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Ticket #8133: pdb1bfp_0.ent

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1	HEADER LUMINESCENCE 09-APR-97 1BFP
2	TITLE BLUE VARIANT OF GREEN FLUORESCENT PROTEIN
3	COMPND MOL_ID: 1;
4	COMPND 2 MOLECULE: BLUE FLUORESCENT PROTEIN;
5	COMPND 3 CHAIN: A;
6	COMPND 4 SYNONYM: BLUE-EMISSION VARIANT;
7	COMPND 5 ENGINEERED: YES;
8	COMPND 6 MUTATION: YES
9	SOURCE MOL_ID: 1;
10	SOURCE 2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;
11	SOURCE 3 ORGANISM_TAXID: 6100;
12	SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
13	SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
14	SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109 (DE3);
15	SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
16	SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETB (INVITROGEN);
17	SOURCE 9 OTHER_DETAILS: THE N-TERMINAL HIS-TAG HAS BEEN REMOVED
18	KEYWDS FLUORESCENT PROTEIN, BLUE EMISSION, MUTANT, FLUOROPHORE,
19	KEYWDS 2 BIOLUMINESCENSE, LUMINESCENCE
20	EXPDTA X-RAY DIFFRACTION
21	AUTHOR R.M.WACHTER,S.J.REMINGTON
22	REVDAT 5 12-MAY-09 1BFP 1 SEQADV
23	REVDAT 4 24-FEB-09 1BFP 1 VERSN
24	REVDAT 3 01-APR-03 1BFP 1 JRNL
25	REVDAT 2 19-OCT-99 1BFP 1 JRNL
26	REVDAT 1 07-JUL-97 1BFP 0
27	JRNL AUTH R.M.WACHTER,B.A.KING,R.HEIM,K.KALLIO,R.Y.TSIEN,
28	JRNL AUTH 2 S.G.BOXER,S.J.REMINGTON
29	JRNL TITL CRYSTAL STRUCTURE AND PHOTODYNAMIC BEHAVIOR OF THE
30	JRNL TITL 2 BLUE EMISSION VARIANT Y66H/Y145F OF GREEN
31	JRNL TITL 3 FLUORESCENT PROTEIN.
32	JRNL REF BIOCHEMISTRY V. 36 9759 1997
33	JRNL REFN ISSN 0006-2960
34	JRNL PMID 9245407
35	JRNL DOI 10.1021/BI970563W
36	REMARK 1
37	REMARK 1 REFERENCE 1
38	REMARK 1 AUTH R.HEIM,R.Y.TSIEN
39	REMARK 1 TITL ENGINEERING GREEN FLUORESCENT PROTEIN FOR IMPROVED
40	REMARK 1 TITL 2 BRIGHTNESS, LONGER WAVELENGTHS AND FLUORESCENCE
41	REMARK 1 TITL 3 RESONANCE ENERGY TRANSFER
42	REMARK 1 REF CURR.BIOL. V. 6 178 1996
43	REMARK 1 REFN ISSN 0960-9822
44	REMARK 2
45	REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
46	REMARK 3
47	REMARK 3 REFINEMENT.
48	REMARK 3 PROGRAM : TNT V. 5-F
49	REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
50	REMARK 3
51	REMARK 3 DATA USED IN REFINEMENT.
52	REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
53	REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
54	REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
55	REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
56	REMARK 3 NUMBER OF REFLECTIONS : 31786
57	REMARK 3
58	REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
59	REMARK 3 CROSS-VALIDATION METHOD : NULL
60	REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
61	REMARK 3 R VALUE (WORKING + TEST SET) : NULL
62	REMARK 3 R VALUE (WORKING SET) : 0.181
63	REMARK 3 FREE R VALUE : NULL
64	REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
65	REMARK 3 FREE R VALUE TEST SET COUNT : NULL
66	REMARK 3
67	REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
68	REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
69	REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1810
70	REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
71	REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
72	REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
73	REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
74	REMARK 3
75	REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
76	REMARK 3 PROTEIN ATOMS : 1784
77	REMARK 3 NUCLEIC ACID ATOMS : 0
78	REMARK 3 HETEROGEN ATOMS : 0
79	REMARK 3 SOLVENT ATOMS : 82
80	REMARK 3
81	REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 19.700
82	REMARK 3
83	REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
84	REMARK 3 BOND LENGTHS (A) : 0.010 ; 1.500 ; 1828
85	REMARK 3 BOND ANGLES (DEGREES) : 1.970 ; 3.000 ; 2465
86	REMARK 3 TORSION ANGLES (DEGREES) : 20.090; 0.000 ; 1064
87	REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
88	REMARK 3 TRIGONAL CARBON PLANES (A) : 0.012 ; 2.000 ; 47
89	REMARK 3 GENERAL PLANES (A) : 0.017 ; 6.000 ; 266
90	REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 5.177 ; 1.500 ; 1803
91	REMARK 3 NON-BONDED CONTACTS (A) : 0.033 ; 10.000; 24
92	REMARK 3
93	REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
94	REMARK 3
95	REMARK 3 BULK SOLVENT MODELING.
96	REMARK 3 METHOD USED : NULL
97	REMARK 3 KSOL : 0.80
98	REMARK 3 BSOL : 300.00
99	REMARK 3
100	REMARK 3 RESTRAINT LIBRARIES.
101	REMARK 3 STEREOCHEMISTRY : TNT
102	REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT
103	REMARK 3
104	REMARK 3 OTHER REFINEMENT REMARKS: NULL
105	REMARK 4
106	REMARK 4 1BFP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
107	REMARK 100
108	REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
109	REMARK 200
110	REMARK 200 EXPERIMENTAL DETAILS
111	REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
112	REMARK 200 DATE OF DATA COLLECTION : 19-SEP-96
113	REMARK 200 TEMPERATURE (KELVIN) : 295
114	REMARK 200 PH : 4.5
115	REMARK 200 NUMBER OF CRYSTALS USED : 1
116	REMARK 200
117	REMARK 200 SYNCHROTRON (Y/N) : N
118	REMARK 200 RADIATION SOURCE : ROTATING ANODE
119	REMARK 200 BEAMLINE : NULL
120	REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
121	REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
122	REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
123	REMARK 200 MONOCHROMATOR : GRAPHITE(002)
124	REMARK 200 OPTICS : COLLIMATOR
125	REMARK 200
126	REMARK 200 DETECTOR TYPE : AREA DETECTOR
127	REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
128	REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DATAC
129	REMARK 200 DATA SCALING SOFTWARE : SCALE1
130	REMARK 200
131	REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12044
132	REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
133	REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
134	REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
135	REMARK 200
136	REMARK 200 OVERALL.
137	REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
138	REMARK 200 DATA REDUNDANCY : 2.640
139	REMARK 200 R MERGE (I) : 0.04100
140	REMARK 200 R SYM (I) : NULL
141	REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
142	REMARK 200
143	REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
144	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
145	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
146	REMARK 200 COMPLETENESS FOR SHELL (%) : 64.0
147	REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
148	REMARK 200 R MERGE FOR SHELL (I) : 0.14000
149	REMARK 200 R SYM FOR SHELL (I) : NULL
150	REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.240
151	REMARK 200
152	REMARK 200 DIFFRACTION PROTOCOL: NULL
153	REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
154	REMARK 200 SOFTWARE USED: TNT
155	REMARK 200 STARTING MODEL: PDB ENTRY 1EMA
156	REMARK 200
157	REMARK 200 REMARK: ISOMORPHOUS REPLACEMENT
158	REMARK 280
159	REMARK 280 CRYSTAL
160	REMARK 280 SOLVENT CONTENT, VS (%): 41.70
161	REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
162	REMARK 280
163	REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED AT 4 DEGC
164	REMARK 280 FROM 100MM SODIUM ACETATE PH 4.5 AND 10-12% PEG3400.,
165	REMARK 280 TEMPERATURE 277K
166	REMARK 290
167	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
168	REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
169	REMARK 290
170	REMARK 290 SYMOP SYMMETRY
171	REMARK 290 NNNMMM OPERATOR
172	REMARK 290 1555 X,Y,Z
173	REMARK 290 2555 -X+1/2,-Y,Z+1/2
174	REMARK 290 3555 -X,Y+1/2,-Z+1/2
175	REMARK 290 4555 X+1/2,-Y+1/2,-Z
176	REMARK 290
177	REMARK 290 WHERE NNN -> OPERATOR NUMBER
178	REMARK 290 MMM -> TRANSLATION VECTOR
179	REMARK 290
180	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
181	REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
182	REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
183	REMARK 290 RELATED MOLECULES.
184	REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
185	REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
186	REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
187	REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.00500
188	REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
189	REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.59000
190	REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
191	REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.54500
192	REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.59000
193	REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.00500
194	REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.54500
195	REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
196	REMARK 290
197	REMARK 290 REMARK: NULL
198	REMARK 300
199	REMARK 300 BIOMOLECULE: 1
200	REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
201	REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
202	REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
203	REMARK 300 BURIED SURFACE AREA.
204	REMARK 350
205	REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
206	REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
207	REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
208	REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
209	REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
210	REMARK 350
211	REMARK 350 BIOMOLECULE: 1
212	REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
213	REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
214	REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
215	REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
216	REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
217	REMARK 465
218	REMARK 465 MISSING RESIDUES
219	REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
220	REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
221	REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
222	REMARK 465
223	REMARK 465 M RES C SSSEQI
224	REMARK 465 THR A 230
225	REMARK 465 HIS A 231
226	REMARK 465 GLY A 232
227	REMARK 465 MET A 233
228	REMARK 465 ASP A 234
229	REMARK 465 GLU A 235
230	REMARK 465 LEU A 236
231	REMARK 465 TYR A 237
232	REMARK 465 LYS A 238
233	REMARK 470
234	REMARK 470 MISSING ATOM
235	REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
236	REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
237	REMARK 470 I=INSERTION CODE):
238	REMARK 470 M RES CSSEQI ATOMS
239	REMARK 470 MET A 1 CB CG SD CE
240	REMARK 470 LYS A 3 CB CG CD CE NZ
241	REMARK 470 GLU A 6 CD OE1 OE2
242	REMARK 470 LYS A 107 CE NZ
243	REMARK 470 LYS A 156 CE NZ
244	REMARK 470 GLN A 157 OE1 NE2
245	REMARK 470 LYS A 158 CG CD CE NZ
246	REMARK 470 LYS A 162 CE NZ
247	REMARK 470 GLU A 172 CD OE1 OE2
248	REMARK 470 GLN A 184 CG CD OE1 NE2
249	REMARK 470 ASN A 212 CG OD1 ND2
250	REMARK 475
251	REMARK 475 ZERO OCCUPANCY RESIDUES
252	REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
253	REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
254	REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
255	REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
256	REMARK 475 M RES C SSEQI
257	REMARK 475 GLN A 157
258	REMARK 475 LYS A 158
259	REMARK 500
260	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
261	REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
262	REMARK 500
263	REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
264	REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
265	REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
266	REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
267	REMARK 500
268	REMARK 500 STANDARD TABLE:
269	REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
270	REMARK 500
271	REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
272	REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
273	REMARK 500
274	REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
275	REMARK 500 ASP A 19 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
276	REMARK 500 ASP A 76 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
277	REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
278	REMARK 500 ASP A 82 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
279	REMARK 500 ASP A 103 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
280	REMARK 500 TYR A 106 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
281	REMARK 500 TYR A 106 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
282	REMARK 500 ASP A 117 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
283	REMARK 500 ASP A 133 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
284	REMARK 500 ASP A 155 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
285	REMARK 500 ASP A 180 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
286	REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
287	REMARK 500 ASP A 197 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
288	REMARK 500 ASP A 210 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
289	REMARK 500 ASP A 216 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
290	REMARK 500
291	REMARK 500 REMARK: NULL
292	REMARK 500
293	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
294	REMARK 500 SUBTOPIC: TORSION ANGLES
295	REMARK 500
296	REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
297	REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
298	REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
299	REMARK 500
300	REMARK 500 STANDARD TABLE:
301	REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
302	REMARK 500
303	REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
304	REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
305	REMARK 500
306	REMARK 500 M RES CSSEQI PSI PHI
307	REMARK 500 SER A 2 124.28 -171.30
308	REMARK 500 GLN A 69 -4.84 -58.05
309	REMARK 500 ASP A 103 -163.24 -162.13
310	REMARK 500 HIS A 148 174.72 176.60
311	REMARK 500 LYS A 156 -147.99 92.81
312	REMARK 500 LYS A 158 -0.81 -173.20
313	REMARK 500 ASN A 159 -116.21 -81.20
314	REMARK 500
315	REMARK 500 REMARK: NULL
316	REMARK 500
317	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
318	REMARK 500 SUBTOPIC: CHIRAL CENTERS
319	REMARK 500
320	REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
321	REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
322	REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
323	REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
324	REMARK 500
325	REMARK 500 STANDARD TABLE:
326	REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
327	REMARK 500
328	REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
329	REMARK 500 VAL A 112 19.8 L L OUTSIDE RANGE
330	REMARK 500 LYS A 156 22.1 L L OUTSIDE RANGE
331	REMARK 500 THR A 225 23.9 L L OUTSIDE RANGE
332	REMARK 500
333	REMARK 500 REMARK: NULL
334	REMARK 525
335	REMARK 525 SOLVENT
336	REMARK 525
337	REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
338	REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
339	REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
340	REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
341	REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
342	REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
343	REMARK 525 NUMBER; I=INSERTION CODE):
344	REMARK 525
345	REMARK 525 M RES CSSEQI
346	REMARK 525 HOH A 403 DISTANCE = 5.30 ANGSTROMS
347	DBREF 1BFP A 1 238 UNP P42212 GFP_AEQVI 1 238
348	SEQADV 1BFP IIC A 66 UNP P42212 SER 65 CHROMOPHORE
349	SEQADV 1BFP IIC A 66 UNP P42212 TYR 66 CHROMOPHORE
350	SEQADV 1BFP IIC A 66 UNP P42212 GLY 67 CHROMOPHORE
351	SEQADV 1BFP ARG A 80 UNP P42212 GLN 80 CLONING ARTIFACT
352	SEQADV 1BFP PHE A 145 UNP P42212 TYR 145 ENGINEERED
353	SEQRES 1 A 236 MET SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO
354	SEQRES 2 A 236 ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS
355	SEQRES 3 A 236 PHE SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR
356	SEQRES 4 A 236 GLY LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS
357	SEQRES 5 A 236 LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR PHE IIC
358	SEQRES 6 A 236 VAL GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS ARG
359	SEQRES 7 A 236 HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL
360	SEQRES 8 A 236 GLN GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR
361	SEQRES 9 A 236 LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU
362	SEQRES 10 A 236 VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU
363	SEQRES 11 A 236 ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN PHE
364	SEQRES 12 A 236 ASN SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS
365	SEQRES 13 A 236 ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE
366	SEQRES 14 A 236 GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN
367	SEQRES 15 A 236 ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP
368	SEQRES 16 A 236 ASN HIS TYR LEU SER THR GLN SER ALA LEU SER LYS ASP
369	SEQRES 17 A 236 PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE
370	SEQRES 18 A 236 VAL THR ALA ALA GLY ILE THR HIS GLY MET ASP GLU LEU
371	SEQRES 19 A 236 TYR LYS
372	MODRES 1BFP IIC A 66 SER
373	MODRES 1BFP IIC A 66 HIS
374	MODRES 1BFP IIC A 66 GLY
375	HET IIC A 66 19
376	HETNAM IIC 4-IMIDAZOLMETHYLENE-5-IMIDAZOLONE CHROMOPHORE
377	FORMUL 1 IIC C11 H15 N5 O4
378	FORMUL 2 HOH *82(H2 O)
379	HELIX 1 1 GLY A 4 PHE A 8 5 5
380	HELIX 2 2 TRP A 57 LEU A 60 1 4
381	HELIX 3 3 GLN A 69 PHE A 71 5 3
382	HELIX 4 4 PHE A 83 SER A 86 1 4
383	SHEET 1 A11 GLY A 160 ASN A 170 0
384	SHEET 2 A11 VAL A 176 PRO A 187 -1 N ASN A 185 O ILE A 161
385	SHEET 3 A11 TYR A 92 PHE A 100 -1 N PHE A 99 O ASP A 180
386	SHEET 4 A11 ASN A 105 GLU A 115 -1 N VAL A 112 O TYR A 92
387	SHEET 5 A11 THR A 118 ILE A 128 -1 N ILE A 128 O ASN A 105
388	SHEET 6 A11 VAL A 12 VAL A 22 1 N LEU A 15 O LEU A 119
389	SHEET 7 A11 HIS A 25 ASP A 36 -1 N GLY A 35 O VAL A 12
390	SHEET 8 A11 LYS A 41 CYS A 48 -1 N ILE A 47 O SER A 30
391	SHEET 9 A11 LEU A 220 ALA A 227 -1 N GLU A 222 O LEU A 42
392	SHEET 10 A11 HIS A 199 LEU A 207 -1 N ALA A 206 O LEU A 221
393	SHEET 11 A11 HIS A 148 ILE A 152 -1 N ILE A 152 O HIS A 199
394	LINK N1 IIC A 66 C PHE A 64 1555 1555 1.33
395	LINK C3 IIC A 66 N VAL A 68 1555 1555 1.32
396	CISPEP 1 MET A 88 PRO A 89 0 4.56
397	CRYST1 52.010 63.090 69.180 90.00 90.00 90.00 P 21 21 21 4
398	ORIGX1 1.000000 0.000000 0.000000 0.00000
399	ORIGX2 0.000000 1.000000 0.000000 0.00000
400	ORIGX3 0.000000 0.000000 1.000000 0.00000
401	SCALE1 0.019227 0.000000 0.000000 0.00000
402	SCALE2 0.000000 0.015850 0.000000 0.00000
403	SCALE3 0.000000 0.000000 0.014455 0.00000
404	ATOM 1 N MET A 1 31.746 5.870 51.376 1.00100.00 N
405	ATOM 2 CA MET A 1 30.876 6.475 52.361 1.00 98.24 C
406	ATOM 3 C MET A 1 30.438 7.873 51.950 1.00100.00 C
407	ATOM 4 O MET A 1 31.080 8.864 52.297 1.00100.00 O
408	ATOM 5 N SER A 2 29.339 7.946 51.195 1.00 99.64 N
409	ATOM 6 CA SER A 2 28.768 9.217 50.771 1.00 98.58 C
410	ATOM 7 C SER A 2 27.414 9.087 50.101 1.00100.00 C
411	ATOM 8 O SER A 2 27.265 8.379 49.104 1.00100.00 O
412	ATOM 9 CB SER A 2 29.691 10.111 49.971 1.00100.00 C
413	ATOM 10 OG SER A 2 29.049 11.363 49.764 1.00100.00 O
414	ATOM 11 N LYS A 3 26.439 9.809 50.656 1.00 95.65 N
415	ATOM 12 CA LYS A 3 25.074 9.797 50.157 1.00 93.12 C
416	ATOM 13 C LYS A 3 24.961 10.089 48.662 1.00 76.78 C
417	ATOM 14 O LYS A 3 24.481 9.258 47.877 1.00 77.51 O
418	ATOM 15 N GLY A 4 25.404 11.281 48.274 1.00 46.22 N
419	ATOM 16 CA GLY A 4 25.297 11.694 46.900 1.00 35.59 C
420	ATOM 17 C GLY A 4 26.425 11.243 46.016 1.00 32.49 C
421	ATOM 18 O GLY A 4 26.300 11.293 44.793 1.00 36.65 O
422	ATOM 19 N GLU A 5 27.529 10.843 46.631 1.00 30.24 N
423	ATOM 20 CA GLU A 5 28.723 10.431 45.905 1.00 34.91 C
424	ATOM 21 C GLU A 5 28.413 9.417 44.813 1.00 27.84 C
425	ATOM 22 O GLU A 5 28.862 9.526 43.658 1.00 17.35 O
426	ATOM 23 CB GLU A 5 29.776 9.843 46.876 1.00 39.20 C
427	ATOM 24 CG GLU A 5 31.177 10.490 46.788 1.00 50.97 C
428	ATOM 25 CD GLU A 5 32.088 10.075 47.919 1.00 60.21 C
429	ATOM 26 OE1 GLU A 5 32.438 10.828 48.814 1.00 94.65 O
430	ATOM 27 OE2 GLU A 5 32.452 8.816 47.850 1.00 98.12 O
431	ATOM 28 N GLU A 6 27.668 8.398 45.212 1.00 25.63 N
432	ATOM 29 CA GLU A 6 27.313 7.312 44.318 1.00 26.01 C
433	ATOM 30 C GLU A 6 26.490 7.762 43.141 1.00 21.95 C
434	ATOM 31 O GLU A 6 26.390 7.090 42.112 1.00 22.10 O
435	ATOM 32 CB GLU A 6 26.565 6.210 45.087 1.00 31.16 C
436	ATOM 33 CG GLU A 6 25.855 6.760 46.343 1.00 53.32 C
437	ATOM 34 N LEU A 7 25.842 8.890 43.314 1.00 26.89 N
438	ATOM 35 CA LEU A 7 24.961 9.387 42.281 1.00 24.30 C
439	ATOM 36 C LEU A 7 25.708 9.966 41.116 1.00 18.12 C
440	ATOM 37 O LEU A 7 25.170 10.099 40.024 1.00 24.69 O
441	ATOM 38 CB LEU A 7 24.045 10.466 42.864 1.00 23.60 C
442	ATOM 39 CG LEU A 7 22.646 10.000 43.211 1.00 28.20 C
443	ATOM 40 CD1 LEU A 7 22.669 8.557 43.673 1.00 38.85 C
444	ATOM 41 CD2 LEU A 7 22.113 10.884 44.324 1.00 9.54 C
445	ATOM 42 N PHE A 8 26.941 10.356 41.367 1.00 24.90 N
446	ATOM 43 CA PHE A 8 27.730 11.041 40.362 1.00 25.44 C
447	ATOM 44 C PHE A 8 28.830 10.206 39.759 1.00 38.38 C
448	ATOM 45 O PHE A 8 29.821 10.700 39.238 1.00 42.24 O
449	ATOM 46 CB PHE A 8 28.273 12.332 40.972 1.00 25.03 C
450	ATOM 47 CG PHE A 8 27.145 13.237 41.396 1.00 20.26 C
451	ATOM 48 CD1 PHE A 8 26.608 13.171 42.682 1.00 14.66 C
452	ATOM 49 CD2 PHE A 8 26.603 14.138 40.479 1.00 6.17 C
453	ATOM 50 CE1 PHE A 8 25.558 14.007 43.066 1.00 15.96 C
454	ATOM 51 CE2 PHE A 8 25.541 14.962 40.844 1.00 12.71 C
455	ATOM 52 CZ PHE A 8 25.034 14.911 42.143 1.00 16.92 C
456	ATOM 53 N THR A 9 28.610 8.928 39.805 1.00 33.81 N
457	ATOM 54 CA THR A 9 29.561 7.987 39.322 1.00 35.71 C
458	ATOM 55 C THR A 9 29.702 7.967 37.805 1.00 42.18 C
459	ATOM 56 O THR A 9 30.804 7.764 37.281 1.00 47.23 O
460	ATOM 57 CB THR A 9 29.276 6.625 39.974 1.00 28.92 C
461	ATOM 58 OG1 THR A 9 30.371 6.348 40.808 1.00 39.56 O
462	ATOM 59 CG2 THR A 9 29.035 5.529 38.946 1.00 41.21 C
463	ATOM 60 N GLY A 10 28.587 8.205 37.103 1.00 26.06 N
464	ATOM 61 CA GLY A 10 28.575 8.214 35.651 1.00 20.91 C
465	ATOM 62 C GLY A 10 28.158 9.571 35.090 1.00 18.71 C
466	ATOM 63 O GLY A 10 28.214 10.577 35.781 1.00 23.66 O
467	ATOM 64 N VAL A 11 27.727 9.566 33.833 1.00 16.79 N
468	ATOM 65 CA VAL A 11 27.229 10.741 33.152 1.00 19.57 C
469	ATOM 66 C VAL A 11 25.778 10.975 33.554 1.00 28.63 C
470	ATOM 67 O VAL A 11 24.930 10.125 33.315 1.00 23.12 O
471	ATOM 68 CB VAL A 11 27.312 10.540 31.645 1.00 22.76 C
472	ATOM 69 CG1 VAL A 11 26.647 11.682 30.887 1.00 20.24 C
473	ATOM 70 CG2 VAL A 11 28.768 10.459 31.231 1.00 25.82 C
474	ATOM 71 N VAL A 12 25.506 12.109 34.189 1.00 20.56 N
475	ATOM 72 CA VAL A 12 24.171 12.482 34.652 1.00 18.94 C
476	ATOM 73 C VAL A 12 23.497 13.529 33.737 1.00 26.05 C
477	ATOM 74 O VAL A 12 24.105 14.542 33.342 1.00 24.01 O
478	ATOM 75 CB VAL A 12 24.260 13.006 36.086 1.00 18.84 C
479	ATOM 76 CG1 VAL A 12 22.942 13.635 36.533 1.00 12.98 C
480	ATOM 77 CG2 VAL A 12 24.749 11.932 37.071 1.00 13.02 C
481	ATOM 78 N PRO A 13 22.229 13.288 33.378 1.00 21.37 N
482	ATOM 79 CA PRO A 13 21.501 14.241 32.553 1.00 10.56 C
483	ATOM 80 C PRO A 13 21.112 15.493 33.352 1.00 13.53 C
484	ATOM 81 O PRO A 13 20.847 15.484 34.567 1.00 16.23 O
485	ATOM 82 CB PRO A 13 20.259 13.535 32.021 1.00 11.34 C
486	ATOM 83 CG PRO A 13 20.232 12.145 32.648 1.00 25.08 C
487	ATOM 84 CD PRO A 13 21.419 12.056 33.606 1.00 26.43 C
488	ATOM 85 N ILE A 14 21.124 16.611 32.658 1.00 17.77 N
489	ATOM 86 CA ILE A 14 20.832 17.863 33.302 1.00 13.75 C
490	ATOM 87 C ILE A 14 19.716 18.580 32.590 1.00 6.99 C
491	ATOM 88 O ILE A 14 19.670 18.607 31.367 1.00 12.55 O
492	ATOM 89 CB ILE A 14 22.068 18.774 33.358 1.00 16.55 C
493	ATOM 90 CG1 ILE A 14 23.261 18.041 33.992 1.00 19.34 C
494	ATOM 91 CG2 ILE A 14 21.727 20.006 34.188 1.00 11.42 C
495	ATOM 92 CD1 ILE A 14 24.614 18.700 33.684 1.00 8.82 C
496	ATOM 93 N LEU A 15 18.885 19.229 33.392 1.00 14.44 N
497	ATOM 94 CA LEU A 15 17.783 20.014 32.885 1.00 19.54 C
498	ATOM 95 C LEU A 15 17.841 21.374 33.558 1.00 21.55 C
499	ATOM 96 O LEU A 15 17.885 21.438 34.771 1.00 18.21 O
500	ATOM 97 CB LEU A 15 16.472 19.306 33.241 1.00 19.55 C
501	ATOM 98 CG LEU A 15 15.401 19.378 32.176 1.00 29.36 C
502	ATOM 99 CD1 LEU A 15 14.056 19.547 32.870 1.00 30.52 C
503	ATOM 100 CD2 LEU A 15 15.648 20.556 31.250 1.00 33.93 C
504	ATOM 101 N VAL A 16 17.902 22.465 32.788 1.00 15.84 N
505	ATOM 102 CA VAL A 16 17.966 23.764 33.443 1.00 20.19 C
506	ATOM 103 C VAL A 16 16.764 24.610 33.033 1.00 18.32 C
507	ATOM 104 O VAL A 16 16.477 24.681 31.856 1.00 17.68 O
508	ATOM 105 CB VAL A 16 19.273 24.494 33.115 1.00 19.33 C
509	ATOM 106 CG1 VAL A 16 19.246 25.888 33.708 1.00 15.19 C
510	ATOM 107 CG2 VAL A 16 20.473 23.762 33.699 1.00 18.11 C
511	ATOM 108 N GLU A 17 16.084 25.236 34.000 1.00 19.42 N
512	ATOM 109 CA GLU A 17 14.904 26.077 33.745 1.00 19.57 C
513	ATOM 110 C GLU A 17 15.000 27.396 34.506 1.00 15.07 C
514	ATOM 111 O GLU A 17 15.042 27.423 35.749 1.00 22.56 O
515	ATOM 112 CB GLU A 17 13.614 25.355 34.211 1.00 20.62 C
516	ATOM 113 CG GLU A 17 13.426 23.962 33.571 1.00 12.97 C
517	ATOM 114 CD GLU A 17 13.112 24.127 32.122 1.00 32.70 C
518	ATOM 115 OE1 GLU A 17 12.822 25.211 31.624 1.00 49.59 O
519	ATOM 116 OE2 GLU A 17 13.199 23.001 31.458 1.00 31.89 O
520	ATOM 117 N LEU A 18 14.989 28.507 33.772 1.00 12.82 N
521	ATOM 118 CA LEU A 18 15.079 29.795 34.436 1.00 17.79 C
522	ATOM 119 C LEU A 18 13.959 30.771 34.050 1.00 28.17 C
523	ATOM 120 O LEU A 18 13.631 30.948 32.884 1.00 23.26 O
524	ATOM 121 CB LEU A 18 16.416 30.471 34.084 1.00 20.03 C
525	ATOM 122 CG LEU A 18 16.417 31.961 34.421 1.00 28.08 C
526	ATOM 123 CD1 LEU A 18 17.672 32.319 35.194 1.00 20.64 C
527	ATOM 124 CD2 LEU A 18 16.314 32.798 33.147 1.00 26.34 C
528	ATOM 125 N ASP A 19 13.455 31.496 35.035 1.00 20.45 N
529	ATOM 126 CA ASP A 19 12.478 32.518 34.784 1.00 27.65 C
530	ATOM 127 C ASP A 19 13.035 33.791 35.300 1.00 23.35 C
531	ATOM 128 O ASP A 19 13.324 33.895 36.490 1.00 19.57 O
532	ATOM 129 CB ASP A 19 11.094 32.250 35.413 1.00 38.34 C
533	ATOM 130 CG ASP A 19 10.251 31.373 34.533 1.00 65.22 C
534	ATOM 131 OD1 ASP A 19 9.676 30.380 34.938 1.00 85.49 O
535	ATOM 132 OD2 ASP A 19 10.287 31.736 33.273 1.00 61.57 O
536	ATOM 133 N GLY A 20 13.218 34.726 34.371 1.00 26.64 N
537	ATOM 134 CA GLY A 20 13.801 36.003 34.700 1.00 27.69 C
538	ATOM 135 C GLY A 20 13.002 37.228 34.272 1.00 25.67 C
539	ATOM 136 O GLY A 20 12.202 37.242 33.336 1.00 29.75 O
540	ATOM 137 N ASP A 21 13.272 38.264 35.017 1.00 21.19 N
541	ATOM 138 CA ASP A 21 12.726 39.552 34.794 1.00 23.50 C
542	ATOM 139 C ASP A 21 13.825 40.527 35.100 1.00 26.32 C
543	ATOM 140 O ASP A 21 14.327 40.555 36.221 1.00 29.78 O
544	ATOM 141 CB ASP A 21 11.567 39.815 35.756 1.00 27.35 C
545	ATOM 142 CG ASP A 21 11.040 41.191 35.528 1.00 35.72 C
546	ATOM 143 OD1 ASP A 21 11.437 41.898 34.627 1.00 48.71 O
547	ATOM 144 OD2 ASP A 21 10.097 41.522 36.362 1.00 36.54 O
548	ATOM 145 N VAL A 22 14.251 41.276 34.100 1.00 21.06 N
549	ATOM 146 CA VAL A 22 15.295 42.257 34.321 1.00 22.69 C
550	ATOM 147 C VAL A 22 14.820 43.623 33.858 1.00 21.80 C
551	ATOM 148 O VAL A 22 14.674 43.841 32.653 1.00 13.86 O
552	ATOM 149 CB VAL A 22 16.597 41.883 33.614 1.00 30.10 C
553	ATOM 150 CG1 VAL A 22 17.602 43.010 33.807 1.00 25.14 C
554	ATOM 151 CG2 VAL A 22 17.168 40.611 34.230 1.00 30.42 C
555	ATOM 152 N ASN A 23 14.560 44.507 34.831 1.00 27.74 N
556	ATOM 153 CA ASN A 23 14.026 45.838 34.569 1.00 32.12 C
557	ATOM 154 C ASN A 23 12.704 45.763 33.797 1.00 39.87 C
558	ATOM 155 O ASN A 23 12.433 46.566 32.898 1.00 37.19 O
559	ATOM 156 CB ASN A 23 15.024 46.725 33.813 1.00 33.62 C
560	ATOM 157 CG ASN A 23 16.059 47.403 34.695 1.00 51.50 C
561	ATOM 158 OD1 ASN A 23 16.366 46.966 35.824 1.00 44.83 O
562	ATOM 159 ND2 ASN A 23 16.594 48.498 34.169 1.00 32.42 N
563	ATOM 160 N GLY A 24 11.880 44.769 34.133 1.00 30.57 N
564	ATOM 161 CA GLY A 24 10.605 44.592 33.455 1.00 23.17 C
565	ATOM 162 C GLY A 24 10.764 43.768 32.194 1.00 31.96 C
566	ATOM 163 O GLY A 24 9.800 43.451 31.499 1.00 36.18 O
567	ATOM 164 N HIS A 25 12.001 43.420 31.893 1.00 20.73 N
568	ATOM 165 CA HIS A 25 12.264 42.554 30.769 1.00 24.81 C
569	ATOM 166 C HIS A 25 12.120 41.119 31.240 1.00 27.98 C
570	ATOM 167 O HIS A 25 12.832 40.636 32.138 1.00 20.49 O
571	ATOM 168 CB HIS A 25 13.647 42.807 30.172 1.00 33.05 C
572	ATOM 169 CG HIS A 25 13.635 44.090 29.431 1.00 43.14 C
573	ATOM 170 ND1 HIS A 25 13.962 45.285 30.061 1.00 49.00 N
574	ATOM 171 CD2 HIS A 25 13.248 44.363 28.153 1.00 47.64 C
575	ATOM 172 CE1 HIS A 25 13.801 46.247 29.151 1.00 51.12 C
576	ATOM 173 NE2 HIS A 25 13.371 45.726 27.997 1.00 50.61 N
577	ATOM 174 N LYS A 26 11.105 40.487 30.692 1.00 27.76 N
578	ATOM 175 CA LYS A 26 10.784 39.131 31.051 1.00 24.82 C
579	ATOM 176 C LYS A 26 11.246 38.211 29.983 1.00 26.94 C
580	ATOM 177 O LYS A 26 11.121 38.527 28.800 1.00 25.31 O
581	ATOM 178 CB LYS A 26 9.305 38.913 31.338 1.00 22.28 C
582	ATOM 179 CG LYS A 26 8.899 39.349 32.736 1.00 31.23 C
583	ATOM 180 CD LYS A 26 7.459 39.851 32.840 1.00 47.26 C
584	ATOM 181 CE LYS A 26 7.211 40.753 34.046 1.00 75.48 C
585	ATOM 182 NZ LYS A 26 7.542 40.112 35.333 1.00100.00 N
586	ATOM 183 N PHE A 27 11.779 37.072 30.429 1.00 17.64 N
587	ATOM 184 CA PHE A 27 12.282 36.098 29.510 1.00 14.49 C
588	ATOM 185 C PHE A 27 12.337 34.754 30.190 1.00 22.72 C
589	ATOM 186 O PHE A 27 12.159 34.660 31.408 1.00 23.37 O
590	ATOM 187 CB PHE A 27 13.663 36.511 28.979 1.00 18.74 C
591	ATOM 188 CG PHE A 27 14.678 36.757 30.089 1.00 19.02 C
592	ATOM 189 CD1 PHE A 27 15.673 35.821 30.371 1.00 20.15 C
593	ATOM 190 CD2 PHE A 27 14.646 37.918 30.861 1.00 23.85 C
594	ATOM 191 CE1 PHE A 27 16.600 36.016 31.396 1.00 14.38 C
595	ATOM 192 CE2 PHE A 27 15.581 38.143 31.876 1.00 28.59 C
596	ATOM 193 CZ PHE A 27 16.562 37.189 32.145 1.00 16.96 C
597	ATOM 194 N SER A 28 12.548 33.711 29.383 1.00 17.14 N
598	ATOM 195 CA SER A 28 12.659 32.377 29.919 1.00 16.88 C
599	ATOM 196 C SER A 28 13.733 31.597 29.183 1.00 16.56 C
600	ATOM 197 O SER A 28 13.862 31.699 27.953 1.00 21.63 O
601	ATOM 198 CB SER A 28 11.333 31.621 29.899 1.00 25.53 C
602	ATOM 199 OG SER A 28 10.451 32.194 30.829 1.00 33.03 O
603	ATOM 200 N VAL A 29 14.486 30.801 29.950 1.00 19.17 N
604	ATOM 201 CA VAL A 29 15.529 29.963 29.363 1.00 18.36 C
605	ATOM 202 C VAL A 29 15.425 28.507 29.766 1.00 24.35 C
606	ATOM 203 O VAL A 29 15.211 28.163 30.933 1.00 22.86 O
607	ATOM 204 CB VAL A 29 16.934 30.442 29.652 1.00 15.08 C
608	ATOM 205 CG1 VAL A 29 17.876 29.787 28.643 1.00 14.92 C
609	ATOM 206 CG2 VAL A 29 17.000 31.949 29.493 1.00 16.43 C
610	ATOM 207 N SER A 30 15.641 27.655 28.773 1.00 24.49 N
611	ATOM 208 CA SER A 30 15.660 26.239 29.013 1.00 23.16 C
612	ATOM 209 C SER A 30 16.996 25.670 28.604 1.00 20.94 C
613	ATOM 210 O SER A 30 17.539 26.038 27.567 1.00 12.63 O
614	ATOM 211 CB SER A 30 14.536 25.516 28.290 1.00 32.79 C
615	ATOM 212 OG SER A 30 14.034 24.484 29.120 1.00 66.33 O
616	ATOM 213 N GLY A 31 17.523 24.782 29.437 1.00 18.03 N
617	ATOM 214 CA GLY A 31 18.777 24.160 29.110 1.00 16.80 C
618	ATOM 215 C GLY A 31 18.766 22.659 29.368 1.00 13.64 C
619	ATOM 216 O GLY A 31 18.174 22.181 30.338 1.00 16.45 O
620	ATOM 217 N GLU A 32 19.518 21.974 28.517 1.00 12.49 N
621	ATOM 218 CA GLU A 32 19.746 20.544 28.548 1.00 14.06 C
622	ATOM 219 C GLU A 32 21.227 20.221 28.351 1.00 21.37 C
623	ATOM 220 O GLU A 32 21.893 20.873 27.570 1.00 14.62 O
624	ATOM 221 CB GLU A 32 19.057 19.887 27.333 1.00 10.61 C
625	ATOM 222 CG GLU A 32 17.538 20.069 27.289 1.00 11.49 C
626	ATOM 223 CD GLU A 32 16.957 19.352 26.098 1.00 35.38 C
627	ATOM 224 OE1 GLU A 32 17.613 18.720 25.293 1.00 30.84 O
628	ATOM 225 OE2 GLU A 32 15.682 19.550 25.978 1.00 32.83 O
629	ATOM 226 N GLY A 33 21.694 19.119 28.940 1.00 16.27 N
630	ATOM 227 CA GLY A 33 23.060 18.639 28.737 1.00 11.40 C
631	ATOM 228 C GLY A 33 23.433 17.517 29.695 1.00 17.29 C
632	ATOM 229 O GLY A 33 22.569 16.814 30.184 1.00 23.74 O
633	ATOM 230 N GLU A 34 24.726 17.351 29.974 1.00 17.15 N
634	ATOM 231 CA GLU A 34 25.153 16.346 30.933 1.00 15.99 C
635	ATOM 232 C GLU A 34 26.363 16.791 31.705 1.00 26.61 C
636	ATOM 233 O GLU A 34 27.075 17.696 31.306 1.00 22.99 O
637	ATOM 234 CB GLU A 34 25.553 15.049 30.278 1.00 13.63 C
638	ATOM 235 CG GLU A 34 25.917 15.242 28.819 1.00 20.94 C
639	ATOM 236 CD GLU A 34 25.868 13.935 28.088 1.00 76.43 C
640	ATOM 237 OE1 GLU A 34 26.791 13.511 27.421 1.00 71.59 O
641	ATOM 238 OE2 GLU A 34 24.764 13.265 28.326 1.00 60.44 O
642	ATOM 239 N GLY A 35 26.604 16.075 32.781 1.00 19.05 N
643	ATOM 240 CA GLY A 35 27.728 16.305 33.636 1.00 25.04 C
644	ATOM 241 C GLY A 35 28.405 14.982 33.979 1.00 33.66 C
645	ATOM 242 O GLY A 35 27.771 13.920 34.033 1.00 19.37 O
646	ATOM 243 N ASP A 36 29.711 15.080 34.186 1.00 24.79 N
647	ATOM 244 CA ASP A 36 30.565 13.970 34.511 1.00 18.45 C
648	ATOM 245 C ASP A 36 31.543 14.463 35.544 1.00 18.56 C
649	ATOM 246 O ASP A 36 32.562 15.094 35.207 1.00 17.62 O
650	ATOM 247 CB ASP A 36 31.276 13.488 33.243 1.00 20.10 C
651	ATOM 248 CG ASP A 36 31.879 12.118 33.355 1.00 23.66 C
652	ATOM 249 OD1 ASP A 36 32.304 11.503 32.400 1.00 31.21 O
653	ATOM 250 OD2 ASP A 36 31.922 11.669 34.572 1.00 17.37 O
654	ATOM 251 N ALA A 37 31.131 14.274 36.797 1.00 13.87 N
655	ATOM 252 CA ALA A 37 31.843 14.752 37.961 1.00 15.81 C
656	ATOM 253 C ALA A 37 33.234 14.130 38.080 1.00 29.91 C
657	ATOM 254 O ALA A 37 34.128 14.687 38.709 1.00 23.70 O
658	ATOM 255 CB ALA A 37 31.015 14.543 39.220 1.00 8.84 C
659	ATOM 256 N THR A 38 33.398 12.975 37.440 1.00 25.49 N
660	ATOM 257 CA THR A 38 34.668 12.281 37.440 1.00 24.30 C
661	ATOM 258 C THR A 38 35.734 13.152 36.813 1.00 17.08 C
662	ATOM 259 O THR A 38 36.846 13.247 37.292 1.00 19.80 O
663	ATOM 260 CB THR A 38 34.581 10.927 36.717 1.00 22.18 C
664	ATOM 261 OG1 THR A 38 33.593 10.118 37.327 1.00 38.17 O
665	ATOM 262 CG2 THR A 38 35.930 10.231 36.822 1.00 28.68 C
666	ATOM 263 N TYR A 39 35.357 13.832 35.756 1.00 13.99 N
667	ATOM 264 CA TYR A 39 36.240 14.734 35.048 1.00 20.60 C
668	ATOM 265 C TYR A 39 35.927 16.190 35.339 1.00 18.00 C
669	ATOM 266 O TYR A 39 36.540 17.046 34.761 1.00 15.48 O
670	ATOM 267 CB TYR A 39 36.216 14.421 33.521 1.00 23.94 C
671	ATOM 268 CG TYR A 39 36.451 12.933 33.350 1.00 30.54 C
672	ATOM 269 CD1 TYR A 39 37.748 12.438 33.238 1.00 29.51 C
673	ATOM 270 CD2 TYR A 39 35.428 12.012 33.568 1.00 36.28 C
674	ATOM 271 CE1 TYR A 39 38.010 11.071 33.242 1.00 19.80 C
675	ATOM 272 CE2 TYR A 39 35.661 10.638 33.576 1.00 37.23 C
676	ATOM 273 CZ TYR A 39 36.964 10.164 33.379 1.00 36.70 C
677	ATOM 274 OH TYR A 39 37.221 8.805 33.339 1.00 49.00 O
678	ATOM 275 N GLY A 40 34.977 16.465 36.241 1.00 17.06 N
679	ATOM 276 CA GLY A 40 34.559 17.839 36.511 1.00 14.89 C
680	ATOM 277 C GLY A 40 34.058 18.508 35.217 1.00 20.88 C
681	ATOM 278 O GLY A 40 34.173 19.715 35.010 1.00 24.07 O
682	ATOM 279 N LYS A 41 33.522 17.692 34.317 1.00 7.48 N
683	ATOM 280 CA LYS A 41 33.096 18.167 33.026 1.00 6.09 C
684	ATOM 281 C LYS A 41 31.579 18.379 32.952 1.00 23.30 C
685	ATOM 282 O LYS A 41 30.803 17.631 33.553 1.00 11.95 O
686	ATOM 283 CB LYS A 41 33.505 17.164 31.972 1.00 6.09 C
687	ATOM 284 CG LYS A 41 33.421 17.683 30.547 1.00 15.03 C
688	ATOM 285 CD LYS A 41 33.649 16.565 29.527 1.00 12.91 C
689	ATOM 286 CE LYS A 41 34.130 17.053 28.171 1.00 33.70 C
690	ATOM 287 NZ LYS A 41 34.795 16.012 27.370 1.00 41.79 N
691	ATOM 288 N LEU A 42 31.192 19.400 32.183 1.00 19.11 N
692	ATOM 289 CA LEU A 42 29.815 19.828 31.972 1.00 20.63 C
693	ATOM 290 C LEU A 42 29.648 20.296 30.570 1.00 22.76 C
694	ATOM 291 O LEU A 42 30.453 21.090 30.089 1.00 26.20 O
695	ATOM 292 CB LEU A 42 29.480 21.101 32.782 1.00 23.21 C
696	ATOM 293 CG LEU A 42 29.049 20.791 34.183 1.00 38.10 C
697	ATOM 294 CD1 LEU A 42 28.675 22.070 34.913 1.00 41.09 C
698	ATOM 295 CD2 LEU A 42 27.891 19.799 34.136 1.00 53.01 C
699	ATOM 296 N THR A 43 28.546 19.888 29.973 1.00 11.64 N
700	ATOM 297 CA THR A 43 28.149 20.344 28.654 1.00 14.41 C
701	ATOM 298 C THR A 43 26.672 20.678 28.690 1.00 24.77 C
702	ATOM 299 O THR A 43 25.852 19.856 29.096 1.00 19.34 O
703	ATOM 300 CB THR A 43 28.481 19.370 27.524 1.00 37.28 C
704	ATOM 301 OG1 THR A 43 29.820 18.934 27.673 1.00 45.14 O
705	ATOM 302 CG2 THR A 43 28.337 20.118 26.205 1.00 43.31 C
706	ATOM 303 N LEU A 44 26.366 21.929 28.386 1.00 19.65 N
707	ATOM 304 CA LEU A 44 25.008 22.433 28.440 1.00 21.77 C
708	ATOM 305 C LEU A 44 24.724 23.301 27.252 1.00 21.19 C
709	ATOM 306 O LEU A 44 25.603 24.004 26.765 1.00 13.09 O
710	ATOM 307 CB LEU A 44 24.796 23.336 29.663 1.00 22.83 C
711	ATOM 308 CG LEU A 44 24.433 22.634 30.968 1.00 30.40 C
712	ATOM 309 CD1 LEU A 44 23.012 22.056 30.918 1.00 29.83 C
713	ATOM 310 CD2 LEU A 44 25.464 21.565 31.277 1.00 45.21 C
714	ATOM 311 N LYS A 45 23.468 23.281 26.838 1.00 19.54 N
715	ATOM 312 CA LYS A 45 22.983 24.104 25.753 1.00 21.19 C
716	ATOM 313 C LYS A 45 21.708 24.783 26.207 1.00 26.01 C
717	ATOM 314 O LYS A 45 20.786 24.093 26.667 1.00 25.78 O
718	ATOM 315 CB LYS A 45 22.757 23.310 24.480 1.00 18.14 C
719	ATOM 316 CG LYS A 45 22.098 24.155 23.426 1.00 17.79 C
720	ATOM 317 CD LYS A 45 22.127 23.547 22.044 1.00 24.09 C
721	ATOM 318 CE LYS A 45 21.552 24.487 21.000 1.00 32.02 C
722	ATOM 319 NZ LYS A 45 20.887 23.777 19.892 1.00 16.34 N
723	ATOM 320 N PHE A 46 21.687 26.119 26.116 1.00 16.33 N
724	ATOM 321 CA PHE A 46 20.552 26.923 26.564 1.00 13.89 C
725	ATOM 322 C PHE A 46 19.816 27.594 25.458 1.00 15.47 C
726	ATOM 323 O PHE A 46 20.409 28.104 24.535 1.00 16.58 O
727	ATOM 324 CB PHE A 46 20.985 28.038 27.499 1.00 16.90 C
728	ATOM 325 CG PHE A 46 21.825 27.493 28.597 1.00 13.49 C
729	ATOM 326 CD1 PHE A 46 23.210 27.500 28.487 1.00 16.33 C
730	ATOM 327 CD2 PHE A 46 21.222 26.962 29.737 1.00 17.49 C
731	ATOM 328 CE1 PHE A 46 24.000 27.018 29.526 1.00 10.21 C
732	ATOM 329 CE2 PHE A 46 21.996 26.466 30.781 1.00 23.53 C
733	ATOM 330 CZ PHE A 46 23.385 26.477 30.653 1.00 13.50 C
734	ATOM 331 N ILE A 47 18.511 27.670 25.608 1.00 20.78 N
735	ATOM 332 CA ILE A 47 17.692 28.319 24.606 1.00 15.95 C
736	ATOM 333 C ILE A 47 16.799 29.339 25.273 1.00 19.35 C
737	ATOM 334 O ILE A 47 16.236 29.074 26.340 1.00 21.56 O
738	ATOM 335 CB ILE A 47 16.837 27.321 23.845 1.00 20.17 C
739	ATOM 336 CG1 ILE A 47 17.676 26.304 23.075 1.00 18.20 C
740	ATOM 337 CG2 ILE A 47 15.890 28.057 22.919 1.00 18.93 C
741	ATOM 338 CD1 ILE A 47 18.955 26.892 22.499 1.00 57.90 C
742	ATOM 339 N CYS A 48 16.735 30.537 24.689 1.00 28.78 N
743	ATOM 340 CA CYS A 48 15.842 31.553 25.222 1.00 27.10 C
744	ATOM 341 C CYS A 48 14.518 31.279 24.595 1.00 26.81 C
745	ATOM 342 O CYS A 48 14.354 31.475 23.401 1.00 22.00 O
746	ATOM 343 CB CYS A 48 16.204 32.990 24.873 1.00 22.73 C
747	ATOM 344 SG CYS A 48 15.033 34.109 25.669 1.00 21.05 S
748	ATOM 345 N THR A 49 13.601 30.768 25.377 1.00 27.65 N
749	ATOM 346 CA THR A 49 12.331 30.369 24.805 1.00 27.42 C
750	ATOM 347 C THR A 49 11.379 31.495 24.443 1.00 27.12 C
751	ATOM 348 O THR A 49 10.547 31.336 23.560 1.00 33.42 O
752	ATOM 349 CB THR A 49 11.699 29.216 25.591 1.00 25.68 C
753	ATOM 350 OG1 THR A 49 11.677 29.489 26.981 1.00 25.38 O
754	ATOM 351 CG2 THR A 49 12.538 27.972 25.342 1.00 17.28 C
755	ATOM 352 N THR A 50 11.552 32.637 25.103 1.00 26.86 N
756	ATOM 353 CA THR A 50 10.732 33.812 24.902 1.00 22.24 C
757	ATOM 354 C THR A 50 11.182 34.700 23.759 1.00 39.07 C
758	ATOM 355 O THR A 50 10.635 35.782 23.550 1.00 46.40 O
759	ATOM 356 CB THR A 50 10.597 34.608 26.199 1.00 18.12 C
760	ATOM 357 OG1 THR A 50 11.885 34.910 26.733 1.00 26.70 O
761	ATOM 358 CG2 THR A 50 9.820 33.773 27.204 1.00 14.08 C
762	ATOM 359 N GLY A 51 12.174 34.239 23.016 1.00 46.87 N
763	ATOM 360 CA GLY A 51 12.701 34.998 21.890 1.00 53.47 C
764	ATOM 361 C GLY A 51 14.213 35.256 21.950 1.00 59.97 C
765	ATOM 362 O GLY A 51 15.023 34.328 21.827 1.00 69.65 O
766	ATOM 363 N LYS A 52 14.565 36.550 22.071 1.00 44.46 N
767	ATOM 364 CA LYS A 52 15.951 37.017 22.154 1.00 40.87 C
768	ATOM 365 C LYS A 52 16.232 37.416 23.584 1.00 36.07 C
769	ATOM 366 O LYS A 52 15.407 38.060 24.223 1.00 31.66 O
770	ATOM 367 CB LYS A 52 16.283 38.165 21.192 1.00 42.34 C
771	ATOM 368 CG LYS A 52 15.945 37.886 19.726 1.00 72.93 C
772	ATOM 369 CD LYS A 52 17.146 37.927 18.781 1.00 94.52 C
773	ATOM 370 CE LYS A 52 17.180 39.167 17.889 1.00100.00 C
774	ATOM 371 NZ LYS A 52 16.369 39.055 16.661 1.00100.00 N
775	ATOM 372 N LEU A 53 17.354 36.963 24.115 1.00 24.07 N
776	ATOM 373 CA LEU A 53 17.676 37.245 25.495 1.00 19.87 C
777	ATOM 374 C LEU A 53 17.874 38.746 25.761 1.00 26.66 C
778	ATOM 375 O LEU A 53 18.646 39.430 25.086 1.00 23.36 O
779	ATOM 376 CB LEU A 53 18.907 36.418 25.900 1.00 16.54 C
780	ATOM 377 CG LEU A 53 19.058 36.285 27.393 1.00 23.01 C
781	ATOM 378 CD1 LEU A 53 17.976 35.316 27.909 1.00 26.89 C
782	ATOM 379 CD2 LEU A 53 20.448 35.718 27.652 1.00 25.23 C
783	ATOM 380 N PRO A 54 17.187 39.274 26.766 1.00 20.52 N
784	ATOM 381 CA PRO A 54 17.286 40.694 27.075 1.00 23.40 C
785	ATOM 382 C PRO A 54 18.653 41.159 27.564 1.00 32.99 C
786	ATOM 383 O PRO A 54 18.983 42.324 27.400 1.00 34.98 O
787	ATOM 384 CB PRO A 54 16.268 40.971 28.184 1.00 24.50 C
788	ATOM 385 CG PRO A 54 15.842 39.623 28.724 1.00 22.34 C
789	ATOM 386 CD PRO A 54 16.227 38.590 27.665 1.00 17.25 C
790	ATOM 387 N VAL A 55 19.392 40.275 28.239 1.00 26.42 N
791	ATOM 388 CA VAL A 55 20.706 40.579 28.771 1.00 18.61 C
792	ATOM 389 C VAL A 55 21.741 39.807 28.016 1.00 19.77 C
793	ATOM 390 O VAL A 55 21.382 39.142 27.071 1.00 21.72 O
794	ATOM 391 CB VAL A 55 20.799 40.307 30.247 1.00 19.81 C
795	ATOM 392 CG1 VAL A 55 19.894 41.282 30.974 1.00 23.23 C
796	ATOM 393 CG2 VAL A 55 20.360 38.875 30.541 1.00 16.72 C
797	ATOM 394 N PRO A 56 23.024 39.881 28.408 1.00 26.31 N
798	ATOM 395 CA PRO A 56 24.005 39.135 27.657 1.00 20.93 C
799	ATOM 396 C PRO A 56 24.267 37.773 28.281 1.00 17.77 C
800	ATOM 397 O PRO A 56 24.340 37.625 29.517 1.00 12.52 O
801	ATOM 398 CB PRO A 56 25.254 40.006 27.534 1.00 22.84 C
802	ATOM 399 CG PRO A 56 24.923 41.326 28.214 1.00 24.17 C
803	ATOM 400 CD PRO A 56 23.673 41.059 29.041 1.00 22.94 C
804	ATOM 401 N TRP A 57 24.342 36.771 27.387 1.00 15.45 N
805	ATOM 402 CA TRP A 57 24.525 35.388 27.794 1.00 20.83 C
806	ATOM 403 C TRP A 57 25.612 35.210 28.856 1.00 20.30 C
807	ATOM 404 O TRP A 57 25.404 34.579 29.893 1.00 22.22 O
808	ATOM 405 CB TRP A 57 24.717 34.433 26.597 1.00 17.50 C
809	ATOM 406 CG TRP A 57 23.487 34.101 25.758 1.00 18.43 C
810	ATOM 407 CD1 TRP A 57 23.239 34.534 24.482 1.00 19.97 C
811	ATOM 408 CD2 TRP A 57 22.421 33.182 26.066 1.00 16.74 C
812	ATOM 409 NE1 TRP A 57 22.101 33.961 23.980 1.00 16.98 N
813	ATOM 410 CE2 TRP A 57 21.564 33.138 24.940 1.00 19.64 C
814	ATOM 411 CE3 TRP A 57 22.074 32.438 27.206 1.00 19.34 C
815	ATOM 412 CZ2 TRP A 57 20.404 32.344 24.926 1.00 18.35 C
816	ATOM 413 CZ3 TRP A 57 20.932 31.650 27.187 1.00 16.63 C
817	ATOM 414 CH2 TRP A 57 20.110 31.607 26.054 1.00 17.29 C
818	ATOM 415 N PRO A 58 26.765 35.826 28.627 1.00 18.82 N
819	ATOM 416 CA PRO A 58 27.833 35.663 29.564 1.00 10.60 C
820	ATOM 417 C PRO A 58 27.468 36.020 30.970 1.00 14.61 C
821	ATOM 418 O PRO A 58 28.036 35.450 31.897 1.00 15.04 O
822	ATOM 419 CB PRO A 58 29.050 36.413 29.029 1.00 13.11 C
823	ATOM 420 CG PRO A 58 28.759 36.696 27.569 1.00 14.99 C
824	ATOM 421 CD PRO A 58 27.248 36.573 27.418 1.00 14.13 C
825	ATOM 422 N THR A 59 26.504 36.925 31.142 1.00 10.55 N
826	ATOM 423 CA THR A 59 26.063 37.291 32.489 1.00 6.26 C
827	ATOM 424 C THR A 59 25.254 36.208 33.127 1.00 4.80 C
828	ATOM 425 O THR A 59 25.015 36.245 34.333 1.00 10.60 O
829	ATOM 426 CB THR A 59 25.186 38.553 32.531 1.00 16.17 C
830	ATOM 427 OG1 THR A 59 23.986 38.328 31.801 1.00 19.28 O
831	ATOM 428 CG2 THR A 59 25.960 39.716 31.938 1.00 28.08 C
832	ATOM 429 N LEU A 60 24.797 35.248 32.333 1.00 6.68 N
833	ATOM 430 CA LEU A 60 23.948 34.194 32.923 1.00 14.48 C
834	ATOM 431 C LEU A 60 24.650 32.914 33.319 1.00 27.20 C
835	ATOM 432 O LEU A 60 24.139 32.170 34.149 1.00 18.33 O
836	ATOM 433 CB LEU A 60 22.756 33.891 32.006 1.00 16.06 C
837	ATOM 434 CG LEU A 60 21.920 35.154 31.818 1.00 17.19 C
838	ATOM 435 CD1 LEU A 60 20.838 34.924 30.789 1.00 21.74 C
839	ATOM 436 CD2 LEU A 60 21.297 35.538 33.146 1.00 15.03 C
840	ATOM 437 N VAL A 61 25.819 32.673 32.702 1.00 24.04 N
841	ATOM 438 CA VAL A 61 26.645 31.495 32.946 1.00 18.36 C
842	ATOM 439 C VAL A 61 26.662 30.966 34.375 1.00 12.19 C
843	ATOM 440 O VAL A 61 26.511 29.763 34.625 1.00 17.44 O
844	ATOM 441 CB VAL A 61 28.078 31.701 32.444 1.00 15.36 C
845	ATOM 442 CG1 VAL A 61 29.028 30.591 32.933 1.00 8.84 C
846	ATOM 443 CG2 VAL A 61 28.090 31.809 30.920 1.00 10.07 C
847	ATOM 444 N THR A 62 26.929 31.836 35.335 1.00 18.60 N
848	ATOM 445 CA THR A 62 27.078 31.359 36.705 1.00 17.78 C
849	ATOM 446 C THR A 62 25.790 30.920 37.361 1.00 16.65 C
850	ATOM 447 O THR A 62 25.774 30.185 38.367 1.00 8.30 O
851	ATOM 448 CB THR A 62 27.830 32.362 37.600 1.00 22.65 C
852	ATOM 449 OG1 THR A 62 27.139 33.604 37.751 1.00 14.82 O
853	ATOM 450 CG2 THR A 62 29.262 32.540 37.118 1.00 14.51 C
854	ATOM 451 N THR A 63 24.723 31.487 36.845 1.00 16.31 N
855	ATOM 452 CA THR A 63 23.396 31.232 37.379 1.00 14.49 C
856	ATOM 453 C THR A 63 22.932 29.884 36.879 1.00 5.42 C
857	ATOM 454 O THR A 63 22.512 29.032 37.647 1.00 13.09 O
858	ATOM 455 CB THR A 63 22.482 32.380 36.914 1.00 19.48 C
859	ATOM 456 OG1 THR A 63 22.854 33.511 37.651 1.00 9.43 O
860	ATOM 457 CG2 THR A 63 21.007 32.072 37.173 1.00 16.12 C
861	ATOM 458 N PHE A 64 23.113 29.704 35.574 1.00 1.67 N
862	ATOM 459 CA PHE A 64 22.798 28.476 34.890 1.00 8.35 C
863	ATOM 460 C PHE A 64 23.647 27.339 35.403 1.00 60.52 C
864	ATOM 461 O PHE A 64 23.164 26.235 35.662 1.00 19.40 O
865	ATOM 462 CB PHE A 64 23.173 28.624 33.428 1.00 9.28 C
866	ATOM 463 CG PHE A 64 22.265 29.526 32.660 1.00 17.39 C
867	ATOM 464 CD1 PHE A 64 22.709 30.113 31.475 1.00 16.38 C
868	ATOM 465 CD2 PHE A 64 20.963 29.770 33.103 1.00 18.65 C
869	ATOM 466 CE1 PHE A 64 21.864 30.933 30.725 1.00 19.75 C
870	ATOM 467 CE2 PHE A 64 20.096 30.560 32.346 1.00 19.37 C
871	ATOM 468 CZ PHE A 64 20.554 31.141 31.162 1.00 18.63 C
872	HETATM 469 C1 IIC A 66 26.589 27.058 37.112 1.00 5.23 C
873	HETATM 470 N2 IIC A 66 27.875 27.700 37.197 1.00 8.50 N
874	HETATM 471 CA2 IIC A 66 28.092 28.054 38.561 1.00 9.52 C
875	HETATM 472 C2 IIC A 66 26.899 27.674 39.362 1.00 1.00 C
876	HETATM 473 O2 IIC A 66 26.769 27.659 40.557 1.00 22.50 O
877	HETATM 474 N3 IIC A 66 26.065 27.009 38.390 1.00 16.14 N
878	HETATM 475 CA1 IIC A 66 25.925 26.647 35.850 1.00 3.62 C
879	HETATM 476 N1 IIC A 66 24.947 27.619 35.442 1.00 30.34 N
880	HETATM 477 CB1 IIC A 66 26.790 26.236 34.651 1.00 19.32 C
881	HETATM 478 OG1 IIC A 66 27.734 25.285 35.063 1.00 18.74 O
882	HETATM 479 CA3 IIC A 66 24.719 26.554 38.680 1.00 17.05 C
883	HETATM 480 C3 IIC A 66 24.595 25.182 39.315 1.00 6.60 C
884	HETATM 481 O3 IIC A 66 23.733 24.940 40.139 1.00 23.88 O
885	HETATM 482 CB2 IIC A 66 29.212 28.660 39.007 1.00 19.99 C
886	HETATM 483 CG2 IIC A 66 30.330 29.074 38.098 1.00 9.87 C
887	HETATM 484 ND1 IIC A 66 30.322 28.828 36.727 1.00 12.20 N
888	HETATM 485 CE1 IIC A 66 31.407 29.416 36.217 1.00 20.41 C
889	HETATM 486 NE2 IIC A 66 32.150 29.936 37.202 1.00 13.18 N
890	HETATM 487 CD2 IIC A 66 31.494 29.748 38.398 1.00 15.02 C
891	ATOM 488 N VAL A 68 25.436 24.274 38.866 1.00 22.04 N
892	ATOM 489 CA VAL A 68 25.384 22.906 39.306 1.00 16.40 C
893	ATOM 490 C VAL A 68 26.746 22.383 39.770 1.00 15.61 C
894	ATOM 491 O VAL A 68 27.269 21.420 39.269 1.00 12.50 O
895	ATOM 492 CB VAL A 68 24.751 22.104 38.184 1.00 20.56 C
896	ATOM 493 CG1 VAL A 68 23.299 22.567 38.079 1.00 19.53 C
897	ATOM 494 CG2 VAL A 68 25.427 22.418 36.859 1.00 19.69 C
898	ATOM 495 N GLN A 69 27.302 23.065 40.759 1.00 13.53 N
899	ATOM 496 CA GLN A 69 28.602 22.771 41.297 1.00 8.18 C
900	ATOM 497 C GLN A 69 28.809 21.371 41.850 1.00 21.98 C
901	ATOM 498 O GLN A 69 29.938 21.029 42.197 1.00 16.93 O
902	ATOM 499 CB GLN A 69 29.020 23.854 42.245 1.00 5.11 C
903	ATOM 500 CG GLN A 69 28.905 25.186 41.506 1.00 10.84 C
904	ATOM 501 CD GLN A 69 29.023 26.340 42.449 1.00 23.39 C
905	ATOM 502 OE1 GLN A 69 28.326 26.396 43.479 1.00 23.51 O
906	ATOM 503 NE2 GLN A 69 29.964 27.224 42.140 1.00 15.55 N
907	ATOM 504 N CYS A 70 27.736 20.557 41.883 1.00 17.36 N
908	ATOM 505 CA CYS A 70 27.829 19.159 42.315 1.00 11.53 C
909	ATOM 506 C CYS A 70 28.562 18.343 41.252 1.00 8.17 C
910	ATOM 507 O CYS A 70 28.969 17.230 41.496 1.00 16.01 O
911	ATOM 508 CB CYS A 70 26.455 18.517 42.660 1.00 8.57 C
912	ATOM 509 SG CYS A 70 25.267 18.752 41.328 1.00 13.38 S
913	ATOM 510 N PHE A 71 28.759 18.925 40.054 1.00 4.75 N
914	ATOM 511 CA PHE A 71 29.511 18.293 38.987 1.00 7.58 C
915	ATOM 512 C PHE A 71 31.022 18.608 39.022 1.00 20.85 C
916	ATOM 513 O PHE A 71 31.748 18.351 38.062 1.00 15.92 O
917	ATOM 514 CB PHE A 71 28.965 18.619 37.591 1.00 9.49 C
918	ATOM 515 CG PHE A 71 27.685 17.860 37.357 1.00 21.79 C
919	ATOM 516 CD1 PHE A 71 27.711 16.472 37.201 1.00 14.23 C
920	ATOM 517 CD2 PHE A 71 26.450 18.508 37.441 1.00 22.20 C
921	ATOM 518 CE1 PHE A 71 26.523 15.755 37.073 1.00 12.68 C
922	ATOM 519 CE2 PHE A 71 25.256 17.805 37.263 1.00 23.89 C
923	ATOM 520 CZ PHE A 71 25.295 16.421 37.081 1.00 10.97 C
924	ATOM 521 N SER A 72 31.467 19.219 40.114 1.00 19.15 N
925	ATOM 522 CA SER A 72 32.854 19.583 40.322 1.00 15.37 C
926	ATOM 523 C SER A 72 33.623 18.342 40.638 1.00 21.33 C
927	ATOM 524 O SER A 72 33.087 17.444 41.275 1.00 15.54 O
928	ATOM 525 CB SER A 72 32.992 20.506 41.534 1.00 15.10 C
929	ATOM 526 OG SER A 72 32.436 21.785 41.264 1.00 21.75 O
930	ATOM 527 N ARG A 73 34.877 18.300 40.236 1.00 22.60 N
931	ATOM 528 CA ARG A 73 35.696 17.149 40.556 1.00 20.31 C
932	ATOM 529 C ARG A 73 36.448 17.413 41.827 1.00 19.69 C
933	ATOM 530 O ARG A 73 37.248 18.327 41.858 1.00 20.20 O
934	ATOM 531 CB ARG A 73 36.713 16.826 39.459 1.00 19.42 C
935	ATOM 532 CG ARG A 73 37.705 15.743 39.890 1.00 19.68 C
936	ATOM 533 CD ARG A 73 38.528 15.173 38.726 1.00 16.80 C
937	ATOM 534 NE ARG A 73 39.699 15.981 38.365 1.00 41.50 N
938	ATOM 535 CZ ARG A 73 40.849 15.995 39.054 1.00 65.64 C
939	ATOM 536 NH1 ARG A 73 41.016 15.257 40.165 1.00 19.31 N
940	ATOM 537 NH2 ARG A 73 41.855 16.776 38.621 1.00 38.45 N
941	ATOM 538 N TYR A 74 36.177 16.628 42.869 1.00 19.12 N
942	ATOM 539 CA TYR A 74 36.894 16.748 44.131 1.00 16.98 C
943	ATOM 540 C TYR A 74 37.983 15.678 44.186 1.00 28.43 C
944	ATOM 541 O TYR A 74 37.668 14.503 44.081 1.00 27.60 O
945	ATOM 542 CB TYR A 74 35.968 16.592 45.336 1.00 12.01 C
946	ATOM 543 CG TYR A 74 35.311 17.882 45.747 1.00 17.78 C
947	ATOM 544 CD1 TYR A 74 34.366 18.509 44.929 1.00 17.25 C
948	ATOM 545 CD2 TYR A 74 35.672 18.497 46.943 1.00 12.25 C
949	ATOM 546 CE1 TYR A 74 33.773 19.717 45.293 1.00 10.72 C
950	ATOM 547 CE2 TYR A 74 35.081 19.694 47.333 1.00 16.66 C
951	ATOM 548 CZ TYR A 74 34.129 20.296 46.510 1.00 18.84 C
952	ATOM 549 OH TYR A 74 33.555 21.469 46.905 1.00 17.48 O
953	ATOM 550 N PRO A 75 39.260 16.071 44.285 1.00 19.31 N
954	ATOM 551 CA PRO A 75 40.303 15.078 44.375 1.00 13.83 C
955	ATOM 552 C PRO A 75 40.022 14.134 45.515 1.00 16.34 C
956	ATOM 553 O PRO A 75 39.403 14.499 46.492 1.00 17.67 O
957	ATOM 554 CB PRO A 75 41.610 15.833 44.635 1.00 16.27 C
958	ATOM 555 CG PRO A 75 41.360 17.275 44.262 1.00 23.36 C
959	ATOM 556 CD PRO A 75 39.852 17.408 44.050 1.00 19.97 C
960	ATOM 557 N ASP A 76 40.498 12.908 45.401 1.00 18.02 N
961	ATOM 558 CA ASP A 76 40.250 11.913 46.430 1.00 20.54 C
962	ATOM 559 C ASP A 76 40.576 12.403 47.822 1.00 24.09 C
963	ATOM 560 O ASP A 76 39.897 12.091 48.790 1.00 20.00 O
964	ATOM 561 CB ASP A 76 40.959 10.569 46.169 1.00 22.20 C
965	ATOM 562 CG ASP A 76 40.855 9.701 47.382 1.00 36.71 C
966	ATOM 563 OD1 ASP A 76 41.613 9.786 48.329 1.00 47.57 O
967	ATOM 564 OD2 ASP A 76 39.749 9.005 47.397 1.00 52.85 O
968	ATOM 565 N HIS A 77 41.646 13.156 47.942 1.00 28.67 N
969	ATOM 566 CA HIS A 77 42.002 13.648 49.259 1.00 31.44 C
970	ATOM 567 C HIS A 77 41.047 14.724 49.766 1.00 28.40 C
971	ATOM 568 O HIS A 77 41.056 15.053 50.933 1.00 23.53 O
972	ATOM 569 CB HIS A 77 43.473 14.123 49.350 1.00 31.77 C
973	ATOM 570 CG HIS A 77 43.749 15.423 48.650 1.00 37.34 C
974	ATOM 571 ND1 HIS A 77 43.852 15.500 47.257 1.00 39.29 N
975	ATOM 572 CD2 HIS A 77 43.953 16.679 49.158 1.00 36.53 C
976	ATOM 573 CE1 HIS A 77 44.107 16.771 46.958 1.00 36.24 C
977	ATOM 574 NE2 HIS A 77 44.175 17.507 48.075 1.00 35.68 N
978	ATOM 575 N MET A 78 40.215 15.283 48.896 1.00 24.27 N
979	ATOM 576 CA MET A 78 39.347 16.362 49.332 1.00 25.38 C
980	ATOM 577 C MET A 78 37.876 16.026 49.437 1.00 24.38 C
981	ATOM 578 O MET A 78 37.053 16.876 49.775 1.00 20.06 O
982	ATOM 579 CB MET A 78 39.497 17.541 48.376 1.00 23.82 C
983	ATOM 580 CG MET A 78 40.681 18.417 48.705 1.00 25.67 C
984	ATOM 581 SD MET A 78 40.782 19.738 47.485 1.00 35.66 S
985	ATOM 582 CE MET A 78 39.543 20.885 48.167 1.00 27.19 C
986	ATOM 583 N LYS A 79 37.550 14.811 49.088 1.00 20.87 N
987	ATOM 584 CA LYS A 79 36.185 14.342 49.074 1.00 26.10 C
988	ATOM 585 C LYS A 79 35.333 14.700 50.297 1.00 27.97 C
989	ATOM 586 O LYS A 79 34.139 15.020 50.182 1.00 31.88 O
990	ATOM 587 CB LYS A 79 36.117 12.872 48.672 1.00 27.38 C
991	ATOM 588 CG LYS A 79 37.049 12.570 47.507 1.00 53.90 C
992	ATOM 589 CD LYS A 79 36.354 11.868 46.357 1.00 61.11 C
993	ATOM 590 CE LYS A 79 37.098 11.968 45.043 1.00 82.64 C
994	ATOM 591 NZ LYS A 79 36.316 12.648 43.998 1.00 94.60 N
995	ATOM 592 N ARG A 80 35.927 14.640 51.479 1.00 23.16 N
996	ATOM 593 CA ARG A 80 35.172 14.966 52.682 1.00 21.86 C
997	ATOM 594 C ARG A 80 34.669 16.404 52.703 1.00 23.08 C
998	ATOM 595 O ARG A 80 33.927 16.802 53.604 1.00 21.18 O
999	ATOM 596 CB ARG A 80 35.921 14.616 53.974 1.00 21.33 C
1000	ATOM 597 CG ARG A 80 36.875 15.717 54.416 1.00 35.67 C
1001	ATOM 598 CD ARG A 80 37.534 15.467 55.779 1.00 36.28 C
1002	ATOM 599 NE ARG A 80 37.053 16.390 56.806 1.00 53.66 N
1003	ATOM 600 CZ ARG A 80 37.799 17.300 57.429 1.00 49.65 C
1004	ATOM 601 NH1 ARG A 80 39.105 17.452 57.184 1.00 31.40 N
1005	ATOM 602 NH2 ARG A 80 37.216 18.080 58.335 1.00 61.68 N
1006	ATOM 603 N HIS A 81 35.051 17.184 51.692 1.00 19.94 N
1007	ATOM 604 CA HIS A 81 34.686 18.587 51.648 1.00 18.08 C
1008	ATOM 605 C HIS A 81 33.590 18.872 50.641 1.00 24.17 C
1009	ATOM 606 O HIS A 81 33.189 20.025 50.447 1.00 24.77 O
1010	ATOM 607 CB HIS A 81 35.941 19.468 51.367 1.00 16.17 C
1011	ATOM 608 CG HIS A 81 36.897 19.433 52.517 1.00 17.82 C
1012	ATOM 609 ND1 HIS A 81 36.601 20.041 53.725 1.00 22.73 N
1013	ATOM 610 CD2 HIS A 81 38.084 18.781 52.648 1.00 21.27 C
1014	ATOM 611 CE1 HIS A 81 37.607 19.779 54.538 1.00 25.75 C
1015	ATOM 612 NE2 HIS A 81 38.527 19.038 53.917 1.00 23.88 N
1016	ATOM 613 N ASP A 82 33.116 17.825 49.985 1.00 13.73 N
1017	ATOM 614 CA ASP A 82 32.127 18.049 48.945 1.00 13.69 C
1018	ATOM 615 C ASP A 82 30.735 18.242 49.480 1.00 23.82 C
1019	ATOM 616 O ASP A 82 29.989 17.303 49.651 1.00 13.71 O
1020	ATOM 617 CB ASP A 82 32.138 16.934 47.921 1.00 10.29 C
1021	ATOM 618 CG ASP A 82 31.432 17.286 46.657 1.00 11.93 C
1022	ATOM 619 OD1 ASP A 82 30.732 18.266 46.519 1.00 22.84 O
1023	ATOM 620 OD2 ASP A 82 31.801 16.525 45.671 1.00 12.25 O
1024	ATOM 621 N PHE A 83 30.370 19.463 49.744 1.00 18.39 N
1025	ATOM 622 CA PHE A 83 29.059 19.686 50.257 1.00 15.21 C
1026	ATOM 623 C PHE A 83 27.990 19.382 49.218 1.00 19.09 C
1027	ATOM 624 O PHE A 83 26.955 18.763 49.500 1.00 17.33 O
1028	ATOM 625 CB PHE A 83 28.938 21.142 50.717 1.00 18.81 C
1029	ATOM 626 CG PHE A 83 27.507 21.622 50.756 1.00 26.80 C
1030	ATOM 627 CD1 PHE A 83 26.749 21.491 51.921 1.00 34.11 C
1031	ATOM 628 CD2 PHE A 83 26.906 22.197 49.632 1.00 31.07 C
1032	ATOM 629 CE1 PHE A 83 25.417 21.912 51.963 1.00 32.69 C
1033	ATOM 630 CE2 PHE A 83 25.575 22.626 49.652 1.00 30.86 C
1034	ATOM 631 CZ PHE A 83 24.837 22.488 50.828 1.00 23.43 C
1035	ATOM 632 N PHE A 84 28.265 19.798 47.997 1.00 13.13 N
1036	ATOM 633 CA PHE A 84 27.319 19.687 46.923 1.00 13.99 C
1037	ATOM 634 C PHE A 84 26.732 18.326 46.688 1.00 27.27 C
1038	ATOM 635 O PHE A 84 25.521 18.187 46.473 1.00 23.91 O
1039	ATOM 636 CB PHE A 84 27.878 20.229 45.624 1.00 11.74 C
1040	ATOM 637 CG PHE A 84 28.372 21.628 45.790 1.00 15.88 C
1041	ATOM 638 CD1 PHE A 84 29.733 21.881 45.950 1.00 19.09 C
1042	ATOM 639 CD2 PHE A 84 27.487 22.706 45.743 1.00 19.11 C
1043	ATOM 640 CE1 PHE A 84 30.196 23.195 46.041 1.00 21.26 C
1044	ATOM 641 CE2 PHE A 84 27.928 24.028 45.828 1.00 19.26 C
1045	ATOM 642 CZ PHE A 84 29.295 24.264 45.975 1.00 23.22 C
1046	ATOM 643 N LYS A 85 27.602 17.337 46.597 1.00 18.65 N
1047	ATOM 644 CA LYS A 85 27.150 15.996 46.312 1.00 12.32 C
1048	ATOM 645 C LYS A 85 26.488 15.393 47.543 1.00 16.37 C
1049	ATOM 646 O LYS A 85 25.575 14.574 47.461 1.00 22.47 O
1050	ATOM 647 CB LYS A 85 28.287 15.136 45.787 1.00 10.89 C
1051	ATOM 648 CG LYS A 85 28.590 15.347 44.319 1.00 8.87 C
1052	ATOM 649 CD LYS A 85 29.725 14.421 43.885 1.00 10.40 C
1053	ATOM 650 CE LYS A 85 30.578 14.914 42.715 1.00 9.93 C
1054	ATOM 651 NZ LYS A 85 31.315 16.170 43.007 1.00 15.77 N
1055	ATOM 652 N SER A 86 26.918 15.852 48.697 1.00 14.84 N
1056	ATOM 653 CA SER A 86 26.383 15.344 49.947 1.00 20.84 C
1057	ATOM 654 C SER A 86 24.908 15.685 50.212 1.00 33.21 C
1058	ATOM 655 O SER A 86 24.270 15.063 51.070 1.00 30.89 O
1059	ATOM 656 CB SER A 86 27.246 15.732 51.135 1.00 9.95 C
1060	ATOM 657 OG SER A 86 26.830 17.006 51.592 1.00 20.44 O
1061	ATOM 658 N ALA A 87 24.372 16.689 49.516 1.00 20.74 N
1062	ATOM 659 CA ALA A 87 22.997 17.107 49.727 1.00 20.17 C
1063	ATOM 660 C ALA A 87 22.029 16.322 48.853 1.00 18.65 C
1064	ATOM 661 O ALA A 87 20.826 16.404 48.995 1.00 26.55 O
1065	ATOM 662 CB ALA A 87 22.850 18.599 49.475 1.00 23.01 C
1066	ATOM 663 N MET A 88 22.578 15.545 47.946 1.00 15.63 N
1067	ATOM 664 CA MET A 88 21.787 14.769 47.025 1.00 11.40 C
1068	ATOM 665 C MET A 88 21.289 13.463 47.638 1.00 16.81 C
1069	ATOM 666 O MET A 88 21.886 12.943 48.578 1.00 24.84 O
1070	ATOM 667 CB MET A 88 22.593 14.555 45.719 1.00 13.60 C
1071	ATOM 668 CG MET A 88 23.016 15.869 45.077 1.00 14.84 C
1072	ATOM 669 SD MET A 88 21.609 16.843 44.472 1.00 19.33 S
1073	ATOM 670 CE MET A 88 22.309 18.509 44.432 1.00 19.42 C
1074	ATOM 671 N PRO A 89 20.157 12.929 47.149 1.00 22.56 N
1075	ATOM 672 CA PRO A 89 19.390 13.425 46.015 1.00 16.83 C
1076	ATOM 673 C PRO A 89 18.390 14.504 46.361 1.00 18.78 C
1077	ATOM 674 O PRO A 89 17.766 15.081 45.465 1.00 18.98 O
1078	ATOM 675 CB PRO A 89 18.591 12.218 45.518 1.00 15.51 C
1079	ATOM 676 CG PRO A 89 18.500 11.255 46.682 1.00 18.88 C
1080	ATOM 677 CD PRO A 89 19.660 11.595 47.598 1.00 22.10 C
1081	ATOM 678 N GLU A 90 18.232 14.764 47.649 1.00 16.94 N
1082	ATOM 679 CA GLU A 90 17.281 15.761 48.118 1.00 22.80 C
1083	ATOM 680 C GLU A 90 17.519 17.162 47.561 1.00 30.75 C
1084	ATOM 681 O GLU A 90 16.575 17.856 47.165 1.00 22.04 O
1085	ATOM 682 CB GLU A 90 17.047 15.717 49.626 1.00 23.90 C
1086	ATOM 683 CG GLU A 90 17.009 14.272 50.171 1.00 35.91 C
1087	ATOM 684 CD GLU A 90 18.360 13.702 50.534 1.00 88.21 C
1088	ATOM 685 OE1 GLU A 90 19.430 14.174 50.171 1.00 81.40 O
1089	ATOM 686 OE2 GLU A 90 18.258 12.609 51.247 1.00100.00 O
1090	ATOM 687 N GLY A 91 18.781 17.575 47.487 1.00 24.20 N
1091	ATOM 688 CA GLY A 91 19.086 18.845 46.860 1.00 17.43 C
1092	ATOM 689 C GLY A 91 19.419 19.968 47.798 1.00 18.58 C
1093	ATOM 690 O GLY A 91 19.503 19.835 49.023 1.00 8.48 O
1094	ATOM 691 N TYR A 92 19.611 21.119 47.184 1.00 18.73 N
1095	ATOM 692 CA TYR A 92 19.945 22.262 47.978 1.00 13.16 C
1096	ATOM 693 C TYR A 92 19.418 23.494 47.327 1.00 15.88 C
1097	ATOM 694 O TYR A 92 19.076 23.482 46.138 1.00 23.77 O
1098	ATOM 695 CB TYR A 92 21.493 22.383 48.239 1.00 11.80 C
1099	ATOM 696 CG TYR A 92 22.370 22.360 46.985 1.00 11.05 C
1100	ATOM 697 CD1 TYR A 92 22.490 23.488 46.177 1.00 8.89 C
1101	ATOM 698 CD2 TYR A 92 23.110 21.232 46.620 1.00 10.20 C
1102	ATOM 699 CE1 TYR A 92 23.307 23.502 45.045 1.00 7.76 C
1103	ATOM 700 CE2 TYR A 92 23.867 21.200 45.450 1.00 9.79 C
1104	ATOM 701 CZ TYR A 92 24.016 22.359 44.688 1.00 14.50 C
1105	ATOM 702 OH TYR A 92 24.779 22.365 43.537 1.00 7.56 O
1106	ATOM 703 N VAL A 93 19.357 24.544 48.127 1.00 20.30 N
1107	ATOM 704 CA VAL A 93 18.980 25.855 47.648 1.00 21.61 C
1108	ATOM 705 C VAL A 93 20.246 26.704 47.428 1.00 11.96 C
1109	ATOM 706 O VAL A 93 21.115 26.814 48.287 1.00 15.91 O
1110	ATOM 707 CB VAL A 93 17.982 26.557 48.571 1.00 19.55 C
1111	ATOM 708 CG1 VAL A 93 17.481 27.867 47.943 1.00 10.57 C
1112	ATOM 709 CG2 VAL A 93 16.797 25.630 48.785 1.00 20.55 C
1113	ATOM 710 N GLN A 94 20.340 27.257 46.249 1.00 13.84 N
1114	ATOM 711 CA GLN A 94 21.417 28.156 45.896 1.00 13.18 C
1115	ATOM 712 C GLN A 94 20.854 29.554 45.692 1.00 11.53 C
1116	ATOM 713 O GLN A 94 20.184 29.816 44.705 1.00 14.94 O
1117	ATOM 714 CB GLN A 94 22.147 27.725 44.613 1.00 8.00 C
1118	ATOM 715 CG GLN A 94 23.360 28.628 44.255 1.00 9.18 C
1119	ATOM 716 CD GLN A 94 24.398 27.874 43.464 1.00 9.74 C
1120	ATOM 717 OE1 GLN A 94 24.910 26.852 43.913 1.00 24.92 O
1121	ATOM 718 NE2 GLN A 94 24.610 28.278 42.224 1.00 12.33 N
1122	ATOM 719 N GLU A 95 21.133 30.455 46.619 1.00 10.74 N
1123	ATOM 720 CA GLU A 95 20.694 31.836 46.461 1.00 18.63 C
1124	ATOM 721 C GLU A 95 21.891 32.758 46.159 1.00 31.16 C
1125	ATOM 722 O GLU A 95 22.989 32.561 46.733 1.00 22.68 O
1126	ATOM 723 CB GLU A 95 20.021 32.325 47.761 1.00 22.08 C
1127	ATOM 724 CG GLU A 95 18.494 32.184 47.752 1.00 50.70 C
1128	ATOM 725 CD GLU A 95 18.000 31.868 49.125 1.00 58.72 C
1129	ATOM 726 OE1 GLU A 95 18.750 31.704 50.059 1.00 38.97 O
1130	ATOM 727 OE2 GLU A 95 16.699 31.730 49.187 1.00 97.13 O
1131	ATOM 728 N ARG A 96 21.659 33.798 45.314 1.00 25.26 N
1132	ATOM 729 CA ARG A 96 22.706 34.764 44.965 1.00 22.64 C
1133	ATOM 730 C ARG A 96 22.239 36.198 44.758 1.00 30.93 C
1134	ATOM 731 O ARG A 96 21.117 36.491 44.336 1.00 19.43 O
1135	ATOM 732 CB ARG A 96 23.373 34.365 43.662 1.00 19.60 C
1136	ATOM 733 CG ARG A 96 24.633 33.577 43.886 1.00 30.44 C
1137	ATOM 734 CD ARG A 96 25.470 33.485 42.634 1.00 28.73 C
1138	ATOM 735 NE ARG A 96 26.300 32.304 42.634 1.00 16.28 N
1139	ATOM 736 CZ ARG A 96 26.353 31.397 41.665 1.00 18.45 C
1140	ATOM 737 NH1 ARG A 96 25.622 31.478 40.553 1.00 9.58 N
1141	ATOM 738 NH2 ARG A 96 27.185 30.370 41.831 1.00 16.70 N
1142	ATOM 739 N THR A 97 23.191 37.087 44.961 1.00 27.65 N
1143	ATOM 740 CA THR A 97 23.076 38.487 44.629 1.00 22.98 C
1144	ATOM 741 C THR A 97 24.327 38.795 43.856 1.00 19.75 C
1145	ATOM 742 O THR A 97 25.415 38.500 44.305 1.00 17.81 O
1146	ATOM 743 CB THR A 97 22.999 39.459 45.810 1.00 34.85 C
1147	ATOM 744 OG1 THR A 97 21.825 39.227 46.548 1.00 23.54 O
1148	ATOM 745 CG2 THR A 97 22.964 40.884 45.255 1.00 23.81 C
1149	ATOM 746 N ILE A 98 24.164 39.277 42.667 1.00 12.66 N
1150	ATOM 747 CA ILE A 98 25.276 39.569 41.841 1.00 7.99 C
1151	ATOM 748 C ILE A 98 25.267 41.049 41.574 1.00 15.70 C
1152	ATOM 749 O ILE A 98 24.387 41.561 40.892 1.00 13.60 O
1153	ATOM 750 CB ILE A 98 25.194 38.783 40.532 1.00 11.66 C
1154	ATOM 751 CG1 ILE A 98 25.150 37.273 40.807 1.00 15.04 C
1155	ATOM 752 CG2 ILE A 98 26.409 39.085 39.666 1.00 14.44 C
1156	ATOM 753 CD1 ILE A 98 24.834 36.445 39.554 1.00 5.92 C
1157	ATOM 754 N PHE A 99 26.238 41.744 42.142 1.00 19.48 N
1158	ATOM 755 CA PHE A 99 26.365 43.182 41.924 1.00 17.97 C
1159	ATOM 756 C PHE A 99 27.239 43.494 40.732 1.00 25.63 C
1160	ATOM 757 O PHE A 99 28.424 43.188 40.733 1.00 30.30 O
1161	ATOM 758 CB PHE A 99 27.020 43.869 43.111 1.00 17.08 C
1162	ATOM 759 CG PHE A 99 26.204 43.735 44.348 1.00 19.05 C
1163	ATOM 760 CD1 PHE A 99 26.488 42.715 45.254 1.00 25.71 C
1164	ATOM 761 CD2 PHE A 99 25.119 44.576 44.583 1.00 21.59 C
1165	ATOM 762 CE1 PHE A 99 25.746 42.558 46.423 1.00 20.80 C
1166	ATOM 763 CE2 PHE A 99 24.356 44.428 45.740 1.00 23.69 C
1167	ATOM 764 CZ PHE A 99 24.680 43.425 46.656 1.00 21.37 C
1168	ATOM 765 N PHE A 100 26.652 44.115 39.724 1.00 24.45 N
1169	ATOM 766 CA PHE A 100 27.400 44.534 38.566 1.00 18.80 C
1170	ATOM 767 C PHE A 100 27.917 45.949 38.830 1.00 28.50 C
1171	ATOM 768 O PHE A 100 27.117 46.858 39.037 1.00 21.89 O
1172	ATOM 769 CB PHE A 100 26.540 44.479 37.299 1.00 17.20 C
1173	ATOM 770 CG PHE A 100 26.194 43.075 36.884 1.00 18.79 C
1174	ATOM 771 CD1 PHE A 100 25.098 42.417 37.439 1.00 21.85 C
1175	ATOM 772 CD2 PHE A 100 26.943 42.403 35.918 1.00 23.92 C
1176	ATOM 773 CE1 PHE A 100 24.791 41.102 37.080 1.00 24.34 C
1177	ATOM 774 CE2 PHE A 100 26.628 41.100 35.516 1.00 23.29 C
1178	ATOM 775 CZ PHE A 100 25.540 40.450 36.099 1.00 19.24 C
1179	ATOM 776 N LYS A 101 29.250 46.112 38.906 1.00 27.81 N
1180	ATOM 777 CA LYS A 101 29.847 47.402 39.233 1.00 25.59 C
1181	ATOM 778 C LYS A 101 29.342 48.524 38.370 1.00 17.47 C
1182	ATOM 779 O LYS A 101 29.290 48.404 37.153 1.00 20.70 O
1183	ATOM 780 CB LYS A 101 31.366 47.391 39.323 1.00 23.95 C
1184	ATOM 781 CG LYS A 101 31.931 48.719 39.818 1.00 14.11 C
1185	ATOM 782 CD LYS A 101 33.425 48.679 40.137 1.00 48.36 C
1186	ATOM 783 CE LYS A 101 33.897 49.782 41.080 1.00 96.64 C
1187	ATOM 784 NZ LYS A 101 35.340 49.713 41.383 1.00100.00 N
1188	ATOM 785 N ASP A 102 28.955 49.615 39.022 1.00 25.46 N
1189	ATOM 786 CA ASP A 102 28.390 50.787 38.327 1.00 29.62 C
1190	ATOM 787 C ASP A 102 27.160 50.440 37.492 1.00 27.47 C
1191	ATOM 788 O ASP A 102 26.929 51.027 36.453 1.00 24.04 O
1192	ATOM 789 CB ASP A 102 29.398 51.648 37.522 1.00 28.63 C
1193	ATOM 790 CG ASP A 102 30.594 52.101 38.324 1.00 62.02 C
1194	ATOM 791 OD1 ASP A 102 31.750 51.902 37.976 1.00 65.03 O
1195	ATOM 792 OD2 ASP A 102 30.265 52.703 39.446 1.00 89.79 O
1196	ATOM 793 N ASP A 103 26.359 49.475 37.955 1.00 22.77 N
1197	ATOM 794 CA ASP A 103 25.180 49.090 37.212 1.00 18.84 C
1198	ATOM 795 C ASP A 103 24.201 48.321 38.092 1.00 23.12 C
1199	ATOM 796 O ASP A 103 24.288 48.419 39.322 1.00 21.68 O
1200	ATOM 797 CB ASP A 103 25.530 48.466 35.836 1.00 19.89 C
1201	ATOM 798 CG ASP A 103 24.413 48.523 34.831 1.00 25.69 C
1202	ATOM 799 OD1 ASP A 103 24.591 48.461 33.630 1.00 36.49 O
1203	ATOM 800 OD2 ASP A 103 23.224 48.508 35.390 1.00 42.24 O
1204	ATOM 801 N GLY A 104 23.235 47.605 37.505 1.00 20.85 N
1205	ATOM 802 CA GLY A 104 22.255 46.926 38.344 1.00 12.94 C
1206	ATOM 803 C GLY A 104 22.783 45.715 39.095 1.00 25.35 C
1207	ATOM 804 O GLY A 104 23.974 45.432 39.163 1.00 27.69 O
1208	ATOM 805 N ASN A 105 21.860 44.980 39.671 1.00 26.64 N
1209	ATOM 806 CA ASN A 105 22.195 43.755 40.363 1.00 25.15 C
1210	ATOM 807 C ASN A 105 21.212 42.629 40.003 1.00 30.97 C
1211	ATOM 808 O ASN A 105 20.129 42.876 39.473 1.00 34.60 O
1212	ATOM 809 CB ASN A 105 22.324 43.974 41.879 1.00 20.27 C
1213	ATOM 810 CG ASN A 105 21.050 44.509 42.515 1.00 59.50 C
1214	ATOM 811 OD1 ASN A 105 20.123 43.738 42.823 1.00 40.77 O
1215	ATOM 812 ND2 ASN A 105 21.003 45.824 42.738 1.00 30.76 N
1216	ATOM 813 N TYR A 106 21.596 41.379 40.243 1.00 27.18 N
1217	ATOM 814 CA TYR A 106 20.720 40.237 39.992 1.00 19.71 C
1218	ATOM 815 C TYR A 106 20.435 39.512 41.306 1.00 23.97 C
1219	ATOM 816 O TYR A 106 21.340 39.260 42.099 1.00 21.67 O
1220	ATOM 817 CB TYR A 106 21.339 39.165 39.080 1.00 13.04 C
1221	ATOM 818 CG TYR A 106 21.488 39.427 37.618 1.00 9.42 C
1222	ATOM 819 CD1 TYR A 106 20.783 40.398 36.907 1.00 14.41 C
1223	ATOM 820 CD2 TYR A 106 22.347 38.592 36.906 1.00 9.45 C
1224	ATOM 821 CE1 TYR A 106 20.946 40.518 35.522 1.00 17.70 C
1225	ATOM 822 CE2 TYR A 106 22.551 38.720 35.535 1.00 10.36 C
1226	ATOM 823 CZ TYR A 106 21.836 39.685 34.833 1.00 17.80 C
1227	ATOM 824 OH TYR A 106 22.035 39.777 33.473 1.00 21.21 O
1228	ATOM 825 N LYS A 107 19.183 39.127 41.521 1.00 19.89 N
1229	ATOM 826 CA LYS A 107 18.844 38.357 42.696 1.00 14.89 C
1230	ATOM 827 C LYS A 107 18.347 37.014 42.198 1.00 23.00 C
1231	ATOM 828 O LYS A 107 17.481 36.965 41.321 1.00 15.79 O
1232	ATOM 829 CB LYS A 107 17.830 39.050 43.579 1.00 23.17 C
1233	ATOM 830 CG LYS A 107 18.360 39.387 44.959 1.00 32.27 C
1234	ATOM 831 CD LYS A 107 18.287 40.871 45.263 1.00 27.32 C
1235	ATOM 832 N THR A 108 18.981 35.936 42.670 1.00 17.26 N
1236	ATOM 833 CA THR A 108 18.636 34.600 42.201 1.00 20.38 C
1237	ATOM 834 C THR A 108 18.314 33.623 43.325 1.00 13.70 C
1238	ATOM 835 O THR A 108 18.834 33.706 44.448 1.00 16.85 O
1239	ATOM 836 CB THR A 108 19.668 33.958 41.203 1.00 25.19 C
1240	ATOM 837 OG1 THR A 108 20.834 33.465 41.837 1.00 22.55 O
1241	ATOM 838 CG2 THR A 108 20.076 34.889 40.095 1.00 12.05 C
1242	ATOM 839 N ARG A 109 17.402 32.701 43.021 1.00 16.07 N
1243	ATOM 840 CA ARG A 109 17.043 31.670 43.971 1.00 12.11 C
1244	ATOM 841 C ARG A 109 16.821 30.415 43.181 1.00 19.15 C
1245	ATOM 842 O ARG A 109 16.033 30.426 42.261 1.00 16.10 O
1246	ATOM 843 CB ARG A 109 15.853 32.059 44.802 1.00 13.43 C
1247	ATOM 844 CG ARG A 109 15.475 31.011 45.847 1.00 34.42 C
1248	ATOM 845 CD ARG A 109 13.956 30.840 45.965 1.00 56.02 C
1249	ATOM 846 NE ARG A 109 13.519 29.452 46.149 1.00 43.45 N
1250	ATOM 847 CZ ARG A 109 13.634 28.804 47.301 1.00 54.15 C
1251	ATOM 848 NH1 ARG A 109 14.170 29.387 48.374 1.00 39.63 N
1252	ATOM 849 NH2 ARG A 109 13.217 27.543 47.377 1.00 50.82 N
1253	ATOM 850 N ALA A 110 17.612 29.378 43.422 1.00 12.95 N
1254	ATOM 851 CA ALA A 110 17.438 28.189 42.613 1.00 7.90 C
1255	ATOM 852 C ALA A 110 17.312 26.965 43.457 1.00 14.34 C
1256	ATOM 853 O ALA A 110 17.685 26.933 44.617 1.00 18.94 O
1257	ATOM 854 CB ALA A 110 18.593 27.984 41.654 1.00 10.39 C
1258	ATOM 855 N GLU A 111 16.755 25.937 42.887 1.00 17.65 N
1259	ATOM 856 CA GLU A 111 16.725 24.699 43.637 1.00 19.69 C
1260	ATOM 857 C GLU A 111 17.396 23.650 42.790 1.00 20.02 C
1261	ATOM 858 O GLU A 111 17.021 23.475 41.623 1.00 17.99 O
1262	ATOM 859 CB GLU A 111 15.316 24.201 43.975 1.00 20.66 C
1263	ATOM 860 CG GLU A 111 14.585 25.021 45.041 1.00 25.98 C
1264	ATOM 861 CD GLU A 111 13.266 24.378 45.390 1.00 94.77 C
1265	ATOM 862 OE1 GLU A 111 12.769 23.431 44.752 1.00 41.74 O
1266	ATOM 863 OE2 GLU A 111 12.741 24.921 46.470 1.00 44.04 O
1267	ATOM 864 N VAL A 112 18.389 22.979 43.377 1.00 15.11 N
1268	ATOM 865 CA VAL A 112 19.065 21.922 42.671 1.00 14.64 C
1269	ATOM 866 C VAL A 112 18.840 20.571 43.298 1.00 4.26 C
1270	ATOM 867 O VAL A 112 19.058 20.381 44.495 1.00 10.95 O
1271	ATOM 868 CB VAL A 112 20.432 22.188 41.996 1.00 18.73 C
1272	ATOM 869 CG1 VAL A 112 20.856 23.659 41.996 1.00 18.26 C
1273	ATOM 870 CG2 VAL A 112 21.525 21.226 42.426 1.00 10.37 C
1274	ATOM 871 N LYS A 113 18.347 19.655 42.454 1.00 12.56 N
1275	ATOM 872 CA LYS A 113 17.988 18.336 42.936 1.00 13.47 C
1276	ATOM 873 C LYS A 113 17.745 17.366 41.824 1.00 7.55 C
1277	ATOM 874 O LYS A 113 17.628 17.729 40.661 1.00 20.91 O
1278	ATOM 875 CB LYS A 113 16.720 18.455 43.766 1.00 21.32 C
1279	ATOM 876 CG LYS A 113 15.566 19.154 43.034 1.00 42.86 C
1280	ATOM 877 CD LYS A 113 14.218 18.437 43.162 1.00 74.11 C
1281	ATOM 878 CE LYS A 113 13.160 19.216 43.943 1.00 31.88 C
1282	ATOM 879 NZ LYS A 113 12.679 20.418 43.235 1.00 62.64 N
1283	ATOM 880 N PHE A 114 17.670 16.098 42.187 1.00 17.88 N
1284	ATOM 881 CA PHE A 114 17.377 15.054 41.208 1.00 16.76 C
1285	ATOM 882 C PHE A 114 15.883 14.863 41.050 1.00 13.91 C
1286	ATOM 883 O PHE A 114 15.157 14.884 42.014 1.00 14.45 O
1287	ATOM 884 CB PHE A 114 17.914 13.719 41.687 1.00 15.79 C
1288	ATOM 885 CG PHE A 114 19.299 13.501 41.205 1.00 14.96 C
1289	ATOM 886 CD1 PHE A 114 20.389 13.776 42.031 1.00 27.70 C
1290	ATOM 887 CD2 PHE A 114 19.518 13.052 39.907 1.00 17.38 C
1291	ATOM 888 CE1 PHE A 114 21.693 13.555 41.587 1.00 23.66 C
1292	ATOM 889 CE2 PHE A 114 20.812 12.824 39.440 1.00 19.57 C
1293	ATOM 890 CZ PHE A 114 21.887 13.069 40.294 1.00 18.03 C
1294	ATOM 891 N GLU A 115 15.448 14.706 39.829 1.00 15.53 N
1295	ATOM 892 CA GLU A 115 14.069 14.413 39.510 1.00 19.01 C
1296	ATOM 893 C GLU A 115 14.201 13.111 38.799 1.00 17.72 C
1297	ATOM 894 O GLU A 115 14.533 13.071 37.626 1.00 17.61 O
1298	ATOM 895 CB GLU A 115 13.372 15.442 38.570 1.00 19.49 C
1299	ATOM 896 CG GLU A 115 13.003 16.784 39.252 1.00 13.95 C
1300	ATOM 897 CD GLU A 115 11.845 16.719 40.207 1.00 30.48 C
1301	ATOM 898 OE1 GLU A 115 11.485 15.708 40.750 1.00 28.18 O
1302	ATOM 899 OE2 GLU A 115 11.318 17.882 40.449 1.00 35.87 O
1303	ATOM 900 N GLY A 116 14.100 12.046 39.557 1.00 18.85 N
1304	ATOM 901 CA GLY A 116 14.330 10.775 38.950 1.00 19.30 C
1305	ATOM 902 C GLY A 116 15.817 10.678 38.783 1.00 24.95 C
1306	ATOM 903 O GLY A 116 16.584 10.855 39.737 1.00 25.59 O
1307	ATOM 904 N ASP A 117 16.233 10.475 37.566 1.00 24.98 N
1308	ATOM 905 CA ASP A 117 17.646 10.417 37.342 1.00 31.68 C
1309	ATOM 906 C ASP A 117 18.178 11.625 36.600 1.00 20.25 C
1310	ATOM 907 O ASP A 117 19.322 11.639 36.125 1.00 19.09 O
1311	ATOM 908 CB ASP A 117 18.156 9.060 36.841 1.00 41.46 C
1312	ATOM 909 CG ASP A 117 17.696 8.774 35.454 1.00 71.03 C
1313	ATOM 910 OD1 ASP A 117 17.314 9.656 34.698 1.00 66.81 O
1314	ATOM 911 OD2 ASP A 117 17.743 7.493 35.160 1.00 88.20 O
1315	ATOM 912 N THR A 118 17.363 12.679 36.594 1.00 16.94 N
1316	ATOM 913 CA THR A 118 17.759 13.926 35.975 1.00 14.90 C
1317	ATOM 914 C THR A 118 18.077 14.958 36.996 1.00 16.74 C
1318	ATOM 915 O THR A 118 17.360 15.067 37.997 1.00 17.81 O
1319	ATOM 916 CB THR A 118 16.792 14.437 34.928 1.00 23.42 C
1320	ATOM 917 OG1 THR A 118 16.776 13.495 33.873 1.00 38.04 O
1321	ATOM 918 CG2 THR A 118 17.283 15.782 34.417 1.00 18.71 C
1322	ATOM 919 N LEU A 119 19.251 15.593 36.819 1.00 19.29 N
1323	ATOM 920 CA LEU A 119 19.679 16.634 37.746 1.00 16.87 C
1324	ATOM 921 C LEU A 119 19.018 17.931 37.298 1.00 20.43 C
1325	ATOM 922 O LEU A 119 19.235 18.392 36.172 1.00 20.02 O
1326	ATOM 923 CB LEU A 119 21.213 16.789 37.782 1.00 19.78 C
1327	ATOM 924 CG LEU A 119 21.774 17.614 38.949 1.00 16.28 C
1328	ATOM 925 CD1 LEU A 119 21.853 19.096 38.571 1.00 19.93 C
1329	ATOM 926 CD2 LEU A 119 20.923 17.436 40.185 1.00 20.69 C
1330	ATOM 927 N VAL A 120 18.158 18.482 38.147 1.00 19.98 N
1331	ATOM 928 CA VAL A 120 17.440 19.687 37.775 1.00 21.37 C
1332	ATOM 929 C VAL A 120 17.879 20.999 38.442 1.00 13.70 C
1333	ATOM 930 O VAL A 120 18.149 21.071 39.615 1.00 12.92 O
1334	ATOM 931 CB VAL A 120 15.942 19.462 37.871 1.00 19.43 C
1335	ATOM 932 CG1 VAL A 120 15.203 20.749 37.515 1.00 15.28 C
1336	ATOM 933 CG2 VAL A 120 15.588 18.342 36.882 1.00 16.30 C
1337	ATOM 934 N ASN A 121 17.944 22.058 37.648 1.00 20.34 N
1338	ATOM 935 CA ASN A 121 18.276 23.383 38.146 1.00 19.67 C
1339	ATOM 936 C ASN A 121 17.136 24.311 37.764 1.00 12.92 C
1340	ATOM 937 O ASN A 121 16.991 24.655 36.584 1.00 13.64 O
1341	ATOM 938 CB ASN A 121 19.614 23.915 37.566 1.00 17.73 C
1342	ATOM 939 CG ASN A 121 20.126 25.146 38.277 1.00 19.56 C
1343	ATOM 940 OD1 ASN A 121 19.700 25.436 39.407 1.00 17.77 O
1344	ATOM 941 ND2 ASN A 121 21.066 25.855 37.637 1.00 9.92 N
1345	ATOM 942 N ARG A 122 16.295 24.625 38.767 1.00 16.81 N
1346	ATOM 943 CA ARG A 122 15.122 25.502 38.622 1.00 15.08 C
1347	ATOM 944 C ARG A 122 15.436 26.861 39.242 1.00 7.55 C
1348	ATOM 945 O ARG A 122 15.678 27.008 40.455 1.00 19.40 O
1349	ATOM 946 CB ARG A 122 13.893 24.923 39.334 1.00 20.79 C
1350	ATOM 947 CG ARG A 122 12.691 24.622 38.443 1.00 48.12 C
1351	ATOM 948 CD ARG A 122 11.672 23.686 39.120 1.00100.00 C
1352	ATOM 949 NE ARG A 122 11.631 22.317 38.573 1.00100.00 N
1353	ATOM 950 CZ ARG A 122 11.049 21.260 39.163 1.00100.00 C
1354	ATOM 951 NH1 ARG A 122 10.439 21.359 40.345 1.00100.00 N
1355	ATOM 952 NH2 ARG A 122 11.086 20.070 38.551 1.00 68.71 N
1356	ATOM 953 N ILE A 123 15.440 27.858 38.398 1.00 14.08 N
1357	ATOM 954 CA ILE A 123 15.815 29.176 38.857 1.00 16.29 C
1358	ATOM 955 C ILE A 123 14.815 30.245 38.500 1.00 14.04 C
1359	ATOM 956 O ILE A 123 14.275 30.287 37.393 1.00 10.60 O
1360	ATOM 957 CB ILE A 123 17.122 29.591 38.127 1.00 20.53 C
1361	ATOM 958 CG1 ILE A 123 18.171 28.455 38.122 1.00 10.68 C
1362	ATOM 959 CG2 ILE A 123 17.690 30.885 38.724 1.00 15.29 C
1363	ATOM 960 CD1 ILE A 123 18.802 28.263 36.758 1.00 3.95 C
1364	ATOM 961 N GLU A 124 14.725 31.198 39.387 1.00 15.00 N
1365	ATOM 962 CA GLU A 124 14.008 32.393 39.068 1.00 22.24 C
1366	ATOM 963 C GLU A 124 14.939 33.560 39.344 1.00 21.22 C
1367	ATOM 964 O GLU A 124 15.566 33.628 40.399 1.00 20.98 O
1368	ATOM 965 CB GLU A 124 12.682 32.558 39.797 1.00 27.17 C
1369	ATOM 966 CG GLU A 124 12.761 32.245 41.286 1.00 51.46 C
1370	ATOM 967 CD GLU A 124 11.408 31.842 41.779 1.00100.00 C
1371	ATOM 968 OE1 GLU A 124 10.449 31.727 41.032 1.00100.00 O
1372	ATOM 969 OE2 GLU A 124 11.376 31.620 43.074 1.00100.00 O
1373	ATOM 970 N LEU A 125 15.080 34.441 38.380 1.00 17.36 N
1374	ATOM 971 CA LEU A 125 15.965 35.570 38.568 1.00 24.36 C
1375	ATOM 972 C LEU A 125 15.230 36.906 38.549 1.00 18.76 C
1376	ATOM 973 O LEU A 125 14.395 37.166 37.684 1.00 19.90 O
1377	ATOM 974 CB LEU A 125 17.059 35.565 37.469 1.00 20.77 C
1378	ATOM 975 CG LEU A 125 18.004 36.786 37.420 1.00 23.85 C
1379	ATOM 976 CD1 LEU A 125 19.187 36.424 36.540 1.00 25.57 C
1380	ATOM 977 CD2 LEU A 125 17.336 38.003 36.782 1.00 25.35 C
1381	ATOM 978 N LYS A 126 15.700 37.806 39.387 1.00 12.48 N
1382	ATOM 979 CA LYS A 126 15.169 39.154 39.404 1.00 19.67 C
1383	ATOM 980 C LYS A 126 16.244 40.217 39.170 1.00 24.30 C
1384	ATOM 981 O LYS A 126 17.128 40.385 39.998 1.00 24.32 O
1385	ATOM 982 CB LYS A 126 14.437 39.412 40.715 1.00 26.90 C
1386	ATOM 983 CG LYS A 126 13.745 40.758 40.775 1.00 27.97 C
1387	ATOM 984 CD LYS A 126 12.254 40.683 40.504 1.00 65.69 C
1388	ATOM 985 CE LYS A 126 11.681 42.020 40.058 1.00 76.79 C
1389	ATOM 986 NZ LYS A 126 12.048 43.134 40.948 1.00 65.77 N
1390	ATOM 987 N GLY A 127 16.139 40.994 38.087 1.00 25.48 N
1391	ATOM 988 CA GLY A 127 17.112 42.050 37.852 1.00 26.49 C
1392	ATOM 989 C GLY A 127 16.552 43.477 37.978 1.00 31.32 C
1393	ATOM 990 O GLY A 127 15.556 43.806 37.326 1.00 28.17 O
1394	ATOM 991 N ILE A 128 17.234 44.328 38.781 1.00 21.27 N
1395	ATOM 992 CA ILE A 128 16.821 45.710 38.988 1.00 25.59 C
1396	ATOM 993 C ILE A 128 17.965 46.699 39.015 1.00 30.89 C
1397	ATOM 994 O ILE A 128 19.057 46.366 39.453 1.00 31.84 O
1398	ATOM 995 CB ILE A 128 16.053 45.897 40.291 1.00 28.51 C
1399	ATOM 996 CG1 ILE A 128 17.017 45.862 41.460 1.00 26.94 C
1400	ATOM 997 CG2 ILE A 128 14.946 44.870 40.465 1.00 23.91 C
1401	ATOM 998 CD1 ILE A 128 16.380 46.231 42.795 1.00 35.73 C
1402	ATOM 999 N ASP A 129 17.670 47.952 38.628 1.00 25.50 N
1403	ATOM 1000 CA ASP A 129 18.638 49.071 38.667 1.00 21.39 C
1404	ATOM 1001 C ASP A 129 19.643 49.069 37.559 1.00 21.94 C
1405	ATOM 1002 O ASP A 129 20.673 49.721 37.653 1.00 22.56 O
1406	ATOM 1003 CB ASP A 129 19.356 49.306 40.009 1.00 16.52 C
1407	ATOM 1004 CG ASP A 129 18.467 49.833 41.092 1.00 55.53 C
1408	ATOM 1005 OD1 ASP A 129 17.432 50.435 40.856 1.00 66.94 O
1409	ATOM 1006 OD2 ASP A 129 18.892 49.531 42.303 1.00 61.33 O
1410	ATOM 1007 N PHE A 130 19.325 48.347 36.505 1.00 15.62 N
1411	ATOM 1008 CA PHE A 130 20.204 48.319 35.384 1.00 21.05 C
1412	ATOM 1009 C PHE A 130 20.096 49.580 34.560 1.00 37.76 C
1413	ATOM 1010 O PHE A 130 19.021 50.167 34.420 1.00 37.56 O
1414	ATOM 1011 CB PHE A 130 19.956 47.066 34.539 1.00 24.92 C
1415	ATOM 1012 CG PHE A 130 20.547 45.889 35.270 1.00 28.13 C
1416	ATOM 1013 CD1 PHE A 130 19.742 45.067 36.056 1.00 26.56 C
1417	ATOM 1014 CD2 PHE A 130 21.926 45.674 35.271 1.00 33.24 C
1418	ATOM 1015 CE1 PHE A 130 20.283 43.992 36.762 1.00 26.52 C
1419	ATOM 1016 CE2 PHE A 130 22.486 44.601 35.961 1.00 36.24 C
1420	ATOM 1017 CZ PHE A 130 21.657 43.766 36.712 1.00 30.94 C
1421	ATOM 1018 N LYS A 131 21.223 50.002 34.018 1.00 31.13 N
1422	ATOM 1019 CA LYS A 131 21.224 51.164 33.175 1.00 25.76 C
1423	ATOM 1020 C LYS A 131 20.787 50.738 31.808 1.00 30.16 C
1424	ATOM 1021 O LYS A 131 21.417 49.882 31.186 1.00 28.79 O
1425	ATOM 1022 CB LYS A 131 22.597 51.780 33.078 1.00 22.78 C
1426	ATOM 1023 CG LYS A 131 22.942 52.562 34.317 1.00 30.62 C
1427	ATOM 1024 CD LYS A 131 24.435 52.860 34.420 1.00 44.97 C
1428	ATOM 1025 CE LYS A 131 24.872 53.205 35.843 1.00 44.45 C
1429	ATOM 1026 NZ LYS A 131 26.201 53.843 35.924 1.00100.00 N
1430	ATOM 1027 N GLU A 132 19.693 51.311 31.339 1.00 32.54 N
1431	ATOM 1028 CA GLU A 132 19.215 50.931 30.023 1.00 31.66 C
1432	ATOM 1029 C GLU A 132 20.313 51.060 28.974 1.00 41.40 C
1433	ATOM 1030 O GLU A 132 20.287 50.420 27.922 1.00 44.02 O
1434	ATOM 1031 CB GLU A 132 17.886 51.625 29.614 1.00 32.13 C
1435	ATOM 1032 CG GLU A 132 16.804 51.629 30.723 1.00 39.57 C
1436	ATOM 1033 CD GLU A 132 15.890 50.409 30.765 1.00100.00 C
1437	ATOM 1034 OE1 GLU A 132 15.861 49.525 29.914 1.00 57.59 O
1438	ATOM 1035 OE2 GLU A 132 15.119 50.392 31.829 1.00100.00 O
1439	ATOM 1036 N ASP A 133 21.316 51.871 29.280 1.00 47.78 N
1440	ATOM 1037 CA ASP A 133 22.423 52.097 28.354 1.00 52.64 C
1441	ATOM 1038 C ASP A 133 23.770 51.544 28.856 1.00 65.87 C
1442	ATOM 1039 O ASP A 133 24.841 51.880 28.327 1.00 59.96 O
1443	ATOM 1040 CB ASP A 133 22.545 53.598 28.026 1.00 48.93 C
1444	ATOM 1041 CG ASP A 133 22.494 54.441 29.267 1.00 83.44 C
1445	ATOM 1042 OD1 ASP A 133 21.726 54.225 30.193 1.00 86.97 O
1446	ATOM 1043 OD2 ASP A 133 23.397 55.393 29.267 1.00100.00 O
1447	ATOM 1044 N GLY A 134 23.711 50.695 29.890 1.00 60.95 N
1448	ATOM 1045 CA GLY A 134 24.909 50.128 30.493 1.00 52.64 C
1449	ATOM 1046 C GLY A 134 25.563 49.072 29.629 1.00 32.85 C
1450	ATOM 1047 O GLY A 134 25.254 48.912 28.455 1.00 30.18 O
1451	ATOM 1048 N ASN A 135 26.504 48.355 30.210 1.00 27.30 N
1452	ATOM 1049 CA ASN A 135 27.174 47.328 29.447 1.00 26.46 C
1453	ATOM 1050 C ASN A 135 26.294 46.114 29.281 1.00 28.23 C
1454	ATOM 1051 O ASN A 135 26.400 45.382 28.287 1.00 25.97 O
1455	ATOM 1052 CB ASN A 135 28.485 46.926 30.105 1.00 32.98 C
1456	ATOM 1053 CG ASN A 135 29.501 48.023 29.966 1.00 20.14 C
1457	ATOM 1054 OD1 ASN A 135 29.668 48.609 28.884 1.00 21.70 O
1458	ATOM 1055 ND2 ASN A 135 30.132 48.343 31.084 1.00 23.65 N
1459	ATOM 1056 N ILE A 136 25.420 45.927 30.276 1.00 19.42 N
1460	ATOM 1057 CA ILE A 136 24.489 44.806 30.296 1.00 23.78 C
1461	ATOM 1058 C ILE A 136 23.306 44.990 29.359 1.00 27.62 C
1462	ATOM 1059 O ILE A 136 23.176 44.268 28.367 1.00 23.61 O
1463	ATOM 1060 CB ILE A 136 24.061 44.389 31.701 1.00 22.75 C
1464	ATOM 1061 CG1 ILE A 136 25.256 43.751 32.380 1.00 17.95 C
1465	ATOM 1062 CG2 ILE A 136 22.941 43.345 31.617 1.00 21.97 C
1466	ATOM 1063 CD1 ILE A 136 26.204 44.793 32.957 1.00 45.55 C
1467	ATOM 1064 N LEU A 137 22.451 45.974 29.676 1.00 23.00 N
1468	ATOM 1065 CA LEU A 137 21.284 46.221 28.839 1.00 23.88 C
1469	ATOM 1066 C LEU A 137 21.734 46.695 27.480 1.00 33.14 C
1470	ATOM 1067 O LEU A 137 21.121 46.403 26.439 1.00 36.93 O
1471	ATOM 1068 CB LEU A 137 20.260 47.178 29.496 1.00 22.67 C
1472	ATOM 1069 CG LEU A 137 19.488 46.528 30.637 1.00 23.84 C
1473	ATOM 1070 CD1 LEU A 137 18.739 47.569 31.460 1.00 24.31 C
1474	ATOM 1071 CD2 LEU A 137 18.525 45.494 30.056 1.00 26.78 C
1475	ATOM 1072 N GLY A 138 22.878 47.378 27.514 1.00 32.19 N
1476	ATOM 1073 CA GLY A 138 23.511 47.911 26.325 1.00 25.52 C
1477	ATOM 1074 C GLY A 138 24.178 46.828 25.492 1.00 28.48 C
1478	ATOM 1075 O GLY A 138 24.583 47.096 24.365 1.00 24.44 O
1479	ATOM 1076 N HIS A 139 24.310 45.610 26.062 1.00 30.52 N
1480	ATOM 1077 CA HIS A 139 24.939 44.479 25.385 1.00 29.39 C
1481	ATOM 1078 C HIS A 139 26.370 44.794 24.894 1.00 30.83 C
1482	ATOM 1079 O HIS A 139 26.746 44.534 23.757 1.00 31.19 O
1483	ATOM 1080 CB HIS A 139 24.074 43.987 24.210 1.00 31.60 C
1484	ATOM 1081 CG HIS A 139 22.741 43.389 24.561 1.00 42.70 C
1485	ATOM 1082 ND1 HIS A 139 22.538 42.001 24.640 1.00 46.60 N
1486	ATOM 1083 CD2 HIS A 139 21.541 43.990 24.801 1.00 48.98 C
1487	ATOM 1084 CE1 HIS A 139 21.257 41.799 24.884 1.00 46.66 C
1488	ATOM 1085 NE2 HIS A 139 20.629 42.972 25.009 1.00 49.79 N
1489	ATOM 1086 N LYS A 140 27.200 45.355 25.749 1.00 28.01 N
1490	ATOM 1087 CA LYS A 140 28.541 45.722 25.321 1.00 29.88 C
1491	ATOM 1088 C LYS A 140 29.591 44.696 25.732 1.00 35.03 C
1492	ATOM 1089 O LYS A 140 30.791 44.961 25.691 1.00 28.53 O
1493	ATOM 1090 CB LYS A 140 28.893 47.071 25.913 1.00 33.86 C
1494	ATOM 1091 CG LYS A 140 28.090 48.211 25.325 1.00 37.07 C
1495	ATOM 1092 CD LYS A 140 28.294 49.490 26.113 1.00 28.88 C
1496	ATOM 1093 CE LYS A 140 27.568 50.689 25.523 1.00 67.23 C
1497	ATOM 1094 NZ LYS A 140 27.148 51.657 26.552 1.00100.00 N
1498	ATOM 1095 N LEU A 141 29.106 43.539 26.167 1.00 33.42 N
1499	ATOM 1096 CA LEU A 141 29.905 42.445 26.664 1.00 20.35 C
1500	ATOM 1097 C LEU A 141 30.338 41.502 25.579 1.00 17.81 C
1501	ATOM 1098 O LEU A 141 29.585 41.161 24.675 1.00 27.36 O
1502	ATOM 1099 CB LEU A 141 29.099 41.680 27.733 1.00 22.90 C
1503	ATOM 1100 CG LEU A 141 29.465 42.117 29.144 1.00 28.50 C
1504	ATOM 1101 CD1 LEU A 141 29.603 43.625 29.231 1.00 25.67 C
1505	ATOM 1102 CD2 LEU A 141 28.461 41.616 30.156 1.00 28.93 C
1506	ATOM 1103 N GLU A 142 31.575 41.056 25.681 1.00 20.99 N
1507	ATOM 1104 CA GLU A 142 32.128 40.098 24.754 1.00 15.92 C
1508	ATOM 1105 C GLU A 142 31.641 38.680 25.054 1.00 18.25 C
1509	ATOM 1106 O GLU A 142 31.340 38.334 26.198 1.00 14.38 O
1510	ATOM 1107 CB GLU A 142 33.641 40.170 24.854 1.00 17.39 C
1511	ATOM 1108 CG GLU A 142 34.159 41.351 24.031 1.00 23.22 C
1512	ATOM 1109 CD GLU A 142 35.648 41.313 23.856 1.00 63.68 C
1513	ATOM 1110 OE1 GLU A 142 36.378 40.661 24.575 1.00 41.67 O
1514	ATOM 1111 OE2 GLU A 142 36.069 42.059 22.863 1.00 59.05 O
1515	ATOM 1112 N TYR A 143 31.557 37.868 24.011 1.00 19.41 N
1516	ATOM 1113 CA TYR A 143 31.087 36.500 24.102 1.00 16.49 C
1517	ATOM 1114 C TYR A 143 32.166 35.538 24.547 1.00 17.01 C
1518	ATOM 1115 O TYR A 143 32.567 34.664 23.803 1.00 17.42 O
1519	ATOM 1116 CB TYR A 143 30.407 36.015 22.792 1.00 20.82 C
1520	ATOM 1117 CG TYR A 143 29.576 34.748 22.962 1.00 20.98 C
1521	ATOM 1118 CD1 TYR A 143 28.462 34.711 23.805 1.00 21.69 C
1522	ATOM 1119 CD2 TYR A 143 29.912 33.579 22.278 1.00 24.99 C
1523	ATOM 1120 CE1 TYR A 143 27.715 33.544 23.984 1.00 24.64 C
1524	ATOM 1121 CE2 TYR A 143 29.158 32.410 22.408 1.00 27.96 C
1525	ATOM 1122 CZ TYR A 143 28.056 32.399 23.266 1.00 22.36 C
1526	ATOM 1123 OH TYR A 143 27.334 31.268 23.437 1.00 24.37 O
1527	ATOM 1124 N ASN A 144 32.595 35.669 25.786 1.00 18.39 N
1528	ATOM 1125 CA ASN A 144 33.638 34.811 26.301 1.00 20.30 C
1529	ATOM 1126 C ASN A 144 33.615 34.805 27.799 1.00 21.82 C
1530	ATOM 1127 O ASN A 144 32.762 35.427 28.418 1.00 20.55 O
1531	ATOM 1128 CB ASN A 144 35.042 35.185 25.788 1.00 17.07 C
1532	ATOM 1129 CG ASN A 144 35.359 36.629 26.077 1.00 30.92 C
1533	ATOM 1130 OD1 ASN A 144 34.969 37.167 27.127 1.00 20.63 O
1534	ATOM 1131 ND2 ASN A 144 35.958 37.289 25.101 1.00 41.87 N
1535	ATOM 1132 N PHE A 145 34.576 34.110 28.379 1.00 25.91 N
1536	ATOM 1133 CA PHE A 145 34.587 33.952 29.806 1.00 21.61 C
1537	ATOM 1134 C PHE A 145 35.943 33.536 30.347 1.00 28.04 C
1538	ATOM 1135 O PHE A 145 36.518 32.555 29.895 1.00 38.57 O
1539	ATOM 1136 CB PHE A 145 33.583 32.829 30.098 1.00 22.63 C
1540	ATOM 1137 CG PHE A 145 32.900 33.034 31.414 1.00 22.26 C
1541	ATOM 1138 CD1 PHE A 145 31.822 33.911 31.514 1.00 23.55 C
1542	ATOM 1139 CD2 PHE A 145 33.320 32.347 32.552 1.00 14.29 C
1543	ATOM 1140 CE1 PHE A 145 31.188 34.109 32.739 1.00 22.32 C
1544	ATOM 1141 CE2 PHE A 145 32.696 32.542 33.785 1.00 17.95 C
1545	ATOM 1142 CZ PHE A 145 31.636 33.441 33.879 1.00 13.29 C
1546	ATOM 1143 N ASN A 146 36.414 34.254 31.355 1.00 17.06 N
1547	ATOM 1144 CA ASN A 146 37.708 34.004 31.955 1.00 19.70 C
1548	ATOM 1145 C ASN A 146 37.705 33.035 33.116 1.00 23.78 C
1549	ATOM 1146 O ASN A 146 36.761 32.966 33.886 1.00 22.45 O
1550	ATOM 1147 CB ASN A 146 38.371 35.319 32.419 1.00 35.43 C
1551	ATOM 1148 CG ASN A 146 38.415 36.394 31.352 1.00 22.17 C
1552	ATOM 1149 OD1 ASN A 146 38.346 36.111 30.143 1.00 48.89 O
1553	ATOM 1150 ND2 ASN A 146 38.475 37.638 31.805 1.00 42.74 N
1554	ATOM 1151 N SER A 147 38.837 32.348 33.258 1.00 25.89 N
1555	ATOM 1152 CA SER A 147 39.079 31.414 34.341 1.00 21.10 C
1556	ATOM 1153 C SER A 147 39.110 32.141 35.646 1.00 16.75 C
1557	ATOM 1154 O SER A 147 39.331 33.339 35.692 1.00 23.94 O
1558	ATOM 1155 CB SER A 147 40.411 30.717 34.155 1.00 23.56 C
1559	ATOM 1156 OG SER A 147 40.401 30.011 32.940 1.00 35.23 O
1560	ATOM 1157 N HIS A 148 38.905 31.408 36.709 1.00 15.20 N
1561	ATOM 1158 CA HIS A 148 38.900 32.012 38.020 1.00 15.54 C
1562	ATOM 1159 C HIS A 148 38.562 30.995 39.096 1.00 18.42 C
1563	ATOM 1160 O HIS A 148 38.216 29.827 38.836 1.00 20.82 O
1564	ATOM 1161 CB HIS A 148 37.916 33.182 38.069 1.00 16.72 C
1565	ATOM 1162 CG HIS A 148 36.531 32.651 37.886 1.00 24.91 C
1566	ATOM 1163 ND1 HIS A 148 36.003 32.428 36.614 1.00 30.79 N
1567	ATOM 1164 CD2 HIS A 148 35.626 32.224 38.805 1.00 21.40 C
1568	ATOM 1165 CE1 HIS A 148 34.802 31.899 36.786 1.00 22.80 C
1569	ATOM 1166 NE2 HIS A 148 34.557 31.750 38.084 1.00 20.34 N
1570	ATOM 1167 N ASN A 149 38.650 31.463 40.317 1.00 11.30 N
1571	ATOM 1168 CA ASN A 149 38.373 30.630 41.455 1.00 15.43 C
1572	ATOM 1169 C ASN A 149 37.118 31.011 42.168 1.00 21.68 C
1573	ATOM 1170 O ASN A 149 36.713 32.167 42.191 1.00 20.86 O
1574	ATOM 1171 CB ASN A 149 39.498 30.691 42.491 1.00 14.74 C
1575	ATOM 1172 CG ASN A 149 40.834 30.300 41.905 1.00 27.37 C
1576	ATOM 1173 OD1 ASN A 149 41.831 30.940 42.197 1.00 34.56 O
1577	ATOM 1174 ND2 ASN A 149 40.866 29.237 41.109 1.00 34.06 N
1578	ATOM 1175 N VAL A 150 36.603 30.021 42.849 1.00 20.03 N
1579	ATOM 1176 CA VAL A 150 35.413 30.149 43.643 1.00 14.96 C
1580	ATOM 1177 C VAL A 150 35.751 29.788 45.071 1.00 15.21 C
1581	ATOM 1178 O VAL A 150 36.219 28.701 45.354 1.00 15.43 O
1582	ATOM 1179 CB VAL A 150 34.336 29.244 43.053 1.00 16.21 C
1583	ATOM 1180 CG1 VAL A 150 33.119 29.207 43.961 1.00 6.90 C
1584	ATOM 1181 CG2 VAL A 150 33.981 29.669 41.613 1.00 9.47 C
1585	ATOM 1182 N TYR A 151 35.583 30.722 45.971 1.00 15.14 N
1586	ATOM 1183 CA TYR A 151 35.951 30.501 47.348 1.00 18.34 C
1587	ATOM 1184 C TYR A 151 34.835 29.954 48.191 1.00 19.62 C
1588	ATOM 1185 O TYR A 151 33.781 30.549 48.273 1.00 25.21 O
1589	ATOM 1186 CB TYR A 151 36.575 31.765 47.962 1.00 23.45 C
1590	ATOM 1187 CG TYR A 151 37.736 32.156 47.096 1.00 26.18 C
1591	ATOM 1188 CD1 TYR A 151 37.559 33.041 46.033 1.00 22.18 C
1592	ATOM 1189 CD2 TYR A 151 38.965 31.509 47.234 1.00 28.89 C
1593	ATOM 1190 CE1 TYR A 151 38.607 33.316 45.155 1.00 25.72 C
1594	ATOM 1191 CE2 TYR A 151 40.030 31.787 46.380 1.00 31.38 C
1595	ATOM 1192 CZ TYR A 151 39.849 32.708 45.349 1.00 27.71 C
1596	ATOM 1193 OH TYR A 151 40.887 32.992 44.500 1.00 36.54 O
1597	ATOM 1194 N ILE A 152 35.116 28.840 48.855 1.00 18.81 N
1598	ATOM 1195 CA ILE A 152 34.135 28.186 49.665 1.00 15.88 C
1599	ATOM 1196 C ILE A 152 34.493 28.143 51.124 1.00 21.46 C
1600	ATOM 1197 O ILE A 152 35.618 27.851 51.481 1.00 28.41 O
1601	ATOM 1198 CB ILE A 152 33.912 26.781 49.135 1.00 17.09 C
1602	ATOM 1199 CG1 ILE A 152 33.401 26.874 47.709 1.00 17.10 C
1603	ATOM 1200 CG2 ILE A 152 32.933 26.010 50.023 1.00 12.11 C
1604	ATOM 1201 CD1 ILE A 152 33.430 25.532 46.994 1.00 20.72 C
1605	ATOM 1202 N MET A 153 33.485 28.408 51.950 1.00 24.27 N
1606	ATOM 1203 CA MET A 153 33.551 28.369 53.412 1.00 23.38 C
1607	ATOM 1204 C MET A 153 32.251 27.811 53.980 1.00 26.97 C
1608	ATOM 1205 O MET A 153 31.175 28.045 53.411 1.00 22.22 O
1609	ATOM 1206 CB MET A 153 33.742 29.754 54.029 1.00 25.74 C
1610	ATOM 1207 CG MET A 153 34.568 30.685 53.187 1.00 48.64 C
1611	ATOM 1208 SD MET A 153 33.964 32.377 53.322 1.00 72.85 S
1612	ATOM 1209 CE MET A 153 33.583 32.675 51.563 1.00 71.06 C
1613	ATOM 1210 N ALA A 154 32.332 27.106 55.113 1.00 25.94 N
1614	ATOM 1211 CA ALA A 154 31.131 26.559 55.746 1.00 30.64 C
1615	ATOM 1212 C ALA A 154 30.264 27.628 56.427 1.00 43.17 C
1616	ATOM 1213 O ALA A 154 30.683 28.751 56.672 1.00 34.72 O
1617	ATOM 1214 CB ALA A 154 31.422 25.409 56.713 1.00 28.15 C
1618	ATOM 1215 N ASP A 155 29.030 27.247 56.734 1.00 47.28 N
1619	ATOM 1216 CA ASP A 155 28.108 28.086 57.451 1.00 44.16 C
1620	ATOM 1217 C ASP A 155 27.425 27.235 58.481 1.00 43.89 C
1621	ATOM 1218 O ASP A 155 26.589 26.434 58.130 1.00 43.49 O
1622	ATOM 1219 CB ASP A 155 27.053 28.758 56.556 1.00 42.46 C
1623	ATOM 1220 CG ASP A 155 26.415 29.940 57.233 1.00 55.84 C
1624	ATOM 1221 OD1 ASP A 155 26.559 30.201 58.417 1.00 54.21 O
1625	ATOM 1222 OD2 ASP A 155 25.738 30.691 56.402 1.00 77.72 O
1626	ATOM 1223 N LYS A 156 27.847 27.357 59.731 1.00 47.41 N
1627	ATOM 1224 CA LYS A 156 27.257 26.634 60.850 1.00 51.10 C
1628	ATOM 1225 C LYS A 156 27.889 25.283 61.247 1.00 64.72 C
1629	ATOM 1226 O LYS A 156 29.096 25.077 61.069 1.00 65.03 O
1630	ATOM 1227 CB LYS A 156 25.729 26.654 60.911 1.00 46.19 C
1631	ATOM 1228 CG LYS A 156 25.264 27.919 61.595 1.00 50.50 C
1632	ATOM 1229 CD LYS A 156 23.754 27.998 61.720 1.00 50.19 C
1633	ATOM 1230 N GLN A 157 26.980 24.389 61.747 0.00 60.96 N
1634	ATOM 1231 CA GLN A 157 27.304 23.039 62.226 0.00 60.51 C
1635	ATOM 1232 C GLN A 157 26.413 21.937 61.605 0.00 63.33 C
1636	ATOM 1233 O GLN A 157 26.493 20.766 62.017 0.00 62.97 O
1637	ATOM 1234 CB GLN A 157 27.163 23.007 63.753 0.00 61.92 C
1638	ATOM 1235 CG GLN A 157 25.778 23.485 64.285 0.00 77.83 C
1639	ATOM 1236 CD GLN A 157 25.008 22.405 65.035 0.00 97.66 C
1640	ATOM 1237 N LYS A 158 25.542 22.286 60.617 0.00 58.62 N
1641	ATOM 1238 CA LYS A 158 24.681 21.270 59.972 0.00 57.57 C
1642	ATOM 1239 C LYS A 158 23.916 21.838 58.798 0.00 59.16 C
1643	ATOM 1240 O LYS A 158 23.191 21.152 58.076 0.00 57.09 O
1644	ATOM 1241 CB LYS A 158 23.725 20.626 60.979 0.00 60.29 C
1645	ATOM 1242 N ASN A 159 24.213 23.140 58.661 1.00 56.54 N
1646	ATOM 1243 CA ASN A 159 23.636 24.135 57.817 1.00 51.04 C
1647	ATOM 1244 C ASN A 159 24.208 24.054 56.386 1.00 46.79 C
1648	ATOM 1245 O ASN A 159 23.980 23.093 55.632 1.00 47.15 O
1649	ATOM 1246 CB ASN A 159 24.061 25.420 58.458 1.00 38.33 C
1650	ATOM 1247 CG ASN A 159 23.166 26.550 58.180 1.00 69.24 C
1651	ATOM 1248 OD1 ASN A 159 22.492 26.558 57.144 1.00 58.18 O
1652	ATOM 1249 ND2 ASN A 159 23.182 27.515 59.098 1.00 30.12 N
1653	ATOM 1250 N GLY A 160 24.915 25.109 55.931 1.00 32.60 N
1654	ATOM 1251 CA GLY A 160 25.407 25.077 54.568 1.00 26.86 C
1655	ATOM 1252 C GLY A 160 26.708 25.789 54.355 1.00 25.83 C
1656	ATOM 1253 O GLY A 160 27.592 25.792 55.189 1.00 18.33 O
1657	ATOM 1254 N ILE A 161 26.799 26.421 53.214 1.00 31.59 N
1658	ATOM 1255 CA ILE A 161 27.989 27.124 52.858 1.00 21.88 C
1659	ATOM 1256 C ILE A 161 27.694 28.481 52.238 1.00 20.25 C
1660	ATOM 1257 O ILE A 161 26.602 28.738 51.700 1.00 16.66 O
1661	ATOM 1258 CB ILE A 161 28.782 26.275 51.880 1.00 17.95 C
1662	ATOM 1259 CG1 ILE A 161 27.965 26.093 50.605 1.00 7.48 C
1663	ATOM 1260 CG2 ILE A 161 29.134 24.931 52.522 1.00 16.41 C
1664	ATOM 1261 CD1 ILE A 161 28.810 25.660 49.426 1.00 16.58 C
1665	ATOM 1262 N LYS A 162 28.736 29.304 52.329 1.00 17.09 N
1666	ATOM 1263 CA LYS A 162 28.864 30.647 51.808 1.00 15.74 C
1667	ATOM 1264 C LYS A 162 30.001 30.607 50.817 1.00 23.93 C
1668	ATOM 1265 O LYS A 162 31.072 30.024 51.062 1.00 19.06 O
1669	ATOM 1266 CB LYS A 162 29.250 31.600 52.920 1.00 23.20 C
1670	ATOM 1267 CG LYS A 162 28.071 32.094 53.726 1.00 39.82 C
1671	ATOM 1268 CD LYS A 162 28.491 32.989 54.883 1.00 63.38 C
1672	ATOM 1269 N VAL A 163 29.742 31.188 49.686 1.00 19.43 N
1673	ATOM 1270 CA VAL A 163 30.661 31.189 48.599 1.00 22.36 C
1674	ATOM 1271 C VAL A 163 30.772 32.608 48.114 1.00 31.89 C
1675	ATOM 1272 O VAL A 163 29.786 33.334 48.132 1.00 25.53 O
1676	ATOM 1273 CB VAL A 163 30.117 30.293 47.478 1.00 22.33 C
1677	ATOM 1274 CG1 VAL A 163 31.066 30.205 46.279 1.00 16.70 C
1678	ATOM 1275 CG2 VAL A 163 29.761 28.907 47.994 1.00 19.83 C
1679	ATOM 1276 N ASN A 164 31.968 33.001 47.702 1.00 29.01 N
1680	ATOM 1277 CA ASN A 164 32.183 34.345 47.229 1.00 27.69 C
1681	ATOM 1278 C ASN A 164 33.161 34.336 46.080 1.00 31.44 C
1682	ATOM 1279 O ASN A 164 34.079 33.521 46.040 1.00 29.97 O
1683	ATOM 1280 CB ASN A 164 32.681 35.279 48.361 1.00 21.39 C
1684	ATOM 1281 CG ASN A 164 33.674 36.287 47.843 1.00 82.39 C
1685	ATOM 1282 OD1 ASN A 164 33.316 37.431 47.530 1.00 96.97 O
1686	ATOM 1283 ND2 ASN A 164 34.917 35.844 47.684 1.00 93.65 N
1687	ATOM 1284 N PHE A 165 32.963 35.250 45.145 1.00 23.08 N
1688	ATOM 1285 CA PHE A 165 33.860 35.368 44.024 1.00 17.33 C
1689	ATOM 1286 C PHE A 165 33.469 36.478 43.081 1.00 25.33 C
1690	ATOM 1287 O PHE A 165 32.345 36.977 43.125 1.00 13.93 O
1691	ATOM 1288 CB PHE A 165 34.013 34.062 43.270 1.00 15.34 C
1692	ATOM 1289 CG PHE A 165 32.741 33.583 42.600 1.00 19.23 C
1693	ATOM 1290 CD1 PHE A 165 32.488 33.837 41.254 1.00 17.68 C
1694	ATOM 1291 CD2 PHE A 165 31.844 32.770 43.293 1.00 17.17 C
1695	ATOM 1292 CE1 PHE A 165 31.334 33.350 40.635 1.00 21.60 C
1696	ATOM 1293 CE2 PHE A 165 30.702 32.246 42.687 1.00 10.85 C
1697	ATOM 1294 CZ PHE A 165 30.445 32.545 41.351 1.00 13.02 C
1698	ATOM 1295 N LYS A 166 34.421 36.850 42.233 1.00 23.13 N
1699	ATOM 1296 CA LYS A 166 34.195 37.888 41.257 1.00 20.67 C
1700	ATOM 1297 C LYS A 166 34.448 37.382 39.887 1.00 20.45 C
1701	ATOM 1298 O LYS A 166 35.389 36.625 39.664 1.00 21.32 O
1702	ATOM 1299 CB LYS A 166 35.079 39.112 41.437 1.00 28.78 C
1703	ATOM 1300 CG LYS A 166 35.197 39.591 42.858 1.00 31.76 C
1704	ATOM 1301 CD LYS A 166 35.778 40.994 42.938 1.00 57.04 C
1705	ATOM 1302 CE LYS A 166 36.167 41.402 44.352 1.00100.00 C
1706	ATOM 1303 NZ LYS A 166 35.533 40.575 45.400 1.00100.00 N
1707	ATOM 1304 N ILE A 167 33.597 37.845 38.985 1.00 14.20 N
1708	ATOM 1305 CA ILE A 167 33.702 37.566 37.596 1.00 9.32 C
1709	ATOM 1306 C ILE A 167 34.100 38.852 36.938 1.00 15.69 C
1710	ATOM 1307 O ILE A 167 33.622 39.898 37.320 1.00 16.92 O
1711	ATOM 1308 CB ILE A 167 32.382 37.148 37.052 1.00 12.14 C
1712	ATOM 1309 CG1 ILE A 167 31.984 35.806 37.656 1.00 18.67 C
1713	ATOM 1310 CG2 ILE A 167 32.440 37.113 35.533 1.00 13.23 C
1714	ATOM 1311 CD1 ILE A 167 32.906 34.667 37.245 1.00 35.18 C
1715	ATOM 1312 N ARG A 168 34.984 38.759 35.970 1.00 16.32 N
1716	ATOM 1313 CA ARG A 168 35.434 39.914 35.234 1.00 19.07 C
1717	ATOM 1314 C ARG A 168 34.989 39.747 33.808 1.00 22.12 C
1718	ATOM 1315 O ARG A 168 35.572 38.945 33.087 1.00 27.16 O
1719	ATOM 1316 CB ARG A 168 36.957 40.021 35.252 1.00 31.75 C
1720	ATOM 1317 CG ARG A 168 37.583 40.300 36.621 1.00 36.42 C
1721	ATOM 1318 CD ARG A 168 37.865 41.794 36.838 1.00100.00 C
1722	ATOM 1319 NE ARG A 168 38.585 42.189 38.069 1.00100.00 N
1723	ATOM 1320 CZ ARG A 168 38.848 41.442 39.152 1.00100.00 C
1724	ATOM 1321 NH1 ARG A 168 38.508 40.159 39.244 1.00100.00 N
1725	ATOM 1322 NH2 ARG A 168 39.499 41.998 40.175 1.00100.00 N
1726	ATOM 1323 N HIS A 169 33.964 40.491 33.400 1.00 14.99 N
1727	ATOM 1324 CA HIS A 169 33.443 40.392 32.055 1.00 17.40 C
1728	ATOM 1325 C HIS A 169 34.168 41.325 31.107 1.00 22.45 C
1729	ATOM 1326 O HIS A 169 34.292 42.500 31.381 1.00 28.10 O
1730	ATOM 1327 CB HIS A 169 31.926 40.724 32.061 1.00 20.64 C
1731	ATOM 1328 CG HIS A 169 31.085 39.748 32.847 1.00 21.34 C
1732	ATOM 1329 ND1 HIS A 169 30.692 38.523 32.318 1.00 21.01 N
1733	ATOM 1330 CD2 HIS A 169 30.568 39.842 34.109 1.00 25.25 C
1734	ATOM 1331 CE1 HIS A 169 29.967 37.918 33.255 1.00 20.94 C
1735	ATOM 1332 NE2 HIS A 169 29.876 38.682 34.344 1.00 21.15 N
1736	ATOM 1333 N ASN A 170 34.629 40.830 29.976 1.00 14.29 N
1737	ATOM 1334 CA ASN A 170 35.315 41.722 29.079 1.00 14.53 C
1738	ATOM 1335 C ASN A 170 34.350 42.540 28.297 1.00 21.60 C
1739	ATOM 1336 O ASN A 170 33.422 41.996 27.730 1.00 29.24 O
1740	ATOM 1337 CB ASN A 170 36.180 41.014 28.006 1.00 18.49 C
1741	ATOM 1338 CG ASN A 170 37.232 40.032 28.492 1.00 32.08 C
1742	ATOM 1339 OD1 ASN A 170 37.629 39.121 27.744 1.00 74.95 O
1743	ATOM 1340 ND2 ASN A 170 37.779 40.283 29.673 1.00 22.44 N
1744	ATOM 1341 N ILE A 171 34.661 43.816 28.159 1.00 21.10 N
1745	ATOM 1342 CA ILE A 171 33.890 44.689 27.327 1.00 16.05 C
1746	ATOM 1343 C ILE A 171 34.542 44.787 25.971 1.00 17.35 C
1747	ATOM 1344 O ILE A 171 35.710 44.462 25.805 1.00 27.50 O
1748	ATOM 1345 CB ILE A 171 33.646 46.046 27.941 1.00 20.76 C
1749	ATOM 1346 CG1 ILE A 171 32.998 45.825 29.277 1.00 22.36 C
1750	ATOM 1347 CG2 ILE A 171 32.676 46.825 27.076 1.00 24.81 C
1751	ATOM 1348 CD1 ILE A 171 34.013 45.906 30.390 1.00 25.76 C
1752	ATOM 1349 N GLU A 172 33.785 45.209 24.991 1.00 20.14 N
1753	ATOM 1350 CA GLU A 172 34.301 45.314 23.648 1.00 28.33 C
1754	ATOM 1351 C GLU A 172 35.461 46.307 23.474 1.00 29.56 C
1755	ATOM 1352 O GLU A 172 36.301 46.114 22.599 1.00 32.44 O
1756	ATOM 1353 CB GLU A 172 33.168 45.539 22.628 1.00 32.63 C
1757	ATOM 1354 CG GLU A 172 31.809 44.973 23.087 1.00 56.28 C
1758	ATOM 1355 N ASP A 173 35.527 47.352 24.327 1.00 25.33 N
1759	ATOM 1356 CA ASP A 173 36.580 48.374 24.252 1.00 20.06 C
1760	ATOM 1357 C ASP A 173 37.888 47.966 24.935 1.00 25.71 C
1761	ATOM 1358 O ASP A 173 38.856 48.717 25.022 1.00 29.54 O
1762	ATOM 1359 CB ASP A 173 36.080 49.721 24.797 1.00 17.51 C
1763	ATOM 1360 CG ASP A 173 35.750 49.692 26.274 1.00 29.64 C
1764	ATOM 1361 OD1 ASP A 173 35.261 50.637 26.863 1.00 33.67 O
1765	ATOM 1362 OD2 ASP A 173 36.026 48.560 26.874 1.00 32.38 O
1766	ATOM 1363 N GLY A 174 37.915 46.760 25.444 1.00 25.32 N
1767	ATOM 1364 CA GLY A 174 39.095 46.297 26.117 1.00 24.38 C
1768	ATOM 1365 C GLY A 174 38.930 46.449 27.614 1.00 27.26 C
1769	ATOM 1366 O GLY A 174 39.711 45.888 28.379 1.00 26.26 O
1770	ATOM 1367 N SER A 175 37.934 47.243 28.038 1.00 16.17 N
1771	ATOM 1368 CA SER A 175 37.723 47.418 29.461 1.00 16.66 C
1772	ATOM 1369 C SER A 175 37.142 46.162 30.110 1.00 26.45 C
1773	ATOM 1370 O SER A 175 36.978 45.140 29.461 1.00 21.15 O
1774	ATOM 1371 CB SER A 175 36.930 48.639 29.829 1.00 22.90 C
1775	ATOM 1372 OG SER A 175 37.264 48.980 31.166 1.00 49.97 O
1776	ATOM 1373 N VAL A 176 36.819 46.240 31.395 1.00 16.22 N
1777	ATOM 1374 CA VAL A 176 36.318 45.090 32.083 1.00 24.83 C
1778	ATOM 1375 C VAL A 176 35.178 45.425 33.042 1.00 34.08 C
1779	ATOM 1376 O VAL A 176 35.284 46.348 33.838 1.00 28.45 O
1780	ATOM 1377 CB VAL A 176 37.476 44.335 32.769 1.00 32.77 C
1781	ATOM 1378 CG1 VAL A 176 37.742 44.870 34.161 1.00 30.36 C
1782	ATOM 1379 CG2 VAL A 176 37.194 42.851 32.850 1.00 36.37 C
1783	ATOM 1380 N GLN A 177 34.082 44.650 32.926 1.00 26.51 N
1784	ATOM 1381 CA GLN A 177 32.905 44.769 33.785 1.00 18.77 C
1785	ATOM 1382 C GLN A 177 32.891 43.722 34.899 1.00 15.72 C
1786	ATOM 1383 O GLN A 177 32.751 42.526 34.645 1.00 14.90 O
1787	ATOM 1384 CB GLN A 177 31.596 44.680 32.971 1.00 19.07 C
1788	ATOM 1385 CG GLN A 177 30.365 44.562 33.895 1.00 23.93 C
1789	ATOM 1386 CD GLN A 177 29.867 45.905 34.425 1.00 21.52 C
1790	ATOM 1387 OE1 GLN A 177 29.414 46.750 33.641 1.00 29.52 O
1791	ATOM 1388 NE2 GLN A 177 29.841 46.060 35.759 1.00 18.24 N
1792	ATOM 1389 N LEU A 178 32.990 44.207 36.125 1.00 11.97 N
1793	ATOM 1390 CA LEU A 178 33.025 43.424 37.337 1.00 16.42 C
1794	ATOM 1391 C LEU A 178 31.637 42.987 37.788 1.00 27.25 C
1795	ATOM 1392 O LEU A 178 30.667 43.758 37.761 1.00 23.48 O
1796	ATOM 1393 CB LEU A 178 33.699 44.261 38.438 1.00 17.69 C
1797	ATOM 1394 CG LEU A 178 34.165 43.519 39.684 1.00 34.96 C
1798	ATOM 1395 CD1 LEU A 178 32.972 43.023 40.483 1.00 52.09 C
1799	ATOM 1396 CD2 LEU A 178 35.061 42.352 39.317 1.00 35.65 C
1800	ATOM 1397 N ALA A 179 31.569 41.722 38.200 1.00 13.82 N
1801	ATOM 1398 CA ALA A 179 30.362 41.098 38.690 1.00 11.02 C
1802	ATOM 1399 C ALA A 179 30.718 40.386 39.945 1.00 15.40 C
1803	ATOM 1400 O ALA A 179 31.275 39.315 39.891 1.00 25.10 O
1804	ATOM 1401 CB ALA A 179 29.841 40.097 37.680 1.00 12.99 C
1805	ATOM 1402 N ASP A 180 30.417 41.014 41.055 1.00 11.38 N
1806	ATOM 1403 CA ASP A 180 30.702 40.517 42.360 1.00 13.79 C
1807	ATOM 1404 C ASP A 180 29.612 39.564 42.831 1.00 22.27 C
1808	ATOM 1405 O ASP A 180 28.487 40.006 43.027 1.00 23.50 O
1809	ATOM 1406 CB ASP A 180 30.668 41.750 43.255 1.00 17.87 C
1810	ATOM 1407 CG ASP A 180 31.903 42.018 44.039 1.00 52.33 C
1811	ATOM 1408 OD1 ASP A 180 32.163 41.443 45.078 1.00 54.34 O
1812	ATOM 1409 OD2 ASP A 180 32.543 43.073 43.592 1.00 75.02 O
1813	ATOM 1410 N HIS A 181 29.941 38.274 43.049 1.00 18.45 N
1814	ATOM 1411 CA HIS A 181 28.953 37.274 43.489 1.00 13.73 C
1815	ATOM 1412 C HIS A 181 28.942 37.004 44.969 1.00 20.26 C
1816	ATOM 1413 O HIS A 181 29.979 36.752 45.550 1.00 19.93 O
1817	ATOM 1414 CB HIS A 181 29.118 35.896 42.798 1.00 11.97 C
1818	ATOM 1415 CG HIS A 181 28.889 35.894 41.308 1.00 11.39 C
1819	ATOM 1416 ND1 HIS A 181 29.510 36.794 40.470 1.00 8.37 N
1820	ATOM 1417 CD2 HIS A 181 28.120 35.081 40.540 1.00 6.05 C
1821	ATOM 1418 CE1 HIS A 181 29.119 36.516 39.218 1.00 12.04 C
1822	ATOM 1419 NE2 HIS A 181 28.282 35.477 39.225 1.00 11.44 N
1823	ATOM 1420 N TYR A 182 27.731 36.999 45.549 1.00 18.05 N
1824	ATOM 1421 CA TYR A 182 27.475 36.614 46.927 1.00 16.99 C
1825	ATOM 1422 C TYR A 182 26.504 35.455 46.864 1.00 20.89 C
1826	ATOM 1423 O TYR A 182 25.517 35.531 46.141 1.00 17.92 O
1827	ATOM 1424 CB TYR A 182 26.999 37.758 47.819 1.00 22.96 C
1828	ATOM 1425 CG TYR A 182 28.073 38.820 47.860 1.00 36.33 C
1829	ATOM 1426 CD1 TYR A 182 28.378 39.564 46.721 1.00 40.23 C
1830	ATOM 1427 CD2 TYR A 182 28.868 39.010 48.989 1.00 37.84 C
1831	ATOM 1428 CE1 TYR A 182 29.401 40.513 46.719 1.00 39.73 C
1832	ATOM 1429 CE2 TYR A 182 29.895 39.958 49.010 1.00 38.43 C
1833	ATOM 1430 CZ TYR A 182 30.166 40.714 47.869 1.00 43.49 C
1834	ATOM 1431 OH TYR A 182 31.189 41.644 47.872 1.00 47.98 O
1835	ATOM 1432 N GLN A 183 26.881 34.333 47.479 1.00 12.15 N
1836	ATOM 1433 CA GLN A 183 26.118 33.114 47.341 1.00 10.16 C
1837	ATOM 1434 C GLN A 183 25.993 32.281 48.621 1.00 23.06 C
1838	ATOM 1435 O GLN A 183 26.933 32.123 49.401 1.00 16.53 O
1839	ATOM 1436 CB GLN A 183 26.722 32.301 46.182 1.00 11.27 C
1840	ATOM 1437 CG GLN A 183 26.419 30.788 46.258 1.00 10.47 C
1841	ATOM 1438 CD GLN A 183 27.097 30.023 45.141 1.00 20.32 C
1842	ATOM 1439 OE1 GLN A 183 27.699 30.618 44.251 1.00 19.13 O
1843	ATOM 1440 NE2 GLN A 183 26.972 28.696 45.157 1.00 13.27 N
1844	ATOM 1441 N GLN A 184 24.781 31.771 48.864 1.00 20.92 N
1845	ATOM 1442 CA GLN A 184 24.545 30.904 50.007 1.00 18.20 C
1846	ATOM 1443 C GLN A 184 23.913 29.595 49.534 1.00 17.70 C
1847	ATOM 1444 O GLN A 184 23.069 29.604 48.647 1.00 22.77 O
1848	ATOM 1445 CB GLN A 184 23.695 31.551 51.120 1.00 19.48 C
1849	ATOM 1446 N ASN A 185 24.343 28.462 50.111 1.00 18.31 N
1850	ATOM 1447 CA ASN A 185 23.762 27.161 49.770 1.00 19.28 C
1851	ATOM 1448 C ASN A 185 23.216 26.461 51.003 1.00 25.54 C
1852	ATOM 1449 O ASN A 185 23.892 26.363 52.027 1.00 26.55 O
1853	ATOM 1450 CB ASN A 185 24.716 26.223 49.039 1.00 19.40 C
1854	ATOM 1451 CG ASN A 185 25.097 26.767 47.696 1.00 10.34 C
1855	ATOM 1452 OD1 ASN A 185 25.772 27.802 47.596 1.00 57.49 O
1856	ATOM 1453 ND2 ASN A 185 24.695 26.041 46.655 1.00 26.13 N
1857	ATOM 1454 N THR A 186 21.980 25.979 50.891 1.00 23.47 N
1858	ATOM 1455 CA THR A 186 21.297 25.288 51.985 1.00 17.89 C
1859	ATOM 1456 C THR A 186 20.644 24.005 51.490 1.00 14.55 C
1860	ATOM 1457 O THR A 186 20.063 23.930 50.398 1.00 15.47 O
1861	ATOM 1458 CB THR A 186 20.309 26.217 52.714 1.00 28.05 C
1862	ATOM 1459 OG1 THR A 186 19.476 26.832 51.762 1.00 42.78 O
1863	ATOM 1460 CG2 THR A 186 21.089 27.297 53.452 1.00 30.06 C
1864	ATOM 1461 N PRO A 187 20.809 22.943 52.250 1.00 17.91 N
1865	ATOM 1462 CA PRO A 187 20.308 21.651 51.802 1.00 22.28 C
1866	ATOM 1463 C PRO A 187 18.799 21.650 51.874 1.00 22.28 C
1867	ATOM 1464 O PRO A 187 18.221 22.270 52.743 1.00 14.52 O
1868	ATOM 1465 CB PRO A 187 20.854 20.630 52.788 1.00 18.02 C
1869	ATOM 1466 CG PRO A 187 21.303 21.414 54.001 1.00 20.57 C
1870	ATOM 1467 CD PRO A 187 21.143 22.901 53.676 1.00 17.53 C
1871	ATOM 1468 N ILE A 188 18.151 20.965 50.969 1.00 20.09 N
1872	ATOM 1469 CA ILE A 188 16.712 20.985 51.050 1.00 23.50 C
1873	ATOM 1470 C ILE A 188 16.103 20.088 52.137 1.00 38.66 C
1874	ATOM 1471 O ILE A 188 15.122 20.454 52.779 1.00 43.14 O
1875	ATOM 1472 CB ILE A 188 16.061 20.783 49.711 1.00 22.12 C
1876	ATOM 1473 CG1 ILE A 188 16.380 21.943 48.775 1.00 13.66 C
1877	ATOM 1474 CG2 ILE A 188 14.565 20.640 49.921 1.00 31.92 C
1878	ATOM 1475 CD1 ILE A 188 15.839 21.724 47.354 1.00 21.23 C
1879	ATOM 1476 N GLY A 189 16.654 18.902 52.361 1.00 36.20 N
1880	ATOM 1477 CA GLY A 189 16.073 18.043 53.383 1.00 43.87 C
1881	ATOM 1478 C GLY A 189 16.511 18.365 54.819 1.00 53.06 C
1882	ATOM 1479 O GLY A 189 16.986 19.452 55.151 1.00 46.18 O
1883	ATOM 1480 N ASP A 190 16.323 17.378 55.684 1.00 59.98 N
1884	ATOM 1481 CA ASP A 190 16.723 17.462 57.080 1.00 64.14 C
1885	ATOM 1482 C ASP A 190 17.835 16.444 57.354 1.00 60.79 C
1886	ATOM 1483 O ASP A 190 18.278 16.225 58.488 1.00 63.52 O
1887	ATOM 1484 CB ASP A 190 15.527 17.259 58.036 1.00 68.17 C
1888	ATOM 1485 CG ASP A 190 15.420 18.327 59.092 1.00 96.99 C
1889	ATOM 1486 OD1 ASP A 190 16.385 18.886 59.589 1.00100.00 O
1890	ATOM 1487 OD2 ASP A 190 14.177 18.582 59.423 1.00100.00 O
1891	ATOM 1488 N GLY A 191 18.267 15.805 56.274 1.00 46.66 N
1892	ATOM 1489 CA GLY A 191 19.300 14.805 56.333 1.00 45.30 C
1893	ATOM 1490 C GLY A 191 20.654 15.453 56.525 1.00 44.47 C
1894	ATOM 1491 O GLY A 191 20.766 16.674 56.388 1.00 45.99 O
1895	ATOM 1492 N PRO A 192 21.672 14.611 56.744 1.00 32.79 N
1896	ATOM 1493 CA PRO A 192 23.030 15.061 56.988 1.00 30.60 C
1897	ATOM 1494 C PRO A 192 23.771 15.586 55.765 1.00 24.21 C
1898	ATOM 1495 O PRO A 192 23.560 15.212 54.608 1.00 33.69 O
1899	ATOM 1496 CB PRO A 192 23.768 13.888 57.638 1.00 33.48 C
1900	ATOM 1497 CG PRO A 192 22.782 12.736 57.733 1.00 32.43 C
1901	ATOM 1498 CD PRO A 192 21.568 13.138 56.917 1.00 24.31 C
1902	ATOM 1499 N VAL A 193 24.697 16.462 56.021 1.00 20.12 N
1903	ATOM 1500 CA VAL A 193 25.386 17.040 54.904 1.00 24.22 C
1904	ATOM 1501 C VAL A 193 26.858 17.236 55.225 1.00 25.67 C
1905	ATOM 1502 O VAL A 193 27.221 17.264 56.390 1.00 26.18 O
1906	ATOM 1503 CB VAL A 193 24.631 18.320 54.585 1.00 24.13 C
1907	ATOM 1504 CG1 VAL A 193 25.241 19.547 55.232 1.00 19.59 C
1908	ATOM 1505 CG2 VAL A 193 24.323 18.485 53.109 1.00 24.51 C
1909	ATOM 1506 N LEU A 194 27.713 17.318 54.218 1.00 23.36 N
1910	ATOM 1507 CA LEU A 194 29.136 17.509 54.477 1.00 22.71 C
1911	ATOM 1508 C LEU A 194 29.541 18.975 54.572 1.00 25.14 C
1912	ATOM 1509 O LEU A 194 29.558 19.687 53.586 1.00 29.25 O
1913	ATOM 1510 CB LEU A 194 29.957 16.913 53.337 1.00 26.63 C
1914	ATOM 1511 CG LEU A 194 30.727 15.661 53.704 1.00 31.66 C
1915	ATOM 1512 CD1 LEU A 194 30.086 14.985 54.897 1.00 27.79 C
1916	ATOM 1513 CD2 LEU A 194 30.731 14.729 52.503 1.00 39.18 C
1917	ATOM 1514 N LEU A 195 29.958 19.420 55.741 1.00 24.97 N
1918	ATOM 1515 CA LEU A 195 30.432 20.786 55.892 1.00 24.74 C
1919	ATOM 1516 C LEU A 195 31.942 20.824 55.686 1.00 29.37 C
1920	ATOM 1517 O LEU A 195 32.668 20.009 56.228 1.00 33.55 O
1921	ATOM 1518 CB LEU A 195 29.985 21.450 57.211 1.00 24.85 C
1922	ATOM 1519 CG LEU A 195 28.468 21.614 57.327 1.00 38.47 C
1923	ATOM 1520 CD1 LEU A 195 28.142 22.683 58.356 1.00 45.74 C
1924	ATOM 1521 CD2 LEU A 195 27.835 21.985 55.983 1.00 25.18 C
1925	ATOM 1522 N PRO A 196 32.427 21.734 54.853 1.00 23.02 N
1926	ATOM 1523 CA PRO A 196 33.844 21.723 54.507 1.00 22.86 C
1927	ATOM 1524 C PRO A 196 34.736 22.777 55.131 1.00 29.60 C
1928	ATOM 1525 O PRO A 196 34.320 23.805 55.638 1.00 28.31 O
1929	ATOM 1526 CB PRO A 196 33.871 21.997 53.004 1.00 23.75 C
1930	ATOM 1527 CG PRO A 196 32.548 22.655 52.649 1.00 26.77 C
1931	ATOM 1528 CD PRO A 196 31.589 22.349 53.792 1.00 12.37 C
1932	ATOM 1529 N ASP A 197 36.018 22.545 54.986 1.00 30.13 N
1933	ATOM 1530 CA ASP A 197 36.961 23.546 55.385 1.00 22.70 C
1934	ATOM 1531 C ASP A 197 37.122 24.422 54.167 1.00 28.34 C
1935	ATOM 1532 O ASP A 197 36.700 24.088 53.061 1.00 22.27 O
1936	ATOM 1533 CB ASP A 197 38.324 22.981 55.831 1.00 20.24 C
1937	ATOM 1534 CG ASP A 197 38.225 22.042 56.987 1.00 21.30 C
1938	ATOM 1535 OD1 ASP A 197 37.347 22.108 57.832 1.00 57.33 O
1939	ATOM 1536 OD2 ASP A 197 39.120 21.097 56.948 1.00 44.62 O
1940	ATOM 1537 N ASN A 198 37.741 25.548 54.353 1.00 23.92 N
1941	ATOM 1538 CA ASN A 198 37.877 26.437 53.251 1.00 16.11 C
1942	ATOM 1539 C ASN A 198 38.716 25.872 52.163 1.00 24.97 C
1943	ATOM 1540 O ASN A 198 39.771 25.302 52.386 1.00 30.00 O
1944	ATOM 1541 CB ASN A 198 38.392 27.796 53.710 1.00 32.20 C
1945	ATOM 1542 CG ASN A 198 37.549 28.325 54.841 1.00 32.43 C
1946	ATOM 1543 OD1 ASN A 198 36.793 27.578 55.478 1.00 71.95 O
1947	ATOM 1544 ND2 ASN A 198 37.603 29.633 55.019 1.00 50.99 N
1948	ATOM 1545 N HIS A 199 38.211 26.061 50.978 1.00 21.23 N
1949	ATOM 1546 CA HIS A 199 38.863 25.646 49.788 1.00 13.52 C
1950	ATOM 1547 C HIS A 199 38.288 26.464 48.668 1.00 14.86 C
1951	ATOM 1548 O HIS A 199 37.498 27.392 48.887 1.00 17.17 O
1952	ATOM 1549 CB HIS A 199 38.721 24.142 49.535 1.00 16.51 C
1953	ATOM 1550 CG HIS A 199 37.305 23.694 49.331 1.00 24.82 C
1954	ATOM 1551 ND1 HIS A 199 36.441 23.529 50.400 1.00 27.44 N
1955	ATOM 1552 CD2 HIS A 199 36.632 23.382 48.187 1.00 22.86 C
1956	ATOM 1553 CE1 HIS A 199 35.281 23.113 49.897 1.00 25.87 C
1957	ATOM 1554 NE2 HIS A 199 35.366 23.011 48.573 1.00 25.12 N
1958	ATOM 1555 N TYR A 200 38.685 26.125 47.470 1.00 14.75 N
1959	ATOM 1556 CA TYR A 200 38.191 26.839 46.344 1.00 13.25 C
1960	ATOM 1557 C TYR A 200 38.024 25.919 45.172 1.00 16.25 C
1961	ATOM 1558 O TYR A 200 38.425 24.763 45.212 1.00 15.38 O
1962	ATOM 1559 CB TYR A 200 39.010 28.110 46.000 1.00 18.31 C
1963	ATOM 1560 CG TYR A 200 40.351 27.746 45.459 1.00 22.76 C
1964	ATOM 1561 CD1 TYR A 200 40.535 27.523 44.096 1.00 26.74 C
1965	ATOM 1562 CD2 TYR A 200 41.424 27.518 46.320 1.00 28.17 C
1966	ATOM 1563 CE1 TYR A 200 41.784 27.146 43.594 1.00 41.53 C
1967	ATOM 1564 CE2 TYR A 200 42.682 27.144 45.839 1.00 26.48 C
1968	ATOM 1565 CZ TYR A 200 42.858 26.953 44.469 1.00 49.44 C
1969	ATOM 1566 OH TYR A 200 44.090 26.559 43.989 1.00 50.60 O
1970	ATOM 1567 N LEU A 201 37.391 26.450 44.143 1.00 13.74 N
1971	ATOM 1568 CA LEU A 201 37.144 25.719 42.948 1.00 14.39 C
1972	ATOM 1569 C LEU A 201 37.750 26.472 41.813 1.00 18.89 C
1973	ATOM 1570 O LEU A 201 37.595 27.687 41.696 1.00 19.12 O
1974	ATOM 1571 CB LEU A 201 35.640 25.566 42.696 1.00 18.62 C
1975	ATOM 1572 CG LEU A 201 34.932 24.769 43.775 1.00 24.46 C
1976	ATOM 1573 CD1 LEU A 201 33.508 24.499 43.333 1.00 27.52 C
1977	ATOM 1574 CD2 LEU A 201 35.633 23.442 43.965 1.00 29.00 C
1978	ATOM 1575 N SER A 202 38.486 25.754 40.998 1.00 16.52 N
1979	ATOM 1576 CA SER A 202 39.095 26.402 39.877 1.00 14.62 C
1980	ATOM 1577 C SER A 202 38.262 26.093 38.669 1.00 16.19 C
1981	ATOM 1578 O SER A 202 38.032 24.939 38.328 1.00 16.30 O
1982	ATOM 1579 CB SER A 202 40.582 26.087 39.736 1.00 13.65 C
1983	ATOM 1580 OG SER A 202 40.897 25.875 38.373 1.00 32.46 O
1984	ATOM 1581 N THR A 203 37.719 27.148 38.082 1.00 19.41 N
1985	ATOM 1582 CA THR A 203 36.823 26.978 36.980 1.00 12.63 C
1986	ATOM 1583 C THR A 203 37.335 27.550 35.717 1.00 19.87 C
1987	ATOM 1584 O THR A 203 38.068 28.524 35.698 1.00 26.55 O
1988	ATOM 1585 CB THR A 203 35.387 27.485 37.278 1.00 17.16 C
1989	ATOM 1586 OG1 THR A 203 35.343 28.867 37.043 1.00 45.79 O
1990	ATOM 1587 CG2 THR A 203 35.056 27.237 38.738 1.00 8.99 C
1991	ATOM 1588 N GLN A 204 36.886 26.895 34.670 1.00 15.38 N
1992	ATOM 1589 CA GLN A 204 37.227 27.181 33.320 1.00 18.56 C
1993	ATOM 1590 C GLN A 204 35.982 26.976 32.484 1.00 23.05 C
1994	ATOM 1591 O GLN A 204 35.324 25.975 32.629 1.00 21.15 O
1995	ATOM 1592 CB GLN A 204 38.301 26.155 32.946 1.00 21.87 C
1996	ATOM 1593 CG GLN A 204 39.111 26.442 31.682 1.00 54.15 C
1997	ATOM 1594 CD GLN A 204 40.213 25.404 31.565 1.00 80.85 C
1998	ATOM 1595 OE1 GLN A 204 40.511 24.881 30.477 1.00 60.93 O
1999	ATOM 1596 NE2 GLN A 204 40.743 25.018 32.725 1.00 63.95 N
2000	ATOM 1597 N SER A 205 35.669 27.924 31.626 1.00 20.98 N
2001	ATOM 1598 CA SER A 205 34.513 27.833 30.774 1.00 21.32 C
2002	ATOM 1599 C SER A 205 34.732 28.336 29.358 1.00 25.83 C
2003	ATOM 1600 O SER A 205 35.387 29.323 29.100 1.00 22.74 O
2004	ATOM 1601 CB SER A 205 33.346 28.538 31.411 1.00 15.54 C
2005	ATOM 1602 OG SER A 205 33.591 28.544 32.809 1.00 25.35 O
2006	ATOM 1603 N ALA A 206 34.115 27.642 28.436 1.00 23.54 N
2007	ATOM 1604 CA ALA A 206 34.157 27.995 27.049 1.00 22.19 C
2008	ATOM 1605 C ALA A 206 32.739 28.110 26.521 1.00 25.30 C
2009	ATOM 1606 O ALA A 206 31.968 27.163 26.646 1.00 21.31 O
2010	ATOM 1607 CB ALA A 206 34.949 26.958 26.251 1.00 20.82 C
2011	ATOM 1608 N LEU A 207 32.419 29.284 25.959 1.00 20.43 N
2012	ATOM 1609 CA LEU A 207 31.127 29.562 25.377 1.00 17.97 C
2013	ATOM 1610 C LEU A 207 31.224 29.407 23.881 1.00 23.64 C
2014	ATOM 1611 O LEU A 207 32.187 29.810 23.246 1.00 24.99 O
2015	ATOM 1612 CB LEU A 207 30.593 30.975 25.676 1.00 20.37 C
2016	ATOM 1613 CG LEU A 207 30.902 31.499 27.067 1.00 22.86 C
2017	ATOM 1614 CD1 LEU A 207 30.054 32.739 27.332 1.00 18.32 C
2018	ATOM 1615 CD2 LEU A 207 30.592 30.440 28.097 1.00 23.75 C
2019	ATOM 1616 N SER A 208 30.216 28.807 23.312 1.00 11.12 N
2020	ATOM 1617 CA SER A 208 30.216 28.609 21.899 1.00 8.25 C
2021	ATOM 1618 C SER A 208 28.813 28.767 21.393 1.00 14.90 C
2022	ATOM 1619 O SER A 208 27.883 29.041 22.161 1.00 25.94 O
2023	ATOM 1620 CB SER A 208 30.749 27.249 21.493 1.00 20.68 C
2024	ATOM 1621 OG SER A 208 30.460 26.288 22.493 1.00 49.73 O
2025	ATOM 1622 N LYS A 209 28.701 28.589 20.099 1.00 17.53 N
2026	ATOM 1623 CA LYS A 209 27.460 28.719 19.365 1.00 24.69 C
2027	ATOM 1624 C LYS A 209 27.274 27.509 18.473 1.00 41.80 C
2028	ATOM 1625 O LYS A 209 28.250 26.954 17.961 1.00 51.95 O
2029	ATOM 1626 CB LYS A 209 27.504 29.969 18.501 1.00 26.95 C
2030	ATOM 1627 CG LYS A 209 26.420 30.976 18.824 1.00 37.54 C
2031	ATOM 1628 CD LYS A 209 26.556 31.576 20.204 1.00 31.71 C
2032	ATOM 1629 CE LYS A 209 25.947 32.963 20.271 1.00 21.44 C
2033	ATOM 1630 NZ LYS A 209 24.873 33.087 21.272 1.00 26.55 N
2034	ATOM 1631 N ASP A 210 26.021 27.094 18.312 1.00 37.99 N
2035	ATOM 1632 CA ASP A 210 25.682 25.978 17.446 1.00 36.60 C
2036	ATOM 1633 C ASP A 210 25.137 26.525 16.137 1.00 42.39 C
2037	ATOM 1634 O ASP A 210 24.074 27.144 16.098 1.00 41.36 O
2038	ATOM 1635 CB ASP A 210 24.713 25.000 18.126 1.00 40.59 C
2039	ATOM 1636 CG ASP A 210 24.354 23.830 17.263 1.00 39.53 C
2040	ATOM 1637 OD1 ASP A 210 24.872 23.606 16.184 1.00 29.36 O
2041	ATOM 1638 OD2 ASP A 210 23.380 23.126 17.776 1.00 55.88 O
2042	ATOM 1639 N PRO A 211 25.928 26.344 15.080 1.00 45.63 N
2043	ATOM 1640 CA PRO A 211 25.677 26.878 13.737 1.00 44.59 C
2044	ATOM 1641 C PRO A 211 24.336 26.494 13.138 1.00 52.67 C
2045	ATOM 1642 O PRO A 211 23.805 27.134 12.223 1.00 50.13 O
2046	ATOM 1643 CB PRO A 211 26.784 26.290 12.867 1.00 44.53 C
2047	ATOM 1644 CG PRO A 211 27.317 25.072 13.614 1.00 44.39 C
2048	ATOM 1645 CD PRO A 211 26.845 25.177 15.057 1.00 35.89 C
2049	ATOM 1646 N ASN A 212 23.821 25.393 13.629 1.00 53.19 N
2050	ATOM 1647 CA ASN A 212 22.575 24.912 13.129 1.00 50.86 C
2051	ATOM 1648 C ASN A 212 21.409 25.514 13.914 1.00 52.16 C
2052	ATOM 1649 O ASN A 212 20.256 25.491 13.471 1.00 56.16 O
2053	ATOM 1650 CB ASN A 212 22.592 23.368 13.042 1.00 36.55 C
2054	ATOM 1651 N GLU A 213 21.726 26.099 15.075 1.00 36.75 N
2055	ATOM 1652 CA GLU A 213 20.704 26.685 15.916 1.00 30.11 C
2056	ATOM 1653 C GLU A 213 20.275 28.074 15.474 1.00 37.62 C
2057	ATOM 1654 O GLU A 213 21.047 29.023 15.504 1.00 36.78 O
2058	ATOM 1655 CB GLU A 213 21.049 26.642 17.409 1.00 28.30 C
2059	ATOM 1656 CG GLU A 213 19.868 27.080 18.304 1.00 26.37 C
2060	ATOM 1657 CD GLU A 213 18.550 26.462 17.908 1.00 27.19 C
2061	ATOM 1658 OE1 GLU A 213 17.568 27.121 17.577 1.00 34.51 O
2062	ATOM 1659 OE2 GLU A 213 18.603 25.150 17.869 1.00 31.18 O
2063	ATOM 1660 N LYS A 214 19.015 28.180 15.075 1.00 36.98 N
2064	ATOM 1661 CA LYS A 214 18.458 29.440 14.632 1.00 37.98 C
2065	ATOM 1662 C LYS A 214 17.919 30.271 15.773 1.00 29.05 C
2066	ATOM 1663 O LYS A 214 17.749 31.475 15.634 1.00 36.83 O
2067	ATOM 1664 CB LYS A 214 17.425 29.308 13.514 1.00 50.77 C
2068	ATOM 1665 CG LYS A 214 17.947 28.557 12.293 1.00 99.98 C
2069	ATOM 1666 CD LYS A 214 18.822 29.389 11.359 1.00100.00 C
2070	ATOM 1667 CE LYS A 214 20.309 29.041 11.438 1.00100.00 C
2071	ATOM 1668 NZ LYS A 214 20.736 28.000 10.485 1.00 95.21 N
2072	ATOM 1669 N ARG A 215 17.609 29.632 16.895 1.00 17.02 N
2073	ATOM 1670 CA ARG A 215 17.141 30.391 18.049 1.00 20.23 C
2074	ATOM 1671 C ARG A 215 18.291 30.953 18.847 1.00 22.41 C
2075	ATOM 1672 O ARG A 215 19.420 30.466 18.785 1.00 22.03 O
2076	ATOM 1673 CB ARG A 215 16.321 29.576 19.022 1.00 28.67 C
2077	ATOM 1674 CG ARG A 215 14.949 29.226 18.497 1.00 27.86 C
2078	ATOM 1675 CD ARG A 215 14.494 27.878 19.009 1.00 24.25 C
2079	ATOM 1676 NE ARG A 215 15.455 26.792 18.771 1.00 25.72 N
2080	ATOM 1677 CZ ARG A 215 15.366 25.652 19.451 1.00 28.66 C
2081	ATOM 1678 NH1 ARG A 215 14.404 25.489 20.347 1.00 20.46 N
2082	ATOM 1679 NH2 ARG A 215 16.231 24.664 19.233 1.00 29.67 N
2083	ATOM 1680 N ASP A 216 17.964 31.967 19.629 1.00 29.90 N
2084	ATOM 1681 CA ASP A 216 18.929 32.582 20.509 1.00 26.94 C
2085	ATOM 1682 C ASP A 216 19.360 31.605 21.599 1.00 30.90 C
2086	ATOM 1683 O ASP A 216 18.549 31.073 22.367 1.00 27.25 O
2087	ATOM 1684 CB ASP A 216 18.451 33.933 21.080 1.00 21.07 C
2088	ATOM 1685 CG ASP A 216 19.617 34.719 21.620 1.00 24.81 C
2089	ATOM 1686 OD1 ASP A 216 19.523 35.519 22.517 1.00 18.28 O
2090	ATOM 1687 OD2 ASP A 216 20.763 34.364 21.075 1.00 32.30 O
2091	ATOM 1688 N HIS A 217 20.654 31.353 21.674 1.00 28.04 N
2092	ATOM 1689 CA HIS A 217 21.117 30.371 22.639 1.00 24.52 C
2093	ATOM 1690 C HIS A 217 22.563 30.531 22.976 1.00 25.09 C
2094	ATOM 1691 O HIS A 217 23.283 31.349 22.435 1.00 22.74 O
2095	ATOM 1692 CB HIS A 217 21.060 28.976 21.989 1.00 20.49 C
2096	ATOM 1693 CG HIS A 217 21.987 28.926 20.808 1.00 24.38 C
2097	ATOM 1694 ND1 HIS A 217 21.776 29.720 19.681 1.00 27.64 N
2098	ATOM 1695 CD2 HIS A 217 23.125 28.208 20.598 1.00 25.86 C
2099	ATOM 1696 CE1 HIS A 217 22.749 29.446 18.816 1.00 20.93 C
2100	ATOM 1697 NE2 HIS A 217 23.581 28.551 19.341 1.00 22.68 N
2101	ATOM 1698 N MET A 218 23.010 29.597 23.785 1.00 21.45 N
2102	ATOM 1699 CA MET A 218 24.396 29.522 24.143 1.00 14.33 C
2103	ATOM 1700 C MET A 218 24.828 28.084 24.402 1.00 18.15 C
2104	ATOM 1701 O MET A 218 24.171 27.321 25.110 1.00 14.60 O
2105	ATOM 1702 CB MET A 218 24.721 30.451 25.337 1.00 16.68 C
2106	ATOM 1703 CG MET A 218 26.000 30.089 26.073 1.00 20.66 C
2107	ATOM 1704 SD MET A 218 26.289 31.075 27.562 1.00 24.66 S
2108	ATOM 1705 CE MET A 218 25.062 30.345 28.674 1.00 21.46 C
2109	ATOM 1706 N VAL A 219 25.969 27.729 23.858 1.00 23.88 N
2110	ATOM 1707 CA VAL A 219 26.584 26.461 24.175 1.00 18.06 C
2111	ATOM 1708 C VAL A 219 27.730 26.730 25.113 1.00 19.50 C
2112	ATOM 1709 O VAL A 219 28.554 27.602 24.831 1.00 17.30 O
2113	ATOM 1710 CB VAL A 219 27.085 25.682 22.993 1.00 11.73 C
2114	ATOM 1711 CG1 VAL A 219 27.709 24.404 23.518 1.00 15.83 C
2115	ATOM 1712 CG2 VAL A 219 25.955 25.385 22.025 1.00 8.85 C
2116	ATOM 1713 N LEU A 220 27.716 25.991 26.223 1.00 16.34 N
2117	ATOM 1714 CA LEU A 220 28.676 26.055 27.307 1.00 12.11 C
2118	ATOM 1715 C LEU A 220 29.353 24.737 27.636 1.00 25.21 C
2119	ATOM 1716 O LEU A 220 28.733 23.681 27.773 1.00 26.93 O
2120	ATOM 1717 CB LEU A 220 28.030 26.617 28.593 1.00 8.44 C
2121	ATOM 1718 CG LEU A 220 28.719 26.286 29.890 1.00 12.18 C
2122	ATOM 1719 CD1 LEU A 220 29.837 27.303 30.172 1.00 15.18 C
2123	ATOM 1720 CD2 LEU A 220 27.689 26.342 31.011 1.00 14.15 C
2124	ATOM 1721 N LEU A 221 30.655 24.857 27.831 1.00 22.76 N
2125	ATOM 1722 CA LEU A 221 31.515 23.782 28.260 1.00 17.08 C
2126	ATOM 1723 C LEU A 221 32.337 24.275 29.459 1.00 15.50 C
2127	ATOM 1724 O LEU A 221 33.059 25.253 29.413 1.00 18.11 O
2128	ATOM 1725 CB LEU A 221 32.382 23.266 27.103 1.00 16.10 C
2129	ATOM 1726 CG LEU A 221 33.436 22.301 27.618 1.00 22.68 C
2130	ATOM 1727 CD1 LEU A 221 32.814 20.928 27.752 1.00 19.65 C
2131	ATOM 1728 CD2 LEU A 221 34.613 22.234 26.663 1.00 9.40 C
2132	ATOM 1729 N GLU A 222 32.188 23.628 30.570 1.00 4.02 N
2133	ATOM 1730 CA GLU A 222 32.817 24.037 31.792 1.00 9.12 C
2134	ATOM 1731 C GLU A 222 33.556 22.884 32.483 1.00 19.60 C
2135	ATOM 1732 O GLU A 222 33.130 21.744 32.450 1.00 19.73 O
2136	ATOM 1733 CB GLU A 222 31.684 24.575 32.671 1.00 10.57 C
2137	ATOM 1734 CG GLU A 222 32.102 25.232 33.970 1.00 24.75 C
2138	ATOM 1735 CD GLU A 222 31.128 26.314 34.314 1.00 22.23 C
2139	ATOM 1736 OE1 GLU A 222 31.072 27.364 33.704 1.00 21.87 O
2140	ATOM 1737 OE2 GLU A 222 30.348 25.999 35.315 1.00 18.97 O
2141	ATOM 1738 N PHE A 223 34.700 23.197 33.091 1.00 15.10 N
2142	ATOM 1739 CA PHE A 223 35.534 22.237 33.793 1.00 10.06 C
2143	ATOM 1740 C PHE A 223 35.792 22.802 35.160 1.00 17.60 C
2144	ATOM 1741 O PHE A 223 36.130 23.980 35.268 1.00 20.07 O
2145	ATOM 1742 CB PHE A 223 36.876 22.008 33.048 1.00 7.64 C
2146	ATOM 1743 CG PHE A 223 36.783 21.141 31.818 1.00 6.94 C
2147	ATOM 1744 CD1 PHE A 223 36.707 19.755 31.925 1.00 12.56 C
2148	ATOM 1745 CD2 PHE A 223 36.808 21.703 30.541 1.00 9.12 C
2149	ATOM 1746 CE1 PHE A 223 36.629 18.962 30.782 1.00 12.43 C
2150	ATOM 1747 CE2 PHE A 223 36.730 20.929 29.387 1.00 14.43 C
2151	ATOM 1748 CZ PHE A 223 36.641 19.546 29.516 1.00 13.06 C
2152	ATOM 1749 N VAL A 224 35.561 22.013 36.209 1.00 7.88 N
2153	ATOM 1750 CA VAL A 224 35.710 22.562 37.548 1.00 14.63 C
2154	ATOM 1751 C VAL A 224 36.396 21.576 38.462 1.00 22.62 C
2155	ATOM 1752 O VAL A 224 36.032 20.398 38.504 1.00 17.49 O
2156	ATOM 1753 CB VAL A 224 34.360 23.037 38.139 1.00 18.15 C
2157	ATOM 1754 CG1 VAL A 224 34.550 23.658 39.512 1.00 12.50 C
2158	ATOM 1755 CG2 VAL A 224 33.750 24.102 37.236 1.00 24.84 C
2159	ATOM 1756 N THR A 225 37.414 22.065 39.178 1.00 19.02 N
2160	ATOM 1757 CA THR A 225 38.170 21.220 40.074 1.00 13.44 C
2161	ATOM 1758 C THR A 225 38.502 21.868 41.404 1.00 13.33 C
2162	ATOM 1759 O THR A 225 38.869 23.045 41.481 1.00 18.01 O
2163	ATOM 1760 CB THR A 225 39.266 20.370 39.392 1.00 19.26 C
2164	ATOM 1761 OG1 THR A 225 40.261 19.934 40.286 1.00 24.17 O
2165	ATOM 1762 CG2 THR A 225 39.839 21.037 38.158 1.00 20.18 C
2166	ATOM 1763 N ALA A 226 38.195 21.133 42.473 1.00 10.01 N
2167	ATOM 1764 CA ALA A 226 38.411 21.635 43.815 1.00 10.09 C
2168	ATOM 1765 C ALA A 226 39.903 21.635 44.131 1.00 28.79 C
2169	ATOM 1766 O ALA A 226 40.646 20.773 43.674 1.00 27.43 O
2170	ATOM 1767 CB ALA A 226 37.644 20.806 44.843 1.00 8.83 C
2171	ATOM 1768 N ALA A 227 40.324 22.582 44.943 1.00 27.75 N
2172	ATOM 1769 CA ALA A 227 41.700 22.690 45.363 1.00 20.70 C
2173	ATOM 1770 C ALA A 227 41.815 23.492 46.626 1.00 29.76 C
2174	ATOM 1771 O ALA A 227 40.811 23.866 47.250 1.00 32.72 O
2175	ATOM 1772 CB ALA A 227 42.535 23.352 44.289 1.00 23.29 C
2176	ATOM 1773 N GLY A 228 43.064 23.776 46.976 1.00 39.08 N
2177	ATOM 1774 CA GLY A 228 43.378 24.556 48.158 1.00 41.94 C
2178	ATOM 1775 C GLY A 228 43.429 23.682 49.393 1.00 53.10 C
2179	ATOM 1776 O GLY A 228 43.286 24.158 50.519 1.00 54.53 O
2180	ATOM 1777 N ILE A 229 43.640 22.389 49.153 1.00 56.04 N
2181	ATOM 1778 CA ILE A 229 43.758 21.390 50.198 1.00 72.55 C
2182	ATOM 1779 C ILE A 229 44.543 20.188 49.677 1.00100.00 C
2183	ATOM 1780 O ILE A 229 45.757 20.077 49.869 1.00100.00 O
2184	ATOM 1781 CB ILE A 229 42.401 20.967 50.747 1.00 73.95 C
2185	ATOM 1782 CG1 ILE A 229 41.828 22.052 51.650 1.00 66.50 C
2186	ATOM 1783 CG2 ILE A 229 42.551 19.662 51.522 1.00 79.78 C
2187	ATOM 1784 CD1 ILE A 229 40.362 21.806 51.996 1.00 48.38 C
2188	TER 1785 ILE A 229
2189	HETATM 1786 O HOH A 301 28.431 12.763 37.223 1.00 20.69 O
2190	HETATM 1787 O HOH A 302 24.921 34.572 36.175 1.00 19.37 O
2191	HETATM 1788 O HOH A 303 27.913 34.736 34.491 1.00 13.27 O
2192	HETATM 1789 O HOH A 304 30.776 18.772 43.859 1.00 23.68 O
2193	HETATM 1790 O HOH A 305 31.894 22.014 48.972 1.00 20.85 O
2194	HETATM 1791 O HOH A 306 21.163 31.128 42.477 1.00 25.10 O
2195	HETATM 1792 O HOH A 307 27.035 48.965 32.805 1.00 41.94 O
2196	HETATM 1793 O HOH A 308 23.155 33.405 40.261 1.00 21.45 O
2197	HETATM 1794 O HOH A 309 23.167 47.840 31.410 1.00 19.55 O
2198	HETATM 1795 O HOH A 310 32.455 39.362 28.812 1.00 30.49 O
2199	HETATM 1796 O HOH A 311 34.536 36.304 32.269 1.00 32.02 O
2200	HETATM 1797 O HOH A 312 32.035 37.320 30.513 1.00 29.80 O
2201	HETATM 1798 O HOH A 313 40.923 29.176 37.390 1.00 48.94 O
2202	HETATM 1799 O HOH A 314 34.889 26.039 55.636 1.00 41.33 O
2203	HETATM 1800 O HOH A 315 37.020 35.216 42.258 1.00 43.02 O
2204	HETATM 1801 O HOH A 316 35.093 30.125 34.470 1.00 30.47 O
2205	HETATM 1802 O HOH A 317 42.964 19.604 42.998 1.00 46.34 O
2206	HETATM 1803 O HOH A 319 29.739 15.697 29.740 1.00 42.82 O
2207	HETATM 1804 O HOH A 320 31.796 20.764 36.179 1.00 24.90 O
2208	HETATM 1805 O HOH A 321 12.579 36.865 25.605 1.00 38.62 O
2209	HETATM 1806 O HOH A 322 27.898 37.348 36.022 1.00 23.11 O
2210	HETATM 1807 O HOH A 323 34.037 14.230 41.803 1.00 44.32 O
2211	HETATM 1808 O HOH A 324 38.739 13.745 52.303 1.00 43.28 O
2212	HETATM 1809 O HOH A 327 37.538 30.277 31.595 1.00 34.29 O
2213	HETATM 1810 O HOH A 329 33.657 47.305 36.323 1.00 36.25 O
2214	HETATM 1811 O HOH A 331 34.582 31.293 25.723 1.00 37.73 O
2215	HETATM 1812 O HOH A 332 36.166 25.306 29.566 1.00 41.36 O
2216	HETATM 1813 O HOH A 334 39.434 23.439 35.992 1.00 41.84 O
2217	HETATM 1814 O HOH A 335 12.615 43.169 37.122 1.00 54.53 O
2218	HETATM 1815 O HOH A 338 16.153 23.748 25.848 1.00 54.54 O
2219	HETATM 1816 O HOH A 341 18.588 22.926 24.703 1.00 32.40 O
2220	HETATM 1817 O HOH A 343 25.217 37.245 24.660 1.00 29.88 O
2221	HETATM 1818 O HOH A 344 22.149 29.403 40.091 1.00 22.04 O
2222	HETATM 1819 O HOH A 345 21.457 26.956 41.037 1.00 17.55 O
2223	HETATM 1820 O HOH A 346 25.540 24.828 42.246 1.00 34.80 O
2224	HETATM 1821 O HOH A 348 32.977 14.159 46.004 1.00 27.62 O
2225	HETATM 1822 O HOH A 351 23.461 47.081 41.440 1.00 71.34 O
2226	HETATM 1823 O HOH A 353 30.222 45.421 42.369 1.00 40.60 O
2227	HETATM 1824 O HOH A 356 21.451 9.317 36.384 1.00 37.11 O
2228	HETATM 1825 O HOH A 358 26.455 41.538 24.939 1.00 40.32 O
2229	HETATM 1826 O HOH A 359 22.634 38.461 24.298 1.00 42.84 O
2230	HETATM 1827 O HOH A 363 35.324 38.059 29.602 1.00 29.85 O
2231	HETATM 1828 O HOH A 366 38.021 29.975 51.516 1.00 43.89 O
2232	HETATM 1829 O HOH A 368 19.458 17.945 51.080 1.00 26.96 O
2233	HETATM 1830 O HOH A 370 31.786 26.650 40.164 1.00 23.44 O
2234	HETATM 1831 O HOH A 371 31.407 25.776 24.717 1.00 37.06 O
2235	HETATM 1832 O HOH A 374 30.666 25.567 37.839 1.00 19.73 O
2236	HETATM 1833 O HOH A 376 31.362 10.849 36.572 1.00 22.87 O
2237	HETATM 1834 O HOH A 379 15.302 48.713 38.036 1.00 27.79 O
2238	HETATM 1835 O HOH A 380 37.442 11.801 39.759 1.00 44.38 O
2239	HETATM 1836 O HOH A 383 30.561 22.730 38.124 1.00 31.28 O
2240	HETATM 1837 O HOH A 387 14.936 35.798 43.273 1.00 35.12 O
2241	HETATM 1838 O HOH A 388 13.336 27.007 42.433 1.00 51.75 O
2242	HETATM 1839 O HOH A 394 28.159 17.122 58.816 1.00 50.62 O
2243	HETATM 1840 O HOH A 395 26.081 8.360 37.830 1.00 47.24 O
2244	HETATM 1841 O HOH A 396 22.473 9.359 39.136 1.00 58.65 O
2245	HETATM 1842 O HOH A 397 34.831 7.498 49.089 1.00 65.10 O
2246	HETATM 1843 O HOH A 398 24.251 7.818 35.804 1.00 39.95 O
2247	HETATM 1844 O HOH A 399 17.765 18.396 23.033 1.00 24.72 O
2248	HETATM 1845 O HOH A 401 19.717 20.698 23.476 1.00 33.88 O
2249	HETATM 1846 O HOH A 402 29.026 11.278 27.232 1.00 44.81 O
2250	HETATM 1847 O HOH A 403 22.243 12.992 23.667 1.00100.00 O
2251	HETATM 1848 O HOH A 404 27.944 24.472 37.604 1.00 15.01 O
2252	HETATM 1849 O HOH A 405 33.556 17.402 56.163 1.00 22.63 O
2253	HETATM 1850 O HOH A 406 32.292 13.258 49.100 1.00 50.92 O
2254	HETATM 1851 O HOH A 407 35.256 52.737 39.747 1.00 49.02 O
2255	HETATM 1852 O HOH A 408 25.869 46.661 41.769 1.00 44.30 O
2256	HETATM 1853 O HOH A 409 13.568 28.848 43.832 1.00 64.00 O
2257	HETATM 1854 O HOH A 410 15.184 13.474 44.844 1.00 49.16 O
2258	HETATM 1855 O HOH A 413 10.009 18.667 43.066 1.00 81.91 O
2259	HETATM 1856 O HOH A 414 33.762 32.347 22.903 1.00 36.63 O
2260	HETATM 1857 O HOH A 415 42.252 28.285 32.120 1.00 60.12 O
2261	HETATM 1858 O HOH A 416 40.960 34.236 34.214 1.00 60.24 O
2262	HETATM 1859 O HOH A 418 36.435 35.964 35.675 1.00 39.53 O
2263	HETATM 1860 O HOH A 420 22.490 29.298 57.390 1.00 47.19 O
2264	HETATM 1861 O HOH A 421 32.253 38.609 45.063 1.00 51.90 O
2265	HETATM 1862 O HOH A 422 36.760 35.135 50.019 1.00 46.83 O
2266	HETATM 1863 O HOH A 425 15.947 21.375 56.908 1.00 65.12 O
2267	HETATM 1864 O HOH A 426 38.451 25.370 57.282 1.00 42.40 O
2268	HETATM 1865 O HOH A 428 24.816 29.485 15.129 1.00 53.53 O
2269	HETATM 1866 O HOH A 429 24.244 20.981 15.051 1.00 43.77 O
2270	HETATM 1867 O HOH A 430 45.696 23.812 45.001 1.00 70.21 O
2271	CONECT 460 476
2272	CONECT 469 470 474 475
2273	CONECT 470 469 471
2274	CONECT 471 470 472 482
2275	CONECT 472 471 473 474
2276	CONECT 473 472
2277	CONECT 474 469 472 479
2278	CONECT 475 469 476 477
2279	CONECT 476 460 475
2280	CONECT 477 475 478
2281	CONECT 478 477
2282	CONECT 479 474 480
2283	CONECT 480 479 481 488
2284	CONECT 481 480
2285	CONECT 482 471 483
2286	CONECT 483 482 484 487
2287	CONECT 484 483 485
2288	CONECT 485 484 486
2289	CONECT 486 485 487
2290	CONECT 487 483 486
2291	CONECT 488 480
2292	MASTER 311 0 1 4 11 0 0 6 1866 1 21 19
2293	END

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