27.066 129.525 1.00 6.96  ? 168 TYR B CB    1 
ATOM   3497 C  CG    . TYR D 2 168 ? 14.946  26.976 130.828 1.00 7.80  ? 168 TYR B CG    1 
ATOM   3498 C  CD1   . TYR D 2 168 ? 14.263  27.189 132.031 1.00 8.26  ? 168 TYR B CD1   1 
ATOM   3499 C  CD2   . TYR D 2 168 ? 16.294  26.691 130.877 1.00 8.05  ? 168 TYR B CD2   1 
ATOM   3500 C  CE1   . TYR D 2 168 ? 14.915  27.117 133.250 1.00 8.09  ? 168 TYR B CE1   1 
ATOM   3501 C  CE2   . TYR D 2 168 ? 16.956  26.612 132.097 1.00 6.74  ? 168 TYR B CE2   1 
ATOM   3502 C  CZ    . TYR D 2 168 ? 16.261  26.824 133.281 1.00 7.22  ? 168 TYR B CZ    1 
ATOM   3503 O  OH    . TYR D 2 168 ? 16.890  26.741 134.507 1.00 7.81  ? 168 TYR B OH    1 
ATOM   3504 N  N     . ALA D 2 169 ? 15.030  28.686 126.949 1.00 9.39  ? 169 ALA B N     1 
ATOM   3505 C  CA    . ALA D 2 169 ? 15.243  28.647 125.505 1.00 10.01 ? 169 ALA B CA    1 
ATOM   3506 C  C     . ALA D 2 169 ? 16.246  27.524 125.233 1.00 11.19 ? 169 ALA B C     1 
ATOM   3507 O  O     . ALA D 2 169 ? 16.286  27.034 124.082 1.00 12.67 ? 169 ALA B O     1 
ATOM   3508 C  CB    . ALA D 2 169 ? 15.694  30.019 125.038 1.00 10.23 ? 169 ALA B CB    1 
ATOM   3509 N  N     . SER D 2 170 ? 17.021  27.110 126.232 1.00 10.94 ? 170 SER B N     1 
ATOM   3510 C  CA    . SER D 2 170 ? 17.999  26.013 126.018 1.00 11.81 ? 170 SER B CA    1 
ATOM   3511 C  C     . SER D 2 170 ? 18.576  25.459 127.315 1.00 12.29 ? 170 SER B C     1 
ATOM   3512 O  O     . SER D 2 170 ? 18.672  26.133 128.347 1.00 14.17 ? 170 SER B O     1 
ATOM   3513 C  CB    . SER D 2 170 ? 19.072  26.429 125.019 1.00 12.54 ? 170 SER B CB    1 
ATOM   3514 O  OG    . SER D 2 170 ? 20.370  26.616 125.541 1.00 11.09 ? 170 SER B OG    1 
ATOM   3515 N  N     . MET D 2 171 ? 18.981  24.193 127.202 1.00 11.77 ? 171 MET B N     1 
ATOM   3516 C  CA    . MET D 2 171 ? 19.592  23.402 128.293 1.00 10.51 ? 171 MET B CA    1 
ATOM   3517 C  C     . MET D 2 171 ? 20.405  22.240 127.744 1.00 10.19 ? 171 MET B C     1 
ATOM   3518 O  O     . MET D 2 171 ? 19.867  21.203 127.302 1.00 10.96 ? 171 MET B O     1 
ATOM   3519 C  CB    . MET D 2 171 ? 18.456  23.007 129.238 1.00 9.12  ? 171 MET B CB    1 
ATOM   3520 C  CG    . MET D 2 171 ? 18.861  22.455 130.561 1.00 9.57  ? 171 MET B CG    1 
ATOM   3521 S  SD    . MET D 2 171 ? 17.371  22.324 131.641 1.00 11.79 ? 171 MET B SD    1 
ATOM   3522 C  CE    . MET D 2 171 ? 16.725  20.735 131.114 1.00 7.44  ? 171 MET B CE    1 
ATOM   3523 N  N     . ASN D 2 172 ? 21.721  22.321 127.748 1.00 9.44  ? 172 ASN B N     1 
ATOM   3524 C  CA    . ASN D 2 172 ? 22.573  21.223 127.258 1.00 9.35  ? 172 ASN B CA    1 
ATOM   3525 C  C     . ASN D 2 172 ? 23.541  20.756 128.369 1.00 9.65  ? 172 ASN B C     1 
ATOM   3526 O  O     . ASN D 2 172 ? 23.658  21.350 129.432 1.00 10.25 ? 172 ASN B O     1 
ATOM   3527 C  CB    . ASN D 2 172 ? 23.323  21.563 125.983 1.00 8.94  ? 172 ASN B CB    1 
ATOM   3528 C  CG    . ASN D 2 172 ? 22.510  22.035 124.807 1.00 10.50 ? 172 ASN B CG    1 
ATOM   3529 O  OD1   . ASN D 2 172 ? 22.063  21.282 123.910 1.00 12.70 ? 172 ASN B OD1   1 
ATOM   3530 N  ND2   . ASN D 2 172 ? 22.338  23.365 124.779 1.00 9.27  ? 172 ASN B ND2   1 
ATOM   3531 N  N     . VAL D 2 173 ? 24.229  19.681 128.034 1.00 9.48  ? 173 VAL B N     1 
ATOM   3532 C  CA    . VAL D 2 173 ? 25.227  18.976 128.826 1.00 9.28  ? 173 VAL B CA    1 
ATOM   3533 C  C     . VAL D 2 173 ? 26.164  18.122 127.957 1.00 10.12 ? 173 VAL B C     1 
ATOM   3534 O  O     . VAL D 2 173 ? 25.770  17.498 126.944 1.00 10.53 ? 173 VAL B O     1 
ATOM   3535 C  CB    . VAL D 2 173 ? 24.528  18.082 129.878 1.00 8.47  ? 173 VAL B CB    1 
ATOM   3536 C  CG1   . VAL D 2 173 ? 23.936  16.826 129.261 1.00 6.52  ? 173 VAL B CG1   1 
ATOM   3537 C  CG2   . VAL D 2 173 ? 25.447  17.774 131.037 1.00 7.16  ? 173 VAL B CG2   1 
ATOM   3538 N  N     . GLY D 2 174 ? 27.415  18.101 128.393 1.00 10.37 ? 174 GLY B N     1 
ATOM   3539 C  CA    . GLY D 2 174 ? 28.465  17.322 127.703 1.00 10.03 ? 174 GLY B CA    1 
ATOM   3540 C  C     . GLY D 2 174 ? 29.510  16.885 128.736 1.00 10.37 ? 174 GLY B C     1 
ATOM   3541 O  O     . GLY D 2 174 ? 29.838  17.651 129.649 1.00 10.05 ? 174 GLY B O     1 
ATOM   3542 N  N     . ILE D 2 175 ? 29.959  15.657 128.576 1.00 10.01 ? 175 ILE B N     1 
ATOM   3543 C  CA    . ILE D 2 175 ? 30.976  15.027 129.422 1.00 9.75  ? 175 ILE B CA    1 
ATOM   3544 C  C     . ILE D 2 175 ? 32.148  14.657 128.511 1.00 10.29 ? 175 ILE B C     1 
ATOM   3545 O  O     . ILE D 2 175 ? 31.974  13.884 127.554 1.00 10.46 ? 175 ILE B O     1 
ATOM   3546 C  CB    . ILE D 2 175 ? 30.463  13.829 130.269 1.00 8.85  ? 175 ILE B CB    1 
ATOM   3547 C  CG1   . ILE D 2 175 ? 29.232  14.289 131.090 1.00 7.89  ? 175 ILE B CG1   1 
ATOM   3548 C  CG2   . ILE D 2 175 ? 31.548  13.233 131.200 1.00 9.26  ? 175 ILE B CG2   1 
ATOM   3549 C  CD1   . ILE D 2 175 ? 28.773  13.271 132.156 1.00 8.74  ? 175 ILE B CD1   1 
ATOM   3550 N  N     . TYR D 2 176 ? 33.278  15.261 128.826 1.00 9.42  ? 176 TYR B N     1 
ATOM   3551 C  CA    . TYR D 2 176 ? 34.495  15.034 128.014 1.00 9.21  ? 176 TYR B CA    1 
ATOM   3552 C  C     . TYR D 2 176 ? 35.548  14.297 128.826 1.00 8.84  ? 176 TYR B C     1 
ATOM   3553 O  O     . TYR D 2 176 ? 36.350  14.914 129.559 1.00 9.09  ? 176 TYR B O     1 
ATOM   3554 C  CB    . TYR D 2 176 ? 34.921  16.418 127.486 1.00 9.49  ? 176 TYR B CB    1 
ATOM   3555 C  CG    . TYR D 2 176 ? 33.794  17.122 126.775 1.00 8.98  ? 176 TYR B CG    1 
ATOM   3556 C  CD1   . TYR D 2 176 ? 33.523  16.874 125.432 1.00 11.00 ? 176 TYR B CD1   1 
ATOM   3557 C  CD2   . TYR D 2 176 ? 32.979  18.037 127.420 1.00 10.09 ? 176 TYR B CD2   1 
ATOM   3558 C  CE1   . TYR D 2 176 ? 32.493  17.524 124.750 1.00 13.05 ? 176 TYR B CE1   1 
ATOM   3559 C  CE2   . TYR D 2 176 ? 31.939  18.693 126.766 1.00 12.12 ? 176 TYR B CE2   1 
ATOM   3560 C  CZ    . TYR D 2 176 ? 31.697  18.443 125.424 1.00 14.66 ? 176 TYR B CZ    1 
ATOM   3561 O  OH    . TYR D 2 176 ? 30.658  19.095 124.804 1.00 17.77 ? 176 TYR B OH    1 
ATOM   3562 N  N     . PRO D 2 177 ? 35.543  12.969 128.692 1.00 8.50  ? 177 PRO B N     1 
ATOM   3563 C  CA    . PRO D 2 177 ? 36.480  12.112 129.428 1.00 8.07  ? 177 PRO B CA    1 
ATOM   3564 C  C     . PRO D 2 177 ? 37.886  12.647 129.206 1.00 8.68  ? 177 PRO B C     1 
ATOM   3565 O  O     . PRO D 2 177 ? 38.194  13.164 128.118 1.00 8.52  ? 177 PRO B O     1 
ATOM   3566 C  CB    . PRO D 2 177 ? 36.253  10.717 128.922 1.00 7.25  ? 177 PRO B CB    1 
ATOM   3567 C  CG    . PRO D 2 177 ? 34.892  10.741 128.287 1.00 7.52  ? 177 PRO B CG    1 
ATOM   3568 C  CD    . PRO D 2 177 ? 34.647  12.180 127.840 1.00 7.99  ? 177 PRO B CD    1 
ATOM   3569 N  N     . THR D 2 178 ? 38.673  12.493 130.245 1.00 9.36  ? 178 THR B N     1 
ATOM   3570 C  CA    . THR D 2 178 ? 40.046  12.950 130.338 1.00 9.43  ? 178 THR B CA    1 
ATOM   3571 C  C     . THR D 2 178 ? 41.084  11.932 130.761 1.00 10.06 ? 178 THR B C     1 
ATOM   3572 O  O     . THR D 2 178 ? 42.313  12.208 130.770 1.00 9.81  ? 178 THR B O     1 
ATOM   3573 C  CB    . THR D 2 178 ? 39.968  14.156 131.396 1.00 9.69  ? 178 THR B CB    1 
ATOM   3574 O  OG1   . THR D 2 178 ? 39.913  15.347 130.565 1.00 11.84 ? 178 THR B OG1   1 
ATOM   3575 C  CG2   . THR D 2 178 ? 41.104  14.103 132.404 1.00 10.55 ? 178 THR B CG2   1 
ATOM   3576 N  N     . SER D 2 179 ? 40.635  10.754 131.145 1.00 10.49 ? 179 SER B N     1 
ATOM   3577 C  CA    . SER D 2 179 ? 41.481  9.651  131.613 1.00 9.64  ? 179 SER B CA    1 
ATOM   3578 C  C     . SER D 2 179 ? 42.205  9.054  130.415 1.00 9.44  ? 179 SER B C     1 
ATOM   3579 O  O     . SER D 2 179 ? 41.713  9.241  129.282 1.00 10.18 ? 179 SER B O     1 
ATOM   3580 C  CB    . SER D 2 179 ? 40.649  8.572  132.284 1.00 9.63  ? 179 SER B CB    1 
ATOM   3581 O  OG    . SER D 2 179 ? 39.638  9.079  133.127 1.00 8.29  ? 179 SER B OG    1 
ATOM   3582 N  N     . ASN D 2 180 ? 43.302  8.388  130.693 1.00 9.40  ? 180 ASN B N     1 
ATOM   3583 C  CA    . ASN D 2 180 ? 44.093  7.755  129.599 1.00 10.37 ? 180 ASN B CA    1 
ATOM   3584 C  C     . ASN D 2 180 ? 43.544  6.329  129.406 1.00 11.25 ? 180 ASN B C     1 
ATOM   3585 O  O     . ASN D 2 180 ? 42.758  5.831  130.225 1.00 12.48 ? 180 ASN B O     1 
ATOM   3586 C  CB    . ASN D 2 180 ? 45.572  7.881  129.949 1.00 9.70  ? 180 ASN B CB    1 
ATOM   3587 C  CG    . ASN D 2 180 ? 45.880  7.039  131.184 1.00 12.70 ? 180 ASN B CG    1 
ATOM   3588 O  OD1   . ASN D 2 180 ? 45.636  5.830  131.172 1.00 14.20 ? 180 ASN B OD1   1 
ATOM   3589 N  ND2   . ASN D 2 180 ? 46.379  7.607  132.263 1.00 11.60 ? 180 ASN B ND2   1 
ATOM   3590 N  N     . LEU D 2 181 ? 43.962  5.712  128.320 1.00 10.87 ? 181 LEU B N     1 
ATOM   3591 C  CA    . LEU D 2 181 ? 43.455  4.391  127.891 1.00 10.91 ? 181 LEU B CA    1 
ATOM   3592 C  C     . LEU D 2 181 ? 43.809  3.246  128.841 1.00 11.49 ? 181 LEU B C     1 
ATOM   3593 O  O     . LEU D 2 181 ? 43.468  2.080  128.591 1.00 13.14 ? 181 LEU B O     1 
ATOM   3594 C  CB    . LEU D 2 181 ? 44.022  4.028  126.525 1.00 8.22  ? 181 LEU B CB    1 
ATOM   3595 C  CG    . LEU D 2 181 ? 43.207  4.633  125.391 1.00 4.58  ? 181 LEU B CG    1 
ATOM   3596 C  CD1   . LEU D 2 181 ? 42.104  5.565  125.900 1.00 2.82  ? 181 LEU B CD1   1 
ATOM   3597 C  CD2   . LEU D 2 181 ? 44.058  5.461  124.430 1.00 3.12  ? 181 LEU B CD2   1 
ATOM   3598 N  N     . MET D 2 182 ? 44.474  3.558  129.924 1.00 11.68 ? 182 MET B N     1 
ATOM   3599 C  CA    . MET D 2 182 ? 44.871  2.515  130.870 1.00 11.85 ? 182 MET B CA    1 
ATOM   3600 C  C     . MET D 2 182 ? 44.192  2.698  132.227 1.00 11.67 ? 182 MET B C     1 
ATOM   3601 O  O     . MET D 2 182 ? 44.346  1.861  133.130 1.00 12.54 ? 182 MET B O     1 
ATOM   3602 C  CB    . MET D 2 182 ? 46.390  2.534  131.060 1.00 12.68 ? 182 MET B CB    1 
ATOM   3603 C  CG    . MET D 2 182 ? 46.828  2.907  132.476 1.00 12.98 ? 182 MET B CG    1 
ATOM   3604 S  SD    . MET D 2 182 ? 48.541  2.534  132.767 1.00 17.29 ? 182 MET B SD    1 
ATOM   3605 C  CE    . MET D 2 182 ? 48.898  0.909  132.137 1.00 15.39 ? 182 MET B CE    1 
ATOM   3606 N  N     . GLN D 2 183 ? 43.415  3.773  132.372 1.00 10.88 ? 183 GLN B N     1 
ATOM   3607 C  CA    . GLN D 2 183 ? 42.813  4.060  133.685 1.00 10.26 ? 183 GLN B CA    1 
ATOM   3608 C  C     . GLN D 2 183 ? 41.315  4.162  133.740 1.00 9.71  ? 183 GLN B C     1 
ATOM   3609 O  O     . GLN D 2 183 ? 40.769  4.023  134.862 1.00 11.63 ? 183 GLN B O     1 
ATOM   3610 C  CB    . GLN D 2 183 ? 43.376  5.349  134.289 1.00 10.53 ? 183 GLN B CB    1 
ATOM   3611 C  CG    . GLN D 2 183 ? 43.115  6.598  133.456 1.00 10.14 ? 183 GLN B CG    1 
ATOM   3612 C  CD    . GLN D 2 183 ? 43.724  7.847  134.094 1.00 10.30 ? 183 GLN B CD    1 
ATOM   3613 O  OE1   . GLN D 2 183 ? 43.456  8.959  133.646 1.00 10.79 ? 183 GLN B OE1   1 
ATOM   3614 N  NE2   . GLN D 2 183 ? 44.536  7.725  135.129 1.00 8.60  ? 183 GLN B NE2   1 
ATOM   3615 N  N     . PHE D 2 184 ? 40.601  4.479  132.718 1.00 8.57  ? 184 PHE B N     1 
ATOM   3616 C  CA    . PHE D 2 184 ? 39.141  4.622  132.734 1.00 8.27  ? 184 PHE B CA    1 
ATOM   3617 C  C     . PHE D 2 184 ? 38.422  3.280  132.714 1.00 8.47  ? 184 PHE B C     1 
ATOM   3618 O  O     . PHE D 2 184 ? 38.931  2.310  132.150 1.00 9.27  ? 184 PHE B O     1 
ATOM   3619 C  CB    . PHE D 2 184 ? 38.709  5.385  131.453 1.00 8.15  ? 184 PHE B CB    1 
ATOM   3620 C  CG    . PHE D 2 184 ? 38.480  4.374  130.363 1.00 6.46  ? 184 PHE B CG    1 
ATOM   3621 C  CD1   . PHE D 2 184 ? 39.571  3.966  129.598 1.00 6.27  ? 184 PHE B CD1   1 
ATOM   3622 C  CD2   . PHE D 2 184 ? 37.230  3.837  130.163 1.00 5.84  ? 184 PHE B CD2   1 
ATOM   3623 C  CE1   . PHE D 2 184 ? 39.407  3.041  128.580 1.00 4.99  ? 184 PHE B CE1   1 
ATOM   3624 C  CE2   . PHE D 2 184 ? 37.025  2.902  129.153 1.00 5.60  ? 184 PHE B CE2   1 
ATOM   3625 C  CZ    . PHE D 2 184 ? 38.132  2.510  128.367 1.00 4.91  ? 184 PHE B CZ    1 
ATOM   3626 N  N     . ALA D 2 185 ? 37.235  3.265  133.270 1.00 7.96  ? 185 ALA B N     1 
ATOM   3627 C  CA    . ALA D 2 185 ? 36.360  2.094  133.320 1.00 8.21  ? 185 ALA B CA    1 
ATOM   3628 C  C     . ALA D 2 185 ? 35.028  2.499  133.965 1.00 8.96  ? 185 ALA B C     1 
ATOM   3629 O  O     . ALA D 2 185 ? 35.015  3.033  135.065 1.00 8.95  ? 185 ALA B O     1 
ATOM   3630 C  CB    . ALA D 2 185 ? 36.864  0.876  134.058 1.00 7.88  ? 185 ALA B CB    1 
ATOM   3631 N  N     . GLY D 2 186 ? 34.014  2.179  133.217 1.00 10.02 ? 186 GLY B N     1 
ATOM   3632 C  CA    . GLY D 2 186 ? 32.634  2.489  133.599 1.00 11.07 ? 186 GLY B CA    1 
ATOM   3633 C  C     . GLY D 2 186 ? 31.885  2.852  132.310 1.00 11.31 ? 186 GLY B C     1 
ATOM   3634 O  O     . GLY D 2 186 ? 32.337  2.660  131.165 1.00 11.84 ? 186 GLY B O     1 
ATOM   3635 N  N     . SER D 2 187 ? 30.709  3.385  132.555 1.00 10.15 ? 187 SER B N     1 
ATOM   3636 C  CA    . SER D 2 187 ? 29.817  3.741  131.440 1.00 10.01 ? 187 SER B CA    1 
ATOM   3637 C  C     . SER D 2 187 ? 29.035  4.990  131.812 1.00 10.29 ? 187 SER B C     1 
ATOM   3638 O  O     . SER D 2 187 ? 29.103  5.366  132.992 1.00 11.05 ? 187 SER B O     1 
ATOM   3639 C  CB    . SER D 2 187 ? 28.818  2.549  131.368 1.00 9.12  ? 187 SER B CB    1 
ATOM   3640 O  OG    . SER D 2 187 ? 28.048  2.639  132.581 1.00 8.74  ? 187 SER B OG    1 
ATOM   3641 N  N     . ILE D 2 188 ? 28.355  5.493  130.818 1.00 9.40  ? 188 ILE B N     1 
ATOM   3642 C  CA    . ILE D 2 188 ? 27.483  6.663  130.919 1.00 10.36 ? 188 ILE B CA    1 
ATOM   3643 C  C     . ILE D 2 188 ? 26.123  6.264  130.334 1.00 11.80 ? 188 ILE B C     1 
ATOM   3644 O  O     . ILE D 2 188 ? 26.037  5.645  129.262 1.00 13.21 ? 188 ILE B O     1 
ATOM   3645 C  CB    . ILE D 2 188 ? 28.095  7.900  130.208 1.00 9.10  ? 188 ILE B CB    1 
ATOM   3646 C  CG1   . ILE D 2 188 ? 29.276  8.480  131.032 1.00 9.13  ? 188 ILE B CG1   1 
ATOM   3647 C  CG2   . ILE D 2 188 ? 27.027  8.975  129.912 1.00 7.08  ? 188 ILE B CG2   1 
ATOM   3648 C  CD1   . ILE D 2 188 ? 30.409  9.078  130.127 1.00 9.69  ? 188 ILE B CD1   1 
ATOM   3649 N  N     . THR D 2 189 ? 25.082  6.576  131.064 1.00 11.67 ? 189 THR B N     1 
ATOM   3650 C  CA    . THR D 2 189 ? 23.707  6.255  130.682 1.00 10.93 ? 189 THR B CA    1 
ATOM   3651 C  C     . THR D 2 189 ? 22.881  7.530  130.874 1.00 10.53 ? 189 THR B C     1 
ATOM   3652 O  O     . THR D 2 189 ? 22.933  8.092  131.975 1.00 10.45 ? 189 THR B O     1 
ATOM   3653 C  CB    . THR D 2 189 ? 23.071  5.123  131.571 1.00 10.21 ? 189 THR B CB    1 
ATOM   3654 O  OG1   . THR D 2 189 ? 24.018  4.022  131.659 1.00 11.16 ? 189 THR B OG1   1 
ATOM   3655 C  CG2   . THR D 2 189 ? 21.679  4.656  131.132 1.00 10.53 ? 189 THR B CG2   1 
ATOM   3656 N  N     . VAL D 2 190 ? 22.148  7.897  129.852 1.00 10.35 ? 190 VAL B N     1 
ATOM   3657 C  CA    . VAL D 2 190 ? 21.292  9.070  129.880 1.00 10.27 ? 190 VAL B CA    1 
ATOM   3658 C  C     . VAL D 2 190 ? 19.853  8.712  129.513 1.00 10.75 ? 190 VAL B C     1 
ATOM   3659 O  O     . VAL D 2 190 ? 19.606  7.863  128.645 1.00 11.67 ? 190 VAL B O     1 
ATOM   3660 C  CB    . VAL D 2 190 ? 21.820  10.123 128.882 1.00 8.96  ? 190 VAL B CB    1 
ATOM   3661 C  CG1   . VAL D 2 190 ? 20.971  11.396 128.852 1.00 6.78  ? 190 VAL B CG1   1 
ATOM   3662 C  CG2   . VAL D 2 190 ? 23.246  10.581 129.195 1.00 8.60  ? 190 VAL B CG2   1 
ATOM   3663 N  N     . TRP D 2 191 ? 18.962  9.380  130.217 1.00 10.02 ? 191 TRP B N     1 
ATOM   3664 C  CA    . TRP D 2 191 ? 17.514  9.282  130.002 1.00 9.78  ? 191 TRP B CA    1 
ATOM   3665 C  C     . TRP D 2 191 ? 16.893  10.566 130.546 1.00 10.48 ? 191 TRP B C     1 
ATOM   3666 O  O     . TRP D 2 191 ? 17.466  11.234 131.418 1.00 11.67 ? 191 TRP B O     1 
ATOM   3667 C  CB    . TRP D 2 191 ? 16.957  7.954  130.589 1.00 9.76  ? 191 TRP B CB    1 
ATOM   3668 C  CG    . TRP D 2 191 ? 16.746  7.851  132.125 1.00 9.87  ? 191 TRP B CG    1 
ATOM   3669 C  CD1   . TRP D 2 191 ? 15.601  8.045  132.807 1.00 10.52 ? 191 TRP B CD1   1 
ATOM   3670 C  CD2   . TRP D 2 191 ? 17.744  7.494  133.082 1.00 8.10  ? 191 TRP B CD2   1 
ATOM   3671 N  NE1   . TRP D 2 191 ? 15.869  7.771  134.191 1.00 10.71 ? 191 TRP B NE1   1 
ATOM   3672 C  CE2   . TRP D 2 191 ? 17.127  7.437  134.327 1.00 9.15  ? 191 TRP B CE2   1 
ATOM   3673 C  CE3   . TRP D 2 191 ? 19.109  7.205  132.986 1.00 8.08  ? 191 TRP B CE3   1 
ATOM   3674 C  CZ2   . TRP D 2 191 ? 17.800  7.066  135.501 1.00 8.52  ? 191 TRP B CZ2   1 
ATOM   3675 C  CZ3   . TRP D 2 191 ? 19.783  6.855  134.175 1.00 8.21  ? 191 TRP B CZ3   1 
ATOM   3676 C  CH2   . TRP D 2 191 ? 19.158  6.785  135.372 1.00 8.56  ? 191 TRP B CH2   1 
ATOM   3677 N  N     . LYS D 2 192 ? 15.747  10.906 129.999 1.00 10.17 ? 192 LYS B N     1 
ATOM   3678 C  CA    . LYS D 2 192 ? 15.046  12.137 130.375 1.00 9.42  ? 192 LYS B CA    1 
ATOM   3679 C  C     . LYS D 2 192 ? 13.748  11.814 131.100 1.00 9.53  ? 192 LYS B C     1 
ATOM   3680 O  O     . LYS D 2 192 ? 13.194  10.719 130.957 1.00 10.01 ? 192 LYS B O     1 
ATOM   3681 C  CB    . LYS D 2 192 ? 14.752  12.965 129.121 1.00 6.03  ? 192 LYS B CB    1 
ATOM   3682 C  CG    . LYS D 2 192 ? 15.973  13.754 128.630 1.00 4.84  ? 192 LYS B CG    1 
ATOM   3683 C  CD    . LYS D 2 192 ? 16.479  13.293 127.260 1.00 3.01  ? 192 LYS B CD    1 
ATOM   3684 C  CE    . LYS D 2 192 ? 17.526  14.237 126.660 1.00 2.73  ? 192 LYS B CE    1 
ATOM   3685 N  NZ    . LYS D 2 192 ? 17.322  14.482 125.224 1.00 3.25  ? 192 LYS B NZ    1 
ATOM   3686 N  N     . CYS D 2 193 ? 13.262  12.771 131.875 1.00 9.99  ? 193 CYS B N     1 
ATOM   3687 C  CA    . CYS D 2 193 ? 12.051  12.530 132.674 1.00 9.84  ? 193 CYS B CA    1 
ATOM   3688 C  C     . CYS D 2 193 ? 11.223  13.783 132.929 1.00 9.50  ? 193 CYS B C     1 
ATOM   3689 O  O     . CYS D 2 193 ? 11.752  14.820 133.362 1.00 10.13 ? 193 CYS B O     1 
ATOM   3690 C  CB    . CYS D 2 193 ? 12.432  11.980 134.037 1.00 10.55 ? 193 CYS B CB    1 
ATOM   3691 S  SG    . CYS D 2 193 ? 13.553  10.505 133.929 1.00 11.35 ? 193 CYS B SG    1 
ATOM   3692 N  N     . PRO D 2 194 ? 9.906   13.711 132.663 1.00 9.00  ? 194 PRO B N     1 
ATOM   3693 C  CA    . PRO D 2 194 ? 9.000   14.822 132.890 1.00 8.87  ? 194 PRO B CA    1 
ATOM   3694 C  C     . PRO D 2 194 ? 8.764   15.139 134.330 1.00 9.55  ? 194 PRO B C     1 
ATOM   3695 O  O     . PRO D 2 194 ? 7.686   14.792 134.890 1.00 10.04 ? 194 PRO B O     1 
ATOM   3696 C  CB    . PRO D 2 194 ? 7.680   14.368 132.345 1.00 8.33  ? 194 PRO B CB    1 
ATOM   3697 C  CG    . PRO D 2 194 ? 7.849   12.948 131.853 1.00 7.54  ? 194 PRO B CG    1 
ATOM   3698 C  CD    . PRO D 2 194 ? 9.266   12.513 132.105 1.00 7.91  ? 194 PRO B CD    1 
ATOM   3699 N  N     . VAL D 2 195 ? 9.674   15.805 134.949 1.00 9.95  ? 195 VAL B N     1 
ATOM   3700 C  CA    . VAL D 2 195 ? 9.425   16.172 136.323 1.00 10.81 ? 195 VAL B CA    1 
ATOM   3701 C  C     . VAL D 2 195 ? 8.905   17.607 136.373 1.00 10.97 ? 195 VAL B C     1 
ATOM   3702 O  O     . VAL D 2 195 ? 9.602   18.550 135.973 1.00 12.25 ? 195 VAL B O     1 
ATOM   3703 C  CB    . VAL D 2 195 ? 10.686  16.025 137.147 1.00 10.43 ? 195 VAL B CB    1 
ATOM   3704 C  CG1   . VAL D 2 195 ? 11.891  15.582 136.323 1.00 9.65  ? 195 VAL B CG1   1 
ATOM   3705 C  CG2   . VAL D 2 195 ? 11.088  17.325 137.834 1.00 10.71 ? 195 VAL B CG2   1 
ATOM   3706 N  N     . LYS D 2 196 ? 7.680   17.715 136.861 1.00 10.27 ? 196 LYS B N     1 
ATOM   3707 C  CA    . LYS D 2 196 ? 6.991   19.005 137.036 1.00 9.53  ? 196 LYS B CA    1 
ATOM   3708 C  C     . LYS D 2 196 ? 6.861   19.315 138.523 1.00 9.41  ? 196 LYS B C     1 
ATOM   3709 O  O     . LYS D 2 196 ? 6.774   18.402 139.358 1.00 8.87  ? 196 LYS B O     1 
ATOM   3710 C  CB    . LYS D 2 196 ? 5.583   18.949 136.438 1.00 7.91  ? 196 LYS B CB    1 
ATOM   3711 C  CG    . LYS D 2 196 ? 5.552   18.372 135.025 1.00 8.61  ? 196 LYS B CG    1 
ATOM   3712 C  CD    . LYS D 2 196 ? 6.431   19.147 134.044 1.00 9.63  ? 196 LYS B CD    1 
ATOM   3713 C  CE    . LYS D 2 196 ? 5.907   19.100 132.607 1.00 12.09 ? 196 LYS B CE    1 
ATOM   3714 N  NZ    . LYS D 2 196 ? 4.927   20.157 132.318 1.00 13.67 ? 196 LYS B NZ    1 
ATOM   3715 N  N     . LEU D 2 197 ? 6.851   20.601 138.799 1.00 9.06  ? 197 LEU B N     1 
ATOM   3716 C  CA    . LEU D 2 197 ? 6.717   21.121 140.162 1.00 9.02  ? 197 LEU B CA    1 
ATOM   3717 C  C     . LEU D 2 197 ? 5.248   21.409 140.450 1.00 9.42  ? 197 LEU B C     1 
ATOM   3718 O  O     . LEU D 2 197 ? 4.687   22.406 139.972 1.00 10.47 ? 197 LEU B O     1 
ATOM   3719 C  CB    . LEU D 2 197 ? 7.493   22.432 140.293 1.00 7.31  ? 197 LEU B CB    1 
ATOM   3720 C  CG    . LEU D 2 197 ? 7.322   23.093 141.662 1.00 6.77  ? 197 LEU B CG    1 
ATOM   3721 C  CD1   . LEU D 2 197 ? 7.886   22.250 142.808 1.00 5.60  ? 197 LEU B CD1   1 
ATOM   3722 C  CD2   . LEU D 2 197 ? 8.022   24.450 141.763 1.00 6.37  ? 197 LEU B CD2   1 
ATOM   3723 N  N     . SER D 2 198 ? 4.680   20.516 141.220 1.00 9.35  ? 198 SER B N     1 
ATOM   3724 C  CA    . SER D 2 198 ? 3.277   20.586 141.627 1.00 9.69  ? 198 SER B CA    1 
ATOM   3725 C  C     . SER D 2 198 ? 3.216   20.804 143.133 1.00 10.79 ? 198 SER B C     1 
ATOM   3726 O  O     . SER D 2 198 ? 4.183   21.260 143.756 1.00 12.07 ? 198 SER B O     1 
ATOM   3727 C  CB    . SER D 2 198 ? 2.586   19.274 141.253 1.00 7.61  ? 198 SER B CB    1 
ATOM   3728 O  OG    . SER D 2 198 ? 1.207   19.340 141.567 1.00 6.98  ? 198 SER B OG    1 
ATOM   3729 N  N     . ASN D 2 199 ? 2.081   20.478 143.706 1.00 11.35 ? 199 ASN B N     1 
ATOM   3730 C  CA    . ASN D 2 199 ? 1.900   20.608 145.160 1.00 11.42 ? 199 ASN B CA    1 
ATOM   3731 C  C     . ASN D 2 199 ? 1.327   19.302 145.758 1.00 12.26 ? 199 ASN B C     1 
ATOM   3732 O  O     . ASN D 2 199 ? 0.856   18.425 145.016 1.00 12.77 ? 199 ASN B O     1 
ATOM   3733 C  CB    . ASN D 2 199 ? 0.957   21.777 145.480 1.00 9.67  ? 199 ASN B CB    1 
ATOM   3734 C  CG    . ASN D 2 199 ? -0.231  21.902 144.520 1.00 10.99 ? 199 ASN B CG    1 
ATOM   3735 O  OD1   . ASN D 2 199 ? -0.939  20.924 144.286 1.00 13.20 ? 199 ASN B OD1   1 
ATOM   3736 N  ND2   . ASN D 2 199 ? -0.500  23.063 143.949 1.00 9.88  ? 199 ASN B ND2   1 
ATOM   3737 N  N     . VAL D 2 200 ? 1.413   19.236 147.105 1.00 12.12 ? 200 VAL B N     1 
ATOM   3738 C  CA    . VAL D 2 200 ? 0.869   18.123 147.960 1.00 11.34 ? 200 VAL B CA    1 
ATOM   3739 C  C     . VAL D 2 200 ? 0.010   18.752 149.064 1.00 11.90 ? 200 VAL B C     1 
ATOM   3740 O  O     . VAL D 2 200 ? 0.540   19.715 149.653 1.00 12.17 ? 200 VAL B O     1 
ATOM   3741 C  CB    . VAL D 2 200 ? 1.993   17.286 148.577 1.00 11.11 ? 200 VAL B CB    1 
ATOM   3742 C  CG1   . VAL D 2 200 ? 2.837   18.057 149.591 1.00 11.10 ? 200 VAL B CG1   1 
ATOM   3743 C  CG2   . VAL D 2 200 ? 1.466   16.054 149.325 1.00 10.41 ? 200 VAL B CG2   1 
ATOM   3744 N  N     . GLN D 2 201 ? -1.157  18.200 149.261 1.00 11.94 ? 201 GLN B N     1 
ATOM   3745 C  CA    . GLN D 2 201 ? -2.046  18.732 150.339 1.00 11.68 ? 201 GLN B CA    1 
ATOM   3746 C  C     . GLN D 2 201 ? -2.330  17.604 151.323 1.00 10.75 ? 201 GLN B C     1 
ATOM   3747 O  O     . GLN D 2 201 ? -2.795  16.521 150.937 1.00 11.03 ? 201 GLN B O     1 
ATOM   3748 C  CB    . GLN D 2 201 ? -3.279  19.384 149.810 1.00 14.14 ? 201 GLN B CB    1 
ATOM   3749 C  CG    . GLN D 2 201 ? -4.581  18.614 149.932 1.00 19.52 ? 201 GLN B CG    1 
ATOM   3750 C  CD    . GLN D 2 201 ? -5.750  19.470 149.426 1.00 23.37 ? 201 GLN B CD    1 
ATOM   3751 O  OE1   . GLN D 2 201 ? -6.802  18.944 149.078 1.00 24.82 ? 201 GLN B OE1   1 
ATOM   3752 N  NE2   . GLN D 2 201 ? -5.620  20.788 149.363 1.00 22.69 ? 201 GLN B NE2   1 
ATOM   3753 N  N     . PHE D 2 202 ? -2.006  17.913 152.566 1.00 10.06 ? 202 PHE B N     1 
ATOM   3754 C  CA    . PHE D 2 202 ? -2.142  16.978 153.684 1.00 10.08 ? 202 PHE B CA    1 
ATOM   3755 C  C     . PHE D 2 202 ? -2.564  17.651 154.979 1.00 10.62 ? 202 PHE B C     1 
ATOM   3756 O  O     . PHE D 2 202 ? -2.005  18.686 155.371 1.00 10.88 ? 202 PHE B O     1 
ATOM   3757 C  CB    . PHE D 2 202 ? -0.793  16.331 153.991 1.00 9.04  ? 202 PHE B CB    1 
ATOM   3758 C  CG    . PHE D 2 202 ? 0.316   17.358 154.228 1.00 8.39  ? 202 PHE B CG    1 
ATOM   3759 C  CD1   . PHE D 2 202 ? 0.756   18.169 153.175 1.00 9.06  ? 202 PHE B CD1   1 
ATOM   3760 C  CD2   . PHE D 2 202 ? 0.890   17.489 155.498 1.00 7.67  ? 202 PHE B CD2   1 
ATOM   3761 C  CE1   . PHE D 2 202 ? 1.769   19.110 153.391 1.00 9.39  ? 202 PHE B CE1   1 
ATOM   3762 C  CE2   . PHE D 2 202 ? 1.904   18.431 155.715 1.00 8.06  ? 202 PHE B CE2   1 
ATOM   3763 C  CZ    . PHE D 2 202 ? 2.343   19.241 154.661 1.00 8.28  ? 202 PHE B CZ    1 
ATOM   3764 N  N     . PRO D 2 203 ? -3.557  17.095 155.673 1.00 10.58 ? 203 PRO B N     1 
ATOM   3765 C  CA    . PRO D 2 203 ? -3.984  17.622 156.953 1.00 10.89 ? 203 PRO B CA    1 
ATOM   3766 C  C     . PRO D 2 203 ? -2.894  17.472 157.997 1.00 11.66 ? 203 PRO B C     1 
ATOM   3767 O  O     . PRO D 2 203 ? -2.317  16.350 158.134 1.00 12.34 ? 203 PRO B O     1 
ATOM   3768 C  CB    . PRO D 2 203 ? -5.156  16.747 157.334 1.00 10.19 ? 203 PRO B CB    1 
ATOM   3769 C  CG    . PRO D 2 203 ? -5.333  15.703 156.242 1.00 9.88  ? 203 PRO B CG    1 
ATOM   3770 C  CD    . PRO D 2 203 ? -4.294  15.925 155.191 1.00 10.08 ? 203 PRO B CD    1 
ATOM   3771 N  N     . VAL D 2 204 ? -2.623  18.565 158.701 1.00 11.89 ? 204 VAL B N     1 
ATOM   3772 C  CA    . VAL D 2 204 ? -1.669  18.565 159.834 1.00 12.93 ? 204 VAL B CA    1 
ATOM   3773 C  C     . VAL D 2 204 ? -2.507  18.637 161.115 1.00 13.87 ? 204 VAL B C     1 
ATOM   3774 O  O     . VAL D 2 204 ? -3.674  19.050 161.089 1.00 14.65 ? 204 VAL B O     1 
ATOM   3775 C  CB    . VAL D 2 204 ? -0.688  19.740 159.725 1.00 14.14 ? 204 VAL B CB    1 
ATOM   3776 C  CG1   . VAL D 2 204 ? -0.566  20.293 158.305 1.00 15.51 ? 204 VAL B CG1   1 
ATOM   3777 C  CG2   . VAL D 2 204 ? -1.074  20.927 160.606 1.00 13.67 ? 204 VAL B CG2   1 
ATOM   3778 N  N     . ALA D 2 205 ? -1.925  18.240 162.228 1.00 13.88 ? 205 ALA B N     1 
ATOM   3779 C  CA    . ALA D 2 205 ? -2.674  18.170 163.499 1.00 14.76 ? 205 ALA B CA    1 
ATOM   3780 C  C     . ALA D 2 205 ? -2.378  19.333 164.449 1.00 15.31 ? 205 ALA B C     1 
ATOM   3781 O  O     . ALA D 2 205 ? -2.239  19.141 165.668 1.00 14.69 ? 205 ALA B O     1 
ATOM   3782 C  CB    . ALA D 2 205 ? -2.324  16.881 164.245 1.00 13.05 ? 205 ALA B CB    1 
ATOM   3783 N  N     . THR D 2 206 ? -2.287  20.516 163.880 1.00 15.31 ? 206 THR B N     1 
ATOM   3784 C  CA    . THR D 2 206 ? -2.103  21.738 164.671 1.00 15.82 ? 206 THR B CA    1 
ATOM   3785 C  C     . THR D 2 206 ? -3.337  21.837 165.597 1.00 17.17 ? 206 THR B C     1 
ATOM   3786 O  O     . THR D 2 206 ? -4.143  20.898 165.689 1.00 18.81 ? 206 THR B O     1 
ATOM   3787 C  CB    . THR D 2 206 ? -1.938  22.922 163.718 1.00 14.71 ? 206 THR B CB    1 
ATOM   3788 O  OG1   . THR D 2 206 ? -0.661  23.516 163.898 1.00 10.76 ? 206 THR B OG1   1 
ATOM   3789 C  CG2   . THR D 2 206 ? -2.986  24.015 163.935 1.00 17.10 ? 206 THR B CG2   1 
ATOM   3790 N  N     . THR D 2 207 ? -3.510  22.957 166.288 1.00 16.46 ? 207 THR B N     1 
ATOM   3791 C  CA    . THR D 2 207 ? -4.642  23.095 167.244 1.00 14.88 ? 207 THR B CA    1 
ATOM   3792 C  C     . THR D 2 207 ? -5.956  23.455 166.546 1.00 14.86 ? 207 THR B C     1 
ATOM   3793 O  O     . THR D 2 207 ? -6.937  22.697 166.590 1.00 15.68 ? 207 THR B O     1 
ATOM   3794 C  CB    . THR D 2 207 ? -4.379  24.156 168.304 1.00 13.41 ? 207 THR B CB    1 
ATOM   3795 O  OG1   . THR D 2 207 ? -5.390  24.085 169.305 1.00 13.33 ? 207 THR B OG1   1 
ATOM   3796 C  CG2   . THR D 2 207 ? -4.386  25.576 167.747 1.00 12.80 ? 207 THR B CG2   1 
ATOM   3797 N  N     . PRO D 2 208 ? -6.113  24.598 165.854 1.00 14.56 ? 208 PRO B N     1 
ATOM   3798 C  CA    . PRO D 2 208 ? -7.376  24.869 165.227 1.00 14.65 ? 208 PRO B CA    1 
ATOM   3799 C  C     . PRO D 2 208 ? -7.660  23.696 164.350 1.00 15.13 ? 208 PRO B C     1 
ATOM   3800 O  O     . PRO D 2 208 ? -8.870  23.437 164.058 1.00 14.01 ? 208 PRO B O     1 
ATOM   3801 C  CB    . PRO D 2 208 ? -7.161  26.179 164.512 1.00 14.61 ? 208 PRO B CB    1 
ATOM   3802 C  CG    . PRO D 2 208 ? -5.736  26.624 164.787 1.00 15.28 ? 208 PRO B CG    1 
ATOM   3803 C  CD    . PRO D 2 208 ? -5.072  25.605 165.671 1.00 14.59 ? 208 PRO B CD    1 
ATOM   3804 N  N     . ALA D 2 209 ? -6.537  23.052 164.003 1.00 15.97 ? 209 ALA B N     1 
ATOM   3805 C  CA    . ALA D 2 209 ? -6.504  21.831 163.173 1.00 15.65 ? 209 ALA B CA    1 
ATOM   3806 C  C     . ALA D 2 209 ? -6.599  22.225 161.688 1.00 16.07 ? 209 ALA B C     1 
ATOM   3807 O  O     . ALA D 2 209 ? -7.722  22.466 161.192 1.00 16.43 ? 209 ALA B O     1 
ATOM   3808 C  CB    . ALA D 2 209 ? -7.661  20.924 163.595 1.00 14.72 ? 209 ALA B CB    1 
ATOM   3809 N  N     . THR D 2 210 ? -5.383  22.250 161.065 1.00 16.22 ? 210 THR B N     1 
ATOM   3810 C  CA    . THR D 2 210 ? -5.145  22.731 159.658 1.00 16.10 ? 210 THR B CA    1 
ATOM   3811 C  C     . THR D 2 210 ? -5.231  21.677 158.545 1.00 16.29 ? 210 THR B C     1 
ATOM   3812 O  O     . THR D 2 210 ? -5.669  20.539 158.782 1.00 15.92 ? 210 THR B O     1 
ATOM   3813 C  CB    . THR D 2 210 ? -3.761  23.357 159.459 1.00 16.42 ? 210 THR B CB    1 
ATOM   3814 O  OG1   . THR D 2 210 ? -2.772  22.598 160.126 1.00 16.85 ? 210 THR B OG1   1 
ATOM   3815 C  CG2   . THR D 2 210 ? -3.675  24.797 159.967 1.00 16.25 ? 210 THR B CG2   1 
ATOM   3816 N  N     . SER D 2 211 ? -4.787  22.216 157.402 1.00 16.54 ? 211 SER B N     1 
ATOM   3817 C  CA    . SER D 2 211 ? -4.659  21.565 156.079 1.00 15.73 ? 211 SER B CA    1 
ATOM   3818 C  C     . SER D 2 211 ? -3.500  22.266 155.326 1.00 15.01 ? 211 SER B C     1 
ATOM   3819 O  O     . SER D 2 211 ? -3.603  23.443 154.945 1.00 15.12 ? 211 SER B O     1 
ATOM   3820 C  CB    . SER D 2 211 ? -5.963  21.730 155.286 1.00 14.93 ? 211 SER B CB    1 
ATOM   3821 O  OG    . SER D 2 211 ? -6.151  20.623 154.417 1.00 14.97 ? 211 SER B OG    1 
ATOM   3822 N  N     . ALA D 2 212 ? -2.416  21.520 155.133 1.00 14.34 ? 212 ALA B N     1 
ATOM   3823 C  CA    . ALA D 2 212 ? -1.166  22.046 154.522 1.00 13.93 ? 212 ALA B CA    1 
ATOM   3824 C  C     . ALA D 2 212 ? -1.081  21.799 153.011 1.00 13.34 ? 212 ALA B C     1 
ATOM   3825 O  O     . ALA D 2 212 ? -1.379  20.686 152.540 1.00 13.83 ? 212 ALA B O     1 
ATOM   3826 C  CB    . ALA D 2 212 ? 0.050   21.372 155.160 1.00 12.14 ? 212 ALA B CB    1 
ATOM   3827 N  N     . LEU D 2 213 ? -0.697  22.838 152.283 1.00 11.49 ? 213 LEU B N     1 
ATOM   3828 C  CA    . LEU D 2 213 ? -0.498  22.832 150.840 1.00 9.91  ? 213 LEU B CA    1 
ATOM   3829 C  C     . LEU D 2 213 ? 0.948   23.282 150.564 1.00 9.58  ? 213 LEU B C     1 
ATOM   3830 O  O     . LEU D 2 213 ? 1.213   24.479 150.800 1.00 8.94  ? 213 LEU B O     1 
ATOM   3831 C  CB    . LEU D 2 213 ? -1.463  23.774 150.099 1.00 9.30  ? 213 LEU B CB    1 
ATOM   3832 C  CG    . LEU D 2 213 ? -1.077  24.055 148.639 1.00 7.77  ? 213 LEU B CG    1 
ATOM   3833 C  CD1   . LEU D 2 213 ? -1.559  22.947 147.719 1.00 7.20  ? 213 LEU B CD1   1 
ATOM   3834 C  CD2   . LEU D 2 213 ? -1.700  25.377 148.210 1.00 7.22  ? 213 LEU B CD2   1 
ATOM   3835 N  N     . VAL D 2 214 ? 1.766   22.359 150.082 1.00 9.51  ? 214 VAL B N     1 
ATOM   3836 C  CA    . VAL D 2 214 ? 3.178   22.726 149.826 1.00 9.74  ? 214 VAL B CA    1 
ATOM   3837 C  C     . VAL D 2 214 ? 3.647   22.184 148.492 1.00 10.35 ? 214 VAL B C     1 
ATOM   3838 O  O     . VAL D 2 214 ? 2.994   21.272 147.973 1.00 10.68 ? 214 VAL B O     1 
ATOM   3839 C  CB    . VAL D 2 214 ? 4.013   22.229 151.024 1.00 9.22  ? 214 VAL B CB    1 
ATOM   3840 C  CG1   . VAL D 2 214 ? 3.082   21.993 152.220 1.00 10.68 ? 214 VAL B CG1   1 
ATOM   3841 C  CG2   . VAL D 2 214 ? 4.808   20.974 150.715 1.00 9.84  ? 214 VAL B CG2   1 
ATOM   3842 N  N     . HIS D 2 215 ? 4.763   22.738 148.042 1.00 9.98  ? 215 HIS B N     1 
ATOM   3843 C  CA    . HIS D 2 215 ? 5.432   22.414 146.793 1.00 9.37  ? 215 HIS B CA    1 
ATOM   3844 C  C     . HIS D 2 215 ? 6.001   20.993 146.872 1.00 10.38 ? 215 HIS B C     1 
ATOM   3845 O  O     . HIS D 2 215 ? 6.521   20.556 147.916 1.00 11.04 ? 215 HIS B O     1 
ATOM   3846 C  CB    . HIS D 2 215 ? 6.606   23.321 146.416 1.00 7.14  ? 215 HIS B CB    1 
ATOM   3847 C  CG    . HIS D 2 215 ? 6.287   24.698 145.958 1.00 12.06 ? 215 HIS B CG    1 
ATOM   3848 N  ND1   . HIS D 2 215 ? 6.952   25.817 146.414 1.00 13.86 ? 215 HIS B ND1   1 
ATOM   3849 C  CD2   . HIS D 2 215 ? 5.383   25.153 145.075 1.00 13.44 ? 215 HIS B CD2   1 
ATOM   3850 C  CE1   . HIS D 2 215 ? 6.465   26.904 145.857 1.00 14.10 ? 215 HIS B CE1   1 
ATOM   3851 N  NE2   . HIS D 2 215 ? 5.506   26.526 145.044 1.00 13.59 ? 215 HIS B NE2   1 
ATOM   3852 N  N     . THR D 2 216 ? 5.905   20.359 145.716 1.00 10.22 ? 216 THR B N     1 
ATOM   3853 C  CA    . THR D 2 216 ? 6.392   18.973 145.600 1.00 10.22 ? 216 THR B CA    1 
ATOM   3854 C  C     . THR D 2 216 ? 6.751   18.691 144.160 1.00 10.78 ? 216 THR B C     1 
ATOM   3855 O  O     . THR D 2 216 ? 6.031   19.122 143.251 1.00 11.56 ? 216 THR B O     1 
ATOM   3856 C  CB    . THR D 2 216 ? 5.288   17.996 146.167 1.00 10.24 ? 216 THR B CB    1 
ATOM   3857 O  OG1   . THR D 2 216 ? 5.928   16.685 146.181 1.00 9.49  ? 216 THR B OG1   1 
ATOM   3858 C  CG2   . THR D 2 216 ? 3.966   18.019 145.394 1.00 10.35 ? 216 THR B CG2   1 
ATOM   3859 N  N     . LEU D 2 217 ? 7.843   17.985 143.957 1.00 9.92  ? 217 LEU B N     1 
ATOM   3860 C  CA    . LEU D 2 217 ? 8.265   17.653 142.579 1.00 9.39  ? 217 LEU B CA    1 
ATOM   3861 C  C     . LEU D 2 217 ? 7.468   16.429 142.169 1.00 10.03 ? 217 LEU B C     1 
ATOM   3862 O  O     . LEU D 2 217 ? 7.340   15.529 143.030 1.00 11.23 ? 217 LEU B O     1 
ATOM   3863 C  CB    . LEU D 2 217 ? 9.775   17.448 142.605 1.00 9.37  ? 217 LEU B CB    1 
ATOM   3864 C  CG    . LEU D 2 217 ? 10.652  18.523 141.970 1.00 11.06 ? 217 LEU B CG    1 
ATOM   3865 C  CD1   . LEU D 2 217 ? 9.839   19.736 141.544 1.00 11.26 ? 217 LEU B CD1   1 
ATOM   3866 C  CD2   . LEU D 2 217 ? 11.711  18.945 142.984 1.00 7.69  ? 217 LEU B CD2   1 
ATOM   3867 N  N     . VAL D 2 218 ? 6.930   16.410 140.972 1.00 9.84  ? 218 VAL B N     1 
ATOM   3868 C  CA    . VAL D 2 218 ? 6.166   15.230 140.506 1.00 9.41  ? 218 VAL B CA    1 
ATOM   3869 C  C     . VAL D 2 218 ? 6.951   14.705 139.296 1.00 9.88  ? 218 VAL B C     1 
ATOM   3870 O  O     . VAL D 2 218 ? 7.330   15.516 138.432 1.00 9.73  ? 218 VAL B O     1 
ATOM   3871 C  CB    . VAL D 2 218 ? 4.708   15.504 140.185 1.00 9.04  ? 218 VAL B CB    1 
ATOM   3872 C  CG1   . VAL D 2 218 ? 3.824   15.755 141.397 1.00 7.42  ? 218 VAL B CG1   1 
ATOM   3873 C  CG2   . VAL D 2 218 ? 4.543   16.633 139.158 1.00 11.16 ? 218 VAL B CG2   1 
ATOM   3874 N  N     . GLY D 2 219 ? 7.199   13.410 139.311 1.00 10.53 ? 219 GLY B N     1 
ATOM   3875 C  CA    . GLY D 2 219 ? 7.929   12.777 138.220 1.00 11.54 ? 219 GLY B CA    1 
ATOM   3876 C  C     . GLY D 2 219 ? 9.351   12.397 138.568 1.00 12.51 ? 219 GLY B C     1 
ATOM   3877 O  O     . GLY D 2 219 ? 10.044  11.785 137.696 1.00 13.44 ? 219 GLY B O     1 
ATOM   3878 N  N     . LEU D 2 220 ? 9.785   12.711 139.773 1.00 11.54 ? 220 LEU B N     1 
ATOM   3879 C  CA    . LEU D 2 220 ? 11.169  12.325 140.130 1.00 10.40 ? 220 LEU B CA    1 
ATOM   3880 C  C     . LEU D 2 220 ? 11.262  10.798 140.225 1.00 9.46  ? 220 LEU B C     1 
ATOM   3881 O  O     . LEU D 2 220 ? 12.360  10.234 140.333 1.00 8.92  ? 220 LEU B O     1 
ATOM   3882 C  CB    . LEU D 2 220 ? 11.525  13.036 141.418 1.00 9.22  ? 220 LEU B CB    1 
ATOM   3883 C  CG    . LEU D 2 220 ? 12.599  14.087 141.461 1.00 9.08  ? 220 LEU B CG    1 
ATOM   3884 C  CD1   . LEU D 2 220 ? 12.753  14.810 140.132 1.00 8.62  ? 220 LEU B CD1   1 
ATOM   3885 C  CD2   . LEU D 2 220 ? 12.205  15.091 142.565 1.00 8.82  ? 220 LEU B CD2   1 
ATOM   3886 N  N     . ASP D 2 221 ? 10.127  10.136 140.212 1.00 8.93  ? 221 ASP B N     1 
ATOM   3887 C  CA    . ASP D 2 221 ? 10.070  8.674  140.342 1.00 9.69  ? 221 ASP B CA    1 
ATOM   3888 C  C     . ASP D 2 221 ? 10.729  7.995  139.154 1.00 10.62 ? 221 ASP B C     1 
ATOM   3889 O  O     . ASP D 2 221 ? 11.042  6.794  139.242 1.00 11.59 ? 221 ASP B O     1 
ATOM   3890 C  CB    . ASP D 2 221 ? 8.607   8.255  140.564 1.00 8.89  ? 221 ASP B CB    1 
ATOM   3891 C  CG    . ASP D 2 221 ? 8.335   8.087  142.039 1.00 12.60 ? 221 ASP B CG    1 
ATOM   3892 O  OD1   . ASP D 2 221 ? 9.002   7.156  142.573 1.00 14.70 ? 221 ASP B OD1   1 
ATOM   3893 O  OD2   . ASP D 2 221 ? 7.555   8.789  142.710 1.00 14.52 ? 221 ASP B OD2   1 
ATOM   3894 N  N     . GLY D 2 222 ? 10.933  8.741  138.080 1.00 11.24 ? 222 GLY B N     1 
ATOM   3895 C  CA    . GLY D 2 222 ? 11.518  8.156  136.861 1.00 11.93 ? 222 GLY B CA    1 
ATOM   3896 C  C     . GLY D 2 222 ? 13.025  8.198  136.854 1.00 12.71 ? 222 GLY B C     1 
ATOM   3897 O  O     . GLY D 2 222 ? 13.691  7.955  135.828 1.00 14.05 ? 222 GLY B O     1 
ATOM   3898 N  N     . VAL D 2 223 ? 13.527  8.546  138.031 1.00 12.35 ? 223 VAL B N     1 
ATOM   3899 C  CA    . VAL D 2 223 ? 15.005  8.626  138.176 1.00 11.29 ? 223 VAL B CA    1 
ATOM   3900 C  C     . VAL D 2 223 ? 15.452  7.237  138.640 1.00 12.08 ? 223 VAL B C     1 
ATOM   3901 O  O     . VAL D 2 223 ? 16.593  6.828  138.364 1.00 11.57 ? 223 VAL B O     1 
ATOM   3902 C  CB    . VAL D 2 223 ? 15.423  9.812  139.063 1.00 6.19  ? 223 VAL B CB    1 
ATOM   3903 C  CG1   . VAL D 2 223 ? 16.914  9.826  139.340 1.00 4.68  ? 223 VAL B CG1   1 
ATOM   3904 C  CG2   . VAL D 2 223 ? 14.939  11.123 138.464 1.00 3.37  ? 223 VAL B CG2   1 
ATOM   3905 N  N     . LEU D 2 224 ? 14.493  6.562  139.282 1.00 12.08 ? 224 LEU B N     1 
ATOM   3906 C  CA    . LEU D 2 224 ? 14.733  5.226  139.825 1.00 13.24 ? 224 LEU B CA    1 
ATOM   3907 C  C     . LEU D 2 224 ? 14.790  4.089  138.831 1.00 13.80 ? 224 LEU B C     1 
ATOM   3908 O  O     . LEU D 2 224 ? 14.767  2.934  139.299 1.00 15.57 ? 224 LEU B O     1 
ATOM   3909 C  CB    . LEU D 2 224 ? 13.678  5.004  140.928 1.00 12.26 ? 224 LEU B CB    1 
ATOM   3910 C  CG    . LEU D 2 224 ? 13.326  6.225  141.774 1.00 12.49 ? 224 LEU B CG    1 
ATOM   3911 C  CD1   . LEU D 2 224 ? 12.155  5.891  142.687 1.00 10.41 ? 224 LEU B CD1   1 
ATOM   3912 C  CD2   . LEU D 2 224 ? 14.535  6.652  142.599 1.00 10.99 ? 224 LEU B CD2   1 
ATOM   3913 N  N     . ALA D 2 225 ? 14.868  4.323  137.550 1.00 13.15 ? 225 ALA B N     1 
ATOM   3914 C  CA    . ALA D 2 225 ? 14.940  3.292  136.514 1.00 12.45 ? 225 ALA B CA    1 
ATOM   3915 C  C     . ALA D 2 225 ? 15.278  3.874  135.140 1.00 12.48 ? 225 ALA B C     1 
ATOM   3916 O  O     . ALA D 2 225 ? 14.827  4.937  134.693 1.00 13.05 ? 225 ALA B O     1 
ATOM   3917 C  CB    . ALA D 2 225 ? 13.667  2.467  136.495 1.00 13.20 ? 225 ALA B CB    1 
ATOM   3918 N  N     . VAL D 2 226 ? 16.126  3.120  134.449 1.00 12.16 ? 226 VAL B N     1 
ATOM   3919 C  CA    . VAL D 2 226 ? 16.579  3.474  133.089 1.00 10.83 ? 226 VAL B CA    1 
ATOM   3920 C  C     . VAL D 2 226 ? 15.548  2.888  132.089 1.00 10.86 ? 226 VAL B C     1 
ATOM   3921 O  O     . VAL D 2 226 ? 15.422  1.663  131.948 1.00 11.10 ? 226 VAL B O     1 
ATOM   3922 C  CB    . VAL D 2 226 ? 17.998  2.936  132.859 1.00 7.98  ? 226 VAL B CB    1 
ATOM   3923 C  CG1   . VAL D 2 226 ? 18.549  3.276  131.473 1.00 6.29  ? 226 VAL B CG1   1 
ATOM   3924 C  CG2   . VAL D 2 226 ? 19.016  3.489  133.858 1.00 5.66  ? 226 VAL B CG2   1 
ATOM   3925 N  N     . GLY D 2 227 ? 14.829  3.801  131.428 1.00 11.02 ? 227 GLY B N     1 
ATOM   3926 C  CA    . GLY D 2 227 ? 13.715  3.474  130.484 1.00 11.13 ? 227 GLY B CA    1 
ATOM   3927 C  C     . GLY D 2 227 ? 14.212  2.944  129.119 1.00 11.59 ? 227 GLY B C     1 
ATOM   3928 O  O     . GLY D 2 227 ? 15.416  2.992  128.821 1.00 10.99 ? 227 GLY B O     1 
ATOM   3929 N  N     . PRO D 2 228 ? 13.298  2.418  128.233 1.00 11.52 ? 228 PRO B N     1 
ATOM   3930 C  CA    . PRO D 2 228 ? 13.682  1.880  126.922 1.00 11.97 ? 228 PRO B CA    1 
ATOM   3931 C  C     . PRO D 2 228 ? 14.312  2.936  126.043 1.00 13.37 ? 228 PRO B C     1 
ATOM   3932 O  O     . PRO D 2 228 ? 14.967  2.569  125.015 1.00 15.61 ? 228 PRO B O     1 
ATOM   3933 C  CB    . PRO D 2 228 ? 12.386  1.403  126.303 1.00 11.24 ? 228 PRO B CB    1 
ATOM   3934 C  CG    . PRO D 2 228 ? 11.266  1.690  127.286 1.00 10.18 ? 228 PRO B CG    1 
ATOM   3935 C  CD    . PRO D 2 228 ? 11.853  2.336  128.512 1.00 10.18 ? 228 PRO B CD    1 
ATOM   3936 N  N     . ASP D 2 229 ? 14.109  4.185  126.440 1.00 12.77 ? 229 ASP B N     1 
ATOM   3937 C  CA    . ASP D 2 229 ? 14.626  5.363  125.707 1.00 12.17 ? 229 ASP B CA    1 
ATOM   3938 C  C     . ASP D 2 229 ? 15.825  5.979  126.433 1.00 12.01 ? 229 ASP B C     1 
ATOM   3939 O  O     . ASP D 2 229 ? 15.716  7.040  127.061 1.00 13.38 ? 229 ASP B O     1 
ATOM   3940 C  CB    . ASP D 2 229 ? 13.563  6.466  125.640 1.00 11.13 ? 229 ASP B CB    1 
ATOM   3941 C  CG    . ASP D 2 229 ? 12.491  6.242  124.572 1.00 12.67 ? 229 ASP B CG    1 
ATOM   3942 O  OD1   . ASP D 2 229 ? 12.295  5.064  124.089 1.00 14.54 ? 229 ASP B OD1   1 
ATOM   3943 O  OD2   . ASP D 2 229 ? 11.779  7.237  124.159 1.00 12.88 ? 229 ASP B OD2   1 
ATOM   3944 N  N     . ASN D 2 230 ? 16.960  5.317  126.333 1.00 10.59 ? 230 ASN B N     1 
ATOM   3945 C  CA    . ASN D 2 230 ? 18.184  5.781  127.005 1.00 10.11 ? 230 ASN B CA    1 
ATOM   3946 C  C     . ASN D 2 230 ? 19.396  5.670  126.090 1.00 9.94  ? 230 ASN B C     1 
ATOM   3947 O  O     . ASN D 2 230 ? 19.279  4.972  125.084 1.00 10.10 ? 230 ASN B O     1 
ATOM   3948 C  CB    . ASN D 2 230 ? 18.463  4.917  128.232 1.00 10.12 ? 230 ASN B CB    1 
ATOM   3949 C  CG    . ASN D 2 230 ? 18.802  3.474  127.860 1.00 7.72  ? 230 ASN B CG    1 
ATOM   3950 O  OD1   . ASN D 2 230 ? 19.960  3.167  127.580 1.00 8.28  ? 230 ASN B OD1   1 
ATOM   3951 N  ND2   . ASN D 2 230 ? 17.851  2.559  127.836 1.00 5.26  ? 230 ASN B ND2   1 
ATOM   3952 N  N     . PHE D 2 231 ? 20.485  6.254  126.508 1.00 9.45  ? 231 PHE B N     1 
ATOM   3953 C  CA    . PHE D 2 231 ? 21.764  6.167  125.773 1.00 8.75  ? 231 PHE B CA    1 
ATOM   3954 C  C     . PHE D 2 231 ? 22.786  5.647  126.793 1.00 9.08  ? 231 PHE B C     1 
ATOM   3955 O  O     . PHE D 2 231 ? 22.883  6.267  127.859 1.00 9.46  ? 231 PHE B O     1 
ATOM   3956 C  CB    . PHE D 2 231 ? 22.223  7.482  125.168 1.00 7.96  ? 231 PHE B CB    1 
ATOM   3957 C  CG    . PHE D 2 231 ? 23.693  7.586  124.930 1.00 8.50  ? 231 PHE B CG    1 
ATOM   3958 C  CD1   . PHE D 2 231 ? 24.555  7.929  125.976 1.00 9.84  ? 231 PHE B CD1   1 
ATOM   3959 C  CD2   . PHE D 2 231 ? 24.232  7.340  123.676 1.00 7.76  ? 231 PHE B CD2   1 
ATOM   3960 C  CE1   . PHE D 2 231 ? 25.927  8.029  125.770 1.00 10.06 ? 231 PHE B CE1   1 
ATOM   3961 C  CE2   . PHE D 2 231 ? 25.619  7.440  123.430 1.00 6.18  ? 231 PHE B CE2   1 
ATOM   3962 C  CZ    . PHE D 2 231 ? 26.457  7.785  124.483 1.00 9.26  ? 231 PHE B CZ    1 
ATOM   3963 N  N     . SER D 2 232 ? 23.438  4.570  126.446 1.00 9.37  ? 232 SER B N     1 
ATOM   3964 C  CA    . SER D 2 232 ? 24.454  4.009  127.368 1.00 9.53  ? 232 SER B CA    1 
ATOM   3965 C  C     . SER D 2 232 ? 25.686  3.580  126.576 1.00 9.62  ? 232 SER B C     1 
ATOM   3966 O  O     . SER D 2 232 ? 25.538  3.071  125.458 1.00 10.01 ? 232 SER B O     1 
ATOM   3967 C  CB    . SER D 2 232 ? 23.883  2.830  128.149 1.00 9.07  ? 232 SER B CB    1 
ATOM   3968 O  OG    . SER D 2 232 ? 23.627  1.725  127.280 1.00 9.89  ? 232 SER B OG    1 
ATOM   3969 N  N     . GLU D 2 233 ? 26.837  3.731  127.204 1.00 9.27  ? 233 GLU B N     1 
ATOM   3970 C  CA    . GLU D 2 233 ? 28.097  3.318  126.512 1.00 8.72  ? 233 GLU B CA    1 
ATOM   3971 C  C     . GLU D 2 233 ? 29.301  3.533  127.403 1.00 8.10  ? 233 GLU B C     1 
ATOM   3972 O  O     . GLU D 2 233 ? 29.183  4.096  128.509 1.00 8.51  ? 233 GLU B O     1 
ATOM   3973 C  CB    . GLU D 2 233 ? 28.168  4.070  125.202 1.00 8.94  ? 233 GLU B CB    1 
ATOM   3974 C  CG    . GLU D 2 233 ? 29.263  3.885  124.201 1.00 11.16 ? 233 GLU B CG    1 
ATOM   3975 C  CD    . GLU D 2 233 ? 29.586  2.527  123.667 1.00 11.61 ? 233 GLU B CD    1 
ATOM   3976 O  OE1   . GLU D 2 233 ? 30.339  1.730  124.223 1.00 11.06 ? 233 GLU B OE1   1 
ATOM   3977 O  OE2   . GLU D 2 233 ? 29.025  2.316  122.549 1.00 13.00 ? 233 GLU B OE2   1 
ATOM   3978 N  N     . SER D 2 234 ? 30.442  3.062  126.964 1.00 8.58  ? 234 SER B N     1 
ATOM   3979 C  CA    . SER D 2 234 ? 31.723  3.153  127.672 1.00 8.95  ? 234 SER B CA    1 
ATOM   3980 C  C     . SER D 2 234 ? 32.006  4.614  128.035 1.00 9.55  ? 234 SER B C     1 
ATOM   3981 O  O     . SER D 2 234 ? 31.781  5.526  127.219 1.00 10.09 ? 234 SER B O     1 
ATOM   3982 C  CB    . SER D 2 234 ? 32.836  2.572  126.840 1.00 10.22 ? 234 SER B CB    1 
ATOM   3983 O  OG    . SER D 2 234 ? 34.099  2.685  127.436 1.00 13.70 ? 234 SER B OG    1 
ATOM   3984 N  N     . PHE D 2 235 ? 32.487  4.793  129.251 1.00 9.38  ? 235 PHE B N     1 
ATOM   3985 C  CA    . PHE D 2 235 ? 32.790  6.076  129.847 1.00 9.26  ? 235 PHE B CA    1 
ATOM   3986 C  C     . PHE D 2 235 ? 33.743  6.920  129.020 1.00 11.21 ? 235 PHE B C     1 
ATOM   3987 O  O     . PHE D 2 235 ? 33.607  8.170  128.935 1.00 13.48 ? 235 PHE B O     1 
ATOM   3988 C  CB    . PHE D 2 235 ? 33.261  5.928  131.315 1.00 5.91  ? 235 PHE B CB    1 
ATOM   3989 C  CG    . PHE D 2 235 ? 33.786  7.235  131.851 1.00 3.88  ? 235 PHE B CG    1 
ATOM   3990 C  CD1   . PHE D 2 235 ? 35.111  7.613  131.626 1.00 2.83  ? 235 PHE B CD1   1 
ATOM   3991 C  CD2   . PHE D 2 235 ? 32.933  8.108  132.521 1.00 3.21  ? 235 PHE B CD2   1 
ATOM   3992 C  CE1   . PHE D 2 235 ? 35.594  8.843  132.088 1.00 3.71  ? 235 PHE B CE1   1 
ATOM   3993 C  CE2   . PHE D 2 235 ? 33.407  9.325  132.976 1.00 3.05  ? 235 PHE B CE2   1 
ATOM   3994 C  CZ    . PHE D 2 235 ? 34.732  9.696  132.765 1.00 3.39  ? 235 PHE B CZ    1 
ATOM   3995 N  N     . ILE D 2 236 ? 34.718  6.289  128.415 1.00 11.63 ? 236 ILE B N     1 
ATOM   3996 C  CA    . ILE D 2 236 ? 35.746  6.978  127.622 1.00 11.79 ? 236 ILE B CA    1 
ATOM   3997 C  C     . ILE D 2 236 ? 35.164  7.728  126.438 1.00 12.33 ? 236 ILE B C     1 
ATOM   3998 O  O     . ILE D 2 236 ? 35.825  8.629  125.869 1.00 13.82 ? 236 ILE B O     1 
ATOM   3999 C  CB    . ILE D 2 236 ? 36.827  5.932  127.139 1.00 9.57  ? 236 ILE B CB    1 
ATOM   4000 C  CG1   . ILE D 2 236 ? 38.143  6.647  126.786 1.00 7.79  ? 236 ILE B CG1   1 
ATOM   4001 C  CG2   . ILE D 2 236 ? 36.252  5.135  125.928 1.00 7.52  ? 236 ILE B CG2   1 
ATOM   4002 C  CD1   . ILE D 2 236 ? 38.325  8.015  127.523 1.00 9.32  ? 236 ILE B CD1   1 
ATOM   4003 N  N     . LYS D 2 237 ? 33.969  7.354  126.053 1.00 11.81 ? 237 LYS B N     1 
ATOM   4004 C  CA    . LYS D 2 237 ? 33.320  7.984  124.899 1.00 12.06 ? 237 LYS B CA    1 
ATOM   4005 C  C     . LYS D 2 237 ? 32.662  9.314  125.217 1.00 12.09 ? 237 LYS B C     1 
ATOM   4006 O  O     . LYS D 2 237 ? 32.378  10.113 124.269 1.00 12.87 ? 237 LYS B O     1 
ATOM   4007 C  CB    . LYS D 2 237 ? 32.378  7.012  124.218 1.00 12.49 ? 237 LYS B CB    1 
ATOM   4008 C  CG    . LYS D 2 237 ? 33.049  5.704  123.766 1.00 12.71 ? 237 LYS B CG    1 
ATOM   4009 C  CD    . LYS D 2 237 ? 32.005  4.750  123.199 1.00 12.15 ? 237 LYS B CD    1 
ATOM   4010 C  CE    . LYS D 2 237 ? 32.628  3.809  122.202 1.00 13.95 ? 237 LYS B CE    1 
ATOM   4011 N  NZ    . LYS D 2 237 ? 31.641  2.767  121.758 1.00 15.79 ? 237 LYS B NZ    1 
ATOM   4012 N  N     . GLY D 2 238 ? 32.439  9.605  126.481 1.00 11.09 ? 238 GLY B N     1 
ATOM   4013 C  CA    . GLY D 2 238 ? 31.817  10.899 126.862 1.00 10.39 ? 238 GLY B CA    1 
ATOM   4014 C  C     . GLY D 2 238 ? 30.419  11.010 126.279 1.00 9.98  ? 238 GLY B C     1 
ATOM   4015 O  O     . GLY D 2 238 ? 29.923  10.056 125.632 1.00 10.13 ? 238 GLY B O     1 
ATOM   4016 N  N     . VAL D 2 239 ? 29.766  12.139 126.505 1.00 9.74  ? 239 VAL B N     1 
ATOM   4017 C  CA    . VAL D 2 239 ? 28.395  12.284 125.963 1.00 10.03 ? 239 VAL B CA    1 
ATOM   4018 C  C     . VAL D 2 239 ? 28.066  13.745 125.675 1.00 10.72 ? 239 VAL B C     1 
ATOM   4019 O  O     . VAL D 2 239 ? 28.789  14.697 126.001 1.00 11.85 ? 239 VAL B O     1 
ATOM   4020 C  CB    . VAL D 2 239 ? 27.416  11.607 126.943 1.00 7.86  ? 239 VAL B CB    1 
ATOM   4021 C  CG1   . VAL D 2 239 ? 27.247  12.445 128.217 1.00 5.76  ? 239 VAL B CG1   1 
ATOM   4022 C  CG2   . VAL D 2 239 ? 26.056  11.291 126.360 1.00 8.01  ? 239 VAL B CG2   1 
ATOM   4023 N  N     . PHE D 2 240 ? 26.937  13.881 125.001 1.00 10.31 ? 240 PHE B N     1 
ATOM   4024 C  CA    . PHE D 2 240 ? 26.360  15.165 124.638 1.00 10.23 ? 240 PHE B CA    1 
ATOM   4025 C  C     . PHE D 2 240 ? 24.828  14.965 124.632 1.00 10.13 ? 240 PHE B C     1 
ATOM   4026 O  O     . PHE D 2 240 ? 24.379  13.924 124.094 1.00 10.46 ? 240 PHE B O     1 
ATOM   4027 C  CB    . PHE D 2 240 ? 26.889  15.859 123.377 1.00 10.27 ? 240 PHE B CB    1 
ATOM   4028 C  CG    . PHE D 2 240 ? 26.292  17.250 123.242 1.00 12.14 ? 240 PHE B CG    1 
ATOM   4029 C  CD1   . PHE D 2 240 ? 26.673  18.257 124.139 1.00 13.86 ? 240 PHE B CD1   1 
ATOM   4030 C  CD2   . PHE D 2 240 ? 25.291  17.492 122.300 1.00 13.64 ? 240 PHE B CD2   1 
ATOM   4031 C  CE1   . PHE D 2 240 ? 26.084  19.516 124.055 1.00 14.71 ? 240 PHE B CE1   1 
ATOM   4032 C  CE2   . PHE D 2 240 ? 24.697  18.762 122.208 1.00 14.45 ? 240 PHE B CE2   1 
ATOM   4033 C  CZ    . PHE D 2 240 ? 25.100  19.773 123.093 1.00 14.16 ? 240 PHE B CZ    1 
ATOM   4034 N  N     . SER D 2 241 ? 24.150  15.925 125.260 1.00 8.80  ? 241 SER B N     1 
ATOM   4035 C  CA    . SER D 2 241 ? 22.685  15.860 125.317 1.00 8.44  ? 241 SER B CA    1 
ATOM   4036 C  C     . SER D 2 241 ? 22.075  17.244 125.467 1.00 8.23  ? 241 SER B C     1 
ATOM   4037 O  O     . SER D 2 241 ? 22.719  18.200 125.924 1.00 8.68  ? 241 SER B O     1 
ATOM   4038 C  CB    . SER D 2 241 ? 22.158  14.905 126.369 1.00 7.79  ? 241 SER B CB    1 
ATOM   4039 O  OG    . SER D 2 241 ? 20.904  14.372 125.963 1.00 6.80  ? 241 SER B OG    1 
ATOM   4040 N  N     . GLN D 2 242 ? 20.830  17.299 125.060 1.00 8.38  ? 242 GLN B N     1 
ATOM   4041 C  CA    . GLN D 2 242 ? 20.022  18.529 125.084 1.00 8.82  ? 242 GLN B CA    1 
ATOM   4042 C  C     . GLN D 2 242 ? 18.654  18.243 125.692 1.00 8.45  ? 242 GLN B C     1 
ATOM   4043 O  O     . GLN D 2 242 ? 18.193  17.095 125.717 1.00 8.82  ? 242 GLN B O     1 
ATOM   4044 C  CB    . GLN D 2 242 ? 19.836  19.080 123.666 1.00 9.41  ? 242 GLN B CB    1 
ATOM   4045 C  CG    . GLN D 2 242 ? 21.128  19.215 122.863 1.00 12.40 ? 242 GLN B CG    1 
ATOM   4046 C  CD    . GLN D 2 242 ? 21.223  18.187 121.739 1.00 13.98 ? 242 GLN B CD    1 
ATOM   4047 O  OE1   . GLN D 2 242 ? 21.744  18.470 120.655 1.00 13.36 ? 242 GLN B OE1   1 
ATOM   4048 N  NE2   . GLN D 2 242 ? 20.696  17.005 122.053 1.00 12.33 ? 242 GLN B NE2   1 
ATOM   4049 N  N     . SER D 2 243 ? 17.987  19.254 126.189 1.00 8.01  ? 243 SER B N     1 
ATOM   4050 C  CA    . SER D 2 243 ? 16.622  19.030 126.714 1.00 8.84  ? 243 SER B CA    1 
ATOM   4051 C  C     . SER D 2 243 ? 15.769  19.875 125.758 1.00 9.77  ? 243 SER B C     1 
ATOM   4052 O  O     . SER D 2 243 ? 16.400  20.505 124.889 1.00 11.32 ? 243 SER B O     1 
ATOM   4053 C  CB    . SER D 2 243 ? 16.416  19.368 128.150 1.00 7.92  ? 243 SER B CB    1 
ATOM   4054 O  OG    . SER D 2 243 ? 15.057  19.044 128.513 1.00 10.45 ? 243 SER B OG    1 
ATOM   4055 N  N     . VAL D 2 244 ? 14.474  19.899 125.899 1.00 9.53  ? 244 VAL B N     1 
ATOM   4056 C  CA    . VAL D 2 244 ? 13.655  20.717 124.970 1.00 9.03  ? 244 VAL B CA    1 
ATOM   4057 C  C     . VAL D 2 244 ? 12.410  21.161 125.719 1.00 9.57  ? 244 VAL B C     1 
ATOM   4058 O  O     . VAL D 2 244 ? 12.109  20.612 126.797 1.00 11.75 ? 244 VAL B O     1 
ATOM   4059 C  CB    . VAL D 2 244 ? 13.438  19.936 123.677 1.00 8.11  ? 244 VAL B CB    1 
ATOM   4060 C  CG1   . VAL D 2 244 ? 11.985  19.858 123.236 1.00 9.20  ? 244 VAL B CG1   1 
ATOM   4061 C  CG2   . VAL D 2 244 ? 14.273  20.503 122.532 1.00 9.15  ? 244 VAL B CG2   1 
ATOM   4062 N  N     . CYS D 2 245 ? 11.757  22.150 125.155 1.00 8.84  ? 245 CYS B N     1 
ATOM   4063 C  CA    . CYS D 2 245 ? 10.544  22.691 125.765 1.00 7.87  ? 245 CYS B CA    1 
ATOM   4064 C  C     . CYS D 2 245 ? 9.527   21.555 125.825 1.00 7.42  ? 245 CYS B C     1 
ATOM   4065 O  O     . CYS D 2 245 ? 9.310   20.941 124.771 1.00 8.00  ? 245 CYS B O     1 
ATOM   4066 C  CB    . CYS D 2 245 ? 10.025  23.876 124.973 1.00 8.67  ? 245 CYS B CB    1 
ATOM   4067 S  SG    . CYS D 2 245 ? 8.619   24.602 125.858 1.00 10.27 ? 245 CYS B SG    1 
ATOM   4068 N  N     . ASN D 2 246 ? 8.966   21.327 126.993 1.00 7.68  ? 246 ASN B N     1 
ATOM   4069 C  CA    . ASN D 2 246 ? 8.005   20.230 127.189 1.00 8.00  ? 246 ASN B CA    1 
ATOM   4070 C  C     . ASN D 2 246 ? 6.553   20.685 127.115 1.00 7.16  ? 246 ASN B C     1 
ATOM   4071 O  O     . ASN D 2 246 ? 5.627   20.002 127.592 1.00 6.23  ? 246 ASN B O     1 
ATOM   4072 C  CB    . ASN D 2 246 ? 8.273   19.460 128.478 1.00 9.52  ? 246 ASN B CB    1 
ATOM   4073 C  CG    . ASN D 2 246 ? 8.090   20.314 129.714 1.00 9.74  ? 246 ASN B CG    1 
ATOM   4074 O  OD1   . ASN D 2 246 ? 8.716   19.960 130.725 1.00 10.35 ? 246 ASN B OD1   1 
ATOM   4075 N  ND2   . ASN D 2 246 ? 7.294   21.362 129.649 1.00 9.15  ? 246 ASN B ND2   1 
ATOM   4076 N  N     . GLU D 2 247 ? 6.423   21.826 126.467 1.00 7.58  ? 247 GLU B N     1 
ATOM   4077 C  CA    . GLU D 2 247 ? 5.088   22.414 126.259 1.00 8.56  ? 247 GLU B CA    1 
ATOM   4078 C  C     . GLU D 2 247 ? 4.914   22.952 124.848 1.00 9.09  ? 247 GLU B C     1 
ATOM   4079 O  O     . GLU D 2 247 ? 5.887   23.365 124.198 1.00 10.53 ? 247 GLU B O     1 
ATOM   4080 C  CB    . GLU D 2 247 ? 4.862   23.482 127.308 1.00 9.77  ? 247 GLU B CB    1 
ATOM   4081 C  CG    . GLU D 2 247 ? 4.826   22.925 128.731 1.00 13.65 ? 247 GLU B CG    1 
ATOM   4082 C  CD    . GLU D 2 247 ? 3.431   22.464 129.152 1.00 15.19 ? 247 GLU B CD    1 
ATOM   4083 O  OE1   . GLU D 2 247 ? 2.475   22.434 128.286 1.00 12.83 ? 247 GLU B OE1   1 
ATOM   4084 O  OE2   . GLU D 2 247 ? 3.212   22.105 130.370 1.00 16.44 ? 247 GLU B OE2   1 
ATOM   4085 N  N     . PRO D 2 248 ? 3.667   22.950 124.357 1.00 9.24  ? 248 PRO B N     1 
ATOM   4086 C  CA    . PRO D 2 248 ? 3.360   23.400 123.011 1.00 10.02 ? 248 PRO B CA    1 
ATOM   4087 C  C     . PRO D 2 248 ? 3.821   24.826 122.774 1.00 10.43 ? 248 PRO B C     1 
ATOM   4088 O  O     . PRO D 2 248 ? 4.260   25.149 121.627 1.00 11.47 ? 248 PRO B O     1 
ATOM   4089 C  CB    . PRO D 2 248 ? 1.862   23.233 122.905 1.00 10.78 ? 248 PRO B CB    1 
ATOM   4090 C  CG    . PRO D 2 248 ? 1.360   22.664 124.224 1.00 10.42 ? 248 PRO B CG    1 
ATOM   4091 C  CD    . PRO D 2 248 ? 2.522   22.486 125.144 1.00 9.87  ? 248 PRO B CD    1 
ATOM   4092 N  N     . ASP D 2 249 ? 3.724   25.657 123.808 1.00 16.34 ? 249 ASP B N     1 
ATOM   4093 C  CA    . ASP D 2 249 ? 4.149   27.083 123.732 1.00 16.95 ? 249 ASP B CA    1 
ATOM   4094 C  C     . ASP D 2 249 ? 5.340   27.320 124.690 1.00 16.43 ? 249 ASP B C     1 
ATOM   4095 O  O     . ASP D 2 249 ? 5.805   26.396 125.375 1.00 13.75 ? 249 ASP B O     1 
ATOM   4096 C  CB    . ASP D 2 249 ? 2.984   28.006 124.105 1.00 19.79 ? 249 ASP B CB    1 
ATOM   4097 C  CG    . ASP D 2 249 ? 1.910   28.096 123.018 1.00 23.89 ? 249 ASP B CG    1 
ATOM   4098 O  OD1   . ASP D 2 249 ? 2.188   27.759 121.804 1.00 26.75 ? 249 ASP B OD1   1 
ATOM   4099 O  OD2   . ASP D 2 249 ? 0.724   28.510 123.315 1.00 26.10 ? 249 ASP B OD2   1 
ATOM   4100 N  N     . PHE D 2 250 ? 5.809   28.563 124.708 1.00 9.34  ? 250 PHE B N     1 
ATOM   4101 C  CA    . PHE D 2 250 ? 6.953   28.995 125.550 1.00 8.78  ? 250 PHE B CA    1 
ATOM   4102 C  C     . PHE D 2 250 ? 6.514   30.111 126.466 1.00 8.58  ? 250 PHE B C     1 
ATOM   4103 O  O     . PHE D 2 250 ? 6.523   31.289 126.089 1.00 7.77  ? 250 PHE B O     1 
ATOM   4104 C  CB    . PHE D 2 250 ? 8.056   29.608 124.701 1.00 7.09  ? 250 PHE B CB    1 
ATOM   4105 C  CG    . PHE D 2 250 ? 8.938   28.573 124.016 1.00 6.04  ? 250 PHE B CG    1 
ATOM   4106 C  CD1   . PHE D 2 250 ? 8.552   28.037 122.783 1.00 7.54  ? 250 PHE B CD1   1 
ATOM   4107 C  CD2   . PHE D 2 250 ? 10.129  28.166 124.622 1.00 6.35  ? 250 PHE B CD2   1 
ATOM   4108 C  CE1   . PHE D 2 250 ? 9.363   27.089 122.153 1.00 8.71  ? 250 PHE B CE1   1 
ATOM   4109 C  CE2   . PHE D 2 250 ? 10.942  27.218 123.992 1.00 7.42  ? 250 PHE B CE2   1 
ATOM   4110 C  CZ    . PHE D 2 250 ? 10.558  26.679 122.756 1.00 8.75  ? 250 PHE B CZ    1 
ATOM   4111 N  N     . GLU D 2 251 ? 6.145   29.742 127.655 1.00 9.00  ? 251 GLU B N     1 
ATOM   4112 C  CA    . GLU D 2 251 ? 5.651   30.724 128.600 1.00 9.52  ? 251 GLU B CA    1 
ATOM   4113 C  C     . GLU D 2 251 ? 6.660   31.008 129.689 1.00 9.15  ? 251 GLU B C     1 
ATOM   4114 O  O     . GLU D 2 251 ? 7.565   30.199 129.950 1.00 9.82  ? 251 GLU B O     1 
ATOM   4115 C  CB    . GLU D 2 251 ? 4.360   30.237 129.221 1.00 14.51 ? 251 GLU B CB    1 
ATOM   4116 C  CG    . GLU D 2 251 ? 3.173   30.407 128.278 1.00 22.87 ? 251 GLU B CG    1 
ATOM   4117 C  CD    . GLU D 2 251 ? 1.867   30.672 129.014 1.00 30.52 ? 251 GLU B CD    1 
ATOM   4118 O  OE1   . GLU D 2 251 ? 1.777   30.407 130.272 1.00 31.92 ? 251 GLU B OE1   1 
ATOM   4119 O  OE2   . GLU D 2 251 ? 0.856   31.152 128.376 1.00 34.45 ? 251 GLU B OE2   1 
ATOM   4120 N  N     . PHE D 2 252 ? 6.423   32.161 130.256 1.00 8.83  ? 252 PHE B N     1 
ATOM   4121 C  CA    . PHE D 2 252 ? 7.214   32.701 131.337 1.00 7.62  ? 252 PHE B CA    1 
ATOM   4122 C  C     . PHE D 2 252 ? 6.774   32.079 132.642 1.00 7.64  ? 252 PHE B C     1 
ATOM   4123 O  O     . PHE D 2 252 ? 5.571   31.990 132.936 1.00 7.85  ? 252 PHE B O     1 
ATOM   4124 C  CB    . PHE D 2 252 ? 7.023   34.210 131.400 1.00 6.57  ? 252 PHE B CB    1 
ATOM   4125 C  CG    . PHE D 2 252 ? 7.870   34.930 130.363 1.00 7.28  ? 252 PHE B CG    1 
ATOM   4126 C  CD1   . PHE D 2 252 ? 9.255   34.987 130.527 1.00 5.75  ? 252 PHE B CD1   1 
ATOM   4127 C  CD2   . PHE D 2 252 ? 7.263   35.520 129.250 1.00 8.40  ? 252 PHE B CD2   1 
ATOM   4128 C  CE1   . PHE D 2 252 ? 10.042  35.639 129.576 1.00 7.65  ? 252 PHE B CE1   1 
ATOM   4129 C  CE2   . PHE D 2 252 ? 8.051   36.173 128.297 1.00 8.42  ? 252 PHE B CE2   1 
ATOM   4130 C  CZ    . PHE D 2 252 ? 9.441   36.232 128.460 1.00 8.35  ? 252 PHE B CZ    1 
ATOM   4131 N  N     . SER D 2 253 ? 7.778   31.666 133.362 1.00 7.96  ? 253 SER B N     1 
ATOM   4132 C  CA    . SER D 2 253 ? 7.610   31.064 134.668 1.00 8.95  ? 253 SER B CA    1 
ATOM   4133 C  C     . SER D 2 253 ? 8.021   32.077 135.715 1.00 9.13  ? 253 SER B C     1 
ATOM   4134 O  O     . SER D 2 253 ? 8.964   32.858 135.517 1.00 9.70  ? 253 SER B O     1 
ATOM   4135 C  CB    . SER D 2 253 ? 8.482   29.811 134.772 1.00 11.84 ? 253 SER B CB    1 
ATOM   4136 O  OG    . SER D 2 253 ? 8.389   29.056 133.572 1.00 16.04 ? 253 SER B OG    1 
ATOM   4137 N  N     . ASP D 2 254 ? 7.299   32.045 136.796 1.00 9.13  ? 254 ASP B N     1 
ATOM   4138 C  CA    . ASP D 2 254 ? 7.537   32.955 137.899 1.00 9.04  ? 254 ASP B CA    1 
ATOM   4139 C  C     . ASP D 2 254 ? 8.712   32.474 138.734 1.00 8.64  ? 254 ASP B C     1 
ATOM   4140 O  O     . ASP D 2 254 ? 9.032   31.271 138.750 1.00 7.88  ? 254 ASP B O     1 
ATOM   4141 C  CB    . ASP D 2 254 ? 6.288   33.034 138.772 1.00 11.03 ? 254 ASP B CB    1 
ATOM   4142 C  CG    . ASP D 2 254 ? 5.112   33.662 138.030 1.00 15.16 ? 254 ASP B CG    1 
ATOM   4143 O  OD1   . ASP D 2 254 ? 5.333   34.538 137.107 1.00 15.94 ? 254 ASP B OD1   1 
ATOM   4144 O  OD2   . ASP D 2 254 ? 3.905   33.319 138.320 1.00 18.99 ? 254 ASP B OD2   1 
ATOM   4145 N  N     . ILE D 2 255 ? 9.315   33.457 139.366 1.00 8.49  ? 255 ILE B N     1 
ATOM   4146 C  CA    . ILE D 2 255 ? 10.396  33.245 140.319 1.00 8.81  ? 255 ILE B CA    1 
ATOM   4147 C  C     . ILE D 2 255 ? 9.686   32.889 141.636 1.00 9.42  ? 255 ILE B C     1 
ATOM   4148 O  O     . ILE D 2 255 ? 8.665   33.524 141.950 1.00 9.60  ? 255 ILE B O     1 
ATOM   4149 C  CB    . ILE D 2 255 ? 11.262  34.506 140.413 1.00 8.23  ? 255 ILE B CB    1 
ATOM   4150 C  CG1   . ILE D 2 255 ? 12.203  34.669 139.208 1.00 7.83  ? 255 ILE B CG1   1 
ATOM   4151 C  CG2   . ILE D 2 255 ? 12.151  34.531 141.659 1.00 5.70  ? 255 ILE B CG2   1 
ATOM   4152 C  CD1   . ILE D 2 255 ? 13.549  33.958 139.382 1.00 6.24  ? 255 ILE B CD1   1 
ATOM   4153 N  N     . LEU D 2 256 ? 10.183  31.869 142.265 1.00 8.65  ? 256 LEU B N     1 
ATOM   4154 C  CA    . LEU D 2 256 ? 9.592   31.399 143.520 1.00 8.69  ? 256 LEU B CA    1 
ATOM   4155 C  C     . LEU D 2 256 ? 10.463  31.961 144.646 1.00 9.28  ? 256 LEU B C     1 
ATOM   4156 O  O     . LEU D 2 256 ? 11.661  32.176 144.440 1.00 9.65  ? 256 LEU B O     1 
ATOM   4157 C  CB    . LEU D 2 256 ? 9.532   29.894 143.395 1.00 7.56  ? 256 LEU B CB    1 
ATOM   4158 C  CG    . LEU D 2 256 ? 8.777   29.170 142.322 1.00 5.45  ? 256 LEU B CG    1 
ATOM   4159 C  CD1   . LEU D 2 256 ? 8.948   27.657 142.544 1.00 5.15  ? 256 LEU B CD1   1 
ATOM   4160 C  CD2   . LEU D 2 256 ? 7.285   29.496 142.392 1.00 4.88  ? 256 LEU B CD2   1 
ATOM   4161 N  N     . GLU D 2 257 ? 9.859   32.133 145.802 1.00 10.45 ? 257 GLU B N     1 
ATOM   4162 C  CA    . GLU D 2 257 ? 10.535  32.639 146.993 1.00 10.84 ? 257 GLU B CA    1 
ATOM   4163 C  C     . GLU D 2 257 ? 10.555  31.684 148.163 1.00 12.09 ? 257 GLU B C     1 
ATOM   4164 O  O     . GLU D 2 257 ? 9.532   31.029 148.423 1.00 14.09 ? 257 GLU B O     1 
ATOM   4165 C  CB    . GLU D 2 257 ? 9.804   33.930 147.430 1.00 8.79  ? 257 GLU B CB    1 
ATOM   4166 C  CG    . GLU D 2 257 ? 9.982   35.032 146.371 1.00 6.95  ? 257 GLU B CG    1 
ATOM   4167 C  CD    . GLU D 2 257 ? 11.335  35.658 146.416 1.00 7.37  ? 257 GLU B CD    1 
ATOM   4168 O  OE1   . GLU D 2 257 ? 12.132  35.053 147.151 1.00 7.56  ? 257 GLU B OE1   1 
ATOM   4169 O  OE2   . GLU D 2 257 ? 11.650  36.676 145.840 1.00 6.08  ? 257 GLU B OE2   1 
ATOM   4170 N  N     . GLY D 2 258 ? 11.686  31.593 148.827 1.00 11.86 ? 258 GLY B N     1 
ATOM   4171 C  CA    . GLY D 2 258 ? 12.016  30.804 149.965 1.00 11.72 ? 258 GLY B CA    1 
ATOM   4172 C  C     . GLY D 2 258 ? 12.257  29.328 149.860 1.00 12.56 ? 258 GLY B C     1 
ATOM   4173 O  O     . GLY D 2 258 ? 12.222  28.681 150.954 1.00 13.88 ? 258 GLY B O     1 
ATOM   4174 N  N     . ILE D 2 259 ? 12.496  28.728 148.684 1.00 12.12 ? 259 ILE B N     1 
ATOM   4175 C  CA    . ILE D 2 259 ? 12.724  27.284 148.584 1.00 10.82 ? 259 ILE B CA    1 
ATOM   4176 C  C     . ILE D 2 259 ? 14.198  26.891 148.686 1.00 11.06 ? 259 ILE B C     1 
ATOM   4177 O  O     . ILE D 2 259 ? 14.948  26.917 147.679 1.00 12.24 ? 259 ILE B O     1 
ATOM   4178 C  CB    . ILE D 2 259 ? 12.125  26.618 147.292 1.00 8.52  ? 259 ILE B CB    1 
ATOM   4179 C  CG1   . ILE D 2 259 ? 10.641  26.921 147.056 1.00 8.18  ? 259 ILE B CG1   1 
ATOM   4180 C  CG2   . ILE D 2 259 ? 12.302  25.057 147.320 1.00 8.76  ? 259 ILE B CG2   1 
ATOM   4181 C  CD1   . ILE D 2 259 ? 10.242  26.745 145.552 1.00 7.74  ? 259 ILE B CD1   1 
ATOM   4182 N  N     . GLN D 2 260 ? 14.658  26.428 149.845 1.00 10.69 ? 260 GLN B N     1 
ATOM   4183 C  CA    . GLN D 2 260 ? 16.076  25.992 149.926 1.00 9.56  ? 260 GLN B CA    1 
ATOM   4184 C  C     . GLN D 2 260 ? 16.176  24.515 149.674 1.00 9.92  ? 260 GLN B C     1 
ATOM   4185 O  O     . GLN D 2 260 ? 17.172  24.030 149.119 1.00 10.22 ? 260 GLN B O     1 
ATOM   4186 C  CB    . GLN D 2 260 ? 16.763  26.357 151.216 1.00 5.56  ? 260 GLN B CB    1 
ATOM   4187 C  CG    . GLN D 2 260 ? 16.965  27.865 151.380 1.00 5.70  ? 260 GLN B CG    1 
ATOM   4188 C  CD    . GLN D 2 260 ? 17.834  28.475 150.278 1.00 6.41  ? 260 GLN B CD    1 
ATOM   4189 O  OE1   . GLN D 2 260 ? 17.459  29.487 149.689 1.00 9.11  ? 260 GLN B OE1   1 
ATOM   4190 N  NE2   . GLN D 2 260 ? 18.986  27.915 149.961 1.00 3.28  ? 260 GLN B NE2   1 
ATOM   4191 N  N     . THR D 2 261 ? 15.140  23.854 150.082 1.00 9.40  ? 261 THR B N     1 
ATOM   4192 C  CA    . THR D 2 261 ? 15.018  22.435 149.860 1.00 9.48  ? 261 THR B CA    1 
ATOM   4193 C  C     . THR D 2 261 ? 13.569  22.091 149.591 1.00 10.58 ? 261 THR B C     1 
ATOM   4194 O  O     . THR D 2 261 ? 12.655  22.786 150.068 1.00 10.24 ? 261 THR B O     1 
ATOM   4195 C  CB    . THR D 2 261 ? 15.533  21.634 151.051 1.00 7.76  ? 261 THR B CB    1 
ATOM   4196 O  OG1   . THR D 2 261 ? 14.444  21.169 151.829 1.00 9.40  ? 261 THR B OG1   1 
ATOM   4197 C  CG2   . THR D 2 261 ? 16.455  22.440 151.963 1.00 8.10  ? 261 THR B CG2   1 
ATOM   4198 N  N     . LEU D 2 262 ? 13.500  21.043 148.834 1.00 11.35 ? 262 LEU B N     1 
ATOM   4199 C  CA    . LEU D 2 262 ? 12.287  20.404 148.360 1.00 11.64 ? 262 LEU B CA    1 
ATOM   4200 C  C     . LEU D 2 262 ? 12.464  18.902 148.615 1.00 12.00 ? 262 LEU B C     1 
ATOM   4201 O  O     . LEU D 2 262 ? 13.351  18.258 148.035 1.00 13.53 ? 262 LEU B O     1 
ATOM   4202 C  CB    . LEU D 2 262 ? 12.213  20.628 146.842 1.00 12.88 ? 262 LEU B CB    1 
ATOM   4203 C  CG    . LEU D 2 262 ? 10.839  21.075 146.342 1.00 11.00 ? 262 LEU B CG    1 
ATOM   4204 C  CD1   . LEU D 2 262 ? 10.261  22.243 147.139 1.00 11.99 ? 262 LEU B CD1   1 
ATOM   4205 C  CD2   . LEU D 2 262 ? 10.864  21.541 144.882 1.00 10.46 ? 262 LEU B CD2   1 
ATOM   4206 N  N     . PRO D 2 263 ? 11.690  18.197 149.465 1.00 11.28 ? 263 PRO B N     1 
ATOM   4207 C  CA    . PRO D 2 263 ? 10.571  18.770 150.224 1.00 9.97  ? 263 PRO B CA    1 
ATOM   4208 C  C     . PRO D 2 263 ? 11.018  19.863 151.176 1.00 9.75  ? 263 PRO B C     1 
ATOM   4209 O  O     . PRO D 2 263 ? 12.111  19.726 151.811 1.00 10.00 ? 263 PRO B O     1 
ATOM   4210 C  CB    . PRO D 2 263 ? 10.028  17.588 151.005 1.00 9.48  ? 263 PRO B CB    1 
ATOM   4211 C  CG    . PRO D 2 263 ? 10.872  16.365 150.662 1.00 10.03 ? 263 PRO B CG    1 
ATOM   4212 C  CD    . PRO D 2 263 ? 11.926  16.766 149.688 1.00 10.72 ? 263 PRO B CD    1 
ATOM   4213 N  N     . PRO D 2 264 ? 10.258  20.983 151.358 1.00 9.09  ? 264 PRO B N     1 
ATOM   4214 C  CA    . PRO D 2 264 ? 10.663  22.013 152.291 1.00 8.70  ? 264 PRO B CA    1 
ATOM   4215 C  C     . PRO D 2 264 ? 10.724  21.394 153.645 1.00 10.24 ? 264 PRO B C     1 
ATOM   4216 O  O     . PRO D 2 264 ? 10.059  20.342 153.876 1.00 11.12 ? 264 PRO B O     1 
ATOM   4217 C  CB    . PRO D 2 264 ? 9.593   23.073 152.187 1.00 7.77  ? 264 PRO B CB    1 
ATOM   4218 C  CG    . PRO D 2 264 ? 8.567   22.591 151.181 1.00 7.79  ? 264 PRO B CG    1 
ATOM   4219 C  CD    . PRO D 2 264 ? 8.993   21.242 150.665 1.00 8.33  ? 264 PRO B CD    1 
ATOM   4220 N  N     . ALA D 2 265 ? 11.485  22.005 154.495 1.00 11.35 ? 265 ALA B N     1 
ATOM   4221 C  CA    . ALA D 2 265 ? 11.676  21.512 155.848 1.00 10.69 ? 265 ALA B CA    1 
ATOM   4222 C  C     . ALA D 2 265 ? 10.357  21.394 156.576 1.00 10.29 ? 265 ALA B C     1 
ATOM   4223 O  O     . ALA D 2 265 ? 9.360   22.047 156.247 1.00 10.61 ? 265 ALA B O     1 
ATOM   4224 C  CB    . ALA D 2 265 ? 12.542  22.479 156.642 1.00 10.95 ? 265 ALA B CB    1 
ATOM   4225 N  N     . ASN D 2 266 ? 10.399  20.566 157.554 1.00 10.32 ? 266 ASN B N     1 
ATOM   4226 C  CA    . ASN D 2 266 ? 9.267   20.367 158.413 1.00 10.28 ? 266 ASN B CA    1 
ATOM   4227 C  C     . ASN D 2 266 ? 8.097   19.811 157.593 1.00 10.57 ? 266 ASN B C     1 
ATOM   4228 O  O     . ASN D 2 266 ? 6.930   20.152 157.843 1.00 10.69 ? 266 ASN B O     1 
ATOM   4229 C  CB    . ASN D 2 266 ? 9.018   21.679 159.145 1.00 10.93 ? 266 ASN B CB    1 
ATOM   4230 C  CG    . ASN D 2 266 ? 10.049  21.849 160.268 1.00 13.31 ? 266 ASN B CG    1 
ATOM   4231 O  OD1   . ASN D 2 266 ? 10.438  20.855 160.888 1.00 16.79 ? 266 ASN B OD1   1 
ATOM   4232 N  ND2   . ASN D 2 266 ? 10.530  23.038 160.572 1.00 13.56 ? 266 ASN B ND2   1 
ATOM   4233 N  N     . VAL D 2 267 ? 8.532   18.965 156.666 1.00 10.24 ? 267 VAL B N     1 
ATOM   4234 C  CA    . VAL D 2 267 ? 7.698   18.089 155.813 1.00 11.11 ? 267 VAL B CA    1 
ATOM   4235 C  C     . VAL D 2 267 ? 8.580   16.921 155.382 1.00 11.82 ? 267 VAL B C     1 
ATOM   4236 O  O     . VAL D 2 267 ? 9.639   17.116 154.765 1.00 11.87 ? 267 VAL B O     1 
ATOM   4237 C  CB    . VAL D 2 267 ? 7.110   18.786 154.582 1.00 10.35 ? 267 VAL B CB    1 
ATOM   4238 C  CG1   . VAL D 2 267 ? 7.508   20.248 154.453 1.00 11.45 ? 267 VAL B CG1   1 
ATOM   4239 C  CG2   . VAL D 2 267 ? 7.518   18.111 153.268 1.00 11.20 ? 267 VAL B CG2   1 
ATOM   4240 N  N     . THR D 2 268 ? 8.095   15.757 155.739 1.00 13.19 ? 268 THR B N     1 
ATOM   4241 C  CA    . THR D 2 268 ? 8.760   14.478 155.483 1.00 13.64 ? 268 THR B CA    1 
ATOM   4242 C  C     . THR D 2 268 ? 8.760   14.144 153.988 1.00 14.30 ? 268 THR B C     1 
ATOM   4243 O  O     . THR D 2 268 ? 7.879   14.582 153.234 1.00 15.51 ? 268 THR B O     1 
ATOM   4244 C  CB    . THR D 2 268 ? 8.005   13.372 156.226 1.00 13.71 ? 268 THR B CB    1 
ATOM   4245 O  OG1   . THR D 2 268 ? 8.758   12.933 157.344 1.00 17.15 ? 268 THR B OG1   1 
ATOM   4246 C  CG2   . THR D 2 268 ? 7.714   12.152 155.352 1.00 13.18 ? 268 THR B CG2   1 
ATOM   4247 N  N     . VAL D 2 269 ? 9.765   13.370 153.594 1.00 13.89 ? 269 VAL B N     1 
ATOM   4248 C  CA    . VAL D 2 269 ? 9.889   12.903 152.205 1.00 13.40 ? 269 VAL B CA    1 
ATOM   4249 C  C     . VAL D 2 269 ? 8.572   12.216 151.842 1.00 13.85 ? 269 VAL B C     1 
ATOM   4250 O  O     . VAL D 2 269 ? 7.844   12.540 150.897 1.00 15.29 ? 269 VAL B O     1 
ATOM   4251 C  CB    . VAL D 2 269 ? 11.072  11.944 152.071 1.00 10.80 ? 269 VAL B CB    1 
ATOM   4252 C  CG1   . VAL D 2 269 ? 10.991  11.065 150.822 1.00 6.26  ? 269 VAL B CG1   1 
ATOM   4253 C  CG2   . VAL D 2 269 ? 12.418  12.669 151.978 1.00 11.45 ? 269 VAL B CG2   1 
ATOM   4254 N  N     . ALA D 2 270 ? 8.252   11.242 152.669 1.00 13.23 ? 270 ALA B N     1 
ATOM   4255 C  CA    . ALA D 2 270 ? 7.040   10.436 152.513 1.00 12.13 ? 270 ALA B CA    1 
ATOM   4256 C  C     . ALA D 2 270 ? 5.783   11.281 152.360 1.00 12.45 ? 270 ALA B C     1 
ATOM   4257 O  O     . ALA D 2 270 ? 4.846   10.800 151.682 1.00 13.53 ? 270 ALA B O     1 
ATOM   4258 C  CB    . ALA D 2 270 ? 6.913   9.477  153.698 1.00 10.03 ? 270 ALA B CB    1 
ATOM   4259 N  N     . THR D 2 271 ? 5.738   12.429 153.002 1.00 12.32 ? 271 THR B N     1 
ATOM   4260 C  CA    . THR D 2 271 ? 4.561   13.303 152.905 1.00 12.47 ? 271 THR B CA    1 
ATOM   4261 C  C     . THR D 2 271 ? 4.561   13.956 151.515 1.00 13.32 ? 271 THR B C     1 
ATOM   4262 O  O     . THR D 2 271 ? 3.547   13.978 150.819 1.00 14.65 ? 271 THR B O     1 
ATOM   4263 C  CB    . THR D 2 271 ? 4.453   14.408 154.017 1.00 11.02 ? 271 THR B CB    1 
ATOM   4264 O  OG1   . THR D 2 271 ? 4.825   13.798 155.293 1.00 13.30 ? 271 THR B OG1   1 
ATOM   4265 C  CG2   . THR D 2 271 ? 3.081   15.091 154.103 1.00 9.48  ? 271 THR B CG2   1 
ATOM   4266 N  N     . SER D 2 272 ? 5.713   14.487 151.164 1.00 13.50 ? 272 SER B N     1 
ATOM   4267 C  CA    . SER D 2 272 ? 5.920   15.136 149.869 1.00 14.55 ? 272 SER B CA    1 
ATOM   4268 C  C     . SER D 2 272 ? 5.571   14.174 148.725 1.00 15.55 ? 272 SER B C     1 
ATOM   4269 O  O     . SER D 2 272 ? 5.085   14.581 147.669 1.00 15.99 ? 272 SER B O     1 
ATOM   4270 C  CB    . SER D 2 272 ? 7.404   15.490 149.688 1.00 14.52 ? 272 SER B CB    1 
ATOM   4271 O  OG    . SER D 2 272 ? 8.119   14.333 149.222 1.00 15.94 ? 272 SER B OG    1 
ATOM   4272 N  N     . GLY D 2 273 ? 5.892   12.921 148.947 1.00 16.66 ? 273 GLY B N     1 
ATOM   4273 C  CA    . GLY D 2 273 ? 5.664   11.915 147.913 1.00 17.28 ? 273 GLY B CA    1 
ATOM   4274 C  C     . GLY D 2 273 ? 6.854   11.872 146.950 1.00 17.10 ? 273 GLY B C     1 
ATOM   4275 O  O     . GLY D 2 273 ? 6.716   11.207 145.879 1.00 18.59 ? 273 GLY B O     1 
ATOM   4276 N  N     . GLN D 2 274 ? 7.956   12.514 147.300 1.00 15.14 ? 274 GLN B N     1 
ATOM   4277 C  CA    . GLN D 2 274 ? 9.154   12.488 146.424 1.00 12.94 ? 274 GLN B CA    1 
ATOM   4278 C  C     . GLN D 2 274 ? 9.986   11.239 146.712 1.00 11.65 ? 274 GLN B C     1 
ATOM   4279 O  O     . GLN D 2 274 ? 10.144  10.833 147.874 1.00 11.81 ? 274 GLN B O     1 
ATOM   4280 C  CB    . GLN D 2 274 ? 9.992   13.729 146.604 1.00 11.20 ? 274 GLN B CB    1 
ATOM   4281 C  CG    . GLN D 2 274 ? 9.433   14.951 145.876 1.00 10.06 ? 274 GLN B CG    1 
ATOM   4282 C  CD    . GLN D 2 274 ? 10.213  16.231 146.184 1.00 12.03 ? 274 GLN B CD    1 
ATOM   4283 O  OE1   . GLN D 2 274 ? 9.694   17.329 145.992 1.00 14.04 ? 274 GLN B OE1   1 
ATOM   4284 N  NE2   . GLN D 2 274 ? 11.443  16.156 146.659 1.00 13.69 ? 274 GLN B NE2   1 
ATOM   4285 N  N     . PRO D 2 275 ? 10.545  10.584 145.680 1.00 10.82 ? 275 PRO B N     1 
ATOM   4286 C  CA    . PRO D 2 275 ? 11.327  9.376  145.878 1.00 10.34 ? 275 PRO B CA    1 
ATOM   4287 C  C     . PRO D 2 275 ? 12.490  9.655  146.790 1.00 10.54 ? 275 PRO B C     1 
ATOM   4288 O  O     . PRO D 2 275 ? 12.845  8.765  147.625 1.00 11.42 ? 275 PRO B O     1 
ATOM   4289 C  CB    . PRO D 2 275 ? 11.765  8.992  144.486 1.00 9.38  ? 275 PRO B CB    1 
ATOM   4290 C  CG    . PRO D 2 275 ? 11.197  10.018 143.518 1.00 9.27  ? 275 PRO B CG    1 
ATOM   4291 C  CD    . PRO D 2 275 ? 10.415  11.032 144.293 1.00 10.11 ? 275 PRO B CD    1 
ATOM   4292 N  N     . PHE D 2 276 ? 13.030  10.842 146.605 1.00 9.90  ? 276 PHE B N     1 
ATOM   4293 C  CA    . PHE D 2 276 ? 14.169  11.361 147.383 1.00 8.95  ? 276 PHE B CA    1 
ATOM   4294 C  C     . PHE D 2 276 ? 14.072  12.876 147.425 1.00 9.78  ? 276 PHE B C     1 
ATOM   4295 O  O     . PHE D 2 276 ? 13.088  13.475 146.992 1.00 9.86  ? 276 PHE B O     1 
ATOM   4296 C  CB    . PHE D 2 276 ? 15.475  10.975 146.723 1.00 6.62  ? 276 PHE B CB    1 
ATOM   4297 C  CG    . PHE D 2 276 ? 15.414  11.178 145.224 1.00 7.24  ? 276 PHE B CG    1 
ATOM   4298 C  CD1   . PHE D 2 276 ? 14.945  10.145 144.415 1.00 5.67  ? 276 PHE B CD1   1 
ATOM   4299 C  CD2   . PHE D 2 276 ? 15.812  12.397 144.672 1.00 7.65  ? 276 PHE B CD2   1 
ATOM   4300 C  CE1   . PHE D 2 276 ? 14.883  10.328 143.031 1.00 4.88  ? 276 PHE B CE1   1 
ATOM   4301 C  CE2   . PHE D 2 276 ? 15.749  12.582 143.289 1.00 6.99  ? 276 PHE B CE2   1 
ATOM   4302 C  CZ    . PHE D 2 276 ? 15.286  11.547 142.468 1.00 5.55  ? 276 PHE B CZ    1 
ATOM   4303 N  N     . ASN D 2 277 ? 15.108  13.525 147.896 1.00 10.45 ? 277 ASN B N     1 
ATOM   4304 C  CA    . ASN D 2 277 ? 15.009  14.969 148.093 1.00 11.42 ? 277 ASN B CA    1 
ATOM   4305 C  C     . ASN D 2 277 ? 16.232  15.729 147.528 1.00 12.26 ? 277 ASN B C     1 
ATOM   4306 O  O     . ASN D 2 277 ? 17.337  15.175 147.409 1.00 13.39 ? 277 ASN B O     1 
ATOM   4307 C  CB    . ASN D 2 277 ? 14.734  15.174 149.594 1.00 11.84 ? 277 ASN B CB    1 
ATOM   4308 C  CG    . ASN D 2 277 ? 15.815  15.906 150.374 1.00 16.03 ? 277 ASN B CG    1 
ATOM   4309 O  OD1   . ASN D 2 277 ? 16.596  16.644 149.789 1.00 21.90 ? 277 ASN B OD1   1 
ATOM   4310 N  ND2   . ASN D 2 277 ? 15.890  15.752 151.686 1.00 14.46 ? 277 ASN B ND2   1 
ATOM   4311 N  N     . LEU D 2 278 ? 15.923  16.990 147.190 1.00 12.18 ? 278 LEU B N     1 
ATOM   4312 C  CA    . LEU D 2 278 ? 16.853  17.990 146.599 1.00 11.22 ? 278 LEU B CA    1 
ATOM   4313 C  C     . LEU D 2 278 ? 17.080  19.156 147.579 1.00 10.10 ? 278 LEU B C     1 
ATOM   4314 O  O     . LEU D 2 278 ? 16.096  19.756 148.063 1.00 9.20  ? 278 LEU B O     1 
ATOM   4315 C  CB    . LEU D 2 278 ? 16.216  18.621 145.351 1.00 12.52 ? 278 LEU B CB    1 
ATOM   4316 C  CG    . LEU D 2 278 ? 16.556  17.911 144.042 1.00 14.73 ? 278 LEU B CG    1 
ATOM   4317 C  CD1   . LEU D 2 278 ? 16.069  16.463 144.001 1.00 16.29 ? 278 LEU B CD1   1 
ATOM   4318 C  CD2   . LEU D 2 278 ? 15.929  18.593 142.821 1.00 15.15 ? 278 LEU B CD2   1 
ATOM   4319 N  N     . ALA D 2 279 ? 18.334  19.451 147.831 1.00 10.25 ? 279 ALA B N     1 
ATOM   4320 C  CA    . ALA D 2 279 ? 18.713  20.547 148.749 1.00 11.61 ? 279 ALA B CA    1 
ATOM   4321 C  C     . ALA D 2 279 ? 19.684  21.518 148.085 1.00 12.67 ? 279 ALA B C     1 
ATOM   4322 O  O     . ALA D 2 279 ? 20.819  21.126 147.753 1.00 14.07 ? 279 ALA B O     1 
ATOM   4323 C  CB    . ALA D 2 279 ? 19.344  19.984 150.001 1.00 9.78  ? 279 ALA B CB    1 
ATOM   4324 N  N     . ALA D 2 280 ? 19.243  22.752 147.923 1.00 12.54 ? 280 ALA B N     1 
ATOM   4325 C  CA    . ALA D 2 280 ? 20.064  23.822 147.324 1.00 12.34 ? 280 ALA B CA    1 
ATOM   4326 C  C     . ALA D 2 280 ? 21.062  24.311 148.389 1.00 12.83 ? 280 ALA B C     1 
ATOM   4327 O  O     . ALA D 2 280 ? 22.042  25.055 148.139 1.00 14.51 ? 280 ALA B O     1 
ATOM   4328 C  CB    . ALA D 2 280 ? 19.207  24.964 146.809 1.00 8.29  ? 280 ALA B CB    1 
ATOM   4329 N  N     . GLY D 2 281 ? 20.802  23.885 149.624 1.00 11.78 ? 281 GLY B N     1 
ATOM   4330 C  CA    . GLY D 2 281 ? 21.666  24.246 150.739 1.00 10.46 ? 281 GLY B CA    1 
ATOM   4331 C  C     . GLY D 2 281 ? 21.337  25.564 151.414 1.00 10.05 ? 281 GLY B C     1 
ATOM   4332 O  O     . GLY D 2 281 ? 20.177  25.962 151.595 1.00 10.09 ? 281 GLY B O     1 
ATOM   4333 N  N     . ALA D 2 282 ? 22.415  26.217 151.844 1.00 9.61  ? 282 ALA B N     1 
ATOM   4334 C  CA    . ALA D 2 282 ? 22.341  27.497 152.553 1.00 10.28 ? 282 ALA B CA    1 
ATOM   4335 C  C     . ALA D 2 282 ? 21.888  28.591 151.600 1.00 11.19 ? 282 ALA B C     1 
ATOM   4336 O  O     . ALA D 2 282 ? 22.327  28.728 150.437 1.00 11.58 ? 282 ALA B O     1 
ATOM   4337 C  CB    . ALA D 2 282 ? 23.666  27.793 153.197 1.00 10.40 ? 282 ALA B CB    1 
ATOM   4338 N  N     . GLU D 2 283 ? 21.002  29.408 152.128 1.00 11.52 ? 283 GLU B N     1 
ATOM   4339 C  CA    . GLU D 2 283 ? 20.385  30.484 151.361 1.00 11.57 ? 283 GLU B CA    1 
ATOM   4340 C  C     . GLU D 2 283 ? 21.330  31.511 150.817 1.00 11.24 ? 283 GLU B C     1 
ATOM   4341 O  O     . GLU D 2 283 ? 21.020  32.183 149.792 1.00 13.36 ? 283 GLU B O     1 
ATOM   4342 C  CB    . GLU D 2 283 ? 19.264  31.119 152.174 1.00 12.63 ? 283 GLU B CB    1 
ATOM   4343 C  CG    . GLU D 2 283 ? 19.531  32.343 153.011 1.00 16.57 ? 283 GLU B CG    1 
ATOM   4344 C  CD    . GLU D 2 283 ? 18.384  32.855 153.831 1.00 20.77 ? 283 GLU B CD    1 
ATOM   4345 O  OE1   . GLU D 2 283 ? 17.275  32.479 153.413 1.00 23.03 ? 283 GLU B OE1   1 
ATOM   4346 O  OE2   . GLU D 2 283 ? 18.536  33.555 154.820 1.00 22.99 ? 283 GLU B OE2   1 
ATOM   4347 N  N     . ALA D 2 284 ? 22.486  31.663 151.440 1.00 10.31 ? 284 ALA B N     1 
ATOM   4348 C  CA    . ALA D 2 284 ? 23.418  32.710 150.933 1.00 10.30 ? 284 ALA B CA    1 
ATOM   4349 C  C     . ALA D 2 284 ? 24.300  32.140 149.843 1.00 11.79 ? 284 ALA B C     1 
ATOM   4350 O  O     . ALA D 2 284 ? 25.089  32.866 149.215 1.00 12.53 ? 284 ALA B O     1 
ATOM   4351 C  CB    . ALA D 2 284 ? 24.204  33.304 152.081 1.00 6.96  ? 284 ALA B CB    1 
ATOM   4352 N  N     . VAL D 2 285 ? 24.100  30.848 149.643 1.00 11.53 ? 285 VAL B N     1 
ATOM   4353 C  CA    . VAL D 2 285 ? 24.895  30.115 148.639 1.00 11.17 ? 285 VAL B CA    1 
ATOM   4354 C  C     . VAL D 2 285 ? 24.138  29.704 147.400 1.00 11.45 ? 285 VAL B C     1 
ATOM   4355 O  O     . VAL D 2 285 ? 24.751  29.811 146.318 1.00 12.41 ? 285 VAL B O     1 
ATOM   4356 C  CB    . VAL D 2 285 ? 25.597  29.008 149.461 1.00 8.86  ? 285 VAL B CB    1 
ATOM   4357 C  CG1   . VAL D 2 285 ? 25.784  27.703 148.738 1.00 8.12  ? 285 VAL B CG1   1 
ATOM   4358 C  CG2   . VAL D 2 285 ? 26.904  29.565 150.012 1.00 8.45  ? 285 VAL B CG2   1 
ATOM   4359 N  N     . SER D 2 286 ? 22.896  29.284 147.470 1.00 10.91 ? 286 SER B N     1 
ATOM   4360 C  CA    . SER D 2 286 ? 22.113  28.856 146.296 1.00 10.85 ? 286 SER B CA    1 
ATOM   4361 C  C     . SER D 2 286 ? 20.643  28.706 146.668 1.00 11.73 ? 286 SER B C     1 
ATOM   4362 O  O     . SER D 2 286 ? 20.257  28.980 147.835 1.00 13.57 ? 286 SER B O     1 
ATOM   4363 C  CB    . SER D 2 286 ? 22.727  27.563 145.784 1.00 10.37 ? 286 SER B CB    1 
ATOM   4364 O  OG    . SER D 2 286 ? 21.956  27.021 144.722 1.00 10.80 ? 286 SER B OG    1 
ATOM   4365 N  N     . GLY D 2 287 ? 19.785  28.289 145.761 1.00 11.38 ? 287 GLY B N     1 
ATOM   4366 C  CA    . GLY D 2 287 ? 18.364  28.104 146.126 1.00 11.38 ? 287 GLY B CA    1 
ATOM   4367 C  C     . GLY D 2 287 ? 17.540  27.654 144.950 1.00 12.14 ? 287 GLY B C     1 
ATOM   4368 O  O     . GLY D 2 287 ? 17.958  27.789 143.781 1.00 12.87 ? 287 GLY B O     1 
ATOM   4369 N  N     . ILE D 2 288 ? 16.371  27.108 145.214 1.00 12.07 ? 288 ILE B N     1 
ATOM   4370 C  CA    . ILE D 2 288 ? 15.450  26.694 144.111 1.00 11.55 ? 288 ILE B CA    1 
ATOM   4371 C  C     . ILE D 2 288 ? 14.597  27.938 143.825 1.00 13.00 ? 288 ILE B C     1 
ATOM   4372 O  O     . ILE D 2 288 ? 13.684  28.240 144.638 1.00 13.92 ? 288 ILE B O     1 
ATOM   4373 C  CB    . ILE D 2 288 ? 14.620  25.432 144.479 1.00 7.18  ? 288 ILE B CB    1 
ATOM   4374 C  CG1   . ILE D 2 288 ? 15.608  24.290 144.827 1.00 7.53  ? 288 ILE B CG1   1 
ATOM   4375 C  CG2   . ILE D 2 288 ? 13.637  25.055 143.343 1.00 4.65  ? 288 ILE B CG2   1 
ATOM   4376 C  CD1   . ILE D 2 288 ? 15.111  23.228 145.797 1.00 6.78  ? 288 ILE B CD1   1 
ATOM   4377 N  N     . VAL D 2 289 ? 14.949  28.657 142.765 1.00 13.10 ? 289 VAL B N     1 
ATOM   4378 C  CA    . VAL D 2 289 ? 14.193  29.869 142.436 1.00 12.15 ? 289 VAL B CA    1 
ATOM   4379 C  C     . VAL D 2 289 ? 13.086  29.672 141.395 1.00 13.09 ? 289 VAL B C     1 
ATOM   4380 O  O     . VAL D 2 289 ? 12.335  30.607 141.078 1.00 15.15 ? 289 VAL B O     1 
ATOM   4381 C  CB    . VAL D 2 289 ? 15.180  30.937 141.925 1.00 8.33  ? 289 VAL B CB    1 
ATOM   4382 C  CG1   . VAL D 2 289 ? 16.170  31.398 142.997 1.00 6.55  ? 289 VAL B CG1   1 
ATOM   4383 C  CG2   . VAL D 2 289 ? 16.033  30.448 140.753 1.00 7.42  ? 289 VAL B CG2   1 
ATOM   4384 N  N     . GLY D 2 290 ? 12.970  28.477 140.869 1.00 12.45 ? 290 GLY B N     1 
ATOM   4385 C  CA    . GLY D 2 290 ? 11.932  28.187 139.866 1.00 11.67 ? 290 GLY B CA    1 
ATOM   4386 C  C     . GLY D 2 290 ? 12.146  26.810 139.257 1.00 11.18 ? 290 GLY B C     1 
ATOM   4387 O  O     . GLY D 2 290 ? 13.099  26.101 139.604 1.00 10.96 ? 290 GLY B O     1 
ATOM   4388 N  N     . TRP D 2 291 ? 11.243  26.475 138.356 1.00 10.05 ? 291 TRP B N     1 
ATOM   4389 C  CA    . TRP D 2 291 ? 11.267  25.183 137.662 1.00 9.02  ? 291 TRP B CA    1 
ATOM   4390 C  C     . TRP D 2 291 ? 10.546  25.305 136.304 1.00 9.69  ? 291 TRP B C     1 
ATOM   4391 O  O     . TRP D 2 291 ? 9.306   25.265 136.239 1.00 10.06 ? 291 TRP B O     1 
ATOM   4392 C  CB    . TRP D 2 291 ? 10.601  24.134 138.544 1.00 7.11  ? 291 TRP B CB    1 
ATOM   4393 C  CG    . TRP D 2 291 ? 10.977  22.730 138.120 1.00 6.61  ? 291 TRP B CG    1 
ATOM   4394 C  CD1   . TRP D 2 291 ? 10.494  22.074 137.070 1.00 6.15  ? 291 TRP B CD1   1 
ATOM   4395 C  CD2   . TRP D 2 291 ? 11.916  21.898 138.782 1.00 7.08  ? 291 TRP B CD2   1 
ATOM   4396 N  NE1   . TRP D 2 291 ? 11.138  20.806 137.042 1.00 7.44  ? 291 TRP B NE1   1 
ATOM   4397 C  CE2   . TRP D 2 291 ? 11.972  20.722 138.049 1.00 7.25  ? 291 TRP B CE2   1 
ATOM   4398 C  CE3   . TRP D 2 291 ? 12.724  22.028 139.921 1.00 7.57  ? 291 TRP B CE3   1 
ATOM   4399 C  CZ2   . TRP D 2 291 ? 12.807  19.651 138.376 1.00 7.47  ? 291 TRP B CZ2   1 
ATOM   4400 C  CZ3   . TRP D 2 291 ? 13.560  20.939 140.248 1.00 8.33  ? 291 TRP B CZ3   1 
ATOM   4401 C  CH2   . TRP D 2 291 ? 13.599  19.807 139.509 1.00 8.55  ? 291 TRP B CH2   1 
ATOM   4402 N  N     . GLY D 2 292 ? 11.387  25.432 135.275 1.00 9.33  ? 292 GLY B N     1 
ATOM   4403 C  CA    . GLY D 2 292 ? 10.986  25.667 133.858 1.00 8.73  ? 292 GLY B CA    1 
ATOM   4404 C  C     . GLY D 2 292 ? 10.347  24.443 133.175 1.00 8.39  ? 292 GLY B C     1 
ATOM   4405 O  O     . GLY D 2 292 ? 10.182  23.375 133.785 1.00 7.93  ? 292 GLY B O     1 
ATOM   4406 N  N     . ASN D 2 293 ? 10.030  24.671 131.895 1.00 9.01  ? 293 ASN B N     1 
ATOM   4407 C  CA    . ASN D 2 293 ? 9.327   23.697 131.039 1.00 10.32 ? 293 ASN B CA    1 
ATOM   4408 C  C     . ASN D 2 293 ? 10.265  22.971 130.122 1.00 11.33 ? 293 ASN B C     1 
ATOM   4409 O  O     . ASN D 2 293 ? 10.154  23.090 128.887 1.00 11.64 ? 293 ASN B O     1 
ATOM   4410 C  CB    . ASN D 2 293 ? 8.211   24.417 130.303 1.00 11.04 ? 293 ASN B CB    1 
ATOM   4411 C  CG    . ASN D 2 293 ? 7.204   25.004 131.297 1.00 11.80 ? 293 ASN B CG    1 
ATOM   4412 O  OD1   . ASN D 2 293 ? 6.381   25.835 130.929 1.00 16.31 ? 293 ASN B OD1   1 
ATOM   4413 N  ND2   . ASN D 2 293 ? 7.227   24.614 132.564 1.00 10.78 ? 293 ASN B ND2   1 
ATOM   4414 N  N     . MET D 2 294 ? 11.111  22.156 130.696 1.00 11.87 ? 294 MET B N     1 
ATOM   4415 C  CA    . MET D 2 294 ? 12.115  21.328 129.989 1.00 11.49 ? 294 MET B CA    1 
ATOM   4416 C  C     . MET D 2 294 ? 12.164  19.937 130.600 1.00 11.34 ? 294 MET B C     1 
ATOM   4417 O  O     . MET D 2 294 ? 11.999  19.872 131.848 1.00 11.53 ? 294 MET B O     1 
ATOM   4418 C  CB    . MET D 2 294 ? 13.477  22.013 130.242 1.00 12.92 ? 294 MET B CB    1 
ATOM   4419 C  CG    . MET D 2 294 ? 13.447  23.447 129.807 1.00 13.74 ? 294 MET B CG    1 
ATOM   4420 S  SD    . MET D 2 294 ? 13.896  23.476 128.021 1.00 19.66 ? 294 MET B SD    1 
ATOM   4421 C  CE    . MET D 2 294 ? 12.324  24.042 127.379 1.00 16.87 ? 294 MET B CE    1 
ATOM   4422 N  N     . ASP D 2 295 ? 12.408  18.869 129.877 1.00 11.27 ? 295 ASP B N     1 
ATOM   4423 C  CA    . ASP D 2 295 ? 12.457  17.552 130.609 1.00 11.09 ? 295 ASP B CA    1 
ATOM   4424 C  C     . ASP D 2 295 ? 13.787  17.529 131.367 1.00 11.28 ? 295 ASP B C     1 
ATOM   4425 O  O     . ASP D 2 295 ? 14.721  18.218 130.908 1.00 11.66 ? 295 ASP B O     1 
ATOM   4426 C  CB    . ASP D 2 295 ? 12.184  16.390 129.714 1.00 11.85 ? 295 ASP B CB    1 
ATOM   4427 C  CG    . ASP D 2 295 ? 10.725  16.150 129.422 1.00 14.64 ? 295 ASP B CG    1 
ATOM   4428 O  OD1   . ASP D 2 295 ? 9.906   16.829 130.066 1.00 13.29 ? 295 ASP B OD1   1 
ATOM   4429 O  OD2   . ASP D 2 295 ? 10.380  15.312 128.581 1.00 17.12 ? 295 ASP B OD2   1 
ATOM   4430 N  N     . THR D 2 296 ? 13.824  16.823 132.491 1.00 10.95 ? 296 THR B N     1 
ATOM   4431 C  CA    . THR D 2 296 ? 15.103  16.766 133.219 1.00 10.70 ? 296 THR B CA    1 
ATOM   4432 C  C     . THR D 2 296 ? 15.977  15.732 132.518 1.00 10.67 ? 296 THR B C     1 
ATOM   4433 O  O     . THR D 2 296 ? 15.420  14.777 131.926 1.00 10.48 ? 296 THR B O     1 
ATOM   4434 C  CB    . THR D 2 296 ? 14.931  16.566 134.751 1.00 11.47 ? 296 THR B CB    1 
ATOM   4435 O  OG1   . THR D 2 296 ? 15.444  17.817 135.346 1.00 14.04 ? 296 THR B OG1   1 
ATOM   4436 C  CG2   . THR D 2 296 ? 15.686  15.377 135.376 1.00 10.22 ? 296 THR B CG2   1 
ATOM   4437 N  N     . ILE D 2 297 ? 17.278  15.941 132.531 1.00 10.75 ? 297 ILE B N     1 
ATOM   4438 C  CA    . ILE D 2 297 ? 18.215  14.990 131.909 1.00 10.58 ? 297 ILE B CA    1 
ATOM   4439 C  C     . ILE D 2 297 ? 18.880  14.182 133.038 1.00 10.74 ? 297 ILE B C     1 
ATOM   4440 O  O     . ILE D 2 297 ? 19.510  14.784 133.943 1.00 11.50 ? 297 ILE B O     1 
ATOM   4441 C  CB    . ILE D 2 297 ? 19.292  15.668 131.008 1.00 8.88  ? 297 ILE B CB    1 
ATOM   4442 C  CG1   . ILE D 2 297 ? 18.641  16.505 129.902 1.00 8.70  ? 297 ILE B CG1   1 
ATOM   4443 C  CG2   . ILE D 2 297 ? 20.299  14.637 130.412 1.00 9.77  ? 297 ILE B CG2   1 
ATOM   4444 C  CD1   . ILE D 2 297 ? 19.651  17.420 129.149 1.00 7.87  ? 297 ILE B CD1   1 
ATOM   4445 N  N     . VAL D 2 298 ? 18.721  12.873 133.011 1.00 10.23 ? 298 VAL B N     1 
ATOM   4446 C  CA    . VAL D 2 298 ? 19.345  12.045 134.059 1.00 9.16  ? 298 VAL B CA    1 
ATOM   4447 C  C     . VAL D 2 298 ? 20.640  11.481 133.466 1.00 9.46  ? 298 VAL B C     1 
ATOM   4448 O  O     . VAL D 2 298 ? 20.626  11.007 132.321 1.00 10.33 ? 298 VAL B O     1 
ATOM   4449 C  CB    . VAL D 2 298 ? 18.418  10.934 134.569 1.00 5.97  ? 298 VAL B CB    1 
ATOM   4450 C  CG1   . VAL D 2 298 ? 19.004  10.265 135.816 1.00 3.72  ? 298 VAL B CG1   1 
ATOM   4451 C  CG2   . VAL D 2 298 ? 17.011  11.430 134.814 1.00 5.22  ? 298 VAL B CG2   1 
ATOM   4452 N  N     . ILE D 2 299 ? 21.684  11.552 134.236 1.00 9.27  ? 299 ILE B N     1 
ATOM   4453 C  CA    . ILE D 2 299 ? 22.986  11.033 133.819 1.00 9.18  ? 299 ILE B CA    1 
ATOM   4454 C  C     . ILE D 2 299 ? 23.436  10.113 134.957 1.00 9.95  ? 299 ILE B C     1 
ATOM   4455 O  O     . ILE D 2 299 ? 23.405  10.530 136.133 1.00 11.61 ? 299 ILE B O     1 
ATOM   4456 C  CB    . ILE D 2 299 ? 24.018  12.162 133.491 1.00 7.22  ? 299 ILE B CB    1 
ATOM   4457 C  CG1   . ILE D 2 299 ? 23.553  13.008 132.286 1.00 7.93  ? 299 ILE B CG1   1 
ATOM   4458 C  CG2   . ILE D 2 299 ? 25.447  11.605 133.226 1.00 6.23  ? 299 ILE B CG2   1 
ATOM   4459 C  CD1   . ILE D 2 299 ? 24.513  14.088 131.745 1.00 5.11  ? 299 ILE B CD1   1 
ATOM   4460 N  N     . ARG D 2 300 ? 23.820  8.893  134.602 1.00 9.37  ? 300 ARG B N     1 
ATOM   4461 C  CA    . ARG D 2 300 ? 24.306  7.986  135.632 1.00 9.55  ? 300 ARG B CA    1 
ATOM   4462 C  C     . ARG D 2 300 ? 25.699  7.488  135.249 1.00 9.60  ? 300 ARG B C     1 
ATOM   4463 O  O     . ARG D 2 300 ? 25.792  6.629  134.359 1.00 9.85  ? 300 ARG B O     1 
ATOM   4464 C  CB    . ARG D 2 300 ? 23.401  6.807  135.955 1.00 10.13 ? 300 ARG B CB    1 
ATOM   4465 C  CG    . ARG D 2 300 ? 24.182  5.714  136.695 1.00 10.74 ? 300 ARG B CG    1 
ATOM   4466 C  CD    . ARG D 2 300 ? 23.497  4.419  136.646 1.00 11.32 ? 300 ARG B CD    1 
ATOM   4467 N  NE    . ARG D 2 300 ? 23.529  3.779  135.319 1.00 12.10 ? 300 ARG B NE    1 
ATOM   4468 C  CZ    . ARG D 2 300 ? 22.752  2.692  135.112 1.00 13.13 ? 300 ARG B CZ    1 
ATOM   4469 N  NH1   . ARG D 2 300 ? 21.948  2.280  136.104 1.00 13.78 ? 300 ARG B NH1   1 
ATOM   4470 N  NH2   . ARG D 2 300 ? 22.763  2.031  133.961 1.00 14.54 ? 300 ARG B NH2   1 
ATOM   4471 N  N     . VAL D 2 301 ? 26.685  8.035  135.946 1.00 9.41  ? 301 VAL B N     1 
ATOM   4472 C  CA    . VAL D 2 301 ? 28.101  7.636  135.757 1.00 8.91  ? 301 VAL B CA    1 
ATOM   4473 C  C     . VAL D 2 301 ? 28.365  6.477  136.736 1.00 9.53  ? 301 VAL B C     1 
ATOM   4474 O  O     . VAL D 2 301 ? 27.995  6.546  137.902 1.00 11.34 ? 301 VAL B O     1 
ATOM   4475 C  CB    . VAL D 2 301 ? 29.114  8.769  135.852 1.00 6.68  ? 301 VAL B CB    1 
ATOM   4476 C  CG1   . VAL D 2 301 ? 30.530  8.291  135.556 1.00 4.74  ? 301 VAL B CG1   1 
ATOM   4477 C  CG2   . VAL D 2 301 ? 28.775  9.953  134.950 1.00 5.13  ? 301 VAL B CG2   1 
ATOM   4478 N  N     . SER D 2 302 ? 28.928  5.427  136.199 1.00 9.30  ? 302 SER B N     1 
ATOM   4479 C  CA    . SER D 2 302 ? 29.212  4.223  136.998 1.00 9.28  ? 302 SER B CA    1 
ATOM   4480 C  C     . SER D 2 302 ? 30.696  3.921  136.845 1.00 9.96  ? 302 SER B C     1 
ATOM   4481 O  O     . SER D 2 302 ? 31.232  4.010  135.726 1.00 10.96 ? 302 SER B O     1 
ATOM   4482 C  CB    . SER D 2 302 ? 28.334  3.083  136.545 1.00 8.48  ? 302 SER B CB    1 
ATOM   4483 O  OG    . SER D 2 302 ? 28.371  2.009  137.475 1.00 10.93 ? 302 SER B OG    1 
ATOM   4484 N  N     . ALA D 2 303 ? 31.336  3.625  137.964 1.00 10.14 ? 303 ALA B N     1 
ATOM   4485 C  CA    . ALA D 2 303 ? 32.783  3.336  137.889 1.00 10.69 ? 303 ALA B CA    1 
ATOM   4486 C  C     . ALA D 2 303 ? 33.132  2.268  138.913 1.00 11.31 ? 303 ALA B C     1 
ATOM   4487 O  O     . ALA D 2 303 ? 32.721  2.360  140.088 1.00 11.64 ? 303 ALA B O     1 
ATOM   4488 C  CB    . ALA D 2 303 ? 33.553  4.642  138.023 1.00 8.50  ? 303 ALA B CB    1 
ATOM   4489 N  N     . PRO D 2 304 ? 33.836  1.258  138.417 1.00 11.44 ? 304 PRO B N     1 
ATOM   4490 C  CA    . PRO D 2 304 ? 34.295  0.149  139.265 1.00 12.00 ? 304 PRO B CA    1 
ATOM   4491 C  C     . PRO D 2 304 ? 35.463  0.626  140.125 1.00 12.51 ? 304 PRO B C     1 
ATOM   4492 O  O     . PRO D 2 304 ? 36.055  1.696  139.900 1.00 13.11 ? 304 PRO B O     1 
ATOM   4493 C  CB    . PRO D 2 304 ? 34.700  -0.923 138.240 1.00 11.36 ? 304 PRO B CB    1 
ATOM   4494 C  CG    . PRO D 2 304 ? 35.179  -0.142 137.047 1.00 11.34 ? 304 PRO B CG    1 
ATOM   4495 C  CD    . PRO D 2 304 ? 34.301  1.110  137.031 1.00 11.45 ? 304 PRO B CD    1 
ATOM   4496 N  N     . THR D 2 305 ? 35.798  -0.168 141.124 1.00 12.62 ? 305 THR B N     1 
ATOM   4497 C  CA    . THR D 2 305 ? 36.928  0.099  142.026 1.00 12.39 ? 305 THR B CA    1 
ATOM   4498 C  C     . THR D 2 305 ? 38.222  -0.051 141.232 1.00 13.02 ? 305 THR B C     1 
ATOM   4499 O  O     . THR D 2 305 ? 38.432  -0.995 140.448 1.00 14.88 ? 305 THR B O     1 
ATOM   4500 C  CB    . THR D 2 305 ? 36.949  -0.885 143.261 1.00 11.06 ? 305 THR B CB    1 
ATOM   4501 O  OG1   . THR D 2 305 ? 35.946  -0.387 144.193 1.00 13.97 ? 305 THR B OG1   1 
ATOM   4502 C  CG2   . THR D 2 305 ? 38.288  -1.024 143.972 1.00 8.36  ? 305 THR B CG2   1 
ATOM   4503 N  N     . GLY D 2 306 ? 39.104  0.895  141.471 1.00 12.55 ? 306 GLY B N     1 
ATOM   4504 C  CA    . GLY D 2 306 ? 40.421  0.843  140.816 1.00 12.62 ? 306 GLY B CA    1 
ATOM   4505 C  C     . GLY D 2 306 ? 40.379  1.644  139.539 1.00 13.21 ? 306 GLY B C     1 
ATOM   4506 O  O     . GLY D 2 306 ? 41.460  1.855  138.917 1.00 14.55 ? 306 GLY B O     1 
ATOM   4507 N  N     . ALA D 2 307 ? 39.206  2.099  139.162 1.00 12.15 ? 307 ALA B N     1 
ATOM   4508 C  CA    . ALA D 2 307 ? 39.140  2.878  137.903 1.00 11.10 ? 307 ALA B CA    1 
ATOM   4509 C  C     . ALA D 2 307 ? 39.367  4.352  138.175 1.00 10.44 ? 307 ALA B C     1 
ATOM   4510 O  O     . ALA D 2 307 ? 38.840  4.832  139.204 1.00 10.20 ? 307 ALA B O     1 
ATOM   4511 C  CB    . ALA D 2 307 ? 37.770  2.625  137.267 1.00 10.69 ? 307 ALA B CB    1 
ATOM   4512 N  N     . VAL D 2 308 ? 40.095  5.037  137.293 1.00 9.51  ? 308 VAL B N     1 
ATOM   4513 C  CA    . VAL D 2 308 ? 40.270  6.496  137.455 1.00 10.56 ? 308 VAL B CA    1 
ATOM   4514 C  C     . VAL D 2 308 ? 39.661  7.165  136.213 1.00 11.71 ? 308 VAL B C     1 
ATOM   4515 O  O     . VAL D 2 308 ? 40.255  7.333  135.149 1.00 12.65 ? 308 VAL B O     1 
ATOM   4516 C  CB    . VAL D 2 308 ? 41.631  6.940  137.930 1.00 10.49 ? 308 VAL B CB    1 
ATOM   4517 C  CG1   . VAL D 2 308 ? 42.686  5.847  137.869 1.00 10.97 ? 308 VAL B CG1   1 
ATOM   4518 C  CG2   . VAL D 2 308 ? 42.108  8.223  137.279 1.00 12.06 ? 308 VAL B CG2   1 
ATOM   4519 N  N     . ASN D 2 309 ? 38.389  7.514  136.429 1.00 11.75 ? 309 ASN B N     1 
ATOM   4520 C  CA    . ASN D 2 309 ? 37.454  8.145  135.520 1.00 10.97 ? 309 ASN B CA    1 
ATOM   4521 C  C     . ASN D 2 309 ? 37.317  9.646  135.821 1.00 11.31 ? 309 ASN B C     1 
ATOM   4522 O  O     . ASN D 2 309 ? 36.681  10.007 136.832 1.00 11.86 ? 309 ASN B O     1 
ATOM   4523 C  CB    . ASN D 2 309 ? 36.049  7.557  135.636 1.00 10.82 ? 309 ASN B CB    1 
ATOM   4524 C  CG    . ASN D 2 309 ? 35.721  6.244  134.991 1.00 12.24 ? 309 ASN B CG    1 
ATOM   4525 O  OD1   . ASN D 2 309 ? 36.516  5.606  134.266 1.00 12.58 ? 309 ASN B OD1   1 
ATOM   4526 N  ND2   . ASN D 2 309 ? 34.487  5.801  135.280 1.00 12.26 ? 309 ASN B ND2   1 
ATOM   4527 N  N     . SER D 2 310 ? 37.865  10.438 134.927 1.00 11.24 ? 310 SER B N     1 
ATOM   4528 C  CA    . SER D 2 310 ? 37.771  11.902 135.115 1.00 11.23 ? 310 SER B CA    1 
ATOM   4529 C  C     . SER D 2 310 ? 37.291  12.483 133.789 1.00 12.44 ? 310 SER B C     1 
ATOM   4530 O  O     . SER D 2 310 ? 37.517  11.863 132.742 1.00 13.23 ? 310 SER B O     1 
ATOM   4531 C  CB    . SER D 2 310 ? 39.024  12.523 135.642 1.00 8.90  ? 310 SER B CB    1 
ATOM   4532 O  OG    . SER D 2 310 ? 40.101  11.605 135.677 1.00 8.33  ? 310 SER B OG    1 
ATOM   4533 N  N     . ALA D 2 311 ? 36.634  13.622 133.945 1.00 12.57 ? 311 ALA B N     1 
ATOM   4534 C  CA    . ALA D 2 311 ? 36.041  14.338 132.821 1.00 12.26 ? 311 ALA B CA    1 
ATOM   4535 C  C     . ALA D 2 311 ? 35.855  15.831 133.049 1.00 12.21 ? 311 ALA B C     1 
ATOM   4536 O  O     . ALA D 2 311 ? 36.020  16.429 134.112 1.00 12.39 ? 311 ALA B O     1 
ATOM   4537 C  CB    . ALA D 2 311 ? 34.655  13.696 132.586 1.00 10.63 ? 311 ALA B CB    1 
ATOM   4538 N  N     . ILE D 2 312 ? 35.518  16.464 131.926 1.00 11.58 ? 312 ILE B N     1 
ATOM   4539 C  CA    . ILE D 2 312 ? 35.195  17.884 131.937 1.00 11.47 ? 312 ILE B CA    1 
ATOM   4540 C  C     . ILE D 2 312 ? 33.640  17.874 131.869 1.00 11.82 ? 312 ILE B C     1 
ATOM   4541 O  O     . ILE D 2 312 ? 33.085  17.354 130.875 1.00 11.98 ? 312 ILE B O     1 
ATOM   4542 C  CB    . ILE D 2 312 ? 35.800  18.784 130.830 1.00 11.28 ? 312 ILE B CB    1 
ATOM   4543 C  CG1   . ILE D 2 312 ? 37.331  18.957 130.973 1.00 11.78 ? 312 ILE B CG1   1 
ATOM   4544 C  CG2   . ILE D 2 312 ? 35.126  20.203 130.838 1.00 9.51  ? 312 ILE B CG2   1 
ATOM   4545 C  CD1   . ILE D 2 312 ? 37.734  20.137 131.931 1.00 10.98 ? 312 ILE B CD1   1 
ATOM   4546 N  N     . LEU D 2 313 ? 33.018  18.351 132.936 1.00 11.79 ? 313 LEU B N     1 
ATOM   4547 C  CA    . LEU D 2 313 ? 31.559  18.443 132.892 1.00 11.74 ? 313 LEU B CA    1 
ATOM   4548 C  C     . LEU D 2 313 ? 31.316  19.888 132.394 1.00 11.87 ? 313 LEU B C     1 
ATOM   4549 O  O     . LEU D 2 313 ? 31.934  20.817 132.928 1.00 12.02 ? 313 LEU B O     1 
ATOM   4550 C  CB    . LEU D 2 313 ? 30.876  18.071 134.186 1.00 11.67 ? 313 LEU B CB    1 
ATOM   4551 C  CG    . LEU D 2 313 ? 29.346  17.890 134.066 1.00 11.91 ? 313 LEU B CG    1 
ATOM   4552 C  CD1   . LEU D 2 313 ? 28.739  17.148 135.246 1.00 12.83 ? 313 LEU B CD1   1 
ATOM   4553 C  CD2   . LEU D 2 313 ? 28.726  19.279 133.972 1.00 12.46 ? 313 LEU B CD2   1 
ATOM   4554 N  N     . LYS D 2 314 ? 30.495  20.011 131.387 1.00 11.43 ? 314 LYS B N     1 
ATOM   4555 C  CA    . LYS D 2 314 ? 30.092  21.280 130.786 1.00 10.94 ? 314 LYS B CA    1 
ATOM   4556 C  C     . LYS D 2 314 ? 28.561  21.273 130.663 1.00 11.11 ? 314 LYS B C     1 
ATOM   4557 O  O     . LYS D 2 314 ? 28.002  20.248 130.214 1.00 13.01 ? 314 LYS B O     1 
ATOM   4558 C  CB    . LYS D 2 314 ? 30.691  21.444 129.408 1.00 9.53  ? 314 LYS B CB    1 
ATOM   4559 C  CG    . LYS D 2 314 ? 31.658  22.618 129.275 1.00 7.78  ? 314 LYS B CG    1 
ATOM   4560 C  CD    . LYS D 2 314 ? 31.930  22.933 127.805 1.00 6.29  ? 314 LYS B CD    1 
ATOM   4561 C  CE    . LYS D 2 314 ? 31.322  24.240 127.351 1.00 5.61  ? 314 LYS B CE    1 
ATOM   4562 N  NZ    . LYS D 2 314 ? 32.325  25.164 126.757 1.00 6.67  ? 314 LYS B NZ    1 
ATOM   4563 N  N     . THR D 2 315 ? 27.922  22.346 131.069 1.00 9.90  ? 315 THR B N     1 
ATOM   4564 C  CA    . THR D 2 315 ? 26.491  22.581 131.032 1.00 9.09  ? 315 THR B CA    1 
ATOM   4565 C  C     . THR D 2 315 ? 26.224  24.000 130.478 1.00 9.10  ? 315 THR B C     1 
ATOM   4566 O  O     . THR D 2 315 ? 26.933  24.960 130.793 1.00 10.33 ? 315 THR B O     1 
ATOM   4567 C  CB    . THR D 2 315 ? 25.714  22.463 132.394 1.00 8.93  ? 315 THR B CB    1 
ATOM   4568 O  OG1   . THR D 2 315 ? 26.221  21.297 133.074 1.00 10.68 ? 315 THR B OG1   1 
ATOM   4569 C  CG2   . THR D 2 315 ? 24.185  22.343 132.250 1.00 7.99  ? 315 THR B CG2   1 
ATOM   4570 N  N     . TRP D 2 316 ? 25.157  24.038 129.695 1.00 8.06  ? 316 TRP B N     1 
ATOM   4571 C  CA    . TRP D 2 316 ? 24.661  25.236 129.041 1.00 7.03  ? 316 TRP B CA    1 
ATOM   4572 C  C     . TRP D 2 316 ? 23.157  25.362 129.324 1.00 5.92  ? 316 TRP B C     1 
ATOM   4573 O  O     . TRP D 2 316 ? 22.457  24.352 129.341 1.00 4.98  ? 316 TRP B O     1 
ATOM   4574 C  CB    . TRP D 2 316 ? 24.827  25.188 127.540 1.00 9.32  ? 316 TRP B CB    1 
ATOM   4575 C  CG    . TRP D 2 316 ? 26.156  25.014 126.930 1.00 12.04 ? 316 TRP B CG    1 
ATOM   4576 C  CD1   . TRP D 2 316 ? 26.979  25.978 126.416 1.00 13.35 ? 316 TRP B CD1   1 
ATOM   4577 C  CD2   . TRP D 2 316 ? 26.836  23.760 126.704 1.00 12.95 ? 316 TRP B CD2   1 
ATOM   4578 N  NE1   . TRP D 2 316 ? 28.113  25.408 125.898 1.00 14.49 ? 316 TRP B NE1   1 
ATOM   4579 C  CE2   . TRP D 2 316 ? 28.048  24.054 126.059 1.00 13.19 ? 316 TRP B CE2   1 
ATOM   4580 C  CE3   . TRP D 2 316 ? 26.503  22.442 127.003 1.00 12.02 ? 316 TRP B CE3   1 
ATOM   4581 C  CZ2   . TRP D 2 316 ? 28.960  23.074 125.699 1.00 12.13 ? 316 TRP B CZ2   1 
ATOM   4582 C  CZ3   . TRP D 2 316 ? 27.420  21.472 126.649 1.00 11.91 ? 316 TRP B CZ3   1 
ATOM   4583 C  CH2   . TRP D 2 316 ? 28.618  21.766 126.008 1.00 11.93 ? 316 TRP B CH2   1 
ATOM   4584 N  N     . ALA D 2 317 ? 22.742  26.595 129.443 1.00 5.80  ? 317 ALA B N     1 
ATOM   4585 C  CA    . ALA D 2 317 ? 21.332  26.929 129.638 1.00 6.37  ? 317 ALA B CA    1 
ATOM   4586 C  C     . ALA D 2 317 ? 21.107  28.367 129.188 1.00 7.06  ? 317 ALA B C     1 
ATOM   4587 O  O     . ALA D 2 317 ? 21.631  29.318 129.770 1.00 7.47  ? 317 ALA B O     1 
ATOM   4588 C  CB    . ALA D 2 317 ? 20.852  26.712 131.046 1.00 5.82  ? 317 ALA B CB    1 
ATOM   4589 N  N     . CYS D 2 318 ? 20.326  28.494 128.130 1.00 7.36  ? 318 CYS B N     1 
ATOM   4590 C  CA    . CYS D 2 318 ? 20.017  29.848 127.646 1.00 7.81  ? 318 CYS B CA    1 
ATOM   4591 C  C     . CYS D 2 318 ? 18.589  30.207 128.076 1.00 8.30  ? 318 CYS B C     1 
ATOM   4592 O  O     . CYS D 2 318 ? 17.649  29.424 127.845 1.00 9.33  ? 318 CYS B O     1 
ATOM   4593 C  CB    . CYS D 2 318 ? 20.206  30.025 126.158 1.00 7.84  ? 318 CYS B CB    1 
ATOM   4594 S  SG    . CYS D 2 318 ? 19.824  31.771 125.713 1.00 14.89 ? 318 CYS B SG    1 
ATOM   4595 N  N     . LEU D 2 319 ? 18.483  31.384 128.715 1.00 7.51  ? 319 LEU B N     1 
ATOM   4596 C  CA    . LEU D 2 319 ? 17.153  31.819 129.139 1.00 7.60  ? 319 LEU B CA    1 
ATOM   4597 C  C     . LEU D 2 319 ? 16.933  33.326 128.958 1.00 8.47  ? 319 LEU B C     1 
ATOM   4598 O  O     . LEU D 2 319 ? 17.819  34.155 128.856 1.00 7.80  ? 319 LEU B O     1 
ATOM   4599 C  CB    . LEU D 2 319 ? 16.751  31.239 130.473 1.00 6.43  ? 319 LEU B CB    1 
ATOM   4600 C  CG    . LEU D 2 319 ? 17.719  31.053 131.628 1.00 4.80  ? 319 LEU B CG    1 
ATOM   4601 C  CD1   . LEU D 2 319 ? 16.944  30.895 132.942 1.00 4.05  ? 319 LEU B CD1   1 
ATOM   4602 C  CD2   . LEU D 2 319 ? 18.554  29.807 131.304 1.00 2.62  ? 319 LEU B CD2   1 
ATOM   4603 N  N     . GLU D 2 320 ? 15.636  33.583 128.887 1.00 8.75  ? 320 GLU B N     1 
ATOM   4604 C  CA    . GLU D 2 320 ? 15.012  34.875 128.760 1.00 10.23 ? 320 GLU B CA    1 
ATOM   4605 C  C     . GLU D 2 320 ? 14.397  35.264 130.106 1.00 10.35 ? 320 GLU B C     1 
ATOM   4606 O  O     . GLU D 2 320 ? 13.493  34.580 130.612 1.00 11.12 ? 320 GLU B O     1 
ATOM   4607 C  CB    . GLU D 2 320 ? 13.849  34.838 127.769 1.00 12.17 ? 320 GLU B CB    1 
ATOM   4608 C  CG    . GLU D 2 320 ? 14.297  35.103 126.335 1.00 17.48 ? 320 GLU B CG    1 
ATOM   4609 C  CD    . GLU D 2 320 ? 13.144  35.516 125.437 1.00 21.94 ? 320 GLU B CD    1 
ATOM   4610 O  OE1   . GLU D 2 320 ? 11.937  35.394 125.864 1.00 24.52 ? 320 GLU B OE1   1 
ATOM   4611 O  OE2   . GLU D 2 320 ? 13.379  35.983 124.262 1.00 24.96 ? 320 GLU B OE2   1 
ATOM   4612 N  N     . TYR D 2 321 ? 14.901  36.347 130.655 1.00 9.74  ? 321 TYR B N     1 
ATOM   4613 C  CA    . TYR D 2 321 ? 14.416  36.879 131.936 1.00 9.13  ? 321 TYR B CA    1 
ATOM   4614 C  C     . TYR D 2 321 ? 13.681  38.186 131.728 1.00 9.53  ? 321 TYR B C     1 
ATOM   4615 O  O     . TYR D 2 321 ? 14.007  38.965 130.822 1.00 9.91  ? 321 TYR B O     1 
ATOM   4616 C  CB    . TYR D 2 321 ? 15.569  37.235 132.875 1.00 7.87  ? 321 TYR B CB    1 
ATOM   4617 C  CG    . TYR D 2 321 ? 16.212  36.039 133.564 1.00 8.34  ? 321 TYR B CG    1 
ATOM   4618 C  CD1   . TYR D 2 321 ? 15.604  35.457 134.684 1.00 8.23  ? 321 TYR B CD1   1 
ATOM   4619 C  CD2   . TYR D 2 321 ? 17.418  35.539 133.074 1.00 8.61  ? 321 TYR B CD2   1 
ATOM   4620 C  CE1   . TYR D 2 321 ? 16.212  34.366 135.315 1.00 7.34  ? 321 TYR B CE1   1 
ATOM   4621 C  CE2   . TYR D 2 321 ? 18.026  34.449 133.705 1.00 8.54  ? 321 TYR B CE2   1 
ATOM   4622 C  CZ    . TYR D 2 321 ? 17.424  33.863 134.825 1.00 8.24  ? 321 TYR B CZ    1 
ATOM   4623 O  OH    . TYR D 2 321 ? 18.018  32.805 135.436 1.00 9.77  ? 321 TYR B OH    1 
ATOM   4624 N  N     . ARG D 2 322 ? 12.711  38.389 132.578 1.00 8.82  ? 322 ARG B N     1 
ATOM   4625 C  CA    . ARG D 2 322 ? 11.961  39.632 132.596 1.00 8.21  ? 322 ARG B CA    1 
ATOM   4626 C  C     . ARG D 2 322 ? 12.651  40.541 133.603 1.00 8.33  ? 322 ARG B C     1 
ATOM   4627 O  O     . ARG D 2 322 ? 12.499  40.368 134.823 1.00 8.71  ? 322 ARG B O     1 
ATOM   4628 C  CB    . ARG D 2 322 ? 10.509  39.357 132.958 1.00 6.20  ? 322 ARG B CB    1 
ATOM   4629 C  CG    . ARG D 2 322 ? 9.712   38.795 131.777 1.00 8.97  ? 322 ARG B CG    1 
ATOM   4630 C  CD    . ARG D 2 322 ? 9.427   39.838 130.694 1.00 8.39  ? 322 ARG B CD    1 
ATOM   4631 N  NE    . ARG D 2 322 ? 8.070   40.387 130.786 1.00 9.02  ? 322 ARG B NE    1 
ATOM   4632 C  CZ    . ARG D 2 322 ? 7.796   41.677 131.008 1.00 10.03 ? 322 ARG B CZ    1 
ATOM   4633 N  NH1   . ARG D 2 322 ? 8.779   42.576 131.154 1.00 9.82  ? 322 ARG B NH1   1 
ATOM   4634 N  NH2   . ARG D 2 322 ? 6.555   42.172 131.104 1.00 10.03 ? 322 ARG B NH2   1 
ATOM   4635 N  N     . PRO D 2 323 ? 13.446  41.499 133.126 1.00 8.41  ? 323 PRO B N     1 
ATOM   4636 C  CA    . PRO D 2 323 ? 14.175  42.403 133.995 1.00 8.57  ? 323 PRO B CA    1 
ATOM   4637 C  C     . PRO D 2 323 ? 13.254  43.305 134.771 1.00 9.22  ? 323 PRO B C     1 
ATOM   4638 O  O     . PRO D 2 323 ? 12.209  43.748 134.208 1.00 9.77  ? 323 PRO B O     1 
ATOM   4639 C  CB    . PRO D 2 323 ? 14.975  43.261 133.045 1.00 8.46  ? 323 PRO B CB    1 
ATOM   4640 C  CG    . PRO D 2 323 ? 14.624  42.837 131.628 1.00 8.39  ? 323 PRO B CG    1 
ATOM   4641 C  CD    . PRO D 2 323 ? 13.636  41.717 131.692 1.00 8.48  ? 323 PRO B CD    1 
ATOM   4642 N  N     . ASN D 2 324 ? 13.641  43.558 136.010 1.00 9.84  ? 324 ASN B N     1 
ATOM   4643 C  CA    . ASN D 2 324 ? 12.943  44.524 136.880 1.00 9.91  ? 324 ASN B CA    1 
ATOM   4644 C  C     . ASN D 2 324 ? 13.615  45.885 136.618 1.00 9.42  ? 324 ASN B C     1 
ATOM   4645 O  O     . ASN D 2 324 ? 14.858  45.914 136.647 1.00 9.22  ? 324 ASN B O     1 
ATOM   4646 C  CB    . ASN D 2 324 ? 13.112  44.126 138.347 1.00 9.54  ? 324 ASN B CB    1 
ATOM   4647 C  CG    . ASN D 2 324 ? 12.092  43.088 138.811 1.00 9.43  ? 324 ASN B CG    1 
ATOM   4648 O  OD1   . ASN D 2 324 ? 12.467  42.092 139.427 1.00 9.73  ? 324 ASN B OD1   1 
ATOM   4649 N  ND2   . ASN D 2 324 ? 10.811  43.261 138.549 1.00 9.56  ? 324 ASN B ND2   1 
ATOM   4650 N  N     . PRO D 2 325 ? 12.818  46.896 136.396 1.00 9.30  ? 325 PRO B N     1 
ATOM   4651 C  CA    . PRO D 2 325 ? 13.325  48.240 136.111 1.00 10.19 ? 325 PRO B CA    1 
ATOM   4652 C  C     . PRO D 2 325 ? 14.294  48.765 137.147 1.00 11.30 ? 325 PRO B C     1 
ATOM   4653 O  O     . PRO D 2 325 ? 15.131  49.654 136.813 1.00 13.63 ? 325 PRO B O     1 
ATOM   4654 C  CB    . PRO D 2 325 ? 12.099  49.089 135.856 1.00 9.70  ? 325 PRO B CB    1 
ATOM   4655 C  CG    . PRO D 2 325 ? 10.967  48.323 136.474 1.00 9.55  ? 325 PRO B CG    1 
ATOM   4656 C  CD    . PRO D 2 325 ? 11.353  46.847 136.340 1.00 9.46  ? 325 PRO B CD    1 
ATOM   4657 N  N     . ASN D 2 326 ? 14.246  48.240 138.347 1.00 10.86 ? 326 ASN B N     1 
ATOM   4658 C  CA    . ASN D 2 326 ? 15.151  48.636 139.421 1.00 10.28 ? 326 ASN B CA    1 
ATOM   4659 C  C     . ASN D 2 326 ? 16.498  47.898 139.346 1.00 11.12 ? 326 ASN B C     1 
ATOM   4660 O  O     . ASN D 2 326 ? 17.466  48.428 139.927 1.00 11.59 ? 326 ASN B O     1 
ATOM   4661 C  CB    . ASN D 2 326 ? 14.535  48.318 140.790 1.00 9.94  ? 326 ASN B CB    1 
ATOM   4662 C  CG    . ASN D 2 326 ? 14.375  46.809 140.956 1.00 10.87 ? 326 ASN B CG    1 
ATOM   4663 O  OD1   . ASN D 2 326 ? 15.026  46.175 141.794 1.00 12.30 ? 326 ASN B OD1   1 
ATOM   4664 N  ND2   . ASN D 2 326 ? 13.487  46.235 140.137 1.00 11.24 ? 326 ASN B ND2   1 
ATOM   4665 N  N     . ALA D 2 327 ? 16.519  46.739 138.741 1.00 11.82 ? 327 ALA B N     1 
ATOM   4666 C  CA    . ALA D 2 327 ? 17.690  45.873 138.601 1.00 12.20 ? 327 ALA B CA    1 
ATOM   4667 C  C     . ALA D 2 327 ? 18.772  46.566 137.795 1.00 12.91 ? 327 ALA B C     1 
ATOM   4668 O  O     . ALA D 2 327 ? 18.404  47.339 136.887 1.00 14.02 ? 327 ALA B O     1 
ATOM   4669 C  CB    . ALA D 2 327 ? 17.262  44.586 137.902 1.00 11.74 ? 327 ALA B CB    1 
ATOM   4670 N  N     . MET D 2 328 ? 20.027  46.278 138.099 1.00 12.76 ? 328 MET B N     1 
ATOM   4671 C  CA    . MET D 2 328 ? 21.131  46.916 137.370 1.00 13.10 ? 328 MET B CA    1 
ATOM   4672 C  C     . MET D 2 328 ? 21.507  46.173 136.094 1.00 13.40 ? 328 MET B C     1 
ATOM   4673 O  O     . MET D 2 328 ? 22.380  46.683 135.331 1.00 14.76 ? 328 MET B O     1 
ATOM   4674 C  CB    . MET D 2 328 ? 22.337  47.234 138.234 1.00 15.96 ? 328 MET B CB    1 
ATOM   4675 C  CG    . MET D 2 328 ? 22.140  48.474 139.086 1.00 19.98 ? 328 MET B CG    1 
ATOM   4676 S  SD    . MET D 2 328 ? 22.242  49.972 138.026 1.00 23.97 ? 328 MET B SD    1 
ATOM   4677 C  CE    . MET D 2 328 ? 20.585  50.665 138.403 1.00 22.68 ? 328 MET B CE    1 
ATOM   4678 N  N     . LEU D 2 329 ? 20.866  45.045 135.863 1.00 12.57 ? 329 LEU B N     1 
ATOM   4679 C  CA    . LEU D 2 329 ? 21.129  44.229 134.641 1.00 10.74 ? 329 LEU B CA    1 
ATOM   4680 C  C     . LEU D 2 329 ? 20.156  44.624 133.543 1.00 10.47 ? 329 LEU B C     1 
ATOM   4681 O  O     . LEU D 2 329 ? 20.132  44.139 132.417 1.00 10.92 ? 329 LEU B O     1 
ATOM   4682 C  CB    . LEU D 2 329 ? 21.034  42.757 135.069 1.00 9.20  ? 329 LEU B CB    1 
ATOM   4683 C  CG    . LEU D 2 329 ? 19.760  41.955 135.044 1.00 10.26 ? 329 LEU B CG    1 
ATOM   4684 C  CD1   . LEU D 2 329 ? 19.804  40.737 135.973 1.00 7.80  ? 329 LEU B CD1   1 
ATOM   4685 C  CD2   . LEU D 2 329 ? 18.586  42.832 135.467 1.00 13.26 ? 329 LEU B CD2   1 
ATOM   4686 N  N     . TYR D 2 330 ? 19.272  45.528 133.905 1.00 9.35  ? 330 TYR B N     1 
ATOM   4687 C  CA    . TYR D 2 330 ? 18.211  45.964 133.000 1.00 8.87  ? 330 TYR B CA    1 
ATOM   4688 C  C     . TYR D 2 330 ? 18.735  46.604 131.737 1.00 9.34  ? 330 TYR B C     1 
ATOM   4689 O  O     . TYR D 2 330 ? 18.175  46.356 130.656 1.00 9.16  ? 330 TYR B O     1 
ATOM   4690 C  CB    . TYR D 2 330 ? 17.250  46.898 133.779 1.00 7.23  ? 330 TYR B CB    1 
ATOM   4691 C  CG    . TYR D 2 330 ? 16.021  47.226 132.983 1.00 6.29  ? 330 TYR B CG    1 
ATOM   4692 C  CD1   . TYR D 2 330 ? 16.083  48.191 131.986 1.00 5.47  ? 330 TYR B CD1   1 
ATOM   4693 C  CD2   . TYR D 2 330 ? 14.816  46.576 133.190 1.00 8.88  ? 330 TYR B CD2   1 
ATOM   4694 C  CE1   . TYR D 2 330 ? 14.976  48.526 131.208 1.00 6.62  ? 330 TYR B CE1   1 
ATOM   4695 C  CE2   . TYR D 2 330 ? 13.693  46.899 132.427 1.00 10.58 ? 330 TYR B CE2   1 
ATOM   4696 C  CZ    . TYR D 2 330 ? 13.782  47.871 131.444 1.00 9.08  ? 330 TYR B CZ    1 
ATOM   4697 O  OH    . TYR D 2 330 ? 12.712  48.221 130.686 1.00 12.29 ? 330 TYR B OH    1 
ATOM   4698 N  N     . GLN D 2 331 ? 19.751  47.440 131.886 1.00 10.00 ? 331 GLN B N     1 
ATOM   4699 C  CA    . GLN D 2 331 ? 20.307  48.191 130.749 1.00 11.32 ? 331 GLN B CA    1 
ATOM   4700 C  C     . GLN D 2 331 ? 21.075  47.328 129.765 1.00 11.76 ? 331 GLN B C     1 
ATOM   4701 O  O     . GLN D 2 331 ? 21.691  47.846 128.818 1.00 14.33 ? 331 GLN B O     1 
ATOM   4702 C  CB    . GLN D 2 331 ? 21.078  49.412 131.246 1.00 10.74 ? 331 GLN B CB    1 
ATOM   4703 C  CG    . GLN D 2 331 ? 21.745  49.127 132.586 1.00 13.20 ? 331 GLN B CG    1 
ATOM   4704 C  CD    . GLN D 2 331 ? 20.872  49.504 133.746 1.00 14.03 ? 331 GLN B CD    1 
ATOM   4705 O  OE1   . GLN D 2 331 ? 20.998  49.079 134.885 1.00 13.68 ? 331 GLN B OE1   1 
ATOM   4706 N  NE2   . GLN D 2 331 ? 19.922  50.369 133.400 1.00 15.61 ? 331 GLN B NE2   1 
ATOM   4707 N  N     . PHE D 2 332 ? 21.047  46.034 129.985 1.00 10.44 ? 332 PHE B N     1 
ATOM   4708 C  CA    . PHE D 2 332 ? 21.657  45.005 129.159 1.00 9.28  ? 332 PHE B CA    1 
ATOM   4709 C  C     . PHE D 2 332 ? 20.466  44.319 128.448 1.00 8.90  ? 332 PHE B C     1 
ATOM   4710 O  O     . PHE D 2 332 ? 20.672  43.370 127.686 1.00 10.63 ? 332 PHE B O     1 
ATOM   4711 C  CB    . PHE D 2 332 ? 22.427  43.940 129.920 1.00 8.39  ? 332 PHE B CB    1 
ATOM   4712 C  CG    . PHE D 2 332 ? 23.641  44.328 130.677 1.00 10.62 ? 332 PHE B CG    1 
ATOM   4713 C  CD1   . PHE D 2 332 ? 24.667  45.052 130.063 1.00 11.49 ? 332 PHE B CD1   1 
ATOM   4714 C  CD2   . PHE D 2 332 ? 23.793  43.980 132.020 1.00 10.95 ? 332 PHE B CD2   1 
ATOM   4715 C  CE1   . PHE D 2 332 ? 25.808  45.446 130.743 1.00 10.63 ? 332 PHE B CE1   1 
ATOM   4716 C  CE2   . PHE D 2 332 ? 24.926  44.365 132.727 1.00 12.71 ? 332 PHE B CE2   1 
ATOM   4717 C  CZ    . PHE D 2 332 ? 25.922  45.101 132.079 1.00 12.20 ? 332 PHE B CZ    1 
ATOM   4718 N  N     . GLY D 2 333 ? 19.274  44.762 128.761 1.00 6.68  ? 333 GLY B N     1 
ATOM   4719 C  CA    . GLY D 2 333 ? 18.032  44.175 128.244 1.00 6.02  ? 333 GLY B CA    1 
ATOM   4720 C  C     . GLY D 2 333 ? 17.864  44.412 126.755 1.00 6.39  ? 333 GLY B C     1 
ATOM   4721 O  O     . GLY D 2 333 ? 18.665  45.130 126.167 1.00 6.81  ? 333 GLY B O     1 
ATOM   4722 N  N     . HIS D 2 334 ? 16.831  43.797 126.228 1.00 6.02  ? 334 HIS B N     1 
ATOM   4723 C  CA    . HIS D 2 334 ? 16.412  43.848 124.819 1.00 6.26  ? 334 HIS B CA    1 
ATOM   4724 C  C     . HIS D 2 334 ? 14.988  43.349 124.646 1.00 6.90  ? 334 HIS B C     1 
ATOM   4725 O  O     . HIS D 2 334 ? 14.376  42.935 125.663 1.00 8.16  ? 334 HIS B O     1 
ATOM   4726 C  CB    . HIS D 2 334 ? 17.351  43.051 123.915 1.00 6.73  ? 334 HIS B CB    1 
ATOM   4727 C  CG    . HIS D 2 334 ? 17.346  41.578 123.959 1.00 8.07  ? 334 HIS B CG    1 
ATOM   4728 N  ND1   . HIS D 2 334 ? 16.404  40.786 123.350 1.00 8.51  ? 334 HIS B ND1   1 
ATOM   4729 C  CD2   . HIS D 2 334 ? 18.250  40.722 124.491 1.00 7.99  ? 334 HIS B CD2   1 
ATOM   4730 C  CE1   . HIS D 2 334 ? 16.716  39.501 123.525 1.00 8.51  ? 334 HIS B CE1   1 
ATOM   4731 N  NE2   . HIS D 2 334 ? 17.832  39.440 124.225 1.00 8.78  ? 334 HIS B NE2   1 
ATOM   4732 N  N     . ASP D 2 335 ? 14.465  43.343 123.436 1.00 6.50  ? 335 ASP B N     1 
ATOM   4733 C  CA    . ASP D 2 335 ? 13.099  42.838 123.151 1.00 7.51  ? 335 ASP B CA    1 
ATOM   4734 C  C     . ASP D 2 335 ? 13.109  41.380 122.684 1.00 8.00  ? 335 ASP B C     1 
ATOM   4735 O  O     . ASP D 2 335 ? 13.912  41.124 121.735 1.00 9.17  ? 335 ASP B O     1 
ATOM   4736 C  CB    . ASP D 2 335 ? 12.517  43.651 121.984 1.00 9.87  ? 335 ASP B CB    1 
ATOM   4737 C  CG    . ASP D 2 335 ? 12.300  45.104 122.272 1.00 13.11 ? 335 ASP B CG    1 
ATOM   4738 O  OD1   . ASP D 2 335 ? 12.031  45.343 123.469 1.00 16.77 ? 335 ASP B OD1   1 
ATOM   4739 O  OD2   . ASP D 2 335 ? 12.378  45.969 121.392 1.00 10.56 ? 335 ASP B OD2   1 
ATOM   4740 N  N     . SER D 2 336 ? 12.267  40.488 123.171 1.00 7.62  ? 336 SER B N     1 
ATOM   4741 C  CA    . SER D 2 336 ? 12.301  39.111 122.564 1.00 8.00  ? 336 SER B CA    1 
ATOM   4742 C  C     . SER D 2 336 ? 12.044  39.324 121.060 1.00 8.90  ? 336 SER B C     1 
ATOM   4743 O  O     . SER D 2 336 ? 11.248  40.271 120.721 1.00 10.48 ? 336 SER B O     1 
ATOM   4744 C  CB    . SER D 2 336 ? 11.209  38.208 123.114 1.00 6.10  ? 336 SER B CB    1 
ATOM   4745 N  N     . PRO D 2 337 ? 12.645  38.518 120.206 1.00 8.69  ? 337 PRO B N     1 
ATOM   4746 C  CA    . PRO D 2 337 ? 12.432  38.666 118.755 1.00 8.39  ? 337 PRO B CA    1 
ATOM   4747 C  C     . PRO D 2 337 ? 11.045  38.193 118.329 1.00 8.36  ? 337 PRO B C     1 
ATOM   4748 O  O     . PRO D 2 337 ? 10.380  37.348 118.986 1.00 9.38  ? 337 PRO B O     1 
ATOM   4749 C  CB    . PRO D 2 337 ? 13.544  37.840 118.140 1.00 8.82  ? 337 PRO B CB    1 
ATOM   4750 C  CG    . PRO D 2 337 ? 13.820  36.758 119.167 1.00 8.94  ? 337 PRO B CG    1 
ATOM   4751 C  CD    . PRO D 2 337 ? 13.578  37.430 120.511 1.00 9.11  ? 337 PRO B CD    1 
ATOM   4752 N  N     . PRO D 2 338 ? 10.614  38.746 117.198 1.00 8.01  ? 338 PRO B N     1 
ATOM   4753 C  CA    . PRO D 2 338 ? 9.338   38.469 116.562 1.00 7.82  ? 338 PRO B CA    1 
ATOM   4754 C  C     . PRO D 2 338 ? 9.151   37.031 116.105 1.00 8.87  ? 338 PRO B C     1 
ATOM   4755 O  O     . PRO D 2 338 ? 10.107  36.307 115.806 1.00 10.38 ? 338 PRO B O     1 
ATOM   4756 C  CB    . PRO D 2 338 ? 9.281   39.381 115.334 1.00 6.63  ? 338 PRO B CB    1 
ATOM   4757 C  CG    . PRO D 2 338 ? 10.566  40.091 115.247 1.00 6.46  ? 338 PRO B CG    1 
ATOM   4758 C  CD    . PRO D 2 338 ? 11.399  39.746 116.453 1.00 7.21  ? 338 PRO B CD    1 
ATOM   4759 N  N     . CYS D 2 339 ? 7.882   36.651 115.968 1.00 9.45  ? 339 CYS B N     1 
ATOM   4760 C  CA    . CYS D 2 339 ? 7.485   35.310 115.566 1.00 9.39  ? 339 CYS B CA    1 
ATOM   4761 C  C     . CYS D 2 339 ? 8.222   34.786 114.350 1.00 10.28 ? 339 CYS B C     1 
ATOM   4762 O  O     . CYS D 2 339 ? 8.252   35.434 113.297 1.00 11.07 ? 339 CYS B O     1 
ATOM   4763 C  CB    . CYS D 2 339 ? 5.972   35.167 115.315 1.00 8.13  ? 339 CYS B CB    1 
ATOM   4764 S  SG    . CYS D 2 339 ? 5.426   33.449 115.624 1.00 11.95 ? 339 CYS B SG    1 
ATOM   4765 N  N     . ASP D 2 340 ? 8.757   33.599 114.528 1.00 10.56 ? 340 ASP B N     1 
ATOM   4766 C  CA    . ASP D 2 340 ? 9.458   32.917 113.408 1.00 10.86 ? 340 ASP B CA    1 
ATOM   4767 C  C     . ASP D 2 340 ? 8.850   31.509 113.326 1.00 12.22 ? 340 ASP B C     1 
ATOM   4768 O  O     . ASP D 2 340 ? 9.299   30.507 113.897 1.00 12.74 ? 340 ASP B O     1 
ATOM   4769 C  CB    . ASP D 2 340 ? 10.953  32.970 113.589 1.00 9.77  ? 340 ASP B CB    1 
ATOM   4770 C  CG    . ASP D 2 340 ? 11.615  31.956 112.665 1.00 11.03 ? 340 ASP B CG    1 
ATOM   4771 O  OD1   . ASP D 2 340 ? 10.810  31.225 112.047 1.00 10.34 ? 340 ASP B OD1   1 
ATOM   4772 O  OD2   . ASP D 2 340 ? 12.851  31.899 112.586 1.00 12.72 ? 340 ASP B OD2   1 
ATOM   4773 N  N     . GLU D 2 341 ? 7.748   31.500 112.614 1.00 12.58 ? 341 GLU B N     1 
ATOM   4774 C  CA    . GLU D 2 341 ? 6.928   30.338 112.361 1.00 12.81 ? 341 GLU B CA    1 
ATOM   4775 C  C     . GLU D 2 341 ? 7.703   29.108 111.917 1.00 13.37 ? 341 GLU B C     1 
ATOM   4776 O  O     . GLU D 2 341 ? 7.381   27.982 112.326 1.00 14.89 ? 341 GLU B O     1 
ATOM   4777 C  CB    . GLU D 2 341 ? 5.906   30.678 111.253 1.00 12.79 ? 341 GLU B CB    1 
ATOM   4778 C  CG    . GLU D 2 341 ? 4.909   29.537 111.017 1.00 17.68 ? 341 GLU B CG    1 
ATOM   4779 C  CD    . GLU D 2 341 ? 4.399   28.940 112.316 1.00 24.04 ? 341 GLU B CD    1 
ATOM   4780 O  OE1   . GLU D 2 341 ? 4.915   29.050 113.414 1.00 26.97 ? 341 GLU B OE1   1 
ATOM   4781 O  OE2   . GLU D 2 341 ? 3.335   28.300 112.096 1.00 27.04 ? 341 GLU B OE2   1 
ATOM   4782 N  N     . VAL D 2 342 ? 8.687   29.325 111.067 1.00 12.36 ? 342 VAL B N     1 
ATOM   4783 C  CA    . VAL D 2 342 ? 9.552   28.285 110.507 1.00 11.03 ? 342 VAL B CA    1 
ATOM   4784 C  C     . VAL D 2 342 ? 10.517  27.739 111.561 1.00 11.52 ? 342 VAL B C     1 
ATOM   4785 O  O     . VAL D 2 342 ? 10.670  26.499 111.652 1.00 12.87 ? 342 VAL B O     1 
ATOM   4786 C  CB    . VAL D 2 342 ? 10.263  28.771 109.235 1.00 8.53  ? 342 VAL B CB    1 
ATOM   4787 C  CG1   . VAL D 2 342 ? 11.398  27.877 108.754 1.00 5.77  ? 342 VAL B CG1   1 
ATOM   4788 C  CG2   . VAL D 2 342 ? 9.285   28.979 108.084 1.00 8.53  ? 342 VAL B CG2   1 
ATOM   4789 N  N     . ALA D 2 343 ? 11.166  28.607 112.300 1.00 11.11 ? 343 ALA B N     1 
ATOM   4790 C  CA    . ALA D 2 343 ? 12.101  28.232 113.361 1.00 10.24 ? 343 ALA B CA    1 
ATOM   4791 C  C     . ALA D 2 343 ? 11.341  27.396 114.397 1.00 9.71  ? 343 ALA B C     1 
ATOM   4792 O  O     . ALA D 2 343 ? 11.743  26.325 114.851 1.00 9.19  ? 343 ALA B O     1 
ATOM   4793 C  CB    . ALA D 2 343 ? 12.697  29.468 114.047 1.00 9.57  ? 343 ALA B CB    1 
ATOM   4794 N  N     . LEU D 2 344 ? 10.194  27.919 114.770 1.00 9.78  ? 344 LEU B N     1 
ATOM   4795 C  CA    . LEU D 2 344 ? 9.315   27.299 115.775 1.00 11.29 ? 344 LEU B CA    1 
ATOM   4796 C  C     . LEU D 2 344 ? 8.919   25.880 115.386 1.00 12.41 ? 344 LEU B C     1 
ATOM   4797 O  O     . LEU D 2 344 ? 8.792   25.024 116.283 1.00 13.33 ? 344 LEU B O     1 
ATOM   4798 C  CB    . LEU D 2 344 ? 8.154   28.253 116.067 1.00 9.95  ? 344 LEU B CB    1 
ATOM   4799 C  CG    . LEU D 2 344 ? 8.388   29.486 116.922 1.00 8.70  ? 344 LEU B CG    1 
ATOM   4800 C  CD1   . LEU D 2 344 ? 7.056   30.129 117.318 1.00 9.28  ? 344 LEU B CD1   1 
ATOM   4801 C  CD2   . LEU D 2 344 ? 9.189   29.108 118.149 1.00 7.63  ? 344 LEU B CD2   1 
ATOM   4802 N  N     . GLN D 2 345 ? 8.716   25.644 114.096 1.00 12.91 ? 345 GLN B N     1 
ATOM   4803 C  CA    . GLN D 2 345 ? 8.342   24.341 113.576 1.00 11.89 ? 345 GLN B CA    1 
ATOM   4804 C  C     . GLN D 2 345 ? 9.573   23.444 113.479 1.00 10.44 ? 345 GLN B C     1 
ATOM   4805 O  O     . GLN D 2 345 ? 9.541   22.354 114.061 1.00 10.90 ? 345 GLN B O     1 
ATOM   4806 C  CB    . GLN D 2 345 ? 7.608   24.311 112.246 1.00 16.05 ? 345 GLN B CB    1 
ATOM   4807 C  CG    . GLN D 2 345 ? 6.811   22.998 112.122 1.00 20.51 ? 345 GLN B CG    1 
ATOM   4808 C  CD    . GLN D 2 345 ? 6.012   22.765 113.405 1.00 24.73 ? 345 GLN B CD    1 
ATOM   4809 O  OE1   . GLN D 2 345 ? 5.059   23.510 113.704 1.00 27.80 ? 345 GLN B OE1   1 
ATOM   4810 N  NE2   . GLN D 2 345 ? 6.415   21.746 114.178 1.00 25.73 ? 345 GLN B NE2   1 
ATOM   4811 N  N     . GLU D 2 346 ? 10.567  23.941 112.784 1.00 9.04  ? 346 GLU B N     1 
ATOM   4812 C  CA    . GLU D 2 346 ? 11.838  23.252 112.576 1.00 8.52  ? 346 GLU B CA    1 
ATOM   4813 C  C     . GLU D 2 346 ? 12.462  22.851 113.910 1.00 8.72  ? 346 GLU B C     1 
ATOM   4814 O  O     . GLU D 2 346 ? 13.355  21.990 113.878 1.00 8.66  ? 346 GLU B O     1 
ATOM   4815 C  CB    . GLU D 2 346 ? 12.908  24.170 111.951 1.00 9.13  ? 346 GLU B CB    1 
ATOM   4816 C  CG    . GLU D 2 346 ? 13.013  24.111 110.426 1.00 11.66 ? 346 GLU B CG    1 
ATOM   4817 C  CD    . GLU D 2 346 ? 12.470  22.772 109.961 1.00 17.15 ? 346 GLU B CD    1 
ATOM   4818 O  OE1   . GLU D 2 346 ? 13.385  21.916 109.980 1.00 20.48 ? 346 GLU B OE1   1 
ATOM   4819 O  OE2   . GLU D 2 346 ? 11.303  22.591 109.673 1.00 16.92 ? 346 GLU B OE2   1 
ATOM   4820 N  N     . TYR D 2 347 ? 12.029  23.510 114.967 1.00 8.67  ? 347 TYR B N     1 
ATOM   4821 C  CA    . TYR D 2 347 ? 12.588  23.292 116.310 1.00 8.56  ? 347 TYR B CA    1 
ATOM   4822 C  C     . TYR D 2 347 ? 12.089  21.986 116.908 1.00 9.14  ? 347 TYR B C     1 
ATOM   4823 O  O     . TYR D 2 347 ? 12.794  21.176 117.521 1.00 9.41  ? 347 TYR B O     1 
ATOM   4824 C  CB    . TYR D 2 347 ? 12.230  24.474 117.217 1.00 7.18  ? 347 TYR B CB    1 
ATOM   4825 C  CG    . TYR D 2 347 ? 12.377  24.270 118.704 1.00 7.30  ? 347 TYR B CG    1 
ATOM   4826 C  CD1   . TYR D 2 347 ? 13.580  24.573 119.347 1.00 7.36  ? 347 TYR B CD1   1 
ATOM   4827 C  CD2   . TYR D 2 347 ? 11.332  23.808 119.489 1.00 6.75  ? 347 TYR B CD2   1 
ATOM   4828 C  CE1   . TYR D 2 347 ? 13.731  24.404 120.711 1.00 9.58  ? 347 TYR B CE1   1 
ATOM   4829 C  CE2   . TYR D 2 347 ? 11.461  23.630 120.865 1.00 8.05  ? 347 TYR B CE2   1 
ATOM   4830 C  CZ    . TYR D 2 347 ? 12.662  23.924 121.475 1.00 10.53 ? 347 TYR B CZ    1 
ATOM   4831 O  OH    . TYR D 2 347 ? 12.794  23.759 122.836 1.00 12.86 ? 347 TYR B OH    1 
ATOM   4832 N  N     . ARG D 2 348 ? 10.799  21.842 116.695 1.00 9.27  ? 348 ARG B N     1 
ATOM   4833 C  CA    . ARG D 2 348 ? 10.021  20.696 117.158 1.00 9.28  ? 348 ARG B CA    1 
ATOM   4834 C  C     . ARG D 2 348 ? 10.380  19.432 116.404 1.00 9.85  ? 348 ARG B C     1 
ATOM   4835 O  O     . ARG D 2 348 ? 10.441  18.361 117.040 1.00 10.01 ? 348 ARG B O     1 
ATOM   4836 C  CB    . ARG D 2 348 ? 8.538   21.054 117.041 1.00 6.63  ? 348 ARG B CB    1 
ATOM   4837 C  CG    . ARG D 2 348 ? 7.800   21.096 118.342 1.00 9.24  ? 348 ARG B CG    1 
ATOM   4838 C  CD    . ARG D 2 348 ? 8.086   22.218 119.266 1.00 10.43 ? 348 ARG B CD    1 
ATOM   4839 N  NE    . ARG D 2 348 ? 7.841   21.795 120.671 1.00 9.78  ? 348 ARG B NE    1 
ATOM   4840 C  CZ    . ARG D 2 348 ? 7.511   22.666 121.628 1.00 7.58  ? 348 ARG B CZ    1 
ATOM   4841 N  NH1   . ARG D 2 348 ? 7.464   23.964 121.286 1.00 7.29  ? 348 ARG B NH1   1 
ATOM   4842 N  NH2   . ARG D 2 348 ? 7.255   22.310 122.870 1.00 7.00  ? 348 ARG B NH2   1 
ATOM   4843 N  N     . THR D 2 349 ? 10.609  19.545 115.101 1.00 10.16 ? 349 THR B N     1 
ATOM   4844 C  CA    . THR D 2 349 ? 10.915  18.323 114.319 1.00 10.82 ? 349 THR B CA    1 
ATOM   4845 C  C     . THR D 2 349 ? 12.352  17.899 114.511 1.00 10.42 ? 349 THR B C     1 
ATOM   4846 O  O     . THR D 2 349 ? 12.604  16.680 114.571 1.00 11.36 ? 349 THR B O     1 
ATOM   4847 C  CB    . THR D 2 349 ? 10.421  18.344 112.831 1.00 11.91 ? 349 THR B CB    1 
ATOM   4848 O  OG1   . THR D 2 349 ? 11.518  18.885 112.037 1.00 11.37 ? 349 THR B OG1   1 
ATOM   4849 C  CG2   . THR D 2 349 ? 9.091   19.101 112.622 1.00 12.61 ? 349 THR B CG2   1 
ATOM   4850 N  N     . VAL D 2 350 ? 13.236  18.868 114.644 1.00 9.86  ? 350 VAL B N     1 
ATOM   4851 C  CA    . VAL D 2 350 ? 14.664  18.566 114.896 1.00 9.16  ? 350 VAL B CA    1 
ATOM   4852 C  C     . VAL D 2 350 ? 14.758  17.885 116.273 1.00 10.00 ? 350 VAL B C     1 
ATOM   4853 O  O     . VAL D 2 350 ? 15.525  16.938 116.510 1.00 9.81  ? 350 VAL B O     1 
ATOM   4854 C  CB    . VAL D 2 350 ? 15.478  19.861 114.783 1.00 6.21  ? 350 VAL B CB    1 
ATOM   4855 C  CG1   . VAL D 2 350 ? 16.815  19.808 115.518 1.00 6.45  ? 350 VAL B CG1   1 
ATOM   4856 C  CG2   . VAL D 2 350 ? 15.687  20.263 113.334 1.00 6.42  ? 350 VAL B CG2   1 
ATOM   4857 N  N     . ALA D 2 351 ? 13.932  18.411 117.184 1.00 10.53 ? 351 ALA B N     1 
ATOM   4858 C  CA    . ALA D 2 351 ? 13.882  17.892 118.556 1.00 11.05 ? 351 ALA B CA    1 
ATOM   4859 C  C     . ALA D 2 351 ? 13.495  16.419 118.576 1.00 10.93 ? 351 ALA B C     1 
ATOM   4860 O  O     . ALA D 2 351 ? 14.213  15.647 119.241 1.00 11.87 ? 351 ALA B O     1 
ATOM   4861 C  CB    . ALA D 2 351 ? 13.058  18.750 119.496 1.00 10.91 ? 351 ALA B CB    1 
ATOM   4862 N  N     . ARG D 2 352 ? 12.444  16.051 117.880 1.00 10.14 ? 352 ARG B N     1 
ATOM   4863 C  CA    . ARG D 2 352 ? 11.943  14.678 117.818 1.00 10.34 ? 352 ARG B CA    1 
ATOM   4864 C  C     . ARG D 2 352 ? 12.846  13.786 116.964 1.00 9.76  ? 352 ARG B C     1 
ATOM   4865 O  O     . ARG D 2 352 ? 12.759  12.548 117.078 1.00 8.99  ? 352 ARG B O     1 
ATOM   4866 C  CB    . ARG D 2 352 ? 10.498  14.514 117.367 1.00 11.45 ? 352 ARG B CB    1 
ATOM   4867 C  CG    . ARG D 2 352 ? 10.175  14.837 115.935 1.00 12.65 ? 352 ARG B CG    1 
ATOM   4868 C  CD    . ARG D 2 352 ? 8.968   14.097 115.454 1.00 16.17 ? 352 ARG B CD    1 
ATOM   4869 N  NE    . ARG D 2 352 ? 9.072   13.825 114.020 1.00 19.70 ? 352 ARG B NE    1 
ATOM   4870 C  CZ    . ARG D 2 352 ? 8.533   14.526 113.030 1.00 19.82 ? 352 ARG B CZ    1 
ATOM   4871 N  NH1   . ARG D 2 352 ? 7.895   15.676 113.226 1.00 19.17 ? 352 ARG B NH1   1 
ATOM   4872 N  NH2   . ARG D 2 352 ? 8.641   14.108 111.753 1.00 18.62 ? 352 ARG B NH2   1 
ATOM   4873 N  N     . SER D 2 353 ? 13.719  14.389 116.175 1.00 9.38  ? 353 SER B N     1 
ATOM   4874 C  CA    . SER D 2 353 ? 14.628  13.622 115.337 1.00 9.66  ? 353 SER B CA    1 
ATOM   4875 C  C     . SER D 2 353 ? 15.939  13.250 115.994 1.00 10.53 ? 353 SER B C     1 
ATOM   4876 O  O     . SER D 2 353 ? 16.589  12.338 115.419 1.00 12.12 ? 353 SER B O     1 
ATOM   4877 C  CB    . SER D 2 353 ? 14.907  14.396 114.043 1.00 9.61  ? 353 SER B CB    1 
ATOM   4878 O  OG    . SER D 2 353 ? 13.703  14.461 113.300 1.00 11.92 ? 353 SER B OG    1 
ATOM   4879 N  N     . LEU D 2 354 ? 16.382  13.870 117.061 1.00 9.75  ? 354 LEU B N     1 
ATOM   4880 C  CA    . LEU D 2 354 ? 17.678  13.524 117.663 1.00 8.86  ? 354 LEU B CA    1 
ATOM   4881 C  C     . LEU D 2 354 ? 17.577  12.365 118.662 1.00 8.05  ? 354 LEU B C     1 
ATOM   4882 O  O     . LEU D 2 354 ? 16.520  12.080 119.250 1.00 8.99  ? 354 LEU B O     1 
ATOM   4883 C  CB    . LEU D 2 354 ? 18.329  14.764 118.245 1.00 8.20  ? 354 LEU B CB    1 
ATOM   4884 C  CG    . LEU D 2 354 ? 18.465  16.028 117.429 1.00 7.96  ? 354 LEU B CG    1 
ATOM   4885 C  CD1   . LEU D 2 354 ? 18.390  17.238 118.378 1.00 8.64  ? 354 LEU B CD1   1 
ATOM   4886 C  CD2   . LEU D 2 354 ? 19.781  16.015 116.679 1.00 6.42  ? 354 LEU B CD2   1 
ATOM   4887 N  N     . PRO D 2 355 ? 18.721  11.712 118.844 1.00 7.00  ? 355 PRO B N     1 
ATOM   4888 C  CA    . PRO D 2 355 ? 18.827  10.582 119.777 1.00 7.00  ? 355 PRO B CA    1 
ATOM   4889 C  C     . PRO D 2 355 ? 18.797  11.094 121.218 1.00 7.63  ? 355 PRO B C     1 
ATOM   4890 O  O     . PRO D 2 355 ? 19.029  12.305 121.430 1.00 8.36  ? 355 PRO B O     1 
ATOM   4891 C  CB    . PRO D 2 355 ? 20.155  9.926  119.446 1.00 6.59  ? 355 PRO B CB    1 
ATOM   4892 C  CG    . PRO D 2 355 ? 20.920  10.892 118.594 1.00 6.59  ? 355 PRO B CG    1 
ATOM   4893 C  CD    . PRO D 2 355 ? 19.996  11.998 118.181 1.00 6.92  ? 355 PRO B CD    1 
ATOM   4894 N  N     . VAL D 2 356 ? 18.551  10.210 122.169 1.00 7.99  ? 356 VAL B N     1 
ATOM   4895 C  CA    . VAL D 2 356 ? 18.504  10.587 123.588 1.00 7.79  ? 356 VAL B CA    1 
ATOM   4896 C  C     . VAL D 2 356 ? 19.784  11.331 123.938 1.00 8.82  ? 356 VAL B C     1 
ATOM   4897 O  O     . VAL D 2 356 ? 19.749  12.287 124.744 1.00 10.12 ? 356 VAL B O     1 
ATOM   4898 C  CB    . VAL D 2 356 ? 18.209  9.363  124.459 1.00 7.05  ? 356 VAL B CB    1 
ATOM   4899 C  CG1   . VAL D 2 356 ? 18.381  9.583  125.957 1.00 6.37  ? 356 VAL B CG1   1 
ATOM   4900 C  CG2   . VAL D 2 356 ? 16.784  8.890  124.204 1.00 8.50  ? 356 VAL B CG2   1 
ATOM   4901 N  N     . ALA D 2 357 ? 20.869  10.873 123.325 1.00 9.18  ? 357 ALA B N     1 
ATOM   4902 C  CA    . ALA D 2 357 ? 22.201  11.493 123.488 1.00 9.35  ? 357 ALA B CA    1 
ATOM   4903 C  C     . ALA D 2 357 ? 23.103  10.946 122.375 1.00 9.84  ? 357 ALA B C     1 
ATOM   4904 O  O     . ALA D 2 357 ? 22.676  10.079 121.609 1.00 10.05 ? 357 ALA B O     1 
ATOM   4905 C  CB    . ALA D 2 357 ? 22.816  11.262 124.831 1.00 7.74  ? 357 ALA B CB    1 
ATOM   4906 N  N     . VAL D 2 358 ? 24.291  11.520 122.338 1.00 10.26 ? 358 VAL B N     1 
ATOM   4907 C  CA    . VAL D 2 358 ? 25.369  11.189 121.409 1.00 10.41 ? 358 VAL B CA    1 
ATOM   4908 C  C     . VAL D 2 358 ? 26.717  11.305 122.131 1.00 10.61 ? 358 VAL B C     1 
ATOM   4909 O  O     . VAL D 2 358 ? 26.862  12.064 123.101 1.00 11.22 ? 358 VAL B O     1 
ATOM   4910 C  CB    . VAL D 2 358 ? 25.377  12.019 120.116 1.00 10.39 ? 358 VAL B CB    1 
ATOM   4911 C  CG1   . VAL D 2 358 ? 23.987  12.195 119.504 1.00 11.07 ? 358 VAL B CG1   1 
ATOM   4912 C  CG2   . VAL D 2 358 ? 25.939  13.427 120.320 1.00 11.30 ? 358 VAL B CG2   1 
ATOM   4913 N  N     . ILE D 2 359 ? 27.667  10.527 121.643 1.00 11.15 ? 359 ILE B N     1 
ATOM   4914 C  CA    . ILE D 2 359 ? 29.044  10.538 122.160 1.00 11.24 ? 359 ILE B CA    1 
ATOM   4915 C  C     . ILE D 2 359 ? 29.635  11.948 121.869 1.00 12.23 ? 359 ILE B C     1 
ATOM   4916 O  O     . ILE D 2 359 ? 29.315  12.573 120.842 1.00 12.71 ? 359 ILE B O     1 
ATOM   4917 C  CB    . ILE D 2 359 ? 29.859  9.470  121.417 1.00 10.34 ? 359 ILE B CB    1 
ATOM   4918 C  CG1   . ILE D 2 359 ? 29.841  9.653  119.898 1.00 11.89 ? 359 ILE B CG1   1 
ATOM   4919 C  CG2   . ILE D 2 359 ? 29.353  8.048  121.670 1.00 7.63  ? 359 ILE B CG2   1 
ATOM   4920 C  CD1   . ILE D 2 359 ? 30.921  8.837  119.185 1.00 12.71 ? 359 ILE B CD1   1 
ATOM   4921 N  N     . ALA D 2 360 ? 30.485  12.389 122.784 1.00 12.93 ? 360 ALA B N     1 
ATOM   4922 C  CA    . ALA D 2 360 ? 31.125  13.738 122.788 1.00 13.33 ? 360 ALA B CA    1 
ATOM   4923 C  C     . ALA D 2 360 ? 31.959  14.073 121.513 1.00 13.95 ? 360 ALA B C     1 
ATOM   4924 O  O     . ALA D 2 360 ? 32.344  15.233 121.293 1.00 15.00 ? 360 ALA B O     1 
ATOM   4925 C  CB    . ALA D 2 360 ? 32.073  13.851 123.983 1.00 10.34 ? 360 ALA B CB    1 
ATOM   4926 N  N     . ALA D 2 361 ? 32.251  13.063 120.698 1.00 14.18 ? 361 ALA B N     1 
ATOM   4927 C  CA    . ALA D 2 361 ? 33.001  13.217 119.421 1.00 13.97 ? 361 ALA B CA    1 
ATOM   4928 C  C     . ALA D 2 361 ? 32.128  13.912 118.346 1.00 15.61 ? 361 ALA B C     1 
ATOM   4929 O  O     . ALA D 2 361 ? 32.608  14.481 117.366 1.00 17.48 ? 361 ALA B O     1 
ATOM   4930 C  CB    . ALA D 2 361 ? 33.406  11.843 118.877 1.00 7.44  ? 361 ALA B CB    1 
ATOM   4931 N  N     . GLN D 2 362 ? 30.824  13.871 118.502 1.00 16.71 ? 362 GLN B N     1 
ATOM   4932 C  CA    . GLN D 2 362 ? 29.919  14.529 117.535 1.00 17.91 ? 362 GLN B CA    1 
ATOM   4933 C  C     . GLN D 2 362 ? 29.064  15.554 118.273 1.00 19.29 ? 362 GLN B C     1 
ATOM   4934 O  O     . GLN D 2 362 ? 27.860  15.350 118.486 1.00 20.74 ? 362 GLN B O     1 
ATOM   4935 C  CB    . GLN D 2 362 ? 29.003  13.482 116.877 1.00 16.09 ? 362 GLN B CB    1 
ATOM   4936 C  CG    . GLN D 2 362 ? 29.411  12.038 117.195 1.00 17.27 ? 362 GLN B CG    1 
ATOM   4937 C  CD    . GLN D 2 362 ? 28.309  11.011 116.899 1.00 20.18 ? 362 GLN B CD    1 
ATOM   4938 O  OE1   . GLN D 2 362 ? 27.127  11.354 116.905 1.00 23.31 ? 362 GLN B OE1   1 
ATOM   4939 N  NE2   . GLN D 2 362 ? 28.626  9.755  116.639 1.00 20.74 ? 362 GLN B NE2   1 
ATOM   4940 N  N     . ASN D 2 363 ? 29.672  16.680 118.657 1.00 19.00 ? 363 ASN B N     1 
ATOM   4941 C  CA    . ASN D 2 363 ? 28.929  17.627 119.494 1.00 19.00 ? 363 ASN B CA    1 
ATOM   4942 C  C     . ASN D 2 363 ? 28.958  19.111 119.118 1.00 18.00 ? 363 ASN B C     1 
ATOM   4943 O  O     . ASN D 2 363 ? 28.526  19.480 118.015 1.00 18.00 ? 363 ASN B O     1 
ATOM   4944 C  CB    . ASN D 2 363 ? 29.398  17.556 120.953 1.00 20.00 ? 363 ASN B CB    1 
ATOM   4945 C  CG    . ASN D 2 363 ? 30.878  17.880 121.147 1.00 22.00 ? 363 ASN B CG    1 
ATOM   4946 O  OD1   . ASN D 2 363 ? 31.383  17.792 122.266 1.00 26.00 ? 363 ASN B OD1   1 
ATOM   4947 N  ND2   . ASN D 2 363 ? 31.613  18.253 120.118 1.00 21.00 ? 363 ASN B ND2   1 
ATOM   4948 O  OXT   . ASN D 2 363 ? 29.413  19.945 119.915 1.00 18.00 ? 363 ASN B OXT   1 
ATOM   4949 N  N     . ALA E 3 1   ? 29.509  13.783 112.792 1.00 20.73 ? 364 ALA E N     1 
ATOM   4950 C  CA    . ALA E 3 1   ? 30.053  15.044 112.251 1.00 19.41 ? 364 ALA E CA    1 
ATOM   4951 C  C     . ALA E 3 1   ? 30.306  15.989 113.407 1.00 18.27 ? 364 ALA E C     1 
ATOM   4952 O  O     . ALA E 3 1   ? 31.255  15.801 114.186 1.00 17.68 ? 364 ALA E O     1 
ATOM   4953 C  CB    . ALA E 3 1   ? 28.974  15.737 111.434 1.00 18.14 ? 364 ALA E CB    1 
ATOM   4954 N  N     . SER E 3 2   ? 29.396  16.922 113.388 1.00 16.53 ? 365 SER E N     1 
ATOM   4955 C  CA    . SER E 3 2   ? 29.191  17.964 114.378 1.00 14.92 ? 365 SER E CA    1 
ATOM   4956 C  C     . SER E 3 2   ? 27.676  17.988 114.563 1.00 15.01 ? 365 SER E C     1 
ATOM   4957 O  O     . SER E 3 2   ? 26.923  17.493 113.712 1.00 15.28 ? 365 SER E O     1 
ATOM   4958 C  CB    . SER E 3 2   ? 29.763  19.289 113.862 1.00 10.59 ? 365 SER E CB    1 
ATOM   4959 O  OG    . SER E 3 2   ? 28.726  20.086 113.315 1.00 4.68  ? 365 SER E OG    1 
ATOM   4960 N  N     . MET E 3 3   ? 27.212  18.538 115.651 1.00 14.24 ? 366 MET E N     1 
ATOM   4961 C  CA    . MET E 3 3   ? 25.770  18.524 115.941 1.00 13.25 ? 366 MET E CA    1 
ATOM   4962 C  C     . MET E 3 3   ? 24.984  19.529 115.086 1.00 12.59 ? 366 MET E C     1 
ATOM   4963 O  O     . MET E 3 3   ? 23.781  19.356 114.840 1.00 12.03 ? 366 MET E O     1 
ATOM   4964 C  CB    . MET E 3 3   ? 25.510  18.865 117.407 1.00 13.22 ? 366 MET E CB    1 
ATOM   4965 C  CG    . MET E 3 3   ? 24.062  18.594 117.828 1.00 14.86 ? 366 MET E CG    1 
ATOM   4966 S  SD    . MET E 3 3   ? 23.201  17.508 116.708 1.00 19.15 ? 366 MET E SD    1 
ATOM   4967 C  CE    . MET E 3 3   ? 23.034  15.892 117.435 1.00 17.17 ? 366 MET E CE    1 
ATOM   4968 N  N     . TRP E 3 4   ? 25.660  20.574 114.645 1.00 11.69 ? 367 TRP E N     1 
ATOM   4969 C  CA    . TRP E 3 4   ? 25.021  21.616 113.815 1.00 12.03 ? 367 TRP E CA    1 
ATOM   4970 C  C     . TRP E 3 4   ? 24.963  21.156 112.357 1.00 13.15 ? 367 TRP E C     1 
ATOM   4971 O  O     . TRP E 3 4   ? 24.122  21.622 111.573 1.00 12.72 ? 367 TRP E O     1 
ATOM   4972 C  CB    . TRP E 3 4   ? 25.797  22.934 113.902 1.00 12.71 ? 367 TRP E CB    1 
ATOM   4973 C  CG    . TRP E 3 4   ? 25.251  24.026 112.967 1.00 13.85 ? 367 TRP E CG    1 
ATOM   4974 C  CD1   . TRP E 3 4   ? 25.929  24.687 112.018 1.00 12.72 ? 367 TRP E CD1   1 
ATOM   4975 C  CD2   . TRP E 3 4   ? 23.914  24.520 112.961 1.00 14.11 ? 367 TRP E CD2   1 
ATOM   4976 N  NE1   . TRP E 3 4   ? 25.018  25.604 111.402 1.00 14.38 ? 367 TRP E NE1   1 
ATOM   4977 C  CE2   . TRP E 3 4   ? 23.843  25.489 111.967 1.00 15.07 ? 367 TRP E CE2   1 
ATOM   4978 C  CE3   . TRP E 3 4   ? 22.765  24.227 113.707 1.00 14.44 ? 367 TRP E CE3   1 
ATOM   4979 C  CZ2   . TRP E 3 4   ? 22.672  26.196 111.664 1.00 14.54 ? 367 TRP E CZ2   1 
ATOM   4980 C  CZ3   . TRP E 3 4   ? 21.590  24.944 113.396 1.00 14.28 ? 367 TRP E CZ3   1 
ATOM   4981 C  CH2   . TRP E 3 4   ? 21.547  25.882 112.422 1.00 14.92 ? 367 TRP E CH2   1 
ATOM   4982 N  N     . GLU E 3 5   ? 25.867  20.245 112.038 1.00 15.16 ? 368 GLU E N     1 
ATOM   4983 C  CA    . GLU E 3 5   ? 25.969  19.663 110.692 1.00 16.78 ? 368 GLU E CA    1 
ATOM   4984 C  C     . GLU E 3 5   ? 24.978  18.502 110.561 1.00 16.66 ? 368 GLU E C     1 
ATOM   4985 O  O     . GLU E 3 5   ? 24.659  18.053 109.450 1.00 17.23 ? 368 GLU E O     1 
ATOM   4986 C  CB    . GLU E 3 5   ? 27.394  19.170 110.436 1.00 19.30 ? 368 GLU E CB    1 
ATOM   4987 C  CG    . GLU E 3 5   ? 28.292  20.239 109.802 1.00 25.17 ? 368 GLU E CG    1 
ATOM   4988 C  CD    . GLU E 3 5   ? 27.524  21.233 108.923 1.00 30.38 ? 368 GLU E CD    1 
ATOM   4989 O  OE1   . GLU E 3 5   ? 26.261  21.072 108.717 1.00 31.41 ? 368 GLU E OE1   1 
ATOM   4990 O  OE2   . GLU E 3 5   ? 28.141  22.232 108.386 1.00 31.85 ? 368 GLU E OE2   1 
ATOM   4991 N  N     . ARG E 3 6   ? 24.522  18.043 111.713 1.00 16.02 ? 369 ARG E N     1 
ATOM   4992 C  CA    . ARG E 3 6   ? 23.518  16.974 111.798 1.00 15.41 ? 369 ARG E CA    1 
ATOM   4993 C  C     . ARG E 3 6   ? 22.136  17.617 111.809 1.00 14.90 ? 369 ARG E C     1 
ATOM   4994 O  O     . ARG E 3 6   ? 21.198  17.131 111.160 1.00 15.42 ? 369 ARG E O     1 
ATOM   4995 C  CB    . ARG E 3 6   ? 23.708  16.154 113.078 1.00 15.00 ? 369 ARG E CB    1 
ATOM   4996 C  CG    . ARG E 3 6   ? 22.933  14.832 113.056 1.00 14.74 ? 369 ARG E CG    1 
ATOM   4997 C  CD    . ARG E 3 6   ? 22.564  14.326 114.453 1.00 15.46 ? 369 ARG E CD    1 
ATOM   4998 N  NE    . ARG E 3 6   ? 23.051  12.963 114.717 1.00 16.90 ? 369 ARG E NE    1 
ATOM   4999 C  CZ    . ARG E 3 6   ? 24.197  12.691 115.355 1.00 16.92 ? 369 ARG E CZ    1 
ATOM   5000 N  NH1   . ARG E 3 6   ? 24.989  13.676 115.801 1.00 16.41 ? 369 ARG E NH1   1 
ATOM   5001 N  NH2   . ARG E 3 6   ? 24.644  11.451 115.598 1.00 16.35 ? 369 ARG E NH2   1 
ATOM   5002 N  N     . VAL E 3 7   ? 22.082  18.703 112.553 1.00 13.76 ? 370 VAL E N     1 
ATOM   5003 C  CA    . VAL E 3 7   ? 20.875  19.513 112.705 1.00 11.53 ? 370 VAL E CA    1 
ATOM   5004 C  C     . VAL E 3 7   ? 20.540  20.179 111.368 1.00 11.98 ? 370 VAL E C     1 
ATOM   5005 O  O     . VAL E 3 7   ? 19.388  20.162 110.916 1.00 11.63 ? 370 VAL E O     1 
ATOM   5006 C  CB    . VAL E 3 7   ? 21.111  20.591 113.768 1.00 7.21  ? 370 VAL E CB    1 
ATOM   5007 C  CG1   . VAL E 3 7   ? 20.047  21.690 113.756 1.00 7.84  ? 370 VAL E CG1   1 
ATOM   5008 C  CG2   . VAL E 3 7   ? 21.116  20.034 115.193 1.00 5.54  ? 370 VAL E CG2   1 
ATOM   5009 N  N     . LYS E 3 8   ? 21.576  20.740 110.772 1.00 12.40 ? 371 LYS E N     1 
ATOM   5010 C  CA    . LYS E 3 8   ? 21.468  21.451 109.490 1.00 13.72 ? 371 LYS E CA    1 
ATOM   5011 C  C     . LYS E 3 8   ? 20.829  20.558 108.419 1.00 13.94 ? 371 LYS E C     1 
ATOM   5012 O  O     . LYS E 3 8   ? 20.046  21.027 107.581 1.00 13.47 ? 371 LYS E O     1 
ATOM   5013 C  CB    . LYS E 3 8   ? 22.854  21.886 109.001 1.00 15.03 ? 371 LYS E CB    1 
ATOM   5014 C  CG    . LYS E 3 8   ? 22.808  23.171 108.168 1.00 15.20 ? 371 LYS E CG    1 
ATOM   5015 C  CD    . LYS E 3 8   ? 24.193  23.745 107.858 1.00 16.79 ? 371 LYS E CD    1 
ATOM   5016 C  CE    . LYS E 3 8   ? 25.303  23.134 108.712 1.00 17.39 ? 371 LYS E CE    1 
ATOM   5017 N  NZ    . LYS E 3 8   ? 26.470  22.716 107.921 1.00 17.74 ? 371 LYS E NZ    1 
ATOM   5018 N  N     . SER E 3 9   ? 21.176  19.284 108.475 1.00 13.43 ? 372 SER E N     1 
ATOM   5019 C  CA    . SER E 3 9   ? 20.692  18.287 107.502 1.00 14.38 ? 372 SER E CA    1 
ATOM   5020 C  C     . SER E 3 9   ? 19.213  17.950 107.734 1.00 14.26 ? 372 SER E C     1 
ATOM   5021 O  O     . SER E 3 9   ? 18.435  17.782 106.785 1.00 13.66 ? 372 SER E O     1 
ATOM   5022 C  CB    . SER E 3 9   ? 21.514  17.002 107.602 1.00 15.95 ? 372 SER E CB    1 
ATOM   5023 O  OG    . SER E 3 9   ? 21.271  16.362 108.843 1.00 20.46 ? 372 SER E OG    1 
ATOM   5024 N  N     . ILE E 3 10  ? 18.832  17.847 108.994 1.00 13.17 ? 373 ILE E N     1 
ATOM   5025 C  CA    . ILE E 3 10  ? 17.438  17.535 109.343 1.00 13.06 ? 373 ILE E CA    1 
ATOM   5026 C  C     . ILE E 3 10  ? 16.524  18.612 108.761 1.00 14.22 ? 373 ILE E C     1 
ATOM   5027 O  O     . ILE E 3 10  ? 15.502  18.313 108.127 1.00 14.42 ? 373 ILE E O     1 
ATOM   5028 C  CB    . ILE E 3 10  ? 17.257  17.474 110.862 1.00 9.04  ? 373 ILE E CB    1 
ATOM   5029 C  CG1   . ILE E 3 10  ? 18.200  16.475 111.536 1.00 7.03  ? 373 ILE E CG1   1 
ATOM   5030 C  CG2   . ILE E 3 10  ? 15.843  17.052 111.277 1.00 6.85  ? 373 ILE E CG2   1 
ATOM   5031 C  CD1   . ILE E 3 10  ? 17.584  15.801 112.765 1.00 5.01  ? 373 ILE E CD1   1 
ATOM   5032 N  N     . ILE E 3 11  ? 16.935  19.843 108.986 1.00 14.74 ? 374 ILE E N     1 
ATOM   5033 C  CA    . ILE E 3 11  ? 16.194  21.019 108.523 1.00 15.46 ? 374 ILE E CA    1 
ATOM   5034 C  C     . ILE E 3 11  ? 16.111  21.031 106.995 1.00 16.33 ? 374 ILE E C     1 
ATOM   5035 O  O     . ILE E 3 11  ? 15.076  21.372 106.410 1.00 16.41 ? 374 ILE E O     1 
ATOM   5036 C  CB    . ILE E 3 11  ? 16.875  22.295 109.013 1.00 14.17 ? 374 ILE E CB    1 
ATOM   5037 C  CG1   . ILE E 3 11  ? 16.591  22.577 110.490 1.00 13.80 ? 374 ILE E CG1   1 
ATOM   5038 C  CG2   . ILE E 3 11  ? 16.423  23.542 108.251 1.00 13.77 ? 374 ILE E CG2   1 
ATOM   5039 C  CD1   . ILE E 3 11  ? 17.308  23.820 111.014 1.00 14.44 ? 374 ILE E CD1   1 
ATOM   5040 N  N     . LYS E 3 12  ? 17.201  20.656 106.356 1.00 16.47 ? 375 LYS E N     1 
ATOM   5041 C  CA    . LYS E 3 12  ? 17.247  20.632 104.890 1.00 16.84 ? 375 LYS E CA    1 
ATOM   5042 C  C     . LYS E 3 12  ? 16.321  19.524 104.361 1.00 17.54 ? 375 LYS E C     1 
ATOM   5043 O  O     . LYS E 3 12  ? 15.829  19.578 103.228 1.00 18.37 ? 375 LYS E O     1 
ATOM   5044 C  CB    . LYS E 3 12  ? 18.687  20.446 104.402 1.00 16.86 ? 375 LYS E CB    1 
ATOM   5045 C  CG    . LYS E 3 12  ? 19.371  21.790 104.110 1.00 19.32 ? 375 LYS E CG    1 
ATOM   5046 C  CD    . LYS E 3 12  ? 20.716  21.655 103.394 1.00 22.00 ? 375 LYS E CD    1 
ATOM   5047 C  CE    . LYS E 3 12  ? 21.700  22.770 103.762 1.00 24.00 ? 375 LYS E CE    1 
ATOM   5048 N  NZ    . LYS E 3 12  ? 23.086  22.293 103.882 1.00 23.75 ? 375 LYS E NZ    1 
ATOM   5049 N  N     . SER E 3 13  ? 16.073  18.532 105.194 1.00 17.99 ? 376 SER E N     1 
ATOM   5050 C  CA    . SER E 3 13  ? 15.196  17.410 104.818 1.00 19.41 ? 376 SER E CA    1 
ATOM   5051 C  C     . SER E 3 13  ? 13.740  17.895 104.610 1.00 20.30 ? 376 SER E C     1 
ATOM   5052 O  O     . SER E 3 13  ? 13.186  17.799 103.505 1.00 19.92 ? 376 SER E O     1 
ATOM   5053 C  CB    . SER E 3 13  ? 15.209  16.331 105.905 1.00 19.54 ? 376 SER E CB    1 
ATOM   5054 O  OG    . SER E 3 13  ? 14.062  15.501 105.780 1.00 21.00 ? 376 SER E OG    1 
ATOM   5055 N  N     . SER E 3 14  ? 13.154  18.423 105.687 1.00 20.78 ? 377 SER E N     1 
ATOM   5056 C  CA    . SER E 3 14  ? 11.731  18.866 105.710 1.00 21.19 ? 377 SER E CA    1 
ATOM   5057 C  C     . SER E 3 14  ? 11.540  20.316 105.262 1.00 21.49 ? 377 SER E C     1 
ATOM   5058 O  O     . SER E 3 14  ? 10.507  20.948 105.533 1.00 22.11 ? 377 SER E O     1 
ATOM   5059 C  CB    . SER E 3 14  ? 11.162  18.772 107.117 1.00 22.21 ? 377 SER E CB    1 
ATOM   5060 O  OG    . SER E 3 14  ? 12.219  18.757 108.057 1.00 22.59 ? 377 SER E OG    1 
ATOM   5061 N  N     . LEU E 3 15  ? 12.531  20.819 104.604 1.00 20.87 ? 378 LEU E N     1 
ATOM   5062 C  CA    . LEU E 3 15  ? 12.464  22.146 104.024 1.00 21.18 ? 378 LEU E CA    1 
ATOM   5063 C  C     . LEU E 3 15  ? 12.622  21.941 102.543 1.00 22.16 ? 378 LEU E C     1 
ATOM   5064 O  O     . LEU E 3 15  ? 12.778  22.904 101.778 1.00 22.42 ? 378 LEU E O     1 
ATOM   5065 C  CB    . LEU E 3 15  ? 13.545  23.032 104.631 1.00 19.91 ? 378 LEU E CB    1 
ATOM   5066 C  CG    . LEU E 3 15  ? 12.974  23.992 105.673 1.00 20.56 ? 378 LEU E CG    1 
ATOM   5067 C  CD1   . LEU E 3 15  ? 13.880  25.191 105.945 1.00 19.05 ? 378 LEU E CD1   1 
ATOM   5068 C  CD2   . LEU E 3 15  ? 11.620  24.577 105.260 1.00 18.11 ? 378 LEU E CD2   1 
ATOM   5069 N  N     . ALA E 3 16  ? 12.556  20.656 102.242 1.00 21.50 ? 379 ALA E N     1 
ATOM   5070 C  CA    . ALA E 3 16  ? 12.706  20.152 100.895 1.00 21.15 ? 379 ALA E CA    1 
ATOM   5071 C  C     . ALA E 3 16  ? 11.754  18.951 100.599 1.00 21.70 ? 379 ALA E C     1 
ATOM   5072 O  O     . ALA E 3 16  ? 11.914  17.830 101.170 1.00 22.07 ? 379 ALA E O     1 
ATOM   5073 C  CB    . ALA E 3 16  ? 14.142  19.676 100.668 1.00 20.82 ? 379 ALA E CB    1 
ATOM   5074 N  N     . THR F 2 20  ? -43.429 7.279  120.258 1.00 13.46 ? 20  THR C N     1 
ATOM   5075 C  CA    . THR F 2 20  ? -41.976 6.908  120.123 1.00 13.09 ? 20  THR C CA    1 
ATOM   5076 C  C     . THR F 2 20  ? -41.363 6.021  121.217 1.00 12.87 ? 20  THR C C     1 
ATOM   5077 O  O     . THR F 2 20  ? -42.037 5.623  122.183 1.00 12.57 ? 20  THR C O     1 
ATOM   5078 C  CB    . THR F 2 20  ? -41.097 8.154  120.136 1.00 12.96 ? 20  THR C CB    1 
ATOM   5079 O  OG1   . THR F 2 20  ? -41.485 9.016  121.195 1.00 12.60 ? 20  THR C OG1   1 
ATOM   5080 C  CG2   . THR F 2 20  ? -41.186 8.945  118.833 1.00 13.42 ? 20  THR C CG2   1 
ATOM   5081 N  N     . GLN F 2 21  ? -40.048 5.783  120.990 1.00 12.88 ? 21  GLN C N     1 
ATOM   5082 C  CA    . GLN F 2 21  ? -39.260 4.848  121.805 1.00 13.19 ? 21  GLN C CA    1 
ATOM   5083 C  C     . GLN F 2 21  ? -37.709 5.102  121.753 1.00 13.52 ? 21  GLN C C     1 
ATOM   5084 O  O     . GLN F 2 21  ? -37.227 6.012  121.050 1.00 13.69 ? 21  GLN C O     1 
ATOM   5085 C  CB    . GLN F 2 21  ? -39.634 3.460  121.320 1.00 12.83 ? 21  GLN C CB    1 
ATOM   5086 C  CG    . GLN F 2 21  ? -41.155 3.221  121.432 1.00 13.77 ? 21  GLN C CG    1 
ATOM   5087 C  CD    . GLN F 2 21  ? -41.984 3.722  120.228 1.00 14.38 ? 21  GLN C CD    1 
ATOM   5088 O  OE1   . GLN F 2 21  ? -42.989 3.099  119.875 1.00 15.08 ? 21  GLN C OE1   1 
ATOM   5089 N  NE2   . GLN F 2 21  ? -41.635 4.812  119.567 1.00 12.91 ? 21  GLN C NE2   1 
ATOM   5090 N  N     . THR F 2 22  ? -37.033 4.221  122.526 1.00 13.32 ? 22  THR C N     1 
ATOM   5091 C  CA    . THR F 2 22  ? -35.578 4.266  122.895 1.00 12.68 ? 22  THR C CA    1 
ATOM   5092 C  C     . THR F 2 22  ? -34.569 3.702  121.868 1.00 12.42 ? 22  THR C C     1 
ATOM   5093 O  O     . THR F 2 22  ? -34.818 2.667  121.220 1.00 12.37 ? 22  THR C O     1 
ATOM   5094 C  CB    . THR F 2 22  ? -35.360 3.470  124.181 1.00 12.71 ? 22  THR C CB    1 
ATOM   5095 O  OG1   . THR F 2 22  ? -35.483 2.079  123.924 1.00 13.85 ? 22  THR C OG1   1 
ATOM   5096 C  CG2   . THR F 2 22  ? -36.379 3.826  125.266 1.00 12.87 ? 22  THR C CG2   1 
ATOM   5097 N  N     . ALA F 2 23  ? -33.460 4.451  121.868 1.00 12.35 ? 23  ALA C N     1 
ATOM   5098 C  CA    . ALA F 2 23  ? -32.278 4.292  120.999 1.00 12.39 ? 23  ALA C CA    1 
ATOM   5099 C  C     . ALA F 2 23  ? -31.388 3.112  121.393 1.00 12.44 ? 23  ALA C C     1 
ATOM   5100 O  O     . ALA F 2 23  ? -31.229 2.795  122.586 1.00 12.92 ? 23  ALA C O     1 
ATOM   5101 C  CB    . ALA F 2 23  ? -31.394 5.543  121.095 1.00 11.84 ? 23  ALA C CB    1 
ATOM   5102 N  N     . PRO F 2 24  ? -30.790 2.446  120.393 1.00 12.23 ? 24  PRO C N     1 
ATOM   5103 C  CA    . PRO F 2 24  ? -29.896 1.334  120.634 1.00 12.60 ? 24  PRO C CA    1 
ATOM   5104 C  C     . PRO F 2 24  ? -28.739 1.811  121.460 1.00 12.91 ? 24  PRO C C     1 
ATOM   5105 O  O     . PRO F 2 24  ? -28.630 3.049  121.712 1.00 13.02 ? 24  PRO C O     1 
ATOM   5106 C  CB    . PRO F 2 24  ? -29.476 0.898  119.250 1.00 12.30 ? 24  PRO C CB    1 
ATOM   5107 C  CG    . PRO F 2 24  ? -30.165 1.810  118.247 1.00 12.25 ? 24  PRO C CG    1 
ATOM   5108 C  CD    . PRO F 2 24  ? -30.999 2.799  118.991 1.00 12.31 ? 24  PRO C CD    1 
ATOM   5109 N  N     . VAL F 2 25  ? -27.911 0.869  121.859 1.00 12.84 ? 25  VAL C N     1 
ATOM   5110 C  CA    . VAL F 2 25  ? -26.739 1.170  122.690 1.00 12.80 ? 25  VAL C CA    1 
ATOM   5111 C  C     . VAL F 2 25  ? -25.455 0.885  121.913 1.00 12.77 ? 25  VAL C C     1 
ATOM   5112 O  O     . VAL F 2 25  ? -25.234 -0.240 121.432 1.00 12.96 ? 25  VAL C O     1 
ATOM   5113 C  CB    . VAL F 2 25  ? -26.786 0.339  123.969 1.00 12.91 ? 25  VAL C CB    1 
ATOM   5114 C  CG1   . VAL F 2 25  ? -26.073 -1.005 123.840 1.00 12.00 ? 25  VAL C CG1   1 
ATOM   5115 C  CG2   . VAL F 2 25  ? -26.138 1.048  125.160 1.00 12.25 ? 25  VAL C CG2   1 
ATOM   5116 N  N     . PRO F 2 26  ? -24.575 1.884  121.764 1.00 12.68 ? 26  PRO C N     1 
ATOM   5117 C  CA    . PRO F 2 26  ? -23.346 1.720  121.026 1.00 12.54 ? 26  PRO C CA    1 
ATOM   5118 C  C     . PRO F 2 26  ? -22.468 0.652  121.603 1.00 12.55 ? 26  PRO C C     1 
ATOM   5119 O  O     . PRO F 2 26  ? -22.008 0.801  122.783 1.00 13.00 ? 26  PRO C O     1 
ATOM   5120 C  CB    . PRO F 2 26  ? -22.671 3.065  121.104 1.00 12.68 ? 26  PRO C CB    1 
ATOM   5121 C  CG    . PRO F 2 26  ? -23.573 3.986  121.900 1.00 12.75 ? 26  PRO C CG    1 
ATOM   5122 C  CD    . PRO F 2 26  ? -24.789 3.220  122.322 1.00 12.55 ? 26  PRO C CD    1 
ATOM   5123 N  N     . GLN F 2 27  ? -22.294 -0.341 120.759 1.00 12.54 ? 27  GLN C N     1 
ATOM   5124 C  CA    . GLN F 2 27  ? -21.383 -1.456 120.983 1.00 12.67 ? 27  GLN C CA    1 
ATOM   5125 C  C     . GLN F 2 27  ? -20.107 -1.100 120.249 1.00 12.98 ? 27  GLN C C     1 
ATOM   5126 O  O     . GLN F 2 27  ? -20.141 -0.406 119.222 1.00 13.47 ? 27  GLN C O     1 
ATOM   5127 C  CB    . GLN F 2 27  ? -21.957 -2.747 120.394 1.00 11.78 ? 27  GLN C CB    1 
ATOM   5128 C  CG    . GLN F 2 27  ? -23.402 -3.004 120.805 1.00 12.71 ? 27  GLN C CG    1 
ATOM   5129 C  CD    . GLN F 2 27  ? -23.613 -2.888 122.312 1.00 13.11 ? 27  GLN C CD    1 
ATOM   5130 O  OE1   . GLN F 2 27  ? -22.795 -3.383 123.085 1.00 13.88 ? 27  GLN C OE1   1 
ATOM   5131 N  NE2   . GLN F 2 27  ? -24.671 -2.256 122.780 1.00 13.24 ? 27  GLN C NE2   1 
ATOM   5132 N  N     . GLN F 2 28  ? -19.008 -1.562 120.774 1.00 13.00 ? 28  GLN C N     1 
ATOM   5133 C  CA    . GLN F 2 28  ? -17.714 -1.269 120.173 1.00 12.95 ? 28  GLN C CA    1 
ATOM   5134 C  C     . GLN F 2 28  ? -16.722 -2.385 120.440 1.00 12.75 ? 28  GLN C C     1 
ATOM   5135 O  O     . GLN F 2 28  ? -16.924 -3.211 121.343 1.00 12.69 ? 28  GLN C O     1 
ATOM   5136 C  CB    . GLN F 2 28  ? -17.144 0.021  120.757 1.00 12.14 ? 28  GLN C CB    1 
ATOM   5137 C  CG    . GLN F 2 28  ? -18.125 1.191  120.705 1.00 12.30 ? 28  GLN C CG    1 
ATOM   5138 C  CD    . GLN F 2 28  ? -17.482 2.516  121.112 1.00 13.72 ? 28  GLN C CD    1 
ATOM   5139 O  OE1   . GLN F 2 28  ? -17.656 2.961  122.245 1.00 14.27 ? 28  GLN C OE1   1 
ATOM   5140 N  NE2   . GLN F 2 28  ? -16.737 3.180  120.248 1.00 13.46 ? 28  GLN C NE2   1 
ATOM   5141 N  N     . ASN F 2 29  ? -15.695 -2.335 119.623 1.00 12.51 ? 29  ASN C N     1 
ATOM   5142 C  CA    . ASN F 2 29  ? -14.571 -3.266 119.667 1.00 12.63 ? 29  ASN C CA    1 
ATOM   5143 C  C     . ASN F 2 29  ? -15.039 -4.683 119.356 1.00 12.62 ? 29  ASN C C     1 
ATOM   5144 O  O     . ASN F 2 29  ? -14.371 -5.666 119.709 1.00 12.74 ? 29  ASN C O     1 
ATOM   5145 C  CB    . ASN F 2 29  ? -13.910 -3.201 121.036 1.00 11.84 ? 29  ASN C CB    1 
ATOM   5146 C  CG    . ASN F 2 29  ? -13.151 -1.889 121.238 1.00 11.81 ? 29  ASN C CG    1 
ATOM   5147 O  OD1   . ASN F 2 29  ? -13.435 -1.154 122.181 1.00 12.08 ? 29  ASN C OD1   1 
ATOM   5148 N  ND2   . ASN F 2 29  ? -12.196 -1.544 120.394 1.00 12.61 ? 29  ASN C ND2   1 
ATOM   5149 N  N     . VAL F 2 30  ? -16.185 -4.738 118.707 1.00 12.31 ? 30  VAL C N     1 
ATOM   5150 C  CA    . VAL F 2 30  ? -16.751 -6.000 118.229 1.00 12.47 ? 30  VAL C CA    1 
ATOM   5151 C  C     . VAL F 2 30  ? -15.923 -6.384 117.007 1.00 12.70 ? 30  VAL C C     1 
ATOM   5152 O  O     . VAL F 2 30  ? -15.915 -5.674 115.990 1.00 13.03 ? 30  VAL C O     1 
ATOM   5153 C  CB    . VAL F 2 30  ? -18.236 -5.807 117.926 1.00 11.77 ? 30  VAL C CB    1 
ATOM   5154 C  CG1   . VAL F 2 30  ? -18.649 -4.335 117.895 1.00 12.38 ? 30  VAL C CG1   1 
ATOM   5155 C  CG2   . VAL F 2 30  ? -18.657 -6.393 116.581 1.00 12.49 ? 30  VAL C CG2   1 
ATOM   5156 N  N     . PRO F 2 31  ? -15.208 -7.503 117.044 1.00 25.00 ? 31  PRO C N     1 
ATOM   5157 C  CA    . PRO F 2 31  ? -14.263 -7.839 115.996 1.00 25.00 ? 31  PRO C CA    1 
ATOM   5158 C  C     . PRO F 2 31  ? -14.850 -7.938 114.628 1.00 25.00 ? 31  PRO C C     1 
ATOM   5159 O  O     . PRO F 2 31  ? -15.961 -8.533 114.483 1.00 25.00 ? 31  PRO C O     1 
ATOM   5160 C  CB    . PRO F 2 31  ? -13.704 -9.177 116.424 1.00 25.00 ? 31  PRO C CB    1 
ATOM   5161 C  CG    . PRO F 2 31  ? -14.364 -9.560 117.740 1.00 25.00 ? 31  PRO C CG    1 
ATOM   5162 C  CD    . PRO F 2 31  ? -15.321 -8.478 118.131 1.00 25.00 ? 31  PRO C CD    1 
ATOM   5163 N  N     . ALA F 2 55  ? -10.671 16.529 100.094 1.00 24.11 ? 55  ALA C N     1 
ATOM   5164 C  CA    . ALA F 2 55  ? -12.141 16.634 100.342 1.00 24.21 ? 55  ALA C CA    1 
ATOM   5165 C  C     . ALA F 2 55  ? -12.264 17.174 101.733 1.00 24.89 ? 55  ALA C C     1 
ATOM   5166 O  O     . ALA F 2 55  ? -12.684 18.329 101.929 1.00 26.11 ? 55  ALA C O     1 
ATOM   5167 C  CB    . ALA F 2 55  ? -12.751 15.250 100.585 1.00 21.06 ? 55  ALA C CB    1 
ATOM   5168 N  N     . LEU F 2 56  ? -11.843 16.180 102.462 1.00 16.57 ? 56  LEU C N     1 
ATOM   5169 C  CA    . LEU F 2 56  ? -11.626 16.073 103.880 1.00 17.00 ? 56  LEU C CA    1 
ATOM   5170 C  C     . LEU F 2 56  ? -10.188 15.579 103.956 1.00 17.23 ? 56  LEU C C     1 
ATOM   5171 O  O     . LEU F 2 56  ? -9.816  14.832 104.871 1.00 17.15 ? 56  LEU C O     1 
ATOM   5172 C  CB    . LEU F 2 56  ? -12.588 15.001 104.413 1.00 15.82 ? 56  LEU C CB    1 
ATOM   5173 C  CG    . LEU F 2 56  ? -13.391 15.432 105.632 1.00 17.10 ? 56  LEU C CG    1 
ATOM   5174 C  CD1   . LEU F 2 56  ? -14.236 14.292 106.211 1.00 14.81 ? 56  LEU C CD1   1 
ATOM   5175 C  CD2   . LEU F 2 56  ? -12.507 15.919 106.777 1.00 17.65 ? 56  LEU C CD2   1 
ATOM   5176 N  N     . THR F 2 57  ? -9.492  16.038 102.924 1.00 17.70 ? 57  THR C N     1 
ATOM   5177 C  CA    . THR F 2 57  ? -8.109  15.673 102.600 1.00 18.06 ? 57  THR C CA    1 
ATOM   5178 C  C     . THR F 2 57  ? -7.091  16.665 103.161 1.00 17.03 ? 57  THR C C     1 
ATOM   5179 O  O     . THR F 2 57  ? -5.916  16.322 103.367 1.00 16.87 ? 57  THR C O     1 
ATOM   5180 C  CB    . THR F 2 57  ? -7.963  15.659 101.077 1.00 20.55 ? 57  THR C CB    1 
ATOM   5181 O  OG1   . THR F 2 57  ? -7.893  14.323 100.612 1.00 23.28 ? 57  THR C OG1   1 
ATOM   5182 C  CG2   . THR F 2 57  ? -6.717  16.392 100.585 1.00 21.83 ? 57  THR C CG2   1 
ATOM   5183 N  N     . ARG F 2 58  ? -7.556  17.867 103.384 1.00 16.07 ? 58  ARG C N     1 
ATOM   5184 C  CA    . ARG F 2 58  ? -6.716  18.944 103.910 1.00 15.30 ? 58  ARG C CA    1 
ATOM   5185 C  C     . ARG F 2 58  ? -6.248  18.595 105.317 1.00 14.76 ? 58  ARG C C     1 
ATOM   5186 O  O     . ARG F 2 58  ? -5.205  19.077 105.777 1.00 14.80 ? 58  ARG C O     1 
ATOM   5187 C  CB    . ARG F 2 58  ? -7.518  20.250 103.930 1.00 16.07 ? 58  ARG C CB    1 
ATOM   5188 C  CG    . ARG F 2 58  ? -8.498  20.372 102.752 1.00 18.67 ? 58  ARG C CG    1 
ATOM   5189 C  CD    . ARG F 2 58  ? -8.720  21.820 102.301 1.00 21.28 ? 58  ARG C CD    1 
ATOM   5190 N  NE    . ARG F 2 58  ? -7.546  22.668 102.534 1.00 25.23 ? 58  ARG C NE    1 
ATOM   5191 C  CZ    . ARG F 2 58  ? -7.599  23.935 102.964 1.00 25.17 ? 58  ARG C CZ    1 
ATOM   5192 N  NH1   . ARG F 2 58  ? -8.770  24.540 103.197 1.00 23.14 ? 58  ARG C NH1   1 
ATOM   5193 N  NH2   . ARG F 2 58  ? -6.515  24.684 103.210 1.00 22.82 ? 58  ARG C NH2   1 
ATOM   5194 N  N     . LEU F 2 59  ? -7.047  17.750 105.944 1.00 14.00 ? 59  LEU C N     1 
ATOM   5195 C  CA    . LEU F 2 59  ? -6.798  17.275 107.310 1.00 12.89 ? 59  LEU C CA    1 
ATOM   5196 C  C     . LEU F 2 59  ? -5.794  16.143 107.307 1.00 12.87 ? 59  LEU C C     1 
ATOM   5197 O  O     . LEU F 2 59  ? -5.905  15.192 106.518 1.00 12.98 ? 59  LEU C O     1 
ATOM   5198 C  CB    . LEU F 2 59  ? -8.093  16.747 107.932 1.00 10.87 ? 59  LEU C CB    1 
ATOM   5199 C  CG    . LEU F 2 59  ? -9.068  17.859 108.324 1.00 11.10 ? 59  LEU C CG    1 
ATOM   5200 C  CD1   . LEU F 2 59  ? -10.327 17.333 109.017 1.00 11.71 ? 59  LEU C CD1   1 
ATOM   5201 C  CD2   . LEU F 2 59  ? -8.457  18.877 109.290 1.00 10.36 ? 59  LEU C CD2   1 
ATOM   5202 N  N     . SER F 2 60  ? -4.843  16.289 108.193 1.00 12.83 ? 60  SER C N     1 
ATOM   5203 C  CA    . SER F 2 60  ? -3.821  15.280 108.393 1.00 12.70 ? 60  SER C CA    1 
ATOM   5204 C  C     . SER F 2 60  ? -4.491  14.066 109.008 1.00 13.38 ? 60  SER C C     1 
ATOM   5205 O  O     . SER F 2 60  ? -5.578  14.158 109.592 1.00 14.47 ? 60  SER C O     1 
ATOM   5206 C  CB    . SER F 2 60  ? -2.736  15.809 109.333 1.00 12.70 ? 60  SER C CB    1 
ATOM   5207 O  OG    . SER F 2 60  ? -3.118  15.599 110.685 1.00 14.98 ? 60  SER C OG    1 
ATOM   5208 N  N     . GLN F 2 61  ? -3.834  12.967 108.860 1.00 13.19 ? 61  GLN C N     1 
ATOM   5209 C  CA    . GLN F 2 61  ? -4.299  11.706 109.404 1.00 13.17 ? 61  GLN C CA    1 
ATOM   5210 C  C     . GLN F 2 61  ? -4.574  11.854 110.906 1.00 13.06 ? 61  GLN C C     1 
ATOM   5211 O  O     . GLN F 2 61  ? -5.720  11.768 111.366 1.00 13.15 ? 61  GLN C O     1 
ATOM   5212 C  CB    . GLN F 2 61  ? -3.232  10.652 109.171 1.00 16.36 ? 61  GLN C CB    1 
ATOM   5213 C  CG    . GLN F 2 61  ? -3.370  9.982  107.811 1.00 20.53 ? 61  GLN C CG    1 
ATOM   5214 C  CD    . GLN F 2 61  ? -4.301  8.777  107.856 1.00 25.29 ? 61  GLN C CD    1 
ATOM   5215 O  OE1   . GLN F 2 61  ? -3.895  7.675  107.494 1.00 27.11 ? 61  GLN C OE1   1 
ATOM   5216 N  NE2   . GLN F 2 61  ? -5.542  8.918  108.286 1.00 26.40 ? 61  GLN C NE2   1 
ATOM   5217 N  N     . PRO F 2 62  ? -3.579  12.079 111.771 1.00 13.17 ? 62  PRO C N     1 
ATOM   5218 C  CA    . PRO F 2 62  ? -3.851  12.206 113.189 1.00 13.66 ? 62  PRO C CA    1 
ATOM   5219 C  C     . PRO F 2 62  ? -4.812  13.340 113.440 1.00 14.22 ? 62  PRO C C     1 
ATOM   5220 O  O     . PRO F 2 62  ? -5.534  13.317 114.484 1.00 15.68 ? 62  PRO C O     1 
ATOM   5221 C  CB    . PRO F 2 62  ? -2.496  12.460 113.801 1.00 12.75 ? 62  PRO C CB    1 
ATOM   5222 C  CG    . PRO F 2 62  ? -1.472  12.462 112.676 1.00 12.83 ? 62  PRO C CG    1 
ATOM   5223 C  CD    . PRO F 2 62  ? -2.176  12.211 111.378 1.00 12.49 ? 62  PRO C CD    1 
ATOM   5224 N  N     . GLY F 2 63  ? -4.807  14.274 112.506 1.00 14.39 ? 63  GLY C N     1 
ATOM   5225 C  CA    . GLY F 2 63  ? -5.647  15.486 112.567 1.00 14.75 ? 63  GLY C CA    1 
ATOM   5226 C  C     . GLY F 2 63  ? -7.139  15.130 112.609 1.00 15.64 ? 63  GLY C C     1 
ATOM   5227 O  O     . GLY F 2 63  ? -7.898  15.660 113.434 1.00 16.63 ? 63  GLY C O     1 
ATOM   5228 N  N     . LEU F 2 64  ? -7.505  14.238 111.709 1.00 15.44 ? 64  LEU C N     1 
ATOM   5229 C  CA    . LEU F 2 64  ? -8.892  13.770 111.539 1.00 14.07 ? 64  LEU C CA    1 
ATOM   5230 C  C     . LEU F 2 64  ? -9.338  12.908 112.732 1.00 13.86 ? 64  LEU C C     1 
ATOM   5231 O  O     . LEU F 2 64  ? -10.452 13.060 113.252 1.00 14.69 ? 64  LEU C O     1 
ATOM   5232 C  CB    . LEU F 2 64  ? -8.986  12.928 110.263 1.00 10.86 ? 64  LEU C CB    1 
ATOM   5233 C  CG    . LEU F 2 64  ? -10.414 12.509 109.912 1.00 8.42  ? 64  LEU C CG    1 
ATOM   5234 C  CD1   . LEU F 2 64  ? -11.233 13.641 109.290 1.00 5.52  ? 64  LEU C CD1   1 
ATOM   5235 C  CD2   . LEU F 2 64  ? -10.466 11.357 108.905 1.00 6.52  ? 64  LEU C CD2   1 
ATOM   5236 N  N     . ALA F 2 65  ? -8.453  12.017 113.137 1.00 13.77 ? 65  ALA C N     1 
ATOM   5237 C  CA    . ALA F 2 65  ? -8.712  11.080 114.247 1.00 15.00 ? 65  ALA C CA    1 
ATOM   5238 C  C     . ALA F 2 65  ? -8.976  11.838 115.555 1.00 15.81 ? 65  ALA C C     1 
ATOM   5239 O  O     . ALA F 2 65  ? -9.630  11.318 116.473 1.00 17.59 ? 65  ALA C O     1 
ATOM   5240 C  CB    . ALA F 2 65  ? -7.497  10.174 114.462 1.00 14.93 ? 65  ALA C CB    1 
ATOM   5241 N  N     . PHE F 2 66  ? -8.457  13.050 115.594 1.00 15.43 ? 66  PHE C N     1 
ATOM   5242 C  CA    . PHE F 2 66  ? -8.548  13.933 116.771 1.00 14.20 ? 66  PHE C CA    1 
ATOM   5243 C  C     . PHE F 2 66  ? -9.945  14.558 116.889 1.00 13.84 ? 66  PHE C C     1 
ATOM   5244 O  O     . PHE F 2 66  ? -10.505 14.680 117.987 1.00 15.09 ? 66  PHE C O     1 
ATOM   5245 C  CB    . PHE F 2 66  ? -7.495  15.038 116.654 1.00 12.31 ? 66  PHE C CB    1 
ATOM   5246 C  CG    . PHE F 2 66  ? -7.775  16.258 117.534 1.00 12.05 ? 66  PHE C CG    1 
ATOM   5247 C  CD1   . PHE F 2 66  ? -7.644  16.168 118.926 1.00 11.55 ? 66  PHE C CD1   1 
ATOM   5248 C  CD2   . PHE F 2 66  ? -8.155  17.468 116.943 1.00 11.51 ? 66  PHE C CD2   1 
ATOM   5249 C  CE1   . PHE F 2 66  ? -7.893  17.291 119.726 1.00 9.43  ? 66  PHE C CE1   1 
ATOM   5250 C  CE2   . PHE F 2 66  ? -8.403  18.591 117.742 1.00 9.73  ? 66  PHE C CE2   1 
ATOM   5251 C  CZ    . PHE F 2 66  ? -8.271  18.503 119.133 1.00 7.76  ? 66  PHE C CZ    1 
ATOM   5252 N  N     . LEU F 2 67  ? -10.489 14.949 115.757 1.00 12.26 ? 67  LEU C N     1 
ATOM   5253 C  CA    . LEU F 2 67  ? -11.818 15.574 115.711 1.00 10.80 ? 67  LEU C CA    1 
ATOM   5254 C  C     . LEU F 2 67  ? -12.894 14.527 115.945 1.00 10.72 ? 67  LEU C C     1 
ATOM   5255 O  O     . LEU F 2 67  ? -13.913 14.799 116.601 1.00 10.74 ? 67  LEU C O     1 
ATOM   5256 C  CB    . LEU F 2 67  ? -12.036 16.227 114.357 1.00 8.14  ? 67  LEU C CB    1 
ATOM   5257 C  CG    . LEU F 2 67  ? -11.354 17.587 114.272 1.00 8.32  ? 67  LEU C CG    1 
ATOM   5258 C  CD1   . LEU F 2 67  ? -11.193 18.068 112.837 1.00 8.22  ? 67  LEU C CD1   1 
ATOM   5259 C  CD2   . LEU F 2 67  ? -12.116 18.691 115.011 1.00 7.68  ? 67  LEU C CD2   1 
ATOM   5260 N  N     . LYS F 2 68  ? -12.601 13.375 115.397 1.00 10.49 ? 68  LYS C N     1 
ATOM   5261 C  CA    . LYS F 2 68  ? -13.470 12.210 115.464 1.00 10.76 ? 68  LYS C CA    1 
ATOM   5262 C  C     . LYS F 2 68  ? -13.734 11.789 116.910 1.00 10.56 ? 68  LYS C C     1 
ATOM   5263 O  O     . LYS F 2 68  ? -14.882 11.574 117.317 1.00 9.43  ? 68  LYS C O     1 
ATOM   5264 C  CB    . LYS F 2 68  ? -12.832 11.045 114.739 1.00 11.10 ? 68  LYS C CB    1 
ATOM   5265 C  CG    . LYS F 2 68  ? -13.537 10.720 113.424 1.00 10.71 ? 68  LYS C CG    1 
ATOM   5266 C  CD    . LYS F 2 68  ? -13.131 9.366  112.848 1.00 11.52 ? 68  LYS C CD    1 
ATOM   5267 C  CE    . LYS F 2 68  ? -12.031 9.475  111.794 1.00 9.33  ? 68  LYS C CE    1 
ATOM   5268 N  NZ    . LYS F 2 68  ? -12.060 8.375  110.821 1.00 8.22  ? 68  LYS C NZ    1 
ATOM   5269 N  N     . CYS F 2 69  ? -12.657 11.676 117.646 1.00 10.43 ? 69  CYS C N     1 
ATOM   5270 C  CA    . CYS F 2 69  ? -12.689 11.269 119.058 1.00 10.85 ? 69  CYS C CA    1 
ATOM   5271 C  C     . CYS F 2 69  ? -13.284 12.413 119.906 1.00 10.19 ? 69  CYS C C     1 
ATOM   5272 O  O     . CYS F 2 69  ? -13.971 12.179 120.911 1.00 10.30 ? 69  CYS C O     1 
ATOM   5273 C  CB    . CYS F 2 69  ? -11.238 10.929 119.476 1.00 15.81 ? 69  CYS C CB    1 
ATOM   5274 S  SG    . CYS F 2 69  ? -10.964 10.638 121.294 1.00 26.51 ? 69  CYS C SG    1 
ATOM   5275 N  N     . ALA F 2 70  ? -13.014 13.621 119.444 1.00 8.61  ? 70  ALA C N     1 
ATOM   5276 C  CA    . ALA F 2 70  ? -13.394 14.867 120.134 1.00 8.49  ? 70  ALA C CA    1 
ATOM   5277 C  C     . ALA F 2 70  ? -14.909 15.167 120.115 1.00 9.45  ? 70  ALA C C     1 
ATOM   5278 O  O     . ALA F 2 70  ? -15.419 15.926 120.953 1.00 10.36 ? 70  ALA C O     1 
ATOM   5279 C  CB    . ALA F 2 70  ? -12.706 16.067 119.475 1.00 7.95  ? 70  ALA C CB    1 
ATOM   5280 N  N     . PHE F 2 71  ? -15.661 14.587 119.179 1.00 10.39 ? 71  PHE C N     1 
ATOM   5281 C  CA    . PHE F 2 71  ? -17.098 14.942 119.073 1.00 10.47 ? 71  PHE C CA    1 
ATOM   5282 C  C     . PHE F 2 71  ? -17.978 13.729 118.881 1.00 10.45 ? 71  PHE C C     1 
ATOM   5283 O  O     . PHE F 2 71  ? -19.185 13.766 119.172 1.00 11.96 ? 71  PHE C O     1 
ATOM   5284 C  CB    . PHE F 2 71  ? -17.295 15.918 117.901 1.00 10.70 ? 71  PHE C CB    1 
ATOM   5285 C  CG    . PHE F 2 71  ? -16.440 17.187 118.035 1.00 10.40 ? 71  PHE C CG    1 
ATOM   5286 C  CD1   . PHE F 2 71  ? -16.721 18.121 119.043 1.00 11.61 ? 71  PHE C CD1   1 
ATOM   5287 C  CD2   . PHE F 2 71  ? -15.375 17.417 117.153 1.00 10.25 ? 71  PHE C CD2   1 
ATOM   5288 C  CE1   . PHE F 2 71  ? -15.940 19.278 119.168 1.00 12.39 ? 71  PHE C CE1   1 
ATOM   5289 C  CE2   . PHE F 2 71  ? -14.594 18.575 117.279 1.00 11.47 ? 71  PHE C CE2   1 
ATOM   5290 C  CZ    . PHE F 2 71  ? -14.877 19.504 118.286 1.00 12.02 ? 71  PHE C CZ    1 
ATOM   5291 N  N     . ALA F 2 72  ? -17.441 12.622 118.406 1.00 10.55 ? 72  ALA C N     1 
ATOM   5292 C  CA    . ALA F 2 72  ? -18.350 11.475 118.250 1.00 10.27 ? 72  ALA C CA    1 
ATOM   5293 C  C     . ALA F 2 72  ? -17.696 10.096 118.455 1.00 10.27 ? 72  ALA C C     1 
ATOM   5294 O  O     . ALA F 2 72  ? -17.656 9.271  117.540 1.00 10.97 ? 72  ALA C O     1 
ATOM   5295 C  CB    . ALA F 2 72  ? -18.975 11.495 116.857 1.00 9.41  ? 72  ALA C CB    1 
ATOM   5296 N  N     . PRO F 2 73  ? -17.169 9.721  119.643 1.00 10.10 ? 73  PRO C N     1 
ATOM   5297 C  CA    . PRO F 2 73  ? -16.542 8.401  119.833 1.00 10.05 ? 73  PRO C CA    1 
ATOM   5298 C  C     . PRO F 2 73  ? -17.500 7.214  119.657 1.00 9.92  ? 73  PRO C C     1 
ATOM   5299 O  O     . PRO F 2 73  ? -17.063 6.137  119.140 1.00 9.83  ? 73  PRO C O     1 
ATOM   5300 C  CB    . PRO F 2 73  ? -16.054 8.424  121.262 1.00 9.85  ? 73  PRO C CB    1 
ATOM   5301 C  CG    . PRO F 2 73  ? -16.438 9.770  121.864 1.00 10.00 ? 73  PRO C CG    1 
ATOM   5302 C  CD    . PRO F 2 73  ? -17.162 10.581 120.831 1.00 10.12 ? 73  PRO C CD    1 
ATOM   5303 N  N     . PRO F 2 74  ? -18.789 7.307  120.046 1.00 9.91  ? 74  PRO C N     1 
ATOM   5304 C  CA    . PRO F 2 74  ? -19.724 6.165  119.997 1.00 9.53  ? 74  PRO C CA    1 
ATOM   5305 C  C     . PRO F 2 74  ? -19.985 5.592  118.610 1.00 9.65  ? 74  PRO C C     1 
ATOM   5306 O  O     . PRO F 2 74  ? -20.586 4.476  118.506 1.00 9.34  ? 74  PRO C O     1 
ATOM   5307 C  CB    . PRO F 2 74  ? -21.015 6.721  120.542 1.00 8.86  ? 74  PRO C CB    1 
ATOM   5308 C  CG    . PRO F 2 74  ? -20.787 8.187  120.886 1.00 9.29  ? 74  PRO C CG    1 
ATOM   5309 C  CD    . PRO F 2 74  ? -19.371 8.551  120.561 1.00 9.74  ? 74  PRO C CD    1 
ATOM   5310 N  N     . ASP F 2 75  ? -19.563 6.297  117.580 1.00 11.00 ? 75  ASP C N     1 
ATOM   5311 C  CA    . ASP F 2 75  ? -19.839 5.892  116.181 1.00 12.00 ? 75  ASP C CA    1 
ATOM   5312 C  C     . ASP F 2 75  ? -18.843 4.856  115.649 1.00 13.50 ? 75  ASP C C     1 
ATOM   5313 O  O     . ASP F 2 75  ? -19.153 4.084  114.728 1.00 15.00 ? 75  ASP C O     1 
ATOM   5314 C  CB    . ASP F 2 75  ? -19.770 7.110  115.265 1.00 15.00 ? 75  ASP C CB    1 
ATOM   5315 C  CG    . ASP F 2 75  ? -20.761 8.199  115.670 1.00 20.00 ? 75  ASP C CG    1 
ATOM   5316 O  OD1   . ASP F 2 75  ? -21.960 7.878  116.021 1.00 22.30 ? 75  ASP C OD1   1 
ATOM   5317 O  OD2   . ASP F 2 75  ? -20.399 9.436  115.662 1.00 24.00 ? 75  ASP C OD2   1 
ATOM   5318 N  N     . PHE F 2 76  ? -17.671 4.859  116.240 1.00 13.11 ? 76  PHE C N     1 
ATOM   5319 C  CA    . PHE F 2 76  ? -16.581 3.973  115.816 1.00 12.63 ? 76  PHE C CA    1 
ATOM   5320 C  C     . PHE F 2 76  ? -16.490 2.754  116.684 1.00 12.48 ? 76  PHE C C     1 
ATOM   5321 O  O     . PHE F 2 76  ? -16.739 2.810  117.898 1.00 12.65 ? 76  PHE C O     1 
ATOM   5322 C  CB    . PHE F 2 76  ? -15.263 4.720  115.897 1.00 13.77 ? 76  PHE C CB    1 
ATOM   5323 C  CG    . PHE F 2 76  ? -15.337 6.035  115.148 1.00 14.69 ? 76  PHE C CG    1 
ATOM   5324 C  CD1   . PHE F 2 76  ? -15.016 6.071  113.792 1.00 14.50 ? 76  PHE C CD1   1 
ATOM   5325 C  CD2   . PHE F 2 76  ? -15.742 7.192  115.818 1.00 14.78 ? 76  PHE C CD2   1 
ATOM   5326 C  CE1   . PHE F 2 76  ? -15.098 7.276  113.093 1.00 15.36 ? 76  PHE C CE1   1 
ATOM   5327 C  CE2   . PHE F 2 76  ? -15.826 8.399  115.121 1.00 16.97 ? 76  PHE C CE2   1 
ATOM   5328 C  CZ    . PHE F 2 76  ? -15.504 8.441  113.757 1.00 16.84 ? 76  PHE C CZ    1 
ATOM   5329 N  N     . ASN F 2 77  ? -16.133 1.693  116.016 1.00 12.28 ? 77  ASN C N     1 
ATOM   5330 C  CA    . ASN F 2 77  ? -15.932 0.435  116.675 1.00 12.48 ? 77  ASN C CA    1 
ATOM   5331 C  C     . ASN F 2 77  ? -14.675 0.538  117.550 1.00 12.75 ? 77  ASN C C     1 
ATOM   5332 O  O     . ASN F 2 77  ? -14.598 -0.071 118.626 1.00 12.30 ? 77  ASN C O     1 
ATOM   5333 C  CB    . ASN F 2 77  ? -15.755 -0.695 115.666 1.00 13.55 ? 77  ASN C CB    1 
ATOM   5334 C  CG    . ASN F 2 77  ? -16.051 -2.070 116.270 1.00 16.05 ? 77  ASN C CG    1 
ATOM   5335 O  OD1   . ASN F 2 77  ? -16.211 -2.184 117.485 1.00 18.23 ? 77  ASN C OD1   1 
ATOM   5336 N  ND2   . ASN F 2 77  ? -16.136 -3.130 115.490 1.00 15.64 ? 77  ASN C ND2   1 
ATOM   5337 N  N     . THR F 2 78  ? -13.723 1.325  117.049 1.00 13.39 ? 78  THR C N     1 
ATOM   5338 C  CA    . THR F 2 78  ? -12.436 1.575  117.739 1.00 14.87 ? 78  THR C CA    1 
ATOM   5339 C  C     . THR F 2 78  ? -12.102 3.075  117.750 1.00 15.59 ? 78  THR C C     1 
ATOM   5340 O  O     . THR F 2 78  ? -12.392 3.801  116.784 1.00 15.59 ? 78  THR C O     1 
ATOM   5341 C  CB    . THR F 2 78  ? -11.292 0.837  117.046 1.00 16.42 ? 78  THR C CB    1 
ATOM   5342 O  OG1   . THR F 2 78  ? -11.520 -0.565 117.100 1.00 16.34 ? 78  THR C OG1   1 
ATOM   5343 C  CG2   . THR F 2 78  ? -9.935  1.113  117.701 1.00 17.44 ? 78  THR C CG2   1 
ATOM   5344 N  N     . ASP F 2 79  ? -11.475 3.483  118.854 1.00 16.23 ? 79  ASP C N     1 
ATOM   5345 C  CA    . ASP F 2 79  ? -11.119 4.892  119.095 1.00 18.18 ? 79  ASP C CA    1 
ATOM   5346 C  C     . ASP F 2 79  ? -9.937  5.309  118.242 1.00 19.00 ? 79  ASP C C     1 
ATOM   5347 O  O     . ASP F 2 79  ? -8.794  4.861  118.476 1.00 18.74 ? 79  ASP C O     1 
ATOM   5348 C  CB    . ASP F 2 79  ? -10.864 5.144  120.568 1.00 23.18 ? 79  ASP C CB    1 
ATOM   5349 C  CG    . ASP F 2 79  ? -12.141 5.621  121.255 1.00 28.73 ? 79  ASP C CG    1 
ATOM   5350 O  OD1   . ASP F 2 79  ? -13.003 6.321  120.591 1.00 30.30 ? 79  ASP C OD1   1 
ATOM   5351 O  OD2   . ASP F 2 79  ? -12.362 5.314  122.482 1.00 29.67 ? 79  ASP C OD2   1 
ATOM   5352 N  N     . PRO F 2 80  ? -10.250 6.176  117.280 1.00 19.99 ? 80  PRO C N     1 
ATOM   5353 C  CA    . PRO F 2 80  ? -9.301  6.660  116.303 1.00 20.07 ? 80  PRO C CA    1 
ATOM   5354 C  C     . PRO F 2 80  ? -8.196  7.464  116.926 1.00 20.29 ? 80  PRO C C     1 
ATOM   5355 O  O     . PRO F 2 80  ? -7.079  7.529  116.338 1.00 20.66 ? 80  PRO C O     1 
ATOM   5356 C  CB    . PRO F 2 80  ? -10.110 7.587  115.429 1.00 20.15 ? 80  PRO C CB    1 
ATOM   5357 C  CG    . PRO F 2 80  ? -11.523 7.631  115.978 1.00 20.43 ? 80  PRO C CG    1 
ATOM   5358 C  CD    . PRO F 2 80  ? -11.612 6.706  117.142 1.00 19.81 ? 80  PRO C CD    1 
ATOM   5359 N  N     . GLY F 2 81  ? -8.511  8.057  118.056 1.00 20.31 ? 81  GLY C N     1 
ATOM   5360 C  CA    . GLY F 2 81  ? -7.589  8.959  118.781 1.00 20.42 ? 81  GLY C CA    1 
ATOM   5361 C  C     . GLY F 2 81  ? -6.132  8.452  118.785 1.00 21.05 ? 81  GLY C C     1 
ATOM   5362 O  O     . GLY F 2 81  ? -5.868  7.260  119.005 1.00 22.11 ? 81  GLY C O     1 
ATOM   5363 N  N     . LYS F 2 82  ? -5.222  9.405  118.538 1.00 21.02 ? 82  LYS C N     1 
ATOM   5364 C  CA    . LYS F 2 82  ? -3.757  9.167  118.582 1.00 20.29 ? 82  LYS C CA    1 
ATOM   5365 C  C     . LYS F 2 82  ? -3.074  10.200 119.487 1.00 19.47 ? 82  LYS C C     1 
ATOM   5366 O  O     . LYS F 2 82  ? -2.105  9.892  120.195 1.00 19.47 ? 82  LYS C O     1 
ATOM   5367 C  CB    . LYS F 2 82  ? -3.082  9.271  117.210 1.00 20.50 ? 82  LYS C CB    1 
ATOM   5368 C  CG    . LYS F 2 82  ? -1.583  9.637  117.317 1.00 20.75 ? 82  LYS C CG    1 
ATOM   5369 C  CD    . LYS F 2 82  ? -0.636  8.423  117.282 1.00 21.28 ? 82  LYS C CD    1 
ATOM   5370 C  CE    . LYS F 2 82  ? 0.850   8.815  117.351 1.00 20.10 ? 82  LYS C CE    1 
ATOM   5371 N  NZ    . LYS F 2 82  ? 1.750   7.776  116.823 1.00 18.90 ? 82  LYS C NZ    1 
ATOM   5372 N  N     . GLY F 2 83  ? -3.576  11.410 119.460 1.00 18.36 ? 83  GLY C N     1 
ATOM   5373 C  CA    . GLY F 2 83  ? -3.018  12.497 120.279 1.00 17.33 ? 83  GLY C CA    1 
ATOM   5374 C  C     . GLY F 2 83  ? -3.534  13.843 119.767 1.00 15.64 ? 83  GLY C C     1 
ATOM   5375 O  O     . GLY F 2 83  ? -4.302  13.862 118.791 1.00 16.95 ? 83  GLY C O     1 
ATOM   5376 N  N     . ILE F 2 84  ? -3.091  14.898 120.400 1.00 12.14 ? 84  ILE C N     1 
ATOM   5377 C  CA    . ILE F 2 84  ? -3.482  16.262 120.024 1.00 10.15 ? 84  ILE C CA    1 
ATOM   5378 C  C     . ILE F 2 84  ? -2.502  16.778 118.979 1.00 10.63 ? 84  ILE C C     1 
ATOM   5379 O  O     . ILE F 2 84  ? -1.306  16.985 119.221 1.00 11.78 ? 84  ILE C O     1 
ATOM   5380 C  CB    . ILE F 2 84  ? -3.619  17.146 121.309 1.00 8.31  ? 84  ILE C CB    1 
ATOM   5381 C  CG1   . ILE F 2 84  ? -4.606  16.462 122.299 1.00 7.45  ? 84  ILE C CG1   1 
ATOM   5382 C  CG2   . ILE F 2 84  ? -4.016  18.612 120.953 1.00 7.95  ? 84  ILE C CG2   1 
ATOM   5383 C  CD1   . ILE F 2 84  ? -4.834  17.245 123.615 1.00 25.00 ? 84  ILE C CD1   1 
ATOM   5384 N  N     . PRO F 2 85  ? -3.031  16.983 117.783 1.00 10.35 ? 85  PRO C N     1 
ATOM   5385 C  CA    . PRO F 2 85  ? -2.258  17.470 116.634 1.00 10.59 ? 85  PRO C CA    1 
ATOM   5386 C  C     . PRO F 2 85  ? -1.876  18.928 116.768 1.00 12.36 ? 85  PRO C C     1 
ATOM   5387 O  O     . PRO F 2 85  ? -2.237  19.743 115.903 1.00 14.20 ? 85  PRO C O     1 
ATOM   5388 C  CB    . PRO F 2 85  ? -3.219  17.275 115.459 1.00 9.72  ? 85  PRO C CB    1 
ATOM   5389 C  CG    . PRO F 2 85  ? -4.554  17.578 116.138 1.00 9.80  ? 85  PRO C CG    1 
ATOM   5390 C  CD    . PRO F 2 85  ? -4.447  16.751 117.423 1.00 10.20 ? 85  PRO C CD    1 
ATOM   5391 N  N     . ASP F 2 86  ? -1.140  19.231 117.820 1.00 12.95 ? 86  ASP C N     1 
ATOM   5392 C  CA    . ASP F 2 86  ? -0.699  20.609 118.091 1.00 12.81 ? 86  ASP C CA    1 
ATOM   5393 C  C     . ASP F 2 86  ? 0.834   20.644 118.072 1.00 13.61 ? 86  ASP C C     1 
ATOM   5394 O  O     . ASP F 2 86  ? 1.475   19.623 117.784 1.00 14.92 ? 86  ASP C O     1 
ATOM   5395 C  CB    . ASP F 2 86  ? -1.311  21.132 119.374 1.00 12.59 ? 86  ASP C CB    1 
ATOM   5396 C  CG    . ASP F 2 86  ? -0.460  20.780 120.577 1.00 13.03 ? 86  ASP C CG    1 
ATOM   5397 O  OD1   . ASP F 2 86  ? 0.253   19.759 120.570 1.00 13.32 ? 86  ASP C OD1   1 
ATOM   5398 O  OD2   . ASP F 2 86  ? -0.549  21.574 121.543 1.00 13.32 ? 86  ASP C OD2   1 
ATOM   5399 N  N     . ARG F 2 87  ? 1.351   21.803 118.422 1.00 12.83 ? 87  ARG C N     1 
ATOM   5400 C  CA    . ARG F 2 87  ? 2.762   22.125 118.422 1.00 13.12 ? 87  ARG C CA    1 
ATOM   5401 C  C     . ARG F 2 87  ? 3.677   21.192 119.173 1.00 13.72 ? 87  ARG C C     1 
ATOM   5402 O  O     . ARG F 2 87  ? 4.854   21.043 118.743 1.00 14.89 ? 87  ARG C O     1 
ATOM   5403 C  CB    . ARG F 2 87  ? 2.997   23.607 118.821 1.00 13.06 ? 87  ARG C CB    1 
ATOM   5404 C  CG    . ARG F 2 87  ? 4.216   24.166 118.085 1.00 13.90 ? 87  ARG C CG    1 
ATOM   5405 C  CD    . ARG F 2 87  ? 4.199   25.626 117.846 1.00 15.77 ? 87  ARG C CD    1 
ATOM   5406 N  NE    . ARG F 2 87  ? 4.375   25.878 116.432 1.00 17.20 ? 87  ARG C NE    1 
ATOM   5407 C  CZ    . ARG F 2 87  ? 3.982   26.935 115.724 1.00 17.07 ? 87  ARG C CZ    1 
ATOM   5408 N  NH1   . ARG F 2 87  ? 3.340   27.977 116.242 1.00 13.30 ? 87  ARG C NH1   1 
ATOM   5409 N  NH2   . ARG F 2 87  ? 4.247   26.897 114.400 1.00 17.77 ? 87  ARG C NH2   1 
ATOM   5410 N  N     . PHE F 2 88  ? 3.206   20.579 120.239 1.00 12.82 ? 88  PHE C N     1 
ATOM   5411 C  CA    . PHE F 2 88  ? 4.025   19.654 121.049 1.00 12.07 ? 88  PHE C CA    1 
ATOM   5412 C  C     . PHE F 2 88  ? 4.061   18.288 120.362 1.00 12.41 ? 88  PHE C C     1 
ATOM   5413 O  O     . PHE F 2 88  ? 3.038   17.732 119.907 1.00 13.18 ? 88  PHE C O     1 
ATOM   5414 C  CB    . PHE F 2 88  ? 3.555   19.626 122.495 1.00 10.63 ? 88  PHE C CB    1 
ATOM   5415 C  CG    . PHE F 2 88  ? 4.022   18.538 123.404 1.00 11.42 ? 88  PHE C CG    1 
ATOM   5416 C  CD1   . PHE F 2 88  ? 3.389   17.303 123.441 1.00 12.66 ? 88  PHE C CD1   1 
ATOM   5417 C  CD2   . PHE F 2 88  ? 5.102   18.736 124.261 1.00 12.28 ? 88  PHE C CD2   1 
ATOM   5418 C  CE1   . PHE F 2 88  ? 3.808   16.270 124.276 1.00 10.93 ? 88  PHE C CE1   1 
ATOM   5419 C  CE2   . PHE F 2 88  ? 5.540   17.727 125.117 1.00 11.09 ? 88  PHE C CE2   1 
ATOM   5420 C  CZ    . PHE F 2 88  ? 4.891   16.488 125.110 1.00 9.19  ? 88  PHE C CZ    1 
ATOM   5421 N  N     . GLU F 2 89  ? 5.272   17.772 120.303 1.00 11.32 ? 89  GLU C N     1 
ATOM   5422 C  CA    . GLU F 2 89  ? 5.604   16.478 119.716 1.00 11.15 ? 89  GLU C CA    1 
ATOM   5423 C  C     . GLU F 2 89  ? 6.456   15.619 120.629 1.00 11.35 ? 89  GLU C C     1 
ATOM   5424 O  O     . GLU F 2 89  ? 7.370   14.894 120.200 1.00 12.15 ? 89  GLU C O     1 
ATOM   5425 C  CB    . GLU F 2 89  ? 6.383   16.732 118.432 1.00 11.40 ? 89  GLU C CB    1 
ATOM   5426 C  CG    . GLU F 2 89  ? 5.659   16.601 117.105 1.00 13.65 ? 89  GLU C CG    1 
ATOM   5427 C  CD    . GLU F 2 89  ? 6.162   17.498 116.001 1.00 15.64 ? 89  GLU C CD    1 
ATOM   5428 O  OE1   . GLU F 2 89  ? 5.821   18.669 115.833 1.00 18.27 ? 89  GLU C OE1   1 
ATOM   5429 O  OE2   . GLU F 2 89  ? 6.945   16.864 115.267 1.00 15.26 ? 89  GLU C OE2   1 
ATOM   5430 N  N     . GLY F 2 90  ? 6.201   15.654 121.916 1.00 11.06 ? 90  GLY C N     1 
ATOM   5431 C  CA    . GLY F 2 90  ? 6.934   14.926 122.957 1.00 11.13 ? 90  GLY C CA    1 
ATOM   5432 C  C     . GLY F 2 90  ? 6.314   13.570 123.260 1.00 11.00 ? 90  GLY C C     1 
ATOM   5433 O  O     . GLY F 2 90  ? 5.314   13.250 122.612 1.00 12.30 ? 90  GLY C O     1 
ATOM   5434 N  N     . LYS F 2 91  ? 6.926   12.865 124.184 1.00 9.55  ? 91  LYS C N     1 
ATOM   5435 C  CA    . LYS F 2 91  ? 6.533   11.525 124.620 1.00 9.42  ? 91  LYS C CA    1 
ATOM   5436 C  C     . LYS F 2 91  ? 5.271   11.608 125.475 1.00 9.00  ? 91  LYS C C     1 
ATOM   5437 O  O     . LYS F 2 91  ? 5.214   12.364 126.466 1.00 9.26  ? 91  LYS C O     1 
ATOM   5438 C  CB    . LYS F 2 91  ? 7.635   10.857 125.409 1.00 10.30 ? 91  LYS C CB    1 
ATOM   5439 C  CG    . LYS F 2 91  ? 7.606   9.330  125.499 1.00 8.76  ? 91  LYS C CG    1 
ATOM   5440 C  CD    . LYS F 2 91  ? 8.496   8.771  124.398 1.00 11.35 ? 91  LYS C CD    1 
ATOM   5441 C  CE    . LYS F 2 91  ? 9.105   7.440  124.748 1.00 13.51 ? 91  LYS C CE    1 
ATOM   5442 N  NZ    . LYS F 2 91  ? 8.378   6.343  124.062 1.00 15.02 ? 91  LYS C NZ    1 
ATOM   5443 N  N     . VAL F 2 92  ? 4.299   10.811 125.081 1.00 8.24  ? 92  VAL C N     1 
ATOM   5444 C  CA    . VAL F 2 92  ? 2.989   10.734 125.717 1.00 8.02  ? 92  VAL C CA    1 
ATOM   5445 C  C     . VAL F 2 92  ? 2.392   9.342  125.481 1.00 8.55  ? 92  VAL C C     1 
ATOM   5446 O  O     . VAL F 2 92  ? 2.745   8.655  124.515 1.00 8.39  ? 92  VAL C O     1 
ATOM   5447 C  CB    . VAL F 2 92  ? 2.034   11.732 124.988 1.00 3.95  ? 92  VAL C CB    1 
ATOM   5448 C  CG1   . VAL F 2 92  ? 2.587   13.156 124.920 1.00 4.10  ? 92  VAL C CG1   1 
ATOM   5449 C  CG2   . VAL F 2 92  ? 1.741   11.324 123.543 1.00 2.76  ? 92  VAL C CG2   1 
ATOM   5450 N  N     . VAL F 2 93  ? 1.511   8.939  126.375 1.00 8.35  ? 93  VAL C N     1 
ATOM   5451 C  CA    . VAL F 2 93  ? 0.714   7.713  126.180 1.00 8.85  ? 93  VAL C CA    1 
ATOM   5452 C  C     . VAL F 2 93  ? -0.735  8.151  126.189 1.00 9.38  ? 93  VAL C C     1 
ATOM   5453 O  O     . VAL F 2 93  ? -1.242  8.661  127.194 1.00 10.10 ? 93  VAL C O     1 
ATOM   5454 C  CB    . VAL F 2 93  ? 0.938   6.644  127.261 1.00 6.36  ? 93  VAL C CB    1 
ATOM   5455 C  CG1   . VAL F 2 93  ? 1.986   7.021  128.296 1.00 5.70  ? 93  VAL C CG1   1 
ATOM   5456 C  CG2   . VAL F 2 93  ? -0.339  6.321  128.049 1.00 4.33  ? 93  VAL C CG2   1 
ATOM   5457 N  N     . THR F 2 94  ? -1.368  7.973  125.062 1.00 9.51  ? 94  THR C N     1 
ATOM   5458 C  CA    . THR F 2 94  ? -2.751  8.405  124.892 1.00 10.16 ? 94  THR C CA    1 
ATOM   5459 C  C     . THR F 2 94  ? -3.705  7.369  125.497 1.00 9.79  ? 94  THR C C     1 
ATOM   5460 O  O     . THR F 2 94  ? -3.992  6.329  124.888 1.00 9.62  ? 94  THR C O     1 
ATOM   5461 C  CB    . THR F 2 94  ? -3.018  8.630  123.404 1.00 11.52 ? 94  THR C CB    1 
ATOM   5462 O  OG1   . THR F 2 94  ? -2.762  7.442  122.674 1.00 15.01 ? 94  THR C OG1   1 
ATOM   5463 C  CG2   . THR F 2 94  ? -2.129  9.729  122.804 1.00 11.21 ? 94  THR C CG2   1 
ATOM   5464 N  N     . ARG F 2 95  ? -4.167  7.701  126.696 1.00 9.48  ? 95  ARG C N     1 
ATOM   5465 C  CA    . ARG F 2 95  ? -5.104  6.859  127.460 1.00 9.08  ? 95  ARG C CA    1 
ATOM   5466 C  C     . ARG F 2 95  ? -6.517  7.032  126.904 1.00 8.70  ? 95  ARG C C     1 
ATOM   5467 O  O     . ARG F 2 95  ? -6.968  8.153  126.639 1.00 9.80  ? 95  ARG C O     1 
ATOM   5468 C  CB    . ARG F 2 95  ? -5.094  7.259  128.939 1.00 8.30  ? 95  ARG C CB    1 
ATOM   5469 C  CG    . ARG F 2 95  ? -4.931  6.059  129.876 1.00 8.97  ? 95  ARG C CG    1 
ATOM   5470 C  CD    . ARG F 2 95  ? -6.266  5.505  130.380 1.00 13.10 ? 95  ARG C CD    1 
ATOM   5471 N  NE    . ARG F 2 95  ? -6.388  4.046  130.227 1.00 11.78 ? 95  ARG C NE    1 
ATOM   5472 C  CZ    . ARG F 2 95  ? -6.973  3.248  131.132 1.00 14.14 ? 95  ARG C CZ    1 
ATOM   5473 N  NH1   . ARG F 2 95  ? -7.489  3.752  132.262 1.00 15.01 ? 95  ARG C NH1   1 
ATOM   5474 N  NH2   . ARG F 2 95  ? -7.094  1.920  130.998 1.00 17.56 ? 95  ARG C NH2   1 
ATOM   5475 N  N     . LYS F 2 96  ? -7.189  5.909  126.734 1.00 7.23  ? 96  LYS C N     1 
ATOM   5476 C  CA    . LYS F 2 96  ? -8.555  5.896  126.194 1.00 7.30  ? 96  LYS C CA    1 
ATOM   5477 C  C     . LYS F 2 96  ? -9.529  5.304  127.206 1.00 7.54  ? 96  LYS C C     1 
ATOM   5478 O  O     . LYS F 2 96  ? -9.761  4.080  127.194 1.00 8.62  ? 96  LYS C O     1 
ATOM   5479 C  CB    . LYS F 2 96  ? -8.613  5.063  124.911 1.00 7.79  ? 96  LYS C CB    1 
ATOM   5480 C  CG    . LYS F 2 96  ? -8.316  5.877  123.648 1.00 10.98 ? 96  LYS C CG    1 
ATOM   5481 C  CD    . LYS F 2 96  ? -6.865  5.740  123.187 1.00 13.37 ? 96  LYS C CD    1 
ATOM   5482 C  CE    . LYS F 2 96  ? -6.721  5.666  121.667 1.00 16.15 ? 96  LYS C CE    1 
ATOM   5483 N  NZ    . LYS F 2 96  ? -7.018  6.942  121.002 1.00 17.38 ? 96  LYS C NZ    1 
ATOM   5484 N  N     . ASP F 2 97  ? -10.082 6.126  128.054 1.00 7.00  ? 97  ASP C N     1 
ATOM   5485 C  CA    . ASP F 2 97  ? -10.994 5.810  129.125 1.00 7.91  ? 97  ASP C CA    1 
ATOM   5486 C  C     . ASP F 2 97  ? -12.435 5.655  128.699 1.00 8.69  ? 97  ASP C C     1 
ATOM   5487 O  O     . ASP F 2 97  ? -12.988 6.619  128.141 1.00 9.56  ? 97  ASP C O     1 
ATOM   5488 C  CB    . ASP F 2 97  ? -10.990 6.994  130.134 1.00 9.50  ? 97  ASP C CB    1 
ATOM   5489 C  CG    . ASP F 2 97  ? -9.821  6.883  131.085 1.00 13.52 ? 97  ASP C CG    1 
ATOM   5490 O  OD1   . ASP F 2 97  ? -9.714  5.755  131.609 1.00 15.53 ? 97  ASP C OD1   1 
ATOM   5491 O  OD2   . ASP F 2 97  ? -9.074  7.855  131.306 1.00 17.38 ? 97  ASP C OD2   1 
ATOM   5492 N  N     . VAL F 2 98  ? -13.056 4.564  129.063 1.00 8.52  ? 98  VAL C N     1 
ATOM   5493 C  CA    . VAL F 2 98  ? -14.490 4.408  128.732 1.00 7.72  ? 98  VAL C CA    1 
ATOM   5494 C  C     . VAL F 2 98  ? -15.166 3.742  129.931 1.00 7.22  ? 98  VAL C C     1 
ATOM   5495 O  O     . VAL F 2 98  ? -14.595 2.803  130.494 1.00 7.86  ? 98  VAL C O     1 
ATOM   5496 C  CB    . VAL F 2 98  ? -14.604 3.537  127.477 1.00 5.89  ? 98  VAL C CB    1 
ATOM   5497 C  CG1   . VAL F 2 98  ? -15.704 4.012  126.547 1.00 4.21  ? 98  VAL C CG1   1 
ATOM   5498 C  CG2   . VAL F 2 98  ? -13.237 3.482  126.829 1.00 9.28  ? 98  VAL C CG2   1 
ATOM   5499 N  N     . LEU F 2 99  ? -16.344 4.247  130.231 1.00 6.85  ? 99  LEU C N     1 
ATOM   5500 C  CA    . LEU F 2 99  ? -17.165 3.736  131.317 1.00 7.52  ? 99  LEU C CA    1 
ATOM   5501 C  C     . LEU F 2 99  ? -18.544 3.335  130.780 1.00 8.12  ? 99  LEU C C     1 
ATOM   5502 O  O     . LEU F 2 99  ? -19.228 4.043  130.015 1.00 7.24  ? 99  LEU C O     1 
ATOM   5503 C  CB    . LEU F 2 99  ? -17.234 4.803  132.424 1.00 6.87  ? 99  LEU C CB    1 
ATOM   5504 C  CG    . LEU F 2 99  ? -18.089 4.418  133.626 1.00 4.57  ? 99  LEU C CG    1 
ATOM   5505 C  CD1   . LEU F 2 99  ? -17.197 3.979  134.767 1.00 5.58  ? 99  LEU C CD1   1 
ATOM   5506 C  CD2   . LEU F 2 99  ? -18.884 5.631  134.087 1.00 6.14  ? 99  LEU C CD2   1 
ATOM   5507 N  N     . ASN F 2 100 ? -18.900 2.159  131.248 1.00 9.43  ? 100 ASN C N     1 
ATOM   5508 C  CA    . ASN F 2 100 ? -20.216 1.556  130.954 1.00 10.04 ? 100 ASN C CA    1 
ATOM   5509 C  C     . ASN F 2 100 ? -20.829 1.421  132.359 1.00 10.37 ? 100 ASN C C     1 
ATOM   5510 O  O     . ASN F 2 100 ? -20.420 0.515  133.123 1.00 10.70 ? 100 ASN C O     1 
ATOM   5511 C  CB    . ASN F 2 100 ? -20.085 0.246  130.214 1.00 10.15 ? 100 ASN C CB    1 
ATOM   5512 C  CG    . ASN F 2 100 ? -21.375 -0.069 129.467 1.00 10.34 ? 100 ASN C CG    1 
ATOM   5513 O  OD1   . ASN F 2 100 ? -22.434 0.018  130.083 1.00 11.64 ? 100 ASN C OD1   1 
ATOM   5514 N  ND2   . ASN F 2 100 ? -21.309 -0.411 128.205 1.00 10.34 ? 100 ASN C ND2   1 
ATOM   5515 N  N     . GLN F 2 101 ? -21.703 2.345  132.680 1.00 10.00 ? 101 GLN C N     1 
ATOM   5516 C  CA    . GLN F 2 101 ? -22.294 2.322  134.036 1.00 10.73 ? 101 GLN C CA    1 
ATOM   5517 C  C     . GLN F 2 101 ? -23.809 2.226  134.022 1.00 11.11 ? 101 GLN C C     1 
ATOM   5518 O  O     . GLN F 2 101 ? -24.535 3.039  133.422 1.00 10.86 ? 101 GLN C O     1 
ATOM   5519 C  CB    . GLN F 2 101 ? -21.840 3.563  134.804 1.00 11.39 ? 101 GLN C CB    1 
ATOM   5520 C  CG    . GLN F 2 101 ? -22.408 3.630  136.198 1.00 11.96 ? 101 GLN C CG    1 
ATOM   5521 C  CD    . GLN F 2 101 ? -21.654 2.672  137.097 1.00 14.81 ? 101 GLN C CD    1 
ATOM   5522 O  OE1   . GLN F 2 101 ? -20.965 1.767  136.636 1.00 16.89 ? 101 GLN C OE1   1 
ATOM   5523 N  NE2   . GLN F 2 101 ? -21.797 2.939  138.395 1.00 14.35 ? 101 GLN C NE2   1 
ATOM   5524 N  N     . SER F 2 102 ? -24.243 1.186  134.743 1.00 11.37 ? 102 SER C N     1 
ATOM   5525 C  CA    . SER F 2 102 ? -25.718 0.990  134.872 1.00 11.94 ? 102 SER C CA    1 
ATOM   5526 C  C     . SER F 2 102 ? -26.117 2.061  135.890 1.00 12.31 ? 102 SER C C     1 
ATOM   5527 O  O     . SER F 2 102 ? -25.316 2.201  136.848 1.00 14.25 ? 102 SER C O     1 
ATOM   5528 C  CB    . SER F 2 102 ? -26.016 -0.380 135.423 1.00 11.69 ? 102 SER C CB    1 
ATOM   5529 O  OG    . SER F 2 102 ? -25.894 -1.321 134.340 1.00 17.43 ? 102 SER C OG    1 
ATOM   5530 N  N     . ILE F 2 103 ? -27.212 2.739  135.682 1.00 11.38 ? 103 ILE C N     1 
ATOM   5531 C  CA    . ILE F 2 103 ? -27.587 3.786  136.671 1.00 11.53 ? 103 ILE C CA    1 
ATOM   5532 C  C     . ILE F 2 103 ? -29.077 3.923  136.858 1.00 11.81 ? 103 ILE C C     1 
ATOM   5533 O  O     . ILE F 2 103 ? -29.859 4.177  135.922 1.00 13.09 ? 103 ILE C O     1 
ATOM   5534 C  CB    . ILE F 2 103 ? -26.804 5.066  136.214 1.00 11.20 ? 103 ILE C CB    1 
ATOM   5535 C  CG1   . ILE F 2 103 ? -27.035 6.226  137.201 1.00 11.74 ? 103 ILE C CG1   1 
ATOM   5536 C  CG2   . ILE F 2 103 ? -27.143 5.482  134.765 1.00 10.05 ? 103 ILE C CG2   1 
ATOM   5537 C  CD1   . ILE F 2 103 ? -26.355 7.547  136.749 1.00 13.95 ? 103 ILE C CD1   1 
ATOM   5538 N  N     . ASN F 2 104 ? -29.555 3.760  138.088 1.00 11.60 ? 104 ASN C N     1 
ATOM   5539 C  CA    . ASN F 2 104 ? -30.999 3.902  138.389 1.00 11.61 ? 104 ASN C CA    1 
ATOM   5540 C  C     . ASN F 2 104 ? -31.187 5.311  138.946 1.00 12.01 ? 104 ASN C C     1 
ATOM   5541 O  O     . ASN F 2 104 ? -30.450 5.679  139.875 1.00 12.39 ? 104 ASN C O     1 
ATOM   5542 C  CB    . ASN F 2 104 ? -31.427 2.837  139.372 1.00 13.06 ? 104 ASN C CB    1 
ATOM   5543 C  CG    . ASN F 2 104 ? -31.186 1.414  138.896 1.00 17.13 ? 104 ASN C CG    1 
ATOM   5544 O  OD1   . ASN F 2 104 ? -31.159 1.163  137.664 1.00 19.96 ? 104 ASN C OD1   1 
ATOM   5545 N  ND2   . ASN F 2 104 ? -31.048 0.496  139.868 1.00 18.96 ? 104 ASN C ND2   1 
ATOM   5546 N  N     . PHE F 2 105 ? -32.085 6.065  138.377 1.00 11.55 ? 105 PHE C N     1 
ATOM   5547 C  CA    . PHE F 2 105 ? -32.376 7.440  138.873 1.00 10.50 ? 105 PHE C CA    1 
ATOM   5548 C  C     . PHE F 2 105 ? -33.541 7.266  139.851 1.00 10.97 ? 105 PHE C C     1 
ATOM   5549 O  O     . PHE F 2 105 ? -34.629 6.815  139.425 1.00 11.96 ? 105 PHE C O     1 
ATOM   5550 C  CB    . PHE F 2 105 ? -32.728 8.361  137.720 1.00 8.82  ? 105 PHE C CB    1 
ATOM   5551 C  CG    . PHE F 2 105 ? -31.562 8.552  136.802 1.00 8.72  ? 105 PHE C CG    1 
ATOM   5552 C  CD1   . PHE F 2 105 ? -30.504 9.338  137.228 1.00 8.98  ? 105 PHE C CD1   1 
ATOM   5553 C  CD2   . PHE F 2 105 ? -31.535 7.919  135.579 1.00 8.34  ? 105 PHE C CD2   1 
ATOM   5554 C  CE1   . PHE F 2 105 ? -29.396 9.501  136.410 1.00 7.97  ? 105 PHE C CE1   1 
ATOM   5555 C  CE2   . PHE F 2 105 ? -30.451 8.070  134.730 1.00 7.70  ? 105 PHE C CE2   1 
ATOM   5556 C  CZ    . PHE F 2 105 ? -29.387 8.865  135.163 1.00 7.91  ? 105 PHE C CZ    1 
ATOM   5557 N  N     . THR F 2 106 ? -33.307 7.587  141.101 1.00 10.78 ? 106 THR C N     1 
ATOM   5558 C  CA    . THR F 2 106 ? -34.346 7.389  142.110 1.00 10.91 ? 106 THR C CA    1 
ATOM   5559 C  C     . THR F 2 106 ? -35.415 8.461  142.145 1.00 10.93 ? 106 THR C C     1 
ATOM   5560 O  O     . THR F 2 106 ? -35.133 9.647  142.261 1.00 10.86 ? 106 THR C O     1 
ATOM   5561 C  CB    . THR F 2 106 ? -33.685 7.118  143.518 1.00 11.10 ? 106 THR C CB    1 
ATOM   5562 O  OG1   . THR F 2 106 ? -34.530 7.925  144.386 1.00 13.26 ? 106 THR C OG1   1 
ATOM   5563 C  CG2   . THR F 2 106 ? -32.191 7.456  143.564 1.00 11.62 ? 106 THR C CG2   1 
ATOM   5564 N  N     . ALA F 2 107 ? -36.650 7.987  142.039 1.00 10.52 ? 107 ALA C N     1 
ATOM   5565 C  CA    . ALA F 2 107 ? -37.880 8.732  142.000 1.00 9.76  ? 107 ALA C CA    1 
ATOM   5566 C  C     . ALA F 2 107 ? -38.026 9.744  143.091 1.00 10.06 ? 107 ALA C C     1 
ATOM   5567 O  O     . ALA F 2 107 ? -37.717 9.472  144.258 1.00 10.11 ? 107 ALA C O     1 
ATOM   5568 C  CB    . ALA F 2 107 ? -39.119 7.856  142.020 1.00 7.53  ? 107 ALA C CB    1 
ATOM   5569 N  N     . ASN F 2 108 ? -38.500 10.884 142.623 1.00 10.13 ? 108 ASN C N     1 
ATOM   5570 C  CA    . ASN F 2 108 ? -38.816 11.985 143.494 1.00 10.25 ? 108 ASN C CA    1 
ATOM   5571 C  C     . ASN F 2 108 ? -37.546 12.585 144.062 1.00 10.92 ? 108 ASN C C     1 
ATOM   5572 O  O     . ASN F 2 108 ? -37.443 12.810 145.278 1.00 11.03 ? 108 ASN C O     1 
ATOM   5573 C  CB    . ASN F 2 108 ? -39.678 11.444 144.605 1.00 10.93 ? 108 ASN C CB    1 
ATOM   5574 C  CG    . ASN F 2 108 ? -40.503 12.512 145.279 1.00 14.17 ? 108 ASN C CG    1 
ATOM   5575 O  OD1   . ASN F 2 108 ? -40.930 13.458 144.625 1.00 14.49 ? 108 ASN C OD1   1 
ATOM   5576 N  ND2   . ASN F 2 108 ? -40.749 12.411 146.567 1.00 16.33 ? 108 ASN C ND2   1 
ATOM   5577 N  N     . ARG F 2 109 ? -36.658 12.794 143.139 1.00 10.70 ? 109 ARG C N     1 
ATOM   5578 C  CA    . ARG F 2 109 ? -35.376 13.432 143.364 1.00 10.46 ? 109 ARG C CA    1 
ATOM   5579 C  C     . ARG F 2 109 ? -34.840 13.914 142.012 1.00 11.29 ? 109 ARG C C     1 
ATOM   5580 O  O     . ARG F 2 109 ? -35.339 13.444 140.971 1.00 12.17 ? 109 ARG C O     1 
ATOM   5581 C  CB    . ARG F 2 109 ? -34.316 12.457 143.894 1.00 7.21  ? 109 ARG C CB    1 
ATOM   5582 C  CG    . ARG F 2 109 ? -34.807 11.525 144.990 1.00 5.66  ? 109 ARG C CG    1 
ATOM   5583 C  CD    . ARG F 2 109 ? -33.781 11.347 146.112 1.00 7.76  ? 109 ARG C CD    1 
ATOM   5584 N  NE    . ARG F 2 109 ? -34.185 12.026 147.347 1.00 8.37  ? 109 ARG C NE    1 
ATOM   5585 C  CZ    . ARG F 2 109 ? -33.453 12.956 147.974 1.00 9.77  ? 109 ARG C CZ    1 
ATOM   5586 N  NH1   . ARG F 2 109 ? -32.258 13.334 147.503 1.00 10.04 ? 109 ARG C NH1   1 
ATOM   5587 N  NH2   . ARG F 2 109 ? -33.842 13.577 149.096 1.00 11.24 ? 109 ARG C NH2   1 
ATOM   5588 N  N     . ASP F 2 110 ? -33.884 14.814 142.066 1.00 11.01 ? 110 ASP C N     1 
ATOM   5589 C  CA    . ASP F 2 110 ? -33.226 15.296 140.833 1.00 10.76 ? 110 ASP C CA    1 
ATOM   5590 C  C     . ASP F 2 110 ? -31.785 14.769 141.003 1.00 11.62 ? 110 ASP C C     1 
ATOM   5591 O  O     . ASP F 2 110 ? -31.212 15.116 142.062 1.00 12.26 ? 110 ASP C O     1 
ATOM   5592 C  CB    . ASP F 2 110 ? -33.250 16.787 140.707 1.00 10.35 ? 110 ASP C CB    1 
ATOM   5593 C  CG    . ASP F 2 110 ? -34.647 17.349 140.584 1.00 12.69 ? 110 ASP C CG    1 
ATOM   5594 O  OD1   . ASP F 2 110 ? -35.574 16.538 140.822 1.00 12.99 ? 110 ASP C OD1   1 
ATOM   5595 O  OD2   . ASP F 2 110 ? -34.763 18.551 140.247 1.00 13.51 ? 110 ASP C OD2   1 
ATOM   5596 N  N     . THR F 2 111 ? -31.311 13.985 140.065 1.00 11.18 ? 111 THR C N     1 
ATOM   5597 C  CA    . THR F 2 111 ? -29.927 13.479 140.211 1.00 11.33 ? 111 THR C CA    1 
ATOM   5598 C  C     . THR F 2 111 ? -29.021 14.424 139.476 1.00 11.45 ? 111 THR C C     1 
ATOM   5599 O  O     . THR F 2 111 ? -29.413 14.805 138.354 1.00 12.66 ? 111 THR C O     1 
ATOM   5600 C  CB    . THR F 2 111 ? -29.812 12.014 139.677 1.00 12.56 ? 111 THR C CB    1 
ATOM   5601 O  OG1   . THR F 2 111 ? -30.966 11.325 140.285 1.00 14.51 ? 111 THR C OG1   1 
ATOM   5602 C  CG2   . THR F 2 111 ? -28.492 11.329 140.038 1.00 11.48 ? 111 THR C CG2   1 
ATOM   5603 N  N     . PHE F 2 112 ? -27.925 14.812 140.076 1.00 10.86 ? 112 PHE C N     1 
ATOM   5604 C  CA    . PHE F 2 112 ? -27.000 15.752 139.401 1.00 10.85 ? 112 PHE C CA    1 
ATOM   5605 C  C     . PHE F 2 112 ? -25.750 14.965 139.026 1.00 11.00 ? 112 PHE C C     1 
ATOM   5606 O  O     . PHE F 2 112 ? -25.167 14.280 139.892 1.00 10.21 ? 112 PHE C O     1 
ATOM   5607 C  CB    . PHE F 2 112 ? -26.663 16.964 140.259 1.00 12.28 ? 112 PHE C CB    1 
ATOM   5608 C  CG    . PHE F 2 112 ? -27.694 18.040 140.169 1.00 13.40 ? 112 PHE C CG    1 
ATOM   5609 C  CD1   . PHE F 2 112 ? -28.843 17.967 140.955 1.00 14.62 ? 112 PHE C CD1   1 
ATOM   5610 C  CD2   . PHE F 2 112 ? -27.549 19.083 139.272 1.00 12.57 ? 112 PHE C CD2   1 
ATOM   5611 C  CE1   . PHE F 2 112 ? -29.833 18.941 140.863 1.00 14.08 ? 112 PHE C CE1   1 
ATOM   5612 C  CE2   . PHE F 2 112 ? -28.516 20.079 139.163 1.00 12.63 ? 112 PHE C CE2   1 
ATOM   5613 C  CZ    . PHE F 2 112 ? -29.655 20.008 139.967 1.00 13.56 ? 112 PHE C CZ    1 
ATOM   5614 N  N     . ILE F 2 113 ? -25.365 15.076 137.771 1.00 11.06 ? 113 ILE C N     1 
ATOM   5615 C  CA    . ILE F 2 113 ? -24.152 14.396 137.315 1.00 10.84 ? 113 ILE C CA    1 
ATOM   5616 C  C     . ILE F 2 113 ? -23.176 15.434 136.783 1.00 11.04 ? 113 ILE C C     1 
ATOM   5617 O  O     . ILE F 2 113 ? -23.494 16.312 135.968 1.00 11.44 ? 113 ILE C O     1 
ATOM   5618 C  CB    . ILE F 2 113 ? -24.406 13.214 136.328 1.00 10.11 ? 113 ILE C CB    1 
ATOM   5619 C  CG1   . ILE F 2 113 ? -25.332 12.169 136.997 1.00 9.62  ? 113 ILE C CG1   1 
ATOM   5620 C  CG2   . ILE F 2 113 ? -23.054 12.595 135.853 1.00 9.64  ? 113 ILE C CG2   1 
ATOM   5621 C  CD1   . ILE F 2 113 ? -25.988 11.118 136.085 1.00 10.03 ? 113 ILE C CD1   1 
ATOM   5622 N  N     . LEU F 2 114 ? -21.949 15.320 137.266 1.00 10.78 ? 114 LEU C N     1 
ATOM   5623 C  CA    . LEU F 2 114 ? -20.914 16.246 136.811 1.00 9.54  ? 114 LEU C CA    1 
ATOM   5624 C  C     . LEU F 2 114 ? -19.856 15.441 136.030 1.00 9.09  ? 114 LEU C C     1 
ATOM   5625 O  O     . LEU F 2 114 ? -19.356 14.467 136.622 1.00 8.93  ? 114 LEU C O     1 
ATOM   5626 C  CB    . LEU F 2 114 ? -20.317 16.941 138.009 1.00 6.77  ? 114 LEU C CB    1 
ATOM   5627 C  CG    . LEU F 2 114 ? -21.130 17.692 139.004 1.00 8.09  ? 114 LEU C CG    1 
ATOM   5628 C  CD1   . LEU F 2 114 ? -20.168 18.140 140.112 1.00 8.57  ? 114 LEU C CD1   1 
ATOM   5629 C  CD2   . LEU F 2 114 ? -21.747 18.918 138.367 1.00 7.72  ? 114 LEU C CD2   1 
ATOM   5630 N  N     . ILE F 2 115 ? -19.613 15.889 134.822 1.00 7.94  ? 115 ILE C N     1 
ATOM   5631 C  CA    . ILE F 2 115 ? -18.544 15.297 133.977 1.00 8.05  ? 115 ILE C CA    1 
ATOM   5632 C  C     . ILE F 2 115 ? -17.445 16.388 134.031 1.00 8.48  ? 115 ILE C C     1 
ATOM   5633 O  O     . ILE F 2 115 ? -17.491 17.410 133.314 1.00 8.46  ? 115 ILE C O     1 
ATOM   5634 C  CB    . ILE F 2 115 ? -19.089 14.867 132.600 1.00 6.86  ? 115 ILE C CB    1 
ATOM   5635 C  CG1   . ILE F 2 115 ? -19.852 13.521 132.707 1.00 7.10  ? 115 ILE C CG1   1 
ATOM   5636 C  CG2   . ILE F 2 115 ? -18.038 14.720 131.477 1.00 7.41  ? 115 ILE C CG2   1 
ATOM   5637 C  CD1   . ILE F 2 115 ? -21.308 13.710 133.188 1.00 8.86  ? 115 ILE C CD1   1 
ATOM   5638 N  N     . ALA F 2 116 ? -16.529 16.178 134.983 1.00 7.46  ? 116 ALA C N     1 
ATOM   5639 C  CA    . ALA F 2 116 ? -15.432 17.142 135.220 1.00 6.89  ? 116 ALA C CA    1 
ATOM   5640 C  C     . ALA F 2 116 ? -14.081 16.588 134.802 1.00 5.99  ? 116 ALA C C     1 
ATOM   5641 O  O     . ALA F 2 116 ? -13.905 15.366 134.925 1.00 4.90  ? 116 ALA C O     1 
ATOM   5642 C  CB    . ALA F 2 116 ? -15.415 17.498 136.717 1.00 7.29  ? 116 ALA C CB    1 
ATOM   5643 N  N     . PRO F 2 117 ? -13.157 17.430 134.376 1.00 6.28  ? 117 PRO C N     1 
ATOM   5644 C  CA    . PRO F 2 117 ? -11.839 17.031 133.922 1.00 8.03  ? 117 PRO C CA    1 
ATOM   5645 C  C     . PRO F 2 117 ? -10.885 16.616 135.016 1.00 10.39 ? 117 PRO C C     1 
ATOM   5646 O  O     . PRO F 2 117 ? -9.801  17.209 135.159 1.00 12.59 ? 117 PRO C O     1 
ATOM   5647 C  CB    . PRO F 2 117 ? -11.283 18.265 133.210 1.00 7.88  ? 117 PRO C CB    1 
ATOM   5648 C  CG    . PRO F 2 117 ? -11.885 19.356 134.066 1.00 7.51  ? 117 PRO C CG    1 
ATOM   5649 C  CD    . PRO F 2 117 ? -13.342 18.887 134.255 1.00 6.41  ? 117 PRO C CD    1 
ATOM   5650 N  N     . THR F 2 118 ? -11.309 15.594 135.723 1.00 10.21 ? 118 THR C N     1 
ATOM   5651 C  CA    . THR F 2 118 ? -10.556 14.974 136.821 1.00 8.33  ? 118 THR C CA    1 
ATOM   5652 C  C     . THR F 2 118 ? -10.067 13.621 136.303 1.00 7.93  ? 118 THR C C     1 
ATOM   5653 O  O     . THR F 2 118 ? -10.878 12.696 136.180 1.00 7.48  ? 118 THR C O     1 
ATOM   5654 C  CB    . THR F 2 118 ? -11.461 14.821 138.105 1.00 5.65  ? 118 THR C CB    1 
ATOM   5655 O  OG1   . THR F 2 118 ? -12.599 13.963 137.736 1.00 7.16  ? 118 THR C OG1   1 
ATOM   5656 C  CG2   . THR F 2 118 ? -11.981 16.111 138.721 1.00 4.79  ? 118 THR C CG2   1 
ATOM   5657 N  N     . PRO F 2 119 ? -8.784  13.548 135.979 1.00 7.97  ? 119 PRO C N     1 
ATOM   5658 C  CA    . PRO F 2 119 ? -8.170  12.306 135.470 1.00 7.77  ? 119 PRO C CA    1 
ATOM   5659 C  C     . PRO F 2 119 ? -8.486  11.132 136.391 1.00 8.62  ? 119 PRO C C     1 
ATOM   5660 O  O     . PRO F 2 119 ? -8.423  11.240 137.639 1.00 10.46 ? 119 PRO C O     1 
ATOM   5661 C  CB    . PRO F 2 119 ? -6.695  12.577 135.404 1.00 5.61  ? 119 PRO C CB    1 
ATOM   5662 C  CG    . PRO F 2 119 ? -6.547  14.055 135.468 1.00 5.79  ? 119 PRO C CG    1 
ATOM   5663 C  CD    . PRO F 2 119 ? -7.804  14.642 136.088 1.00 7.09  ? 119 PRO C CD    1 
ATOM   5664 N  N     . GLY F 2 120 ? -8.886  10.033 135.776 1.00 8.32  ? 120 GLY C N     1 
ATOM   5665 C  CA    . GLY F 2 120 ? -9.212  8.784  136.404 1.00 9.12  ? 120 GLY C CA    1 
ATOM   5666 C  C     . GLY F 2 120 ? -10.624 8.562  136.841 1.00 10.61 ? 120 GLY C C     1 
ATOM   5667 O  O     . GLY F 2 120 ? -10.997 7.369  136.911 1.00 12.11 ? 120 GLY C O     1 
ATOM   5668 N  N     . VAL F 2 121 ? -11.378 9.604  137.162 1.00 10.80 ? 121 VAL C N     1 
ATOM   5669 C  CA    . VAL F 2 121 ? -12.786 9.428  137.622 1.00 10.45 ? 121 VAL C CA    1 
ATOM   5670 C  C     . VAL F 2 121 ? -13.725 9.922  136.537 1.00 9.98  ? 121 VAL C C     1 
ATOM   5671 O  O     . VAL F 2 121 ? -13.543 11.044 136.028 1.00 10.29 ? 121 VAL C O     1 
ATOM   5672 C  CB    . VAL F 2 121 ? -13.000 10.006 139.015 1.00 10.50 ? 121 VAL C CB    1 
ATOM   5673 C  CG1   . VAL F 2 121 ? -11.670 10.226 139.735 1.00 11.11 ? 121 VAL C CG1   1 
ATOM   5674 C  CG2   . VAL F 2 121 ? -13.913 11.201 139.079 1.00 11.87 ? 121 VAL C CG2   1 
ATOM   5675 N  N     . ALA F 2 122 ? -14.702 9.094  136.189 1.00 9.19  ? 122 ALA C N     1 
ATOM   5676 C  CA    . ALA F 2 122 ? -15.613 9.420  135.098 1.00 8.69  ? 122 ALA C CA    1 
ATOM   5677 C  C     . ALA F 2 122 ? -16.639 10.475 135.393 1.00 9.73  ? 122 ALA C C     1 
ATOM   5678 O  O     . ALA F 2 122 ? -16.846 11.325 134.492 1.00 11.67 ? 122 ALA C O     1 
ATOM   5679 C  CB    . ALA F 2 122 ? -16.268 8.168  134.525 1.00 5.97  ? 122 ALA C CB    1 
ATOM   5680 N  N     . TYR F 2 123 ? -17.289 10.430 136.549 1.00 9.67  ? 123 TYR C N     1 
ATOM   5681 C  CA    . TYR F 2 123 ? -18.324 11.489 136.803 1.00 9.05  ? 123 TYR C CA    1 
ATOM   5682 C  C     . TYR F 2 123 ? -18.558 11.610 138.284 1.00 8.52  ? 123 TYR C C     1 
ATOM   5683 O  O     . TYR F 2 123 ? -18.088 10.700 139.013 1.00 8.54  ? 123 TYR C O     1 
ATOM   5684 C  CB    . TYR F 2 123 ? -19.565 11.126 135.998 1.00 9.55  ? 123 TYR C CB    1 
ATOM   5685 C  CG    . TYR F 2 123 ? -20.362 9.950  136.498 1.00 9.00  ? 123 TYR C CG    1 
ATOM   5686 C  CD1   . TYR F 2 123 ? -21.194 10.078 137.609 1.00 10.35 ? 123 TYR C CD1   1 
ATOM   5687 C  CD2   . TYR F 2 123 ? -20.313 8.720  135.848 1.00 8.81  ? 123 TYR C CD2   1 
ATOM   5688 C  CE1   . TYR F 2 123 ? -21.931 8.992  138.082 1.00 11.63 ? 123 TYR C CE1   1 
ATOM   5689 C  CE2   . TYR F 2 123 ? -21.047 7.619  136.294 1.00 8.41  ? 123 TYR C CE2   1 
ATOM   5690 C  CZ    . TYR F 2 123 ? -21.852 7.764  137.418 1.00 10.20 ? 123 TYR C CZ    1 
ATOM   5691 O  OH    . TYR F 2 123 ? -22.571 6.693  137.865 1.00 10.13 ? 123 TYR C OH    1 
ATOM   5692 N  N     . TRP F 2 124 ? -19.206 12.671 138.697 1.00 7.79  ? 124 TRP C N     1 
ATOM   5693 C  CA    . TRP F 2 124 ? -19.499 12.877 140.162 1.00 7.95  ? 124 TRP C CA    1 
ATOM   5694 C  C     . TRP F 2 124 ? -21.018 12.906 140.295 1.00 8.30  ? 124 TRP C C     1 
ATOM   5695 O  O     . TRP F 2 124 ? -21.679 13.663 139.540 1.00 8.52  ? 124 TRP C O     1 
ATOM   5696 C  CB    . TRP F 2 124 ? -18.773 14.111 140.673 1.00 6.13  ? 124 TRP C CB    1 
ATOM   5697 C  CG    . TRP F 2 124 ? -17.295 14.089 140.416 1.00 7.09  ? 124 TRP C CG    1 
ATOM   5698 C  CD1   . TRP F 2 124 ? -16.616 14.238 139.232 1.00 8.15  ? 124 TRP C CD1   1 
ATOM   5699 C  CD2   . TRP F 2 124 ? -16.290 13.878 141.428 1.00 8.15  ? 124 TRP C CD2   1 
ATOM   5700 N  NE1   . TRP F 2 124 ? -15.256 14.129 139.445 1.00 7.99  ? 124 TRP C NE1   1 
ATOM   5701 C  CE2   . TRP F 2 124 ? -15.036 13.901 140.773 1.00 7.42  ? 124 TRP C CE2   1 
ATOM   5702 C  CE3   . TRP F 2 124 ? -16.342 13.677 142.804 1.00 7.87  ? 124 TRP C CE3   1 
ATOM   5703 C  CZ2   . TRP F 2 124 ? -13.864 13.724 141.490 1.00 6.35  ? 124 TRP C CZ2   1 
ATOM   5704 C  CZ3   . TRP F 2 124 ? -15.168 13.487 143.499 1.00 8.56  ? 124 TRP C CZ3   1 
ATOM   5705 C  CH2   . TRP F 2 124 ? -13.942 13.506 142.860 1.00 7.95  ? 124 TRP C CH2   1 
ATOM   5706 N  N     . VAL F 2 125 ? -21.610 12.099 141.162 1.00 8.04  ? 125 VAL C N     1 
ATOM   5707 C  CA    . VAL F 2 125 ? -23.081 12.137 141.223 1.00 8.22  ? 125 VAL C CA    1 
ATOM   5708 C  C     . VAL F 2 125 ? -23.612 12.521 142.597 1.00 8.44  ? 125 VAL C C     1 
ATOM   5709 O  O     . VAL F 2 125 ? -22.965 12.309 143.632 1.00 8.43  ? 125 VAL C O     1 
ATOM   5710 C  CB    . VAL F 2 125 ? -23.703 10.766 140.811 1.00 8.34  ? 125 VAL C CB    1 
ATOM   5711 C  CG1   . VAL F 2 125 ? -23.213 9.635  141.696 1.00 7.30  ? 125 VAL C CG1   1 
ATOM   5712 C  CG2   . VAL F 2 125 ? -25.221 10.852 140.781 1.00 9.15  ? 125 VAL C CG2   1 
ATOM   5713 N  N     . ALA F 2 126 ? -24.844 12.990 142.557 1.00 8.95  ? 126 ALA C N     1 
ATOM   5714 C  CA    . ALA F 2 126 ? -25.568 13.378 143.764 1.00 9.92  ? 126 ALA C CA    1 
ATOM   5715 C  C     . ALA F 2 126 ? -27.022 13.639 143.407 1.00 11.60 ? 126 ALA C C     1 
ATOM   5716 O  O     . ALA F 2 126 ? -27.329 14.096 142.295 1.00 13.88 ? 126 ALA C O     1 
ATOM   5717 C  CB    . ALA F 2 126 ? -24.891 14.617 144.357 1.00 7.65  ? 126 ALA C CB    1 
ATOM   5718 N  N     . ASP F 2 127 ? -27.895 13.320 144.348 1.00 11.79 ? 127 ASP C N     1 
ATOM   5719 C  CA    . ASP F 2 127 ? -29.323 13.583 144.095 1.00 11.38 ? 127 ASP C CA    1 
ATOM   5720 C  C     . ASP F 2 127 ? -29.840 14.372 145.309 1.00 11.27 ? 127 ASP C C     1 
ATOM   5721 O  O     . ASP F 2 127 ? -29.340 14.178 146.418 1.00 11.62 ? 127 ASP C O     1 
ATOM   5722 C  CB    . ASP F 2 127 ? -30.139 12.354 143.838 1.00 11.61 ? 127 ASP C CB    1 
ATOM   5723 C  CG    . ASP F 2 127 ? -30.212 11.420 145.031 1.00 12.40 ? 127 ASP C CG    1 
ATOM   5724 O  OD1   . ASP F 2 127 ? -30.755 11.699 146.104 1.00 13.03 ? 127 ASP C OD1   1 
ATOM   5725 O  OD2   . ASP F 2 127 ? -29.664 10.312 144.824 1.00 14.79 ? 127 ASP C OD2   1 
ATOM   5726 N  N     . VAL F 2 128 ? -30.825 15.167 144.996 1.00 10.93 ? 128 VAL C N     1 
ATOM   5727 C  CA    . VAL F 2 128 ? -31.491 15.999 146.004 1.00 10.34 ? 128 VAL C CA    1 
ATOM   5728 C  C     . VAL F 2 128 ? -33.005 15.900 145.799 1.00 10.28 ? 128 VAL C C     1 
ATOM   5729 O  O     . VAL F 2 128 ? -33.503 15.388 144.772 1.00 10.64 ? 128 VAL C O     1 
ATOM   5730 C  CB    . VAL F 2 128 ? -30.922 17.431 145.832 1.00 9.86  ? 128 VAL C CB    1 
ATOM   5731 C  CG1   . VAL F 2 128 ? -29.396 17.449 145.827 1.00 7.91  ? 128 VAL C CG1   1 
ATOM   5732 C  CG2   . VAL F 2 128 ? -31.453 18.113 144.576 1.00 9.05  ? 128 VAL C CG2   1 
ATOM   5733 N  N     . PRO F 2 129 ? -33.736 16.437 146.769 1.00 9.86  ? 129 PRO C N     1 
ATOM   5734 C  CA    . PRO F 2 129 ? -35.197 16.483 146.699 1.00 9.54  ? 129 PRO C CA    1 
ATOM   5735 C  C     . PRO F 2 129 ? -35.575 17.173 145.383 1.00 9.52  ? 129 PRO C C     1 
ATOM   5736 O  O     . PRO F 2 129 ? -35.010 18.229 145.059 1.00 9.25  ? 129 PRO C O     1 
ATOM   5737 C  CB    . PRO F 2 129 ? -35.570 17.383 147.859 1.00 8.87  ? 129 PRO C CB    1 
ATOM   5738 C  CG    . PRO F 2 129 ? -34.500 17.028 148.862 1.00 9.07  ? 129 PRO C CG    1 
ATOM   5739 C  CD    . PRO F 2 129 ? -33.236 17.064 148.002 1.00 9.57  ? 129 PRO C CD    1 
ATOM   5740 N  N     . ALA F 2 130 ? -36.511 16.543 144.711 1.00 9.41  ? 130 ALA C N     1 
ATOM   5741 C  CA    . ALA F 2 130 ? -37.053 17.006 143.440 1.00 9.20  ? 130 ALA C CA    1 
ATOM   5742 C  C     . ALA F 2 130 ? -37.371 18.495 143.519 1.00 10.09 ? 130 ALA C C     1 
ATOM   5743 O  O     . ALA F 2 130 ? -37.956 18.967 144.493 1.00 10.96 ? 130 ALA C O     1 
ATOM   5744 C  CB    . ALA F 2 130 ? -38.328 16.215 143.130 1.00 5.70  ? 130 ALA C CB    1 
ATOM   5745 N  N     . GLY F 2 131 ? -36.996 19.226 142.505 1.00 10.39 ? 131 GLY C N     1 
ATOM   5746 C  CA    . GLY F 2 131 ? -37.248 20.651 142.408 1.00 11.01 ? 131 GLY C CA    1 
ATOM   5747 C  C     . GLY F 2 131 ? -36.189 21.489 143.066 1.00 12.08 ? 131 GLY C C     1 
ATOM   5748 O  O     . GLY F 2 131 ? -36.299 22.738 143.012 1.00 13.88 ? 131 GLY C O     1 
ATOM   5749 N  N     . THR F 2 132 ? -35.166 20.883 143.637 1.00 11.48 ? 132 THR C N     1 
ATOM   5750 C  CA    . THR F 2 132 ? -34.129 21.709 144.317 1.00 12.03 ? 132 THR C CA    1 
ATOM   5751 C  C     . THR F 2 132 ? -32.758 21.510 143.728 1.00 13.01 ? 132 THR C C     1 
ATOM   5752 O  O     . THR F 2 132 ? -32.657 20.709 142.775 1.00 14.15 ? 132 THR C O     1 
ATOM   5753 C  CB    . THR F 2 132 ? -34.204 21.299 145.848 1.00 10.92 ? 132 THR C CB    1 
ATOM   5754 O  OG1   . THR F 2 132 ? -33.250 20.201 146.011 1.00 10.54 ? 132 THR C OG1   1 
ATOM   5755 C  CG2   . THR F 2 132 ? -35.630 20.864 146.204 1.00 9.91  ? 132 THR C CG2   1 
ATOM   5756 N  N     . PHE F 2 133 ? -31.765 22.184 144.288 1.00 12.66 ? 133 PHE C N     1 
ATOM   5757 C  CA    . PHE F 2 133 ? -30.362 22.046 143.858 1.00 12.41 ? 133 PHE C CA    1 
ATOM   5758 C  C     . PHE F 2 133 ? -29.469 21.743 145.076 1.00 12.70 ? 133 PHE C C     1 
ATOM   5759 O  O     . PHE F 2 133 ? -29.877 21.890 146.236 1.00 13.21 ? 133 PHE C O     1 
ATOM   5760 C  CB    . PHE F 2 133 ? -29.846 23.289 143.139 1.00 9.08  ? 133 PHE C CB    1 
ATOM   5761 C  CG    . PHE F 2 133 ? -30.440 23.534 141.793 1.00 6.46  ? 133 PHE C CG    1 
ATOM   5762 C  CD1   . PHE F 2 133 ? -31.678 24.145 141.675 1.00 3.18  ? 133 PHE C CD1   1 
ATOM   5763 C  CD2   . PHE F 2 133 ? -29.748 23.130 140.650 1.00 6.20  ? 133 PHE C CD2   1 
ATOM   5764 C  CE1   . PHE F 2 133 ? -32.241 24.359 140.427 1.00 3.51  ? 133 PHE C CE1   1 
ATOM   5765 C  CE2   . PHE F 2 133 ? -30.283 23.350 139.374 1.00 4.33  ? 133 PHE C CE2   1 
ATOM   5766 C  CZ    . PHE F 2 133 ? -31.552 23.962 139.276 1.00 4.01  ? 133 PHE C CZ    1 
ATOM   5767 N  N     . PRO F 2 134 ? -28.242 21.353 144.772 1.00 12.12 ? 134 PRO C N     1 
ATOM   5768 C  CA    . PRO F 2 134 ? -27.265 21.025 145.829 1.00 11.91 ? 134 PRO C CA    1 
ATOM   5769 C  C     . PRO F 2 134 ? -27.150 22.137 146.850 1.00 11.57 ? 134 PRO C C     1 
ATOM   5770 O  O     . PRO F 2 134 ? -27.309 23.343 146.596 1.00 12.04 ? 134 PRO C O     1 
ATOM   5771 C  CB    . PRO F 2 134 ? -25.979 20.725 145.059 1.00 11.58 ? 134 PRO C CB    1 
ATOM   5772 C  CG    . PRO F 2 134 ? -26.495 20.211 143.721 1.00 11.62 ? 134 PRO C CG    1 
ATOM   5773 C  CD    . PRO F 2 134 ? -27.676 21.134 143.422 1.00 11.93 ? 134 PRO C CD    1 
ATOM   5774 N  N     . ILE F 2 135 ? -26.905 21.746 148.089 1.00 10.60 ? 135 ILE C N     1 
ATOM   5775 C  CA    . ILE F 2 135 ? -26.754 22.717 149.192 1.00 9.76  ? 135 ILE C CA    1 
ATOM   5776 C  C     . ILE F 2 135 ? -25.384 22.464 149.812 1.00 10.36 ? 135 ILE C C     1 
ATOM   5777 O  O     . ILE F 2 135 ? -24.741 21.445 149.465 1.00 10.55 ? 135 ILE C O     1 
ATOM   5778 C  CB    . ILE F 2 135 ? -27.935 22.590 150.173 1.00 7.67  ? 135 ILE C CB    1 
ATOM   5779 C  CG1   . ILE F 2 135 ? -27.627 21.445 151.173 1.00 8.43  ? 135 ILE C CG1   1 
ATOM   5780 C  CG2   . ILE F 2 135 ? -29.266 22.341 149.438 1.00 5.67  ? 135 ILE C CG2   1 
ATOM   5781 C  CD1   . ILE F 2 135 ? -28.880 21.151 152.076 1.00 10.27 ? 135 ILE C CD1   1 
ATOM   5782 N  N     . SER F 2 136 ? -24.960 23.355 150.669 1.00 10.47 ? 136 SER C N     1 
ATOM   5783 C  CA    . SER F 2 136 ? -23.630 23.225 151.299 1.00 10.95 ? 136 SER C CA    1 
ATOM   5784 C  C     . SER F 2 136 ? -23.463 21.831 151.881 1.00 11.48 ? 136 SER C C     1 
ATOM   5785 O  O     . SER F 2 136 ? -22.383 21.230 152.014 1.00 12.62 ? 136 SER C O     1 
ATOM   5786 C  CB    . SER F 2 136 ? -23.556 24.264 152.411 1.00 11.08 ? 136 SER C CB    1 
ATOM   5787 O  OG    . SER F 2 136 ? -24.618 23.967 153.327 1.00 12.86 ? 136 SER C OG    1 
ATOM   5788 N  N     . THR F 2 137 ? -24.619 21.322 152.238 1.00 10.90 ? 137 THR C N     1 
ATOM   5789 C  CA    . THR F 2 137 ? -24.757 20.005 152.845 1.00 11.26 ? 137 THR C CA    1 
ATOM   5790 C  C     . THR F 2 137 ? -24.497 18.849 151.900 1.00 12.13 ? 137 THR C C     1 
ATOM   5791 O  O     . THR F 2 137 ? -24.126 17.761 152.370 1.00 13.66 ? 137 THR C O     1 
ATOM   5792 C  CB    . THR F 2 137 ? -26.223 19.879 153.453 1.00 11.50 ? 137 THR C CB    1 
ATOM   5793 O  OG1   . THR F 2 137 ? -25.943 20.176 154.856 1.00 14.18 ? 137 THR C OG1   1 
ATOM   5794 C  CG2   . THR F 2 137 ? -26.899 18.543 153.182 1.00 10.84 ? 137 THR C CG2   1 
ATOM   5795 N  N     . THR F 2 138 ? -24.725 19.098 150.626 1.00 10.86 ? 138 THR C N     1 
ATOM   5796 C  CA    . THR F 2 138 ? -24.584 18.133 149.541 1.00 9.18  ? 138 THR C CA    1 
ATOM   5797 C  C     . THR F 2 138 ? -23.134 17.693 149.405 1.00 9.10  ? 138 THR C C     1 
ATOM   5798 O  O     . THR F 2 138 ? -22.250 18.507 149.745 1.00 10.08 ? 138 THR C O     1 
ATOM   5799 C  CB    . THR F 2 138 ? -25.038 18.766 148.160 1.00 7.80  ? 138 THR C CB    1 
ATOM   5800 O  OG1   . THR F 2 138 ? -26.264 19.501 148.419 1.00 7.33  ? 138 THR C OG1   1 
ATOM   5801 C  CG2   . THR F 2 138 ? -25.262 17.748 147.053 1.00 7.58  ? 138 THR C CG2   1 
ATOM   5802 N  N     . THR F 2 139 ? -22.935 16.471 148.941 1.00 8.64  ? 139 THR C N     1 
ATOM   5803 C  CA    . THR F 2 139 ? -21.557 15.996 148.719 1.00 9.06  ? 139 THR C CA    1 
ATOM   5804 C  C     . THR F 2 139 ? -21.562 14.977 147.584 1.00 8.88  ? 139 THR C C     1 
ATOM   5805 O  O     . THR F 2 139 ? -22.128 13.874 147.662 1.00 9.01  ? 139 THR C O     1 
ATOM   5806 C  CB    . THR F 2 139 ? -20.800 15.589 150.014 1.00 10.12 ? 139 THR C CB    1 
ATOM   5807 O  OG1   . THR F 2 139 ? -20.220 14.265 149.756 1.00 10.85 ? 139 THR C OG1   1 
ATOM   5808 C  CG2   . THR F 2 139 ? -21.658 15.634 151.268 1.00 11.71 ? 139 THR C CG2   1 
ATOM   5809 N  N     . PHE F 2 140 ? -20.929 15.394 146.486 1.00 8.48  ? 140 PHE C N     1 
ATOM   5810 C  CA    . PHE F 2 140 ? -20.808 14.585 145.269 1.00 8.22  ? 140 PHE C CA    1 
ATOM   5811 C  C     . PHE F 2 140 ? -19.731 13.524 145.430 1.00 8.56  ? 140 PHE C C     1 
ATOM   5812 O  O     . PHE F 2 140 ? -18.562 13.871 145.683 1.00 9.94  ? 140 PHE C O     1 
ATOM   5813 C  CB    . PHE F 2 140 ? -20.478 15.461 144.040 1.00 8.22  ? 140 PHE C CB    1 
ATOM   5814 C  CG    . PHE F 2 140 ? -21.624 16.281 143.532 1.00 8.62  ? 140 PHE C CG    1 
ATOM   5815 C  CD1   . PHE F 2 140 ? -22.020 17.437 144.226 1.00 6.52  ? 140 PHE C CD1   1 
ATOM   5816 C  CD2   . PHE F 2 140 ? -22.313 15.901 142.386 1.00 8.80  ? 140 PHE C CD2   1 
ATOM   5817 C  CE1   . PHE F 2 140 ? -23.087 18.213 143.778 1.00 8.63  ? 140 PHE C CE1   1 
ATOM   5818 C  CE2   . PHE F 2 140 ? -23.391 16.660 141.927 1.00 7.76  ? 140 PHE C CE2   1 
ATOM   5819 C  CZ    . PHE F 2 140 ? -23.769 17.817 142.619 1.00 9.17  ? 140 PHE C CZ    1 
ATOM   5820 N  N     . ASN F 2 141 ? -20.109 12.289 145.269 1.00 8.71  ? 141 ASN C N     1 
ATOM   5821 C  CA    . ASN F 2 141 ? -19.141 11.161 145.365 1.00 8.89  ? 141 ASN C CA    1 
ATOM   5822 C  C     . ASN F 2 141 ? -18.798 10.772 143.922 1.00 9.66  ? 141 ASN C C     1 
ATOM   5823 O  O     . ASN F 2 141 ? -19.687 10.777 143.059 1.00 9.72  ? 141 ASN C O     1 
ATOM   5824 C  CB    . ASN F 2 141 ? -19.721 10.009 146.162 1.00 10.68 ? 141 ASN C CB    1 
ATOM   5825 C  CG    . ASN F 2 141 ? -20.316 10.431 147.497 1.00 12.74 ? 141 ASN C CG    1 
ATOM   5826 O  OD1   . ASN F 2 141 ? -21.531 10.232 147.698 1.00 14.48 ? 141 ASN C OD1   1 
ATOM   5827 N  ND2   . ASN F 2 141 ? -19.508 11.021 148.389 1.00 13.69 ? 141 ASN C ND2   1 
ATOM   5828 N  N     . ALA F 2 142 ? -17.544 10.464 143.726 1.00 10.02 ? 142 ALA C N     1 
ATOM   5829 C  CA    . ALA F 2 142 ? -16.951 10.095 142.450 1.00 9.66  ? 142 ALA C CA    1 
ATOM   5830 C  C     . ALA F 2 142 ? -17.125 8.656  141.996 1.00 10.08 ? 142 ALA C C     1 
ATOM   5831 O  O     . ALA F 2 142 ? -17.056 7.720  142.823 1.00 10.95 ? 142 ALA C O     1 
ATOM   5832 C  CB    . ALA F 2 142 ? -15.418 10.343 142.588 1.00 8.56  ? 142 ALA C CB    1 
ATOM   5833 N  N     . VAL F 2 143 ? -17.299 8.496  140.693 1.00 9.46  ? 143 VAL C N     1 
ATOM   5834 C  CA    . VAL F 2 143 ? -17.401 7.158  140.075 1.00 8.67  ? 143 VAL C CA    1 
ATOM   5835 C  C     . VAL F 2 143 ? -16.183 7.056  139.136 1.00 9.39  ? 143 VAL C C     1 
ATOM   5836 O  O     . VAL F 2 143 ? -16.115 7.889  138.196 1.00 9.64  ? 143 VAL C O     1 
ATOM   5837 C  CB    . VAL F 2 143 ? -18.725 6.971  139.330 1.00 7.75  ? 143 VAL C CB    1 
ATOM   5838 C  CG1   . VAL F 2 143 ? -18.691 5.690  138.490 1.00 6.96  ? 143 VAL C CG1   1 
ATOM   5839 C  CG2   . VAL F 2 143 ? -19.954 7.053  140.213 1.00 5.18  ? 143 VAL C CG2   1 
ATOM   5840 N  N     . ASN F 2 144 ? -15.307 6.121  139.355 1.00 9.88  ? 144 ASN C N     1 
ATOM   5841 C  CA    . ASN F 2 144 ? -14.086 5.917  138.587 1.00 10.40 ? 144 ASN C CA    1 
ATOM   5842 C  C     . ASN F 2 144 ? -14.259 5.214  137.237 1.00 11.17 ? 144 ASN C C     1 
ATOM   5843 O  O     . ASN F 2 144 ? -15.161 4.410  136.960 1.00 12.75 ? 144 ASN C O     1 
ATOM   5844 C  CB    . ASN F 2 144 ? -13.062 5.084  139.388 1.00 9.46  ? 144 ASN C CB    1 
ATOM   5845 C  CG    . ASN F 2 144 ? -12.435 5.692  140.600 1.00 10.38 ? 144 ASN C CG    1 
ATOM   5846 O  OD1   . ASN F 2 144 ? -12.603 6.868  140.980 1.00 10.50 ? 144 ASN C OD1   1 
ATOM   5847 N  ND2   . ASN F 2 144 ? -11.601 4.879  141.299 1.00 9.76  ? 144 ASN C ND2   1 
ATOM   5848 N  N     . PHE F 2 145 ? -13.260 5.499  136.419 1.00 10.78 ? 145 PHE C N     1 
ATOM   5849 C  CA    . PHE F 2 145 ? -13.126 4.820  135.094 1.00 9.87  ? 145 PHE C CA    1 
ATOM   5850 C  C     . PHE F 2 145 ? -12.354 3.543  135.490 1.00 10.12 ? 145 PHE C C     1 
ATOM   5851 O  O     . PHE F 2 145 ? -11.560 3.614  136.471 1.00 10.42 ? 145 PHE C O     1 
ATOM   5852 C  CB    . PHE F 2 145 ? -12.312 5.688  134.162 1.00 7.68  ? 145 PHE C CB    1 
ATOM   5853 C  CG    . PHE F 2 145 ? -12.995 6.582  133.193 1.00 7.45  ? 145 PHE C CG    1 
ATOM   5854 C  CD1   . PHE F 2 145 ? -13.795 6.049  132.186 1.00 9.24  ? 145 PHE C CD1   1 
ATOM   5855 C  CD2   . PHE F 2 145 ? -12.825 7.956  133.256 1.00 5.79  ? 145 PHE C CD2   1 
ATOM   5856 C  CE1   . PHE F 2 145 ? -14.430 6.873  131.268 1.00 8.53  ? 145 PHE C CE1   1 
ATOM   5857 C  CE2   . PHE F 2 145 ? -13.446 8.802  132.338 1.00 6.33  ? 145 PHE C CE2   1 
ATOM   5858 C  CZ    . PHE F 2 145 ? -14.253 8.263  131.334 1.00 7.48  ? 145 PHE C CZ    1 
ATOM   5859 N  N     . PRO F 2 146 ? -12.557 2.439  134.820 1.00 10.10 ? 146 PRO C N     1 
ATOM   5860 C  CA    . PRO F 2 146 ? -11.791 1.217  135.173 1.00 10.67 ? 146 PRO C CA    1 
ATOM   5861 C  C     . PRO F 2 146 ? -10.307 1.565  135.106 1.00 11.84 ? 146 PRO C C     1 
ATOM   5862 O  O     . PRO F 2 146 ? -9.950  2.485  134.348 1.00 11.97 ? 146 PRO C O     1 
ATOM   5863 C  CB    . PRO F 2 146 ? -12.198 0.206  134.117 1.00 10.12 ? 146 PRO C CB    1 
ATOM   5864 C  CG    . PRO F 2 146 ? -13.448 0.728  133.492 1.00 10.08 ? 146 PRO C CG    1 
ATOM   5865 C  CD    . PRO F 2 146 ? -13.439 2.244  133.676 1.00 9.92  ? 146 PRO C CD    1 
ATOM   5866 N  N     . GLY F 2 147 ? -9.469  0.894  135.856 1.00 13.61 ? 147 GLY C N     1 
ATOM   5867 C  CA    . GLY F 2 147 ? -8.022  1.066  135.879 1.00 15.22 ? 147 GLY C CA    1 
ATOM   5868 C  C     . GLY F 2 147 ? -7.475  2.227  136.667 1.00 16.79 ? 147 GLY C C     1 
ATOM   5869 O  O     . GLY F 2 147 ? -6.370  2.723  136.337 1.00 18.54 ? 147 GLY C O     1 
ATOM   5870 N  N     . PHE F 2 148 ? -8.136  2.700  137.710 1.00 16.50 ? 148 PHE C N     1 
ATOM   5871 C  CA    . PHE F 2 148 ? -7.718  3.825  138.537 1.00 15.41 ? 148 PHE C CA    1 
ATOM   5872 C  C     . PHE F 2 148 ? -6.476  3.542  139.366 1.00 15.77 ? 148 PHE C C     1 
ATOM   5873 O  O     . PHE F 2 148 ? -5.503  4.300  139.224 1.00 15.90 ? 148 PHE C O     1 
ATOM   5874 C  CB    . PHE F 2 148 ? -8.837  4.389  139.442 1.00 12.35 ? 148 PHE C CB    1 
ATOM   5875 C  CG    . PHE F 2 148 ? -8.396  5.583  140.236 1.00 12.04 ? 148 PHE C CG    1 
ATOM   5876 C  CD1   . PHE F 2 148 ? -7.645  5.441  141.401 1.00 12.51 ? 148 PHE C CD1   1 
ATOM   5877 C  CD2   . PHE F 2 148 ? -8.679  6.873  139.786 1.00 11.95 ? 148 PHE C CD2   1 
ATOM   5878 C  CE1   . PHE F 2 148 ? -7.211  6.555  142.130 1.00 12.16 ? 148 PHE C CE1   1 
ATOM   5879 C  CE2   . PHE F 2 148 ? -8.232  7.996  140.472 1.00 12.18 ? 148 PHE C CE2   1 
ATOM   5880 C  CZ    . PHE F 2 148 ? -7.505  7.847  141.644 1.00 11.22 ? 148 PHE C CZ    1 
ATOM   5881 N  N     . ASN F 2 149 ? -6.520  2.555  140.236 1.00 15.67 ? 149 ASN C N     1 
ATOM   5882 C  CA    . ASN F 2 149 ? -5.377  2.240  141.096 1.00 14.88 ? 149 ASN C CA    1 
ATOM   5883 C  C     . ASN F 2 149 ? -4.198  1.785  140.239 1.00 14.26 ? 149 ASN C C     1 
ATOM   5884 O  O     . ASN F 2 149 ? -3.066  2.017  140.655 1.00 15.17 ? 149 ASN C O     1 
ATOM   5885 C  CB    . ASN F 2 149 ? -5.619  1.160  142.133 1.00 16.65 ? 149 ASN C CB    1 
ATOM   5886 C  CG    . ASN F 2 149 ? -6.787  1.445  143.038 1.00 20.30 ? 149 ASN C CG    1 
ATOM   5887 O  OD1   . ASN F 2 149 ? -7.891  0.915  142.793 1.00 23.57 ? 149 ASN C OD1   1 
ATOM   5888 N  ND2   . ASN F 2 149 ? -6.551  2.297  144.034 1.00 20.86 ? 149 ASN C ND2   1 
ATOM   5889 N  N     . SER F 2 150 ? -4.546  1.123  139.164 1.00 13.64 ? 150 SER C N     1 
ATOM   5890 C  CA    . SER F 2 150 ? -3.478  0.582  138.285 1.00 12.76 ? 150 SER C CA    1 
ATOM   5891 C  C     . SER F 2 150 ? -2.619  1.739  137.783 1.00 11.60 ? 150 SER C C     1 
ATOM   5892 O  O     . SER F 2 150 ? -1.398  1.669  137.549 1.00 12.14 ? 150 SER C O     1 
ATOM   5893 C  CB    . SER F 2 150 ? -4.089  -0.195 137.130 1.00 14.05 ? 150 SER C CB    1 
ATOM   5894 O  OG    . SER F 2 150 ? -4.543  0.675  136.113 1.00 16.50 ? 150 SER C OG    1 
ATOM   5895 N  N     . MET F 2 151 ? -3.348  2.824  137.642 1.00 10.28 ? 151 MET C N     1 
ATOM   5896 C  CA    . MET F 2 151 ? -2.795  4.073  137.100 1.00 8.31  ? 151 MET C CA    1 
ATOM   5897 C  C     . MET F 2 151 ? -2.356  5.046  138.160 1.00 7.60  ? 151 MET C C     1 
ATOM   5898 O  O     . MET F 2 151 ? -1.201  5.530  138.068 1.00 7.16  ? 151 MET C O     1 
ATOM   5899 C  CB    . MET F 2 151 ? -3.908  4.577  136.177 1.00 7.17  ? 151 MET C CB    1 
ATOM   5900 C  CG    . MET F 2 151 ? -3.683  5.924  135.608 1.00 11.75 ? 151 MET C CG    1 
ATOM   5901 S  SD    . MET F 2 151 ? -3.428  5.653  133.811 1.00 17.69 ? 151 MET C SD    1 
ATOM   5902 C  CE    . MET F 2 151 ? -1.810  6.465  133.694 1.00 14.40 ? 151 MET C CE    1 
ATOM   5903 N  N     . PHE F 2 152 ? -3.187  5.327  139.164 1.00 7.49  ? 152 PHE C N     1 
ATOM   5904 C  CA    . PHE F 2 152 ? -2.848  6.322  140.175 1.00 8.19  ? 152 PHE C CA    1 
ATOM   5905 C  C     . PHE F 2 152 ? -2.478  5.849  141.556 1.00 8.55  ? 152 PHE C C     1 
ATOM   5906 O  O     . PHE F 2 152 ? -2.285  6.726  142.447 1.00 7.61  ? 152 PHE C O     1 
ATOM   5907 C  CB    . PHE F 2 152 ? -3.928  7.425  140.213 1.00 9.95  ? 152 PHE C CB    1 
ATOM   5908 C  CG    . PHE F 2 152 ? -4.195  8.034  138.870 1.00 11.80 ? 152 PHE C CG    1 
ATOM   5909 C  CD1   . PHE F 2 152 ? -3.288  8.896  138.286 1.00 12.21 ? 152 PHE C CD1   1 
ATOM   5910 C  CD2   . PHE F 2 152 ? -5.376  7.741  138.193 1.00 12.83 ? 152 PHE C CD2   1 
ATOM   5911 C  CE1   . PHE F 2 152 ? -3.549  9.482  137.043 1.00 11.60 ? 152 PHE C CE1   1 
ATOM   5912 C  CE2   . PHE F 2 152 ? -5.660  8.306  136.971 1.00 11.05 ? 152 PHE C CE2   1 
ATOM   5913 C  CZ    . PHE F 2 152 ? -4.746  9.172  136.389 1.00 11.47 ? 152 PHE C CZ    1 
ATOM   5914 N  N     . GLY F 2 153 ? -2.367  4.563  141.788 1.00 9.39  ? 153 GLY C N     1 
ATOM   5915 C  CA    . GLY F 2 153 ? -1.975  4.034  143.096 1.00 9.98  ? 153 GLY C CA    1 
ATOM   5916 C  C     . GLY F 2 153 ? -3.103  3.822  144.060 1.00 11.34 ? 153 GLY C C     1 
ATOM   5917 O  O     . GLY F 2 153 ? -4.273  3.977  143.721 1.00 12.18 ? 153 GLY C O     1 
ATOM   5918 N  N     . ASN F 2 154 ? -2.733  3.477  145.277 1.00 12.52 ? 154 ASN C N     1 
ATOM   5919 C  CA    . ASN F 2 154 ? -3.672  3.191  146.366 1.00 13.81 ? 154 ASN C CA    1 
ATOM   5920 C  C     . ASN F 2 154 ? -3.356  4.013  147.613 1.00 14.00 ? 154 ASN C C     1 
ATOM   5921 O  O     . ASN F 2 154 ? -3.623  3.530  148.730 1.00 15.31 ? 154 ASN C O     1 
ATOM   5922 C  CB    . ASN F 2 154 ? -3.658  1.672  146.626 1.00 14.33 ? 154 ASN C CB    1 
ATOM   5923 C  CG    . ASN F 2 154 ? -2.222  1.241  146.911 1.00 18.39 ? 154 ASN C CG    1 
ATOM   5924 O  OD1   . ASN F 2 154 ? -1.924  0.083  147.263 1.00 20.88 ? 154 ASN C OD1   1 
ATOM   5925 N  ND2   . ASN F 2 154 ? -1.269  2.182  146.768 1.00 17.24 ? 154 ASN C ND2   1 
ATOM   5926 N  N     . ALA F 2 155 ? -2.831  5.197  147.445 1.00 13.80 ? 155 ALA C N     1 
ATOM   5927 C  CA    . ALA F 2 155 ? -2.520  6.119  148.551 1.00 13.46 ? 155 ALA C CA    1 
ATOM   5928 C  C     . ALA F 2 155 ? -2.376  7.537  147.978 1.00 13.49 ? 155 ALA C C     1 
ATOM   5929 O  O     . ALA F 2 155 ? -1.858  7.763  146.859 1.00 13.97 ? 155 ALA C O     1 
ATOM   5930 C  CB    . ALA F 2 155 ? -1.314  5.649  149.296 1.00 14.28 ? 155 ALA C CB    1 
ATOM   5931 N  N     . ALA F 2 156 ? -2.856  8.500  148.751 1.00 12.11 ? 156 ALA C N     1 
ATOM   5932 C  CA    . ALA F 2 156 ? -2.873  9.896  148.384 1.00 11.56 ? 156 ALA C CA    1 
ATOM   5933 C  C     . ALA F 2 156 ? -1.579  10.522 147.944 1.00 11.62 ? 156 ALA C C     1 
ATOM   5934 O  O     . ALA F 2 156 ? -1.640  11.578 147.226 1.00 11.47 ? 156 ALA C O     1 
ATOM   5935 C  CB    . ALA F 2 156 ? -3.576  10.699 149.478 1.00 10.59 ? 156 ALA C CB    1 
ATOM   5936 N  N     . ALA F 2 157 ? -0.400  10.052 148.272 1.00 12.37 ? 157 ALA C N     1 
ATOM   5937 C  CA    . ALA F 2 157 ? 0.803   10.753 147.769 1.00 13.82 ? 157 ALA C CA    1 
ATOM   5938 C  C     . ALA F 2 157 ? 1.522   9.850  146.783 1.00 14.97 ? 157 ALA C C     1 
ATOM   5939 O  O     . ALA F 2 157 ? 2.730   9.993  146.544 1.00 16.15 ? 157 ALA C O     1 
ATOM   5940 C  CB    . ALA F 2 157 ? 1.671   11.201 148.898 1.00 16.18 ? 157 ALA C CB    1 
ATOM   5941 N  N     . SER F 2 158 ? 0.776   8.916  146.223 1.00 15.95 ? 158 SER C N     1 
ATOM   5942 C  CA    . SER F 2 158 ? 1.312   7.946  145.262 1.00 16.26 ? 158 SER C CA    1 
ATOM   5943 C  C     . SER F 2 158 ? 0.821   8.212  143.849 1.00 16.35 ? 158 SER C C     1 
ATOM   5944 O  O     . SER F 2 158 ? 1.136   7.397  142.966 1.00 17.26 ? 158 SER C O     1 
ATOM   5945 C  CB    . SER F 2 158 ? 0.823   6.537  145.627 1.00 14.81 ? 158 SER C CB    1 
ATOM   5946 O  OG    . SER F 2 158 ? 1.718   5.970  146.584 1.00 13.94 ? 158 SER C OG    1 
ATOM   5947 N  N     . ARG F 2 159 ? 0.096   9.293  143.718 1.00 13.53 ? 159 ARG C N     1 
ATOM   5948 C  CA    . ARG F 2 159 ? -0.517  9.672  142.467 1.00 11.76 ? 159 ARG C CA    1 
ATOM   5949 C  C     . ARG F 2 159 ? 0.347   9.966  141.285 1.00 11.92 ? 159 ARG C C     1 
ATOM   5950 O  O     . ARG F 2 159 ? -0.233  9.919  140.152 1.00 14.40 ? 159 ARG C O     1 
ATOM   5951 C  CB    . ARG F 2 159 ? -1.485  10.858 142.717 1.00 7.22  ? 159 ARG C CB    1 
ATOM   5952 C  CG    . ARG F 2 159 ? -2.166  10.639 144.069 1.00 6.30  ? 159 ARG C CG    1 
ATOM   5953 C  CD    . ARG F 2 159 ? -3.489  10.010 143.897 1.00 7.78  ? 159 ARG C CD    1 
ATOM   5954 N  NE    . ARG F 2 159 ? -3.557  8.600  144.176 1.00 8.61  ? 159 ARG C NE    1 
ATOM   5955 C  CZ    . ARG F 2 159 ? -4.448  8.049  145.007 1.00 9.06  ? 159 ARG C CZ    1 
ATOM   5956 N  NH1   . ARG F 2 159 ? -5.286  8.813  145.691 1.00 8.77  ? 159 ARG C NH1   1 
ATOM   5957 N  NH2   . ARG F 2 159 ? -4.507  6.733  145.188 1.00 9.03  ? 159 ARG C NH2   1 
ATOM   5958 N  N     . SER F 2 160 ? 1.622   10.249 141.425 1.00 9.97  ? 160 SER C N     1 
ATOM   5959 C  CA    . SER F 2 160 ? 2.390   10.543 140.173 1.00 7.91  ? 160 SER C CA    1 
ATOM   5960 C  C     . SER F 2 160 ? 3.578   9.615  140.008 1.00 8.27  ? 160 SER C C     1 
ATOM   5961 O  O     . SER F 2 160 ? 4.637   10.008 139.467 1.00 8.03  ? 160 SER C O     1 
ATOM   5962 C  CB    . SER F 2 160 ? 2.722   12.012 140.139 1.00 3.25  ? 160 SER C CB    1 
ATOM   5963 O  OG    . SER F 2 160 ? 3.398   12.416 141.310 1.00 3.27  ? 160 SER C OG    1 
ATOM   5964 N  N     . ASP F 2 161 ? 3.383   8.384  140.461 1.00 7.90  ? 161 ASP C N     1 
ATOM   5965 C  CA    . ASP F 2 161 ? 4.410   7.345  140.412 1.00 7.77  ? 161 ASP C CA    1 
ATOM   5966 C  C     . ASP F 2 161 ? 4.756   6.925  138.993 1.00 8.58  ? 161 ASP C C     1 
ATOM   5967 O  O     . ASP F 2 161 ? 5.930   6.609  138.742 1.00 8.62  ? 161 ASP C O     1 
ATOM   5968 C  CB    . ASP F 2 161 ? 3.991   6.182  141.299 1.00 8.71  ? 161 ASP C CB    1 
ATOM   5969 C  CG    . ASP F 2 161 ? 4.451   6.311  142.732 1.00 12.77 ? 161 ASP C CG    1 
ATOM   5970 O  OD1   . ASP F 2 161 ? 4.920   7.401  143.114 1.00 16.34 ? 161 ASP C OD1   1 
ATOM   5971 O  OD2   . ASP F 2 161 ? 4.338   5.305  143.472 1.00 14.31 ? 161 ASP C OD2   1 
ATOM   5972 N  N     . GLN F 2 162 ? 3.796   6.928  138.108 1.00 9.18  ? 162 GLN C N     1 
ATOM   5973 C  CA    . GLN F 2 162 ? 3.890   6.518  136.707 1.00 10.57 ? 162 GLN C CA    1 
ATOM   5974 C  C     . GLN F 2 162 ? 3.668   7.581  135.644 1.00 12.06 ? 162 GLN C C     1 
ATOM   5975 O  O     . GLN F 2 162 ? 4.137   7.465  134.496 1.00 13.63 ? 162 GLN C O     1 
ATOM   5976 C  CB    . GLN F 2 162 ? 2.774   5.468  136.471 1.00 9.18  ? 162 GLN C CB    1 
ATOM   5977 C  CG    . GLN F 2 162 ? 2.679   4.510  137.647 1.00 10.39 ? 162 GLN C CG    1 
ATOM   5978 C  CD    . GLN F 2 162 ? 1.900   3.291  137.208 1.00 13.43 ? 162 GLN C CD    1 
ATOM   5979 O  OE1   . GLN F 2 162 ? 1.973   2.962  136.011 1.00 16.18 ? 162 GLN C OE1   1 
ATOM   5980 N  NE2   . GLN F 2 162 ? 1.193   2.674  138.143 1.00 14.84 ? 162 GLN C NE2   1 
ATOM   5981 N  N     . VAL F 2 163 ? 2.915   8.602  135.996 1.00 11.87 ? 163 VAL C N     1 
ATOM   5982 C  CA    . VAL F 2 163 ? 2.573   9.722  135.084 1.00 10.90 ? 163 VAL C CA    1 
ATOM   5983 C  C     . VAL F 2 163 ? 2.781   11.027 135.818 1.00 11.37 ? 163 VAL C C     1 
ATOM   5984 O  O     . VAL F 2 163 ? 2.316   11.161 136.960 1.00 12.49 ? 163 VAL C O     1 
ATOM   5985 C  CB    . VAL F 2 163 ? 1.126   9.389  134.667 1.00 9.78  ? 163 VAL C CB    1 
ATOM   5986 C  CG1   . VAL F 2 163 ? 0.155   10.485 135.013 1.00 7.88  ? 163 VAL C CG1   1 
ATOM   5987 C  CG2   . VAL F 2 163 ? 1.102   8.947  133.236 1.00 9.17  ? 163 VAL C CG2   1 
ATOM   5988 N  N     . SER F 2 164 ? 3.491   11.960 135.211 1.00 11.63 ? 164 SER C N     1 
ATOM   5989 C  CA    . SER F 2 164 ? 3.788   13.256 135.831 1.00 11.31 ? 164 SER C CA    1 
ATOM   5990 C  C     . SER F 2 164 ? 2.777   14.331 135.498 1.00 10.90 ? 164 SER C C     1 
ATOM   5991 O  O     . SER F 2 164 ? 2.563   15.217 136.352 1.00 11.73 ? 164 SER C O     1 
ATOM   5992 C  CB    . SER F 2 164 ? 5.217   13.682 135.548 1.00 12.57 ? 164 SER C CB    1 
ATOM   5993 O  OG    . SER F 2 164 ? 5.328   14.573 134.452 1.00 13.01 ? 164 SER C OG    1 
ATOM   5994 N  N     . SER F 2 165 ? 2.195   14.328 134.319 1.00 10.10 ? 165 SER C N     1 
ATOM   5995 C  CA    . SER F 2 165 ? 1.199   15.357 133.930 1.00 9.50  ? 165 SER C CA    1 
ATOM   5996 C  C     . SER F 2 165 ? 0.332   14.786 132.801 1.00 9.54  ? 165 SER C C     1 
ATOM   5997 O  O     . SER F 2 165 ? 0.689   13.733 132.253 1.00 10.25 ? 165 SER C O     1 
ATOM   5998 C  CB    . SER F 2 165 ? 1.824   16.676 133.540 1.00 8.94  ? 165 SER C CB    1 
ATOM   5999 O  OG    . SER F 2 165 ? 3.093   16.461 132.954 1.00 12.09 ? 165 SER C OG    1 
ATOM   6000 N  N     . PHE F 2 166 ? -0.747  15.493 132.516 1.00 9.10  ? 166 PHE C N     1 
ATOM   6001 C  CA    . PHE F 2 166 ? -1.718  15.046 131.508 1.00 9.13  ? 166 PHE C CA    1 
ATOM   6002 C  C     . PHE F 2 166 ? -2.344  16.254 130.821 1.00 9.59  ? 166 PHE C C     1 
ATOM   6003 O  O     . PHE F 2 166 ? -2.132  17.398 131.231 1.00 9.10  ? 166 PHE C O     1 
ATOM   6004 C  CB    . PHE F 2 166 ? -2.832  14.257 132.252 1.00 7.28  ? 166 PHE C CB    1 
ATOM   6005 C  CG    . PHE F 2 166 ? -3.634  15.214 133.129 1.00 6.93  ? 166 PHE C CG    1 
ATOM   6006 C  CD1   . PHE F 2 166 ? -3.215  15.515 134.419 1.00 5.20  ? 166 PHE C CD1   1 
ATOM   6007 C  CD2   . PHE F 2 166 ? -4.803  15.815 132.628 1.00 6.04  ? 166 PHE C CD2   1 
ATOM   6008 C  CE1   . PHE F 2 166 ? -3.929  16.397 135.220 1.00 5.00  ? 166 PHE C CE1   1 
ATOM   6009 C  CE2   . PHE F 2 166 ? -5.512  16.703 133.426 1.00 7.35  ? 166 PHE C CE2   1 
ATOM   6010 C  CZ    . PHE F 2 166 ? -5.083  17.000 134.719 1.00 6.67  ? 166 PHE C CZ    1 
ATOM   6011 N  N     . ARG F 2 167 ? -3.164  15.943 129.829 1.00 9.90  ? 167 ARG C N     1 
ATOM   6012 C  CA    . ARG F 2 167 ? -3.874  17.002 129.063 1.00 10.07 ? 167 ARG C CA    1 
ATOM   6013 C  C     . ARG F 2 167 ? -4.995  16.314 128.319 1.00 10.93 ? 167 ARG C C     1 
ATOM   6014 O  O     . ARG F 2 167 ? -4.747  15.287 127.665 1.00 11.56 ? 167 ARG C O     1 
ATOM   6015 C  CB    . ARG F 2 167 ? -2.881  17.765 128.209 1.00 8.71  ? 167 ARG C CB    1 
ATOM   6016 C  CG    . ARG F 2 167 ? -2.784  17.473 126.754 1.00 10.76 ? 167 ARG C CG    1 
ATOM   6017 C  CD    . ARG F 2 167 ? -1.422  17.350 126.192 1.00 13.71 ? 167 ARG C CD    1 
ATOM   6018 N  NE    . ARG F 2 167 ? -1.066  18.458 125.372 1.00 12.80 ? 167 ARG C NE    1 
ATOM   6019 C  CZ    . ARG F 2 167 ? -0.609  18.514 124.138 1.00 14.74 ? 167 ARG C CZ    1 
ATOM   6020 N  NH1   . ARG F 2 167 ? -0.486  17.448 123.357 1.00 13.15 ? 167 ARG C NH1   1 
ATOM   6021 N  NH2   . ARG F 2 167 ? -0.264  19.691 123.594 1.00 17.42 ? 167 ARG C NH2   1 
ATOM   6022 N  N     . TYR F 2 168 ? -6.216  16.812 128.485 1.00 11.52 ? 168 TYR C N     1 
ATOM   6023 C  CA    . TYR F 2 168 ? -7.394  16.218 127.840 1.00 12.12 ? 168 TYR C CA    1 
ATOM   6024 C  C     . TYR F 2 168 ? -7.483  16.522 126.343 1.00 12.30 ? 168 TYR C C     1 
ATOM   6025 O  O     . TYR F 2 168 ? -7.197  17.624 125.839 1.00 11.92 ? 168 TYR C O     1 
ATOM   6026 C  CB    . TYR F 2 168 ? -8.705  16.666 128.488 1.00 12.28 ? 168 TYR C CB    1 
ATOM   6027 C  CG    . TYR F 2 168 ? -9.094  15.995 129.772 1.00 12.07 ? 168 TYR C CG    1 
ATOM   6028 C  CD1   . TYR F 2 168 ? -8.559  16.435 130.979 1.00 9.96  ? 168 TYR C CD1   1 
ATOM   6029 C  CD2   . TYR F 2 168 ? -10.018 14.955 129.813 1.00 11.77 ? 168 TYR C CD2   1 
ATOM   6030 C  CE1   . TYR F 2 168 ? -8.902  15.863 132.191 1.00 8.36  ? 168 TYR C CE1   1 
ATOM   6031 C  CE2   . TYR F 2 168 ? -10.375 14.361 131.011 1.00 10.89 ? 168 TYR C CE2   1 
ATOM   6032 C  CZ    . TYR F 2 168 ? -9.809  14.821 132.200 1.00 10.31 ? 168 TYR C CZ    1 
ATOM   6033 O  OH    . TYR F 2 168 ? -10.140 14.257 133.414 1.00 12.27 ? 168 TYR C OH    1 
ATOM   6034 N  N     . ALA F 2 169 ? -7.967  15.498 125.652 1.00 12.77 ? 169 ALA C N     1 
ATOM   6035 C  CA    . ALA F 2 169 ? -8.153  15.636 124.200 1.00 13.50 ? 169 ALA C CA    1 
ATOM   6036 C  C     . ALA F 2 169 ? -9.647  15.642 123.895 1.00 14.02 ? 169 ALA C C     1 
ATOM   6037 O  O     . ALA F 2 169 ? -10.128 16.366 122.990 1.00 14.66 ? 169 ALA C O     1 
ATOM   6038 C  CB    . ALA F 2 169 ? -7.381  14.549 123.494 1.00 13.40 ? 169 ALA C CB    1 
ATOM   6039 N  N     . SER F 2 170 ? -10.374 14.867 124.699 1.00 14.29 ? 170 SER C N     1 
ATOM   6040 C  CA    . SER F 2 170 ? -11.827 14.686 124.527 1.00 13.91 ? 170 SER C CA    1 
ATOM   6041 C  C     . SER F 2 170 ? -12.483 14.317 125.832 1.00 14.53 ? 170 SER C C     1 
ATOM   6042 O  O     . SER F 2 170 ? -11.847 13.739 126.732 1.00 15.46 ? 170 SER C O     1 
ATOM   6043 C  CB    . SER F 2 170 ? -12.026 13.640 123.446 1.00 11.54 ? 170 SER C CB    1 
ATOM   6044 O  OG    . SER F 2 170 ? -12.772 12.507 123.787 1.00 10.97 ? 170 SER C OG    1 
ATOM   6045 N  N     . MET F 2 171 ? -13.764 14.644 125.911 1.00 14.50 ? 171 MET C N     1 
ATOM   6046 C  CA    . MET F 2 171 ? -14.583 14.332 127.113 1.00 13.01 ? 171 MET C CA    1 
ATOM   6047 C  C     . MET F 2 171 ? -16.075 14.370 126.721 1.00 12.34 ? 171 MET C C     1 
ATOM   6048 O  O     . MET F 2 171 ? -16.659 15.448 126.539 1.00 13.00 ? 171 MET C O     1 
ATOM   6049 C  CB    . MET F 2 171 ? -14.292 15.316 128.239 1.00 12.36 ? 171 MET C CB    1 
ATOM   6050 C  CG    . MET F 2 171 ? -14.920 14.936 129.579 1.00 12.71 ? 171 MET C CG    1 
ATOM   6051 S  SD    . MET F 2 171 ? -14.818 16.252 130.779 1.00 14.45 ? 171 MET C SD    1 
ATOM   6052 C  CE    . MET F 2 171 ? -13.114 16.648 131.113 1.00 15.12 ? 171 MET C CE    1 
ATOM   6053 N  N     . ASN F 2 172 ? -16.656 13.173 126.587 1.00 11.54 ? 172 ASN C N     1 
ATOM   6054 C  CA    . ASN F 2 172 ? -18.083 13.011 126.203 1.00 10.33 ? 172 ASN C CA    1 
ATOM   6055 C  C     . ASN F 2 172 ? -18.842 12.055 127.139 1.00 9.85  ? 172 ASN C C     1 
ATOM   6056 O  O     . ASN F 2 172 ? -18.239 11.177 127.780 1.00 9.77  ? 172 ASN C O     1 
ATOM   6057 C  CB    . ASN F 2 172 ? -18.239 12.401 124.801 1.00 10.53 ? 172 ASN C CB    1 
ATOM   6058 C  CG    . ASN F 2 172 ? -17.174 12.841 123.798 1.00 11.19 ? 172 ASN C CG    1 
ATOM   6059 O  OD1   . ASN F 2 172 ? -16.050 12.348 123.845 1.00 12.82 ? 172 ASN C OD1   1 
ATOM   6060 N  ND2   . ASN F 2 172 ? -17.466 13.739 122.875 1.00 10.60 ? 172 ASN C ND2   1 
ATOM   6061 N  N     . VAL F 2 173 ? -20.152 12.284 127.148 1.00 9.20  ? 173 VAL C N     1 
ATOM   6062 C  CA    . VAL F 2 173 ? -21.136 11.504 127.923 1.00 9.01  ? 173 VAL C CA    1 
ATOM   6063 C  C     . VAL F 2 173 ? -22.304 11.087 127.042 1.00 9.73  ? 173 VAL C C     1 
ATOM   6064 O  O     . VAL F 2 173 ? -22.645 11.775 126.068 1.00 11.07 ? 173 VAL C O     1 
ATOM   6065 C  CB    . VAL F 2 173 ? -21.772 12.336 129.037 1.00 7.23  ? 173 VAL C CB    1 
ATOM   6066 C  CG1   . VAL F 2 173 ? -20.939 12.375 130.312 1.00 6.69  ? 173 VAL C CG1   1 
ATOM   6067 C  CG2   . VAL F 2 173 ? -22.007 13.791 128.631 1.00 7.57  ? 173 VAL C CG2   1 
ATOM   6068 N  N     . GLY F 2 174 ? -22.885 9.980  127.429 1.00 8.94  ? 174 GLY C N     1 
ATOM   6069 C  CA    . GLY F 2 174 ? -24.038 9.414  126.739 1.00 7.79  ? 174 GLY C CA    1 
ATOM   6070 C  C     . GLY F 2 174 ? -24.876 8.605  127.722 1.00 7.74  ? 174 GLY C C     1 
ATOM   6071 O  O     . GLY F 2 174 ? -24.378 7.674  128.370 1.00 6.95  ? 174 GLY C O     1 
ATOM   6072 N  N     . ILE F 2 175 ? -26.129 8.998  127.811 1.00 8.52  ? 175 ILE C N     1 
ATOM   6073 C  CA    . ILE F 2 175 ? -27.112 8.308  128.652 1.00 8.56  ? 175 ILE C CA    1 
ATOM   6074 C  C     . ILE F 2 175 ? -28.151 7.646  127.717 1.00 8.72  ? 175 ILE C C     1 
ATOM   6075 O  O     . ILE F 2 175 ? -28.865 8.367  127.002 1.00 8.26  ? 175 ILE C O     1 
ATOM   6076 C  CB    . ILE F 2 175 ? -27.769 9.285  129.628 1.00 7.60  ? 175 ILE C CB    1 
ATOM   6077 C  CG1   . ILE F 2 175 ? -26.825 9.712  130.758 1.00 5.91  ? 175 ILE C CG1   1 
ATOM   6078 C  CG2   . ILE F 2 175 ? -29.002 8.696  130.321 1.00 6.88  ? 175 ILE C CG2   1 
ATOM   6079 C  CD1   . ILE F 2 175 ? -27.243 11.020 131.431 1.00 5.13  ? 175 ILE C CD1   1 
ATOM   6080 N  N     . TYR F 2 176 ? -28.180 6.347  127.760 1.00 8.71  ? 176 TYR C N     1 
ATOM   6081 C  CA    . TYR F 2 176 ? -29.079 5.482  126.977 1.00 9.76  ? 176 TYR C CA    1 
ATOM   6082 C  C     . TYR F 2 176 ? -30.123 4.848  127.882 1.00 10.38 ? 176 TYR C C     1 
ATOM   6083 O  O     . TYR F 2 176 ? -29.869 3.808  128.533 1.00 11.56 ? 176 TYR C O     1 
ATOM   6084 C  CB    . TYR F 2 176 ? -28.159 4.420  126.318 1.00 10.10 ? 176 TYR C CB    1 
ATOM   6085 C  CG    . TYR F 2 176 ? -27.023 5.093  125.560 1.00 9.27  ? 176 TYR C CG    1 
ATOM   6086 C  CD1   . TYR F 2 176 ? -27.247 5.639  124.296 1.00 9.46  ? 176 TYR C CD1   1 
ATOM   6087 C  CD2   . TYR F 2 176 ? -25.741 5.201  126.090 1.00 8.04  ? 176 TYR C CD2   1 
ATOM   6088 C  CE1   . TYR F 2 176 ? -26.241 6.278  123.598 1.00 10.28 ? 176 TYR C CE1   1 
ATOM   6089 C  CE2   . TYR F 2 176 ? -24.725 5.838  125.390 1.00 9.32  ? 176 TYR C CE2   1 
ATOM   6090 C  CZ    . TYR F 2 176 ? -24.971 6.376  124.140 1.00 10.55 ? 176 TYR C CZ    1 
ATOM   6091 O  OH    . TYR F 2 176 ? -23.961 7.001  123.464 1.00 9.48  ? 176 TYR C OH    1 
ATOM   6092 N  N     . PRO F 2 177 ? -31.285 5.483  127.981 1.00 9.81  ? 177 PRO C N     1 
ATOM   6093 C  CA    . PRO F 2 177 ? -32.361 5.014  128.878 1.00 9.35  ? 177 PRO C CA    1 
ATOM   6094 C  C     . PRO F 2 177 ? -32.690 3.557  128.646 1.00 8.98  ? 177 PRO C C     1 
ATOM   6095 O  O     . PRO F 2 177 ? -32.689 3.114  127.478 1.00 9.90  ? 177 PRO C O     1 
ATOM   6096 C  CB    . PRO F 2 177 ? -33.528 5.958  128.636 1.00 9.42  ? 177 PRO C CB    1 
ATOM   6097 C  CG    . PRO F 2 177 ? -32.957 7.161  127.944 1.00 9.78  ? 177 PRO C CG    1 
ATOM   6098 C  CD    . PRO F 2 177 ? -31.653 6.722  127.284 1.00 9.33  ? 177 PRO C CD    1 
ATOM   6099 N  N     . THR F 2 178 ? -32.932 2.816  129.724 1.00 7.86  ? 178 THR C N     1 
ATOM   6100 C  CA    . THR F 2 178 ? -33.256 1.388  129.566 1.00 7.56  ? 178 THR C CA    1 
ATOM   6101 C  C     . THR F 2 178 ? -34.621 1.124  130.205 1.00 8.45  ? 178 THR C C     1 
ATOM   6102 O  O     . THR F 2 178 ? -34.881 -0.041 130.581 1.00 9.23  ? 178 THR C O     1 
ATOM   6103 C  CB    . THR F 2 178 ? -32.187 0.404  130.139 1.00 6.61  ? 178 THR C CB    1 
ATOM   6104 O  OG1   . THR F 2 178 ? -31.973 0.805  131.523 1.00 7.66  ? 178 THR C OG1   1 
ATOM   6105 C  CG2   . THR F 2 178 ? -30.846 0.302  129.429 1.00 6.47  ? 178 THR C CG2   1 
ATOM   6106 N  N     . SER F 2 179 ? -35.417 2.190  130.319 1.00 8.97  ? 179 SER C N     1 
ATOM   6107 C  CA    . SER F 2 179 ? -36.766 2.018  130.899 1.00 9.89  ? 179 SER C CA    1 
ATOM   6108 C  C     . SER F 2 179 ? -37.746 1.635  129.781 1.00 10.73 ? 179 SER C C     1 
ATOM   6109 O  O     . SER F 2 179 ? -37.398 1.769  128.607 1.00 12.42 ? 179 SER C O     1 
ATOM   6110 C  CB    . SER F 2 179 ? -37.277 3.244  131.607 1.00 10.46 ? 179 SER C CB    1 
ATOM   6111 O  OG    . SER F 2 179 ? -36.245 4.094  132.049 1.00 12.16 ? 179 SER C OG    1 
ATOM   6112 N  N     . ASN F 2 180 ? -38.914 1.192  130.211 1.00 10.65 ? 180 ASN C N     1 
ATOM   6113 C  CA    . ASN F 2 180 ? -39.993 0.815  129.254 1.00 9.88  ? 180 ASN C CA    1 
ATOM   6114 C  C     . ASN F 2 180 ? -40.799 2.104  129.014 1.00 9.66  ? 180 ASN C C     1 
ATOM   6115 O  O     . ASN F 2 180 ? -40.742 3.024  129.862 1.00 10.64 ? 180 ASN C O     1 
ATOM   6116 C  CB    . ASN F 2 180 ? -40.717 -0.411 129.745 1.00 9.61  ? 180 ASN C CB    1 
ATOM   6117 C  CG    . ASN F 2 180 ? -41.707 -0.145 130.863 1.00 9.56  ? 180 ASN C CG    1 
ATOM   6118 O  OD1   . ASN F 2 180 ? -42.541 0.761  130.725 1.00 8.00  ? 180 ASN C OD1   1 
ATOM   6119 N  ND2   . ASN F 2 180 ? -41.631 -0.888 131.957 1.00 11.74 ? 180 ASN C ND2   1 
ATOM   6120 N  N     . LEU F 2 181 ? -41.474 2.236  127.900 1.00 9.13  ? 181 LEU C N     1 
ATOM   6121 C  CA    . LEU F 2 181 ? -42.175 3.455  127.517 1.00 7.87  ? 181 LEU C CA    1 
ATOM   6122 C  C     . LEU F 2 181 ? -43.453 3.675  128.303 1.00 8.23  ? 181 LEU C C     1 
ATOM   6123 O  O     . LEU F 2 181 ? -44.236 4.601  128.007 1.00 9.43  ? 181 LEU C O     1 
ATOM   6124 C  CB    . LEU F 2 181 ? -42.430 3.421  126.000 1.00 3.68  ? 181 LEU C CB    1 
ATOM   6125 C  CG    . LEU F 2 181 ? -41.278 3.344  125.016 1.00 3.28  ? 181 LEU C CG    1 
ATOM   6126 C  CD1   . LEU F 2 181 ? -41.772 3.369  123.568 1.00 2.24  ? 181 LEU C CD1   1 
ATOM   6127 C  CD2   . LEU F 2 181 ? -40.334 4.528  125.247 1.00 4.69  ? 181 LEU C CD2   1 
ATOM   6128 N  N     . MET F 2 182 ? -43.652 2.835  129.291 1.00 7.51  ? 182 MET C N     1 
ATOM   6129 C  CA    . MET F 2 182 ? -44.896 2.908  130.084 1.00 7.64  ? 182 MET C CA    1 
ATOM   6130 C  C     . MET F 2 182 ? -44.693 3.391  131.502 1.00 8.65  ? 182 MET C C     1 
ATOM   6131 O  O     . MET F 2 182 ? -45.670 3.903  132.111 1.00 10.76 ? 182 MET C O     1 
ATOM   6132 C  CB    . MET F 2 182 ? -45.576 1.529  129.994 1.00 5.45  ? 182 MET C CB    1 
ATOM   6133 C  CG    . MET F 2 182 ? -46.873 1.534  129.282 1.00 5.83  ? 182 MET C CG    1 
ATOM   6134 S  SD    . MET F 2 182 ? -46.753 2.207  127.559 1.00 8.02  ? 182 MET C SD    1 
ATOM   6135 C  CE    . MET F 2 182 ? -48.440 1.762  127.057 1.00 7.95  ? 182 MET C CE    1 
ATOM   6136 N  N     . GLN F 2 183 ? -43.493 3.273  132.027 1.00 8.56  ? 183 GLN C N     1 
ATOM   6137 C  CA    . GLN F 2 183 ? -43.173 3.657  133.398 1.00 8.66  ? 183 GLN C CA    1 
ATOM   6138 C  C     . GLN F 2 183 ? -42.129 4.715  133.639 1.00 9.73  ? 183 GLN C C     1 
ATOM   6139 O  O     . GLN F 2 183 ? -41.855 4.993  134.859 1.00 10.70 ? 183 GLN C O     1 
ATOM   6140 C  CB    . GLN F 2 183 ? -42.673 2.363  134.098 1.00 8.32  ? 183 GLN C CB    1 
ATOM   6141 C  CG    . GLN F 2 183 ? -43.745 1.301  133.764 1.00 12.19 ? 183 GLN C CG    1 
ATOM   6142 C  CD    . GLN F 2 183 ? -44.723 1.310  134.922 1.00 15.54 ? 183 GLN C CD    1 
ATOM   6143 O  OE1   . GLN F 2 183 ? -44.619 0.463  135.805 1.00 16.99 ? 183 GLN C OE1   1 
ATOM   6144 N  NE2   . GLN F 2 183 ? -45.678 2.228  134.815 1.00 18.85 ? 183 GLN C NE2   1 
ATOM   6145 N  N     . PHE F 2 184 ? -41.539 5.246  132.585 1.00 9.06  ? 184 PHE C N     1 
ATOM   6146 C  CA    . PHE F 2 184 ? -40.508 6.295  132.771 1.00 9.15  ? 184 PHE C CA    1 
ATOM   6147 C  C     . PHE F 2 184 ? -41.289 7.606  132.945 1.00 10.27 ? 184 PHE C C     1 
ATOM   6148 O  O     . PHE F 2 184 ? -42.492 7.682  132.654 1.00 11.74 ? 184 PHE C O     1 
ATOM   6149 C  CB    . PHE F 2 184 ? -39.597 6.389  131.547 1.00 7.01  ? 184 PHE C CB    1 
ATOM   6150 C  CG    . PHE F 2 184 ? -40.232 7.187  130.437 1.00 7.41  ? 184 PHE C CG    1 
ATOM   6151 C  CD1   . PHE F 2 184 ? -41.057 6.534  129.504 1.00 7.05  ? 184 PHE C CD1   1 
ATOM   6152 C  CD2   . PHE F 2 184 ? -40.072 8.569  130.364 1.00 6.84  ? 184 PHE C CD2   1 
ATOM   6153 C  CE1   . PHE F 2 184 ? -41.696 7.259  128.518 1.00 5.64  ? 184 PHE C CE1   1 
ATOM   6154 C  CE2   . PHE F 2 184 ? -40.720 9.322  129.381 1.00 4.63  ? 184 PHE C CE2   1 
ATOM   6155 C  CZ    . PHE F 2 184 ? -41.524 8.655  128.459 1.00 4.57  ? 184 PHE C CZ    1 
ATOM   6156 N  N     . ALA F 2 185 ? -40.560 8.606  133.353 1.00 9.81  ? 185 ALA C N     1 
ATOM   6157 C  CA    . ALA F 2 185 ? -41.111 9.960  133.520 1.00 9.72  ? 185 ALA C CA    1 
ATOM   6158 C  C     . ALA F 2 185 ? -39.946 10.866 133.920 1.00 10.64 ? 185 ALA C C     1 
ATOM   6159 O  O     . ALA F 2 185 ? -39.039 10.345 134.594 1.00 11.74 ? 185 ALA C O     1 
ATOM   6160 C  CB    . ALA F 2 185 ? -42.168 9.980  134.597 1.00 7.87  ? 185 ALA C CB    1 
ATOM   6161 N  N     . GLY F 2 186 ? -40.034 12.111 133.530 1.00 10.81 ? 186 GLY C N     1 
ATOM   6162 C  CA    . GLY F 2 186 ? -38.987 13.074 133.848 1.00 10.68 ? 186 GLY C CA    1 
ATOM   6163 C  C     . GLY F 2 186 ? -38.341 13.656 132.600 1.00 10.67 ? 186 GLY C C     1 
ATOM   6164 O  O     . GLY F 2 186 ? -38.680 13.411 131.430 1.00 11.00 ? 186 GLY C O     1 
ATOM   6165 N  N     . SER F 2 187 ? -37.337 14.466 132.903 1.00 10.44 ? 187 SER C N     1 
ATOM   6166 C  CA    . SER F 2 187 ? -36.584 15.188 131.863 1.00 9.72  ? 187 SER C CA    1 
ATOM   6167 C  C     . SER F 2 187 ? -35.095 15.047 132.193 1.00 9.90  ? 187 SER C C     1 
ATOM   6168 O  O     . SER F 2 187 ? -34.786 14.676 133.333 1.00 10.26 ? 187 SER C O     1 
ATOM   6169 C  CB    . SER F 2 187 ? -37.012 16.653 131.937 1.00 8.88  ? 187 SER C CB    1 
ATOM   6170 O  OG    . SER F 2 187 ? -36.816 17.157 133.270 1.00 5.57  ? 187 SER C OG    1 
ATOM   6171 N  N     . ILE F 2 188 ? -34.312 15.332 131.186 1.00 9.41  ? 188 ILE C N     1 
ATOM   6172 C  CA    . ILE F 2 188 ? -32.862 15.368 131.186 1.00 9.68  ? 188 ILE C CA    1 
ATOM   6173 C  C     . ILE F 2 188 ? -32.477 16.801 130.744 1.00 10.60 ? 188 ILE C C     1 
ATOM   6174 O  O     . ILE F 2 188 ? -33.044 17.306 129.755 1.00 11.76 ? 188 ILE C O     1 
ATOM   6175 C  CB    . ILE F 2 188 ? -32.186 14.314 130.283 1.00 8.83  ? 188 ILE C CB    1 
ATOM   6176 C  CG1   . ILE F 2 188 ? -32.377 12.890 130.858 1.00 7.06  ? 188 ILE C CG1   1 
ATOM   6177 C  CG2   . ILE F 2 188 ? -30.677 14.666 130.057 1.00 8.59  ? 188 ILE C CG2   1 
ATOM   6178 C  CD1   . ILE F 2 188 ? -31.507 11.853 130.084 1.00 6.60  ? 188 ILE C CD1   1 
ATOM   6179 N  N     . THR F 2 189 ? -31.591 17.376 131.522 1.00 10.42 ? 189 THR C N     1 
ATOM   6180 C  CA    . THR F 2 189 ? -31.130 18.754 131.303 1.00 9.62  ? 189 THR C CA    1 
ATOM   6181 C  C     . THR F 2 189 ? -29.613 18.861 131.408 1.00 9.05  ? 189 THR C C     1 
ATOM   6182 O  O     . THR F 2 189 ? -29.039 18.511 132.446 1.00 7.42  ? 189 THR C O     1 
ATOM   6183 C  CB    . THR F 2 189 ? -31.810 19.769 132.297 1.00 9.71  ? 189 THR C CB    1 
ATOM   6184 O  OG1   . THR F 2 189 ? -33.128 19.201 132.627 1.00 12.50 ? 189 THR C OG1   1 
ATOM   6185 C  CG2   . THR F 2 189 ? -31.911 21.180 131.759 1.00 7.45  ? 189 THR C CG2   1 
ATOM   6186 N  N     . VAL F 2 190 ? -29.027 19.359 130.330 1.00 9.12  ? 190 VAL C N     1 
ATOM   6187 C  CA    . VAL F 2 190 ? -27.605 19.572 130.201 1.00 9.46  ? 190 VAL C CA    1 
ATOM   6188 C  C     . VAL F 2 190 ? -27.246 21.058 130.041 1.00 9.87  ? 190 VAL C C     1 
ATOM   6189 O  O     . VAL F 2 190 ? -27.885 21.797 129.295 1.00 10.87 ? 190 VAL C O     1 
ATOM   6190 C  CB    . VAL F 2 190 ? -27.018 18.816 128.981 1.00 10.08 ? 190 VAL C CB    1 
ATOM   6191 C  CG1   . VAL F 2 190 ? -25.503 19.032 128.912 1.00 9.73  ? 190 VAL C CG1   1 
ATOM   6192 C  CG2   . VAL F 2 190 ? -27.397 17.358 128.943 1.00 10.41 ? 190 VAL C CG2   1 
ATOM   6193 N  N     . TRP F 2 191 ? -26.166 21.391 130.707 1.00 9.64  ? 191 TRP C N     1 
ATOM   6194 C  CA    . TRP F 2 191 ? -25.577 22.747 130.661 1.00 8.53  ? 191 TRP C CA    1 
ATOM   6195 C  C     . TRP F 2 191 ? -24.110 22.572 131.047 1.00 8.42  ? 191 TRP C C     1 
ATOM   6196 O  O     . TRP F 2 191 ? -23.770 21.533 131.675 1.00 7.83  ? 191 TRP C O     1 
ATOM   6197 C  CB    . TRP F 2 191 ? -26.369 23.750 131.402 1.00 8.55  ? 191 TRP C CB    1 
ATOM   6198 C  CG    . TRP F 2 191 ? -26.350 23.881 132.872 1.00 9.00  ? 191 TRP C CG    1 
ATOM   6199 C  CD1   . TRP F 2 191 ? -25.538 24.667 133.648 1.00 8.78  ? 191 TRP C CD1   1 
ATOM   6200 C  CD2   . TRP F 2 191 ? -27.234 23.213 133.792 1.00 8.80  ? 191 TRP C CD2   1 
ATOM   6201 N  NE1   . TRP F 2 191 ? -25.841 24.507 134.973 1.00 7.84  ? 191 TRP C NE1   1 
ATOM   6202 C  CE2   . TRP F 2 191 ? -26.871 23.621 135.088 1.00 7.54  ? 191 TRP C CE2   1 
ATOM   6203 C  CE3   . TRP F 2 191 ? -28.267 22.306 133.617 1.00 9.73  ? 191 TRP C CE3   1 
ATOM   6204 C  CZ2   . TRP F 2 191 ? -27.520 23.145 136.221 1.00 8.03  ? 191 TRP C CZ2   1 
ATOM   6205 C  CZ3   . TRP F 2 191 ? -28.942 21.855 134.725 1.00 9.00  ? 191 TRP C CZ3   1 
ATOM   6206 C  CH2   . TRP F 2 191 ? -28.573 22.255 136.011 1.00 9.53  ? 191 TRP C CH2   1 
ATOM   6207 N  N     . LYS F 2 192 ? -23.285 23.537 130.667 1.00 8.29  ? 192 LYS C N     1 
ATOM   6208 C  CA    . LYS F 2 192 ? -21.841 23.379 131.015 1.00 8.36  ? 192 LYS C CA    1 
ATOM   6209 C  C     . LYS F 2 192 ? -21.299 24.600 131.724 1.00 8.91  ? 192 LYS C C     1 
ATOM   6210 O  O     . LYS F 2 192 ? -21.608 25.759 131.389 1.00 8.74  ? 192 LYS C O     1 
ATOM   6211 C  CB    . LYS F 2 192 ? -21.047 23.000 129.776 1.00 6.58  ? 192 LYS C CB    1 
ATOM   6212 C  CG    . LYS F 2 192 ? -21.802 22.000 128.893 1.00 5.81  ? 192 LYS C CG    1 
ATOM   6213 C  CD    . LYS F 2 192 ? -21.362 22.076 127.448 1.00 5.51  ? 192 LYS C CD    1 
ATOM   6214 C  CE    . LYS F 2 192 ? -21.959 20.924 126.668 1.00 6.46  ? 192 LYS C CE    1 
ATOM   6215 N  NZ    . LYS F 2 192 ? -22.111 21.284 125.247 1.00 9.83  ? 192 LYS C NZ    1 
ATOM   6216 N  N     . CYS F 2 193 ? -20.485 24.276 132.730 1.00 9.25  ? 193 CYS C N     1 
ATOM   6217 C  CA    . CYS F 2 193 ? -19.857 25.293 133.579 1.00 9.42  ? 193 CYS C CA    1 
ATOM   6218 C  C     . CYS F 2 193 ? -18.351 25.318 133.440 1.00 9.29  ? 193 CYS C C     1 
ATOM   6219 O  O     . CYS F 2 193 ? -17.722 24.260 133.241 1.00 8.08  ? 193 CYS C O     1 
ATOM   6220 C  CB    . CYS F 2 193 ? -20.258 25.036 135.043 1.00 12.84 ? 193 CYS C CB    1 
ATOM   6221 S  SG    . CYS F 2 193 ? -22.061 24.819 135.239 1.00 18.61 ? 193 CYS C SG    1 
ATOM   6222 N  N     . PRO F 2 194 ? -17.787 26.510 133.569 1.00 9.78  ? 194 PRO C N     1 
ATOM   6223 C  CA    . PRO F 2 194 ? -16.324 26.696 133.498 1.00 10.16 ? 194 PRO C CA    1 
ATOM   6224 C  C     . PRO F 2 194 ? -15.726 26.652 134.903 1.00 10.87 ? 194 PRO C C     1 
ATOM   6225 O  O     . PRO F 2 194 ? -15.211 27.681 135.355 1.00 12.80 ? 194 PRO C O     1 
ATOM   6226 C  CB    . PRO F 2 194 ? -16.228 28.099 132.887 1.00 9.15  ? 194 PRO C CB    1 
ATOM   6227 C  CG    . PRO F 2 194 ? -17.298 28.809 133.688 1.00 9.33  ? 194 PRO C CG    1 
ATOM   6228 C  CD    . PRO F 2 194 ? -18.451 27.801 133.815 1.00 9.13  ? 194 PRO C CD    1 
ATOM   6229 N  N     . VAL F 2 195 ? -15.823 25.499 135.542 1.00 10.16 ? 195 VAL C N     1 
ATOM   6230 C  CA    . VAL F 2 195 ? -15.285 25.260 136.884 1.00 9.80  ? 195 VAL C CA    1 
ATOM   6231 C  C     . VAL F 2 195 ? -13.744 25.145 136.818 1.00 9.99  ? 195 VAL C C     1 
ATOM   6232 O  O     . VAL F 2 195 ? -13.332 24.188 136.136 1.00 10.98 ? 195 VAL C O     1 
ATOM   6233 C  CB    . VAL F 2 195 ? -15.806 23.963 137.547 1.00 6.63  ? 195 VAL C CB    1 
ATOM   6234 C  CG1   . VAL F 2 195 ? -15.120 23.740 138.897 1.00 6.61  ? 195 VAL C CG1   1 
ATOM   6235 C  CG2   . VAL F 2 195 ? -17.300 23.887 137.684 1.00 4.05  ? 195 VAL C CG2   1 
ATOM   6236 N  N     . LYS F 2 196 ? -13.024 26.020 137.470 1.00 8.22  ? 196 LYS C N     1 
ATOM   6237 C  CA    . LYS F 2 196 ? -11.547 25.945 137.457 1.00 6.60  ? 196 LYS C CA    1 
ATOM   6238 C  C     . LYS F 2 196 ? -11.074 25.680 138.893 1.00 6.24  ? 196 LYS C C     1 
ATOM   6239 O  O     . LYS F 2 196 ? -11.815 25.910 139.861 1.00 5.88  ? 196 LYS C O     1 
ATOM   6240 C  CB    . LYS F 2 196 ? -10.860 27.207 137.010 1.00 4.53  ? 196 LYS C CB    1 
ATOM   6241 C  CG    . LYS F 2 196 ? -11.682 28.009 135.999 1.00 5.36  ? 196 LYS C CG    1 
ATOM   6242 C  CD    . LYS F 2 196 ? -11.436 27.577 134.552 1.00 6.55  ? 196 LYS C CD    1 
ATOM   6243 C  CE    . LYS F 2 196 ? -10.907 28.711 133.671 1.00 10.79 ? 196 LYS C CE    1 
ATOM   6244 N  NZ    . LYS F 2 196 ? -9.528  29.100 134.003 1.00 15.67 ? 196 LYS C NZ    1 
ATOM   6245 N  N     . LEU F 2 197 ? -9.850  25.201 139.008 1.00 6.64  ? 197 LEU C N     1 
ATOM   6246 C  CA    . LEU F 2 197 ? -9.248  24.902 140.319 1.00 6.85  ? 197 LEU C CA    1 
ATOM   6247 C  C     . LEU F 2 197 ? -8.211  25.967 140.705 1.00 7.83  ? 197 LEU C C     1 
ATOM   6248 O  O     . LEU F 2 197 ? -7.082  25.972 140.182 1.00 8.91  ? 197 LEU C O     1 
ATOM   6249 C  CB    . LEU F 2 197 ? -8.573  23.528 140.295 1.00 4.69  ? 197 LEU C CB    1 
ATOM   6250 C  CG    . LEU F 2 197 ? -8.055  23.091 141.666 1.00 6.31  ? 197 LEU C CG    1 
ATOM   6251 C  CD1   . LEU F 2 197 ? -9.176  22.707 142.634 1.00 6.85  ? 197 LEU C CD1   1 
ATOM   6252 C  CD2   . LEU F 2 197 ? -7.132  21.873 141.597 1.00 7.65  ? 197 LEU C CD2   1 
ATOM   6253 N  N     . SER F 2 198 ? -8.675  26.802 141.621 1.00 8.54  ? 198 SER C N     1 
ATOM   6254 C  CA    . SER F 2 198 ? -7.939  27.945 142.194 1.00 9.33  ? 198 SER C CA    1 
ATOM   6255 C  C     . SER F 2 198 ? -7.531  27.646 143.641 1.00 11.17 ? 198 SER C C     1 
ATOM   6256 O  O     . SER F 2 198 ? -7.487  26.477 144.060 1.00 12.99 ? 198 SER C O     1 
ATOM   6257 C  CB    . SER F 2 198 ? -8.863  29.168 142.226 1.00 6.12  ? 198 SER C CB    1 
ATOM   6258 O  OG    . SER F 2 198 ? -8.459  30.117 141.256 1.00 6.15  ? 198 SER C OG    1 
ATOM   6259 N  N     . ASN F 2 199 ? -7.236  28.733 144.356 1.00 11.47 ? 199 ASN C N     1 
ATOM   6260 C  CA    . ASN F 2 199 ? -6.872  28.674 145.788 1.00 11.37 ? 199 ASN C CA    1 
ATOM   6261 C  C     . ASN F 2 199 ? -7.726  29.659 146.625 1.00 12.13 ? 199 ASN C C     1 
ATOM   6262 O  O     . ASN F 2 199 ? -8.352  30.581 146.075 1.00 12.47 ? 199 ASN C O     1 
ATOM   6263 C  CB    . ASN F 2 199 ? -5.388  29.030 146.039 1.00 10.69 ? 199 ASN C CB    1 
ATOM   6264 C  CG    . ASN F 2 199 ? -4.611  29.528 144.812 1.00 11.12 ? 199 ASN C CG    1 
ATOM   6265 O  OD1   . ASN F 2 199 ? -4.699  30.704 144.459 1.00 10.49 ? 199 ASN C OD1   1 
ATOM   6266 N  ND2   . ASN F 2 199 ? -3.827  28.700 144.144 1.00 11.46 ? 199 ASN C ND2   1 
ATOM   6267 N  N     . VAL F 2 200 ? -7.703  29.381 147.934 1.00 12.53 ? 200 VAL C N     1 
ATOM   6268 C  CA    . VAL F 2 200 ? -8.374  30.172 149.012 1.00 11.75 ? 200 VAL C CA    1 
ATOM   6269 C  C     . VAL F 2 200 ? -7.356  30.414 150.087 1.00 11.56 ? 200 VAL C C     1 
ATOM   6270 O  O     . VAL F 2 200 ? -6.823  29.480 150.698 1.00 12.53 ? 200 VAL C O     1 
ATOM   6271 C  CB    . VAL F 2 200 ? -9.558  29.392 149.585 1.00 9.76  ? 200 VAL C CB    1 
ATOM   6272 C  CG1   . VAL F 2 200 ? -9.133  28.293 150.561 1.00 8.47  ? 200 VAL C CG1   1 
ATOM   6273 C  CG2   . VAL F 2 200 ? -10.535 30.279 150.362 1.00 7.75  ? 200 VAL C CG2   1 
ATOM   6274 N  N     . GLN F 2 201 ? -7.134  31.656 150.262 1.00 10.51 ? 201 GLN C N     1 
ATOM   6275 C  CA    . GLN F 2 201 ? -6.215  32.158 151.240 1.00 9.91  ? 201 GLN C CA    1 
ATOM   6276 C  C     . GLN F 2 201 ? -7.069  32.711 152.385 1.00 9.99  ? 201 GLN C C     1 
ATOM   6277 O  O     . GLN F 2 201 ? -7.898  33.610 152.162 1.00 9.82  ? 201 GLN C O     1 
ATOM   6278 C  CB    . GLN F 2 201 ? -5.328  33.158 150.511 1.00 10.75 ? 201 GLN C CB    1 
ATOM   6279 C  CG    . GLN F 2 201 ? -5.163  34.494 151.204 1.00 12.32 ? 201 GLN C CG    1 
ATOM   6280 C  CD    . GLN F 2 201 ? -3.778  35.070 150.942 1.00 17.22 ? 201 GLN C CD    1 
ATOM   6281 O  OE1   . GLN F 2 201 ? -3.653  36.079 150.249 1.00 18.62 ? 201 GLN C OE1   1 
ATOM   6282 N  NE2   . GLN F 2 201 ? -2.716  34.480 151.460 1.00 18.00 ? 201 GLN C NE2   1 
ATOM   6283 N  N     . PHE F 2 202 ? -6.821  32.105 153.582 1.00 10.51 ? 202 PHE C N     1 
ATOM   6284 C  CA    . PHE F 2 202 ? -7.549  32.437 154.844 1.00 10.81 ? 202 PHE C CA    1 
ATOM   6285 C  C     . PHE F 2 202 ? -6.730  32.290 156.115 1.00 11.35 ? 202 PHE C C     1 
ATOM   6286 O  O     . PHE F 2 202 ? -6.068  31.263 156.333 1.00 11.78 ? 202 PHE C O     1 
ATOM   6287 C  CB    . PHE F 2 202 ? -8.804  31.577 154.975 1.00 9.22  ? 202 PHE C CB    1 
ATOM   6288 C  CG    . PHE F 2 202 ? -8.525  30.084 155.162 1.00 9.67  ? 202 PHE C CG    1 
ATOM   6289 C  CD1   . PHE F 2 202 ? -8.304  29.268 154.047 1.00 10.05 ? 202 PHE C CD1   1 
ATOM   6290 C  CD2   . PHE F 2 202 ? -8.502  29.533 156.449 1.00 10.04 ? 202 PHE C CD2   1 
ATOM   6291 C  CE1   . PHE F 2 202 ? -8.059  27.900 154.219 1.00 11.75 ? 202 PHE C CE1   1 
ATOM   6292 C  CE2   . PHE F 2 202 ? -8.257  28.166 156.621 1.00 12.38 ? 202 PHE C CE2   1 
ATOM   6293 C  CZ    . PHE F 2 202 ? -8.036  27.349 155.506 1.00 11.50 ? 202 PHE C CZ    1 
ATOM   6294 N  N     . PRO F 2 203 ? -6.777  33.333 156.959 1.00 11.19 ? 203 PRO C N     1 
ATOM   6295 C  CA    . PRO F 2 203 ? -6.096  33.341 158.241 1.00 11.26 ? 203 PRO C CA    1 
ATOM   6296 C  C     . PRO F 2 203 ? -6.664  32.287 159.164 1.00 12.31 ? 203 PRO C C     1 
ATOM   6297 O  O     . PRO F 2 203 ? -7.918  32.085 159.176 1.00 13.26 ? 203 PRO C O     1 
ATOM   6298 C  CB    . PRO F 2 203 ? -6.385  34.718 158.799 1.00 10.44 ? 203 PRO C CB    1 
ATOM   6299 C  CG    . PRO F 2 203 ? -7.265  35.454 157.801 1.00 10.87 ? 203 PRO C CG    1 
ATOM   6300 C  CD    . PRO F 2 203 ? -7.522  34.555 156.636 1.00 10.96 ? 203 PRO C CD    1 
ATOM   6301 N  N     . VAL F 2 204 ? -5.763  31.651 159.904 1.00 12.80 ? 204 VAL C N     1 
ATOM   6302 C  CA    . VAL F 2 204 ? -6.120  30.629 160.914 1.00 13.14 ? 204 VAL C CA    1 
ATOM   6303 C  C     . VAL F 2 204 ? -5.646  31.104 162.303 1.00 14.34 ? 204 VAL C C     1 
ATOM   6304 O  O     . VAL F 2 204 ? -4.820  32.023 162.415 1.00 15.57 ? 204 VAL C O     1 
ATOM   6305 C  CB    . VAL F 2 204 ? -5.502  29.273 160.553 1.00 12.93 ? 204 VAL C CB    1 
ATOM   6306 C  CG1   . VAL F 2 204 ? -4.670  29.318 159.270 1.00 12.64 ? 204 VAL C CG1   1 
ATOM   6307 C  CG2   . VAL F 2 204 ? -4.566  28.736 161.637 1.00 12.46 ? 204 VAL C CG2   1 
ATOM   6308 N  N     . ALA F 2 205 ? -6.188  30.458 163.332 1.00 14.01 ? 205 ALA C N     1 
ATOM   6309 C  CA    . ALA F 2 205 ? -5.907  30.812 164.744 1.00 14.08 ? 205 ALA C CA    1 
ATOM   6310 C  C     . ALA F 2 205 ? -4.910  29.846 165.388 1.00 14.61 ? 205 ALA C C     1 
ATOM   6311 O  O     . ALA F 2 205 ? -5.179  29.266 166.452 1.00 12.59 ? 205 ALA C O     1 
ATOM   6312 C  CB    . ALA F 2 205 ? -7.197  30.780 165.563 1.00 11.03 ? 205 ALA C CB    1 
ATOM   6313 N  N     . THR F 2 206 ? -3.794  29.720 164.710 1.00 15.48 ? 206 THR C N     1 
ATOM   6314 C  CA    . THR F 2 206 ? -2.657  28.904 165.150 1.00 15.72 ? 206 THR C CA    1 
ATOM   6315 C  C     . THR F 2 206 ? -1.779  29.826 166.030 1.00 16.66 ? 206 THR C C     1 
ATOM   6316 O  O     . THR F 2 206 ? -1.467  30.962 165.648 1.00 17.75 ? 206 THR C O     1 
ATOM   6317 C  CB    . THR F 2 206 ? -1.958  28.384 163.885 1.00 14.57 ? 206 THR C CB    1 
ATOM   6318 O  OG1   . THR F 2 206 ? -1.646  27.008 164.022 1.00 13.82 ? 206 THR C OG1   1 
ATOM   6319 C  CG2   . THR F 2 206 ? -0.668  29.128 163.559 1.00 13.05 ? 206 THR C CG2   1 
ATOM   6320 N  N     . THR F 2 207 ? -1.392  29.343 167.216 1.00 16.95 ? 207 THR C N     1 
ATOM   6321 C  CA    . THR F 2 207 ? -0.645  30.180 168.204 1.00 15.93 ? 207 THR C CA    1 
ATOM   6322 C  C     . THR F 2 207 ? 0.528   30.931 167.551 1.00 15.63 ? 207 THR C C     1 
ATOM   6323 O  O     . THR F 2 207 ? 0.641   32.161 167.642 1.00 16.49 ? 207 THR C O     1 
ATOM   6324 C  CB    . THR F 2 207 ? -0.163  29.373 169.406 1.00 13.53 ? 207 THR C CB    1 
ATOM   6325 O  OG1   . THR F 2 207 ? -0.590  30.019 170.608 1.00 12.04 ? 207 THR C OG1   1 
ATOM   6326 C  CG2   . THR F 2 207 ? 1.355   29.246 169.482 1.00 12.06 ? 207 THR C CG2   1 
ATOM   6327 N  N     . PRO F 2 208 ? 1.523   30.345 166.851 1.00 14.99 ? 208 PRO C N     1 
ATOM   6328 C  CA    . PRO F 2 208 ? 2.487   31.199 166.211 1.00 15.12 ? 208 PRO C CA    1 
ATOM   6329 C  C     . PRO F 2 208 ? 1.664   32.115 165.343 1.00 15.18 ? 208 PRO C C     1 
ATOM   6330 O  O     . PRO F 2 208 ? 2.158   33.230 164.986 1.00 15.79 ? 208 PRO C O     1 
ATOM   6331 C  CB    . PRO F 2 208 ? 3.408   30.241 165.498 1.00 15.47 ? 208 PRO C CB    1 
ATOM   6332 C  CG    . PRO F 2 208 ? 2.920   28.831 165.788 1.00 15.49 ? 208 PRO C CG    1 
ATOM   6333 C  CD    . PRO F 2 208 ? 1.708   28.907 166.680 1.00 15.08 ? 208 PRO C CD    1 
ATOM   6334 N  N     . ALA F 2 209 ? 0.457   31.582 165.082 1.00 14.81 ? 209 ALA C N     1 
ATOM   6335 C  CA    . ALA F 2 209 ? -0.651  32.232 164.320 1.00 14.70 ? 209 ALA C CA    1 
ATOM   6336 C  C     . ALA F 2 209 ? -0.282  32.323 162.822 1.00 15.77 ? 209 ALA C C     1 
ATOM   6337 O  O     . ALA F 2 209 ? 0.722   32.943 162.446 1.00 16.92 ? 209 ALA C O     1 
ATOM   6338 C  CB    . ALA F 2 209 ? -0.915  33.628 164.879 1.00 9.94  ? 209 ALA C CB    1 
ATOM   6339 N  N     . THR F 2 210 ? -1.119  31.710 161.969 1.00 16.12 ? 210 THR C N     1 
ATOM   6340 C  CA    . THR F 2 210 ? -0.832  31.649 160.511 1.00 15.93 ? 210 THR C CA    1 
ATOM   6341 C  C     . THR F 2 210 ? -1.994  32.048 159.586 1.00 15.70 ? 210 THR C C     1 
ATOM   6342 O  O     . THR F 2 210 ? -3.104  32.362 160.049 1.00 15.72 ? 210 THR C O     1 
ATOM   6343 C  CB    . THR F 2 210 ? -0.491  30.226 160.068 1.00 17.69 ? 210 THR C CB    1 
ATOM   6344 O  OG1   . THR F 2 210 ? -1.502  29.326 160.497 1.00 20.09 ? 210 THR C OG1   1 
ATOM   6345 C  CG2   . THR F 2 210 ? 0.839   29.729 160.625 1.00 15.78 ? 210 THR C CG2   1 
ATOM   6346 N  N     . SER F 2 211 ? -1.593  31.983 158.315 1.00 15.20 ? 211 SER C N     1 
ATOM   6347 C  CA    . SER F 2 211 ? -2.402  32.258 157.116 1.00 14.23 ? 211 SER C CA    1 
ATOM   6348 C  C     . SER F 2 211 ? -2.351  31.024 156.204 1.00 13.96 ? 211 SER C C     1 
ATOM   6349 O  O     . SER F 2 211 ? -1.268  30.535 155.847 1.00 15.27 ? 211 SER C O     1 
ATOM   6350 C  CB    . SER F 2 211 ? -1.802  33.446 156.352 1.00 14.38 ? 211 SER C CB    1 
ATOM   6351 O  OG    . SER F 2 211 ? -2.599  34.602 156.538 1.00 15.32 ? 211 SER C OG    1 
ATOM   6352 N  N     . ALA F 2 212 ? -3.524  30.541 155.840 1.00 12.49 ? 212 ALA C N     1 
ATOM   6353 C  CA    . ALA F 2 212 ? -3.653  29.328 155.012 1.00 10.94 ? 212 ALA C CA    1 
ATOM   6354 C  C     . ALA F 2 212 ? -3.947  29.664 153.542 1.00 10.57 ? 212 ALA C C     1 
ATOM   6355 O  O     . ALA F 2 212 ? -4.445  30.754 153.222 1.00 9.74  ? 212 ALA C O     1 
ATOM   6356 C  CB    . ALA F 2 212 ? -4.798  28.457 155.534 1.00 7.86  ? 212 ALA C CB    1 
ATOM   6357 N  N     . LEU F 2 213 ? -3.604  28.678 152.736 1.00 11.48 ? 213 LEU C N     1 
ATOM   6358 C  CA    . LEU F 2 213 ? -3.818  28.643 151.279 1.00 12.11 ? 213 LEU C CA    1 
ATOM   6359 C  C     . LEU F 2 213 ? -4.080  27.158 150.934 1.00 12.32 ? 213 LEU C C     1 
ATOM   6360 O  O     . LEU F 2 213 ? -3.207  26.322 151.205 1.00 12.89 ? 213 LEU C O     1 
ATOM   6361 C  CB    . LEU F 2 213 ? -2.604  29.209 150.554 1.00 12.82 ? 213 LEU C CB    1 
ATOM   6362 C  CG    . LEU F 2 213 ? -2.753  29.173 149.035 1.00 13.34 ? 213 LEU C CG    1 
ATOM   6363 C  CD1   . LEU F 2 213 ? -2.989  30.555 148.422 1.00 12.59 ? 213 LEU C CD1   1 
ATOM   6364 C  CD2   . LEU F 2 213 ? -1.513  28.602 148.349 1.00 13.26 ? 213 LEU C CD2   1 
ATOM   6365 N  N     . VAL F 2 214 ? -5.278  26.955 150.426 1.00 11.63 ? 214 VAL C N     1 
ATOM   6366 C  CA    . VAL F 2 214 ? -5.754  25.618 150.065 1.00 10.84 ? 214 VAL C CA    1 
ATOM   6367 C  C     . VAL F 2 214 ? -6.474  25.682 148.716 1.00 11.17 ? 214 VAL C C     1 
ATOM   6368 O  O     . VAL F 2 214 ? -6.833  26.753 148.217 1.00 12.06 ? 214 VAL C O     1 
ATOM   6369 C  CB    . VAL F 2 214 ? -6.625  24.992 151.157 1.00 11.61 ? 214 VAL C CB    1 
ATOM   6370 C  CG1   . VAL F 2 214 ? -5.882  24.900 152.490 1.00 11.72 ? 214 VAL C CG1   1 
ATOM   6371 C  CG2   . VAL F 2 214 ? -7.939  25.757 151.304 1.00 13.88 ? 214 VAL C CG2   1 
ATOM   6372 N  N     . HIS F 2 215 ? -6.626  24.478 148.179 1.00 10.75 ? 215 HIS C N     1 
ATOM   6373 C  CA    . HIS F 2 215 ? -7.272  24.296 146.877 1.00 10.38 ? 215 HIS C CA    1 
ATOM   6374 C  C     . HIS F 2 215 ? -8.774  24.581 147.046 1.00 11.70 ? 215 HIS C C     1 
ATOM   6375 O  O     . HIS F 2 215 ? -9.402  24.241 148.071 1.00 14.05 ? 215 HIS C O     1 
ATOM   6376 C  CB    . HIS F 2 215 ? -7.143  22.885 146.283 1.00 10.24 ? 215 HIS C CB    1 
ATOM   6377 C  CG    . HIS F 2 215 ? -5.775  22.558 145.778 1.00 12.10 ? 215 HIS C CG    1 
ATOM   6378 N  ND1   . HIS F 2 215 ? -5.048  21.478 146.221 1.00 12.56 ? 215 HIS C ND1   1 
ATOM   6379 C  CD2   . HIS F 2 215 ? -5.031  23.185 144.830 1.00 13.52 ? 215 HIS C CD2   1 
ATOM   6380 C  CE1   . HIS F 2 215 ? -3.902  21.444 145.568 1.00 14.32 ? 215 HIS C CE1   1 
ATOM   6381 N  NE2   . HIS F 2 215 ? -3.859  22.463 144.741 1.00 15.04 ? 215 HIS C NE2   1 
ATOM   6382 N  N     . THR F 2 216 ? -9.306  25.183 145.986 1.00 11.20 ? 216 THR C N     1 
ATOM   6383 C  CA    . THR F 2 216 ? -10.740 25.486 145.986 1.00 10.24 ? 216 THR C CA    1 
ATOM   6384 C  C     . THR F 2 216 ? -11.265 25.514 144.567 1.00 8.59  ? 216 THR C C     1 
ATOM   6385 O  O     . THR F 2 216 ? -10.650 26.084 143.661 1.00 7.91  ? 216 THR C O     1 
ATOM   6386 C  CB    . THR F 2 216 ? -10.965 26.837 146.757 1.00 14.64 ? 216 THR C CB    1 
ATOM   6387 O  OG1   . THR F 2 216 ? -12.393 26.855 147.045 1.00 16.98 ? 216 THR C OG1   1 
ATOM   6388 C  CG2   . THR F 2 216 ? -10.476 28.037 145.945 1.00 18.95 ? 216 THR C CG2   1 
ATOM   6389 N  N     . LEU F 2 217 ? -12.393 24.869 144.369 1.00 7.44  ? 217 LEU C N     1 
ATOM   6390 C  CA    . LEU F 2 217 ? -13.035 24.851 143.054 1.00 7.62  ? 217 LEU C CA    1 
ATOM   6391 C  C     . LEU F 2 217 ? -13.801 26.175 142.891 1.00 8.71  ? 217 LEU C C     1 
ATOM   6392 O  O     . LEU F 2 217 ? -14.694 26.542 143.697 1.00 9.90  ? 217 LEU C O     1 
ATOM   6393 C  CB    . LEU F 2 217 ? -13.898 23.607 143.033 1.00 5.18  ? 217 LEU C CB    1 
ATOM   6394 C  CG    . LEU F 2 217 ? -13.495 22.379 142.284 1.00 4.17  ? 217 LEU C CG    1 
ATOM   6395 C  CD1   . LEU F 2 217 ? -12.008 22.347 141.954 1.00 3.71  ? 217 LEU C CD1   1 
ATOM   6396 C  CD2   . LEU F 2 217 ? -13.872 21.153 143.132 1.00 3.89  ? 217 LEU C CD2   1 
ATOM   6397 N  N     . VAL F 2 218 ? -13.445 26.895 141.835 1.00 8.16  ? 218 VAL C N     1 
ATOM   6398 C  CA    . VAL F 2 218 ? -14.121 28.146 141.485 1.00 8.80  ? 218 VAL C CA    1 
ATOM   6399 C  C     . VAL F 2 218 ? -15.026 27.815 140.285 1.00 9.92  ? 218 VAL C C     1 
ATOM   6400 O  O     . VAL F 2 218 ? -14.578 27.085 139.386 1.00 10.87 ? 218 VAL C O     1 
ATOM   6401 C  CB    . VAL F 2 218 ? -13.200 29.338 141.265 1.00 8.49  ? 218 VAL C CB    1 
ATOM   6402 C  CG1   . VAL F 2 218 ? -12.539 29.796 142.555 1.00 8.29  ? 218 VAL C CG1   1 
ATOM   6403 C  CG2   . VAL F 2 218 ? -12.155 29.119 140.206 1.00 10.67 ? 218 VAL C CG2   1 
ATOM   6404 N  N     . GLY F 2 219 ? -16.251 28.321 140.345 1.00 10.77 ? 219 GLY C N     1 
ATOM   6405 C  CA    . GLY F 2 219 ? -17.209 28.111 139.261 1.00 11.21 ? 219 GLY C CA    1 
ATOM   6406 C  C     . GLY F 2 219 ? -18.286 27.085 139.484 1.00 11.10 ? 219 GLY C C     1 
ATOM   6407 O  O     . GLY F 2 219 ? -19.101 26.860 138.569 1.00 11.44 ? 219 GLY C O     1 
ATOM   6408 N  N     . LEU F 2 220 ? -18.328 26.495 140.647 1.00 11.35 ? 220 LEU C N     1 
ATOM   6409 C  CA    . LEU F 2 220 ? -19.267 25.463 141.066 1.00 11.62 ? 220 LEU C CA    1 
ATOM   6410 C  C     . LEU F 2 220 ? -20.673 25.981 141.302 1.00 12.28 ? 220 LEU C C     1 
ATOM   6411 O  O     . LEU F 2 220 ? -21.612 25.156 141.370 1.00 13.56 ? 220 LEU C O     1 
ATOM   6412 C  CB    . LEU F 2 220 ? -18.628 24.738 142.269 1.00 10.95 ? 220 LEU C CB    1 
ATOM   6413 C  CG    . LEU F 2 220 ? -18.553 23.220 142.218 1.00 11.59 ? 220 LEU C CG    1 
ATOM   6414 C  CD1   . LEU F 2 220 ? -18.264 22.715 140.805 1.00 10.32 ? 220 LEU C CD1   1 
ATOM   6415 C  CD2   . LEU F 2 220 ? -17.449 22.736 143.164 1.00 11.04 ? 220 LEU C CD2   1 
ATOM   6416 N  N     . ASP F 2 221 ? -20.879 27.286 141.400 1.00 12.76 ? 221 ASP C N     1 
ATOM   6417 C  CA    . ASP F 2 221 ? -22.235 27.815 141.659 1.00 13.29 ? 221 ASP C CA    1 
ATOM   6418 C  C     . ASP F 2 221 ? -23.054 27.700 140.374 1.00 14.19 ? 221 ASP C C     1 
ATOM   6419 O  O     . ASP F 2 221 ? -24.265 27.989 140.363 1.00 15.82 ? 221 ASP C O     1 
ATOM   6420 C  CB    . ASP F 2 221 ? -22.222 29.196 142.285 1.00 12.98 ? 221 ASP C CB    1 
ATOM   6421 C  CG    . ASP F 2 221 ? -21.638 29.308 143.667 1.00 16.62 ? 221 ASP C CG    1 
ATOM   6422 O  OD1   . ASP F 2 221 ? -20.374 29.204 143.754 1.00 17.88 ? 221 ASP C OD1   1 
ATOM   6423 O  OD2   . ASP F 2 221 ? -22.276 29.498 144.716 1.00 18.00 ? 221 ASP C OD2   1 
ATOM   6424 N  N     . GLY F 2 222 ? -22.360 27.269 139.342 1.00 13.71 ? 222 GLY C N     1 
ATOM   6425 C  CA    . GLY F 2 222 ? -22.996 27.130 138.009 1.00 14.10 ? 222 GLY C CA    1 
ATOM   6426 C  C     . GLY F 2 222 ? -23.968 25.938 138.015 1.00 14.14 ? 222 GLY C C     1 
ATOM   6427 O  O     . GLY F 2 222 ? -24.909 25.904 137.209 1.00 14.60 ? 222 GLY C O     1 
ATOM   6428 N  N     . VAL F 2 223 ? -23.659 25.003 138.914 1.00 13.20 ? 223 VAL C N     1 
ATOM   6429 C  CA    . VAL F 2 223 ? -24.459 23.794 139.082 1.00 11.61 ? 223 VAL C CA    1 
ATOM   6430 C  C     . VAL F 2 223 ? -25.792 24.152 139.744 1.00 12.66 ? 223 VAL C C     1 
ATOM   6431 O  O     . VAL F 2 223 ? -26.778 23.405 139.580 1.00 13.96 ? 223 VAL C O     1 
ATOM   6432 C  CB    . VAL F 2 223 ? -23.691 22.729 139.874 1.00 6.93  ? 223 VAL C CB    1 
ATOM   6433 C  CG1   . VAL F 2 223 ? -24.393 21.377 139.851 1.00 5.74  ? 223 VAL C CG1   1 
ATOM   6434 C  CG2   . VAL F 2 223 ? -22.249 22.602 139.441 1.00 5.75  ? 223 VAL C CG2   1 
ATOM   6435 N  N     . LEU F 2 224 ? -25.796 25.291 140.422 1.00 12.65 ? 224 LEU C N     1 
ATOM   6436 C  CA    . LEU F 2 224 ? -26.948 25.797 141.157 1.00 13.07 ? 224 LEU C CA    1 
ATOM   6437 C  C     . LEU F 2 224 ? -28.137 26.287 140.353 1.00 12.77 ? 224 LEU C C     1 
ATOM   6438 O  O     . LEU F 2 224 ? -29.176 26.614 141.000 1.00 13.68 ? 224 LEU C O     1 
ATOM   6439 C  CB    . LEU F 2 224 ? -26.431 26.854 142.138 1.00 13.59 ? 224 LEU C CB    1 
ATOM   6440 C  CG    . LEU F 2 224 ? -25.323 26.433 143.070 1.00 13.34 ? 224 LEU C CG    1 
ATOM   6441 C  CD1   . LEU F 2 224 ? -24.961 27.592 143.983 1.00 10.54 ? 224 LEU C CD1   1 
ATOM   6442 C  CD2   . LEU F 2 224 ? -25.758 25.226 143.876 1.00 15.30 ? 224 LEU C CD2   1 
ATOM   6443 N  N     . ALA F 2 225 ? -28.066 26.342 139.043 1.00 12.29 ? 225 ALA C N     1 
ATOM   6444 C  CA    . ALA F 2 225 ? -29.223 26.817 138.241 1.00 11.46 ? 225 ALA C CA    1 
ATOM   6445 C  C     . ALA F 2 225 ? -29.149 26.242 136.839 1.00 10.86 ? 225 ALA C C     1 
ATOM   6446 O  O     . ALA F 2 225 ? -28.013 26.043 136.371 1.00 11.76 ? 225 ALA C O     1 
ATOM   6447 C  CB    . ALA F 2 225 ? -29.112 28.340 138.149 1.00 11.82 ? 225 ALA C CB    1 
ATOM   6448 N  N     . VAL F 2 226 ? -30.277 26.002 136.209 1.00 10.12 ? 226 VAL C N     1 
ATOM   6449 C  CA    . VAL F 2 226 ? -30.180 25.495 134.809 1.00 9.69  ? 226 VAL C CA    1 
ATOM   6450 C  C     . VAL F 2 226 ? -29.584 26.664 134.007 1.00 9.68  ? 226 VAL C C     1 
ATOM   6451 O  O     . VAL F 2 226 ? -30.186 27.761 134.012 1.00 10.66 ? 226 VAL C O     1 
ATOM   6452 C  CB    . VAL F 2 226 ? -31.530 25.008 134.320 1.00 8.39  ? 226 VAL C CB    1 
ATOM   6453 C  CG1   . VAL F 2 226 ? -31.411 24.370 132.928 1.00 5.82  ? 226 VAL C CG1   1 
ATOM   6454 C  CG2   . VAL F 2 226 ? -32.220 24.041 135.267 1.00 9.78  ? 226 VAL C CG2   1 
ATOM   6455 N  N     . GLY F 2 227 ? -28.436 26.482 133.364 1.00 9.72  ? 227 GLY C N     1 
ATOM   6456 C  CA    . GLY F 2 227 ? -27.831 27.624 132.631 1.00 10.02 ? 227 GLY C CA    1 
ATOM   6457 C  C     . GLY F 2 227 ? -28.671 27.957 131.413 1.00 10.47 ? 227 GLY C C     1 
ATOM   6458 O  O     . GLY F 2 227 ? -29.216 27.006 130.830 1.00 11.11 ? 227 GLY C O     1 
ATOM   6459 N  N     . PRO F 2 228 ? -28.724 29.230 131.050 1.00 10.18 ? 228 PRO C N     1 
ATOM   6460 C  CA    . PRO F 2 228 ? -29.496 29.695 129.877 1.00 9.69  ? 228 PRO C CA    1 
ATOM   6461 C  C     . PRO F 2 228 ? -29.173 28.881 128.643 1.00 9.58  ? 228 PRO C C     1 
ATOM   6462 O  O     . PRO F 2 228 ? -30.092 28.430 127.904 1.00 11.28 ? 228 PRO C O     1 
ATOM   6463 C  CB    . PRO F 2 228 ? -29.260 31.179 129.817 1.00 9.41  ? 228 PRO C CB    1 
ATOM   6464 C  CG    . PRO F 2 228 ? -28.789 31.574 131.187 1.00 9.43  ? 228 PRO C CG    1 
ATOM   6465 C  CD    . PRO F 2 228 ? -28.073 30.354 131.736 1.00 9.63  ? 228 PRO C CD    1 
ATOM   6466 N  N     . ASP F 2 229 ? -27.899 28.630 128.357 1.00 8.69  ? 229 ASP C N     1 
ATOM   6467 C  CA    . ASP F 2 229 ? -27.562 27.777 127.194 1.00 9.22  ? 229 ASP C CA    1 
ATOM   6468 C  C     . ASP F 2 229 ? -27.662 26.318 127.721 1.00 10.46 ? 229 ASP C C     1 
ATOM   6469 O  O     . ASP F 2 229 ? -26.659 25.813 128.290 1.00 12.45 ? 229 ASP C O     1 
ATOM   6470 C  CB    . ASP F 2 229 ? -26.241 28.037 126.533 1.00 6.96  ? 229 ASP C CB    1 
ATOM   6471 C  CG    . ASP F 2 229 ? -25.883 29.419 126.126 1.00 6.28  ? 229 ASP C CG    1 
ATOM   6472 O  OD1   . ASP F 2 229 ? -26.668 29.990 125.347 1.00 7.09  ? 229 ASP C OD1   1 
ATOM   6473 O  OD2   . ASP F 2 229 ? -24.855 29.985 126.533 1.00 5.08  ? 229 ASP C OD2   1 
ATOM   6474 N  N     . ASN F 2 230 ? -28.806 25.703 127.508 1.00 10.43 ? 230 ASN C N     1 
ATOM   6475 C  CA    . ASN F 2 230 ? -28.971 24.322 127.999 1.00 10.80 ? 230 ASN C CA    1 
ATOM   6476 C  C     . ASN F 2 230 ? -29.787 23.493 127.011 1.00 11.53 ? 230 ASN C C     1 
ATOM   6477 O  O     . ASN F 2 230 ? -30.331 24.039 126.047 1.00 12.23 ? 230 ASN C O     1 
ATOM   6478 C  CB    . ASN F 2 230 ? -29.707 24.374 129.358 1.00 10.71 ? 230 ASN C CB    1 
ATOM   6479 C  CG    . ASN F 2 230 ? -31.164 24.750 129.129 1.00 11.27 ? 230 ASN C CG    1 
ATOM   6480 O  OD1   . ASN F 2 230 ? -32.004 23.969 128.670 1.00 12.78 ? 230 ASN C OD1   1 
ATOM   6481 N  ND2   . ASN F 2 230 ? -31.478 26.004 129.428 1.00 12.91 ? 230 ASN C ND2   1 
ATOM   6482 N  N     . PHE F 2 231 ? -29.884 22.235 127.352 1.00 11.33 ? 231 PHE C N     1 
ATOM   6483 C  CA    . PHE F 2 231 ? -30.654 21.224 126.620 1.00 9.91  ? 231 PHE C CA    1 
ATOM   6484 C  C     . PHE F 2 231 ? -31.589 20.539 127.620 1.00 10.06 ? 231 PHE C C     1 
ATOM   6485 O  O     . PHE F 2 231 ? -31.184 20.131 128.712 1.00 10.64 ? 231 PHE C O     1 
ATOM   6486 C  CB    . PHE F 2 231 ? -29.776 20.249 125.869 1.00 6.06  ? 231 PHE C CB    1 
ATOM   6487 C  CG    . PHE F 2 231 ? -30.426 18.999 125.369 1.00 6.48  ? 231 PHE C CG    1 
ATOM   6488 C  CD1   . PHE F 2 231 ? -30.726 17.964 126.250 1.00 6.87  ? 231 PHE C CD1   1 
ATOM   6489 C  CD2   . PHE F 2 231 ? -30.729 18.843 124.022 1.00 5.37  ? 231 PHE C CD2   1 
ATOM   6490 C  CE1   . PHE F 2 231 ? -31.325 16.796 125.812 1.00 5.29  ? 231 PHE C CE1   1 
ATOM   6491 C  CE2   . PHE F 2 231 ? -31.334 17.671 123.570 1.00 3.60  ? 231 PHE C CE2   1 
ATOM   6492 C  CZ    . PHE F 2 231 ? -31.638 16.650 124.470 1.00 3.98  ? 231 PHE C CZ    1 
ATOM   6493 N  N     . SER F 2 232 ? -32.832 20.414 127.234 1.00 10.41 ? 232 SER C N     1 
ATOM   6494 C  CA    . SER F 2 232 ? -33.839 19.766 128.110 1.00 10.40 ? 232 SER C CA    1 
ATOM   6495 C  C     . SER F 2 232 ? -34.754 18.928 127.232 1.00 10.41 ? 232 SER C C     1 
ATOM   6496 O  O     . SER F 2 232 ? -35.177 19.432 126.178 1.00 10.83 ? 232 SER C O     1 
ATOM   6497 C  CB    . SER F 2 232 ? -34.612 20.846 128.844 1.00 11.15 ? 232 SER C CB    1 
ATOM   6498 O  OG    . SER F 2 232 ? -34.821 20.543 130.216 1.00 11.75 ? 232 SER C OG    1 
ATOM   6499 N  N     . GLU F 2 233 ? -35.039 17.706 127.624 1.00 10.31 ? 233 GLU C N     1 
ATOM   6500 C  CA    . GLU F 2 233 ? -35.965 16.870 126.855 1.00 10.38 ? 233 GLU C CA    1 
ATOM   6501 C  C     . GLU F 2 233 ? -36.449 15.698 127.681 1.00 10.17 ? 233 GLU C C     1 
ATOM   6502 O  O     . GLU F 2 233 ? -35.985 15.456 128.805 1.00 11.35 ? 233 GLU C O     1 
ATOM   6503 C  CB    . GLU F 2 233 ? -35.464 16.383 125.516 1.00 12.00 ? 233 GLU C CB    1 
ATOM   6504 C  CG    . GLU F 2 233 ? -36.159 16.956 124.285 1.00 15.04 ? 233 GLU C CG    1 
ATOM   6505 C  CD    . GLU F 2 233 ? -37.357 16.268 123.745 1.00 16.52 ? 233 GLU C CD    1 
ATOM   6506 O  OE1   . GLU F 2 233 ? -38.261 15.800 124.417 1.00 16.81 ? 233 GLU C OE1   1 
ATOM   6507 O  OE2   . GLU F 2 233 ? -37.347 16.237 122.484 1.00 16.74 ? 233 GLU C OE2   1 
ATOM   6508 N  N     . SER F 2 234 ? -37.406 14.989 127.093 1.00 9.06  ? 234 SER C N     1 
ATOM   6509 C  CA    . SER F 2 234 ? -37.995 13.831 127.798 1.00 9.06  ? 234 SER C CA    1 
ATOM   6510 C  C     . SER F 2 234 ? -36.857 12.868 128.107 1.00 9.20  ? 234 SER C C     1 
ATOM   6511 O  O     . SER F 2 234 ? -35.983 12.645 127.248 1.00 9.92  ? 234 SER C O     1 
ATOM   6512 C  CB    . SER F 2 234 ? -39.077 13.195 126.967 1.00 9.27  ? 234 SER C CB    1 
ATOM   6513 O  OG    . SER F 2 234 ? -39.330 11.871 127.391 1.00 12.39 ? 234 SER C OG    1 
ATOM   6514 N  N     . PHE F 2 235 ? -36.896 12.317 129.300 1.00 9.06  ? 235 PHE C N     1 
ATOM   6515 C  CA    . PHE F 2 235 ? -35.876 11.367 129.751 1.00 8.72  ? 235 PHE C CA    1 
ATOM   6516 C  C     . PHE F 2 235 ? -35.751 10.122 128.844 1.00 8.28  ? 235 PHE C C     1 
ATOM   6517 O  O     . PHE F 2 235 ? -34.639 9.668  128.531 1.00 7.36  ? 235 PHE C O     1 
ATOM   6518 C  CB    . PHE F 2 235 ? -36.114 10.918 131.201 1.00 10.07 ? 235 PHE C CB    1 
ATOM   6519 C  CG    . PHE F 2 235 ? -35.304 9.673  131.567 1.00 10.21 ? 235 PHE C CG    1 
ATOM   6520 C  CD1   . PHE F 2 235 ? -33.960 9.798  131.937 1.00 9.92  ? 235 PHE C CD1   1 
ATOM   6521 C  CD2   . PHE F 2 235 ? -35.906 8.410  131.525 1.00 9.28  ? 235 PHE C CD2   1 
ATOM   6522 C  CE1   . PHE F 2 235 ? -33.217 8.659  132.267 1.00 10.00 ? 235 PHE C CE1   1 
ATOM   6523 C  CE2   . PHE F 2 235 ? -35.162 7.270  131.855 1.00 8.96  ? 235 PHE C CE2   1 
ATOM   6524 C  CZ    . PHE F 2 235 ? -33.818 7.395  132.226 1.00 10.61 ? 235 PHE C CZ    1 
ATOM   6525 N  N     . ILE F 2 236 ? -36.876 9.576  128.424 1.00 8.52  ? 236 ILE C N     1 
ATOM   6526 C  CA    . ILE F 2 236 ? -36.896 8.356  127.581 1.00 9.84  ? 236 ILE C CA    1 
ATOM   6527 C  C     . ILE F 2 236 ? -36.313 8.617  126.182 1.00 10.91 ? 236 ILE C C     1 
ATOM   6528 O  O     . ILE F 2 236 ? -36.612 7.895  125.219 1.00 13.03 ? 236 ILE C O     1 
ATOM   6529 C  CB    . ILE F 2 236 ? -38.331 7.862  127.386 1.00 9.26  ? 236 ILE C CB    1 
ATOM   6530 C  CG1   . ILE F 2 236 ? -38.405 6.455  126.787 1.00 8.68  ? 236 ILE C CG1   1 
ATOM   6531 C  CG2   . ILE F 2 236 ? -39.143 8.752  126.443 1.00 5.37  ? 236 ILE C CG2   1 
ATOM   6532 C  CD1   . ILE F 2 236 ? -38.261 5.350  127.835 1.00 25.00 ? 236 ILE C CD1   1 
ATOM   6533 N  N     . LYS F 2 237 ? -35.483 9.640  126.091 1.00 10.94 ? 237 LYS C N     1 
ATOM   6534 C  CA    . LYS F 2 237 ? -34.864 10.038 124.812 1.00 10.46 ? 237 LYS C CA    1 
ATOM   6535 C  C     . LYS F 2 237 ? -33.341 10.117 124.941 1.00 11.31 ? 237 LYS C C     1 
ATOM   6536 O  O     . LYS F 2 237 ? -32.630 10.324 123.942 1.00 11.90 ? 237 LYS C O     1 
ATOM   6537 C  CB    . LYS F 2 237 ? -35.388 11.409 124.386 1.00 9.23  ? 237 LYS C CB    1 
ATOM   6538 C  CG    . LYS F 2 237 ? -36.719 11.331 123.637 1.00 8.81  ? 237 LYS C CG    1 
ATOM   6539 C  CD    . LYS F 2 237 ? -37.153 12.674 123.050 1.00 9.83  ? 237 LYS C CD    1 
ATOM   6540 C  CE    . LYS F 2 237 ? -37.928 12.531 121.739 1.00 13.34 ? 237 LYS C CE    1 
ATOM   6541 N  NZ    . LYS F 2 237 ? -38.055 13.799 121.006 1.00 14.81 ? 237 LYS C NZ    1 
ATOM   6542 N  N     . GLY F 2 238 ? -32.903 9.949  126.174 1.00 11.10 ? 238 GLY C N     1 
ATOM   6543 C  CA    . GLY F 2 238 ? -31.479 9.990  126.540 1.00 11.06 ? 238 GLY C CA    1 
ATOM   6544 C  C     . GLY F 2 238 ? -30.860 11.313 126.085 1.00 11.05 ? 238 GLY C C     1 
ATOM   6545 O  O     . GLY F 2 238 ? -31.571 12.248 125.693 1.00 12.17 ? 238 GLY C O     1 
ATOM   6546 N  N     . VAL F 2 239 ? -29.545 11.342 126.165 1.00 10.25 ? 239 VAL C N     1 
ATOM   6547 C  CA    . VAL F 2 239 ? -28.734 12.496 125.750 1.00 9.57  ? 239 VAL C CA    1 
ATOM   6548 C  C     . VAL F 2 239 ? -27.328 11.998 125.383 1.00 9.54  ? 239 VAL C C     1 
ATOM   6549 O  O     . VAL F 2 239 ? -27.006 10.829 125.609 1.00 9.71  ? 239 VAL C O     1 
ATOM   6550 C  CB    . VAL F 2 239 ? -28.662 13.534 126.872 1.00 8.88  ? 239 VAL C CB    1 
ATOM   6551 C  CG1   . VAL F 2 239 ? -27.772 13.102 128.036 1.00 7.81  ? 239 VAL C CG1   1 
ATOM   6552 C  CG2   . VAL F 2 239 ? -28.107 14.881 126.400 1.00 8.34  ? 239 VAL C CG2   1 
ATOM   6553 N  N     . PHE F 2 240 ? -26.584 12.895 124.814 1.00 9.35  ? 240 PHE C N     1 
ATOM   6554 C  CA    . PHE F 2 240 ? -25.184 12.682 124.396 1.00 9.32  ? 240 PHE C CA    1 
ATOM   6555 C  C     . PHE F 2 240 ? -24.688 14.131 124.175 1.00 9.74  ? 240 PHE C C     1 
ATOM   6556 O  O     . PHE F 2 240 ? -25.299 14.761 123.301 1.00 9.94  ? 240 PHE C O     1 
ATOM   6557 C  CB    . PHE F 2 240 ? -24.989 11.826 123.180 1.00 8.74  ? 240 PHE C CB    1 
ATOM   6558 C  CG    . PHE F 2 240 ? -23.569 11.837 122.656 1.00 8.35  ? 240 PHE C CG    1 
ATOM   6559 C  CD1   . PHE F 2 240 ? -22.668 10.886 123.146 1.00 9.58  ? 240 PHE C CD1   1 
ATOM   6560 C  CD2   . PHE F 2 240 ? -23.150 12.748 121.699 1.00 7.09  ? 240 PHE C CD2   1 
ATOM   6561 C  CE1   . PHE F 2 240 ? -21.359 10.845 122.710 1.00 8.73  ? 240 PHE C CE1   1 
ATOM   6562 C  CE2   . PHE F 2 240 ? -21.833 12.725 121.249 1.00 7.53  ? 240 PHE C CE2   1 
ATOM   6563 C  CZ    . PHE F 2 240 ? -20.947 11.776 121.763 1.00 9.03  ? 240 PHE C CZ    1 
ATOM   6564 N  N     . SER F 2 241 ? -23.741 14.553 124.977 1.00 9.02  ? 241 SER C N     1 
ATOM   6565 C  CA    . SER F 2 241 ? -23.211 15.939 124.859 1.00 8.67  ? 241 SER C CA    1 
ATOM   6566 C  C     . SER F 2 241 ? -21.704 15.815 124.916 1.00 8.48  ? 241 SER C C     1 
ATOM   6567 O  O     . SER F 2 241 ? -21.265 14.699 125.215 1.00 9.56  ? 241 SER C O     1 
ATOM   6568 C  CB    . SER F 2 241 ? -23.793 16.824 125.939 1.00 8.04  ? 241 SER C CB    1 
ATOM   6569 O  OG    . SER F 2 241 ? -23.058 18.023 126.116 1.00 7.70  ? 241 SER C OG    1 
ATOM   6570 N  N     . GLN F 2 242 ? -20.961 16.839 124.635 1.00 8.26  ? 242 GLN C N     1 
ATOM   6571 C  CA    . GLN F 2 242 ? -19.489 16.805 124.703 1.00 8.35  ? 242 GLN C CA    1 
ATOM   6572 C  C     . GLN F 2 242 ? -18.948 18.127 125.254 1.00 7.87  ? 242 GLN C C     1 
ATOM   6573 O  O     . GLN F 2 242 ? -19.618 19.170 125.366 1.00 7.99  ? 242 GLN C O     1 
ATOM   6574 C  CB    . GLN F 2 242 ? -18.799 16.408 123.421 1.00 7.67  ? 242 GLN C CB    1 
ATOM   6575 C  CG    . GLN F 2 242 ? -19.187 17.144 122.174 1.00 9.73  ? 242 GLN C CG    1 
ATOM   6576 C  CD    . GLN F 2 242 ? -20.338 16.545 121.418 1.00 12.58 ? 242 GLN C CD    1 
ATOM   6577 O  OE1   . GLN F 2 242 ? -21.477 17.009 121.526 1.00 14.97 ? 242 GLN C OE1   1 
ATOM   6578 N  NE2   . GLN F 2 242 ? -20.088 15.509 120.617 1.00 12.49 ? 242 GLN C NE2   1 
ATOM   6579 N  N     . SER F 2 243 ? -17.679 18.046 125.617 1.00 7.43  ? 243 SER C N     1 
ATOM   6580 C  CA    . SER F 2 243 ? -16.980 19.247 126.124 1.00 7.37  ? 243 SER C CA    1 
ATOM   6581 C  C     . SER F 2 243 ? -15.814 19.572 125.188 1.00 6.65  ? 243 SER C C     1 
ATOM   6582 O  O     . SER F 2 243 ? -15.426 18.715 124.373 1.00 7.95  ? 243 SER C O     1 
ATOM   6583 C  CB    . SER F 2 243 ? -16.510 19.078 127.555 1.00 8.49  ? 243 SER C CB    1 
ATOM   6584 O  OG    . SER F 2 243 ? -16.422 20.390 128.123 1.00 9.84  ? 243 SER C OG    1 
ATOM   6585 N  N     . VAL F 2 244 ? -15.280 20.772 125.244 1.00 6.20  ? 244 VAL C N     1 
ATOM   6586 C  CA    . VAL F 2 244 ? -14.111 21.143 124.429 1.00 6.40  ? 244 VAL C CA    1 
ATOM   6587 C  C     . VAL F 2 244 ? -13.155 21.936 125.344 1.00 7.38  ? 244 VAL C C     1 
ATOM   6588 O  O     . VAL F 2 244 ? -13.577 22.503 126.374 1.00 8.63  ? 244 VAL C O     1 
ATOM   6589 C  CB    . VAL F 2 244 ? -14.428 21.869 123.130 1.00 4.93  ? 244 VAL C CB    1 
ATOM   6590 C  CG1   . VAL F 2 244 ? -14.912 20.924 122.039 1.00 3.96  ? 244 VAL C CG1   1 
ATOM   6591 C  CG2   . VAL F 2 244 ? -15.387 23.027 123.341 1.00 2.77  ? 244 VAL C CG2   1 
ATOM   6592 N  N     . CYS F 2 245 ? -11.902 21.921 124.912 1.00 7.07  ? 245 CYS C N     1 
ATOM   6593 C  CA    . CYS F 2 245 ? -10.857 22.650 125.638 1.00 7.19  ? 245 CYS C CA    1 
ATOM   6594 C  C     . CYS F 2 245 ? -11.294 24.094 125.864 1.00 7.24  ? 245 CYS C C     1 
ATOM   6595 O  O     . CYS F 2 245 ? -11.741 24.750 124.905 1.00 6.87  ? 245 CYS C O     1 
ATOM   6596 C  CB    . CYS F 2 245 ? -9.557  22.597 124.830 1.00 8.55  ? 245 CYS C CB    1 
ATOM   6597 S  SG    . CYS F 2 245 ? -8.257  23.559 125.649 1.00 10.75 ? 245 CYS C SG    1 
ATOM   6598 N  N     . ASN F 2 246 ? -11.173 24.581 127.079 1.00 7.69  ? 246 ASN C N     1 
ATOM   6599 C  CA    . ASN F 2 246 ? -11.590 25.944 127.416 1.00 7.52  ? 246 ASN C CA    1 
ATOM   6600 C  C     . ASN F 2 246 ? -10.421 26.923 127.405 1.00 7.48  ? 246 ASN C C     1 
ATOM   6601 O  O     . ASN F 2 246 ? -10.495 27.935 128.135 1.00 8.10  ? 246 ASN C O     1 
ATOM   6602 C  CB    . ASN F 2 246 ? -12.397 26.009 128.702 1.00 6.83  ? 246 ASN C CB    1 
ATOM   6603 C  CG    . ASN F 2 246 ? -11.688 25.447 129.909 1.00 11.24 ? 246 ASN C CG    1 
ATOM   6604 O  OD1   . ASN F 2 246 ? -12.365 25.019 130.857 1.00 12.57 ? 246 ASN C OD1   1 
ATOM   6605 N  ND2   . ASN F 2 246 ? -10.361 25.421 129.938 1.00 13.72 ? 246 ASN C ND2   1 
ATOM   6606 N  N     . GLU F 2 247 ? -9.435  26.624 126.601 1.00 7.22  ? 247 GLU C N     1 
ATOM   6607 C  CA    . GLU F 2 247 ? -8.286  27.539 126.481 1.00 8.06  ? 247 GLU C CA    1 
ATOM   6608 C  C     . GLU F 2 247 ? -7.814  27.596 125.027 1.00 8.47  ? 247 GLU C C     1 
ATOM   6609 O  O     . GLU F 2 247 ? -7.963  26.623 124.271 1.00 8.74  ? 247 GLU C O     1 
ATOM   6610 C  CB    . GLU F 2 247 ? -7.160  27.141 127.413 1.00 10.84 ? 247 GLU C CB    1 
ATOM   6611 C  CG    . GLU F 2 247 ? -7.645  26.793 128.822 1.00 13.08 ? 247 GLU C CG    1 
ATOM   6612 C  CD    . GLU F 2 247 ? -7.435  27.930 129.825 1.00 16.31 ? 247 GLU C CD    1 
ATOM   6613 O  OE1   . GLU F 2 247 ? -6.839  29.012 129.457 1.00 13.53 ? 247 GLU C OE1   1 
ATOM   6614 O  OE2   . GLU F 2 247 ? -7.855  27.805 131.038 1.00 17.69 ? 247 GLU C OE2   1 
ATOM   6615 N  N     . PRO F 2 248 ? -7.232  28.727 124.603 1.00 9.73  ? 248 PRO C N     1 
ATOM   6616 C  CA    . PRO F 2 248 ? -6.826  28.927 123.219 1.00 9.91  ? 248 PRO C CA    1 
ATOM   6617 C  C     . PRO F 2 248 ? -5.851  27.883 122.723 1.00 12.97 ? 248 PRO C C     1 
ATOM   6618 O  O     . PRO F 2 248 ? -5.616  27.799 121.478 1.00 13.43 ? 248 PRO C O     1 
ATOM   6619 C  CB    . PRO F 2 248 ? -6.217  30.306 123.207 1.00 8.85  ? 248 PRO C CB    1 
ATOM   6620 C  CG    . PRO F 2 248 ? -6.309  30.869 124.615 1.00 9.58  ? 248 PRO C CG    1 
ATOM   6621 C  CD    . PRO F 2 248 ? -6.962  29.854 125.499 1.00 7.73  ? 248 PRO C CD    1 
ATOM   6622 N  N     . ASP F 2 249 ? -5.284  27.108 123.632 1.00 15.34 ? 249 ASP C N     1 
ATOM   6623 C  CA    . ASP F 2 249 ? -4.328  26.045 123.244 1.00 15.32 ? 249 ASP C CA    1 
ATOM   6624 C  C     . ASP F 2 249 ? -4.485  24.827 124.170 1.00 12.61 ? 249 ASP C C     1 
ATOM   6625 O  O     . ASP F 2 249 ? -5.415  24.757 124.982 1.00 12.52 ? 249 ASP C O     1 
ATOM   6626 C  CB    . ASP F 2 249 ? -2.894  26.584 123.259 1.00 22.56 ? 249 ASP C CB    1 
ATOM   6627 C  CG    . ASP F 2 249 ? -2.502  27.246 124.574 1.00 24.49 ? 249 ASP C CG    1 
ATOM   6628 O  OD1   . ASP F 2 249 ? -2.007  26.532 125.524 1.00 27.95 ? 249 ASP C OD1   1 
ATOM   6629 O  OD2   . ASP F 2 249 ? -2.660  28.517 124.730 1.00 19.85 ? 249 ASP C OD2   1 
ATOM   6630 N  N     . PHE F 2 250 ? -3.561  23.881 124.031 1.00 9.62  ? 250 PHE C N     1 
ATOM   6631 C  CA    . PHE F 2 250 ? -3.625  22.596 124.769 1.00 10.61 ? 250 PHE C CA    1 
ATOM   6632 C  C     . PHE F 2 250 ? -2.376  22.314 125.602 1.00 12.44 ? 250 PHE C C     1 
ATOM   6633 O  O     . PHE F 2 250 ? -1.436  21.649 125.150 1.00 14.89 ? 250 PHE C O     1 
ATOM   6634 C  CB    . PHE F 2 250 ? -3.725  21.443 123.779 1.00 7.93  ? 250 PHE C CB    1 
ATOM   6635 C  CG    . PHE F 2 250 ? -5.116  21.289 123.181 1.00 7.41  ? 250 PHE C CG    1 
ATOM   6636 C  CD1   . PHE F 2 250 ? -6.063  20.503 123.838 1.00 8.17  ? 250 PHE C CD1   1 
ATOM   6637 C  CD2   . PHE F 2 250 ? -5.438  21.933 121.982 1.00 8.38  ? 250 PHE C CD2   1 
ATOM   6638 C  CE1   . PHE F 2 250 ? -7.340  20.352 123.294 1.00 8.90  ? 250 PHE C CE1   1 
ATOM   6639 C  CE2   . PHE F 2 250 ? -6.716  21.781 121.434 1.00 7.56  ? 250 PHE C CE2   1 
ATOM   6640 C  CZ    . PHE F 2 250 ? -7.667  20.989 122.091 1.00 6.83  ? 250 PHE C CZ    1 
ATOM   6641 N  N     . GLU F 2 251 ? -2.392  22.780 126.826 1.00 13.92 ? 251 GLU C N     1 
ATOM   6642 C  CA    . GLU F 2 251 ? -1.244  22.610 127.711 1.00 12.66 ? 251 GLU C CA    1 
ATOM   6643 C  C     . GLU F 2 251 ? -1.464  21.496 128.706 1.00 11.53 ? 251 GLU C C     1 
ATOM   6644 O  O     . GLU F 2 251 ? -2.582  20.982 128.867 1.00 13.54 ? 251 GLU C O     1 
ATOM   6645 C  CB    . GLU F 2 251 ? -0.967  23.892 128.466 1.00 16.22 ? 251 GLU C CB    1 
ATOM   6646 C  CG    . GLU F 2 251 ? -0.187  24.885 127.617 1.00 24.16 ? 251 GLU C CG    1 
ATOM   6647 C  CD    . GLU F 2 251 ? 0.278   26.101 128.402 1.00 31.33 ? 251 GLU C CD    1 
ATOM   6648 O  OE1   . GLU F 2 251 ? -0.053  26.231 129.640 1.00 31.86 ? 251 GLU C OE1   1 
ATOM   6649 O  OE2   . GLU F 2 251 ? 0.999   26.997 127.821 1.00 30.02 ? 251 GLU C OE2   1 
ATOM   6650 N  N     . PHE F 2 252 ? -0.365  21.192 129.327 1.00 10.79 ? 252 PHE C N     1 
ATOM   6651 C  CA    . PHE F 2 252 ? -0.293  20.135 130.301 1.00 10.39 ? 252 PHE C CA    1 
ATOM   6652 C  C     . PHE F 2 252 ? -0.569  20.662 131.695 1.00 11.08 ? 252 PHE C C     1 
ATOM   6653 O  O     . PHE F 2 252 ? 0.008   21.673 132.124 1.00 12.34 ? 252 PHE C O     1 
ATOM   6654 C  CB    . PHE F 2 252 ? 1.102   19.523 130.291 1.00 8.41  ? 252 PHE C CB    1 
ATOM   6655 C  CG    . PHE F 2 252 ? 1.363   18.642 129.070 1.00 7.91  ? 252 PHE C CG    1 
ATOM   6656 C  CD1   . PHE F 2 252 ? 0.972   17.299 129.085 1.00 6.77  ? 252 PHE C CD1   1 
ATOM   6657 C  CD2   . PHE F 2 252 ? 1.992   19.178 127.941 1.00 5.79  ? 252 PHE C CD2   1 
ATOM   6658 C  CE1   . PHE F 2 252 ? 1.220   16.487 127.973 1.00 6.43  ? 252 PHE C CE1   1 
ATOM   6659 C  CE2   . PHE F 2 252 ? 2.243   18.365 126.829 1.00 4.51  ? 252 PHE C CE2   1 
ATOM   6660 C  CZ    . PHE F 2 252 ? 1.858   17.019 126.846 1.00 4.97  ? 252 PHE C CZ    1 
ATOM   6661 N  N     . SER F 2 253 ? -1.456  19.944 132.335 1.00 10.38 ? 253 SER C N     1 
ATOM   6662 C  CA    . SER F 2 253 ? -1.805  20.173 133.727 1.00 9.42  ? 253 SER C CA    1 
ATOM   6663 C  C     . SER F 2 253 ? -0.928  19.211 134.550 1.00 9.62  ? 253 SER C C     1 
ATOM   6664 O  O     . SER F 2 253 ? -0.611  18.119 134.041 1.00 9.09  ? 253 SER C O     1 
ATOM   6665 C  CB    . SER F 2 253 ? -3.290  19.880 133.950 1.00 7.45  ? 253 SER C CB    1 
ATOM   6666 O  OG    . SER F 2 253 ? -4.083  20.845 133.275 1.00 10.08 ? 253 SER C OG    1 
ATOM   6667 N  N     . ASP F 2 254 ? -0.569  19.584 135.759 1.00 10.29 ? 254 ASP C N     1 
ATOM   6668 C  CA    . ASP F 2 254 ? 0.257   18.708 136.608 1.00 11.30 ? 254 ASP C CA    1 
ATOM   6669 C  C     . ASP F 2 254 ? -0.612  17.776 137.441 1.00 10.99 ? 254 ASP C C     1 
ATOM   6670 O  O     . ASP F 2 254 ? -1.777  18.052 137.755 1.00 11.37 ? 254 ASP C O     1 
ATOM   6671 C  CB    . ASP F 2 254 ? 1.231   19.519 137.439 1.00 13.78 ? 254 ASP C CB    1 
ATOM   6672 C  CG    . ASP F 2 254 ? 2.219   20.347 136.647 1.00 16.51 ? 254 ASP C CG    1 
ATOM   6673 O  OD1   . ASP F 2 254 ? 2.531   19.983 135.486 1.00 17.86 ? 254 ASP C OD1   1 
ATOM   6674 O  OD2   . ASP F 2 254 ? 2.711   21.357 137.204 1.00 17.27 ? 254 ASP C OD2   1 
ATOM   6675 N  N     . ILE F 2 255 ? -0.026  16.644 137.774 1.00 11.09 ? 255 ILE C N     1 
ATOM   6676 C  CA    . ILE F 2 255 ? -0.700  15.623 138.635 1.00 10.69 ? 255 ILE C CA    1 
ATOM   6677 C  C     . ILE F 2 255 ? -0.644  16.285 140.023 1.00 10.91 ? 255 ILE C C     1 
ATOM   6678 O  O     . ILE F 2 255 ? 0.350   17.007 140.253 1.00 10.79 ? 255 ILE C O     1 
ATOM   6679 C  CB    . ILE F 2 255 ? 0.002   14.241 138.584 1.00 8.72  ? 255 ILE C CB    1 
ATOM   6680 C  CG1   . ILE F 2 255 ? -0.494  13.471 137.336 1.00 8.92  ? 255 ILE C CG1   1 
ATOM   6681 C  CG2   . ILE F 2 255 ? -0.119  13.403 139.874 1.00 6.53  ? 255 ILE C CG2   1 
ATOM   6682 C  CD1   . ILE F 2 255 ? -1.999  13.116 137.352 1.00 9.87  ? 255 ILE C CD1   1 
ATOM   6683 N  N     . LEU F 2 256 ? -1.658  16.111 140.819 1.00 11.11 ? 256 LEU C N     1 
ATOM   6684 C  CA    . LEU F 2 256 ? -1.730  16.732 142.153 1.00 10.68 ? 256 LEU C CA    1 
ATOM   6685 C  C     . LEU F 2 256 ? -1.639  15.700 143.257 1.00 11.25 ? 256 LEU C C     1 
ATOM   6686 O  O     . LEU F 2 256 ? -2.445  14.728 143.225 1.00 13.22 ? 256 LEU C O     1 
ATOM   6687 C  CB    . LEU F 2 256 ? -3.093  17.473 142.164 1.00 7.69  ? 256 LEU C CB    1 
ATOM   6688 C  CG    . LEU F 2 256 ? -3.315  18.563 141.128 1.00 6.72  ? 256 LEU C CG    1 
ATOM   6689 C  CD1   . LEU F 2 256 ? -4.786  18.993 141.050 1.00 5.07  ? 256 LEU C CD1   1 
ATOM   6690 C  CD2   . LEU F 2 256 ? -2.447  19.760 141.518 1.00 4.58  ? 256 LEU C CD2   1 
ATOM   6691 N  N     . GLU F 2 257 ? -0.776  15.897 144.234 1.00 10.31 ? 257 GLU C N     1 
ATOM   6692 C  CA    . GLU F 2 257 ? -0.703  14.894 145.329 1.00 9.28  ? 257 GLU C CA    1 
ATOM   6693 C  C     . GLU F 2 257 ? -1.533  15.241 146.592 1.00 8.89  ? 257 GLU C C     1 
ATOM   6694 O  O     . GLU F 2 257 ? -1.598  16.403 147.017 1.00 9.64  ? 257 GLU C O     1 
ATOM   6695 C  CB    . GLU F 2 257 ? 0.761   14.696 145.750 1.00 9.02  ? 257 GLU C CB    1 
ATOM   6696 C  CG    . GLU F 2 257 ? 1.610   14.029 144.668 1.00 8.02  ? 257 GLU C CG    1 
ATOM   6697 C  CD    . GLU F 2 257 ? 1.493   12.504 144.677 1.00 7.92  ? 257 GLU C CD    1 
ATOM   6698 O  OE1   . GLU F 2 257 ? 0.340   11.948 144.831 1.00 4.94  ? 257 GLU C OE1   1 
ATOM   6699 O  OE2   . GLU F 2 257 ? 2.548   11.776 144.533 1.00 8.71  ? 257 GLU C OE2   1 
ATOM   6700 N  N     . GLY F 2 258 ? -2.143  14.160 147.107 1.00 7.98  ? 258 GLY C N     1 
ATOM   6701 C  CA    . GLY F 2 258 ? -2.866  14.098 148.410 1.00 8.65  ? 258 GLY C CA    1 
ATOM   6702 C  C     . GLY F 2 258 ? -4.302  14.692 148.460 1.00 8.79  ? 258 GLY C C     1 
ATOM   6703 O  O     . GLY F 2 258 ? -4.849  14.948 149.541 1.00 9.69  ? 258 GLY C O     1 
ATOM   6704 N  N     . ILE F 2 259 ? -4.966  14.915 147.341 1.00 7.92  ? 259 ILE C N     1 
ATOM   6705 C  CA    . ILE F 2 259 ? -6.341  15.495 147.389 1.00 7.27  ? 259 ILE C CA    1 
ATOM   6706 C  C     . ILE F 2 259 ? -7.407  14.385 147.327 1.00 7.81  ? 259 ILE C C     1 
ATOM   6707 O  O     . ILE F 2 259 ? -7.507  13.649 146.338 1.00 7.94  ? 259 ILE C O     1 
ATOM   6708 C  CB    . ILE F 2 259 ? -6.563  16.460 146.223 1.00 6.35  ? 259 ILE C CB    1 
ATOM   6709 C  CG1   . ILE F 2 259 ? -5.538  17.595 146.188 1.00 5.66  ? 259 ILE C CG1   1 
ATOM   6710 C  CG2   . ILE F 2 259 ? -7.935  17.141 146.263 1.00 4.98  ? 259 ILE C CG2   1 
ATOM   6711 C  CD1   . ILE F 2 259 ? -5.596  18.416 144.899 1.00 4.13  ? 259 ILE C CD1   1 
ATOM   6712 N  N     . GLN F 2 260 ? -8.202  14.285 148.392 1.00 8.28  ? 260 GLN C N     1 
ATOM   6713 C  CA    . GLN F 2 260 ? -9.260  13.251 148.488 1.00 9.20  ? 260 GLN C CA    1 
ATOM   6714 C  C     . GLN F 2 260 ? -10.616 13.890 148.434 1.00 11.52 ? 260 GLN C C     1 
ATOM   6715 O  O     . GLN F 2 260 ? -11.437 13.567 147.562 1.00 12.13 ? 260 GLN C O     1 
ATOM   6716 C  CB    . GLN F 2 260 ? -9.031  12.406 149.739 1.00 5.11  ? 260 GLN C CB    1 
ATOM   6717 C  CG    . GLN F 2 260 ? -7.743  11.562 149.641 1.00 3.20  ? 260 GLN C CG    1 
ATOM   6718 C  CD    . GLN F 2 260 ? -7.827  10.434 148.600 1.00 4.83  ? 260 GLN C CD    1 
ATOM   6719 O  OE1   . GLN F 2 260 ? -6.835  10.125 147.936 1.00 5.95  ? 260 GLN C OE1   1 
ATOM   6720 N  NE2   . GLN F 2 260 ? -8.964  9.789  148.417 1.00 5.76  ? 260 GLN C NE2   1 
ATOM   6721 N  N     . THR F 2 261 ? -10.824 14.762 149.358 1.00 13.06 ? 261 THR C N     1 
ATOM   6722 C  CA    . THR F 2 261 ? -12.014 15.568 149.350 1.00 14.90 ? 261 THR C CA    1 
ATOM   6723 C  C     . THR F 2 261 ? -11.560 16.981 149.052 1.00 16.58 ? 261 THR C C     1 
ATOM   6724 O  O     . THR F 2 261 ? -10.388 17.326 149.272 1.00 18.58 ? 261 THR C O     1 
ATOM   6725 C  CB    . THR F 2 261 ? -12.771 15.470 150.670 1.00 13.86 ? 261 THR C CB    1 
ATOM   6726 O  OG1   . THR F 2 261 ? -12.454 16.580 151.491 1.00 15.22 ? 261 THR C OG1   1 
ATOM   6727 C  CG2   . THR F 2 261 ? -12.452 14.198 151.452 1.00 11.32 ? 261 THR C CG2   1 
ATOM   6728 N  N     . LEU F 2 262 ? -12.506 17.696 148.558 1.00 16.67 ? 262 LEU C N     1 
ATOM   6729 C  CA    . LEU F 2 262 ? -12.384 19.084 148.147 1.00 16.79 ? 262 LEU C CA    1 
ATOM   6730 C  C     . LEU F 2 262 ? -13.678 19.744 148.582 1.00 18.32 ? 262 LEU C C     1 
ATOM   6731 O  O     . LEU F 2 262 ? -14.737 19.489 148.014 1.00 22.42 ? 262 LEU C O     1 
ATOM   6732 C  CB    . LEU F 2 262 ? -12.316 19.081 146.606 1.00 13.74 ? 262 LEU C CB    1 
ATOM   6733 C  CG    . LEU F 2 262 ? -11.337 20.066 145.968 1.00 12.44 ? 262 LEU C CG    1 
ATOM   6734 C  CD1   . LEU F 2 262 ? -9.997  20.154 146.691 1.00 10.53 ? 262 LEU C CD1   1 
ATOM   6735 C  CD2   . LEU F 2 262 ? -10.999 19.694 144.515 1.00 11.86 ? 262 LEU C CD2   1 
ATOM   6736 N  N     . PRO F 2 263 ? -13.793 20.631 149.585 1.00 15.86 ? 263 PRO C N     1 
ATOM   6737 C  CA    . PRO F 2 263 ? -12.687 21.130 150.392 1.00 13.50 ? 263 PRO C CA    1 
ATOM   6738 C  C     . PRO F 2 263 ? -11.954 20.073 151.145 1.00 11.97 ? 263 PRO C C     1 
ATOM   6739 O  O     . PRO F 2 263 ? -12.594 19.055 151.559 1.00 12.82 ? 263 PRO C O     1 
ATOM   6740 C  CB    . PRO F 2 263 ? -13.341 22.097 151.355 1.00 12.72 ? 263 PRO C CB    1 
ATOM   6741 C  CG    . PRO F 2 263 ? -14.837 22.108 151.051 1.00 13.69 ? 263 PRO C CG    1 
ATOM   6742 C  CD    . PRO F 2 263 ? -15.116 21.161 149.918 1.00 14.07 ? 263 PRO C CD    1 
ATOM   6743 N  N     . PRO F 2 264 ? -10.642 20.281 151.331 1.00 10.20 ? 264 PRO C N     1 
ATOM   6744 C  CA    . PRO F 2 264 ? -9.809  19.368 152.088 1.00 9.30  ? 264 PRO C CA    1 
ATOM   6745 C  C     . PRO F 2 264 ? -10.265 19.330 153.518 1.00 9.97  ? 264 PRO C C     1 
ATOM   6746 O  O     . PRO F 2 264 ? -10.961 20.288 153.975 1.00 10.71 ? 264 PRO C O     1 
ATOM   6747 C  CB    . PRO F 2 264 ? -8.426  19.974 151.997 1.00 8.01  ? 264 PRO C CB    1 
ATOM   6748 C  CG    . PRO F 2 264 ? -8.532  21.257 151.187 1.00 7.96  ? 264 PRO C CG    1 
ATOM   6749 C  CD    . PRO F 2 264 ? -9.955  21.448 150.777 1.00 9.47  ? 264 PRO C CD    1 
ATOM   6750 N  N     . ALA F 2 265 ? -9.891  18.267 154.201 1.00 10.52 ? 265 ALA C N     1 
ATOM   6751 C  CA    . ALA F 2 265 ? -10.216 18.123 155.617 1.00 10.12 ? 265 ALA C CA    1 
ATOM   6752 C  C     . ALA F 2 265 ? -9.777  19.377 156.346 1.00 10.21 ? 265 ALA C C     1 
ATOM   6753 O  O     . ALA F 2 265 ? -8.893  20.111 155.885 1.00 11.28 ? 265 ALA C O     1 
ATOM   6754 C  CB    . ALA F 2 265 ? -9.450  16.947 156.231 1.00 6.29  ? 265 ALA C CB    1 
ATOM   6755 N  N     . ASN F 2 266 ? -10.412 19.596 157.454 1.00 10.44 ? 266 ASN C N     1 
ATOM   6756 C  CA    . ASN F 2 266 ? -10.041 20.687 158.336 1.00 10.37 ? 266 ASN C CA    1 
ATOM   6757 C  C     . ASN F 2 266 ? -10.101 22.031 157.608 1.00 10.82 ? 266 ASN C C     1 
ATOM   6758 O  O     . ASN F 2 266 ? -9.385  22.977 157.958 1.00 11.56 ? 266 ASN C O     1 
ATOM   6759 C  CB    . ASN F 2 266 ? -8.652  20.384 158.867 1.00 9.76  ? 266 ASN C CB    1 
ATOM   6760 C  CG    . ASN F 2 266 ? -8.590  18.966 159.440 1.00 12.64 ? 266 ASN C CG    1 
ATOM   6761 O  OD1   . ASN F 2 266 ? -9.637  18.347 159.647 1.00 13.12 ? 266 ASN C OD1   1 
ATOM   6762 N  ND2   . ASN F 2 266 ? -7.430  18.408 159.715 1.00 13.60 ? 266 ASN C ND2   1 
ATOM   6763 N  N     . VAL F 2 267 ? -10.954 22.048 156.616 1.00 10.26 ? 267 VAL C N     1 
ATOM   6764 C  CA    . VAL F 2 267 ? -11.307 23.259 155.869 1.00 10.87 ? 267 VAL C CA    1 
ATOM   6765 C  C     . VAL F 2 267 ? -12.808 23.160 155.666 1.00 11.24 ? 267 VAL C C     1 
ATOM   6766 O  O     . VAL F 2 267 ? -13.164 22.102 155.090 1.00 13.05 ? 267 VAL C O     1 
ATOM   6767 C  CB    . VAL F 2 267 ? -10.474 23.389 154.589 1.00 11.08 ? 267 VAL C CB    1 
ATOM   6768 C  CG1   . VAL F 2 267 ? -9.945  22.058 154.068 1.00 11.36 ? 267 VAL C CG1   1 
ATOM   6769 C  CG2   . VAL F 2 267 ? -11.244 24.027 153.433 1.00 10.25 ? 267 VAL C CG2   1 
ATOM   6770 N  N     . THR F 2 268 ? -13.551 24.097 156.232 1.00 10.73 ? 268 THR C N     1 
ATOM   6771 C  CA    . THR F 2 268 ? -15.025 23.984 156.119 1.00 11.05 ? 268 THR C CA    1 
ATOM   6772 C  C     . THR F 2 268 ? -15.450 24.484 154.760 1.00 11.50 ? 268 THR C C     1 
ATOM   6773 O  O     . THR F 2 268 ? -14.675 25.142 154.051 1.00 11.49 ? 268 THR C O     1 
ATOM   6774 C  CB    . THR F 2 268 ? -15.760 24.822 157.232 1.00 12.09 ? 268 THR C CB    1 
ATOM   6775 O  OG1   . THR F 2 268 ? -15.600 26.210 156.969 1.00 13.82 ? 268 THR C OG1   1 
ATOM   6776 C  CG2   . THR F 2 268 ? -15.222 24.546 158.637 1.00 12.69 ? 268 THR C CG2   1 
ATOM   6777 N  N     . VAL F 2 269 ? -16.666 24.154 154.470 1.00 12.71 ? 269 VAL C N     1 
ATOM   6778 C  CA    . VAL F 2 269 ? -17.285 24.426 153.184 1.00 13.87 ? 269 VAL C CA    1 
ATOM   6779 C  C     . VAL F 2 269 ? -17.608 25.893 153.000 1.00 15.00 ? 269 VAL C C     1 
ATOM   6780 O  O     . VAL F 2 269 ? -17.898 26.361 151.893 1.00 16.86 ? 269 VAL C O     1 
ATOM   6781 C  CB    . VAL F 2 269 ? -18.569 23.635 153.096 1.00 12.34 ? 269 VAL C CB    1 
ATOM   6782 C  CG1   . VAL F 2 269 ? -19.493 24.121 151.981 1.00 10.68 ? 269 VAL C CG1   1 
ATOM   6783 C  CG2   . VAL F 2 269 ? -18.318 22.150 152.835 1.00 13.72 ? 269 VAL C CG2   1 
ATOM   6784 N  N     . ALA F 2 270 ? -17.577 26.600 154.067 1.00 14.21 ? 270 ALA C N     1 
ATOM   6785 C  CA    . ALA F 2 270 ? -17.855 28.017 154.022 1.00 13.60 ? 270 ALA C CA    1 
ATOM   6786 C  C     . ALA F 2 270 ? -16.549 28.770 153.800 1.00 13.82 ? 270 ALA C C     1 
ATOM   6787 O  O     . ALA F 2 270 ? -16.528 29.849 153.192 1.00 14.85 ? 270 ALA C O     1 
ATOM   6788 C  CB    . ALA F 2 270 ? -18.501 28.449 155.335 1.00 13.36 ? 270 ALA C CB    1 
ATOM   6789 N  N     . THR F 2 271 ? -15.482 28.176 154.302 1.00 13.06 ? 271 THR C N     1 
ATOM   6790 C  CA    . THR F 2 271 ? -14.140 28.759 154.190 1.00 13.17 ? 271 THR C CA    1 
ATOM   6791 C  C     . THR F 2 271 ? -13.691 28.781 152.727 1.00 14.11 ? 271 THR C C     1 
ATOM   6792 O  O     . THR F 2 271 ? -13.272 29.826 152.206 1.00 15.56 ? 271 THR C O     1 
ATOM   6793 C  CB    . THR F 2 271 ? -13.115 27.949 154.988 1.00 12.49 ? 271 THR C CB    1 
ATOM   6794 O  OG1   . THR F 2 271 ? -13.296 28.169 156.379 1.00 13.29 ? 271 THR C OG1   1 
ATOM   6795 C  CG2   . THR F 2 271 ? -11.669 28.322 154.652 1.00 12.43 ? 271 THR C CG2   1 
ATOM   6796 N  N     . SER F 2 272 ? -13.816 27.603 152.147 1.00 14.37 ? 272 SER C N     1 
ATOM   6797 C  CA    . SER F 2 272 ? -13.432 27.301 150.757 1.00 15.44 ? 272 SER C CA    1 
ATOM   6798 C  C     . SER F 2 272 ? -14.258 28.093 149.741 1.00 16.64 ? 272 SER C C     1 
ATOM   6799 O  O     . SER F 2 272 ? -13.880 28.209 148.566 1.00 18.66 ? 272 SER C O     1 
ATOM   6800 C  CB    . SER F 2 272 ? -13.694 25.829 150.469 1.00 13.72 ? 272 SER C CB    1 
ATOM   6801 O  OG    . SER F 2 272 ? -15.096 25.613 150.380 1.00 11.86 ? 272 SER C OG    1 
ATOM   6802 N  N     . GLY F 2 273 ? -15.377 28.594 150.213 1.00 16.30 ? 273 GLY C N     1 
ATOM   6803 C  CA    . GLY F 2 273 ? -16.300 29.397 149.395 1.00 15.69 ? 273 GLY C CA    1 
ATOM   6804 C  C     . GLY F 2 273 ? -16.979 28.557 148.291 1.00 15.77 ? 273 GLY C C     1 
ATOM   6805 O  O     . GLY F 2 273 ? -17.419 29.085 147.265 1.00 17.73 ? 273 GLY C O     1 
ATOM   6806 N  N     . GLN F 2 274 ? -17.076 27.252 148.504 1.00 13.71 ? 274 GLN C N     1 
ATOM   6807 C  CA    . GLN F 2 274 ? -17.727 26.343 147.522 1.00 11.45 ? 274 GLN C CA    1 
ATOM   6808 C  C     . GLN F 2 274 ? -19.182 26.123 147.897 1.00 11.30 ? 274 GLN C C     1 
ATOM   6809 O  O     . GLN F 2 274 ? -19.499 26.142 149.115 1.00 12.54 ? 274 GLN C O     1 
ATOM   6810 C  CB    . GLN F 2 274 ? -17.025 24.993 147.511 1.00 8.82  ? 274 GLN C CB    1 
ATOM   6811 C  CG    . GLN F 2 274 ? -15.887 24.917 146.500 1.00 9.64  ? 274 GLN C CG    1 
ATOM   6812 C  CD    . GLN F 2 274 ? -15.146 23.589 146.574 1.00 11.40 ? 274 GLN C CD    1 
ATOM   6813 O  OE1   . GLN F 2 274 ? -13.919 23.568 146.517 1.00 12.43 ? 274 GLN C OE1   1 
ATOM   6814 N  NE2   . GLN F 2 274 ? -15.833 22.470 146.705 1.00 11.17 ? 274 GLN C NE2   1 
ATOM   6815 N  N     . PRO F 2 275 ? -20.054 25.857 146.934 1.00 10.07 ? 275 PRO C N     1 
ATOM   6816 C  CA    . PRO F 2 275 ? -21.466 25.589 147.219 1.00 10.40 ? 275 PRO C CA    1 
ATOM   6817 C  C     . PRO F 2 275 ? -21.703 24.212 147.834 1.00 11.22 ? 275 PRO C C     1 
ATOM   6818 O  O     . PRO F 2 275 ? -22.758 24.070 148.509 1.00 11.29 ? 275 PRO C O     1 
ATOM   6819 C  CB    . PRO F 2 275 ? -22.209 25.780 145.900 1.00 9.66  ? 275 PRO C CB    1 
ATOM   6820 C  CG    . PRO F 2 275 ? -21.177 25.723 144.834 1.00 9.63  ? 275 PRO C CG    1 
ATOM   6821 C  CD    . PRO F 2 275 ? -19.801 25.791 145.494 1.00 9.61  ? 275 PRO C CD    1 
ATOM   6822 N  N     . PHE F 2 276 ? -20.823 23.258 147.631 1.00 11.65 ? 276 PHE C N     1 
ATOM   6823 C  CA    . PHE F 2 276 ? -20.948 21.881 148.121 1.00 12.35 ? 276 PHE C CA    1 
ATOM   6824 C  C     . PHE F 2 276 ? -19.557 21.226 148.109 1.00 13.55 ? 276 PHE C C     1 
ATOM   6825 O  O     . PHE F 2 276 ? -18.580 21.978 147.961 1.00 14.09 ? 276 PHE C O     1 
ATOM   6826 C  CB    . PHE F 2 276 ? -21.937 21.003 147.331 1.00 9.94  ? 276 PHE C CB    1 
ATOM   6827 C  CG    . PHE F 2 276 ? -21.876 21.187 145.853 1.00 10.82 ? 276 PHE C CG    1 
ATOM   6828 C  CD1   . PHE F 2 276 ? -20.999 20.423 145.080 1.00 11.50 ? 276 PHE C CD1   1 
ATOM   6829 C  CD2   . PHE F 2 276 ? -22.656 22.146 145.212 1.00 11.46 ? 276 PHE C CD2   1 
ATOM   6830 C  CE1   . PHE F 2 276 ? -20.893 20.602 143.704 1.00 12.23 ? 276 PHE C CE1   1 
ATOM   6831 C  CE2   . PHE F 2 276 ? -22.580 22.362 143.833 1.00 9.75  ? 276 PHE C CE2   1 
ATOM   6832 C  CZ    . PHE F 2 276 ? -21.683 21.578 143.087 1.00 10.69 ? 276 PHE C CZ    1 
ATOM   6833 N  N     . ASN F 2 277 ? -19.562 19.903 148.232 1.00 14.16 ? 277 ASN C N     1 
ATOM   6834 C  CA    . ASN F 2 277 ? -18.372 19.077 148.271 1.00 13.28 ? 277 ASN C CA    1 
ATOM   6835 C  C     . ASN F 2 277 ? -18.245 18.006 147.176 1.00 13.57 ? 277 ASN C C     1 
ATOM   6836 O  O     . ASN F 2 277 ? -19.202 17.504 146.574 1.00 14.37 ? 277 ASN C O     1 
ATOM   6837 C  CB    . ASN F 2 277 ? -18.267 18.305 149.606 1.00 12.72 ? 277 ASN C CB    1 
ATOM   6838 C  CG    . ASN F 2 277 ? -18.435 19.202 150.798 1.00 16.42 ? 277 ASN C CG    1 
ATOM   6839 O  OD1   . ASN F 2 277 ? -17.537 19.247 151.674 1.00 21.14 ? 277 ASN C OD1   1 
ATOM   6840 N  ND2   . ASN F 2 277 ? -19.597 19.898 150.855 1.00 15.30 ? 277 ASN C ND2   1 
ATOM   6841 N  N     . LEU F 2 278 ? -16.985 17.608 147.034 1.00 13.09 ? 278 LEU C N     1 
ATOM   6842 C  CA    . LEU F 2 278 ? -16.586 16.551 146.097 1.00 11.14 ? 278 LEU C CA    1 
ATOM   6843 C  C     . LEU F 2 278 ? -15.703 15.571 146.885 1.00 10.78 ? 278 LEU C C     1 
ATOM   6844 O  O     . LEU F 2 278 ? -14.528 15.928 147.165 1.00 9.71  ? 278 LEU C O     1 
ATOM   6845 C  CB    . LEU F 2 278 ? -15.971 17.247 144.894 1.00 10.18 ? 278 LEU C CB    1 
ATOM   6846 C  CG    . LEU F 2 278 ? -16.735 17.394 143.595 1.00 12.05 ? 278 LEU C CG    1 
ATOM   6847 C  CD1   . LEU F 2 278 ? -17.396 18.749 143.430 1.00 12.40 ? 278 LEU C CD1   1 
ATOM   6848 C  CD2   . LEU F 2 278 ? -15.754 17.191 142.426 1.00 11.65 ? 278 LEU C CD2   1 
ATOM   6849 N  N     . ALA F 2 279 ? -16.244 14.411 147.319 1.00 10.39 ? 279 ALA C N     1 
ATOM   6850 C  CA    . ALA F 2 279 ? -15.406 13.447 148.060 1.00 9.93  ? 279 ALA C CA    1 
ATOM   6851 C  C     . ALA F 2 279 ? -15.052 12.346 147.057 1.00 10.79 ? 279 ALA C C     1 
ATOM   6852 O  O     . ALA F 2 279 ? -15.966 11.964 146.308 1.00 12.30 ? 279 ALA C O     1 
ATOM   6853 C  CB    . ALA F 2 279 ? -15.996 12.807 149.274 1.00 7.17  ? 279 ALA C CB    1 
ATOM   6854 N  N     . ALA F 2 280 ? -13.821 11.930 147.088 1.00 10.88 ? 280 ALA C N     1 
ATOM   6855 C  CA    . ALA F 2 280 ? -13.345 10.880 146.172 1.00 10.22 ? 280 ALA C CA    1 
ATOM   6856 C  C     . ALA F 2 280 ? -13.182 9.603  146.993 1.00 10.25 ? 280 ALA C C     1 
ATOM   6857 O  O     . ALA F 2 280 ? -12.678 8.568  146.509 1.00 11.46 ? 280 ALA C O     1 
ATOM   6858 C  CB    . ALA F 2 280 ? -12.010 11.242 145.540 1.00 7.85  ? 280 ALA C CB    1 
ATOM   6859 N  N     . GLY F 2 281 ? -13.555 9.750  148.253 1.00 9.83  ? 281 GLY C N     1 
ATOM   6860 C  CA    . GLY F 2 281 ? -13.479 8.609  149.172 1.00 9.58  ? 281 GLY C CA    1 
ATOM   6861 C  C     . GLY F 2 281 ? -12.102 8.318  149.714 1.00 9.43  ? 281 GLY C C     1 
ATOM   6862 O  O     . GLY F 2 281 ? -11.286 9.198  149.960 1.00 9.81  ? 281 GLY C O     1 
ATOM   6863 N  N     . ALA F 2 282 ? -11.892 7.044  149.943 1.00 9.17  ? 282 ALA C N     1 
ATOM   6864 C  CA    . ALA F 2 282 ? -10.685 6.438  150.455 1.00 8.70  ? 282 ALA C CA    1 
ATOM   6865 C  C     . ALA F 2 282 ? -9.570  6.547  149.409 1.00 10.03 ? 282 ALA C C     1 
ATOM   6866 O  O     . ALA F 2 282 ? -9.845  6.418  148.198 1.00 10.35 ? 282 ALA C O     1 
ATOM   6867 C  CB    . ALA F 2 282 ? -11.034 4.947  150.612 1.00 6.10  ? 282 ALA C CB    1 
ATOM   6868 N  N     . GLU F 2 283 ? -8.351  6.696  149.911 1.00 10.99 ? 283 GLU C N     1 
ATOM   6869 C  CA    . GLU F 2 283 ? -7.146  6.764  149.076 1.00 12.06 ? 283 GLU C CA    1 
ATOM   6870 C  C     . GLU F 2 283 ? -7.090  5.532  148.156 1.00 12.35 ? 283 GLU C C     1 
ATOM   6871 O  O     . GLU F 2 283 ? -6.867  5.594  146.943 1.00 13.84 ? 283 GLU C O     1 
ATOM   6872 C  CB    . GLU F 2 283 ? -5.864  6.691  149.878 1.00 11.51 ? 283 GLU C CB    1 
ATOM   6873 C  CG    . GLU F 2 283 ? -5.629  7.627  151.061 1.00 13.04 ? 283 GLU C CG    1 
ATOM   6874 C  CD    . GLU F 2 283 ? -4.338  7.233  151.740 1.00 17.08 ? 283 GLU C CD    1 
ATOM   6875 O  OE1   . GLU F 2 283 ? -4.176  6.138  152.277 1.00 19.28 ? 283 GLU C OE1   1 
ATOM   6876 O  OE2   . GLU F 2 283 ? -3.454  8.102  151.625 1.00 18.68 ? 283 GLU C OE2   1 
ATOM   6877 N  N     . ALA F 2 284 ? -7.254  4.416  148.847 1.00 11.49 ? 284 ALA C N     1 
ATOM   6878 C  CA    . ALA F 2 284 ? -7.240  3.093  148.242 1.00 11.27 ? 284 ALA C CA    1 
ATOM   6879 C  C     . ALA F 2 284 ? -8.268  2.942  147.111 1.00 11.51 ? 284 ALA C C     1 
ATOM   6880 O  O     . ALA F 2 284 ? -8.202  2.001  146.308 1.00 13.10 ? 284 ALA C O     1 
ATOM   6881 C  CB    . ALA F 2 284 ? -7.611  2.104  149.342 1.00 8.76  ? 284 ALA C CB    1 
ATOM   6882 N  N     . VAL F 2 285 ? -9.208  3.866  147.050 1.00 10.50 ? 285 VAL C N     1 
ATOM   6883 C  CA    . VAL F 2 285 ? -10.305 3.783  146.067 1.00 10.58 ? 285 VAL C CA    1 
ATOM   6884 C  C     . VAL F 2 285 ? -10.106 4.763  144.912 1.00 10.78 ? 285 VAL C C     1 
ATOM   6885 O  O     . VAL F 2 285 ? -9.935  4.359  143.752 1.00 10.11 ? 285 VAL C O     1 
ATOM   6886 C  CB    . VAL F 2 285 ? -11.634 4.021  146.781 1.00 10.00 ? 285 VAL C CB    1 
ATOM   6887 C  CG1   . VAL F 2 285 ? -12.848 3.709  145.904 1.00 11.05 ? 285 VAL C CG1   1 
ATOM   6888 C  CG2   . VAL F 2 285 ? -11.798 3.164  148.038 1.00 9.49  ? 285 VAL C CG2   1 
ATOM   6889 N  N     . SER F 2 286 ? -10.119 6.034  145.235 1.00 10.68 ? 286 SER C N     1 
ATOM   6890 C  CA    . SER F 2 286 ? -10.027 7.078  144.212 1.00 10.82 ? 286 SER C CA    1 
ATOM   6891 C  C     . SER F 2 286 ? -9.400  8.346  144.790 1.00 11.15 ? 286 SER C C     1 
ATOM   6892 O  O     . SER F 2 286 ? -8.721  8.318  145.824 1.00 12.10 ? 286 SER C O     1 
ATOM   6893 C  CB    . SER F 2 286 ? -11.442 7.363  143.693 1.00 9.93  ? 286 SER C CB    1 
ATOM   6894 O  OG    . SER F 2 286 ? -11.736 8.745  143.782 1.00 9.08  ? 286 SER C OG    1 
ATOM   6895 N  N     . GLY F 2 287 ? -9.631  9.431  144.087 1.00 10.23 ? 287 GLY C N     1 
ATOM   6896 C  CA    . GLY F 2 287 ? -9.122  10.747 144.475 1.00 10.12 ? 287 GLY C CA    1 
ATOM   6897 C  C     . GLY F 2 287 ? -9.188  11.701 143.288 1.00 10.25 ? 287 GLY C C     1 
ATOM   6898 O  O     . GLY F 2 287 ? -9.536  11.299 142.169 1.00 11.78 ? 287 GLY C O     1 
ATOM   6899 N  N     . ILE F 2 288 ? -8.867  12.936 143.602 1.00 9.32  ? 288 ILE C N     1 
ATOM   6900 C  CA    . ILE F 2 288 ? -8.790  14.031 142.629 1.00 9.17  ? 288 ILE C CA    1 
ATOM   6901 C  C     . ILE F 2 288 ? -7.313  14.245 142.331 1.00 9.80  ? 288 ILE C C     1 
ATOM   6902 O  O     . ILE F 2 288 ? -6.581  14.848 143.126 1.00 9.90  ? 288 ILE C O     1 
ATOM   6903 C  CB    . ILE F 2 288 ? -9.393  15.300 143.239 1.00 8.10  ? 288 ILE C CB    1 
ATOM   6904 C  CG1   . ILE F 2 288 ? -10.904 15.202 143.465 1.00 5.96  ? 288 ILE C CG1   1 
ATOM   6905 C  CG2   . ILE F 2 288 ? -9.183  16.542 142.372 1.00 6.88  ? 288 ILE C CG2   1 
ATOM   6906 C  CD1   . ILE F 2 288 ? -11.330 15.640 144.869 1.00 4.32  ? 288 ILE C CD1   1 
ATOM   6907 N  N     . VAL F 2 289 ? -6.875  13.746 141.192 1.00 10.31 ? 289 VAL C N     1 
ATOM   6908 C  CA    . VAL F 2 289 ? -5.447  13.793 140.876 1.00 10.29 ? 289 VAL C CA    1 
ATOM   6909 C  C     . VAL F 2 289 ? -5.058  14.934 139.965 1.00 11.62 ? 289 VAL C C     1 
ATOM   6910 O  O     . VAL F 2 289 ? -3.857  15.051 139.682 1.00 14.53 ? 289 VAL C O     1 
ATOM   6911 C  CB    . VAL F 2 289 ? -4.970  12.467 140.279 1.00 7.91  ? 289 VAL C CB    1 
ATOM   6912 C  CG1   . VAL F 2 289 ? -5.396  11.254 141.113 1.00 6.45  ? 289 VAL C CG1   1 
ATOM   6913 C  CG2   . VAL F 2 289 ? -5.487  12.211 138.868 1.00 7.13  ? 289 VAL C CG2   1 
ATOM   6914 N  N     . GLY F 2 290 ? -5.992  15.745 139.544 1.00 11.44 ? 290 GLY C N     1 
ATOM   6915 C  CA    . GLY F 2 290 ? -5.731  16.898 138.679 1.00 11.34 ? 290 GLY C CA    1 
ATOM   6916 C  C     . GLY F 2 290 ? -7.048  17.536 138.234 1.00 11.37 ? 290 GLY C C     1 
ATOM   6917 O  O     . GLY F 2 290 ? -8.125  17.000 138.537 1.00 10.94 ? 290 GLY C O     1 
ATOM   6918 N  N     . TRP F 2 291 ? -6.929  18.634 137.511 1.00 11.38 ? 291 TRP C N     1 
ATOM   6919 C  CA    . TRP F 2 291 ? -8.127  19.357 136.992 1.00 10.87 ? 291 TRP C CA    1 
ATOM   6920 C  C     . TRP F 2 291 ? -7.713  19.974 135.663 1.00 10.67 ? 291 TRP C C     1 
ATOM   6921 O  O     . TRP F 2 291 ? -7.025  21.008 135.558 1.00 10.69 ? 291 TRP C O     1 
ATOM   6922 C  CB    . TRP F 2 291 ? -8.679  20.231 138.117 1.00 9.80  ? 291 TRP C CB    1 
ATOM   6923 C  CG    . TRP F 2 291 ? -10.090 20.619 137.851 1.00 9.26  ? 291 TRP C CG    1 
ATOM   6924 C  CD1   . TRP F 2 291 ? -10.516 21.518 136.914 1.00 8.49  ? 291 TRP C CD1   1 
ATOM   6925 C  CD2   . TRP F 2 291 ? -11.270 20.104 138.477 1.00 9.28  ? 291 TRP C CD2   1 
ATOM   6926 N  NE1   . TRP F 2 291 ? -11.890 21.574 136.921 1.00 9.18  ? 291 TRP C NE1   1 
ATOM   6927 C  CE2   . TRP F 2 291 ? -12.377 20.738 137.875 1.00 8.68  ? 291 TRP C CE2   1 
ATOM   6928 C  CE3   . TRP F 2 291 ? -11.498 19.176 139.492 1.00 9.58  ? 291 TRP C CE3   1 
ATOM   6929 C  CZ2   . TRP F 2 291 ? -13.687 20.469 138.251 1.00 9.28  ? 291 TRP C CZ2   1 
ATOM   6930 C  CZ3   . TRP F 2 291 ? -12.811 18.913 139.866 1.00 10.69 ? 291 TRP C CZ3   1 
ATOM   6931 C  CH2   . TRP F 2 291 ? -13.888 19.535 139.250 1.00 10.76 ? 291 TRP C CH2   1 
ATOM   6932 N  N     . GLY F 2 292 ? -8.077  19.300 134.573 1.00 10.25 ? 292 GLY C N     1 
ATOM   6933 C  CA    . GLY F 2 292 ? -7.735  19.688 133.206 1.00 8.79  ? 292 GLY C CA    1 
ATOM   6934 C  C     . GLY F 2 292 ? -8.536  20.904 132.740 1.00 8.89  ? 292 GLY C C     1 
ATOM   6935 O  O     . GLY F 2 292 ? -9.408  21.422 133.463 1.00 9.28  ? 292 GLY C O     1 
ATOM   6936 N  N     . ASN F 2 293 ? -8.250  21.342 131.503 1.00 8.47  ? 293 ASN C N     1 
ATOM   6937 C  CA    . ASN F 2 293 ? -8.960  22.493 130.951 1.00 8.51  ? 293 ASN C CA    1 
ATOM   6938 C  C     . ASN F 2 293 ? -10.162 22.168 130.077 1.00 9.35  ? 293 ASN C C     1 
ATOM   6939 O  O     . ASN F 2 293 ? -10.181 22.474 128.876 1.00 10.30 ? 293 ASN C O     1 
ATOM   6940 C  CB    . ASN F 2 293 ? -7.997  23.454 130.279 1.00 8.90  ? 293 ASN C CB    1 
ATOM   6941 C  CG    . ASN F 2 293 ? -6.722  23.684 131.062 1.00 11.16 ? 293 ASN C CG    1 
ATOM   6942 O  OD1   . ASN F 2 293 ? -6.750  24.142 132.206 1.00 14.45 ? 293 ASN C OD1   1 
ATOM   6943 N  ND2   . ASN F 2 293 ? -5.573  23.378 130.448 1.00 13.40 ? 293 ASN C ND2   1 
ATOM   6944 N  N     . MET F 2 294 ? -11.198 21.614 130.667 1.00 9.28  ? 294 MET C N     1 
ATOM   6945 C  CA    . MET F 2 294 ? -12.437 21.292 129.966 1.00 8.76  ? 294 MET C CA    1 
ATOM   6946 C  C     . MET F 2 294 ? -13.595 21.836 130.820 1.00 8.84  ? 294 MET C C     1 
ATOM   6947 O  O     . MET F 2 294 ? -13.577 21.750 132.060 1.00 9.33  ? 294 MET C O     1 
ATOM   6948 C  CB    . MET F 2 294 ? -12.618 19.795 129.788 1.00 8.91  ? 294 MET C CB    1 
ATOM   6949 C  CG    . MET F 2 294 ? -11.523 19.046 129.136 1.00 8.89  ? 294 MET C CG    1 
ATOM   6950 S  SD    . MET F 2 294 ? -11.492 19.421 127.336 1.00 9.34  ? 294 MET C SD    1 
ATOM   6951 C  CE    . MET F 2 294 ? -11.620 17.775 126.646 1.00 8.94  ? 294 MET C CE    1 
ATOM   6952 N  N     . ASP F 2 295 ? -14.580 22.413 130.133 1.00 8.82  ? 295 ASP C N     1 
ATOM   6953 C  CA    . ASP F 2 295 ? -15.766 22.892 130.899 1.00 8.82  ? 295 ASP C CA    1 
ATOM   6954 C  C     . ASP F 2 295 ? -16.413 21.583 131.402 1.00 8.87  ? 295 ASP C C     1 
ATOM   6955 O  O     . ASP F 2 295 ? -16.396 20.556 130.690 1.00 9.81  ? 295 ASP C O     1 
ATOM   6956 C  CB    . ASP F 2 295 ? -16.707 23.727 130.078 1.00 10.36 ? 295 ASP C CB    1 
ATOM   6957 C  CG    . ASP F 2 295 ? -16.313 25.194 130.071 1.00 12.74 ? 295 ASP C CG    1 
ATOM   6958 O  OD1   . ASP F 2 295 ? -15.330 25.502 130.779 1.00 10.16 ? 295 ASP C OD1   1 
ATOM   6959 O  OD2   . ASP F 2 295 ? -16.993 25.965 129.363 1.00 15.95 ? 295 ASP C OD2   1 
ATOM   6960 N  N     . THR F 2 296 ? -16.907 21.649 132.633 1.00 8.52  ? 296 THR C N     1 
ATOM   6961 C  CA    . THR F 2 296 ? -17.550 20.406 133.133 1.00 7.70  ? 296 THR C CA    1 
ATOM   6962 C  C     . THR F 2 296 ? -18.998 20.451 132.644 1.00 8.82  ? 296 THR C C     1 
ATOM   6963 O  O     . THR F 2 296 ? -19.635 21.516 132.545 1.00 8.31  ? 296 THR C O     1 
ATOM   6964 C  CB    . THR F 2 296 ? -17.393 20.217 134.674 1.00 3.99  ? 296 THR C CB    1 
ATOM   6965 O  OG1   . THR F 2 296 ? -18.777 20.274 135.185 1.00 4.17  ? 296 THR C OG1   1 
ATOM   6966 C  CG2   . THR F 2 296 ? -16.453 21.242 135.311 1.00 3.81  ? 296 THR C CG2   1 
ATOM   6967 N  N     . ILE F 2 297 ? -19.447 19.242 132.325 1.00 8.90  ? 297 ILE C N     1 
ATOM   6968 C  CA    . ILE F 2 297 ? -20.814 19.058 131.821 1.00 8.98  ? 297 ILE C CA    1 
ATOM   6969 C  C     . ILE F 2 297 ? -21.690 18.714 133.025 1.00 9.23  ? 297 ILE C C     1 
ATOM   6970 O  O     . ILE F 2 297 ? -21.247 17.855 133.824 1.00 10.19 ? 297 ILE C O     1 
ATOM   6971 C  CB    . ILE F 2 297 ? -20.840 17.915 130.741 1.00 9.26  ? 297 ILE C CB    1 
ATOM   6972 C  CG1   . ILE F 2 297 ? -19.923 18.245 129.549 1.00 8.75  ? 297 ILE C CG1   1 
ATOM   6973 C  CG2   . ILE F 2 297 ? -22.297 17.561 130.308 1.00 10.17 ? 297 ILE C CG2   1 
ATOM   6974 C  CD1   . ILE F 2 297 ? -19.722 17.141 128.483 1.00 8.82  ? 297 ILE C CD1   1 
ATOM   6975 N  N     . VAL F 2 298 ? -22.840 19.345 133.110 1.00 8.77  ? 298 VAL C N     1 
ATOM   6976 C  CA    . VAL F 2 298 ? -23.780 19.069 134.209 1.00 8.12  ? 298 VAL C CA    1 
ATOM   6977 C  C     . VAL F 2 298 ? -25.070 18.505 133.625 1.00 8.12  ? 298 VAL C C     1 
ATOM   6978 O  O     . VAL F 2 298 ? -25.662 19.150 132.730 1.00 8.12  ? 298 VAL C O     1 
ATOM   6979 C  CB    . VAL F 2 298 ? -24.037 20.335 135.040 1.00 7.12  ? 298 VAL C CB    1 
ATOM   6980 C  CG1   . VAL F 2 298 ? -25.028 20.076 136.175 1.00 4.82  ? 298 VAL C CG1   1 
ATOM   6981 C  CG2   . VAL F 2 298 ? -22.751 20.951 135.568 1.00 6.87  ? 298 VAL C CG2   1 
ATOM   6982 N  N     . ILE F 2 299 ? -25.483 17.371 134.116 1.00 7.61  ? 299 ILE C N     1 
ATOM   6983 C  CA    . ILE F 2 299 ? -26.717 16.720 133.648 1.00 7.79  ? 299 ILE C CA    1 
ATOM   6984 C  C     . ILE F 2 299 ? -27.599 16.544 134.879 1.00 8.19  ? 299 ILE C C     1 
ATOM   6985 O  O     . ILE F 2 299 ? -27.083 16.086 135.914 1.00 8.15  ? 299 ILE C O     1 
ATOM   6986 C  CB    . ILE F 2 299 ? -26.387 15.355 132.976 1.00 7.58  ? 299 ILE C CB    1 
ATOM   6987 C  CG1   . ILE F 2 299 ? -25.377 15.554 131.824 1.00 7.72  ? 299 ILE C CG1   1 
ATOM   6988 C  CG2   . ILE F 2 299 ? -27.679 14.614 132.558 1.00 8.84  ? 299 ILE C CG2   1 
ATOM   6989 C  CD1   . ILE F 2 299 ? -24.638 14.225 131.482 1.00 4.81  ? 299 ILE C CD1   1 
ATOM   6990 N  N     . ARG F 2 300 ? -28.849 16.914 134.774 1.00 8.35  ? 300 ARG C N     1 
ATOM   6991 C  CA    . ARG F 2 300 ? -29.720 16.740 135.952 1.00 8.82  ? 300 ARG C CA    1 
ATOM   6992 C  C     . ARG F 2 300 ? -30.846 15.820 135.532 1.00 9.27  ? 300 ARG C C     1 
ATOM   6993 O  O     . ARG F 2 300 ? -31.590 16.185 134.598 1.00 9.64  ? 300 ARG C O     1 
ATOM   6994 C  CB    . ARG F 2 300 ? -30.242 18.054 136.493 1.00 8.28  ? 300 ARG C CB    1 
ATOM   6995 C  CG    . ARG F 2 300 ? -31.389 17.882 137.499 1.00 10.78 ? 300 ARG C CG    1 
ATOM   6996 C  CD    . ARG F 2 300 ? -32.140 19.177 137.588 1.00 13.45 ? 300 ARG C CD    1 
ATOM   6997 N  NE    . ARG F 2 300 ? -32.910 19.404 136.357 1.00 16.46 ? 300 ARG C NE    1 
ATOM   6998 C  CZ    . ARG F 2 300 ? -33.618 20.530 136.211 1.00 18.04 ? 300 ARG C CZ    1 
ATOM   6999 N  NH1   . ARG F 2 300 ? -33.598 21.488 137.152 1.00 17.05 ? 300 ARG C NH1   1 
ATOM   7000 N  NH2   . ARG F 2 300 ? -34.368 20.778 135.139 1.00 18.65 ? 300 ARG C NH2   1 
ATOM   7001 N  N     . VAL F 2 301 ? -30.927 14.649 136.122 1.00 9.28  ? 301 VAL C N     1 
ATOM   7002 C  CA    . VAL F 2 301 ? -32.054 13.776 135.731 1.00 9.47  ? 301 VAL C CA    1 
ATOM   7003 C  C     . VAL F 2 301 ? -33.126 14.116 136.768 1.00 11.26 ? 301 VAL C C     1 
ATOM   7004 O  O     . VAL F 2 301 ? -32.811 14.320 137.949 1.00 14.01 ? 301 VAL C O     1 
ATOM   7005 C  CB    . VAL F 2 301 ? -31.715 12.308 135.601 1.00 6.69  ? 301 VAL C CB    1 
ATOM   7006 C  CG1   . VAL F 2 301 ? -32.975 11.464 135.308 1.00 5.03  ? 301 VAL C CG1   1 
ATOM   7007 C  CG2   . VAL F 2 301 ? -30.612 12.056 134.586 1.00 4.44  ? 301 VAL C CG2   1 
ATOM   7008 N  N     . SER F 2 302 ? -34.347 14.193 136.311 1.00 10.99 ? 302 SER C N     1 
ATOM   7009 C  CA    . SER F 2 302 ? -35.468 14.510 137.208 1.00 9.46  ? 302 SER C CA    1 
ATOM   7010 C  C     . SER F 2 302 ? -36.653 13.581 137.013 1.00 8.90  ? 302 SER C C     1 
ATOM   7011 O  O     . SER F 2 302 ? -37.437 13.727 136.063 1.00 8.84  ? 302 SER C O     1 
ATOM   7012 C  CB    . SER F 2 302 ? -35.873 15.965 136.994 1.00 10.20 ? 302 SER C CB    1 
ATOM   7013 O  OG    . SER F 2 302 ? -35.942 16.533 138.287 1.00 13.61 ? 302 SER C OG    1 
ATOM   7014 N  N     . ALA F 2 303 ? -36.750 12.651 137.936 1.00 8.27  ? 303 ALA C N     1 
ATOM   7015 C  CA    . ALA F 2 303 ? -37.809 11.646 137.940 1.00 8.39  ? 303 ALA C CA    1 
ATOM   7016 C  C     . ALA F 2 303 ? -38.851 11.899 139.021 1.00 9.27  ? 303 ALA C C     1 
ATOM   7017 O  O     . ALA F 2 303 ? -38.545 11.843 140.223 1.00 9.73  ? 303 ALA C O     1 
ATOM   7018 C  CB    . ALA F 2 303 ? -37.187 10.269 138.183 1.00 7.76  ? 303 ALA C CB    1 
ATOM   7019 N  N     . PRO F 2 304 ? -40.098 12.201 138.628 1.00 9.66  ? 304 PRO C N     1 
ATOM   7020 C  CA    . PRO F 2 304 ? -41.183 12.391 139.582 1.00 10.12 ? 304 PRO C CA    1 
ATOM   7021 C  C     . PRO F 2 304 ? -41.440 11.088 140.314 1.00 11.64 ? 304 PRO C C     1 
ATOM   7022 O  O     . PRO F 2 304 ? -40.827 10.037 139.953 1.00 11.65 ? 304 PRO C O     1 
ATOM   7023 C  CB    . PRO F 2 304 ? -42.353 12.796 138.718 1.00 9.14  ? 304 PRO C CB    1 
ATOM   7024 C  CG    . PRO F 2 304 ? -41.889 12.784 137.268 1.00 9.95  ? 304 PRO C CG    1 
ATOM   7025 C  CD    . PRO F 2 304 ? -40.458 12.357 137.220 1.00 9.42  ? 304 PRO C CD    1 
ATOM   7026 N  N     . THR F 2 305 ? -42.320 11.128 141.312 1.00 13.69 ? 305 THR C N     1 
ATOM   7027 C  CA    . THR F 2 305 ? -42.630 9.918  142.106 1.00 15.59 ? 305 THR C CA    1 
ATOM   7028 C  C     . THR F 2 305 ? -43.445 8.935  141.271 1.00 16.58 ? 305 THR C C     1 
ATOM   7029 O  O     . THR F 2 305 ? -44.371 9.331  140.543 1.00 18.91 ? 305 THR C O     1 
ATOM   7030 C  CB    . THR F 2 305 ? -43.397 10.254 143.393 1.00 15.97 ? 305 THR C CB    1 
ATOM   7031 O  OG1   . THR F 2 305 ? -44.702 10.716 143.088 1.00 14.47 ? 305 THR C OG1   1 
ATOM   7032 C  CG2   . THR F 2 305 ? -42.704 11.326 144.236 1.00 16.44 ? 305 THR C CG2   1 
ATOM   7033 N  N     . GLY F 2 306 ? -43.041 7.689  141.418 1.00 15.73 ? 306 GLY C N     1 
ATOM   7034 C  CA    . GLY F 2 306 ? -43.646 6.556  140.719 1.00 14.36 ? 306 GLY C CA    1 
ATOM   7035 C  C     . GLY F 2 306 ? -42.951 6.329  139.371 1.00 13.57 ? 306 GLY C C     1 
ATOM   7036 O  O     . GLY F 2 306 ? -43.433 5.567  138.526 1.00 14.31 ? 306 GLY C O     1 
ATOM   7037 N  N     . ALA F 2 307 ? -41.825 6.997  139.189 1.00 12.15 ? 307 ALA C N     1 
ATOM   7038 C  CA    . ALA F 2 307 ? -41.041 6.880  137.944 1.00 11.65 ? 307 ALA C CA    1 
ATOM   7039 C  C     . ALA F 2 307 ? -40.133 5.653  138.019 1.00 12.02 ? 307 ALA C C     1 
ATOM   7040 O  O     . ALA F 2 307 ? -39.665 5.248  139.112 1.00 13.09 ? 307 ALA C O     1 
ATOM   7041 C  CB    . ALA F 2 307 ? -40.184 8.132  137.742 1.00 8.56  ? 307 ALA C CB    1 
ATOM   7042 N  N     . VAL F 2 308 ? -39.901 5.036  136.864 1.00 10.96 ? 308 VAL C N     1 
ATOM   7043 C  CA    . VAL F 2 308 ? -38.933 3.895  136.824 1.00 9.86  ? 308 VAL C CA    1 
ATOM   7044 C  C     . VAL F 2 308 ? -37.928 4.283  135.736 1.00 10.50 ? 308 VAL C C     1 
ATOM   7045 O  O     . VAL F 2 308 ? -38.097 3.958  134.554 1.00 10.89 ? 308 VAL C O     1 
ATOM   7046 C  CB    . VAL F 2 308 ? -39.638 2.571  136.725 1.00 8.04  ? 308 VAL C CB    1 
ATOM   7047 C  CG1   . VAL F 2 308 ? -38.801 1.405  137.245 1.00 8.44  ? 308 VAL C CG1   1 
ATOM   7048 C  CG2   . VAL F 2 308 ? -40.975 2.650  137.449 1.00 6.62  ? 308 VAL C CG2   1 
ATOM   7049 N  N     . ASN F 2 309 ? -36.945 5.071  136.196 1.00 10.17 ? 309 ASN C N     1 
ATOM   7050 C  CA    . ASN F 2 309 ? -35.924 5.584  135.298 1.00 9.70  ? 309 ASN C CA    1 
ATOM   7051 C  C     . ASN F 2 309 ? -34.563 4.906  135.551 1.00 9.66  ? 309 ASN C C     1 
ATOM   7052 O  O     . ASN F 2 309 ? -33.946 5.121  136.602 1.00 9.94  ? 309 ASN C O     1 
ATOM   7053 C  CB    . ASN F 2 309 ? -35.735 7.087  135.399 1.00 8.98  ? 309 ASN C CB    1 
ATOM   7054 C  CG    . ASN F 2 309 ? -36.893 7.998  135.189 1.00 9.41  ? 309 ASN C CG    1 
ATOM   7055 O  OD1   . ASN F 2 309 ? -37.967 7.553  134.746 1.00 6.62  ? 309 ASN C OD1   1 
ATOM   7056 N  ND2   . ASN F 2 309 ? -36.711 9.294  135.494 1.00 9.49  ? 309 ASN C ND2   1 
ATOM   7057 N  N     . SER F 2 310 ? -34.135 4.216  134.522 1.00 9.55  ? 310 SER C N     1 
ATOM   7058 C  CA    . SER F 2 310 ? -32.815 3.558  134.554 1.00 9.94  ? 310 SER C CA    1 
ATOM   7059 C  C     . SER F 2 310 ? -32.208 3.768  133.176 1.00 10.29 ? 310 SER C C     1 
ATOM   7060 O  O     . SER F 2 310 ? -32.966 3.771  132.177 1.00 11.35 ? 310 SER C O     1 
ATOM   7061 C  CB    . SER F 2 310 ? -33.059 2.091  134.847 1.00 9.86  ? 310 SER C CB    1 
ATOM   7062 O  OG    . SER F 2 310 ? -34.055 1.673  133.905 1.00 10.97 ? 310 SER C OG    1 
ATOM   7063 N  N     . ALA F 2 311 ? -30.912 3.934  133.124 1.00 10.10 ? 311 ALA C N     1 
ATOM   7064 C  CA    . ALA F 2 311 ? -30.220 4.126  131.833 1.00 10.76 ? 311 ALA C CA    1 
ATOM   7065 C  C     . ALA F 2 311 ? -28.831 3.493  131.909 1.00 10.90 ? 311 ALA C C     1 
ATOM   7066 O  O     . ALA F 2 311 ? -28.390 3.027  132.961 1.00 10.07 ? 311 ALA C O     1 
ATOM   7067 C  CB    . ALA F 2 311 ? -30.166 5.607  131.496 1.00 11.07 ? 311 ALA C CB    1 
ATOM   7068 N  N     . ILE F 2 312 ? -28.204 3.437  130.741 1.00 10.28 ? 312 ILE C N     1 
ATOM   7069 C  CA    . ILE F 2 312 ? -26.834 2.943  130.635 1.00 9.62  ? 312 ILE C CA    1 
ATOM   7070 C  C     . ILE F 2 312 ? -26.009 4.260  130.445 1.00 10.31 ? 312 ILE C C     1 
ATOM   7071 O  O     . ILE F 2 312 ? -26.350 4.989  129.505 1.00 11.68 ? 312 ILE C O     1 
ATOM   7072 C  CB    . ILE F 2 312 ? -26.529 1.934  129.515 1.00 6.63  ? 312 ILE C CB    1 
ATOM   7073 C  CG1   . ILE F 2 312 ? -27.119 0.540  129.757 1.00 8.02  ? 312 ILE C CG1   1 
ATOM   7074 C  CG2   . ILE F 2 312 ? -24.983 1.841  129.279 1.00 6.42  ? 312 ILE C CG2   1 
ATOM   7075 C  CD1   . ILE F 2 312 ? -27.278 -0.346 128.457 1.00 6.43  ? 312 ILE C CD1   1 
ATOM   7076 N  N     . LEU F 2 313 ? -25.097 4.525  131.343 1.00 9.25  ? 313 LEU C N     1 
ATOM   7077 C  CA    . LEU F 2 313 ? -24.265 5.722  131.256 1.00 9.17  ? 313 LEU C CA    1 
ATOM   7078 C  C     . LEU F 2 313 ? -22.926 5.277  130.667 1.00 9.56  ? 313 LEU C C     1 
ATOM   7079 O  O     . LEU F 2 313 ? -22.351 4.282  131.142 1.00 9.65  ? 313 LEU C O     1 
ATOM   7080 C  CB    . LEU F 2 313 ? -24.138 6.409  132.606 1.00 7.49  ? 313 LEU C CB    1 
ATOM   7081 C  CG    . LEU F 2 313 ? -23.705 7.872  132.556 1.00 6.95  ? 313 LEU C CG    1 
ATOM   7082 C  CD1   . LEU F 2 313 ? -24.340 8.644  133.706 1.00 8.50  ? 313 LEU C CD1   1 
ATOM   7083 C  CD2   . LEU F 2 313 ? -22.188 7.919  132.656 1.00 8.93  ? 313 LEU C CD2   1 
ATOM   7084 N  N     . LYS F 2 314 ? -22.495 6.000  129.667 1.00 9.30  ? 314 LYS C N     1 
ATOM   7085 C  CA    . LYS F 2 314 ? -21.215 5.680  128.992 1.00 8.76  ? 314 LYS C CA    1 
ATOM   7086 C  C     . LYS F 2 314 ? -20.471 6.994  128.867 1.00 9.45  ? 314 LYS C C     1 
ATOM   7087 O  O     . LYS F 2 314 ? -21.026 8.006  128.424 1.00 10.49 ? 314 LYS C O     1 
ATOM   7088 C  CB    . LYS F 2 314 ? -21.430 5.169  127.581 1.00 7.02  ? 314 LYS C CB    1 
ATOM   7089 C  CG    . LYS F 2 314 ? -20.833 3.784  127.347 1.00 6.34  ? 314 LYS C CG    1 
ATOM   7090 C  CD    . LYS F 2 314 ? -21.761 2.869  126.549 1.00 8.25  ? 314 LYS C CD    1 
ATOM   7091 C  CE    . LYS F 2 314 ? -21.399 1.391  126.685 1.00 9.77  ? 314 LYS C CE    1 
ATOM   7092 N  NZ    . LYS F 2 314 ? -20.138 1.046  126.014 1.00 11.13 ? 314 LYS C NZ    1 
ATOM   7093 N  N     . THR F 2 315 ? -19.236 7.017  129.269 1.00 9.31  ? 315 THR C N     1 
ATOM   7094 C  CA    . THR F 2 315 ? -18.467 8.246  129.131 1.00 9.40  ? 315 THR C CA    1 
ATOM   7095 C  C     . THR F 2 315 ? -17.073 7.907  128.624 1.00 9.93  ? 315 THR C C     1 
ATOM   7096 O  O     . THR F 2 315 ? -16.470 6.900  129.033 1.00 9.55  ? 315 THR C O     1 
ATOM   7097 C  CB    . THR F 2 315 ? -18.466 9.031  130.450 1.00 9.47  ? 315 THR C CB    1 
ATOM   7098 O  OG1   . THR F 2 315 ? -17.203 9.640  130.664 1.00 9.17  ? 315 THR C OG1   1 
ATOM   7099 C  CG2   . THR F 2 315 ? -18.783 8.173  131.673 1.00 8.76  ? 315 THR C CG2   1 
ATOM   7100 N  N     . TRP F 2 316 ? -16.658 8.772  127.729 1.00 10.62 ? 316 TRP C N     1 
ATOM   7101 C  CA    . TRP F 2 316 ? -15.367 8.704  127.054 1.00 10.71 ? 316 TRP C CA    1 
ATOM   7102 C  C     . TRP F 2 316 ? -14.581 9.991  127.324 1.00 11.18 ? 316 TRP C C     1 
ATOM   7103 O  O     . TRP F 2 316 ? -15.143 11.109 127.349 1.00 12.54 ? 316 TRP C O     1 
ATOM   7104 C  CB    . TRP F 2 316 ? -15.579 8.629  125.521 1.00 11.94 ? 316 TRP C CB    1 
ATOM   7105 C  CG    . TRP F 2 316 ? -16.376 7.406  124.997 1.00 12.88 ? 316 TRP C CG    1 
ATOM   7106 C  CD1   . TRP F 2 316 ? -15.878 6.214  124.627 1.00 12.69 ? 316 TRP C CD1   1 
ATOM   7107 C  CD2   . TRP F 2 316 ? -17.793 7.348  124.801 1.00 12.73 ? 316 TRP C CD2   1 
ATOM   7108 N  NE1   . TRP F 2 316 ? -16.976 5.408  124.177 1.00 13.59 ? 316 TRP C NE1   1 
ATOM   7109 C  CE2   . TRP F 2 316 ? -18.086 6.092  124.280 1.00 12.77 ? 316 TRP C CE2   1 
ATOM   7110 C  CE3   . TRP F 2 316 ? -18.839 8.254  125.015 1.00 11.23 ? 316 TRP C CE3   1 
ATOM   7111 C  CZ2   . TRP F 2 316 ? -19.385 5.685  123.937 1.00 11.99 ? 316 TRP C CZ2   1 
ATOM   7112 C  CZ3   . TRP F 2 316 ? -20.144 7.831  124.678 1.00 10.57 ? 316 TRP C CZ3   1 
ATOM   7113 C  CH2   . TRP F 2 316 ? -20.402 6.608  124.163 1.00 11.21 ? 316 TRP C CH2   1 
ATOM   7114 N  N     . ALA F 2 317 ? -13.300 9.787  127.509 1.00 11.17 ? 317 ALA C N     1 
ATOM   7115 C  CA    . ALA F 2 317 ? -12.349 10.874 127.727 1.00 11.22 ? 317 ALA C CA    1 
ATOM   7116 C  C     . ALA F 2 317 ? -11.002 10.315 127.226 1.00 12.29 ? 317 ALA C C     1 
ATOM   7117 O  O     . ALA F 2 317 ? -10.600 9.255  127.694 1.00 12.88 ? 317 ALA C O     1 
ATOM   7118 C  CB    . ALA F 2 317 ? -12.200 11.311 129.141 1.00 9.33  ? 317 ALA C CB    1 
ATOM   7119 N  N     . CYS F 2 318 ? -10.448 11.073 126.322 1.00 12.33 ? 318 CYS C N     1 
ATOM   7120 C  CA    . CYS F 2 318 ? -9.133  10.776 125.733 1.00 11.36 ? 318 CYS C CA    1 
ATOM   7121 C  C     . CYS F 2 318 ? -8.118  11.760 126.335 1.00 10.27 ? 318 CYS C C     1 
ATOM   7122 O  O     . CYS F 2 318 ? -8.243  12.983 126.176 1.00 8.03  ? 318 CYS C O     1 
ATOM   7123 C  CB    . CYS F 2 318 ? -9.219  10.899 124.214 1.00 13.20 ? 318 CYS C CB    1 
ATOM   7124 S  SG    . CYS F 2 318 ? -7.721  10.222 123.344 1.00 20.72 ? 318 CYS C SG    1 
ATOM   7125 N  N     . LEU F 2 319 ? -7.150  11.193 127.044 1.00 10.93 ? 319 LEU C N     1 
ATOM   7126 C  CA    . LEU F 2 319 ? -6.061  11.966 127.673 1.00 11.59 ? 319 LEU C CA    1 
ATOM   7127 C  C     . LEU F 2 319 ? -4.717  11.649 127.023 1.00 13.17 ? 319 LEU C C     1 
ATOM   7128 O  O     . LEU F 2 319 ? -4.502  10.542 126.512 1.00 15.11 ? 319 LEU C O     1 
ATOM   7129 C  CB    . LEU F 2 319 ? -5.806  11.579 129.150 1.00 6.72  ? 319 LEU C CB    1 
ATOM   7130 C  CG    . LEU F 2 319 ? -6.968  11.789 130.131 1.00 3.58  ? 319 LEU C CG    1 
ATOM   7131 C  CD1   . LEU F 2 319 ? -7.086  13.222 130.655 1.00 4.18  ? 319 LEU C CD1   1 
ATOM   7132 C  CD2   . LEU F 2 319 ? -8.326  11.437 129.542 1.00 4.03  ? 319 LEU C CD2   1 
ATOM   7133 N  N     . GLU F 2 320 ? -3.870  12.640 127.079 1.00 13.19 ? 320 GLU C N     1 
ATOM   7134 C  CA    . GLU F 2 320 ? -2.470  12.540 126.669 1.00 12.98 ? 320 GLU C CA    1 
ATOM   7135 C  C     . GLU F 2 320 ? -1.688  12.747 127.973 1.00 14.02 ? 320 GLU C C     1 
ATOM   7136 O  O     . GLU F 2 320 ? -1.855  13.814 128.593 1.00 16.06 ? 320 GLU C O     1 
ATOM   7137 C  CB    . GLU F 2 320 ? -2.156  13.633 125.646 1.00 8.47  ? 320 GLU C CB    1 
ATOM   7138 C  CG    . GLU F 2 320 ? -1.425  13.111 124.408 1.00 7.27  ? 320 GLU C CG    1 
ATOM   7139 C  CD    . GLU F 2 320 ? -0.949  14.233 123.484 1.00 10.00 ? 320 GLU C CD    1 
ATOM   7140 O  OE1   . GLU F 2 320 ? -0.389  15.284 123.982 1.00 12.22 ? 320 GLU C OE1   1 
ATOM   7141 O  OE2   . GLU F 2 320 ? -1.108  14.130 122.208 1.00 9.53  ? 320 GLU C OE2   1 
ATOM   7142 N  N     . TYR F 2 321 ? -0.966  11.745 128.379 1.00 12.96 ? 321 TYR C N     1 
ATOM   7143 C  CA    . TYR F 2 321 ? -0.190  11.725 129.601 1.00 11.85 ? 321 TYR C CA    1 
ATOM   7144 C  C     . TYR F 2 321 ? 1.307   11.745 129.358 1.00 11.52 ? 321 TYR C C     1 
ATOM   7145 O  O     . TYR F 2 321 ? 1.759   11.295 128.307 1.00 12.30 ? 321 TYR C O     1 
ATOM   7146 C  CB    . TYR F 2 321 ? -0.470  10.363 130.289 1.00 11.10 ? 321 TYR C CB    1 
ATOM   7147 C  CG    . TYR F 2 321 ? -1.699  10.321 131.148 1.00 8.37  ? 321 TYR C CG    1 
ATOM   7148 C  CD1   . TYR F 2 321 ? -1.722  10.941 132.393 1.00 7.94  ? 321 TYR C CD1   1 
ATOM   7149 C  CD2   . TYR F 2 321 ? -2.846  9.621  130.718 1.00 8.01  ? 321 TYR C CD2   1 
ATOM   7150 C  CE1   . TYR F 2 321 ? -2.852  10.893 133.205 1.00 9.65  ? 321 TYR C CE1   1 
ATOM   7151 C  CE2   . TYR F 2 321 ? -3.990  9.581  131.515 1.00 9.56  ? 321 TYR C CE2   1 
ATOM   7152 C  CZ    . TYR F 2 321 ? -3.970  10.215 132.757 1.00 10.26 ? 321 TYR C CZ    1 
ATOM   7153 O  OH    . TYR F 2 321 ? -5.048  10.179 133.576 1.00 11.44 ? 321 TYR C OH    1 
ATOM   7154 N  N     . ARG F 2 322 ? 2.032   12.189 130.350 1.00 11.00 ? 322 ARG C N     1 
ATOM   7155 C  CA    . ARG F 2 322 ? 3.517   12.178 130.299 1.00 10.90 ? 322 ARG C CA    1 
ATOM   7156 C  C     . ARG F 2 322 ? 3.896   10.969 131.149 1.00 11.47 ? 322 ARG C C     1 
ATOM   7157 O  O     . ARG F 2 322 ? 3.606   10.952 132.356 1.00 12.78 ? 322 ARG C O     1 
ATOM   7158 C  CB    . ARG F 2 322 ? 4.094   13.491 130.790 1.00 8.61  ? 322 ARG C CB    1 
ATOM   7159 C  CG    . ARG F 2 322 ? 3.791   14.561 129.726 1.00 7.75  ? 322 ARG C CG    1 
ATOM   7160 C  CD    . ARG F 2 322 ? 4.528   14.258 128.435 1.00 6.88  ? 322 ARG C CD    1 
ATOM   7161 N  NE    . ARG F 2 322 ? 5.696   15.121 128.407 1.00 8.71  ? 322 ARG C NE    1 
ATOM   7162 C  CZ    . ARG F 2 322 ? 6.969   14.787 128.457 1.00 9.74  ? 322 ARG C CZ    1 
ATOM   7163 N  NH1   . ARG F 2 322 ? 7.365   13.522 128.329 1.00 11.27 ? 322 ARG C NH1   1 
ATOM   7164 N  NH2   . ARG F 2 322 ? 7.896   15.752 128.572 1.00 10.53 ? 322 ARG C NH2   1 
ATOM   7165 N  N     . PRO F 2 323 ? 4.414   9.952  130.475 1.00 10.89 ? 323 PRO C N     1 
ATOM   7166 C  CA    . PRO F 2 323 ? 4.784   8.699  131.140 1.00 10.24 ? 323 PRO C CA    1 
ATOM   7167 C  C     . PRO F 2 323 ? 6.171   8.794  131.733 1.00 10.19 ? 323 PRO C C     1 
ATOM   7168 O  O     . PRO F 2 323 ? 7.045   9.461  131.159 1.00 10.41 ? 323 PRO C O     1 
ATOM   7169 C  CB    . PRO F 2 323 ? 4.750   7.714  129.979 1.00 10.17 ? 323 PRO C CB    1 
ATOM   7170 C  CG    . PRO F 2 323 ? 5.261   8.512  128.804 1.00 11.14 ? 323 PRO C CG    1 
ATOM   7171 C  CD    . PRO F 2 323 ? 4.734   9.924  129.033 1.00 11.13 ? 323 PRO C CD    1 
ATOM   7172 N  N     . ASN F 2 324 ? 6.348   8.139  132.838 1.00 9.89  ? 324 ASN C N     1 
ATOM   7173 C  CA    . ASN F 2 324 ? 7.582   8.027  133.592 1.00 9.52  ? 324 ASN C CA    1 
ATOM   7174 C  C     . ASN F 2 324 ? 8.382   6.774  133.179 1.00 8.68  ? 324 ASN C C     1 
ATOM   7175 O  O     . ASN F 2 324 ? 7.844   5.674  133.151 1.00 7.35  ? 324 ASN C O     1 
ATOM   7176 C  CB    . ASN F 2 324 ? 7.225   7.909  135.085 1.00 11.77 ? 324 ASN C CB    1 
ATOM   7177 C  CG    . ASN F 2 324 ? 6.730   9.183  135.739 1.00 13.66 ? 324 ASN C CG    1 
ATOM   7178 O  OD1   . ASN F 2 324 ? 6.796   10.270 135.149 1.00 11.29 ? 324 ASN C OD1   1 
ATOM   7179 N  ND2   . ASN F 2 324 ? 6.254   9.038  136.986 1.00 14.92 ? 324 ASN C ND2   1 
ATOM   7180 N  N     . PRO F 2 325 ? 9.660   6.967  132.937 1.00 8.89  ? 325 PRO C N     1 
ATOM   7181 C  CA    . PRO F 2 325 ? 10.591  5.920  132.550 1.00 9.60  ? 325 PRO C CA    1 
ATOM   7182 C  C     . PRO F 2 325 ? 10.478  4.664  133.392 1.00 10.61 ? 325 PRO C C     1 
ATOM   7183 O  O     . PRO F 2 325 ? 10.809  3.557  132.903 1.00 10.62 ? 325 PRO C O     1 
ATOM   7184 C  CB    . PRO F 2 325 ? 11.972  6.582  132.813 1.00 9.38  ? 325 PRO C CB    1 
ATOM   7185 C  CG    . PRO F 2 325 ? 11.733  8.011  132.381 1.00 8.96  ? 325 PRO C CG    1 
ATOM   7186 C  CD    . PRO F 2 325 ? 10.343  8.292  132.950 1.00 9.05  ? 325 PRO C CD    1 
ATOM   7187 N  N     . ASN F 2 326 ? 10.063  4.859  134.641 1.00 11.22 ? 326 ASN C N     1 
ATOM   7188 C  CA    . ASN F 2 326 ? 9.926   3.733  135.588 1.00 11.20 ? 326 ASN C CA    1 
ATOM   7189 C  C     . ASN F 2 326 ? 8.590   3.010  135.452 1.00 12.08 ? 326 ASN C C     1 
ATOM   7190 O  O     . ASN F 2 326 ? 8.453   1.867  135.938 1.00 13.43 ? 326 ASN C O     1 
ATOM   7191 C  CB    . ASN F 2 326 ? 10.119  4.227  137.032 1.00 8.30  ? 326 ASN C CB    1 
ATOM   7192 C  CG    . ASN F 2 326 ? 9.010   5.189  137.432 1.00 8.96  ? 326 ASN C CG    1 
ATOM   7193 O  OD1   . ASN F 2 326 ? 8.953   6.353  136.991 1.00 10.51 ? 326 ASN C OD1   1 
ATOM   7194 N  ND2   . ASN F 2 326 ? 8.086   4.738  138.268 1.00 6.87  ? 326 ASN C ND2   1 
ATOM   7195 N  N     . ALA F 2 327 ? 7.610   3.660  134.863 1.00 12.05 ? 327 ALA C N     1 
ATOM   7196 C  CA    . ALA F 2 327 ? 6.267   3.067  134.700 1.00 11.82 ? 327 ALA C CA    1 
ATOM   7197 C  C     . ALA F 2 327 ? 6.247   2.123  133.505 1.00 11.37 ? 327 ALA C C     1 
ATOM   7198 O  O     . ALA F 2 327 ? 6.965   2.346  132.521 1.00 11.25 ? 327 ALA C O     1 
ATOM   7199 C  CB    . ALA F 2 327 ? 5.242   4.193  134.540 1.00 11.68 ? 327 ALA C CB    1 
ATOM   7200 N  N     . MET F 2 328 ? 5.411   1.100  133.561 1.00 10.68 ? 328 MET C N     1 
ATOM   7201 C  CA    . MET F 2 328 ? 5.315   0.131  132.477 1.00 10.18 ? 328 MET C CA    1 
ATOM   7202 C  C     . MET F 2 328 ? 4.582   0.708  131.284 1.00 11.27 ? 328 MET C C     1 
ATOM   7203 O  O     . MET F 2 328 ? 4.852   0.269  130.144 1.00 12.22 ? 328 MET C O     1 
ATOM   7204 C  CB    . MET F 2 328 ? 4.704   -1.172 132.965 1.00 7.81  ? 328 MET C CB    1 
ATOM   7205 C  CG    . MET F 2 328 ? 4.115   -1.963 131.812 1.00 8.14  ? 328 MET C CG    1 
ATOM   7206 S  SD    . MET F 2 328 ? 2.323   -1.541 131.714 1.00 13.08 ? 328 MET C SD    1 
ATOM   7207 C  CE    . MET F 2 328 ? 1.716   -3.159 131.148 1.00 11.45 ? 328 MET C CE    1 
ATOM   7208 N  N     . LEU F 2 329 ? 3.656   1.627  131.519 1.00 11.48 ? 329 LEU C N     1 
ATOM   7209 C  CA    . LEU F 2 329 ? 2.878   2.246  130.420 1.00 11.44 ? 329 LEU C CA    1 
ATOM   7210 C  C     . LEU F 2 329 ? 3.866   2.959  129.494 1.00 11.30 ? 329 LEU C C     1 
ATOM   7211 O  O     . LEU F 2 329 ? 3.606   3.173  128.309 1.00 12.51 ? 329 LEU C O     1 
ATOM   7212 C  CB    . LEU F 2 329 ? 1.774   3.142  130.953 1.00 12.12 ? 329 LEU C CB    1 
ATOM   7213 C  CG    . LEU F 2 329 ? 2.091   4.192  132.005 1.00 10.95 ? 329 LEU C CG    1 
ATOM   7214 C  CD1   . LEU F 2 329 ? 3.211   5.124  131.581 1.00 10.10 ? 329 LEU C CD1   1 
ATOM   7215 C  CD2   . LEU F 2 329 ? 0.825   5.015  132.291 1.00 11.12 ? 329 LEU C CD2   1 
ATOM   7216 N  N     . TYR F 2 330 ? 5.003   3.291  130.077 1.00 10.92 ? 330 TYR C N     1 
ATOM   7217 C  CA    . TYR F 2 330 ? 6.043   3.967  129.304 1.00 10.83 ? 330 TYR C CA    1 
ATOM   7218 C  C     . TYR F 2 330 ? 6.273   3.214  127.985 1.00 11.03 ? 330 TYR C C     1 
ATOM   7219 O  O     . TYR F 2 330 ? 6.692   3.777  126.969 1.00 12.23 ? 330 TYR C O     1 
ATOM   7220 C  CB    . TYR F 2 330 ? 7.400   3.990  130.042 1.00 10.56 ? 330 TYR C CB    1 
ATOM   7221 C  CG    . TYR F 2 330 ? 8.306   4.981  129.336 1.00 10.51 ? 330 TYR C CG    1 
ATOM   7222 C  CD1   . TYR F 2 330 ? 9.051   4.603  128.236 1.00 11.21 ? 330 TYR C CD1   1 
ATOM   7223 C  CD2   . TYR F 2 330 ? 8.332   6.302  129.766 1.00 10.78 ? 330 TYR C CD2   1 
ATOM   7224 C  CE1   . TYR F 2 330 ? 9.874   5.512  127.559 1.00 11.87 ? 330 TYR C CE1   1 
ATOM   7225 C  CE2   . TYR F 2 330 ? 9.137   7.225  129.108 1.00 11.02 ? 330 TYR C CE2   1 
ATOM   7226 C  CZ    . TYR F 2 330 ? 9.894   6.824  128.016 1.00 11.25 ? 330 TYR C CZ    1 
ATOM   7227 O  OH    . TYR F 2 330 ? 10.688  7.720  127.359 1.00 12.92 ? 330 TYR C OH    1 
ATOM   7228 N  N     . GLN F 2 331 ? 6.022   1.929  128.100 1.00 11.22 ? 331 GLN C N     1 
ATOM   7229 C  CA    . GLN F 2 331 ? 6.195   1.003  126.990 1.00 11.69 ? 331 GLN C CA    1 
ATOM   7230 C  C     . GLN F 2 331 ? 5.369   1.462  125.800 1.00 12.37 ? 331 GLN C C     1 
ATOM   7231 O  O     . GLN F 2 331 ? 5.935   1.471  124.713 1.00 12.99 ? 331 GLN C O     1 
ATOM   7232 C  CB    . GLN F 2 331 ? 5.864   -0.457 127.320 1.00 11.58 ? 331 GLN C CB    1 
ATOM   7233 C  CG    . GLN F 2 331 ? 5.861   -1.354 126.094 1.00 12.21 ? 331 GLN C CG    1 
ATOM   7234 C  CD    . GLN F 2 331 ? 5.658   -2.816 126.417 1.00 13.56 ? 331 GLN C CD    1 
ATOM   7235 O  OE1   . GLN F 2 331 ? 5.066   -3.571 125.625 1.00 14.58 ? 331 GLN C OE1   1 
ATOM   7236 N  NE2   . GLN F 2 331 ? 6.143   -3.239 127.577 1.00 13.83 ? 331 GLN C NE2   1 
ATOM   7237 N  N     . PHE F 2 332 ? 4.136   1.808  126.039 1.00 13.23 ? 332 PHE C N     1 
ATOM   7238 C  CA    . PHE F 2 332 ? 3.162   2.197  125.010 1.00 14.62 ? 332 PHE C CA    1 
ATOM   7239 C  C     . PHE F 2 332 ? 3.229   3.629  124.532 1.00 15.22 ? 332 PHE C C     1 
ATOM   7240 O  O     . PHE F 2 332 ? 2.407   4.054  123.691 1.00 17.06 ? 332 PHE C O     1 
ATOM   7241 C  CB    . PHE F 2 332 ? 1.733   1.798  125.494 1.00 15.60 ? 332 PHE C CB    1 
ATOM   7242 C  CG    . PHE F 2 332 ? 1.740   0.433  126.119 1.00 17.59 ? 332 PHE C CG    1 
ATOM   7243 C  CD1   . PHE F 2 332 ? 2.057   -0.680 125.353 1.00 16.76 ? 332 PHE C CD1   1 
ATOM   7244 C  CD2   . PHE F 2 332 ? 1.495   0.301  127.480 1.00 19.00 ? 332 PHE C CD2   1 
ATOM   7245 C  CE1   . PHE F 2 332 ? 2.115   -1.952 125.917 1.00 16.39 ? 332 PHE C CE1   1 
ATOM   7246 C  CE2   . PHE F 2 332 ? 1.537   -0.960 128.077 1.00 19.34 ? 332 PHE C CE2   1 
ATOM   7247 C  CZ    . PHE F 2 332 ? 1.849   -2.079 127.291 1.00 18.36 ? 332 PHE C CZ    1 
ATOM   7248 N  N     . GLY F 2 333 ? 4.201   4.359  125.029 1.00 14.43 ? 333 GLY C N     1 
ATOM   7249 C  CA    . GLY F 2 333 ? 4.381   5.760  124.660 1.00 13.54 ? 333 GLY C CA    1 
ATOM   7250 C  C     . GLY F 2 333 ? 4.743   5.940  123.189 1.00 12.23 ? 333 GLY C C     1 
ATOM   7251 O  O     . GLY F 2 333 ? 5.377   5.082  122.573 1.00 13.47 ? 333 GLY C O     1 
ATOM   7252 N  N     . HIS F 2 334 ? 4.332   7.082  122.690 1.00 10.32 ? 334 HIS C N     1 
ATOM   7253 C  CA    . HIS F 2 334 ? 4.538   7.558  121.322 1.00 8.34  ? 334 HIS C CA    1 
ATOM   7254 C  C     . HIS F 2 334 ? 4.699   9.074  121.333 1.00 7.69  ? 334 HIS C C     1 
ATOM   7255 O  O     . HIS F 2 334 ? 4.608   9.680  122.423 1.00 6.49  ? 334 HIS C O     1 
ATOM   7256 C  CB    . HIS F 2 334 ? 3.393   7.132  120.409 1.00 7.60  ? 334 HIS C CB    1 
ATOM   7257 C  CG    . HIS F 2 334 ? 2.056   7.725  120.677 1.00 4.82  ? 334 HIS C CG    1 
ATOM   7258 N  ND1   . HIS F 2 334 ? 1.611   8.891  120.089 1.00 5.62  ? 334 HIS C ND1   1 
ATOM   7259 C  CD2   . HIS F 2 334 ? 1.001   7.289  121.385 1.00 5.76  ? 334 HIS C CD2   1 
ATOM   7260 C  CE1   . HIS F 2 334 ? 0.370   9.180  120.465 1.00 6.04  ? 334 HIS C CE1   1 
ATOM   7261 N  NE2   . HIS F 2 334 ? -0.018  8.207  121.243 1.00 7.25  ? 334 HIS C NE2   1 
ATOM   7262 N  N     . ASP F 2 335 ? 4.964   9.704  120.207 1.00 7.91  ? 335 ASP C N     1 
ATOM   7263 C  CA    . ASP F 2 335 ? 5.128   11.172 120.201 1.00 9.47  ? 335 ASP C CA    1 
ATOM   7264 C  C     . ASP F 2 335 ? 3.749   11.780 119.903 1.00 10.00 ? 335 ASP C C     1 
ATOM   7265 O  O     . ASP F 2 335 ? 3.050   11.195 119.064 1.00 11.08 ? 335 ASP C O     1 
ATOM   7266 C  CB    . ASP F 2 335 ? 6.128   11.666 119.179 1.00 14.07 ? 335 ASP C CB    1 
ATOM   7267 C  CG    . ASP F 2 335 ? 7.563   11.236 119.265 1.00 19.30 ? 335 ASP C CG    1 
ATOM   7268 O  OD1   . ASP F 2 335 ? 8.106   11.296 120.397 1.00 21.22 ? 335 ASP C OD1   1 
ATOM   7269 O  OD2   . ASP F 2 335 ? 8.250   10.860 118.280 1.00 21.44 ? 335 ASP C OD2   1 
ATOM   7270 N  N     . SER F 2 336 ? 3.472   12.905 120.518 1.00 10.24 ? 336 SER C N     1 
ATOM   7271 C  CA    . SER F 2 336 ? 2.193   13.606 120.223 1.00 9.44  ? 336 SER C CA    1 
ATOM   7272 C  C     . SER F 2 336 ? 2.324   13.997 118.744 1.00 8.89  ? 336 SER C C     1 
ATOM   7273 O  O     . SER F 2 336 ? 3.437   14.374 118.313 1.00 9.56  ? 336 SER C O     1 
ATOM   7274 C  CB    . SER F 2 336 ? 2.022   14.812 121.105 1.00 10.66 ? 336 SER C CB    1 
ATOM   7275 O  OG    . SER F 2 336 ? 1.139   15.763 120.543 1.00 12.86 ? 336 SER C OG    1 
ATOM   7276 N  N     . PRO F 2 337 ? 1.246   13.854 117.999 1.00 7.89  ? 337 PRO C N     1 
ATOM   7277 C  CA    . PRO F 2 337 ? 1.252   14.203 116.574 1.00 7.24  ? 337 PRO C CA    1 
ATOM   7278 C  C     . PRO F 2 337 ? 1.586   15.687 116.406 1.00 7.55  ? 337 PRO C C     1 
ATOM   7279 O  O     . PRO F 2 337 ? 1.353   16.519 117.299 1.00 6.94  ? 337 PRO C O     1 
ATOM   7280 C  CB    . PRO F 2 337 ? -0.138  13.862 116.082 1.00 7.51  ? 337 PRO C CB    1 
ATOM   7281 C  CG    . PRO F 2 337 ? -0.992  13.828 117.313 1.00 7.14  ? 337 PRO C CG    1 
ATOM   7282 C  CD    . PRO F 2 337 ? -0.080  13.404 118.452 1.00 7.57  ? 337 PRO C CD    1 
ATOM   7283 N  N     . PRO F 2 338 ? 2.116   15.987 115.221 1.00 7.99  ? 338 PRO C N     1 
ATOM   7284 C  CA    . PRO F 2 338 ? 2.513   17.330 114.825 1.00 7.98  ? 338 PRO C CA    1 
ATOM   7285 C  C     . PRO F 2 338 ? 1.362   18.266 114.503 1.00 8.41  ? 338 PRO C C     1 
ATOM   7286 O  O     . PRO F 2 338 ? 0.247   17.824 114.202 1.00 8.02  ? 338 PRO C O     1 
ATOM   7287 C  CB    . PRO F 2 338 ? 3.357   17.140 113.580 1.00 8.02  ? 338 PRO C CB    1 
ATOM   7288 C  CG    . PRO F 2 338 ? 3.219   15.742 113.148 1.00 8.05  ? 338 PRO C CG    1 
ATOM   7289 C  CD    . PRO F 2 338 ? 2.393   15.002 114.156 1.00 8.26  ? 338 PRO C CD    1 
ATOM   7290 N  N     . CYS F 2 339 ? 1.679   19.552 114.550 1.00 9.22  ? 339 CYS C N     1 
ATOM   7291 C  CA    . CYS F 2 339 ? 0.724   20.620 114.282 1.00 9.65  ? 339 CYS C CA    1 
ATOM   7292 C  C     . CYS F 2 339 ? -0.080  20.400 113.000 1.00 9.40  ? 339 CYS C C     1 
ATOM   7293 O  O     . CYS F 2 339 ? 0.437   20.267 111.882 1.00 10.11 ? 339 CYS C O     1 
ATOM   7294 C  CB    . CYS F 2 339 ? 1.386   22.002 114.211 1.00 11.80 ? 339 CYS C CB    1 
ATOM   7295 S  SG    . CYS F 2 339 ? 0.256   23.392 114.525 1.00 17.75 ? 339 CYS C SG    1 
ATOM   7296 N  N     . ASP F 2 340 ? -1.377  20.390 113.203 1.00 9.15  ? 340 ASP C N     1 
ATOM   7297 C  CA    . ASP F 2 340 ? -2.376  20.285 112.137 1.00 9.03  ? 340 ASP C CA    1 
ATOM   7298 C  C     . ASP F 2 340 ? -3.257  21.544 112.350 1.00 9.48  ? 340 ASP C C     1 
ATOM   7299 O  O     . ASP F 2 340 ? -4.268  21.483 113.059 1.00 9.82  ? 340 ASP C O     1 
ATOM   7300 C  CB    . ASP F 2 340 ? -3.140  18.983 112.129 1.00 8.04  ? 340 ASP C CB    1 
ATOM   7301 C  CG    . ASP F 2 340 ? -4.029  18.924 110.885 1.00 9.19  ? 340 ASP C CG    1 
ATOM   7302 O  OD1   . ASP F 2 340 ? -4.150  20.003 110.264 1.00 11.26 ? 340 ASP C OD1   1 
ATOM   7303 O  OD2   . ASP F 2 340 ? -4.555  17.850 110.549 1.00 9.04  ? 340 ASP C OD2   1 
ATOM   7304 N  N     . GLU F 2 341 ? -2.773  22.641 111.777 1.00 10.39 ? 341 GLU C N     1 
ATOM   7305 C  CA    . GLU F 2 341 ? -3.448  23.932 111.895 1.00 10.61 ? 341 GLU C CA    1 
ATOM   7306 C  C     . GLU F 2 341 ? -4.911  23.847 111.460 1.00 10.10 ? 341 GLU C C     1 
ATOM   7307 O  O     . GLU F 2 341 ? -5.782  24.529 112.015 1.00 9.89  ? 341 GLU C O     1 
ATOM   7308 C  CB    . GLU F 2 341 ? -2.740  25.052 111.175 1.00 13.44 ? 341 GLU C CB    1 
ATOM   7309 C  CG    . GLU F 2 341 ? -2.617  26.351 111.990 1.00 20.25 ? 341 GLU C CG    1 
ATOM   7310 C  CD    . GLU F 2 341 ? -3.734  27.362 111.700 1.00 25.84 ? 341 GLU C CD    1 
ATOM   7311 O  OE1   . GLU F 2 341 ? -4.944  26.946 111.554 1.00 27.50 ? 341 GLU C OE1   1 
ATOM   7312 O  OE2   . GLU F 2 341 ? -3.472  28.624 111.614 1.00 27.95 ? 341 GLU C OE2   1 
ATOM   7313 N  N     . VAL F 2 342 ? -5.199  23.003 110.491 1.00 9.90  ? 342 VAL C N     1 
ATOM   7314 C  CA    . VAL F 2 342 ? -6.583  22.875 110.007 1.00 9.42  ? 342 VAL C CA    1 
ATOM   7315 C  C     . VAL F 2 342 ? -7.431  22.061 110.997 1.00 8.42  ? 342 VAL C C     1 
ATOM   7316 O  O     . VAL F 2 342 ? -8.611  22.347 111.223 1.00 8.87  ? 342 VAL C O     1 
ATOM   7317 C  CB    . VAL F 2 342 ? -6.629  22.244 108.618 1.00 8.75  ? 342 VAL C CB    1 
ATOM   7318 C  CG1   . VAL F 2 342 ? -8.054  21.897 108.172 1.00 8.64  ? 342 VAL C CG1   1 
ATOM   7319 C  CG2   . VAL F 2 342 ? -6.080  23.177 107.532 1.00 8.57  ? 342 VAL C CG2   1 
ATOM   7320 N  N     . ALA F 2 343 ? -6.835  21.049 111.592 1.00 7.69  ? 343 ALA C N     1 
ATOM   7321 C  CA    . ALA F 2 343 ? -7.550  20.229 112.579 1.00 7.87  ? 343 ALA C CA    1 
ATOM   7322 C  C     . ALA F 2 343 ? -7.894  21.094 113.798 1.00 9.61  ? 343 ALA C C     1 
ATOM   7323 O  O     . ALA F 2 343 ? -8.985  20.979 114.378 1.00 10.62 ? 343 ALA C O     1 
ATOM   7324 C  CB    . ALA F 2 343 ? -6.677  19.055 113.028 1.00 4.02  ? 343 ALA C CB    1 
ATOM   7325 N  N     . LEU F 2 344 ? -6.937  21.946 114.120 1.00 10.23 ? 344 LEU C N     1 
ATOM   7326 C  CA    . LEU F 2 344 ? -6.995  22.837 115.289 1.00 10.19 ? 344 LEU C CA    1 
ATOM   7327 C  C     . LEU F 2 344 ? -8.047  23.955 115.129 1.00 10.33 ? 344 LEU C C     1 
ATOM   7328 O  O     . LEU F 2 344 ? -8.727  24.339 116.087 1.00 10.71 ? 344 LEU C O     1 
ATOM   7329 C  CB    . LEU F 2 344 ? -5.620  23.462 115.530 1.00 8.70  ? 344 LEU C CB    1 
ATOM   7330 C  CG    . LEU F 2 344 ? -4.620  22.465 116.132 1.00 9.88  ? 344 LEU C CG    1 
ATOM   7331 C  CD1   . LEU F 2 344 ? -3.415  23.141 116.788 1.00 8.46  ? 344 LEU C CD1   1 
ATOM   7332 C  CD2   . LEU F 2 344 ? -5.238  21.579 117.218 1.00 8.89  ? 344 LEU C CD2   1 
ATOM   7333 N  N     . GLN F 2 345 ? -8.199  24.500 113.929 1.00 9.70  ? 345 GLN C N     1 
ATOM   7334 C  CA    . GLN F 2 345 ? -9.191  25.583 113.719 1.00 8.95  ? 345 GLN C CA    1 
ATOM   7335 C  C     . GLN F 2 345 ? -10.598 25.002 113.524 1.00 8.31  ? 345 GLN C C     1 
ATOM   7336 O  O     . GLN F 2 345 ? -11.589 25.538 114.042 1.00 8.07  ? 345 GLN C O     1 
ATOM   7337 C  CB    . GLN F 2 345 ? -8.845  26.446 112.505 1.00 11.69 ? 345 GLN C CB    1 
ATOM   7338 C  CG    . GLN F 2 345 ? -9.492  27.840 112.574 1.00 14.13 ? 345 GLN C CG    1 
ATOM   7339 C  CD    . GLN F 2 345 ? -9.015  28.665 113.776 1.00 17.00 ? 345 GLN C CD    1 
ATOM   7340 O  OE1   . GLN F 2 345 ? -9.833  29.187 114.534 1.00 18.92 ? 345 GLN C OE1   1 
ATOM   7341 N  NE2   . GLN F 2 345 ? -7.722  28.817 113.998 1.00 17.43 ? 345 GLN C NE2   1 
ATOM   7342 N  N     . GLU F 2 346 ? -10.652 23.913 112.777 1.00 8.11  ? 346 GLU C N     1 
ATOM   7343 C  CA    . GLU F 2 346 ? -11.915 23.211 112.480 1.00 9.24  ? 346 GLU C CA    1 
ATOM   7344 C  C     . GLU F 2 346 ? -12.567 22.741 113.781 1.00 9.27  ? 346 GLU C C     1 
ATOM   7345 O  O     . GLU F 2 346 ? -13.799 22.753 113.920 1.00 10.13 ? 346 GLU C O     1 
ATOM   7346 C  CB    . GLU F 2 346 ? -11.644 21.993 111.597 1.00 11.47 ? 346 GLU C CB    1 
ATOM   7347 C  CG    . GLU F 2 346 ? -11.689 22.318 110.104 1.00 15.59 ? 346 GLU C CG    1 
ATOM   7348 C  CD    . GLU F 2 346 ? -12.919 23.137 109.708 1.00 20.48 ? 346 GLU C CD    1 
ATOM   7349 O  OE1   . GLU F 2 346 ? -14.101 22.642 109.863 1.00 22.66 ? 346 GLU C OE1   1 
ATOM   7350 O  OE2   . GLU F 2 346 ? -12.775 24.322 109.218 1.00 20.71 ? 346 GLU C OE2   1 
ATOM   7351 N  N     . TYR F 2 347 ? -11.697 22.340 114.681 1.00 9.19  ? 347 TYR C N     1 
ATOM   7352 C  CA    . TYR F 2 347 ? -12.068 21.860 116.016 1.00 8.71  ? 347 TYR C CA    1 
ATOM   7353 C  C     . TYR F 2 347 ? -12.852 22.948 116.737 1.00 8.13  ? 347 TYR C C     1 
ATOM   7354 O  O     . TYR F 2 347 ? -13.882 22.685 117.359 1.00 7.70  ? 347 TYR C O     1 
ATOM   7355 C  CB    . TYR F 2 347 ? -10.782 21.532 116.784 1.00 8.67  ? 347 TYR C CB    1 
ATOM   7356 C  CG    . TYR F 2 347 ? -10.998 21.249 118.268 1.00 8.94  ? 347 TYR C CG    1 
ATOM   7357 C  CD1   . TYR F 2 347 ? -11.462 19.998 118.678 1.00 9.09  ? 347 TYR C CD1   1 
ATOM   7358 C  CD2   . TYR F 2 347 ? -10.725 22.241 119.218 1.00 9.33  ? 347 TYR C CD2   1 
ATOM   7359 C  CE1   . TYR F 2 347 ? -11.649 19.733 120.038 1.00 9.57  ? 347 TYR C CE1   1 
ATOM   7360 C  CE2   . TYR F 2 347 ? -10.911 21.976 120.580 1.00 8.94  ? 347 TYR C CE2   1 
ATOM   7361 C  CZ    . TYR F 2 347 ? -11.372 20.721 120.990 1.00 8.77  ? 347 TYR C CZ    1 
ATOM   7362 O  OH    . TYR F 2 347 ? -11.553 20.458 122.313 1.00 8.45  ? 347 TYR C OH    1 
ATOM   7363 N  N     . ARG F 2 348 ? -12.314 24.150 116.602 1.00 8.07  ? 348 ARG C N     1 
ATOM   7364 C  CA    . ARG F 2 348 ? -12.904 25.336 117.256 1.00 9.56  ? 348 ARG C CA    1 
ATOM   7365 C  C     . ARG F 2 348 ? -14.257 25.694 116.675 1.00 11.00 ? 348 ARG C C     1 
ATOM   7366 O  O     . ARG F 2 348 ? -15.213 26.005 117.421 1.00 12.08 ? 348 ARG C O     1 
ATOM   7367 C  CB    . ARG F 2 348 ? -11.934 26.500 117.234 1.00 5.88  ? 348 ARG C CB    1 
ATOM   7368 C  CG    . ARG F 2 348 ? -11.215 26.874 118.492 1.00 5.57  ? 348 ARG C CG    1 
ATOM   7369 C  CD    . ARG F 2 348 ? -10.547 25.793 119.275 1.00 4.53  ? 348 ARG C CD    1 
ATOM   7370 N  NE    . ARG F 2 348 ? -10.757 26.024 120.711 1.00 4.60  ? 348 ARG C NE    1 
ATOM   7371 C  CZ    . ARG F 2 348 ? -9.867  25.860 121.682 1.00 5.56  ? 348 ARG C CZ    1 
ATOM   7372 N  NH1   . ARG F 2 348 ? -8.649  25.382 121.355 1.00 5.67  ? 348 ARG C NH1   1 
ATOM   7373 N  NH2   . ARG F 2 348 ? -10.068 26.135 122.966 1.00 7.97  ? 348 ARG C NH2   1 
ATOM   7374 N  N     . THR F 2 349 ? -14.397 25.643 115.362 1.00 11.55 ? 349 THR C N     1 
ATOM   7375 C  CA    . THR F 2 349 ? -15.614 25.994 114.647 1.00 12.10 ? 349 THR C CA    1 
ATOM   7376 C  C     . THR F 2 349 ? -16.712 24.934 114.768 1.00 12.31 ? 349 THR C C     1 
ATOM   7377 O  O     . THR F 2 349 ? -17.899 25.258 114.919 1.00 13.71 ? 349 THR C O     1 
ATOM   7378 C  CB    . THR F 2 349 ? -15.331 26.295 113.125 1.00 12.23 ? 349 THR C CB    1 
ATOM   7379 O  OG1   . THR F 2 349 ? -15.757 25.201 112.326 1.00 14.72 ? 349 THR C OG1   1 
ATOM   7380 C  CG2   . THR F 2 349 ? -13.848 26.529 112.828 1.00 13.89 ? 349 THR C CG2   1 
ATOM   7381 N  N     . VAL F 2 350 ? -16.326 23.683 114.704 1.00 11.24 ? 350 VAL C N     1 
ATOM   7382 C  CA    . VAL F 2 350 ? -17.296 22.581 114.799 1.00 10.61 ? 350 VAL C CA    1 
ATOM   7383 C  C     . VAL F 2 350 ? -18.019 22.615 116.150 1.00 11.67 ? 350 VAL C C     1 
ATOM   7384 O  O     . VAL F 2 350 ? -19.252 22.507 116.218 1.00 12.03 ? 350 VAL C O     1 
ATOM   7385 C  CB    . VAL F 2 350 ? -16.590 21.235 114.650 1.00 8.26  ? 350 VAL C CB    1 
ATOM   7386 C  CG1   . VAL F 2 350 ? -17.352 20.085 115.311 1.00 6.16  ? 350 VAL C CG1   1 
ATOM   7387 C  CG2   . VAL F 2 350 ? -16.397 20.820 113.190 1.00 9.85  ? 350 VAL C CG2   1 
ATOM   7388 N  N     . ALA F 2 351 ? -17.220 22.770 117.186 1.00 11.88 ? 351 ALA C N     1 
ATOM   7389 C  CA    . ALA F 2 351 ? -17.702 22.798 118.576 1.00 12.54 ? 351 ALA C CA    1 
ATOM   7390 C  C     . ALA F 2 351 ? -18.709 23.934 118.797 1.00 13.19 ? 351 ALA C C     1 
ATOM   7391 O  O     . ALA F 2 351 ? -19.627 23.824 119.623 1.00 14.44 ? 351 ALA C O     1 
ATOM   7392 C  CB    . ALA F 2 351 ? -16.527 23.013 119.533 1.00 11.99 ? 351 ALA C CB    1 
ATOM   7393 N  N     . ARG F 2 352 ? -18.518 25.004 118.050 1.00 13.05 ? 352 ARG C N     1 
ATOM   7394 C  CA    . ARG F 2 352 ? -19.359 26.207 118.166 1.00 12.49 ? 352 ARG C CA    1 
ATOM   7395 C  C     . ARG F 2 352 ? -20.634 26.096 117.319 1.00 12.57 ? 352 ARG C C     1 
ATOM   7396 O  O     . ARG F 2 352 ? -21.555 26.918 117.438 1.00 12.64 ? 352 ARG C O     1 
ATOM   7397 C  CB    . ARG F 2 352 ? -18.583 27.437 117.695 1.00 10.64 ? 352 ARG C CB    1 
ATOM   7398 C  CG    . ARG F 2 352 ? -19.178 28.751 118.205 1.00 11.61 ? 352 ARG C CG    1 
ATOM   7399 C  CD    . ARG F 2 352 ? -18.941 29.919 117.248 1.00 12.76 ? 352 ARG C CD    1 
ATOM   7400 N  NE    . ARG F 2 352 ? -18.117 29.544 116.091 1.00 14.17 ? 352 ARG C NE    1 
ATOM   7401 C  CZ    . ARG F 2 352 ? -18.313 30.004 114.849 1.00 16.42 ? 352 ARG C CZ    1 
ATOM   7402 N  NH1   . ARG F 2 352 ? -19.304 30.864 114.580 1.00 14.90 ? 352 ARG C NH1   1 
ATOM   7403 N  NH2   . ARG F 2 352 ? -17.561 29.657 113.796 1.00 17.19 ? 352 ARG C NH2   1 
ATOM   7404 N  N     . SER F 2 353 ? -20.677 25.079 116.480 1.00 12.19 ? 353 SER C N     1 
ATOM   7405 C  CA    . SER F 2 353 ? -21.822 24.860 115.577 1.00 11.69 ? 353 SER C CA    1 
ATOM   7406 C  C     . SER F 2 353 ? -22.718 23.716 116.063 1.00 11.00 ? 353 SER C C     1 
ATOM   7407 O  O     . SER F 2 353 ? -23.748 23.405 115.448 1.00 11.76 ? 353 SER C O     1 
ATOM   7408 C  CB    . SER F 2 353 ? -21.335 24.492 114.173 1.00 13.55 ? 353 SER C CB    1 
ATOM   7409 O  OG    . SER F 2 353 ? -20.011 24.959 113.975 1.00 15.46 ? 353 SER C OG    1 
ATOM   7410 N  N     . LEU F 2 354 ? -22.323 23.110 117.165 1.00 9.25  ? 354 LEU C N     1 
ATOM   7411 C  CA    . LEU F 2 354 ? -23.047 21.952 117.716 1.00 7.98  ? 354 LEU C CA    1 
ATOM   7412 C  C     . LEU F 2 354 ? -23.943 22.336 118.897 1.00 7.71  ? 354 LEU C C     1 
ATOM   7413 O  O     . LEU F 2 354 ? -23.558 23.149 119.754 1.00 7.74  ? 354 LEU C O     1 
ATOM   7414 C  CB    . LEU F 2 354 ? -22.053 20.895 118.190 1.00 8.02  ? 354 LEU C CB    1 
ATOM   7415 C  CG    . LEU F 2 354 ? -21.371 20.171 117.029 1.00 8.13  ? 354 LEU C CG    1 
ATOM   7416 C  CD1   . LEU F 2 354 ? -20.336 19.145 117.489 1.00 7.07  ? 354 LEU C CD1   1 
ATOM   7417 C  CD2   . LEU F 2 354 ? -22.356 19.404 116.145 1.00 8.13  ? 354 LEU C CD2   1 
ATOM   7418 N  N     . PRO F 2 355 ? -25.161 21.766 118.969 1.00 7.57  ? 355 PRO C N     1 
ATOM   7419 C  CA    . PRO F 2 355 ? -26.072 22.024 120.074 1.00 8.10  ? 355 PRO C CA    1 
ATOM   7420 C  C     . PRO F 2 355 ? -25.431 21.569 121.362 1.00 9.14  ? 355 PRO C C     1 
ATOM   7421 O  O     . PRO F 2 355 ? -24.672 20.553 121.348 1.00 10.32 ? 355 PRO C O     1 
ATOM   7422 C  CB    . PRO F 2 355 ? -27.297 21.204 119.732 1.00 8.13  ? 355 PRO C CB    1 
ATOM   7423 C  CG    . PRO F 2 355 ? -27.026 20.485 118.418 1.00 7.30  ? 355 PRO C CG    1 
ATOM   7424 C  CD    . PRO F 2 355 ? -25.657 20.849 117.941 1.00 7.71  ? 355 PRO C CD    1 
ATOM   7425 N  N     . VAL F 2 356 ? -25.724 22.286 122.439 1.00 9.49  ? 356 VAL C N     1 
ATOM   7426 C  CA    . VAL F 2 356 ? -25.147 21.980 123.768 1.00 9.27  ? 356 VAL C CA    1 
ATOM   7427 C  C     . VAL F 2 356 ? -25.269 20.484 124.080 1.00 10.03 ? 356 VAL C C     1 
ATOM   7428 O  O     . VAL F 2 356 ? -24.415 19.899 124.762 1.00 10.91 ? 356 VAL C O     1 
ATOM   7429 C  CB    . VAL F 2 356 ? -25.857 22.764 124.875 1.00 7.71  ? 356 VAL C CB    1 
ATOM   7430 C  CG1   . VAL F 2 356 ? -26.836 23.808 124.342 1.00 8.54  ? 356 VAL C CG1   1 
ATOM   7431 C  CG2   . VAL F 2 356 ? -26.669 21.872 125.817 1.00 7.71  ? 356 VAL C CG2   1 
ATOM   7432 N  N     . ALA F 2 357 ? -26.334 19.898 123.573 1.00 9.69  ? 357 ALA C N     1 
ATOM   7433 C  CA    . ALA F 2 357 ? -26.614 18.468 123.764 1.00 9.63  ? 357 ALA C CA    1 
ATOM   7434 C  C     . ALA F 2 357 ? -27.494 17.956 122.629 1.00 9.32  ? 357 ALA C C     1 
ATOM   7435 O  O     . ALA F 2 357 ? -28.195 18.728 121.963 1.00 10.69 ? 357 ALA C O     1 
ATOM   7436 C  CB    . ALA F 2 357 ? -27.335 18.245 125.094 1.00 10.70 ? 357 ALA C CB    1 
ATOM   7437 N  N     . VAL F 2 358 ? -27.427 16.659 122.447 1.00 8.84  ? 358 VAL C N     1 
ATOM   7438 C  CA    . VAL F 2 358 ? -28.189 15.966 121.409 1.00 7.80  ? 358 VAL C CA    1 
ATOM   7439 C  C     . VAL F 2 358 ? -28.746 14.670 122.002 1.00 7.87  ? 358 VAL C C     1 
ATOM   7440 O  O     . VAL F 2 358 ? -28.173 14.101 122.945 1.00 7.61  ? 358 VAL C O     1 
ATOM   7441 C  CB    . VAL F 2 358 ? -27.261 15.696 120.217 1.00 6.49  ? 358 VAL C CB    1 
ATOM   7442 C  CG1   . VAL F 2 358 ? -27.308 14.252 119.723 1.00 6.26  ? 358 VAL C CG1   1 
ATOM   7443 C  CG2   . VAL F 2 358 ? -27.585 16.563 118.996 1.00 8.35  ? 358 VAL C CG2   1 
ATOM   7444 N  N     . ILE F 2 359 ? -29.869 14.234 121.454 1.00 8.14  ? 359 ILE C N     1 
ATOM   7445 C  CA    . ILE F 2 359 ? -30.505 12.993 121.910 1.00 8.52  ? 359 ILE C CA    1 
ATOM   7446 C  C     . ILE F 2 359 ? -29.641 11.819 121.443 1.00 9.06  ? 359 ILE C C     1 
ATOM   7447 O  O     . ILE F 2 359 ? -28.887 11.931 120.465 1.00 9.62  ? 359 ILE C O     1 
ATOM   7448 C  CB    . ILE F 2 359 ? -31.923 12.850 121.377 1.00 8.01  ? 359 ILE C CB    1 
ATOM   7449 C  CG1   . ILE F 2 359 ? -32.142 13.585 120.053 1.00 9.79  ? 359 ILE C CG1   1 
ATOM   7450 C  CG2   . ILE F 2 359 ? -32.980 13.399 122.337 1.00 4.45  ? 359 ILE C CG2   1 
ATOM   7451 C  CD1   . ILE F 2 359 ? -33.047 12.817 119.087 1.00 25.00 ? 359 ILE C CD1   1 
ATOM   7452 N  N     . ALA F 2 360 ? -29.770 10.728 122.165 1.00 10.38 ? 360 ALA C N     1 
ATOM   7453 C  CA    . ALA F 2 360 ? -29.003 9.500  121.904 1.00 11.71 ? 360 ALA C CA    1 
ATOM   7454 C  C     . ALA F 2 360 ? -29.036 9.135  120.417 1.00 14.01 ? 360 ALA C C     1 
ATOM   7455 O  O     . ALA F 2 360 ? -28.017 9.228  119.715 1.00 15.89 ? 360 ALA C O     1 
ATOM   7456 C  CB    . ALA F 2 360 ? -29.597 8.335  122.698 1.00 6.91  ? 360 ALA C CB    1 
ATOM   7457 N  N     . ALA F 2 361 ? -30.217 8.730  120.002 1.00 14.82 ? 361 ALA C N     1 
ATOM   7458 C  CA    . ALA F 2 361 ? -30.500 8.292  118.627 1.00 15.95 ? 361 ALA C CA    1 
ATOM   7459 C  C     . ALA F 2 361 ? -29.616 9.015  117.602 1.00 16.74 ? 361 ALA C C     1 
ATOM   7460 O  O     . ALA F 2 361 ? -29.271 8.459  116.551 1.00 18.64 ? 361 ALA C O     1 
ATOM   7461 C  CB    . ALA F 2 361 ? -31.961 8.585  118.278 1.00 12.88 ? 361 ALA C CB    1 
ATOM   7462 N  N     . GLN F 2 362 ? -29.265 10.242 117.925 1.00 16.14 ? 362 GLN C N     1 
ATOM   7463 C  CA    . GLN F 2 362 ? -28.465 11.094 117.029 1.00 15.99 ? 362 GLN C CA    1 
ATOM   7464 C  C     . GLN F 2 362 ? -26.997 11.167 117.436 1.00 16.23 ? 362 GLN C C     1 
ATOM   7465 O  O     . GLN F 2 362 ? -26.318 12.176 117.208 1.00 17.35 ? 362 GLN C O     1 
ATOM   7466 C  CB    . GLN F 2 362 ? -28.935 12.550 117.104 1.00 13.86 ? 362 GLN C CB    1 
ATOM   7467 C  CG    . GLN F 2 362 ? -30.233 12.833 116.356 1.00 15.57 ? 362 GLN C CG    1 
ATOM   7468 C  CD    . GLN F 2 362 ? -30.699 14.281 116.538 1.00 19.61 ? 362 GLN C CD    1 
ATOM   7469 O  OE1   . GLN F 2 362 ? -31.478 14.785 115.732 1.00 23.19 ? 362 GLN C OE1   1 
ATOM   7470 N  NE2   . GLN F 2 362 ? -30.263 14.991 117.565 1.00 19.01 ? 362 GLN C NE2   1 
ATOM   7471 N  N     . ASN F 2 363 ? -26.457 10.121 118.026 1.00 14.50 ? 363 ASN C N     1 
ATOM   7472 C  CA    . ASN F 2 363 ? -25.076 10.238 118.498 1.00 13.00 ? 363 ASN C CA    1 
ATOM   7473 C  C     . ASN F 2 363 ? -24.201 9.875  117.602 1.00 12.00 ? 363 ASN C C     1 
ATOM   7474 O  O     . ASN F 2 363 ? -24.580 9.384  116.529 1.00 10.50 ? 363 ASN C O     1 
ATOM   7475 C  CB    . ASN F 2 363 ? -24.878 9.556  119.865 1.00 13.00 ? 363 ASN C CB    1 
ATOM   7476 C  CG    . ASN F 2 363 ? -24.853 8.037  119.852 1.00 14.00 ? 363 ASN C CG    1 
ATOM   7477 O  OD1   . ASN F 2 363 ? -23.817 7.442  120.145 1.00 14.00 ? 363 ASN C OD1   1 
ATOM   7478 N  ND2   . ASN F 2 363 ? -25.945 7.368  119.549 1.00 15.70 ? 363 ASN C ND2   1 
ATOM   7479 O  OXT   . ASN F 2 363 ? -22.990 10.021 117.824 1.00 10.50 ? 363 ASN C OXT   1 
ATOM   7480 N  N     . ALA G 3 1   ? -29.655 11.028 112.470 1.00 19.85 ? 364 ALA F N     1 
ATOM   7481 C  CA    . ALA G 3 1   ? -28.311 10.504 112.173 1.00 19.63 ? 364 ALA F CA    1 
ATOM   7482 C  C     . ALA G 3 1   ? -27.223 10.986 113.111 1.00 18.99 ? 364 ALA F C     1 
ATOM   7483 O  O     . ALA G 3 1   ? -27.372 12.026 113.772 1.00 19.93 ? 364 ALA F O     1 
ATOM   7484 C  CB    . ALA G 3 1   ? -28.262 11.366 110.610 1.00 18.82 ? 364 ALA F CB    1 
ATOM   7485 N  N     . SER G 3 2   ? -26.197 10.176 113.024 1.00 17.14 ? 365 SER F N     1 
ATOM   7486 C  CA    . SER G 3 2   ? -24.946 10.269 113.765 1.00 15.01 ? 365 SER F CA    1 
ATOM   7487 C  C     . SER G 3 2   ? -24.420 11.697 113.891 1.00 13.94 ? 365 SER F C     1 
ATOM   7488 O  O     . SER G 3 2   ? -24.773 12.581 113.089 1.00 12.96 ? 365 SER F O     1 
ATOM   7489 C  CB    . SER G 3 2   ? -23.873 9.468  113.033 1.00 14.73 ? 365 SER F CB    1 
ATOM   7490 O  OG    . SER G 3 2   ? -24.039 9.612  111.628 1.00 16.21 ? 365 SER F OG    1 
ATOM   7491 N  N     . MET G 3 3   ? -23.584 11.782 114.910 1.00 13.01 ? 366 MET F N     1 
ATOM   7492 C  CA    . MET G 3 3   ? -22.865 12.984 115.340 1.00 12.74 ? 366 MET F CA    1 
ATOM   7493 C  C     . MET G 3 3   ? -21.702 13.255 114.381 1.00 12.96 ? 366 MET F C     1 
ATOM   7494 O  O     . MET G 3 3   ? -21.424 14.408 114.020 1.00 13.82 ? 366 MET F O     1 
ATOM   7495 C  CB    . MET G 3 3   ? -22.321 12.734 116.753 1.00 12.92 ? 366 MET F CB    1 
ATOM   7496 C  CG    . MET G 3 3   ? -21.667 13.957 117.388 1.00 14.92 ? 366 MET F CG    1 
ATOM   7497 S  SD    . MET G 3 3   ? -22.546 15.465 117.052 1.00 17.44 ? 366 MET F SD    1 
ATOM   7498 C  CE    . MET G 3 3   ? -23.515 15.943 118.467 1.00 16.32 ? 366 MET F CE    1 
ATOM   7499 N  N     . TRP G 3 4   ? -21.041 12.175 113.986 1.00 11.95 ? 367 TRP F N     1 
ATOM   7500 C  CA    . TRP G 3 4   ? -19.897 12.260 113.064 1.00 12.70 ? 367 TRP F CA    1 
ATOM   7501 C  C     . TRP G 3 4   ? -20.359 12.690 111.675 1.00 12.97 ? 367 TRP F C     1 
ATOM   7502 O  O     . TRP G 3 4   ? -19.660 13.428 110.970 1.00 12.39 ? 367 TRP F O     1 
ATOM   7503 C  CB    . TRP G 3 4   ? -19.183 10.919 112.898 1.00 12.88 ? 367 TRP F CB    1 
ATOM   7504 C  CG    . TRP G 3 4   ? -18.052 11.016 111.866 1.00 12.76 ? 367 TRP F CG    1 
ATOM   7505 C  CD1   . TRP G 3 4   ? -17.895 10.279 110.756 1.00 12.02 ? 367 TRP F CD1   1 
ATOM   7506 C  CD2   . TRP G 3 4   ? -16.974 11.938 111.931 1.00 12.12 ? 367 TRP F CD2   1 
ATOM   7507 N  NE1   . TRP G 3 4   ? -16.704 10.744 110.106 1.00 10.97 ? 367 TRP F NE1   1 
ATOM   7508 C  CE2   . TRP G 3 4   ? -16.181 11.718 110.811 1.00 12.38 ? 367 TRP F CE2   1 
ATOM   7509 C  CE3   . TRP G 3 4   ? -16.608 12.934 112.842 1.00 11.84 ? 367 TRP F CE3   1 
ATOM   7510 C  CZ2   . TRP G 3 4   ? -15.022 12.455 110.539 1.00 13.15 ? 367 TRP F CZ2   1 
ATOM   7511 C  CZ3   . TRP G 3 4   ? -15.437 13.669 112.561 1.00 12.07 ? 367 TRP F CZ3   1 
ATOM   7512 C  CH2   . TRP G 3 4   ? -14.683 13.440 111.463 1.00 12.37 ? 367 TRP F CH2   1 
ATOM   7513 N  N     . GLU G 3 5   ? -21.531 12.210 111.311 1.00 13.63 ? 368 GLU F N     1 
ATOM   7514 C  CA    . GLU G 3 5   ? -22.132 12.528 110.011 1.00 14.35 ? 368 GLU F CA    1 
ATOM   7515 C  C     . GLU G 3 5   ? -22.317 14.045 109.894 1.00 14.69 ? 368 GLU F C     1 
ATOM   7516 O  O     . GLU G 3 5   ? -22.003 14.649 108.859 1.00 14.89 ? 368 GLU F O     1 
ATOM   7517 C  CB    . GLU G 3 5   ? -23.490 11.834 109.875 1.00 17.29 ? 368 GLU F CB    1 
ATOM   7518 C  CG    . GLU G 3 5   ? -23.618 11.007 108.591 1.00 21.17 ? 368 GLU F CG    1 
ATOM   7519 C  CD    . GLU G 3 5   ? -22.284 10.429 108.108 1.00 25.21 ? 368 GLU F CD    1 
ATOM   7520 O  OE1   . GLU G 3 5   ? -21.846 9.317  108.594 1.00 26.63 ? 368 GLU F OE1   1 
ATOM   7521 O  OE2   . GLU G 3 5   ? -21.597 11.054 107.212 1.00 26.19 ? 368 GLU F OE2   1 
ATOM   7522 N  N     . ARG G 3 6   ? -22.819 14.607 110.978 1.00 15.09 ? 369 ARG F N     1 
ATOM   7523 C  CA    . ARG G 3 6   ? -23.094 16.048 111.089 1.00 15.24 ? 369 ARG F CA    1 
ATOM   7524 C  C     . ARG G 3 6   ? -21.781 16.841 111.137 1.00 16.04 ? 369 ARG F C     1 
ATOM   7525 O  O     . ARG G 3 6   ? -21.638 17.882 110.479 1.00 16.79 ? 369 ARG F O     1 
ATOM   7526 C  CB    . ARG G 3 6   ? -23.906 16.313 112.360 1.00 12.56 ? 369 ARG F CB    1 
ATOM   7527 C  CG    . ARG G 3 6   ? -23.523 17.610 113.074 1.00 13.18 ? 369 ARG F CG    1 
ATOM   7528 C  CD    . ARG G 3 6   ? -24.527 17.997 114.163 1.00 14.45 ? 369 ARG F CD    1 
ATOM   7529 N  NE    . ARG G 3 6   ? -25.687 17.093 114.213 1.00 16.18 ? 369 ARG F NE    1 
ATOM   7530 C  CZ    . ARG G 3 6   ? -26.767 17.293 114.980 1.00 18.61 ? 369 ARG F CZ    1 
ATOM   7531 N  NH1   . ARG G 3 6   ? -26.859 18.365 115.778 1.00 18.03 ? 369 ARG F NH1   1 
ATOM   7532 N  NH2   . ARG G 3 6   ? -27.821 16.466 115.020 1.00 18.86 ? 369 ARG F NH2   1 
ATOM   7533 N  N     . VAL G 3 7   ? -20.853 16.320 111.920 1.00 15.85 ? 370 VAL F N     1 
ATOM   7534 C  CA    . VAL G 3 7   ? -19.527 16.936 112.107 1.00 14.99 ? 370 VAL F CA    1 
ATOM   7535 C  C     . VAL G 3 7   ? -18.763 16.972 110.780 1.00 15.49 ? 370 VAL F C     1 
ATOM   7536 O  O     . VAL G 3 7   ? -18.080 17.958 110.463 1.00 16.03 ? 370 VAL F O     1 
ATOM   7537 C  CB    . VAL G 3 7   ? -18.711 16.131 113.121 1.00 12.65 ? 370 VAL F CB    1 
ATOM   7538 C  CG1   . VAL G 3 7   ? -17.277 16.641 113.274 1.00 9.87  ? 370 VAL F CG1   1 
ATOM   7539 C  CG2   . VAL G 3 7   ? -19.312 16.157 114.528 1.00 10.71 ? 370 VAL F CG2   1 
ATOM   7540 N  N     . LYS G 3 8   ? -18.906 15.886 110.044 1.00 15.43 ? 371 LYS F N     1 
ATOM   7541 C  CA    . LYS G 3 8   ? -18.251 15.708 108.738 1.00 15.20 ? 371 LYS F CA    1 
ATOM   7542 C  C     . LYS G 3 8   ? -18.736 16.769 107.747 1.00 15.22 ? 371 LYS F C     1 
ATOM   7543 O  O     . LYS G 3 8   ? -17.933 17.398 107.041 1.00 15.77 ? 371 LYS F O     1 
ATOM   7544 C  CB    . LYS G 3 8   ? -18.581 14.326 108.171 1.00 14.33 ? 371 LYS F CB    1 
ATOM   7545 C  CG    . LYS G 3 8   ? -17.585 13.248 108.602 1.00 14.32 ? 371 LYS F CG    1 
ATOM   7546 C  CD    . LYS G 3 8   ? -17.423 12.135 107.565 1.00 16.05 ? 371 LYS F CD    1 
ATOM   7547 C  CE    . LYS G 3 8   ? -18.657 11.959 106.677 1.00 16.94 ? 371 LYS F CE    1 
ATOM   7548 N  NZ    . LYS G 3 8   ? -18.484 10.918 105.653 1.00 17.07 ? 371 LYS F NZ    1 
ATOM   7549 N  N     . SER G 3 9   ? -20.045 16.929 107.728 1.00 14.51 ? 372 SER F N     1 
ATOM   7550 C  CA    . SER G 3 9   ? -20.723 17.885 106.840 1.00 14.50 ? 372 SER F CA    1 
ATOM   7551 C  C     . SER G 3 9   ? -20.299 19.319 107.174 1.00 13.89 ? 372 SER F C     1 
ATOM   7552 O  O     . SER G 3 9   ? -20.029 20.131 106.277 1.00 13.19 ? 372 SER F O     1 
ATOM   7553 C  CB    . SER G 3 9   ? -22.240 17.762 106.999 1.00 15.53 ? 372 SER F CB    1 
ATOM   7554 O  OG    . SER G 3 9   ? -22.696 18.645 108.011 1.00 20.41 ? 372 SER F OG    1 
ATOM   7555 N  N     . ILE G 3 10  ? -20.253 19.592 108.466 1.00 12.77 ? 373 ILE F N     1 
ATOM   7556 C  CA    . ILE G 3 10  ? -19.871 20.916 108.983 1.00 12.53 ? 373 ILE F CA    1 
ATOM   7557 C  C     . ILE G 3 10  ? -18.458 21.279 108.519 1.00 13.59 ? 373 ILE F C     1 
ATOM   7558 O  O     . ILE G 3 10  ? -18.220 22.377 107.996 1.00 14.17 ? 373 ILE F O     1 
ATOM   7559 C  CB    . ILE G 3 10  ? -19.890 20.920 110.514 1.00 10.95 ? 373 ILE F CB    1 
ATOM   7560 C  CG1   . ILE G 3 10  ? -21.268 20.613 111.102 1.00 11.23 ? 373 ILE F CG1   1 
ATOM   7561 C  CG2   . ILE G 3 10  ? -19.482 22.269 111.112 1.00 11.61 ? 373 ILE F CG2   1 
ATOM   7562 C  CD1   . ILE G 3 10  ? -21.385 20.991 112.581 1.00 25.00 ? 373 ILE F CD1   1 
ATOM   7563 N  N     . ILE G 3 11  ? -17.563 20.332 108.730 1.00 13.57 ? 374 ILE F N     1 
ATOM   7564 C  CA    . ILE G 3 11  ? -16.143 20.475 108.373 1.00 14.08 ? 374 ILE F CA    1 
ATOM   7565 C  C     . ILE G 3 11  ? -15.994 20.797 106.883 1.00 14.65 ? 374 ILE F C     1 
ATOM   7566 O  O     . ILE G 3 11  ? -15.223 21.687 106.496 1.00 14.69 ? 374 ILE F O     1 
ATOM   7567 C  CB    . ILE G 3 11  ? -15.394 19.175 108.672 1.00 14.61 ? 374 ILE F CB    1 
ATOM   7568 C  CG1   . ILE G 3 11  ? -14.893 19.092 110.116 1.00 15.37 ? 374 ILE F CG1   1 
ATOM   7569 C  CG2   . ILE G 3 11  ? -14.156 18.983 107.793 1.00 13.66 ? 374 ILE F CG2   1 
ATOM   7570 C  CD1   . ILE G 3 11  ? -14.262 17.740 110.454 1.00 25.00 ? 374 ILE F CD1   1 
ATOM   7571 N  N     . LYS G 3 12  ? -16.742 20.054 106.090 1.00 14.78 ? 375 LYS F N     1 
ATOM   7572 C  CA    . LYS G 3 12  ? -16.737 20.189 104.625 1.00 15.09 ? 375 LYS F CA    1 
ATOM   7573 C  C     . LYS G 3 12  ? -17.160 21.602 104.209 1.00 15.28 ? 375 LYS F C     1 
ATOM   7574 O  O     . LYS G 3 12  ? -16.512 22.240 103.367 1.00 15.00 ? 375 LYS F O     1 
ATOM   7575 C  CB    . LYS G 3 12  ? -17.716 19.192 104.002 1.00 13.39 ? 375 LYS F CB    1 
ATOM   7576 C  CG    . LYS G 3 12  ? -17.388 17.737 104.341 1.00 12.36 ? 375 LYS F CG    1 
ATOM   7577 C  CD    . LYS G 3 12  ? -17.042 16.900 103.108 1.00 13.50 ? 375 LYS F CD    1 
ATOM   7578 C  CE    . LYS G 3 12  ? -17.627 15.487 103.162 1.00 14.89 ? 375 LYS F CE    1 
ATOM   7579 N  NZ    . LYS G 3 12  ? -17.943 14.945 101.832 1.00 12.77 ? 375 LYS F NZ    1 
ATOM   7580 N  N     . SER G 3 13  ? -18.242 22.041 104.820 1.00 16.06 ? 376 SER F N     1 
ATOM   7581 C  CA    . SER G 3 13  ? -18.848 23.355 104.549 1.00 17.58 ? 376 SER F CA    1 
ATOM   7582 C  C     . SER G 3 13  ? -17.875 24.498 104.867 1.00 18.52 ? 376 SER F C     1 
ATOM   7583 O  O     . SER G 3 13  ? -17.765 25.473 104.111 1.00 19.53 ? 376 SER F O     1 
ATOM   7584 C  CB    . SER G 3 13  ? -20.099 23.541 105.409 1.00 19.18 ? 376 SER F CB    1 
ATOM   7585 O  OG    . SER G 3 13  ? -20.107 24.841 105.980 1.00 23.86 ? 376 SER F OG    1 
ATOM   7586 N  N     . SER G 3 14  ? -17.193 24.345 105.985 1.00 18.17 ? 377 SER F N     1 
ATOM   7587 C  CA    . SER G 3 14  ? -16.245 25.356 106.486 1.00 17.88 ? 377 SER F CA    1 
ATOM   7588 C  C     . SER G 3 14  ? -14.961 25.395 105.649 1.00 17.61 ? 377 SER F C     1 
ATOM   7589 O  O     . SER G 3 14  ? -14.315 26.445 105.517 1.00 18.41 ? 377 SER F O     1 
ATOM   7590 C  CB    . SER G 3 14  ? -15.857 25.038 107.932 1.00 17.19 ? 377 SER F CB    1 
ATOM   7591 O  OG    . SER G 3 14  ? -16.244 26.105 108.784 1.00 19.43 ? 377 SER F OG    1 
ATOM   7592 N  N     . LEU G 3 15  ? -14.619 24.248 105.098 1.00 17.39 ? 378 LEU F N     1 
ATOM   7593 C  CA    . LEU G 3 15  ? -13.388 24.085 104.307 1.00 17.64 ? 378 LEU F CA    1 
ATOM   7594 C  C     . LEU G 3 15  ? -13.549 24.614 102.876 1.00 18.29 ? 378 LEU F C     1 
ATOM   7595 O  O     . LEU G 3 15  ? -12.563 24.942 102.201 1.00 19.11 ? 378 LEU F O     1 
ATOM   7596 C  CB    . LEU G 3 15  ? -13.010 22.605 104.220 1.00 16.78 ? 378 LEU F CB    1 
ATOM   7597 C  CG    . LEU G 3 15  ? -11.700 22.281 104.940 1.00 17.59 ? 378 LEU F CG    1 
ATOM   7598 C  CD1   . LEU G 3 15  ? -11.741 22.616 106.432 1.00 17.97 ? 378 LEU F CD1   1 
ATOM   7599 C  CD2   . LEU G 3 15  ? -11.322 20.801 104.857 1.00 17.40 ? 378 LEU F CD2   1 
ATOM   7600 N  N     . ALA G 3 16  ? -14.789 24.694 102.430 1.00 17.91 ? 379 ALA F N     1 
ATOM   7601 C  CA    . ALA G 3 16  ? -15.090 25.132 101.056 1.00 19.20 ? 379 ALA F CA    1 
ATOM   7602 C  C     . ALA G 3 16  ? -15.859 26.400 101.029 1.00 20.96 ? 379 ALA F C     1 
ATOM   7603 O  O     . ALA G 3 16  ? -16.884 26.514 100.341 1.00 22.12 ? 379 ALA F O     1 
ATOM   7604 C  CB    . ALA G 3 16  ? -15.920 24.067 100.336 1.00 17.28 ? 379 ALA F CB    1 
HETATM 7605 CA CA    . CA  H 4 .   ? 11.632  41.388 146.975 1.00 13.86 ? 364 CA  A CA    1 
HETATM 7606 CA CA    . CA  I 4 .   ? -0.125  28.243 131.453 1.00 50.80 ? 365 CA  A CA    1 
HETATM 7607 CA CA    . CA  J 4 .   ? 6.043   9.181  144.377 1.00 12.81 ? 364 CA  B CA    1 
HETATM 7608 CA CA    . CA  K 4 .   ? -18.743 30.268 146.025 1.00 16.92 ? 364 CA  C CA    1 
HETATM 7609 CA CA    . CA  L 4 .   ? -0.038  28.755 125.978 1.00 26.61 ? 365 CA  C CA    1 
HETATM 7610 O  O     . HOH M 5 .   ? -17.562 47.397 116.579 0.75 24.15 ? 366 HOH A O     1 
HETATM 7611 O  O     . HOH M 5 .   ? -18.139 40.706 112.934 0.75 17.54 ? 367 HOH A O     1 
HETATM 7612 O  O     . HOH M 5 .   ? -11.823 43.967 122.767 0.75 7.38  ? 368 HOH A O     1 
HETATM 7613 O  O     . HOH M 5 .   ? -15.529 62.720 138.192 0.75 18.25 ? 369 HOH A O     1 
HETATM 7614 O  O     . HOH M 5 .   ? -20.113 55.126 136.773 0.75 18.02 ? 370 HOH A O     1 
HETATM 7615 O  O     . HOH M 5 .   ? -16.353 65.238 141.588 0.75 21.73 ? 371 HOH A O     1 
HETATM 7616 O  O     . HOH M 5 .   ? -8.704  64.834 146.705 0.75 18.43 ? 372 HOH A O     1 
HETATM 7617 O  O     . HOH M 5 .   ? -7.171  65.782 149.299 0.75 18.41 ? 373 HOH A O     1 
HETATM 7618 O  O     . HOH M 5 .   ? -11.391 66.151 148.774 0.75 18.33 ? 374 HOH A O     1 
HETATM 7619 O  O     . HOH M 5 .   ? -4.179  68.098 148.927 0.75 6.73  ? 375 HOH A O     1 
HETATM 7620 O  O     . HOH M 5 .   ? -9.533  61.858 149.615 0.75 24.25 ? 376 HOH A O     1 
HETATM 7621 O  O     . HOH M 5 .   ? 3.094   56.671 152.925 0.75 16.97 ? 377 HOH A O     1 
HETATM 7622 O  O     . HOH M 5 .   ? -3.094  56.167 149.093 0.75 22.09 ? 378 HOH A O     1 
HETATM 7623 O  O     . HOH M 5 .   ? -0.499  55.323 151.687 0.75 15.32 ? 379 HOH A O     1 
HETATM 7624 O  O     . HOH M 5 .   ? 3.978   59.977 155.616 0.75 8.94  ? 380 HOH A O     1 
HETATM 7625 O  O     . HOH M 5 .   ? 9.722   60.498 156.287 0.75 16.95 ? 381 HOH A O     1 
HETATM 7626 O  O     . HOH M 5 .   ? 4.144   62.669 157.969 0.75 15.64 ? 382 HOH A O     1 
HETATM 7627 O  O     . HOH M 5 .   ? 4.959   67.046 154.034 0.75 20.26 ? 383 HOH A O     1 
HETATM 7628 O  O     . HOH M 5 .   ? 17.361  46.559 158.831 0.75 15.19 ? 384 HOH A O     1 
HETATM 7629 O  O     . HOH M 5 .   ? -22.794 43.838 136.935 0.75 18.36 ? 385 HOH A O     1 
HETATM 7630 O  O     . HOH M 5 .   ? -22.629 52.498 134.929 0.75 7.87  ? 386 HOH A O     1 
HETATM 7631 O  O     . HOH M 5 .   ? -26.180 42.239 136.385 0.75 9.39  ? 387 HOH A O     1 
HETATM 7632 O  O     . HOH M 5 .   ? -27.925 39.529 141.028 0.75 26.55 ? 388 HOH A O     1 
HETATM 7633 O  O     . HOH M 5 .   ? 8.698   62.070 126.279 0.75 11.05 ? 389 HOH A O     1 
HETATM 7634 O  O     . HOH M 5 .   ? 13.821  56.117 128.798 0.75 5.82  ? 390 HOH A O     1 
HETATM 7635 O  O     . HOH M 5 .   ? -0.857  25.157 167.262 0.75 3.26  ? 391 HOH A O     1 
HETATM 7636 O  O     . HOH M 5 .   ? 15.449  51.266 126.310 0.75 7.70  ? 392 HOH A O     1 
HETATM 7637 O  O     . HOH M 5 .   ? 5.975   60.594 123.966 0.75 9.76  ? 393 HOH A O     1 
HETATM 7638 O  O     . HOH M 5 .   ? 7.523   66.205 125.461 0.75 8.14  ? 394 HOH A O     1 
HETATM 7639 O  O     . HOH M 5 .   ? -5.541  68.604 131.042 0.75 2.74  ? 395 HOH A O     1 
HETATM 7640 O  O     . HOH M 5 .   ? -5.623  28.239 133.913 0.75 14.58 ? 396 HOH A O     1 
HETATM 7641 O  O     . HOH M 5 .   ? -1.048  41.301 161.395 0.75 17.41 ? 397 HOH A O     1 
HETATM 7642 O  O     . HOH M 5 .   ? 8.518   43.283 157.613 0.75 3.90  ? 398 HOH A O     1 
HETATM 7643 O  O     . HOH M 5 .   ? 13.664  41.856 163.136 0.75 12.05 ? 399 HOH A O     1 
HETATM 7644 O  O     . HOH M 5 .   ? 16.206  44.285 160.536 0.75 20.41 ? 400 HOH A O     1 
HETATM 7645 O  O     . HOH M 5 .   ? 10.981  35.511 159.767 0.75 21.85 ? 401 HOH A O     1 
HETATM 7646 O  O     . HOH M 5 .   ? 9.933   38.706 160.736 0.75 15.45 ? 402 HOH A O     1 
HETATM 7647 O  O     . HOH M 5 .   ? 0.720   45.131 161.768 0.75 8.65  ? 403 HOH A O     1 
HETATM 7648 O  O     . HOH M 5 .   ? -2.984  44.728 160.845 0.75 20.30 ? 404 HOH A O     1 
HETATM 7649 O  O     . HOH M 5 .   ? 13.212  53.665 148.768 0.75 24.32 ? 405 HOH A O     1 
HETATM 7650 O  O     . HOH M 5 .   ? 4.020   47.447 154.610 0.75 6.02  ? 406 HOH A O     1 
HETATM 7651 O  O     . HOH M 5 .   ? 1.193   47.833 156.757 0.75 16.56 ? 407 HOH A O     1 
HETATM 7652 O  O     . HOH M 5 .   ? 1.042   51.531 156.576 0.75 15.73 ? 408 HOH A O     1 
HETATM 7653 O  O     . HOH M 5 .   ? -5.472  51.205 155.341 0.75 23.40 ? 409 HOH A O     1 
HETATM 7654 O  O     . HOH M 5 .   ? 13.085  45.009 150.532 0.75 16.02 ? 410 HOH A O     1 
HETATM 7655 O  O     . HOH M 5 .   ? -13.104 35.219 156.050 0.75 13.78 ? 411 HOH A O     1 
HETATM 7656 O  O     . HOH M 5 .   ? -1.939  33.232 135.173 0.75 10.55 ? 412 HOH A O     1 
HETATM 7657 O  O     . HOH M 5 .   ? -3.049  33.630 138.737 0.75 15.04 ? 413 HOH A O     1 
HETATM 7658 O  O     . HOH M 5 .   ? -7.121  75.035 143.791 0.75 12.56 ? 414 HOH A O     1 
HETATM 7659 O  O     . HOH M 5 .   ? -2.031  73.786 148.801 0.75 13.27 ? 415 HOH A O     1 
HETATM 7660 O  O     . HOH M 5 .   ? -26.530 35.957 140.351 0.75 7.74  ? 416 HOH A O     1 
HETATM 7661 O  O     . HOH M 5 .   ? -30.809 32.024 139.493 0.75 19.22 ? 417 HOH A O     1 
HETATM 7662 O  O     . HOH M 5 .   ? -22.878 40.449 123.062 0.75 7.96  ? 418 HOH A O     1 
HETATM 7663 O  O     . HOH M 5 .   ? -19.975 41.424 120.390 0.75 18.13 ? 419 HOH A O     1 
HETATM 7664 O  O     . HOH M 5 .   ? -4.605  44.848 125.123 0.75 4.59  ? 420 HOH A O     1 
HETATM 7665 O  O     . HOH M 5 .   ? -4.062  32.020 116.399 0.75 21.91 ? 421 HOH A O     1 
HETATM 7666 O  O     . HOH M 5 .   ? 6.796   55.435 115.589 0.75 17.91 ? 422 HOH A O     1 
HETATM 7667 O  O     . HOH M 5 .   ? 9.531   51.725 112.026 0.75 7.81  ? 423 HOH A O     1 
HETATM 7668 O  O     . HOH M 5 .   ? 10.573  48.155 112.399 0.75 7.94  ? 424 HOH A O     1 
HETATM 7669 O  O     . HOH M 5 .   ? 4.598   43.565 121.392 0.75 12.63 ? 425 HOH A O     1 
HETATM 7670 O  O     . HOH M 5 .   ? 2.863   51.336 125.089 0.75 10.78 ? 426 HOH A O     1 
HETATM 7671 O  O     . HOH M 5 .   ? 3.311   47.984 126.347 0.75 5.11  ? 427 HOH A O     1 
HETATM 7672 O  O     . HOH M 5 .   ? -0.110  82.440 133.848 1.00 0.00  ? 428 HOH A O     1 
HETATM 7673 O  O     . HOH M 5 .   ? 13.295  36.794 157.319 0.75 14.14 ? 429 HOH A O     1 
HETATM 7674 O  O     . HOH M 5 .   ? 3.443   29.116 141.002 0.75 28.95 ? 430 HOH A O     1 
HETATM 7675 O  O     . HOH M 5 .   ? 6.868   18.686 162.237 0.75 10.11 ? 431 HOH A O     1 
HETATM 7676 O  O     . HOH M 5 .   ? -17.360 26.508 123.400 0.75 11.94 ? 432 HOH A O     1 
HETATM 7677 O  O     . HOH M 5 .   ? -5.795  33.287 146.933 0.75 3.09  ? 433 HOH A O     1 
HETATM 7678 O  O     . HOH N 5 .   ? 7.301   53.253 109.078 0.75 9.16  ? 61  HOH D O     1 
HETATM 7679 O  O     . HOH O 5 .   ? 15.937  45.614 146.309 0.75 9.91  ? 365 HOH B O     1 
HETATM 7680 O  O     . HOH O 5 .   ? 2.454   32.610 138.553 0.75 17.99 ? 366 HOH B O     1 
HETATM 7681 O  O     . HOH O 5 .   ? 13.087  44.416 118.067 0.75 18.02 ? 367 HOH B O     1 
HETATM 7682 O  O     . HOH O 5 .   ? 16.338  44.693 121.335 0.75 13.90 ? 368 HOH B O     1 
HETATM 7683 O  O     . HOH O 5 .   ? 7.619   46.572 123.304 0.75 13.07 ? 369 HOH B O     1 
HETATM 7684 O  O     . HOH O 5 .   ? 11.797  48.777 119.801 0.75 2.71  ? 370 HOH B O     1 
HETATM 7685 O  O     . HOH O 5 .   ? 13.408  36.545 106.500 0.75 19.21 ? 371 HOH B O     1 
HETATM 7686 O  O     . HOH O 5 .   ? 15.881  39.123 110.495 0.75 12.67 ? 372 HOH B O     1 
HETATM 7687 O  O     . HOH O 5 .   ? 8.328   35.864 108.939 0.75 18.49 ? 373 HOH B O     1 
HETATM 7688 O  O     . HOH O 5 .   ? 24.965  29.111 109.432 0.75 12.36 ? 374 HOH B O     1 
HETATM 7689 O  O     . HOH O 5 .   ? 34.981  33.500 121.541 0.75 15.71 ? 375 HOH B O     1 
HETATM 7690 O  O     . HOH O 5 .   ? 5.771   26.281 120.312 0.75 7.09  ? 376 HOH B O     1 
HETATM 7691 O  O     . HOH O 5 .   ? 3.113   31.361 119.373 0.75 20.57 ? 377 HOH B O     1 
HETATM 7692 O  O     . HOH O 5 .   ? 0.484   28.772 118.707 0.75 11.09 ? 378 HOH B O     1 
HETATM 7693 O  O     . HOH O 5 .   ? 17.610  48.089 128.022 0.75 4.40  ? 379 HOH B O     1 
HETATM 7694 O  O     . HOH O 5 .   ? 28.261  31.225 133.219 0.75 8.20  ? 380 HOH B O     1 
HETATM 7695 O  O     . HOH O 5 .   ? 39.774  5.775  141.376 0.75 15.59 ? 381 HOH B O     1 
HETATM 7696 O  O     . HOH O 5 .   ? 36.788  -0.693 147.104 0.75 19.15 ? 382 HOH B O     1 
HETATM 7697 O  O     . HOH O 5 .   ? 19.752  21.766 136.998 0.75 2.97  ? 383 HOH B O     1 
HETATM 7698 O  O     . HOH O 5 .   ? 10.572  26.530 129.996 0.75 11.78 ? 384 HOH B O     1 
HETATM 7699 O  O     . HOH O 5 .   ? 24.033  12.997 148.452 0.75 21.75 ? 385 HOH B O     1 
HETATM 7700 O  O     . HOH O 5 .   ? 16.814  2.206  145.487 0.75 14.45 ? 386 HOH B O     1 
HETATM 7701 O  O     . HOH O 5 .   ? 12.111  1.533  141.126 0.75 9.28  ? 387 HOH B O     1 
HETATM 7702 O  O     . HOH O 5 .   ? 14.969  0.452  139.165 0.75 7.32  ? 388 HOH B O     1 
HETATM 7703 O  O     . HOH O 5 .   ? 17.004  0.454  135.499 0.75 6.03  ? 389 HOH B O     1 
HETATM 7704 O  O     . HOH O 5 .   ? 14.778  1.267  143.302 0.75 10.33 ? 390 HOH B O     1 
HETATM 7705 O  O     . HOH O 5 .   ? 12.225  5.295  146.758 0.75 11.44 ? 391 HOH B O     1 
HETATM 7706 O  O     . HOH O 5 .   ? 26.596  5.760  151.486 0.75 21.17 ? 392 HOH B O     1 
HETATM 7707 O  O     . HOH O 5 .   ? 25.996  8.710  152.368 0.75 10.25 ? 393 HOH B O     1 
HETATM 7708 O  O     . HOH O 5 .   ? 23.320  5.661  153.531 0.75 13.13 ? 394 HOH B O     1 
HETATM 7709 O  O     . HOH O 5 .   ? 27.382  33.256 143.865 0.75 8.20  ? 395 HOH B O     1 
HETATM 7710 O  O     . HOH O 5 .   ? 29.655  38.210 140.767 0.75 11.87 ? 396 HOH B O     1 
HETATM 7711 O  O     . HOH O 5 .   ? 28.914  32.504 147.925 0.75 24.91 ? 397 HOH B O     1 
HETATM 7712 O  O     . HOH O 5 .   ? 14.480  34.694 154.869 0.75 19.86 ? 398 HOH B O     1 
HETATM 7713 O  O     . HOH O 5 .   ? 12.513  29.498 153.567 0.75 8.69  ? 399 HOH B O     1 
HETATM 7714 O  O     . HOH O 5 .   ? 16.274  28.953 155.661 0.75 23.51 ? 400 HOH B O     1 
HETATM 7715 O  O     . HOH O 5 .   ? 18.169  25.268 154.435 0.75 20.11 ? 401 HOH B O     1 
HETATM 7716 O  O     . HOH O 5 .   ? 16.099  21.738 156.306 0.75 18.20 ? 402 HOH B O     1 
HETATM 7717 O  O     . HOH O 5 .   ? 22.484  23.963 155.017 0.75 12.51 ? 403 HOH B O     1 
HETATM 7718 O  O     . HOH O 5 .   ? 22.483  27.109 125.465 0.75 9.04  ? 404 HOH B O     1 
HETATM 7719 O  O     . HOH O 5 .   ? 14.182  15.686 123.422 0.75 15.87 ? 405 HOH B O     1 
HETATM 7720 O  O     . HOH O 5 .   ? 11.043  11.832 127.876 0.75 13.15 ? 406 HOH B O     1 
HETATM 7721 O  O     . HOH O 5 .   ? 8.304   12.652 142.479 0.75 2.00  ? 407 HOH B O     1 
HETATM 7722 O  O     . HOH O 5 .   ? -2.822  14.126 151.180 0.75 9.25  ? 408 HOH B O     1 
HETATM 7723 O  O     . HOH O 5 .   ? 34.193  6.803  119.695 0.75 10.14 ? 409 HOH B O     1 
HETATM 7724 O  O     . HOH O 5 .   ? 40.806  10.818 126.931 0.75 18.10 ? 410 HOH B O     1 
HETATM 7725 O  O     . HOH O 5 .   ? 36.778  11.449 123.221 0.75 9.13  ? 411 HOH B O     1 
HETATM 7726 O  O     . HOH O 5 .   ? 8.307   19.208 121.190 0.75 3.30  ? 412 HOH B O     1 
HETATM 7727 O  O     . HOH O 5 .   ? 13.590  16.227 154.158 0.75 3.52  ? 413 HOH B O     1 
HETATM 7728 O  O     . HOH O 5 .   ? 19.707  20.561 151.847 0.75 15.96 ? 414 HOH B O     1 
HETATM 7729 O  O     . HOH O 5 .   ? 6.916   10.998 159.468 0.75 21.23 ? 415 HOH B O     1 
HETATM 7730 O  O     . HOH O 5 .   ? 5.572   13.616 145.615 1.00 0.00  ? 416 HOH B O     1 
HETATM 7731 O  O     . HOH O 5 .   ? 27.684  26.240 152.485 0.75 10.42 ? 417 HOH B O     1 
HETATM 7732 O  O     . HOH O 5 .   ? 30.851  29.388 149.558 0.75 27.03 ? 418 HOH B O     1 
HETATM 7733 O  O     . HOH O 5 .   ? 4.729   17.891 129.294 0.75 3.69  ? 419 HOH B O     1 
HETATM 7734 O  O     . HOH O 5 .   ? 31.409  11.782 142.436 0.75 8.03  ? 420 HOH B O     1 
HETATM 7735 O  O     . HOH O 5 .   ? 41.014  8.628  145.197 0.75 19.98 ? 421 HOH B O     1 
HETATM 7736 O  O     . HOH O 5 .   ? 39.650  2.735  144.206 0.75 19.29 ? 422 HOH B O     1 
HETATM 7737 O  O     . HOH O 5 .   ? 43.020  4.746  145.543 0.75 24.77 ? 423 HOH B O     1 
HETATM 7738 O  O     . HOH O 5 .   ? 43.811  2.967  141.358 0.75 16.80 ? 424 HOH B O     1 
HETATM 7739 O  O     . HOH O 5 .   ? 27.528  33.620 127.141 0.75 3.33  ? 425 HOH B O     1 
HETATM 7740 O  O     . HOH O 5 .   ? 10.419  38.436 110.586 0.75 20.79 ? 426 HOH B O     1 
HETATM 7741 O  O     . HOH O 5 .   ? 4.544   37.493 108.921 0.75 11.80 ? 427 HOH B O     1 
HETATM 7742 O  O     . HOH O 5 .   ? 4.980   31.113 107.605 0.75 21.97 ? 428 HOH B O     1 
HETATM 7743 O  O     . HOH O 5 .   ? -2.615  20.183 145.261 0.75 7.94  ? 429 HOH B O     1 
HETATM 7744 O  O     . HOH O 5 .   ? -0.124  31.897 118.571 0.75 6.55  ? 430 HOH B O     1 
HETATM 7745 O  O     . HOH O 5 .   ? -2.958  23.621 140.772 0.75 20.04 ? 431 HOH B O     1 
HETATM 7746 O  O     . HOH O 5 .   ? 5.012   12.798 110.121 0.75 14.27 ? 432 HOH B O     1 
HETATM 7747 O  O     . HOH O 5 .   ? 8.402   12.629 110.302 0.75 12.59 ? 433 HOH B O     1 
HETATM 7748 O  O     . HOH O 5 .   ? 30.842  2.999  119.168 0.75 18.44 ? 434 HOH B O     1 
HETATM 7749 O  O     . HOH P 5 .   ? -27.536 26.606 150.163 0.75 10.38 ? 366 HOH C O     1 
HETATM 7750 O  O     . HOH P 5 .   ? -37.467 4.888  143.310 0.75 10.48 ? 367 HOH C O     1 
HETATM 7751 O  O     . HOH P 5 .   ? -15.312 1.089  137.334 0.75 6.69  ? 368 HOH C O     1 
HETATM 7752 O  O     . HOH P 5 .   ? -17.514 1.792  139.059 0.75 10.11 ? 369 HOH C O     1 
HETATM 7753 O  O     . HOH P 5 .   ? 8.671   0.437  130.960 0.75 4.99  ? 370 HOH C O     1 
HETATM 7754 O  O     . HOH P 5 .   ? -9.287  8.472  111.375 0.75 6.56  ? 371 HOH C O     1 
HETATM 7755 O  O     . HOH P 5 .   ? -13.487 16.438 123.467 0.75 3.89  ? 372 HOH C O     1 
HETATM 7756 O  O     . HOH P 5 .   ? -6.191  4.225  119.554 0.75 19.80 ? 373 HOH C O     1 
HETATM 7757 O  O     . HOH P 5 .   ? -39.781 24.627 140.482 0.75 25.00 ? 374 HOH C O     1 
HETATM 7758 O  O     . HOH P 5 .   ? -15.249 -2.164 112.012 0.75 14.36 ? 375 HOH C O     1 
HETATM 7759 O  O     . HOH P 5 .   ? -13.814 1.586  112.336 0.75 18.87 ? 376 HOH C O     1 
HETATM 7760 O  O     . HOH P 5 .   ? 1.105   17.436 119.077 0.75 2.00  ? 377 HOH C O     1 
HETATM 7761 O  O     . HOH P 5 .   ? -7.409  12.092 120.424 0.75 2.00  ? 378 HOH C O     1 
HETATM 7762 O  O     . HOH P 5 .   ? 9.402   13.155 124.928 0.75 12.11 ? 379 HOH C O     1 
HETATM 7763 O  O     . HOH P 5 .   ? -21.389 -1.347 125.698 0.75 6.78  ? 380 HOH C O     1 
HETATM 7764 O  O     . HOH P 5 .   ? -30.406 9.343  141.408 0.75 2.92  ? 381 HOH C O     1 
HETATM 7765 O  O     . HOH P 5 .   ? -30.031 6.348  146.638 0.75 16.27 ? 382 HOH C O     1 
HETATM 7766 O  O     . HOH P 5 .   ? -42.401 13.464 149.897 0.75 16.50 ? 383 HOH C O     1 
HETATM 7767 O  O     . HOH P 5 .   ? -43.799 14.764 136.300 0.75 16.12 ? 384 HOH C O     1 
HETATM 7768 O  O     . HOH P 5 .   ? -41.465 17.027 133.318 0.75 5.72  ? 385 HOH C O     1 
HETATM 7769 O  O     . HOH P 5 .   ? -24.979 5.999  141.032 0.75 8.95  ? 386 HOH C O     1 
HETATM 7770 O  O     . HOH P 5 .   ? -32.826 20.514 147.690 0.75 13.84 ? 387 HOH C O     1 
HETATM 7771 O  O     . HOH P 5 .   ? -35.461 22.452 132.186 0.75 26.62 ? 388 HOH C O     1 
HETATM 7772 O  O     . HOH P 5 .   ? -37.726 27.992 137.349 0.75 10.69 ? 389 HOH C O     1 
HETATM 7773 O  O     . HOH P 5 .   ? -40.133 28.674 140.558 0.75 13.92 ? 390 HOH C O     1 
HETATM 7774 O  O     . HOH P 5 .   ? -42.629 26.997 142.997 0.75 18.50 ? 391 HOH C O     1 
HETATM 7775 O  O     . HOH P 5 .   ? -23.022 5.049  142.643 0.75 8.21  ? 392 HOH C O     1 
HETATM 7776 O  O     . HOH P 5 .   ? -17.632 5.856  143.868 0.75 16.91 ? 393 HOH C O     1 
HETATM 7777 O  O     . HOH P 5 .   ? -20.727 7.480  152.613 0.75 18.27 ? 394 HOH C O     1 
HETATM 7778 O  O     . HOH P 5 .   ? -6.835  -2.628 142.472 0.75 15.99 ? 395 HOH C O     1 
HETATM 7779 O  O     . HOH P 5 .   ? -5.473  4.268  155.399 0.75 22.51 ? 396 HOH C O     1 
HETATM 7780 O  O     . HOH P 5 .   ? -10.110 6.206  153.986 0.75 18.94 ? 397 HOH C O     1 
HETATM 7781 O  O     . HOH P 5 .   ? -18.158 23.458 124.214 0.75 10.05 ? 398 HOH C O     1 
HETATM 7782 O  O     . HOH P 5 .   ? -20.201 26.567 126.795 0.75 6.87  ? 399 HOH C O     1 
HETATM 7783 O  O     . HOH P 5 .   ? -15.559 13.874 135.982 0.75 14.81 ? 400 HOH C O     1 
HETATM 7784 O  O     . HOH P 5 .   ? -7.664  24.994 136.584 0.75 12.86 ? 401 HOH C O     1 
HETATM 7785 O  O     . HOH P 5 .   ? -24.241 30.559 145.281 0.75 14.30 ? 402 HOH C O     1 
HETATM 7786 O  O     . HOH P 5 .   ? -28.851 30.120 142.464 0.75 16.31 ? 403 HOH C O     1 
HETATM 7787 O  O     . HOH P 5 .   ? -31.826 32.672 146.321 0.75 17.06 ? 404 HOH C O     1 
HETATM 7788 O  O     . HOH P 5 .   ? -28.646 30.657 147.191 0.75 20.36 ? 405 HOH C O     1 
HETATM 7789 O  O     . HOH P 5 .   ? -32.745 20.457 121.128 0.75 12.73 ? 406 HOH C O     1 
HETATM 7790 O  O     . HOH P 5 .   ? -42.382 11.979 122.900 0.75 16.73 ? 407 HOH C O     1 
HETATM 7791 O  O     . HOH P 5 .   ? -5.234  20.201 129.842 0.75 11.88 ? 408 HOH C O     1 
HETATM 7792 O  O     . HOH P 5 .   ? -13.629 26.812 121.380 0.75 8.69  ? 409 HOH C O     1 
HETATM 7793 O  O     . HOH P 5 .   ? -3.756  19.320 137.306 0.75 5.96  ? 410 HOH C O     1 
HETATM 7794 O  O     . HOH P 5 .   ? 0.361   22.222 137.635 0.75 10.24 ? 411 HOH C O     1 
HETATM 7795 O  O     . HOH P 5 .   ? -15.313 18.994 154.104 0.75 13.37 ? 412 HOH C O     1 
HETATM 7796 O  O     . HOH P 5 .   ? -13.125 12.642 159.031 0.75 28.45 ? 413 HOH C O     1 
HETATM 7797 O  O     . HOH P 5 .   ? -15.814 11.571 154.853 0.75 17.72 ? 414 HOH C O     1 
HETATM 7798 O  O     . HOH P 5 .   ? -13.698 15.251 155.928 0.75 20.70 ? 415 HOH C O     1 
HETATM 7799 O  O     . HOH P 5 .   ? -21.778 15.364 153.871 0.75 18.35 ? 416 HOH C O     1 
HETATM 7800 O  O     . HOH P 5 .   ? -9.723  15.220 159.772 0.75 17.82 ? 417 HOH C O     1 
HETATM 7801 O  O     . HOH P 5 .   ? -16.342 2.440  146.234 0.75 13.90 ? 418 HOH C O     1 
HETATM 7802 O  O     . HOH P 5 .   ? -20.390 10.689 150.732 0.75 7.48  ? 419 HOH C O     1 
HETATM 7803 O  O     . HOH P 5 .   ? -23.903 9.709  149.809 0.75 28.24 ? 420 HOH C O     1 
HETATM 7804 O  O     . HOH P 5 .   ? -15.308 25.879 126.508 0.75 15.89 ? 421 HOH C O     1 
HETATM 7805 O  O     . HOH P 5 .   ? -45.827 12.609 134.082 0.75 11.40 ? 422 HOH C O     1 
HETATM 7806 O  O     . HOH P 5 .   ? 2.892   4.098  119.365 0.75 13.54 ? 423 HOH C O     1 
HETATM 7807 O  O     . HOH P 5 .   ? -0.536  12.973 106.749 0.75 10.80 ? 424 HOH C O     1 
HETATM 7808 O  O     . HOH P 5 .   ? 0.709   23.066 109.520 0.75 20.53 ? 425 HOH C O     1 
HETATM 7809 O  O     . HOH P 5 .   ? -5.356  27.670 105.474 0.75 20.53 ? 426 HOH C O     1 
HETATM 7810 O  O     . HOH P 5 .   ? -20.061 32.549 111.742 0.75 18.98 ? 427 HOH C O     1 
HETATM 7811 O  O     . HOH P 5 .   ? -40.148 10.666 150.190 0.75 18.00 ? 428 HOH C O     1 
HETATM 7812 O  O     . HOH P 5 .   ? -44.202 8.661  146.905 0.75 18.00 ? 429 HOH C O     1 
HETATM 7813 O  O     . HOH P 5 .   ? -26.902 13.047 115.743 0.75 18.00 ? 430 HOH C O     1 
HETATM 7814 O  O     . HOH Q 5 .   ? -20.161 7.203  110.263 0.75 11.47 ? 204 HOH F O     1 
HETATM 7815 O  O     . HOH Q 5 .   ? -16.860 6.939  107.735 0.75 11.68 ? 205 HOH F O     1 
HETATM 7816 O  O     . HOH Q 5 .   ? -21.468 3.532  109.475 0.75 18.23 ? 206 HOH F O     1 
HETATM 7817 O  O     . HOH Q 5 .   ? -26.598 21.065 114.264 0.75 8.16  ? 267 HOH F O     1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   U   1   1   1   U   U   N . n 
A 1 2   C   2   2   2   C   C   N . n 
A 1 3   U   3   3   3   U   U   N . n 
A 1 4   U   4   4   4   U   U   N . n 
A 1 5   A   5   5   5   A   A   N . n 
A 1 6   U   6   6   6   U   U   N . n 
A 1 7   A   7   7   7   A   A   N . n 
A 1 8   U   8   8   8   U   U   N . n 
A 1 9   C   9   9   9   C   C   N . n 
A 1 10  U   10  10  10  U   U   N . n 
B 2 1   MET 1   1   ?   ?   ?   A . n 
B 2 2   VAL 2   2   ?   ?   ?   A . n 
B 2 3   ARG 3   3   ?   ?   ?   A . n 
B 2 4   ASN 4   4   ?   ?   ?   A . n 
B 2 5   ASN 5   5   ?   ?   ?   A . n 
B 2 6   ASN 6   6   ?   ?   ?   A . n 
B 2 7   ARG 7   7   ?   ?   ?   A . n 
B 2 8   ARG 8   8   ?   ?   ?   A . n 
B 2 9   ARG 9   9   ?   ?   ?   A . n 
B 2 10  GLN 10  10  ?   ?   ?   A . n 
B 2 11  ARG 11  11  ?   ?   ?   A . n 
B 2 12  THR 12  12  ?   ?   ?   A . n 
B 2 13  GLN 13  13  ?   ?   ?   A . n 
B 2 14  ARG 14  14  ?   ?   ?   A . n 
B 2 15  ILE 15  15  ?   ?   ?   A . n 
B 2 16  VAL 16  16  ?   ?   ?   A . n 
B 2 17  THR 17  17  ?   ?   ?   A . n 
B 2 18  THR 18  18  ?   ?   ?   A . n 
B 2 19  THR 19  19  ?   ?   ?   A . n 
B 2 20  THR 20  20  ?   ?   ?   A . n 
B 2 21  GLN 21  21  ?   ?   ?   A . n 
B 2 22  THR 22  22  ?   ?   ?   A . n 
B 2 23  ALA 23  23  ?   ?   ?   A . n 
B 2 24  PRO 24  24  ?   ?   ?   A . n 
B 2 25  VAL 25  25  ?   ?   ?   A . n 
B 2 26  PRO 26  26  ?   ?   ?   A . n 
B 2 27  GLN 27  27  ?   ?   ?   A . n 
B 2 28  GLN 28  28  ?   ?   ?   A . n 
B 2 29  ASN 29  29  ?   ?   ?   A . n 
B 2 30  VAL 30  30  ?   ?   ?   A . n 
B 2 31  PRO 31  31  ?   ?   ?   A . n 
B 2 32  LYS 32  32  ?   ?   ?   A . n 
B 2 33  GLN 33  33  ?   ?   ?   A . n 
B 2 34  PRO 34  34  ?   ?   ?   A . n 
B 2 35  ARG 35  35  ?   ?   ?   A . n 
B 2 36  ARG 36  36  ?   ?   ?   A . n 
B 2 37  ARG 37  37  ?   ?   ?   A . n 
B 2 38  ARG 38  38  ?   ?   ?   A . n 
B 2 39  ASN 39  39  ?   ?   ?   A . n 
B 2 40  ARG 40  40  ?   ?   ?   A . n 
B 2 41  ALA 41  41  ?   ?   ?   A . n 
B 2 42  ARG 42  42  ?   ?   ?   A . n 
B 2 43  ARG 43  43  ?   ?   ?   A . n 
B 2 44  ASN 44  44  ?   ?   ?   A . n 
B 2 45  ARG 45  45  ?   ?   ?   A . n 
B 2 46  ARG 46  46  ?   ?   ?   A . n 
B 2 47  GLN 47  47  ?   ?   ?   A . n 
B 2 48  GLY 48  48  ?   ?   ?   A . n 
B 2 49  ARG 49  49  ?   ?   ?   A . n 
B 2 50  ALA 50  50  ?   ?   ?   A . n 
B 2 51  MET 51  51  ?   ?   ?   A . n 
B 2 52  ASN 52  52  ?   ?   ?   A . n 
B 2 53  MET 53  53  ?   ?   ?   A . n 
B 2 54  GLY 54  54  ?   ?   ?   A . n 
B 2 55  ALA 55  55  ?   ?   ?   A . n 
B 2 56  LEU 56  56  56  LEU LEU A . n 
B 2 57  THR 57  57  57  THR THR A . n 
B 2 58  ARG 58  58  58  ARG ARG A . n 
B 2 59  LEU 59  59  59  LEU LEU A . n 
B 2 60  SER 60  60  60  SER SER A . n 
B 2 61  GLN 61  61  61  GLN GLN A . n 
B 2 62  PRO 62  62  62  PRO PRO A . n 
B 2 63  GLY 63  63  63  GLY GLY A . n 
B 2 64  LEU 64  64  64  LEU LEU A . n 
B 2 65  ALA 65  65  65  ALA ALA A . n 
B 2 66  PHE 66  66  66  PHE PHE A . n 
B 2 67  LEU 67  67  67  LEU LEU A . n 
B 2 68  LYS 68  68  68  LYS LYS A . n 
B 2 69  CYS 69  69  69  CYS CYS A . n 
B 2 70  ALA 70  70  70  ALA ALA A . n 
B 2 71  PHE 71  71  71  PHE PHE A . n 
B 2 72  ALA 72  72  72  ALA ALA A . n 
B 2 73  PRO 73  73  73  PRO PRO A . n 
B 2 74  PRO 74  74  74  PRO PRO A . n 
B 2 75  ASP 75  75  75  ASP ASP A . n 
B 2 76  PHE 76  76  76  PHE PHE A . n 
B 2 77  ASN 77  77  77  ASN ASN A . n 
B 2 78  THR 78  78  78  THR THR A . n 
B 2 79  ASP 79  79  79  ASP ASP A . n 
B 2 80  PRO 80  80  80  PRO PRO A . n 
B 2 81  GLY 81  81  81  GLY GLY A . n 
B 2 82  LYS 82  82  82  LYS LYS A . n 
B 2 83  GLY 83  83  83  GLY GLY A . n 
B 2 84  ILE 84  84  84  ILE ILE A . n 
B 2 85  PRO 85  85  85  PRO PRO A . n 
B 2 86  ASP 86  86  86  ASP ASP A . n 
B 2 87  ARG 87  87  87  ARG ARG A . n 
B 2 88  PHE 88  88  88  PHE PHE A . n 
B 2 89  GLU 89  89  89  GLU GLU A . n 
B 2 90  GLY 90  90  90  GLY GLY A . n 
B 2 91  LYS 91  91  91  LYS LYS A . n 
B 2 92  VAL 92  92  92  VAL VAL A . n 
B 2 93  VAL 93  93  93  VAL VAL A . n 
B 2 94  THR 94  94  94  THR THR A . n 
B 2 95  ARG 95  95  95  ARG ARG A . n 
B 2 96  LYS 96  96  96  LYS LYS A . n 
B 2 97  ASP 97  97  97  ASP ASP A . n 
B 2 98  VAL 98  98  98  VAL VAL A . n 
B 2 99  LEU 99  99  99  LEU LEU A . n 
B 2 100 ASN 100 100 100 ASN ASN A . n 
B 2 101 GLN 101 101 101 GLN GLN A . n 
B 2 102 SER 102 102 102 SER SER A . n 
B 2 103 ILE 103 103 103 ILE ILE A . n 
B 2 104 ASN 104 104 104 ASN ASN A . n 
B 2 105 PHE 105 105 105 PHE PHE A . n 
B 2 106 THR 106 106 106 THR THR A . n 
B 2 107 ALA 107 107 107 ALA ALA A . n 
B 2 108 ASN 108 108 108 ASN ASN A . n 
B 2 109 ARG 109 109 109 ARG ARG A . n 
B 2 110 ASP 110 110 110 ASP ASP A . n 
B 2 111 THR 111 111 111 THR THR A . n 
B 2 112 PHE 112 112 112 PHE PHE A . n 
B 2 113 ILE 113 113 113 ILE ILE A . n 
B 2 114 LEU 114 114 114 LEU LEU A . n 
B 2 115 ILE 115 115 115 ILE ILE A . n 
B 2 116 ALA 116 116 116 ALA ALA A . n 
B 2 117 PRO 117 117 117 PRO PRO A . n 
B 2 118 THR 118 118 118 THR THR A . n 
B 2 119 PRO 119 119 119 PRO PRO A . n 
B 2 120 GLY 120 120 120 GLY GLY A . n 
B 2 121 VAL 121 121 121 VAL VAL A . n 
B 2 122 ALA 122 122 122 ALA ALA A . n 
B 2 123 TYR 123 123 123 TYR TYR A . n 
B 2 124 TRP 124 124 124 TRP TRP A . n 
B 2 125 VAL 125 125 125 VAL VAL A . n 
B 2 126 ALA 126 126 126 ALA ALA A . n 
B 2 127 ASP 127 127 127 ASP ASP A . n 
B 2 128 VAL 128 128 128 VAL VAL A . n 
B 2 129 PRO 129 129 129 PRO PRO A . n 
B 2 130 ALA 130 130 130 ALA ALA A . n 
B 2 131 GLY 131 131 131 GLY GLY A . n 
B 2 132 THR 132 132 132 THR THR A . n 
B 2 133 PHE 133 133 133 PHE PHE A . n 
B 2 134 PRO 134 134 134 PRO PRO A . n 
B 2 135 ILE 135 135 135 ILE ILE A . n 
B 2 136 SER 136 136 136 SER SER A . n 
B 2 137 THR 137 137 137 THR THR A . n 
B 2 138 THR 138 138 138 THR THR A . n 
B 2 139 THR 139 139 139 THR THR A . n 
B 2 140 PHE 140 140 140 PHE PHE A . n 
B 2 141 ASN 141 141 141 ASN ASN A . n 
B 2 142 ALA 142 142 142 ALA ALA A . n 
B 2 143 VAL 143 143 143 VAL VAL A . n 
B 2 144 ASN 144 144 144 ASN ASN A . n 
B 2 145 PHE 145 145 145 PHE PHE A . n 
B 2 146 PRO 146 146 146 PRO PRO A . n 
B 2 147 GLY 147 147 147 GLY GLY A . n 
B 2 148 PHE 148 148 148 PHE PHE A . n 
B 2 149 ASN 149 149 149 ASN ASN A . n 
B 2 150 SER 150 150 150 SER SER A . n 
B 2 151 MET 151 151 151 MET MET A . n 
B 2 152 PHE 152 152 152 PHE PHE A . n 
B 2 153 GLY 153 153 153 GLY GLY A . n 
B 2 154 ASN 154 154 154 ASN ASN A . n 
B 2 155 ALA 155 155 155 ALA ALA A . n 
B 2 156 ALA 156 156 156 ALA ALA A . n 
B 2 157 ALA 157 157 157 ALA ALA A . n 
B 2 158 SER 158 158 158 SER SER A . n 
B 2 159 ARG 159 159 159 ARG ARG A . n 
B 2 160 SER 160 160 160 SER SER A . n 
B 2 161 ASP 161 161 161 ASP ASP A . n 
B 2 162 GLN 162 162 162 GLN GLN A . n 
B 2 163 VAL 163 163 163 VAL VAL A . n 
B 2 164 SER 164 164 164 SER SER A . n 
B 2 165 SER 165 165 165 SER SER A . n 
B 2 166 PHE 166 166 166 PHE PHE A . n 
B 2 167 ARG 167 167 167 ARG ARG A . n 
B 2 168 TYR 168 168 168 TYR TYR A . n 
B 2 169 ALA 169 169 169 ALA ALA A . n 
B 2 170 SER 170 170 170 SER SER A . n 
B 2 171 MET 171 171 171 MET MET A . n 
B 2 172 ASN 172 172 172 ASN ASN A . n 
B 2 173 VAL 173 173 173 VAL VAL A . n 
B 2 174 GLY 174 174 174 GLY GLY A . n 
B 2 175 ILE 175 175 175 ILE ILE A . n 
B 2 176 TYR 176 176 176 TYR TYR A . n 
B 2 177 PRO 177 177 177 PRO PRO A . n 
B 2 178 THR 178 178 178 THR THR A . n 
B 2 179 SER 179 179 179 SER SER A . n 
B 2 180 ASN 180 180 180 ASN ASN A . n 
B 2 181 LEU 181 181 181 LEU LEU A . n 
B 2 182 MET 182 182 182 MET MET A . n 
B 2 183 GLN 183 183 183 GLN GLN A . n 
B 2 184 PHE 184 184 184 PHE PHE A . n 
B 2 185 ALA 185 185 185 ALA ALA A . n 
B 2 186 GLY 186 186 186 GLY GLY A . n 
B 2 187 SER 187 187 187 SER SER A . n 
B 2 188 ILE 188 188 188 ILE ILE A . n 
B 2 189 THR 189 189 189 THR THR A . n 
B 2 190 VAL 190 190 190 VAL VAL A . n 
B 2 191 TRP 191 191 191 TRP TRP A . n 
B 2 192 LYS 192 192 192 LYS LYS A . n 
B 2 193 CYS 193 193 193 CYS CYS A . n 
B 2 194 PRO 194 194 194 PRO PRO A . n 
B 2 195 VAL 195 195 195 VAL VAL A . n 
B 2 196 LYS 196 196 196 LYS LYS A . n 
B 2 197 LEU 197 197 197 LEU LEU A . n 
B 2 198 SER 198 198 198 SER SER A . n 
B 2 199 ASN 199 199 199 ASN ASN A . n 
B 2 200 VAL 200 200 200 VAL VAL A . n 
B 2 201 GLN 201 201 201 GLN GLN A . n 
B 2 202 PHE 202 202 202 PHE PHE A . n 
B 2 203 PRO 203 203 203 PRO PRO A . n 
B 2 204 VAL 204 204 204 VAL VAL A . n 
B 2 205 ALA 205 205 205 ALA ALA A . n 
B 2 206 THR 206 206 206 THR THR A . n 
B 2 207 THR 207 207 207 THR THR A . n 
B 2 208 PRO 208 208 208 PRO PRO A . n 
B 2 209 ALA 209 209 209 ALA ALA A . n 
B 2 210 THR 210 210 210 THR THR A . n 
B 2 211 SER 211 211 211 SER SER A . n 
B 2 212 ALA 212 212 212 ALA ALA A . n 
B 2 213 LEU 213 213 213 LEU LEU A . n 
B 2 214 VAL 214 214 214 VAL VAL A . n 
B 2 215 HIS 215 215 215 HIS HIS A . n 
B 2 216 THR 216 216 216 THR THR A . n 
B 2 217 LEU 217 217 217 LEU LEU A . n 
B 2 218 VAL 218 218 218 VAL VAL A . n 
B 2 219 GLY 219 219 219 GLY GLY A . n 
B 2 220 LEU 220 220 220 LEU LEU A . n 
B 2 221 ASP 221 221 221 ASP ASP A . n 
B 2 222 GLY 222 222 222 GLY GLY A . n 
B 2 223 VAL 223 223 223 VAL VAL A . n 
B 2 224 LEU 224 224 224 LEU LEU A . n 
B 2 225 ALA 225 225 225 ALA ALA A . n 
B 2 226 VAL 226 226 226 VAL VAL A . n 
B 2 227 GLY 227 227 227 GLY GLY A . n 
B 2 228 PRO 228 228 228 PRO PRO A . n 
B 2 229 ASP 229 229 229 ASP ASP A . n 
B 2 230 ASN 230 230 230 ASN ASN A . n 
B 2 231 PHE 231 231 231 PHE PHE A . n 
B 2 232 SER 232 232 232 SER SER A . n 
B 2 233 GLU 233 233 233 GLU GLU A . n 
B 2 234 SER 234 234 234 SER SER A . n 
B 2 235 PHE 235 235 235 PHE PHE A . n 
B 2 236 ILE 236 236 236 ILE ILE A . n 
B 2 237 LYS 237 237 237 LYS LYS A . n 
B 2 238 GLY 238 238 238 GLY GLY A . n 
B 2 239 VAL 239 239 239 VAL VAL A . n 
B 2 240 PHE 240 240 240 PHE PHE A . n 
B 2 241 SER 241 241 241 SER SER A . n 
B 2 242 GLN 242 242 242 GLN GLN A . n 
B 2 243 SER 243 243 243 SER SER A . n 
B 2 244 VAL 244 244 244 VAL VAL A . n 
B 2 245 CYS 245 245 245 CYS CYS A . n 
B 2 246 ASN 246 246 246 ASN ASN A . n 
B 2 247 GLU 247 247 247 GLU GLU A . n 
B 2 248 PRO 248 248 248 PRO PRO A . n 
B 2 249 ASP 249 249 249 ASP ASP A . n 
B 2 250 PHE 250 250 250 PHE PHE A . n 
B 2 251 GLU 251 251 251 GLU GLU A . n 
B 2 252 PHE 252 252 252 PHE PHE A . n 
B 2 253 SER 253 253 253 SER SER A . n 
B 2 254 ASP 254 254 254 ASP ASP A . n 
B 2 255 ILE 255 255 255 ILE ILE A . n 
B 2 256 LEU 256 256 256 LEU LEU A . n 
B 2 257 GLU 257 257 257 GLU GLU A . n 
B 2 258 GLY 258 258 258 GLY GLY A . n 
B 2 259 ILE 259 259 259 ILE ILE A . n 
B 2 260 GLN 260 260 260 GLN GLN A . n 
B 2 261 THR 261 261 261 THR THR A . n 
B 2 262 LEU 262 262 262 LEU LEU A . n 
B 2 263 PRO 263 263 263 PRO PRO A . n 
B 2 264 PRO 264 264 264 PRO PRO A . n 
B 2 265 ALA 265 265 265 ALA ALA A . n 
B 2 266 ASN 266 266 266 ASN ASN A . n 
B 2 267 VAL 267 267 267 VAL VAL A . n 
B 2 268 THR 268 268 268 THR THR A . n 
B 2 269 VAL 269 269 269 VAL VAL A . n 
B 2 270 ALA 270 270 270 ALA ALA A . n 
B 2 271 THR 271 271 271 THR THR A . n 
B 2 272 SER 272 272 272 SER SER A . n 
B 2 273 GLY 273 273 273 GLY GLY A . n 
B 2 274 GLN 274 274 274 GLN GLN A . n 
B 2 275 PRO 275 275 275 PRO PRO A . n 
B 2 276 PHE 276 276 276 PHE PHE A . n 
B 2 277 ASN 277 277 277 ASN ASN A . n 
B 2 278 LEU 278 278 278 LEU LEU A . n 
B 2 279 ALA 279 279 279 ALA ALA A . n 
B 2 280 ALA 280 280 280 ALA ALA A . n 
B 2 281 GLY 281 281 281 GLY GLY A . n 
B 2 282 ALA 282 282 282 ALA ALA A . n 
B 2 283 GLU 283 283 283 GLU GLU A . n 
B 2 284 ALA 284 284 284 ALA ALA A . n 
B 2 285 VAL 285 285 285 VAL VAL A . n 
B 2 286 SER 286 286 286 SER SER A . n 
B 2 287 GLY 287 287 287 GLY GLY A . n 
B 2 288 ILE 288 288 288 ILE ILE A . n 
B 2 289 VAL 289 289 289 VAL VAL A . n 
B 2 290 GLY 290 290 290 GLY GLY A . n 
B 2 291 TRP 291 291 291 TRP TRP A . n 
B 2 292 GLY 292 292 292 GLY GLY A . n 
B 2 293 ASN 293 293 293 ASN ASN A . n 
B 2 294 MET 294 294 294 MET MET A . n 
B 2 295 ASP 295 295 295 ASP ASP A . n 
B 2 296 THR 296 296 296 THR THR A . n 
B 2 297 ILE 297 297 297 ILE ILE A . n 
B 2 298 VAL 298 298 298 VAL VAL A . n 
B 2 299 ILE 299 299 299 ILE ILE A . n 
B 2 300 ARG 300 300 300 ARG ARG A . n 
B 2 301 VAL 301 301 301 VAL VAL A . n 
B 2 302 SER 302 302 302 SER SER A . n 
B 2 303 ALA 303 303 303 ALA ALA A . n 
B 2 304 PRO 304 304 304 PRO PRO A . n 
B 2 305 THR 305 305 305 THR THR A . n 
B 2 306 GLY 306 306 306 GLY GLY A . n 
B 2 307 ALA 307 307 307 ALA ALA A . n 
B 2 308 VAL 308 308 308 VAL VAL A . n 
B 2 309 ASN 309 309 309 ASN ASN A . n 
B 2 310 SER 310 310 310 SER SER A . n 
B 2 311 ALA 311 311 311 ALA ALA A . n 
B 2 312 ILE 312 312 312 ILE ILE A . n 
B 2 313 LEU 313 313 313 LEU LEU A . n 
B 2 314 LYS 314 314 314 LYS LYS A . n 
B 2 315 THR 315 315 315 THR THR A . n 
B 2 316 TRP 316 316 316 TRP TRP A . n 
B 2 317 ALA 317 317 317 ALA ALA A . n 
B 2 318 CYS 318 318 318 CYS CYS A . n 
B 2 319 LEU 319 319 319 LEU LEU A . n 
B 2 320 GLU 320 320 320 GLU GLU A . n 
B 2 321 TYR 321 321 321 TYR TYR A . n 
B 2 322 ARG 322 322 322 ARG ARG A . n 
B 2 323 PRO 323 323 323 PRO PRO A . n 
B 2 324 ASN 324 324 324 ASN ASN A . n 
B 2 325 PRO 325 325 325 PRO PRO A . n 
B 2 326 ASN 326 326 326 ASN ASN A . n 
B 2 327 ALA 327 327 327 ALA ALA A . n 
B 2 328 MET 328 328 328 MET MET A . n 
B 2 329 LEU 329 329 329 LEU LEU A . n 
B 2 330 TYR 330 330 330 TYR TYR A . n 
B 2 331 GLN 331 331 331 GLN GLN A . n 
B 2 332 PHE 332 332 332 PHE PHE A . n 
B 2 333 GLY 333 333 333 GLY GLY A . n 
B 2 334 HIS 334 334 334 HIS HIS A . n 
B 2 335 ASP 335 335 335 ASP ASP A . n 
B 2 336 SER 336 336 336 SER SER A . n 
B 2 337 PRO 337 337 337 PRO PRO A . n 
B 2 338 PRO 338 338 338 PRO PRO A . n 
B 2 339 CYS 339 339 339 CYS CYS A . n 
B 2 340 ASP 340 340 340 ASP ASP A . n 
B 2 341 GLU 341 341 341 GLU GLU A . n 
B 2 342 VAL 342 342 342 VAL VAL A . n 
B 2 343 ALA 343 343 343 ALA ALA A . n 
B 2 344 LEU 344 344 344 LEU LEU A . n 
B 2 345 GLN 345 345 345 GLN GLN A . n 
B 2 346 GLU 346 346 346 GLU GLU A . n 
B 2 347 TYR 347 347 347 TYR TYR A . n 
B 2 348 ARG 348 348 348 ARG ARG A . n 
B 2 349 THR 349 349 349 THR THR A . n 
B 2 350 VAL 350 350 350 VAL VAL A . n 
B 2 351 ALA 351 351 351 ALA ALA A . n 
B 2 352 ARG 352 352 352 ARG ARG A . n 
B 2 353 SER 353 353 353 SER SER A . n 
B 2 354 LEU 354 354 354 LEU LEU A . n 
B 2 355 PRO 355 355 355 PRO PRO A . n 
B 2 356 VAL 356 356 356 VAL VAL A . n 
B 2 357 ALA 357 357 357 ALA ALA A . n 
B 2 358 VAL 358 358 358 VAL VAL A . n 
B 2 359 ILE 359 359 359 ILE ILE A . n 
B 2 360 ALA 360 360 360 ALA ALA A . n 
B 2 361 ALA 361 361 361 ALA ALA A . n 
B 2 362 GLN 362 362 362 GLN GLN A . n 
B 2 363 ASN 363 363 363 ASN ASN A . n 
C 3 1   ALA 1   364 364 ALA ALA D . n 
C 3 2   SER 2   365 365 SER SER D . n 
C 3 3   MET 3   366 366 MET MET D . n 
C 3 4   TRP 4   367 367 TRP TRP D . n 
C 3 5   GLU 5   368 368 GLU GLU D . n 
C 3 6   ARG 6   369 369 ARG ARG D . n 
C 3 7   VAL 7   370 370 VAL VAL D . n 
C 3 8   LYS 8   371 371 LYS LYS D . n 
C 3 9   SER 9   372 372 SER SER D . n 
C 3 10  ILE 10  373 373 ILE ILE D . n 
C 3 11  ILE 11  374 374 ILE ILE D . n 
C 3 12  LYS 12  375 375 LYS LYS D . n 
C 3 13  SER 13  376 376 SER SER D . n 
C 3 14  SER 14  377 377 SER SER D . n 
C 3 15  LEU 15  378 378 LEU LEU D . n 
C 3 16  ALA 16  379 379 ALA ALA D . n 
C 3 17  MET 17  380 ?   ?   ?   D . n 
C 3 18  ALA 18  381 ?   ?   ?   D . n 
C 3 19  SER 19  382 ?   ?   ?   D . n 
C 3 20  ASN 20  383 ?   ?   ?   D . n 
C 3 21  VAL 21  384 ?   ?   ?   D . n 
C 3 22  PRO 22  385 ?   ?   ?   D . n 
C 3 23  GLY 23  386 ?   ?   ?   D . n 
C 3 24  PRO 24  387 ?   ?   ?   D . n 
C 3 25  ILE 25  388 ?   ?   ?   D . n 
C 3 26  GLY 26  389 ?   ?   ?   D . n 
C 3 27  ILE 27  390 ?   ?   ?   D . n 
C 3 28  ALA 28  391 ?   ?   ?   D . n 
C 3 29  ALA 29  392 ?   ?   ?   D . n 
C 3 30  SER 30  393 ?   ?   ?   D . n 
C 3 31  GLY 31  394 ?   ?   ?   D . n 
C 3 32  LEU 32  395 ?   ?   ?   D . n 
C 3 33  SER 33  396 ?   ?   ?   D . n 
C 3 34  GLY 34  397 ?   ?   ?   D . n 
C 3 35  LEU 35  398 ?   ?   ?   D . n 
C 3 36  SER 36  399 ?   ?   ?   D . n 
C 3 37  ALA 37  400 ?   ?   ?   D . n 
C 3 38  LEU 38  401 ?   ?   ?   D . n 
C 3 39  PHE 39  402 ?   ?   ?   D . n 
C 3 40  GLU 40  403 ?   ?   ?   D . n 
C 3 41  GLY 41  404 ?   ?   ?   D . n 
C 3 42  PHE 42  405 ?   ?   ?   D . n 
C 3 43  GLY 43  406 ?   ?   ?   D . n 
C 3 44  PHE 44  407 ?   ?   ?   D . n 
D 2 1   MET 1   1   ?   ?   ?   B . n 
D 2 2   VAL 2   2   ?   ?   ?   B . n 
D 2 3   ARG 3   3   ?   ?   ?   B . n 
D 2 4   ASN 4   4   ?   ?   ?   B . n 
D 2 5   ASN 5   5   ?   ?   ?   B . n 
D 2 6   ASN 6   6   ?   ?   ?   B . n 
D 2 7   ARG 7   7   ?   ?   ?   B . n 
D 2 8   ARG 8   8   ?   ?   ?   B . n 
D 2 9   ARG 9   9   ?   ?   ?   B . n 
D 2 10  GLN 10  10  ?   ?   ?   B . n 
D 2 11  ARG 11  11  ?   ?   ?   B . n 
D 2 12  THR 12  12  ?   ?   ?   B . n 
D 2 13  GLN 13  13  ?   ?   ?   B . n 
D 2 14  ARG 14  14  ?   ?   ?   B . n 
D 2 15  ILE 15  15  ?   ?   ?   B . n 
D 2 16  VAL 16  16  ?   ?   ?   B . n 
D 2 17  THR 17  17  ?   ?   ?   B . n 
D 2 18  THR 18  18  ?   ?   ?   B . n 
D 2 19  THR 19  19  ?   ?   ?   B . n 
D 2 20  THR 20  20  ?   ?   ?   B . n 
D 2 21  GLN 21  21  ?   ?   ?   B . n 
D 2 22  THR 22  22  ?   ?   ?   B . n 
D 2 23  ALA 23  23  ?   ?   ?   B . n 
D 2 24  PRO 24  24  ?   ?   ?   B . n 
D 2 25  VAL 25  25  ?   ?   ?   B . n 
D 2 26  PRO 26  26  ?   ?   ?   B . n 
D 2 27  GLN 27  27  ?   ?   ?   B . n 
D 2 28  GLN 28  28  ?   ?   ?   B . n 
D 2 29  ASN 29  29  ?   ?   ?   B . n 
D 2 30  VAL 30  30  ?   ?   ?   B . n 
D 2 31  PRO 31  31  ?   ?   ?   B . n 
D 2 32  LYS 32  32  ?   ?   ?   B . n 
D 2 33  GLN 33  33  ?   ?   ?   B . n 
D 2 34  PRO 34  34  ?   ?   ?   B . n 
D 2 35  ARG 35  35  ?   ?   ?   B . n 
D 2 36  ARG 36  36  ?   ?   ?   B . n 
D 2 37  ARG 37  37  ?   ?   ?   B . n 
D 2 38  ARG 38  38  ?   ?   ?   B . n 
D 2 39  ASN 39  39  ?   ?   ?   B . n 
D 2 40  ARG 40  40  ?   ?   ?   B . n 
D 2 41  ALA 41  41  ?   ?   ?   B . n 
D 2 42  ARG 42  42  ?   ?   ?   B . n 
D 2 43  ARG 43  43  ?   ?   ?   B . n 
D 2 44  ASN 44  44  ?   ?   ?   B . n 
D 2 45  ARG 45  45  ?   ?   ?   B . n 
D 2 46  ARG 46  46  ?   ?   ?   B . n 
D 2 47  GLN 47  47  ?   ?   ?   B . n 
D 2 48  GLY 48  48  ?   ?   ?   B . n 
D 2 49  ARG 49  49  ?   ?   ?   B . n 
D 2 50  ALA 50  50  ?   ?   ?   B . n 
D 2 51  MET 51  51  ?   ?   ?   B . n 
D 2 52  ASN 52  52  ?   ?   ?   B . n 
D 2 53  MET 53  53  ?   ?   ?   B . n 
D 2 54  GLY 54  54  ?   ?   ?   B . n 
D 2 55  ALA 55  55  ?   ?   ?   B . n 
D 2 56  LEU 56  56  56  LEU LEU B . n 
D 2 57  THR 57  57  57  THR THR B . n 
D 2 58  ARG 58  58  58  ARG ARG B . n 
D 2 59  LEU 59  59  59  LEU LEU B . n 
D 2 60  SER 60  60  60  SER SER B . n 
D 2 61  GLN 61  61  61  GLN GLN B . n 
D 2 62  PRO 62  62  62  PRO PRO B . n 
D 2 63  GLY 63  63  63  GLY GLY B . n 
D 2 64  LEU 64  64  64  LEU LEU B . n 
D 2 65  ALA 65  65  65  ALA ALA B . n 
D 2 66  PHE 66  66  66  PHE PHE B . n 
D 2 67  LEU 67  67  67  LEU LEU B . n 
D 2 68  LYS 68  68  68  LYS LYS B . n 
D 2 69  CYS 69  69  69  CYS CYS B . n 
D 2 70  ALA 70  70  70  ALA ALA B . n 
D 2 71  PHE 71  71  71  PHE PHE B . n 
D 2 72  ALA 72  72  72  ALA ALA B . n 
D 2 73  PRO 73  73  73  PRO PRO B . n 
D 2 74  PRO 74  74  74  PRO PRO B . n 
D 2 75  ASP 75  75  75  ASP ASP B . n 
D 2 76  PHE 76  76  76  PHE PHE B . n 
D 2 77  ASN 77  77  77  ASN ASN B . n 
D 2 78  THR 78  78  78  THR THR B . n 
D 2 79  ASP 79  79  79  ASP ASP B . n 
D 2 80  PRO 80  80  80  PRO PRO B . n 
D 2 81  GLY 81  81  81  GLY GLY B . n 
D 2 82  LYS 82  82  82  LYS LYS B . n 
D 2 83  GLY 83  83  83  GLY GLY B . n 
D 2 84  ILE 84  84  84  ILE ILE B . n 
D 2 85  PRO 85  85  85  PRO PRO B . n 
D 2 86  ASP 86  86  86  ASP ASP B . n 
D 2 87  ARG 87  87  87  ARG ARG B . n 
D 2 88  PHE 88  88  88  PHE PHE B . n 
D 2 89  GLU 89  89  89  GLU GLU B . n 
D 2 90  GLY 90  90  90  GLY GLY B . n 
D 2 91  LYS 91  91  91  LYS LYS B . n 
D 2 92  VAL 92  92  92  VAL VAL B . n 
D 2 93  VAL 93  93  93  VAL VAL B . n 
D 2 94  THR 94  94  94  THR THR B . n 
D 2 95  ARG 95  95  95  ARG ARG B . n 
D 2 96  LYS 96  96  96  LYS LYS B . n 
D 2 97  ASP 97  97  97  ASP ASP B . n 
D 2 98  VAL 98  98  98  VAL VAL B . n 
D 2 99  LEU 99  99  99  LEU LEU B . n 
D 2 100 ASN 100 100 100 ASN ASN B . n 
D 2 101 GLN 101 101 101 GLN GLN B . n 
D 2 102 SER 102 102 102 SER SER B . n 
D 2 103 ILE 103 103 103 ILE ILE B . n 
D 2 104 ASN 104 104 104 ASN ASN B . n 
D 2 105 PHE 105 105 105 PHE PHE B . n 
D 2 106 THR 106 106 106 THR THR B . n 
D 2 107 ALA 107 107 107 ALA ALA B . n 
D 2 108 ASN 108 108 108 ASN ASN B . n 
D 2 109 ARG 109 109 109 ARG ARG B . n 
D 2 110 ASP 110 110 110 ASP ASP B . n 
D 2 111 THR 111 111 111 THR THR B . n 
D 2 112 PHE 112 112 112 PHE PHE B . n 
D 2 113 ILE 113 113 113 ILE ILE B . n 
D 2 114 LEU 114 114 114 LEU LEU B . n 
D 2 115 ILE 115 115 115 ILE ILE B . n 
D 2 116 ALA 116 116 116 ALA ALA B . n 
D 2 117 PRO 117 117 117 PRO PRO B . n 
D 2 118 THR 118 118 118 THR THR B . n 
D 2 119 PRO 119 119 119 PRO PRO B . n 
D 2 120 GLY 120 120 120 GLY GLY B . n 
D 2 121 VAL 121 121 121 VAL VAL B . n 
D 2 122 ALA 122 122 122 ALA ALA B . n 
D 2 123 TYR 123 123 123 TYR TYR B . n 
D 2 124 TRP 124 124 124 TRP TRP B . n 
D 2 125 VAL 125 125 125 VAL VAL B . n 
D 2 126 ALA 126 126 126 ALA ALA B . n 
D 2 127 ASP 127 127 127 ASP ASP B . n 
D 2 128 VAL 128 128 128 VAL VAL B . n 
D 2 129 PRO 129 129 129 PRO PRO B . n 
D 2 130 ALA 130 130 130 ALA ALA B . n 
D 2 131 GLY 131 131 131 GLY GLY B . n 
D 2 132 THR 132 132 132 THR THR B . n 
D 2 133 PHE 133 133 133 PHE PHE B . n 
D 2 134 PRO 134 134 134 PRO PRO B . n 
D 2 135 ILE 135 135 135 ILE ILE B . n 
D 2 136 SER 136 136 136 SER SER B . n 
D 2 137 THR 137 137 137 THR THR B . n 
D 2 138 THR 138 138 138 THR THR B . n 
D 2 139 THR 139 139 139 THR THR B . n 
D 2 140 PHE 140 140 140 PHE PHE B . n 
D 2 141 ASN 141 141 141 ASN ASN B . n 
D 2 142 ALA 142 142 142 ALA ALA B . n 
D 2 143 VAL 143 143 143 VAL VAL B . n 
D 2 144 ASN 144 144 144 ASN ASN B . n 
D 2 145 PHE 145 145 145 PHE PHE B . n 
D 2 146 PRO 146 146 146 PRO PRO B . n 
D 2 147 GLY 147 147 147 GLY GLY B . n 
D 2 148 PHE 148 148 148 PHE PHE B . n 
D 2 149 ASN 149 149 149 ASN ASN B . n 
D 2 150 SER 150 150 150 SER SER B . n 
D 2 151 MET 151 151 151 MET MET B . n 
D 2 152 PHE 152 152 152 PHE PHE B . n 
D 2 153 GLY 153 153 153 GLY GLY B . n 
D 2 154 ASN 154 154 154 ASN ASN B . n 
D 2 155 ALA 155 155 155 ALA ALA B . n 
D 2 156 ALA 156 156 156 ALA ALA B . n 
D 2 157 ALA 157 157 157 ALA ALA B . n 
D 2 158 SER 158 158 158 SER SER B . n 
D 2 159 ARG 159 159 159 ARG ARG B . n 
D 2 160 SER 160 160 160 SER SER B . n 
D 2 161 ASP 161 161 161 ASP ASP B . n 
D 2 162 GLN 162 162 162 GLN GLN B . n 
D 2 163 VAL 163 163 163 VAL VAL B . n 
D 2 164 SER 164 164 164 SER SER B . n 
D 2 165 SER 165 165 165 SER SER B . n 
D 2 166 PHE 166 166 166 PHE PHE B . n 
D 2 167 ARG 167 167 167 ARG ARG B . n 
D 2 168 TYR 168 168 168 TYR TYR B . n 
D 2 169 ALA 169 169 169 ALA ALA B . n 
D 2 170 SER 170 170 170 SER SER B . n 
D 2 171 MET 171 171 171 MET MET B . n 
D 2 172 ASN 172 172 172 ASN ASN B . n 
D 2 173 VAL 173 173 173 VAL VAL B . n 
D 2 174 GLY 174 174 174 GLY GLY B . n 
D 2 175 ILE 175 175 175 ILE ILE B . n 
D 2 176 TYR 176 176 176 TYR TYR B . n 
D 2 177 PRO 177 177 177 PRO PRO B . n 
D 2 178 THR 178 178 178 THR THR B . n 
D 2 179 SER 179 179 179 SER SER B . n 
D 2 180 ASN 180 180 180 ASN ASN B . n 
D 2 181 LEU 181 181 181 LEU LEU B . n 
D 2 182 MET 182 182 182 MET MET B . n 
D 2 183 GLN 183 183 183 GLN GLN B . n 
D 2 184 PHE 184 184 184 PHE PHE B . n 
D 2 185 ALA 185 185 185 ALA ALA B . n 
D 2 186 GLY 186 186 186 GLY GLY B . n 
D 2 187 SER 187 187 187 SER SER B . n 
D 2 188 ILE 188 188 188 ILE ILE B . n 
D 2 189 THR 189 189 189 THR THR B . n 
D 2 190 VAL 190 190 190 VAL VAL B . n 
D 2 191 TRP 191 191 191 TRP TRP B . n 
D 2 192 LYS 192 192 192 LYS LYS B . n 
D 2 193 CYS 193 193 193 CYS CYS B . n 
D 2 194 PRO 194 194 194 PRO PRO B . n 
D 2 195 VAL 195 195 195 VAL VAL B . n 
D 2 196 LYS 196 196 196 LYS LYS B . n 
D 2 197 LEU 197 197 197 LEU LEU B . n 
D 2 198 SER 198 198 198 SER SER B . n 
D 2 199 ASN 199 199 199 ASN ASN B . n 
D 2 200 VAL 200 200 200 VAL VAL B . n 
D 2 201 GLN 201 201 201 GLN GLN B . n 
D 2 202 PHE 202 202 202 PHE PHE B . n 
D 2 203 PRO 203 203 203 PRO PRO B . n 
D 2 204 VAL 204 204 204 VAL VAL B . n 
D 2 205 ALA 205 205 205 ALA ALA B . n 
D 2 206 THR 206 206 206 THR THR B . n 
D 2 207 THR 207 207 207 THR THR B . n 
D 2 208 PRO 208 208 208 PRO PRO B . n 
D 2 209 ALA 209 209 209 ALA ALA B . n 
D 2 210 THR 210 210 210 THR THR B . n 
D 2 211 SER 211 211 211 SER SER B . n 
D 2 212 ALA 212 212 212 ALA ALA B . n 
D 2 213 LEU 213 213 213 LEU LEU B . n 
D 2 214 VAL 214 214 214 VAL VAL B . n 
D 2 215 HIS 215 215 215 HIS HIS B . n 
D 2 216 THR 216 216 216 THR THR B . n 
D 2 217 LEU 217 217 217 LEU LEU B . n 
D 2 218 VAL 218 218 218 VAL VAL B . n 
D 2 219 GLY 219 219 219 GLY GLY B . n 
D 2 220 LEU 220 220 220 LEU LEU B . n 
D 2 221 ASP 221 221 221 ASP ASP B . n 
D 2 222 GLY 222 222 222 GLY GLY B . n 
D 2 223 VAL 223 223 223 VAL VAL B . n 
D 2 224 LEU 224 224 224 LEU LEU B . n 
D 2 225 ALA 225 225 225 ALA ALA B . n 
D 2 226 VAL 226 226 226 VAL VAL B . n 
D 2 227 GLY 227 227 227 GLY GLY B . n 
D 2 228 PRO 228 228 228 PRO PRO B . n 
D 2 229 ASP 229 229 229 ASP ASP B . n 
D 2 230 ASN 230 230 230 ASN ASN B . n 
D 2 231 PHE 231 231 231 PHE PHE B . n 
D 2 232 SER 232 232 232 SER SER B . n 
D 2 233 GLU 233 233 233 GLU GLU B . n 
D 2 234 SER 234 234 234 SER SER B . n 
D 2 235 PHE 235 235 235 PHE PHE B . n 
D 2 236 ILE 236 236 236 ILE ILE B . n 
D 2 237 LYS 237 237 237 LYS LYS B . n 
D 2 238 GLY 238 238 238 GLY GLY B . n 
D 2 239 VAL 239 239 239 VAL VAL B . n 
D 2 240 PHE 240 240 240 PHE PHE B . n 
D 2 241 SER 241 241 241 SER SER B . n 
D 2 242 GLN 242 242 242 GLN GLN B . n 
D 2 243 SER 243 243 243 SER SER B . n 
D 2 244 VAL 244 244 244 VAL VAL B . n 
D 2 245 CYS 245 245 245 CYS CYS B . n 
D 2 246 ASN 246 246 246 ASN ASN B . n 
D 2 247 GLU 247 247 247 GLU GLU B . n 
D 2 248 PRO 248 248 248 PRO PRO B . n 
D 2 249 ASP 249 249 249 ASP ASP B . n 
D 2 250 PHE 250 250 250 PHE PHE B . n 
D 2 251 GLU 251 251 251 GLU GLU B . n 
D 2 252 PHE 252 252 252 PHE PHE B . n 
D 2 253 SER 253 253 253 SER SER B . n 
D 2 254 ASP 254 254 254 ASP ASP B . n 
D 2 255 ILE 255 255 255 ILE ILE B . n 
D 2 256 LEU 256 256 256 LEU LEU B . n 
D 2 257 GLU 257 257 257 GLU GLU B . n 
D 2 258 GLY 258 258 258 GLY GLY B . n 
D 2 259 ILE 259 259 259 ILE ILE B . n 
D 2 260 GLN 260 260 260 GLN GLN B . n 
D 2 261 THR 261 261 261 THR THR B . n 
D 2 262 LEU 262 262 262 LEU LEU B . n 
D 2 263 PRO 263 263 263 PRO PRO B . n 
D 2 264 PRO 264 264 264 PRO PRO B . n 
D 2 265 ALA 265 265 265 ALA ALA B . n 
D 2 266 ASN 266 266 266 ASN ASN B . n 
D 2 267 VAL 267 267 267 VAL VAL B . n 
D 2 268 THR 268 268 268 THR THR B . n 
D 2 269 VAL 269 269 269 VAL VAL B . n 
D 2 270 ALA 270 270 270 ALA ALA B . n 
D 2 271 THR 271 271 271 THR THR B . n 
D 2 272 SER 272 272 272 SER SER B . n 
D 2 273 GLY 273 273 273 GLY GLY B . n 
D 2 274 GLN 274 274 274 GLN GLN B . n 
D 2 275 PRO 275 275 275 PRO PRO B . n 
D 2 276 PHE 276 276 276 PHE PHE B . n 
D 2 277 ASN 277 277 277 ASN ASN B . n 
D 2 278 LEU 278 278 278 LEU LEU B . n 
D 2 279 ALA 279 279 279 ALA ALA B . n 
D 2 280 ALA 280 280 280 ALA ALA B . n 
D 2 281 GLY 281 281 281 GLY GLY B . n 
D 2 282 ALA 282 282 282 ALA ALA B . n 
D 2 283 GLU 283 283 283 GLU GLU B . n 
D 2 284 ALA 284 284 284 ALA ALA B . n 
D 2 285 VAL 285 285 285 VAL VAL B . n 
D 2 286 SER 286 286 286 SER SER B . n 
D 2 287 GLY 287 287 287 GLY GLY B . n 
D 2 288 ILE 288 288 288 ILE ILE B . n 
D 2 289 VAL 289 289 289 VAL VAL B . n 
D 2 290 GLY 290 290 290 GLY GLY B . n 
D 2 291 TRP 291 291 291 TRP TRP B . n 
D 2 292 GLY 292 292 292 GLY GLY B . n 
D 2 293 ASN 293 293 293 ASN ASN B . n 
D 2 294 MET 294 294 294 MET MET B . n 
D 2 295 ASP 295 295 295 ASP ASP B . n 
D 2 296 THR 296 296 296 THR THR B . n 
D 2 297 ILE 297 297 297 ILE ILE B . n 
D 2 298 VAL 298 298 298 VAL VAL B . n 
D 2 299 ILE 299 299 299 ILE ILE B . n 
D 2 300 ARG 300 300 300 ARG ARG B . n 
D 2 301 VAL 301 301 301 VAL VAL B . n 
D 2 302 SER 302 302 302 SER SER B . n 
D 2 303 ALA 303 303 303 ALA ALA B . n 
D 2 304 PRO 304 304 304 PRO PRO B . n 
D 2 305 THR 305 305 305 THR THR B . n 
D 2 306 GLY 306 306 306 GLY GLY B . n 
D 2 307 ALA 307 307 307 ALA ALA B . n 
D 2 308 VAL 308 308 308 VAL VAL B . n 
D 2 309 ASN 309 309 309 ASN ASN B . n 
D 2 310 SER 310 310 310 SER SER B . n 
D 2 311 ALA 311 311 311 ALA ALA B . n 
D 2 312 ILE 312 312 312 ILE ILE B . n 
D 2 313 LEU 313 313 313 LEU LEU B . n 
D 2 314 LYS 314 314 314 LYS LYS B . n 
D 2 315 THR 315 315 315 THR THR B . n 
D 2 316 TRP 316 316 316 TRP TRP B . n 
D 2 317 ALA 317 317 317 ALA ALA B . n 
D 2 318 CYS 318 318 318 CYS CYS B . n 
D 2 319 LEU 319 319 319 LEU LEU B . n 
D 2 320 GLU 320 320 320 GLU GLU B . n 
D 2 321 TYR 321 321 321 TYR TYR B . n 
D 2 322 ARG 322 322 322 ARG ARG B . n 
D 2 323 PRO 323 323 323 PRO PRO B . n 
D 2 324 ASN 324 324 324 ASN ASN B . n 
D 2 325 PRO 325 325 325 PRO PRO B . n 
D 2 326 ASN 326 326 326 ASN ASN B . n 
D 2 327 ALA 327 327 327 ALA ALA B . n 
D 2 328 MET 328 328 328 MET MET B . n 
D 2 329 LEU 329 329 329 LEU LEU B . n 
D 2 330 TYR 330 330 330 TYR TYR B . n 
D 2 331 GLN 331 331 331 GLN GLN B . n 
D 2 332 PHE 332 332 332 PHE PHE B . n 
D 2 333 GLY 333 333 333 GLY GLY B . n 
D 2 334 HIS 334 334 334 HIS HIS B . n 
D 2 335 ASP 335 335 335 ASP ASP B . n 
D 2 336 SER 336 336 336 SER SER B . n 
D 2 337 PRO 337 337 337 PRO PRO B . n 
D 2 338 PRO 338 338 338 PRO PRO B . n 
D 2 339 CYS 339 339 339 CYS CYS B . n 
D 2 340 ASP 340 340 340 ASP ASP B . n 
D 2 341 GLU 341 341 341 GLU GLU B . n 
D 2 342 VAL 342 342 342 VAL VAL B . n 
D 2 343 ALA 343 343 343 ALA ALA B . n 
D 2 344 LEU 344 344 344 LEU LEU B . n 
D 2 345 GLN 345 345 345 GLN GLN B . n 
D 2 346 GLU 346 346 346 GLU GLU B . n 
D 2 347 TYR 347 347 347 TYR TYR B . n 
D 2 348 ARG 348 348 348 ARG ARG B . n 
D 2 349 THR 349 349 349 THR THR B . n 
D 2 350 VAL 350 350 350 VAL VAL B . n 
D 2 351 ALA 351 351 351 ALA ALA B . n 
D 2 352 ARG 352 352 352 ARG ARG B . n 
D 2 353 SER 353 353 353 SER SER B . n 
D 2 354 LEU 354 354 354 LEU LEU B . n 
D 2 355 PRO 355 355 355 PRO PRO B . n 
D 2 356 VAL 356 356 356 VAL VAL B . n 
D 2 357 ALA 357 357 357 ALA ALA B . n 
D 2 358 VAL 358 358 358 VAL VAL B . n 
D 2 359 ILE 359 359 359 ILE ILE B . n 
D 2 360 ALA 360 360 360 ALA ALA B . n 
D 2 361 ALA 361 361 361 ALA ALA B . n 
D 2 362 GLN 362 362 362 GLN GLN B . n 
D 2 363 ASN 363 363 363 ASN ASN B . n 
E 3 1   ALA 1   364 364 ALA ALA E . n 
E 3 2   SER 2   365 365 SER SER E . n 
E 3 3   MET 3   366 366 MET MET E . n 
E 3 4   TRP 4   367 367 TRP TRP E . n 
E 3 5   GLU 5   368 368 GLU GLU E . n 
E 3 6   ARG 6   369 369 ARG ARG E . n 
E 3 7   VAL 7   370 370 VAL VAL E . n 
E 3 8   LYS 8   371 371 LYS LYS E . n 
E 3 9   SER 9   372 372 SER SER E . n 
E 3 10  ILE 10  373 373 ILE ILE E . n 
E 3 11  ILE 11  374 374 ILE ILE E . n 
E 3 12  LYS 12  375 375 LYS LYS E . n 
E 3 13  SER 13  376 376 SER SER E . n 
E 3 14  SER 14  377 377 SER SER E . n 
E 3 15  LEU 15  378 378 LEU LEU E . n 
E 3 16  ALA 16  379 379 ALA ALA E . n 
E 3 17  MET 17  380 ?   ?   ?   E . n 
E 3 18  ALA 18  381 ?   ?   ?   E . n 
E 3 19  SER 19  382 ?   ?   ?   E . n 
E 3 20  ASN 20  383 ?   ?   ?   E . n 
E 3 21  VAL 21  384 ?   ?   ?   E . n 
E 3 22  PRO 22  385 ?   ?   ?   E . n 
E 3 23  GLY 23  386 ?   ?   ?   E . n 
E 3 24  PRO 24  387 ?   ?   ?   E . n 
E 3 25  ILE 25  388 ?   ?   ?   E . n 
E 3 26  GLY 26  389 ?   ?   ?   E . n 
E 3 27  ILE 27  390 ?   ?   ?   E . n 
E 3 28  ALA 28  391 ?   ?   ?   E . n 
E 3 29  ALA 29  392 ?   ?   ?   E . n 
E 3 30  SER 30  393 ?   ?   ?   E . n 
E 3 31  GLY 31  394 ?   ?   ?   E . n 
E 3 32  LEU 32  395 ?   ?   ?   E . n 
E 3 33  SER 33  396 ?   ?   ?   E . n 
E 3 34  GLY 34  397 ?   ?   ?   E . n 
E 3 35  LEU 35  398 ?   ?   ?   E . n 
E 3 36  SER 36  399 ?   ?   ?   E . n 
E 3 37  ALA 37  400 ?   ?   ?   E . n 
E 3 38  LEU 38  401 ?   ?   ?   E . n 
E 3 39  PHE 39  402 ?   ?   ?   E . n 
E 3 40  GLU 40  403 ?   ?   ?   E . n 
E 3 41  GLY 41  404 ?   ?   ?   E . n 
E 3 42  PHE 42  405 ?   ?   ?   E . n 
E 3 43  GLY 43  406 ?   ?   ?   E . n 
E 3 44  PHE 44  407 ?   ?   ?   E . n 
F 2 1   MET 1   1   ?   ?   ?   C . n 
F 2 2   VAL 2   2   ?   ?   ?   C . n 
F 2 3   ARG 3   3   ?   ?   ?   C . n 
F 2 4   ASN 4   4   ?   ?   ?   C . n 
F 2 5   ASN 5   5   ?   ?   ?   C . n 
F 2 6   ASN 6   6   ?   ?   ?   C . n 
F 2 7   ARG 7   7   ?   ?   ?   C . n 
F 2 8   ARG 8   8   ?   ?   ?   C . n 
F 2 9   ARG 9   9   ?   ?   ?   C . n 
F 2 10  GLN 10  10  ?   ?   ?   C . n 
F 2 11  ARG 11  11  ?   ?   ?   C . n 
F 2 12  THR 12  12  ?   ?   ?   C . n 
F 2 13  GLN 13  13  ?   ?   ?   C . n 
F 2 14  ARG 14  14  ?   ?   ?   C . n 
F 2 15  ILE 15  15  ?   ?   ?   C . n 
F 2 16  VAL 16  16  ?   ?   ?   C . n 
F 2 17  THR 17  17  ?   ?   ?   C . n 
F 2 18  THR 18  18  ?   ?   ?   C . n 
F 2 19  THR 19  19  ?   ?   ?   C . n 
F 2 20  THR 20  20  20  THR THR C . n 
F 2 21  GLN 21  21  21  GLN GLN C . n 
F 2 22  THR 22  22  22  THR THR C . n 
F 2 23  ALA 23  23  23  ALA ALA C . n 
F 2 24  PRO 24  24  24  PRO PRO C . n 
F 2 25  VAL 25  25  25  VAL VAL C . n 
F 2 26  PRO 26  26  26  PRO PRO C . n 
F 2 27  GLN 27  27  27  GLN GLN C . n 
F 2 28  GLN 28  28  28  GLN GLN C . n 
F 2 29  ASN 29  29  29  ASN ASN C . n 
F 2 30  VAL 30  30  30  VAL VAL C . n 
F 2 31  PRO 31  31  31  PRO PRO C . n 
F 2 32  LYS 32  32  ?   ?   ?   C . n 
F 2 33  GLN 33  33  ?   ?   ?   C . n 
F 2 34  PRO 34  34  ?   ?   ?   C . n 
F 2 35  ARG 35  35  ?   ?   ?   C . n 
F 2 36  ARG 36  36  ?   ?   ?   C . n 
F 2 37  ARG 37  37  ?   ?   ?   C . n 
F 2 38  ARG 38  38  ?   ?   ?   C . n 
F 2 39  ASN 39  39  ?   ?   ?   C . n 
F 2 40  ARG 40  40  ?   ?   ?   C . n 
F 2 41  ALA 41  41  ?   ?   ?   C . n 
F 2 42  ARG 42  42  ?   ?   ?   C . n 
F 2 43  ARG 43  43  ?   ?   ?   C . n 
F 2 44  ASN 44  44  ?   ?   ?   C . n 
F 2 45  ARG 45  45  ?   ?   ?   C . n 
F 2 46  ARG 46  46  ?   ?   ?   C . n 
F 2 47  GLN 47  47  ?   ?   ?   C . n 
F 2 48  GLY 48  48  ?   ?   ?   C . n 
F 2 49  ARG 49  49  ?   ?   ?   C . n 
F 2 50  ALA 50  50  ?   ?   ?   C . n 
F 2 51  MET 51  51  ?   ?   ?   C . n 
F 2 52  ASN 52  52  ?   ?   ?   C . n 
F 2 53  MET 53  53  ?   ?   ?   C . n 
F 2 54  GLY 54  54  ?   ?   ?   C . n 
F 2 55  ALA 55  55  55  ALA ALA C . n 
F 2 56  LEU 56  56  56  LEU LEU C . n 
F 2 57  THR 57  57  57  THR THR C . n 
F 2 58  ARG 58  58  58  ARG ARG C . n 
F 2 59  LEU 59  59  59  LEU LEU C . n 
F 2 60  SER 60  60  60  SER SER C . n 
F 2 61  GLN 61  61  61  GLN GLN C . n 
F 2 62  PRO 62  62  62  PRO PRO C . n 
F 2 63  GLY 63  63  63  GLY GLY C . n 
F 2 64  LEU 64  64  64  LEU LEU C . n 
F 2 65  ALA 65  65  65  ALA ALA C . n 
F 2 66  PHE 66  66  66  PHE PHE C . n 
F 2 67  LEU 67  67  67  LEU LEU C . n 
F 2 68  LYS 68  68  68  LYS LYS C . n 
F 2 69  CYS 69  69  69  CYS CYS C . n 
F 2 70  ALA 70  70  70  ALA ALA C . n 
F 2 71  PHE 71  71  71  PHE PHE C . n 
F 2 72  ALA 72  72  72  ALA ALA C . n 
F 2 73  PRO 73  73  73  PRO PRO C . n 
F 2 74  PRO 74  74  74  PRO PRO C . n 
F 2 75  ASP 75  75  75  ASP ASP C . n 
F 2 76  PHE 76  76  76  PHE PHE C . n 
F 2 77  ASN 77  77  77  ASN ASN C . n 
F 2 78  THR 78  78  78  THR THR C . n 
F 2 79  ASP 79  79  79  ASP ASP C . n 
F 2 80  PRO 80  80  80  PRO PRO C . n 
F 2 81  GLY 81  81  81  GLY GLY C . n 
F 2 82  LYS 82  82  82  LYS LYS C . n 
F 2 83  GLY 83  83  83  GLY GLY C . n 
F 2 84  ILE 84  84  84  ILE ILE C . n 
F 2 85  PRO 85  85  85  PRO PRO C . n 
F 2 86  ASP 86  86  86  ASP ASP C . n 
F 2 87  ARG 87  87  87  ARG ARG C . n 
F 2 88  PHE 88  88  88  PHE PHE C . n 
F 2 89  GLU 89  89  89  GLU GLU C . n 
F 2 90  GLY 90  90  90  GLY GLY C . n 
F 2 91  LYS 91  91  91  LYS LYS C . n 
F 2 92  VAL 92  92  92  VAL VAL C . n 
F 2 93  VAL 93  93  93  VAL VAL C . n 
F 2 94  THR 94  94  94  THR THR C . n 
F 2 95  ARG 95  95  95  ARG ARG C . n 
F 2 96  LYS 96  96  96  LYS LYS C . n 
F 2 97  ASP 97  97  97  ASP ASP C . n 
F 2 98  VAL 98  98  98  VAL VAL C . n 
F 2 99  LEU 99  99  99  LEU LEU C . n 
F 2 100 ASN 100 100 100 ASN ASN C . n 
F 2 101 GLN 101 101 101 GLN GLN C . n 
F 2 102 SER 102 102 102 SER SER C . n 
F 2 103 ILE 103 103 103 ILE ILE C . n 
F 2 104 ASN 104 104 104 ASN ASN C . n 
F 2 105 PHE 105 105 105 PHE PHE C . n 
F 2 106 THR 106 106 106 THR THR C . n 
F 2 107 ALA 107 107 107 ALA ALA C . n 
F 2 108 ASN 108 108 108 ASN ASN C . n 
F 2 109 ARG 109 109 109 ARG ARG C . n 
F 2 110 ASP 110 110 110 ASP ASP C . n 
F 2 111 THR 111 111 111 THR THR C . n 
F 2 112 PHE 112 112 112 PHE PHE C . n 
F 2 113 ILE 113 113 113 ILE ILE C . n 
F 2 114 LEU 114 114 114 LEU LEU C . n 
F 2 115 ILE 115 115 115 ILE ILE C . n 
F 2 116 ALA 116 116 116 ALA ALA C . n 
F 2 117 PRO 117 117 117 PRO PRO C . n 
F 2 118 THR 118 118 118 THR THR C . n 
F 2 119 PRO 119 119 119 PRO PRO C . n 
F 2 120 GLY 120 120 120 GLY GLY C . n 
F 2 121 VAL 121 121 121 VAL VAL C . n 
F 2 122 ALA 122 122 122 ALA ALA C . n 
F 2 123 TYR 123 123 123 TYR TYR C . n 
F 2 124 TRP 124 124 124 TRP TRP C . n 
F 2 125 VAL 125 125 125 VAL VAL C . n 
F 2 126 ALA 126 126 126 ALA ALA C . n 
F 2 127 ASP 127 127 127 ASP ASP C . n 
F 2 128 VAL 128 128 128 VAL VAL C . n 
F 2 129 PRO 129 129 129 PRO PRO C . n 
F 2 130 ALA 130 130 130 ALA ALA C . n 
F 2 131 GLY 131 131 131 GLY GLY C . n 
F 2 132 THR 132 132 132 THR THR C . n 
F 2 133 PHE 133 133 133 PHE PHE C . n 
F 2 134 PRO 134 134 134 PRO PRO C . n 
F 2 135 ILE 135 135 135 ILE ILE C . n 
F 2 136 SER 136 136 136 SER SER C . n 
F 2 137 THR 137 137 137 THR THR C . n 
F 2 138 THR 138 138 138 THR THR C . n 
F 2 139 THR 139 139 139 THR THR C . n 
F 2 140 PHE 140 140 140 PHE PHE C . n 
F 2 141 ASN 141 141 141 ASN ASN C . n 
F 2 142 ALA 142 142 142 ALA ALA C . n 
F 2 143 VAL 143 143 143 VAL VAL C . n 
F 2 144 ASN 144 144 144 ASN ASN C . n 
F 2 145 PHE 145 145 145 PHE PHE C . n 
F 2 146 PRO 146 146 146 PRO PRO C . n 
F 2 147 GLY 147 147 147 GLY GLY C . n 
F 2 148 PHE 148 148 148 PHE PHE C . n 
F 2 149 ASN 149 149 149 ASN ASN C . n 
F 2 150 SER 150 150 150 SER SER C . n 
F 2 151 MET 151 151 151 MET MET C . n 
F 2 152 PHE 152 152 152 PHE PHE C . n 
F 2 153 GLY 153 153 153 GLY GLY C . n 
F 2 154 ASN 154 154 154 ASN ASN C . n 
F 2 155 ALA 155 155 155 ALA ALA C . n 
F 2 156 ALA 156 156 156 ALA ALA C . n 
F 2 157 ALA 157 157 157 ALA ALA C . n 
F 2 158 SER 158 158 158 SER SER C . n 
F 2 159 ARG 159 159 159 ARG ARG C . n 
F 2 160 SER 160 160 160 SER SER C . n 
F 2 161 ASP 161 161 161 ASP ASP C . n 
F 2 162 GLN 162 162 162 GLN GLN C . n 
F 2 163 VAL 163 163 163 VAL VAL C . n 
F 2 164 SER 164 164 164 SER SER C . n 
F 2 165 SER 165 165 165 SER SER C . n 
F 2 166 PHE 166 166 166 PHE PHE C . n 
F 2 167 ARG 167 167 167 ARG ARG C . n 
F 2 168 TYR 168 168 168 TYR TYR C . n 
F 2 169 ALA 169 169 169 ALA ALA C . n 
F 2 170 SER 170 170 170 SER SER C . n 
F 2 171 MET 171 171 171 MET MET C . n 
F 2 172 ASN 172 172 172 ASN ASN C . n 
F 2 173 VAL 173 173 173 VAL VAL C . n 
F 2 174 GLY 174 174 174 GLY GLY C . n 
F 2 175 ILE 175 175 175 ILE ILE C . n 
F 2 176 TYR 176 176 176 TYR TYR C . n 
F 2 177 PRO 177 177 177 PRO PRO C . n 
F 2 178 THR 178 178 178 THR THR C . n 
F 2 179 SER 179 179 179 SER SER C . n 
F 2 180 ASN 180 180 180 ASN ASN C . n 
F 2 181 LEU 181 181 181 LEU LEU C . n 
F 2 182 MET 182 182 182 MET MET C . n 
F 2 183 GLN 183 183 183 GLN GLN C . n 
F 2 184 PHE 184 184 184 PHE PHE C . n 
F 2 185 ALA 185 185 185 ALA ALA C . n 
F 2 186 GLY 186 186 186 GLY GLY C . n 
F 2 187 SER 187 187 187 SER SER C . n 
F 2 188 ILE 188 188 188 ILE ILE C . n 
F 2 189 THR 189 189 189 THR THR C . n 
F 2 190 VAL 190 190 190 VAL VAL C . n 
F 2 191 TRP 191 191 191 TRP TRP C . n 
F 2 192 LYS 192 192 192 LYS LYS C . n 
F 2 193 CYS 193 193 193 CYS CYS C . n 
F 2 194 PRO 194 194 194 PRO PRO C . n 
F 2 195 VAL 195 195 195 VAL VAL C . n 
F 2 196 LYS 196 196 196 LYS LYS C . n 
F 2 197 LEU 197 197 197 LEU LEU C . n 
F 2 198 SER 198 198 198 SER SER C . n 
F 2 199 ASN 199 199 199 ASN ASN C . n 
F 2 200 VAL 200 200 200 VAL VAL C . n 
F 2 201 GLN 201 201 201 GLN GLN C . n 
F 2 202 PHE 202 202 202 PHE PHE C . n 
F 2 203 PRO 203 203 203 PRO PRO C . n 
F 2 204 VAL 204 204 204 VAL VAL C . n 
F 2 205 ALA 205 205 205 ALA ALA C . n 
F 2 206 THR 206 206 206 THR THR C . n 
F 2 207 THR 207 207 207 THR THR C . n 
F 2 208 PRO 208 208 208 PRO PRO C . n 
F 2 209 ALA 209 209 209 ALA ALA C . n 
F 2 210 THR 210 210 210 THR THR C . n 
F 2 211 SER 211 211 211 SER SER C . n 
F 2 212 ALA 212 212 212 ALA ALA C . n 
F 2 213 LEU 213 213 213 LEU LEU C . n 
F 2 214 VAL 214 214 214 VAL VAL C . n 
F 2 215 HIS 215 215 215 HIS HIS C . n 
F 2 216 THR 216 216 216 THR THR C . n 
F 2 217 LEU 217 217 217 LEU LEU C . n 
F 2 218 VAL 218 218 218 VAL VAL C . n 
F 2 219 GLY 219 219 219 GLY GLY C . n 
F 2 220 LEU 220 220 220 LEU LEU C . n 
F 2 221 ASP 221 221 221 ASP ASP C . n 
F 2 222 GLY 222 222 222 GLY GLY C . n 
F 2 223 VAL 223 223 223 VAL VAL C . n 
F 2 224 LEU 224 224 224 LEU LEU C . n 
F 2 225 ALA 225 225 225 ALA ALA C . n 
F 2 226 VAL 226 226 226 VAL VAL C . n 
F 2 227 GLY 227 227 227 GLY GLY C . n 
F 2 228 PRO 228 228 228 PRO PRO C . n 
F 2 229 ASP 229 229 229 ASP ASP C . n 
F 2 230 ASN 230 230 230 ASN ASN C . n 
F 2 231 PHE 231 231 231 PHE PHE C . n 
F 2 232 SER 232 232 232 SER SER C . n 
F 2 233 GLU 233 233 233 GLU GLU C . n 
F 2 234 SER 234 234 234 SER SER C . n 
F 2 235 PHE 235 235 235 PHE PHE C . n 
F 2 236 ILE 236 236 236 ILE ILE C . n 
F 2 237 LYS 237 237 237 LYS LYS C . n 
F 2 238 GLY 238 238 238 GLY GLY C . n 
F 2 239 VAL 239 239 239 VAL VAL C . n 
F 2 240 PHE 240 240 240 PHE PHE C . n 
F 2 241 SER 241 241 241 SER SER C . n 
F 2 242 GLN 242 242 242 GLN GLN C . n 
F 2 243 SER 243 243 243 SER SER C . n 
F 2 244 VAL 244 244 244 VAL VAL C . n 
F 2 245 CYS 245 245 245 CYS CYS C . n 
F 2 246 ASN 246 246 246 ASN ASN C . n 
F 2 247 GLU 247 247 247 GLU GLU C . n 
F 2 248 PRO 248 248 248 PRO PRO C . n 
F 2 249 ASP 249 249 249 ASP ASP C . n 
F 2 250 PHE 250 250 250 PHE PHE C . n 
F 2 251 GLU 251 251 251 GLU GLU C . n 
F 2 252 PHE 252 252 252 PHE PHE C . n 
F 2 253 SER 253 253 253 SER SER C . n 
F 2 254 ASP 254 254 254 ASP ASP C . n 
F 2 255 ILE 255 255 255 ILE ILE C . n 
F 2 256 LEU 256 256 256 LEU LEU C . n 
F 2 257 GLU 257 257 257 GLU GLU C . n 
F 2 258 GLY 258 258 258 GLY GLY C . n 
F 2 259 ILE 259 259 259 ILE ILE C . n 
F 2 260 GLN 260 260 260 GLN GLN C . n 
F 2 261 THR 261 261 261 THR THR C . n 
F 2 262 LEU 262 262 262 LEU LEU C . n 
F 2 263 PRO 263 263 263 PRO PRO C . n 
F 2 264 PRO 264 264 264 PRO PRO C . n 
F 2 265 ALA 265 265 265 ALA ALA C . n 
F 2 266 ASN 266 266 266 ASN ASN C . n 
F 2 267 VAL 267 267 267 VAL VAL C . n 
F 2 268 THR 268 268 268 THR THR C . n 
F 2 269 VAL 269 269 269 VAL VAL C . n 
F 2 270 ALA 270 270 270 ALA ALA C . n 
F 2 271 THR 271 271 271 THR THR C . n 
F 2 272 SER 272 272 272 SER SER C . n 
F 2 273 GLY 273 273 273 GLY GLY C . n 
F 2 274 GLN 274 274 274 GLN GLN C . n 
F 2 275 PRO 275 275 275 PRO PRO C . n 
F 2 276 PHE 276 276 276 PHE PHE C . n 
F 2 277 ASN 277 277 277 ASN ASN C . n 
F 2 278 LEU 278 278 278 LEU LEU C . n 
F 2 279 ALA 279 279 279 ALA ALA C . n 
F 2 280 ALA 280 280 280 ALA ALA C . n 
F 2 281 GLY 281 281 281 GLY GLY C . n 
F 2 282 ALA 282 282 282 ALA ALA C . n 
F 2 283 GLU 283 283 283 GLU GLU C . n 
F 2 284 ALA 284 284 284 ALA ALA C . n 
F 2 285 VAL 285 285 285 VAL VAL C . n 
F 2 286 SER 286 286 286 SER SER C . n 
F 2 287 GLY 287 287 287 GLY GLY C . n 
F 2 288 ILE 288 288 288 ILE ILE C . n 
F 2 289 VAL 289 289 289 VAL VAL C . n 
F 2 290 GLY 290 290 290 GLY GLY C . n 
F 2 291 TRP 291 291 291 TRP TRP C . n 
F 2 292 GLY 292 292 292 GLY GLY C . n 
F 2 293 ASN 293 293 293 ASN ASN C . n 
F 2 294 MET 294 294 294 MET MET C . n 
F 2 295 ASP 295 295 295 ASP ASP C . n 
F 2 296 THR 296 296 296 THR THR C . n 
F 2 297 ILE 297 297 297 ILE ILE C . n 
F 2 298 VAL 298 298 298 VAL VAL C . n 
F 2 299 ILE 299 299 299 ILE ILE C . n 
F 2 300 ARG 300 300 300 ARG ARG C . n 
F 2 301 VAL 301 301 301 VAL VAL C . n 
F 2 302 SER 302 302 302 SER SER C . n 
F 2 303 ALA 303 303 303 ALA ALA C . n 
F 2 304 PRO 304 304 304 PRO PRO C . n 
F 2 305 THR 305 305 305 THR THR C . n 
F 2 306 GLY 306 306 306 GLY GLY C . n 
F 2 307 ALA 307 307 307 ALA ALA C . n 
F 2 308 VAL 308 308 308 VAL VAL C . n 
F 2 309 ASN 309 309 309 ASN ASN C . n 
F 2 310 SER 310 310 310 SER SER C . n 
F 2 311 ALA 311 311 311 ALA ALA C . n 
F 2 312 ILE 312 312 312 ILE ILE C . n 
F 2 313 LEU 313 313 313 LEU LEU C . n 
F 2 314 LYS 314 314 314 LYS LYS C . n 
F 2 315 THR 315 315 315 THR THR C . n 
F 2 316 TRP 316 316 316 TRP TRP C . n 
F 2 317 ALA 317 317 317 ALA ALA C . n 
F 2 318 CYS 318 318 318 CYS CYS C . n 
F 2 319 LEU 319 319 319 LEU LEU C . n 
F 2 320 GLU 320 320 320 GLU GLU C . n 
F 2 321 TYR 321 321 321 TYR TYR C . n 
F 2 322 ARG 322 322 322 ARG ARG C . n 
F 2 323 PRO 323 323 323 PRO PRO C . n 
F 2 324 ASN 324 324 324 ASN ASN C . n 
F 2 325 PRO 325 325 325 PRO PRO C . n 
F 2 326 ASN 326 326 326 ASN ASN C . n 
F 2 327 ALA 327 327 327 ALA ALA C . n 
F 2 328 MET 328 328 328 MET MET C . n 
F 2 329 LEU 329 329 329 LEU LEU C . n 
F 2 330 TYR 330 330 330 TYR TYR C . n 
F 2 331 GLN 331 331 331 GLN GLN C . n 
F 2 332 PHE 332 332 332 PHE PHE C . n 
F 2 333 GLY 333 333 333 GLY GLY C . n 
F 2 334 HIS 334 334 334 HIS HIS C . n 
F 2 335 ASP 335 335 335 ASP ASP C . n 
F 2 336 SER 336 336 336 SER SER C . n 
F 2 337 PRO 337 337 337 PRO PRO C . n 
F 2 338 PRO 338 338 338 PRO PRO C . n 
F 2 339 CYS 339 339 339 CYS CYS C . n 
F 2 340 ASP 340 340 340 ASP ASP C . n 
F 2 341 GLU 341 341 341 GLU GLU C . n 
F 2 342 VAL 342 342 342 VAL VAL C . n 
F 2 343 ALA 343 343 343 ALA ALA C . n 
F 2 344 LEU 344 344 344 LEU LEU C . n 
F 2 345 GLN 345 345 345 GLN GLN C . n 
F 2 346 GLU 346 346 346 GLU GLU C . n 
F 2 347 TYR 347 347 347 TYR TYR C . n 
F 2 348 ARG 348 348 348 ARG ARG C . n 
F 2 349 THR 349 349 349 THR THR C . n 
F 2 350 VAL 350 350 350 VAL VAL C . n 
F 2 351 ALA 351 351 351 ALA ALA C . n 
F 2 352 ARG 352 352 352 ARG ARG C . n 
F 2 353 SER 353 353 353 SER SER C . n 
F 2 354 LEU 354 354 354 LEU LEU C . n 
F 2 355 PRO 355 355 355 PRO PRO C . n 
F 2 356 VAL 356 356 356 VAL VAL C . n 
F 2 357 ALA 357 357 357 ALA ALA C . n 
F 2 358 VAL 358 358 358 VAL VAL C . n 
F 2 359 ILE 359 359 359 ILE ILE C . n 
F 2 360 ALA 360 360 360 ALA ALA C . n 
F 2 361 ALA 361 361 361 ALA ALA C . n 
F 2 362 GLN 362 362 362 GLN GLN C . n 
F 2 363 ASN 363 363 363 ASN ASN C . n 
G 3 1   ALA 1   364 364 ALA ALA F . n 
G 3 2   SER 2   365 365 SER SER F . n 
G 3 3   MET 3   366 366 MET MET F . n 
G 3 4   TRP 4   367 367 TRP TRP F . n 
G 3 5   GLU 5   368 368 GLU GLU F . n 
G 3 6   ARG 6   369 369 ARG ARG F . n 
G 3 7   VAL 7   370 370 VAL VAL F . n 
G 3 8   LYS 8   371 371 LYS LYS F . n 
G 3 9   SER 9   372 372 SER SER F . n 
G 3 10  ILE 10  373 373 ILE ILE F . n 
G 3 11  ILE 11  374 374 ILE ILE F . n 
G 3 12  LYS 12  375 375 LYS LYS F . n 
G 3 13  SER 13  376 376 SER SER F . n 
G 3 14  SER 14  377 377 SER SER F . n 
G 3 15  LEU 15  378 378 LEU LEU F . n 
G 3 16  ALA 16  379 379 ALA ALA F . n 
G 3 17  MET 17  380 ?   ?   ?   F . n 
G 3 18  ALA 18  381 ?   ?   ?   F . n 
G 3 19  SER 19  382 ?   ?   ?   F . n 
G 3 20  ASN 20  383 ?   ?   ?   F . n 
G 3 21  VAL 21  384 ?   ?   ?   F . n 
G 3 22  PRO 22  385 ?   ?   ?   F . n 
G 3 23  GLY 23  386 ?   ?   ?   F . n 
G 3 24  PRO 24  387 ?   ?   ?   F . n 
G 3 25  ILE 25  388 ?   ?   ?   F . n 
G 3 26  GLY 26  389 ?   ?   ?   F . n 
G 3 27  ILE 27  390 ?   ?   ?   F . n 
G 3 28  ALA 28  391 ?   ?   ?   F . n 
G 3 29  ALA 29  392 ?   ?   ?   F . n 
G 3 30  SER 30  393 ?   ?   ?   F . n 
G 3 31  GLY 31  394 ?   ?   ?   F . n 
G 3 32  LEU 32  395 ?   ?   ?   F . n 
G 3 33  SER 33  396 ?   ?   ?   F . n 
G 3 34  GLY 34  397 ?   ?   ?   F . n 
G 3 35  LEU 35  398 ?   ?   ?   F . n 
G 3 36  SER 36  399 ?   ?   ?   F . n 
G 3 37  ALA 37  400 ?   ?   ?   F . n 
G 3 38  LEU 38  401 ?   ?   ?   F . n 
G 3 39  PHE 39  402 ?   ?   ?   F . n 
G 3 40  GLU 40  403 ?   ?   ?   F . n 
G 3 41  GLY 41  404 ?   ?   ?   F . n 
G 3 42  PHE 42  405 ?   ?   ?   F . n 
G 3 43  GLY 43  406 ?   ?   ?   F . n 
G 3 44  PHE 44  407 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
H 4 CA  1  364 1   CA  CA  A . 
I 4 CA  1  365 5   CA  CA  A . 
J 4 CA  1  364 2   CA  CA  B . 
K 4 CA  1  364 3   CA  CA  C . 
L 4 CA  1  365 4   CA  CA  C . 
M 5 HOH 1  366 1   HOH HOH A . 
M 5 HOH 2  367 2   HOH HOH A . 
M 5 HOH 3  368 3   HOH HOH A . 
M 5 HOH 4  369 4   HOH HOH A . 
M 5 HOH 5  370 5   HOH HOH A . 
M 5 HOH 6  371 6   HOH HOH A . 
M 5 HOH 7  372 7   HOH HOH A . 
M 5 HOH 8  373 8   HOH HOH A . 
M 5 HOH 9  374 9   HOH HOH A . 
M 5 HOH 10 375 10  HOH HOH A . 
M 5 HOH 11 376 11  HOH HOH A . 
M 5 HOH 12 377 12  HOH HOH A . 
M 5 HOH 13 378 13  HOH HOH A . 
M 5 HOH 14 379 14  HOH HOH A . 
M 5 HOH 15 380 15  HOH HOH A . 
M 5 HOH 16 381 16  HOH HOH A . 
M 5 HOH 17 382 17  HOH HOH A . 
M 5 HOH 18 383 18  HOH HOH A . 
M 5 HOH 19 384 19  HOH HOH A . 
M 5 HOH 20 385 20  HOH HOH A . 
M 5 HOH 21 386 21  HOH HOH A . 
M 5 HOH 22 387 22  HOH HOH A . 
M 5 HOH 23 388 23  HOH HOH A . 
M 5 HOH 24 389 25  HOH HOH A . 
M 5 HOH 25 390 26  HOH HOH A . 
M 5 HOH 26 391 27  HOH HOH A . 
M 5 HOH 27 392 29  HOH HOH A . 
M 5 HOH 28 393 30  HOH HOH A . 
M 5 HOH 29 394 31  HOH HOH A . 
M 5 HOH 30 395 32  HOH HOH A . 
M 5 HOH 31 396 33  HOH HOH A . 
M 5 HOH 32 397 34  HOH HOH A . 
M 5 HOH 33 398 35  HOH HOH A . 
M 5 HOH 34 399 36  HOH HOH A . 
M 5 HOH 35 400 37  HOH HOH A . 
M 5 HOH 36 401 38  HOH HOH A . 
M 5 HOH 37 402 39  HOH HOH A . 
M 5 HOH 38 403 40  HOH HOH A . 
M 5 HOH 39 404 41  HOH HOH A . 
M 5 HOH 40 405 42  HOH HOH A . 
M 5 HOH 41 406 43  HOH HOH A . 
M 5 HOH 42 407 44  HOH HOH A . 
M 5 HOH 43 408 45  HOH HOH A . 
M 5 HOH 44 409 46  HOH HOH A . 
M 5 HOH 45 410 47  HOH HOH A . 
M 5 HOH 46 411 48  HOH HOH A . 
M 5 HOH 47 412 49  HOH HOH A . 
M 5 HOH 48 413 50  HOH HOH A . 
M 5 HOH 49 414 52  HOH HOH A . 
M 5 HOH 50 415 53  HOH HOH A . 
M 5 HOH 51 416 54  HOH HOH A . 
M 5 HOH 52 417 55  HOH HOH A . 
M 5 HOH 53 418 56  HOH HOH A . 
M 5 HOH 54 419 57  HOH HOH A . 
M 5 HOH 55 420 58  HOH HOH A . 
M 5 HOH 56 421 59  HOH HOH A . 
M 5 HOH 57 422 60  HOH HOH A . 
M 5 HOH 58 423 62  HOH HOH A . 
M 5 HOH 59 424 63  HOH HOH A . 
M 5 HOH 60 425 66  HOH HOH A . 
M 5 HOH 61 426 68  HOH HOH A . 
M 5 HOH 62 427 69  HOH HOH A . 
M 5 HOH 63 428 71  HOH HOH A . 
M 5 HOH 64 429 131 HOH HOH A . 
M 5 HOH 65 430 138 HOH HOH A . 
M 5 HOH 66 431 151 HOH HOH A . 
M 5 HOH 67 432 232 HOH HOH A . 
M 5 HOH 68 433 235 HOH HOH A . 
N 5 HOH 1  61  61  HOH HOH D . 
O 5 HOH 1  365 28  HOH HOH B . 
O 5 HOH 2  366 51  HOH HOH B . 
O 5 HOH 3  367 64  HOH HOH B . 
O 5 HOH 4  368 65  HOH HOH B . 
O 5 HOH 5  369 67  HOH HOH B . 
O 5 HOH 6  370 70  HOH HOH B . 
O 5 HOH 7  371 101 HOH HOH B . 
O 5 HOH 8  372 102 HOH HOH B . 
O 5 HOH 9  373 103 HOH HOH B . 
O 5 HOH 10 374 104 HOH HOH B . 
O 5 HOH 11 375 105 HOH HOH B . 
O 5 HOH 12 376 106 HOH HOH B . 
O 5 HOH 13 377 107 HOH HOH B . 
O 5 HOH 14 378 108 HOH HOH B . 
O 5 HOH 15 379 109 HOH HOH B . 
O 5 HOH 16 380 110 HOH HOH B . 
O 5 HOH 17 381 111 HOH HOH B . 
O 5 HOH 18 382 112 HOH HOH B . 
O 5 HOH 19 383 114 HOH HOH B . 
O 5 HOH 20 384 115 HOH HOH B . 
O 5 HOH 21 385 116 HOH HOH B . 
O 5 HOH 22 386 117 HOH HOH B . 
O 5 HOH 23 387 118 HOH HOH B . 
O 5 HOH 24 388 119 HOH HOH B . 
O 5 HOH 25 389 121 HOH HOH B . 
O 5 HOH 26 390 123 HOH HOH B . 
O 5 HOH 27 391 124 HOH HOH B . 
O 5 HOH 28 392 125 HOH HOH B . 
O 5 HOH 29 393 126 HOH HOH B . 
O 5 HOH 30 394 127 HOH HOH B . 
O 5 HOH 31 395 128 HOH HOH B . 
O 5 HOH 32 396 129 HOH HOH B . 
O 5 HOH 33 397 130 HOH HOH B . 
O 5 HOH 34 398 132 HOH HOH B . 
O 5 HOH 35 399 133 HOH HOH B . 
O 5 HOH 36 400 134 HOH HOH B . 
O 5 HOH 37 401 135 HOH HOH B . 
O 5 HOH 38 402 136 HOH HOH B . 
O 5 HOH 39 403 137 HOH HOH B . 
O 5 HOH 40 404 139 HOH HOH B . 
O 5 HOH 41 405 140 HOH HOH B . 
O 5 HOH 42 406 141 HOH HOH B . 
O 5 HOH 43 407 142 HOH HOH B . 
O 5 HOH 44 408 143 HOH HOH B . 
O 5 HOH 45 409 145 HOH HOH B . 
O 5 HOH 46 410 146 HOH HOH B . 
O 5 HOH 47 411 147 HOH HOH B . 
O 5 HOH 48 412 148 HOH HOH B . 
O 5 HOH 49 413 149 HOH HOH B . 
O 5 HOH 50 414 150 HOH HOH B . 
O 5 HOH 51 415 152 HOH HOH B . 
O 5 HOH 52 416 153 HOH HOH B . 
O 5 HOH 53 417 154 HOH HOH B . 
O 5 HOH 54 418 155 HOH HOH B . 
O 5 HOH 55 419 156 HOH HOH B . 
O 5 HOH 56 420 157 HOH HOH B . 
O 5 HOH 57 421 158 HOH HOH B . 
O 5 HOH 58 422 159 HOH HOH B . 
O 5 HOH 59 423 160 HOH HOH B . 
O 5 HOH 60 424 161 HOH HOH B . 
O 5 HOH 61 425 162 HOH HOH B . 
O 5 HOH 62 426 163 HOH HOH B . 
O 5 HOH 63 427 164 HOH HOH B . 
O 5 HOH 64 428 165 HOH HOH B . 
O 5 HOH 65 429 236 HOH HOH B . 
O 5 HOH 66 430 246 HOH HOH B . 
O 5 HOH 67 431 248 HOH HOH B . 
O 5 HOH 68 432 262 HOH HOH B . 
O 5 HOH 69 433 263 HOH HOH B . 
O 5 HOH 70 434 269 HOH HOH B . 
P 5 HOH 1  366 24  HOH HOH C . 
P 5 HOH 2  367 113 HOH HOH C . 
P 5 HOH 3  368 120 HOH HOH C . 
P 5 HOH 4  369 122 HOH HOH C . 
P 5 HOH 5  370 144 HOH HOH C . 
P 5 HOH 6  371 201 HOH HOH C . 
P 5 HOH 7  372 202 HOH HOH C . 
P 5 HOH 8  373 203 HOH HOH C . 
P 5 HOH 9  374 207 HOH HOH C . 
P 5 HOH 10 375 208 HOH HOH C . 
P 5 HOH 11 376 209 HOH HOH C . 
P 5 HOH 12 377 210 HOH HOH C . 
P 5 HOH 13 378 211 HOH HOH C . 
P 5 HOH 14 379 212 HOH HOH C . 
P 5 HOH 15 380 213 HOH HOH C . 
P 5 HOH 16 381 214 HOH HOH C . 
P 5 HOH 17 382 215 HOH HOH C . 
P 5 HOH 18 383 216 HOH HOH C . 
P 5 HOH 19 384 217 HOH HOH C . 
P 5 HOH 20 385 218 HOH HOH C . 
P 5 HOH 21 386 219 HOH HOH C . 
P 5 HOH 22 387 220 HOH HOH C . 
P 5 HOH 23 388 221 HOH HOH C . 
P 5 HOH 24 389 222 HOH HOH C . 
P 5 HOH 25 390 223 HOH HOH C . 
P 5 HOH 26 391 224 HOH HOH C . 
P 5 HOH 27 392 225 HOH HOH C . 
P 5 HOH 28 393 226 HOH HOH C . 
P 5 HOH 29 394 227 HOH HOH C . 
P 5 HOH 30 395 228 HOH HOH C . 
P 5 HOH 31 396 229 HOH HOH C . 
P 5 HOH 32 397 230 HOH HOH C . 
P 5 HOH 33 398 231 HOH HOH C . 
P 5 HOH 34 399 233 HOH HOH C . 
P 5 HOH 35 400 234 HOH HOH C . 
P 5 HOH 36 401 237 HOH HOH C . 
P 5 HOH 37 402 238 HOH HOH C . 
P 5 HOH 38 403 239 HOH HOH C . 
P 5 HOH 39 404 240 HOH HOH C . 
P 5 HOH 40 405 241 HOH HOH C . 
P 5 HOH 41 406 242 HOH HOH C . 
P 5 HOH 42 407 243 HOH HOH C . 
P 5 HOH 43 408 244 HOH HOH C . 
P 5 HOH 44 409 245 HOH HOH C . 
P 5 HOH 45 410 247 HOH HOH C . 
P 5 HOH 46 411 249 HOH HOH C . 
P 5 HOH 47 412 250 HOH HOH C . 
P 5 HOH 48 413 251 HOH HOH C . 
P 5 HOH 49 414 252 HOH HOH C . 
P 5 HOH 50 415 253 HOH HOH C . 
P 5 HOH 51 416 254 HOH HOH C . 
P 5 HOH 52 417 255 HOH HOH C . 
P 5 HOH 53 418 256 HOH HOH C . 
P 5 HOH 54 419 257 HOH HOH C . 
P 5 HOH 55 420 258 HOH HOH C . 
P 5 HOH 56 421 259 HOH HOH C . 
P 5 HOH 57 422 260 HOH HOH C . 
P 5 HOH 58 423 261 HOH HOH C . 
P 5 HOH 59 424 264 HOH HOH C . 
P 5 HOH 60 425 265 HOH HOH C . 
P 5 HOH 61 426 266 HOH HOH C . 
P 5 HOH 62 427 268 HOH HOH C . 
P 5 HOH 63 428 270 HOH HOH C . 
P 5 HOH 64 429 281 HOH HOH C . 
P 5 HOH 65 430 282 HOH HOH C . 
Q 5 HOH 1  204 204 HOH HOH F . 
Q 5 HOH 2  205 205 HOH HOH F . 
Q 5 HOH 3  206 206 HOH HOH F . 
Q 5 HOH 4  267 267 HOH HOH F . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 'complete icosahedral assembly'                ? 420-MERIC  420 
2 'icosahedral asymmetric unit'                  ? heptameric 7   
3 'icosahedral pentamer'                         ? 35-meric   35  
4 'icosahedral 23 hexamer'                       ? 42-meric   42  
5 'icosahedral asymmetric unit, std point frame' ? heptameric 7   
6 'crystal asymmetric unit, crystal frame'       ? 35-meric   35  
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 '(1-60)'           A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
2 1                  A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
3 '(1-5)'            A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
4 '(1,2,6,10,23,24)' A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
5 P                  A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
6 '(X0)(1-5)'        A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
P  'transform to point frame'   ? ? 1.00000000  0.00000000  0.00000000  -0.00000 0.00000000  1.00000000  0.00000000  -0.00000 
0.00000000  0.00000000  1.00000000  -0.00000 
X0 'transform to crystal frame' ? ? 1.00000000  0.00000000  0.00000000  0.00000  0.00000000  1.00000000  0.00000000  0.00000  
0.00000000  0.00000000  1.00000000  0.00000  
1  'point symmetry operation'   ? ? 1.00000000  0.00000000  0.00000000  0.00000  0.00000000  1.00000000  0.00000000  0.00000  
0.00000000  0.00000000  1.00000000  0.00000  
2  'point symmetry operation'   ? ? 0.30901699  -0.80901699 0.50000000  0.00000  0.80901699  0.50000000  0.30901699  0.00000  
-0.50000000 0.30901699  0.80901699  0.00000  
3  'point symmetry operation'   ? ? -0.80901699 -0.50000000 0.30901699  0.00000  0.50000000  -0.30901699 0.80901699  0.00000  
-0.30901699 0.80901699  0.50000000  0.00000  
4  'point symmetry operation'   ? ? -0.80901699 0.50000000  -0.30901699 0.00000  -0.50000000 -0.30901699 0.80901699  0.00000  
0.30901699  0.80901699  0.50000000  0.00000  
5  'point symmetry operation'   ? ? 0.30901699  0.80901699  -0.50000000 0.00000  -0.80901699 0.50000000  0.30901699  0.00000  
0.50000000  0.30901699  0.80901699  0.00000  
6  'point symmetry operation'   ? ? -1.00000000 0.00000000  0.00000000  0.00000  0.00000000  -1.00000000 0.00000000  0.00000  
0.00000000  0.00000000  1.00000000  0.00000  
7  'point symmetry operation'   ? ? -0.30901699 0.80901699  -0.50000000 0.00000  -0.80901699 -0.50000000 -0.30901699 0.00000  
-0.50000000 0.30901699  0.80901699  0.00000  
8  'point symmetry operation'   ? ? 0.80901699  0.50000000  -0.30901699 0.00000  -0.50000000 0.30901699  -0.80901699 0.00000  
-0.30901699 0.80901699  0.50000000  0.00000  
9  'point symmetry operation'   ? ? 0.80901699  -0.50000000 0.30901699  0.00000  0.50000000  0.30901699  -0.80901699 0.00000  
0.30901699  0.80901699  0.50000000  0.00000  
10 'point symmetry operation'   ? ? -0.30901699 -0.80901699 0.50000000  0.00000  0.80901699  -0.50000000 -0.30901699 0.00000  
0.50000000  0.30901699  0.80901699  0.00000  
11 'point symmetry operation'   ? ? -1.00000000 0.00000000  0.00000000  0.00000  0.00000000  1.00000000  0.00000000  0.00000  
0.00000000  0.00000000  -1.00000000 0.00000  
12 'point symmetry operation'   ? ? -0.30901699 0.80901699  -0.50000000 0.00000  0.80901699  0.50000000  0.30901699  0.00000  
0.50000000  -0.30901699 -0.80901699 0.00000  
13 'point symmetry operation'   ? ? 0.80901699  0.50000000  -0.30901699 0.00000  0.50000000  -0.30901699 0.80901699  0.00000  
0.30901699  -0.80901699 -0.50000000 0.00000  
14 'point symmetry operation'   ? ? 0.80901699  -0.50000000 0.30901699  0.00000  -0.50000000 -0.30901699 0.80901699  0.00000  
-0.30901699 -0.80901699 -0.50000000 0.00000  
15 'point symmetry operation'   ? ? -0.30901699 -0.80901699 0.50000000  0.00000  -0.80901699 0.50000000  0.30901699  0.00000  
-0.50000000 -0.30901699 -0.80901699 0.00000  
16 'point symmetry operation'   ? ? 1.00000000  0.00000000  0.00000000  0.00000  0.00000000  -1.00000000 0.00000000  0.00000  
0.00000000  0.00000000  -1.00000000 0.00000  
17 'point symmetry operation'   ? ? 0.30901699  -0.80901699 0.50000000  0.00000  -0.80901699 -0.50000000 -0.30901699 0.00000  
0.50000000  -0.30901699 -0.80901699 0.00000  
18 'point symmetry operation'   ? ? -0.80901699 -0.50000000 0.30901699  0.00000  -0.50000000 0.30901699  -0.80901699 0.00000  
0.30901699  -0.80901699 -0.50000000 0.00000  
19 'point symmetry operation'   ? ? -0.80901699 0.50000000  -0.30901699 0.00000  0.50000000  0.30901699  -0.80901699 0.00000  
-0.30901699 -0.80901699 -0.50000000 0.00000  
20 'point symmetry operation'   ? ? 0.30901699  0.80901699  -0.50000000 0.00000  0.80901699  -0.50000000 -0.30901699 0.00000  
-0.50000000 -0.30901699 -0.80901699 0.00000  
21 'point symmetry operation'   ? ? 0.00000000  0.00000000  1.00000000  0.00000  1.00000000  0.00000000  0.00000000  0.00000  
0.00000000  1.00000000  0.00000000  0.00000  
22 'point symmetry operation'   ? ? -0.50000000 0.30901699  0.80901699  0.00000  0.30901699  -0.80901699 0.50000000  0.00000  
0.80901699  0.50000000  0.30901699  0.00000  
23 'point symmetry operation'   ? ? -0.30901699 0.80901699  0.50000000  0.00000  -0.80901699 -0.50000000 0.30901699  0.00000  
0.50000000  -0.30901699 0.80901699  0.00000  
24 'point symmetry operation'   ? ? 0.30901699  0.80901699  0.50000000  0.00000  -0.80901699 0.50000000  -0.30901699 0.00000  
-0.50000000 -0.30901699 0.80901699  0.00000  
25 'point symmetry operation'   ? ? 0.50000000  0.30901699  0.80901699  0.00000  0.30901699  0.80901699  -0.50000000 0.00000  
-0.80901699 0.50000000  0.30901699  0.00000  
26 'point symmetry operation'   ? ? 0.00000000  0.00000000  1.00000000  0.00000  -1.00000000 0.00000000  0.00000000  0.00000  
0.00000000  -1.00000000 0.00000000  0.00000  
27 'point symmetry operation'   ? ? -0.50000000 0.30901699  0.80901699  0.00000  -0.30901699 0.80901699  -0.50000000 0.00000  
-0.80901699 -0.50000000 -0.30901699 0.00000  
28 'point symmetry operation'   ? ? -0.30901699 0.80901699  0.50000000  0.00000  0.80901699  0.50000000  -0.30901699 0.00000  
-0.50000000 0.30901699  -0.80901699 0.00000  
29 'point symmetry operation'   ? ? 0.30901699  0.80901699  0.50000000  0.00000  0.80901699  -0.50000000 0.30901699  0.00000  
0.50000000  0.30901699  -0.80901699 0.00000  
30 'point symmetry operation'   ? ? 0.50000000  0.30901699  0.80901699  0.00000  -0.30901699 -0.80901699 0.50000000  0.00000  
0.80901699  -0.50000000 -0.30901699 0.00000  
31 'point symmetry operation'   ? ? 0.00000000  0.00000000  -1.00000000 0.00000  -1.00000000 0.00000000  0.00000000  0.00000  
0.00000000  1.00000000  0.00000000  0.00000  
32 'point symmetry operation'   ? ? 0.50000000  -0.30901699 -0.80901699 0.00000  -0.30901699 0.80901699  -0.50000000 0.00000  
0.80901699  0.50000000  0.30901699  0.00000  
33 'point symmetry operation'   ? ? 0.30901699  -0.80901699 -0.50000000 0.00000  0.80901699  0.50000000  -0.30901699 0.00000  
0.50000000  -0.30901699 0.80901699  0.00000  
34 'point symmetry operation'   ? ? -0.30901699 -0.80901699 -0.50000000 0.00000  0.80901699  -0.50000000 0.30901699  0.00000  
-0.50000000 -0.30901699 0.80901699  0.00000  
35 'point symmetry operation'   ? ? -0.50000000 -0.30901699 -0.80901699 0.00000  -0.30901699 -0.80901699 0.50000000  0.00000  
-0.80901699 0.50000000  0.30901699  0.00000  
36 'point symmetry operation'   ? ? 0.00000000  0.00000000  -1.00000000 0.00000  1.00000000  0.00000000  0.00000000  0.00000  
0.00000000  -1.00000000 0.00000000  0.00000  
37 'point symmetry operation'   ? ? 0.50000000  -0.30901699 -0.80901699 0.00000  0.30901699  -0.80901699 0.50000000  0.00000  
-0.80901699 -0.50000000 -0.30901699 0.00000  
38 'point symmetry operation'   ? ? 0.30901699  -0.80901699 -0.50000000 0.00000  -0.80901699 -0.50000000 0.30901699  0.00000  
-0.50000000 0.30901699  -0.80901699 0.00000  
39 'point symmetry operation'   ? ? -0.30901699 -0.80901699 -0.50000000 0.00000  -0.80901699 0.50000000  -0.30901699 0.00000  
0.50000000  0.30901699  -0.80901699 0.00000  
40 'point symmetry operation'   ? ? -0.50000000 -0.30901699 -0.80901699 0.00000  0.30901699  0.80901699  -0.50000000 0.00000  
0.80901699  -0.50000000 -0.30901699 0.00000  
41 'point symmetry operation'   ? ? 0.00000000  1.00000000  0.00000000  0.00000  0.00000000  0.00000000  1.00000000  0.00000  
1.00000000  0.00000000  0.00000000  0.00000  
42 'point symmetry operation'   ? ? 0.80901699  0.50000000  0.30901699  0.00000  -0.50000000 0.30901699  0.80901699  0.00000  
0.30901699  -0.80901699 0.50000000  0.00000  
43 'point symmetry operation'   ? ? 0.50000000  -0.30901699 0.80901699  0.00000  -0.30901699 0.80901699  0.50000000  0.00000  
-0.80901699 -0.50000000 0.30901699  0.00000  
44 'point symmetry operation'   ? ? -0.50000000 -0.30901699 0.80901699  0.00000  0.30901699  0.80901699  0.50000000  0.00000  
-0.80901699 0.50000000  -0.30901699 0.00000  
45 'point symmetry operation'   ? ? -0.80901699 0.50000000  0.30901699  0.00000  0.50000000  0.30901699  0.80901699  0.00000  
0.30901699  0.80901699  -0.50000000 0.00000  
46 'point symmetry operation'   ? ? 0.00000000  -1.00000000 0.00000000  0.00000  0.00000000  0.00000000  1.00000000  0.00000  
-1.00000000 0.00000000  0.00000000  0.00000  
47 'point symmetry operation'   ? ? -0.80901699 -0.50000000 -0.30901699 0.00000  -0.50000000 0.30901699  0.80901699  0.00000  
-0.30901699 0.80901699  -0.50000000 0.00000  
48 'point symmetry operation'   ? ? -0.50000000 0.30901699  -0.80901699 0.00000  -0.30901699 0.80901699  0.50000000  0.00000  
0.80901699  0.50000000  -0.30901699 0.00000  
49 'point symmetry operation'   ? ? 0.50000000  0.30901699  -0.80901699 0.00000  0.30901699  0.80901699  0.50000000  0.00000  
0.80901699  -0.50000000 0.30901699  0.00000  
50 'point symmetry operation'   ? ? 0.80901699  -0.50000000 -0.30901699 0.00000  0.50000000  0.30901699  0.80901699  0.00000  
-0.30901699 -0.80901699 0.50000000  0.00000  
51 'point symmetry operation'   ? ? 0.00000000  1.00000000  0.00000000  0.00000  0.00000000  0.00000000  -1.00000000 0.00000  
-1.00000000 0.00000000  0.00000000  0.00000  
52 'point symmetry operation'   ? ? 0.80901699  0.50000000  0.30901699  0.00000  0.50000000  -0.30901699 -0.80901699 0.00000  
-0.30901699 0.80901699  -0.50000000 0.00000  
53 'point symmetry operation'   ? ? 0.50000000  -0.30901699 0.80901699  0.00000  0.30901699  -0.80901699 -0.50000000 0.00000  
0.80901699  0.50000000  -0.30901699 0.00000  
54 'point symmetry operation'   ? ? -0.50000000 -0.30901699 0.80901699  0.00000  -0.30901699 -0.80901699 -0.50000000 0.00000  
0.80901699  -0.50000000 0.30901699  0.00000  
55 'point symmetry operation'   ? ? -0.80901699 0.50000000  0.30901699  0.00000  -0.50000000 -0.30901699 -0.80901699 0.00000  
-0.30901699 -0.80901699 0.50000000  0.00000  
56 'point symmetry operation'   ? ? 0.00000000  -1.00000000 0.00000000  0.00000  0.00000000  0.00000000  -1.00000000 0.00000  
1.00000000  0.00000000  0.00000000  0.00000  
57 'point symmetry operation'   ? ? -0.80901699 -0.50000000 -0.30901699 0.00000  0.50000000  -0.30901699 -0.80901699 0.00000  
0.30901699  -0.80901699 0.50000000  0.00000  
58 'point symmetry operation'   ? ? -0.50000000 0.30901699  -0.80901699 0.00000  0.30901699  -0.80901699 -0.50000000 0.00000  
-0.80901699 -0.50000000 0.30901699  0.00000  
59 'point symmetry operation'   ? ? 0.50000000  0.30901699  -0.80901699 0.00000  -0.30901699 -0.80901699 -0.50000000 0.00000  
-0.80901699 0.50000000  -0.30901699 0.00000  
60 'point symmetry operation'   ? ? 0.80901699  -0.50000000 -0.30901699 0.00000  -0.50000000 -0.30901699 -0.80901699 0.00000  
0.30901699  0.80901699  -0.50000000 0.00000  
# 
_pdbx_point_symmetry.entry_id             2BBV 
_pdbx_point_symmetry.Schoenflies_symbol   I 
_pdbx_point_symmetry.H-M_notation         532 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? B GLY 273 ? A GLY 273 ? 1_555 CA ? H CA . ? A CA 364 ? 1_555 OD2 ? B ASP 221 ? A ASP 221 ? 1_555 139.5 ? 
2  O   ? B GLY 273 ? A GLY 273 ? 1_555 CA ? H CA . ? A CA 364 ? 1_555 OD1 ? D ASP 161 ? B ASP 161 ? 1_555 156.7 ? 
3  OD2 ? B ASP 221 ? A ASP 221 ? 1_555 CA ? H CA . ? A CA 364 ? 1_555 OD1 ? D ASP 161 ? B ASP 161 ? 1_555 63.0  ? 
4  OE1 ? F GLU 251 ? C GLU 251 ? 1_555 CA ? I CA . ? A CA 365 ? 1_555 OE1 ? B GLU 251 ? A GLU 251 ? 1_555 89.7  ? 
5  OE1 ? F GLU 251 ? C GLU 251 ? 1_555 CA ? I CA . ? A CA 365 ? 1_555 OE1 ? D GLU 251 ? B GLU 251 ? 1_555 104.2 ? 
6  OE1 ? B GLU 251 ? A GLU 251 ? 1_555 CA ? I CA . ? A CA 365 ? 1_555 OE1 ? D GLU 251 ? B GLU 251 ? 1_555 95.7  ? 
7  OD2 ? D ASP 221 ? B ASP 221 ? 1_555 CA ? J CA . ? B CA 364 ? 1_555 OD1 ? F ASP 161 ? C ASP 161 ? 1_555 78.6  ? 
8  OD2 ? D ASP 221 ? B ASP 221 ? 1_555 CA ? J CA . ? B CA 364 ? 1_555 O   ? D GLY 273 ? B GLY 273 ? 1_555 112.5 ? 
9  OD1 ? F ASP 161 ? C ASP 161 ? 1_555 CA ? J CA . ? B CA 364 ? 1_555 O   ? D GLY 273 ? B GLY 273 ? 1_555 167.7 ? 
10 O   ? F GLY 273 ? C GLY 273 ? 1_555 CA ? K CA . ? C CA 364 ? 1_555 OD1 ? F ASP 221 ? C ASP 221 ? 1_555 125.0 ? 
11 OD1 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? F ASP 249 ? C ASP 249 ? 1_555 44.4  ? 
12 OD1 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OE2 ? F GLU 251 ? C GLU 251 ? 1_555 82.8  ? 
13 OD2 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OE2 ? F GLU 251 ? C GLU 251 ? 1_555 125.0 ? 
14 OD1 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? B ASP 249 ? A ASP 249 ? 1_555 116.0 ? 
15 OD2 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? B ASP 249 ? A ASP 249 ? 1_555 71.6  ? 
16 OE2 ? F GLU 251 ? C GLU 251 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? B ASP 249 ? A ASP 249 ? 1_555 155.5 ? 
17 OD1 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? D ASP 249 ? B ASP 249 ? 1_555 88.3  ? 
18 OD2 ? F ASP 249 ? C ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? D ASP 249 ? B ASP 249 ? 1_555 80.2  ? 
19 OE2 ? F GLU 251 ? C GLU 251 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? D ASP 249 ? B ASP 249 ? 1_555 118.8 ? 
20 OD2 ? B ASP 249 ? A ASP 249 ? 1_555 CA ? L CA . ? C CA 365 ? 1_555 OD2 ? D ASP 249 ? B ASP 249 ? 1_555 79.3  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 1994-08-31 
2 'Structure model' 1 1 2008-05-22 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-11-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' struct_conf      
2 4 'Structure model' struct_conf_type 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
X-PLOR refinement . ? 1 
PROLSQ refinement . ? 2 
# 
loop_
_pdbx_database_remark.id 
_pdbx_database_remark.text 
700 
;SHEET
EACH SUBUNIT (A OR B OR C) IS ROUGHLY MADE UP OF TWO
DOMAINS, A BETA-BARREL DOMAIN AND AN ALPHA-HELICAL DOMAIN.
THE BETA-BARREL DOMAIN CONSISTS OF AN EIGHT-STRANDED
ANTI-PARALLEL BETA-BARREL AND THE INSERTIONS BETWEEN THE
STRANDS OF THE BARREL.  THE BETA-BARREL CONTAINS TWO BETA
SHEETS, ?BG AND ?CF (? CORRESPONDS TO A OR B OR C DEPENDING
ON THE SUBUNIT).  SHEETS ?BG AND ?CF EACH CONTAIN FOUR
STRANDS (IN SHEET ?BG STRANDS 1, 2, 3, AND, 4 CORRESPOND TO
STRANDS B, I, D, AND G, RESPECTIVELY, WHEREAS IN SHEET ?CF
STRANDS 1, 2, 3, AND 4 CORRESPOND TO STRANDS C, H, E, AND
F, RESPECTIVELY.  THE LETTERS INDICATE THE ORDER OF THE
STRANDS IN THE PRIMARY STRUCTURE).  THERE IS ANOTHER SHEET
?EX, WHICH CONTAINS FOUR STRANDS (OF WHICH TWO ARE SHORT
STRANDS) AND A PAIR OF PROTRUDING STRANDS, DESIGNATED AS
?PR BELONG TO THE SAME B-BARREL DOMAIN.
;
650 
;HELIX
THE ALPHA-HELICAL DOMAIN CONSISTS OF THREE ALPHA-HELICES
(?H1, ?H2, AND ?H3), WHICH ARE LOCATED INSIDE THE PROTEIN
CONTIGUOUS SHELL.  (? CORRESPONDS TO A OR B OR C DEPENDING
ON THE SUBUNIT).
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE2 E GLU 368 ? ? NZ  E LYS 371 ? ? 1.80 
2  1 OE1 E GLU 368 ? ? NZ  E LYS 371 ? ? 1.84 
3  1 OD1 A ASP 75  ? ? OXT A ASN 363 ? ? 1.84 
4  1 O   C THR 206 ? ? CA  C ALA 209 ? ? 2.01 
5  1 O   A PRO 129 ? ? CG2 A THR 132 ? ? 2.04 
6  1 O   C PRO 264 ? ? CG1 C VAL 267 ? ? 2.04 
7  1 O   A LEU 56  ? ? N   A ARG 58  ? ? 2.06 
8  1 CD  E GLU 368 ? ? NZ  E LYS 371 ? ? 2.08 
9  1 O   C THR 206 ? ? N   C ALA 209 ? ? 2.10 
10 1 CG1 C VAL 25  ? ? NE2 C GLN 27  ? ? 2.16 
11 1 O   B GLU 247 ? ? NH2 B ARG 348 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N9 N A   7   ? ? C4 N A   7   ? ? 1.311 1.374 -0.063 0.006 N 
2 1 CA C ASN 363 ? ? C  C ASN 363 ? ? 1.304 1.525 -0.221 0.026 N 
3 1 CA F ALA 364 ? ? CB F ALA 364 ? ? 1.786 1.520 0.266  0.021 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 C4 N A   7   ? ? C5 N A   7   ? ? C6  N A   7   ? ? 113.97 117.00 -3.03  0.50 N 
2  1 C8 N A   7   ? ? N9 N A   7   ? ? C4  N A   7   ? ? 108.60 105.80 2.80   0.40 N 
3  1 NE A ARG 58  ? ? CZ A ARG 58  ? ? NH2 A ARG 58  ? ? 124.07 120.30 3.77   0.50 N 
4  1 CD A ARG 87  ? ? NE A ARG 87  ? ? CZ  A ARG 87  ? ? 115.09 123.60 -8.51  1.40 N 
5  1 NE A ARG 87  ? ? CZ A ARG 87  ? ? NH1 A ARG 87  ? ? 116.46 120.30 -3.84  0.50 N 
6  1 NE A ARG 109 ? ? CZ A ARG 109 ? ? NH2 A ARG 109 ? ? 123.43 120.30 3.13   0.50 N 
7  1 CG A MET 182 ? ? SD A MET 182 ? ? CE  A MET 182 ? ? 110.36 100.20 10.16  1.60 N 
8  1 CB A ASP 229 ? ? CG A ASP 229 ? ? OD2 A ASP 229 ? ? 126.16 118.30 7.86   0.90 N 
9  1 NE A ARG 300 ? ? CZ A ARG 300 ? ? NH2 A ARG 300 ? ? 123.39 120.30 3.09   0.50 N 
10 1 CD A ARG 352 ? ? NE A ARG 352 ? ? CZ  A ARG 352 ? ? 135.46 123.60 11.86  1.40 N 
11 1 NE A ARG 352 ? ? CZ A ARG 352 ? ? NH1 A ARG 352 ? ? 126.24 120.30 5.94   0.50 N 
12 1 CA D ALA 364 ? ? C  D ALA 364 ? ? N   D SER 365 ? ? 103.83 117.20 -13.37 2.20 Y 
13 1 O  D ALA 364 ? ? C  D ALA 364 ? ? N   D SER 365 ? ? 135.08 122.70 12.38  1.60 Y 
14 1 CG D MET 366 ? ? SD D MET 366 ? ? CE  D MET 366 ? ? 110.23 100.20 10.03  1.60 N 
15 1 NE D ARG 369 ? ? CZ D ARG 369 ? ? NH2 D ARG 369 ? ? 124.03 120.30 3.73   0.50 N 
16 1 NE B ARG 87  ? ? CZ B ARG 87  ? ? NH1 B ARG 87  ? ? 125.11 120.30 4.81   0.50 N 
17 1 NE B ARG 87  ? ? CZ B ARG 87  ? ? NH2 B ARG 87  ? ? 117.01 120.30 -3.29  0.50 N 
18 1 NE B ARG 109 ? ? CZ B ARG 109 ? ? NH2 B ARG 109 ? ? 124.05 120.30 3.75   0.50 N 
19 1 CB B ASP 221 ? ? CG B ASP 221 ? ? OD2 B ASP 221 ? ? 125.21 118.30 6.91   0.90 N 
20 1 NE B ARG 322 ? ? CZ B ARG 322 ? ? NH2 B ARG 322 ? ? 123.93 120.30 3.63   0.50 N 
21 1 NE B ARG 348 ? ? CZ B ARG 348 ? ? NH1 B ARG 348 ? ? 117.16 120.30 -3.14  0.50 N 
22 1 CG E MET 366 ? ? SD E MET 366 ? ? CE  E MET 366 ? ? 110.00 100.20 9.80   1.60 N 
23 1 NE E ARG 369 ? ? CZ E ARG 369 ? ? NH2 E ARG 369 ? ? 124.02 120.30 3.72   0.50 N 
24 1 CB C ALA 55  ? ? CA C ALA 55  ? ? C   C ALA 55  ? ? 98.38  110.10 -11.72 1.50 N 
25 1 CA C ALA 55  ? ? C  C ALA 55  ? ? N   C LEU 56  ? ? 102.60 117.20 -14.60 2.20 Y 
26 1 O  C ALA 55  ? ? C  C ALA 55  ? ? N   C LEU 56  ? ? 136.81 122.70 14.11  1.60 Y 
27 1 NE C ARG 58  ? ? CZ C ARG 58  ? ? NH2 C ARG 58  ? ? 123.76 120.30 3.46   0.50 N 
28 1 NE C ARG 87  ? ? CZ C ARG 87  ? ? NH1 C ARG 87  ? ? 123.90 120.30 3.60   0.50 N 
29 1 NE C ARG 87  ? ? CZ C ARG 87  ? ? NH2 C ARG 87  ? ? 116.16 120.30 -4.14  0.50 N 
30 1 NE C ARG 95  ? ? CZ C ARG 95  ? ? NH2 C ARG 95  ? ? 124.17 120.30 3.87   0.50 N 
31 1 NE C ARG 109 ? ? CZ C ARG 109 ? ? NH2 C ARG 109 ? ? 123.72 120.30 3.42   0.50 N 
32 1 CB C ASP 127 ? ? CG C ASP 127 ? ? OD1 C ASP 127 ? ? 124.44 118.30 6.14   0.90 N 
33 1 NE C ARG 167 ? ? CZ C ARG 167 ? ? NH1 C ARG 167 ? ? 123.32 120.30 3.02   0.50 N 
34 1 CG C MET 171 ? ? SD C MET 171 ? ? CE  C MET 171 ? ? 110.17 100.20 9.97   1.60 N 
35 1 CB C ASP 221 ? ? CG C ASP 221 ? ? OD2 C ASP 221 ? ? 125.99 118.30 7.69   0.90 N 
36 1 CB C ASP 335 ? ? CG C ASP 335 ? ? OD2 C ASP 335 ? ? 124.25 118.30 5.95   0.90 N 
37 1 NE C ARG 348 ? ? CZ C ARG 348 ? ? NH2 C ARG 348 ? ? 125.45 120.30 5.15   0.50 N 
38 1 NE C ARG 352 ? ? CZ C ARG 352 ? ? NH2 C ARG 352 ? ? 123.92 120.30 3.62   0.50 N 
39 1 N  F ALA 364 ? ? CA F ALA 364 ? ? CB  F ALA 364 ? ? 91.71  110.10 -18.39 1.40 N 
40 1 CG F MET 366 ? ? SD F MET 366 ? ? CE  F MET 366 ? ? 110.28 100.20 10.08  1.60 N 
41 1 NE F ARG 369 ? ? CZ F ARG 369 ? ? NH2 F ARG 369 ? ? 123.98 120.30 3.68   0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 57  ? ? -45.18  52.95   
2  1 THR A 78  ? ? -174.73 126.29  
3  1 ASP A 79  ? ? -47.49  103.65  
4  1 LYS A 82  ? ? -140.28 36.93   
5  1 VAL A 92  ? ? -170.72 146.20  
6  1 ALA A 126 ? ? 175.61  145.16  
7  1 MET A 171 ? ? -168.20 105.94  
8  1 LEU A 181 ? ? -71.05  29.51   
9  1 MET A 182 ? ? -140.09 -22.82  
10 1 ALA A 185 ? ? -175.41 138.80  
11 1 SER A 198 ? ? -115.86 -163.56 
12 1 THR A 206 ? ? -43.89  156.90  
13 1 PRO A 208 ? ? -56.01  -8.72   
14 1 ALA A 209 ? ? 54.91   121.63  
15 1 ASP A 249 ? ? -139.80 -159.99 
16 1 PRO A 264 ? ? -59.67  176.77  
17 1 ASN A 293 ? ? -103.88 54.73   
18 1 VAL A 308 ? ? -116.76 78.62   
19 1 ALA A 317 ? ? -161.73 111.84  
20 1 THR B 57  ? ? -107.19 48.59   
21 1 ARG B 58  ? ? -131.79 -32.85  
22 1 LYS B 82  ? ? -152.09 24.71   
23 1 PRO B 85  ? ? -73.37  49.63   
24 1 ASP B 86  ? ? -102.01 -169.12 
25 1 ASN B 154 ? ? -143.41 37.74   
26 1 LEU B 181 ? ? -65.79  1.83    
27 1 ALA B 185 ? ? -176.23 126.63  
28 1 PRO B 194 ? ? -69.45  78.55   
29 1 SER B 198 ? ? -114.29 -159.57 
30 1 ALA B 205 ? ? -102.81 41.42   
31 1 THR B 206 ? ? -60.63  -170.73 
32 1 ALA B 209 ? ? 81.92   98.78   
33 1 ASP B 229 ? ? -105.18 74.96   
34 1 ASN B 293 ? ? -100.86 67.66   
35 1 ALA C 126 ? ? -170.15 146.40  
36 1 MET C 171 ? ? -160.17 104.15  
37 1 ALA C 185 ? ? -176.43 149.36  
38 1 SER C 198 ? ? -107.89 -160.66 
39 1 ALA C 205 ? ? -102.13 53.83   
40 1 ALA C 209 ? ? 70.50   121.18  
41 1 ILE C 236 ? ? -67.35  23.47   
42 1 PHE C 240 ? ? -164.50 115.16  
43 1 PHE C 276 ? ? -160.78 -165.25 
44 1 VAL C 285 ? ? -104.48 -63.58  
45 1 ALA C 361 ? ? -30.84  -30.99  
46 1 SER F 365 ? ? -41.29  158.82  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     58 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.206 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A SER 336 ? OG ? B SER 336 OG 
2 1 Y 1 B SER 336 ? OG ? D SER 336 OG 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? B MET 1  
2   1 Y 1 A VAL 2   ? B VAL 2  
3   1 Y 1 A ARG 3   ? B ARG 3  
4   1 Y 1 A ASN 4   ? B ASN 4  
5   1 Y 1 A ASN 5   ? B ASN 5  
6   1 Y 1 A ASN 6   ? B ASN 6  
7   1 Y 1 A ARG 7   ? B ARG 7  
8   1 Y 1 A ARG 8   ? B ARG 8  
9   1 Y 1 A ARG 9   ? B ARG 9  
10  1 Y 1 A GLN 10  ? B GLN 10 
11  1 Y 1 A ARG 11  ? B ARG 11 
12  1 Y 1 A THR 12  ? B THR 12 
13  1 Y 1 A GLN 13  ? B GLN 13 
14  1 Y 1 A ARG 14  ? B ARG 14 
15  1 Y 1 A ILE 15  ? B ILE 15 
16  1 Y 1 A VAL 16  ? B VAL 16 
17  1 Y 1 A THR 17  ? B THR 17 
18  1 Y 1 A THR 18  ? B THR 18 
19  1 Y 1 A THR 19  ? B THR 19 
20  1 Y 1 A THR 20  ? B THR 20 
21  1 Y 1 A GLN 21  ? B GLN 21 
22  1 Y 1 A THR 22  ? B THR 22 
23  1 Y 1 A ALA 23  ? B ALA 23 
24  1 Y 1 A PRO 24  ? B PRO 24 
25  1 Y 1 A VAL 25  ? B VAL 25 
26  1 Y 1 A PRO 26  ? B PRO 26 
27  1 Y 1 A GLN 27  ? B GLN 27 
28  1 Y 1 A GLN 28  ? B GLN 28 
29  1 Y 1 A ASN 29  ? B ASN 29 
30  1 Y 1 A VAL 30  ? B VAL 30 
31  1 Y 1 A PRO 31  ? B PRO 31 
32  1 Y 1 A LYS 32  ? B LYS 32 
33  1 Y 1 A GLN 33  ? B GLN 33 
34  1 Y 1 A PRO 34  ? B PRO 34 
35  1 Y 1 A ARG 35  ? B ARG 35 
36  1 Y 1 A ARG 36  ? B ARG 36 
37  1 Y 1 A ARG 37  ? B ARG 37 
38  1 Y 1 A ARG 38  ? B ARG 38 
39  1 Y 1 A ASN 39  ? B ASN 39 
40  1 Y 1 A ARG 40  ? B ARG 40 
41  1 Y 1 A ALA 41  ? B ALA 41 
42  1 Y 1 A ARG 42  ? B ARG 42 
43  1 Y 1 A ARG 43  ? B ARG 43 
44  1 Y 1 A ASN 44  ? B ASN 44 
45  1 Y 1 A ARG 45  ? B ARG 45 
46  1 Y 1 A ARG 46  ? B ARG 46 
47  1 Y 1 A GLN 47  ? B GLN 47 
48  1 Y 1 A GLY 48  ? B GLY 48 
49  1 Y 1 A ARG 49  ? B ARG 49 
50  1 Y 1 A ALA 50  ? B ALA 50 
51  1 Y 1 A MET 51  ? B MET 51 
52  1 Y 1 A ASN 52  ? B ASN 52 
53  1 Y 1 A MET 53  ? B MET 53 
54  1 Y 1 A GLY 54  ? B GLY 54 
55  1 Y 1 A ALA 55  ? B ALA 55 
56  1 Y 1 D MET 380 ? C MET 17 
57  1 Y 1 D ALA 381 ? C ALA 18 
58  1 Y 1 D SER 382 ? C SER 19 
59  1 Y 1 D ASN 383 ? C ASN 20 
60  1 Y 1 D VAL 384 ? C VAL 21 
61  1 Y 1 D PRO 385 ? C PRO 22 
62  1 Y 1 D GLY 386 ? C GLY 23 
63  1 Y 1 D PRO 387 ? C PRO 24 
64  1 Y 1 D ILE 388 ? C ILE 25 
65  1 Y 1 D GLY 389 ? C GLY 26 
66  1 Y 1 D ILE 390 ? C ILE 27 
67  1 Y 1 D ALA 391 ? C ALA 28 
68  1 Y 1 D ALA 392 ? C ALA 29 
69  1 Y 1 D SER 393 ? C SER 30 
70  1 Y 1 D GLY 394 ? C GLY 31 
71  1 Y 1 D LEU 395 ? C LEU 32 
72  1 Y 1 D SER 396 ? C SER 33 
73  1 Y 1 D GLY 397 ? C GLY 34 
74  1 Y 1 D LEU 398 ? C LEU 35 
75  1 Y 1 D SER 399 ? C SER 36 
76  1 Y 1 D ALA 400 ? C ALA 37 
77  1 Y 1 D LEU 401 ? C LEU 38 
78  1 Y 1 D PHE 402 ? C PHE 39 
79  1 Y 1 D GLU 403 ? C GLU 40 
80  1 Y 1 D GLY 404 ? C GLY 41 
81  1 Y 1 D PHE 405 ? C PHE 42 
82  1 Y 1 D GLY 406 ? C GLY 43 
83  1 Y 1 D PHE 407 ? C PHE 44 
84  1 Y 1 B MET 1   ? D MET 1  
85  1 Y 1 B VAL 2   ? D VAL 2  
86  1 Y 1 B ARG 3   ? D ARG 3  
87  1 Y 1 B ASN 4   ? D ASN 4  
88  1 Y 1 B ASN 5   ? D ASN 5  
89  1 Y 1 B ASN 6   ? D ASN 6  
90  1 Y 1 B ARG 7   ? D ARG 7  
91  1 Y 1 B ARG 8   ? D ARG 8  
92  1 Y 1 B ARG 9   ? D ARG 9  
93  1 Y 1 B GLN 10  ? D GLN 10 
94  1 Y 1 B ARG 11  ? D ARG 11 
95  1 Y 1 B THR 12  ? D THR 12 
96  1 Y 1 B GLN 13  ? D GLN 13 
97  1 Y 1 B ARG 14  ? D ARG 14 
98  1 Y 1 B ILE 15  ? D ILE 15 
99  1 Y 1 B VAL 16  ? D VAL 16 
100 1 Y 1 B THR 17  ? D THR 17 
101 1 Y 1 B THR 18  ? D THR 18 
102 1 Y 1 B THR 19  ? D THR 19 
103 1 Y 1 B THR 20  ? D THR 20 
104 1 Y 1 B GLN 21  ? D GLN 21 
105 1 Y 1 B THR 22  ? D THR 22 
106 1 Y 1 B ALA 23  ? D ALA 23 
107 1 Y 1 B PRO 24  ? D PRO 24 
108 1 Y 1 B VAL 25  ? D VAL 25 
109 1 Y 1 B PRO 26  ? D PRO 26 
110 1 Y 1 B GLN 27  ? D GLN 27 
111 1 Y 1 B GLN 28  ? D GLN 28 
112 1 Y 1 B ASN 29  ? D ASN 29 
113 1 Y 1 B VAL 30  ? D VAL 30 
114 1 Y 1 B PRO 31  ? D PRO 31 
115 1 Y 1 B LYS 32  ? D LYS 32 
116 1 Y 1 B GLN 33  ? D GLN 33 
117 1 Y 1 B PRO 34  ? D PRO 34 
118 1 Y 1 B ARG 35  ? D ARG 35 
119 1 Y 1 B ARG 36  ? D ARG 36 
120 1 Y 1 B ARG 37  ? D ARG 37 
121 1 Y 1 B ARG 38  ? D ARG 38 
122 1 Y 1 B ASN 39  ? D ASN 39 
123 1 Y 1 B ARG 40  ? D ARG 40 
124 1 Y 1 B ALA 41  ? D ALA 41 
125 1 Y 1 B ARG 42  ? D ARG 42 
126 1 Y 1 B ARG 43  ? D ARG 43 
127 1 Y 1 B ASN 44  ? D ASN 44 
128 1 Y 1 B ARG 45  ? D ARG 45 
129 1 Y 1 B ARG 46  ? D ARG 46 
130 1 Y 1 B GLN 47  ? D GLN 47 
131 1 Y 1 B GLY 48  ? D GLY 48 
132 1 Y 1 B ARG 49  ? D ARG 49 
133 1 Y 1 B ALA 50  ? D ALA 50 
134 1 Y 1 B MET 51  ? D MET 51 
135 1 Y 1 B ASN 52  ? D ASN 52 
136 1 Y 1 B MET 53  ? D MET 53 
137 1 Y 1 B GLY 54  ? D GLY 54 
138 1 Y 1 B ALA 55  ? D ALA 55 
139 1 Y 1 E MET 380 ? E MET 17 
140 1 Y 1 E ALA 381 ? E ALA 18 
141 1 Y 1 E SER 382 ? E SER 19 
142 1 Y 1 E ASN 383 ? E ASN 20 
143 1 Y 1 E VAL 384 ? E VAL 21 
144 1 Y 1 E PRO 385 ? E PRO 22 
145 1 Y 1 E GLY 386 ? E GLY 23 
146 1 Y 1 E PRO 387 ? E PRO 24 
147 1 Y 1 E ILE 388 ? E ILE 25 
148 1 Y 1 E GLY 389 ? E GLY 26 
149 1 Y 1 E ILE 390 ? E ILE 27 
150 1 Y 1 E ALA 391 ? E ALA 28 
151 1 Y 1 E ALA 392 ? E ALA 29 
152 1 Y 1 E SER 393 ? E SER 30 
153 1 Y 1 E GLY 394 ? E GLY 31 
154 1 Y 1 E LEU 395 ? E LEU 32 
155 1 Y 1 E SER 396 ? E SER 33 
156 1 Y 1 E GLY 397 ? E GLY 34 
157 1 Y 1 E LEU 398 ? E LEU 35 
158 1 Y 1 E SER 399 ? E SER 36 
159 1 Y 1 E ALA 400 ? E ALA 37 
160 1 Y 1 E LEU 401 ? E LEU 38 
161 1 Y 1 E PHE 402 ? E PHE 39 
162 1 Y 1 E GLU 403 ? E GLU 40 
163 1 Y 1 E GLY 404 ? E GLY 41 
164 1 Y 1 E PHE 405 ? E PHE 42 
165 1 Y 1 E GLY 406 ? E GLY 43 
166 1 Y 1 E PHE 407 ? E PHE 44 
167 1 Y 1 C MET 1   ? F MET 1  
168 1 Y 1 C VAL 2   ? F VAL 2  
169 1 Y 1 C ARG 3   ? F ARG 3  
170 1 Y 1 C ASN 4   ? F ASN 4  
171 1 Y 1 C ASN 5   ? F ASN 5  
172 1 Y 1 C ASN 6   ? F ASN 6  
173 1 Y 1 C ARG 7   ? F ARG 7  
174 1 Y 1 C ARG 8   ? F ARG 8  
175 1 Y 1 C ARG 9   ? F ARG 9  
176 1 Y 1 C GLN 10  ? F GLN 10 
177 1 Y 1 C ARG 11  ? F ARG 11 
178 1 Y 1 C THR 12  ? F THR 12 
179 1 Y 1 C GLN 13  ? F GLN 13 
180 1 Y 1 C ARG 14  ? F ARG 14 
181 1 Y 1 C ILE 15  ? F ILE 15 
182 1 Y 1 C VAL 16  ? F VAL 16 
183 1 Y 1 C THR 17  ? F THR 17 
184 1 Y 1 C THR 18  ? F THR 18 
185 1 Y 1 C THR 19  ? F THR 19 
186 1 Y 1 C LYS 32  ? F LYS 32 
187 1 Y 1 C GLN 33  ? F GLN 33 
188 1 Y 1 C PRO 34  ? F PRO 34 
189 1 Y 1 C ARG 35  ? F ARG 35 
190 1 Y 1 C ARG 36  ? F ARG 36 
191 1 Y 1 C ARG 37  ? F ARG 37 
192 1 Y 1 C ARG 38  ? F ARG 38 
193 1 Y 1 C ASN 39  ? F ASN 39 
194 1 Y 1 C ARG 40  ? F ARG 40 
195 1 Y 1 C ALA 41  ? F ALA 41 
196 1 Y 1 C ARG 42  ? F ARG 42 
197 1 Y 1 C ARG 43  ? F ARG 43 
198 1 Y 1 C ASN 44  ? F ASN 44 
199 1 Y 1 C ARG 45  ? F ARG 45 
200 1 Y 1 C ARG 46  ? F ARG 46 
201 1 Y 1 C GLN 47  ? F GLN 47 
202 1 Y 1 C GLY 48  ? F GLY 48 
203 1 Y 1 C ARG 49  ? F ARG 49 
204 1 Y 1 C ALA 50  ? F ALA 50 
205 1 Y 1 C MET 51  ? F MET 51 
206 1 Y 1 C ASN 52  ? F ASN 52 
207 1 Y 1 C MET 53  ? F MET 53 
208 1 Y 1 C GLY 54  ? F GLY 54 
209 1 Y 1 F MET 380 ? G MET 17 
210 1 Y 1 F ALA 381 ? G ALA 18 
211 1 Y 1 F SER 382 ? G SER 19 
212 1 Y 1 F ASN 383 ? G ASN 20 
213 1 Y 1 F VAL 384 ? G VAL 21 
214 1 Y 1 F PRO 385 ? G PRO 22 
215 1 Y 1 F GLY 386 ? G GLY 23 
216 1 Y 1 F PRO 387 ? G PRO 24 
217 1 Y 1 F ILE 388 ? G ILE 25 
218 1 Y 1 F GLY 389 ? G GLY 26 
219 1 Y 1 F ILE 390 ? G ILE 27 
220 1 Y 1 F ALA 391 ? G ALA 28 
221 1 Y 1 F ALA 392 ? G ALA 29 
222 1 Y 1 F SER 393 ? G SER 30 
223 1 Y 1 F GLY 394 ? G GLY 31 
224 1 Y 1 F LEU 395 ? G LEU 32 
225 1 Y 1 F SER 396 ? G SER 33 
226 1 Y 1 F GLY 397 ? G GLY 34 
227 1 Y 1 F LEU 398 ? G LEU 35 
228 1 Y 1 F SER 399 ? G SER 36 
229 1 Y 1 F ALA 400 ? G ALA 37 
230 1 Y 1 F LEU 401 ? G LEU 38 
231 1 Y 1 F PHE 402 ? G PHE 39 
232 1 Y 1 F GLU 403 ? G GLU 40 
233 1 Y 1 F GLY 404 ? G GLY 41 
234 1 Y 1 F PHE 405 ? G PHE 42 
235 1 Y 1 F GLY 406 ? G GLY 43 
236 1 Y 1 F PHE 407 ? G PHE 44 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
2BBV 'double helix'         
2BBV 'mismatched base pair' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 A U 3 1_555 A U 8 2_555 -1.307 -1.193 0.804  -1.140  11.588  -2.510   1 N_U3:U8_N N 3 ? N 8 ? ?  ? 
1 A U 4 1_555 A A 7 2_555 0.700  -0.769 0.878  -14.357 0.817   3.715    2 N_U4:A7_N N 4 ? N 7 ? 20 1 
1 A A 5 1_555 A U 6 2_555 0.528  -1.892 2.038  -8.051  27.062  109.172  3 N_A5:U6_N N 5 ? N 6 ? ?  ? 
1 A U 6 1_555 A A 5 2_555 -0.528 1.892  -2.038 8.051   -27.062 -109.172 4 N_U6:A5_N N 6 ? N 5 ? ?  ? 
1 A A 7 1_555 A U 4 2_555 -0.700 -0.769 0.878  14.357  0.817   3.715    5 N_A7:U4_N N 7 ? N 4 ? 20 1 
1 A U 8 1_555 A U 3 2_555 1.307  -1.193 0.804  1.140   11.588  -2.510   6 N_U8:U3_N N 8 ? N 3 ? ?  ? 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 A U 3 1_555 A U 8 2_555 A U 4 1_555 A A 7 2_555 -0.638 -3.174 3.061 -8.148   11.162  48.722  -4.392 0.255  2.396 13.224  9.653   
50.529  1 NN_U3U4:A7U8_NN N 3 ? N 8 ? N 4 ? N 7 ? 
1 A U 4 1_555 A A 7 2_555 A A 5 1_555 A U 6 2_555 -1.705 -3.548 0.145 -164.445 29.860  79.605  -1.824 0.617  0.893 15.342  84.490  
170.124 2 NN_U4A5:U6A7_NN N 4 ? N 7 ? N 5 ? N 6 ? 
1 A A 5 1_555 A U 6 2_555 A U 6 1_555 A A 5 2_555 3.274  -0.862 0.000 -81.665  153.602 180.000 -0.431 -1.637 0.000 76.801  40.832  
180.000 3 NN_A5U6:A5U6_NN N 5 ? N 6 ? N 6 ? N 5 ? 
1 A U 6 1_555 A A 5 2_555 A A 7 1_555 A U 4 2_555 0.895  -0.557 3.795 -9.884   8.236   -20.583 -1.949 -1.800 3.778 -20.649 -24.781 
-24.237 4 NN_U6A7:U4A5_NN N 6 ? N 5 ? N 7 ? N 4 ? 
1 A A 7 1_555 A U 4 2_555 A U 8 1_555 A U 3 2_555 0.638  -3.174 3.061 8.148    11.162  48.722  -4.392 -0.255 2.396 13.224  -9.653  
50.529  5 NN_A7U8:U3U4_NN N 7 ? N 4 ? N 8 ? N 3 ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CALCIUM ION' CA  
5 water         HOH 
#