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Ticket #8035: 1av7.pdb

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1	HEADER SERINE PROTEASE 29-SEP-97 1AV7
2	TITLE SUBTILISIN CARLSBERG L-NAPHTHYL-1-ACETAMIDO BORONIC ACID
3	TITLE 2 INHIBITOR COMPLEX
4	COMPND MOL_ID: 1;
5	COMPND 2 MOLECULE: SUBTILISIN CARLSBERG, TYPE VIII;
6	COMPND 3 CHAIN: A;
7	COMPND 4 SYNONYM: SUBTILOPEPTIDASE A;
8	COMPND 5 EC: 3.4.21.62
9	SOURCE MOL_ID: 1;
10	SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
11	SOURCE 3 ORGANISM_TAXID: 1402;
12	SOURCE 4 OTHER_DETAILS: PURCHASED FROM SIGMA
13	KEYWDS SERINE PROTEASE, HYDROLASE, BORONIC ACID INHIBITORS
14	EXPDTA X-RAY DIFFRACTION
15	AUTHOR V.S.STOLL,B.T.EGER,R.C.HYNES,V.MARTICHONOK,J.B.JONES,E.F.PAI
16	REVDAT 2 24-FEB-09 1AV7 1 VERSN
17	REVDAT 1 01-APR-98 1AV7 0
18	JRNL AUTH V.S.STOLL,B.T.EGER,R.C.HYNES,V.MARTICHONOK,
19	JRNL AUTH 2 J.B.JONES,E.F.PAI
20	JRNL TITL DIFFERENCES IN BINDING MODES OF ENANTIOMERS OF
21	JRNL TITL 2 1-ACETAMIDO BORONIC ACID BASED PROTEASE
22	JRNL TITL 3 INHIBITORS: CRYSTAL STRUCTURES OF
23	JRNL TITL 4 GAMMA-CHYMOTRYPSIN AND SUBTILISIN CARLSBERG
24	JRNL TITL 5 COMPLEXES.
25	JRNL REF BIOCHEMISTRY V. 37 451 1998
26	JRNL REFN ISSN 0006-2960
27	JRNL PMID 9425066
28	JRNL DOI 10.1021/BI971166O
29	REMARK 1
30	REMARK 1 REFERENCE 1
31	REMARK 1 AUTH V.MARTICHONOK,J.B.JONES
32	REMARK 1 TITL PROBING THE SPECIFICITY OF THE SERINE PROTEASES
33	REMARK 1 TITL 2 SUBTILISIN CARLSBERG AND A-CHYMOTRYPSIN WITH
34	REMARK 1 TITL 3 ENANTIOMERIC 1-ACETAMIDO BORONIC ACIDS. AN
35	REMARK 1 TITL 4 UNEXPECTED REVERSAL OF THE NORMAL
36	REMARK 1 TITL 5 "L"-STEREOSELECTIVITY PREFERENCE
37	REMARK 1 REF J.AM.CHEM.SOC. V. 118 950 1996
38	REMARK 1 REFN ISSN 0002-7863
39	REMARK 1 REFERENCE 2
40	REMARK 1 AUTH P.SEUFER-WASSERTHAL,V.MARTICHONOK,T.H.KELLER,
41	REMARK 1 AUTH 2 B.CHIN,R.MARTIN,J.B.JONES
42	REMARK 1 TITL PROBING THE SPECIFICITY OF THE S1 BINDING SITE OF
43	REMARK 1 TITL 2 SUBTILISIN CARLSBERG WITH BORONIC ACIDS
44	REMARK 1 REF BIOORG.MED.CHEM. V. 2 35 1994
45	REMARK 1 REFN ISSN 0968-0896
46	REMARK 1 REFERENCE 3
47	REMARK 1 AUTH P.A.FITZPATRICK,A.C.STEINMETZ,D.RINGE,A.M.KLIBANOV
48	REMARK 1 TITL ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT
49	REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 8653 1993
50	REMARK 1 REFN ISSN 0027-8424
51	REMARK 1 REFERENCE 4
52	REMARK 1 AUTH G.A.PETSKO,D.TSERNOGLOU
53	REMARK 1 TITL THE STRUCTURE OF SUBTILOPEPTIDASE A. I. X-RAY
54	REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA
55	REMARK 1 REF J.MOL.BIOL. V. 106 453 1976
56	REMARK 1 REFN ISSN 0022-2836
57	REMARK 2
58	REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
59	REMARK 3
60	REMARK 3 REFINEMENT.
61	REMARK 3 PROGRAM : X-PLOR 3.1
62	REMARK 3 AUTHORS : BRUNGER
63	REMARK 3
64	REMARK 3 DATA USED IN REFINEMENT.
65	REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
66	REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
67	REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
68	REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
69	REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
70	REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
71	REMARK 3 NUMBER OF REFLECTIONS : 5346
72	REMARK 3
73	REMARK 3 FIT TO DATA USED IN REFINEMENT.
74	REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
75	REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
76	REMARK 3 R VALUE (WORKING SET) : 0.148
77	REMARK 3 FREE R VALUE : 0.273
78	REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
79	REMARK 3 FREE R VALUE TEST SET COUNT : 530
80	REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
81	REMARK 3
82	REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
83	REMARK 3 TOTAL NUMBER OF BINS USED : 8
84	REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
85	REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.70
86	REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 12.00
87	REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 85
88	REMARK 3 BIN R VALUE (WORKING SET) : 0.1680
89	REMARK 3 BIN FREE R VALUE : 0.3090
90	REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.70
91	REMARK 3 BIN FREE R VALUE TEST SET COUNT : 13
92	REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.086
93	REMARK 3
94	REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
95	REMARK 3 PROTEIN ATOMS : 1920
96	REMARK 3 NUCLEIC ACID ATOMS : 0
97	REMARK 3 HETEROGEN ATOMS : 21
98	REMARK 3 SOLVENT ATOMS : 27
99	REMARK 3
100	REMARK 3 B VALUES.
101	REMARK 3 FROM WILSON PLOT (A**2) : NULL
102	REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.10
103	REMARK 3 OVERALL ANISOTROPIC B VALUE.
104	REMARK 3 B11 (A**2) : NULL
105	REMARK 3 B22 (A**2) : NULL
106	REMARK 3 B33 (A**2) : NULL
107	REMARK 3 B12 (A**2) : NULL
108	REMARK 3 B13 (A**2) : NULL
109	REMARK 3 B23 (A**2) : NULL
110	REMARK 3
111	REMARK 3 ESTIMATED COORDINATE ERROR.
112	REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
113	REMARK 3 ESD FROM SIGMAA (A) : NULL
114	REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
115	REMARK 3
116	REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
117	REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
118	REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
119	REMARK 3
120	REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
121	REMARK 3 BOND LENGTHS (A) : 0.011
122	REMARK 3 BOND ANGLES (DEGREES) : 1.71
123	REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10
124	REMARK 3 IMPROPER ANGLES (DEGREES) : 1.56
125	REMARK 3
126	REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED
127	REMARK 3
128	REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
129	REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
130	REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
131	REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
132	REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
133	REMARK 3
134	REMARK 3 NCS MODEL : NULL
135	REMARK 3
136	REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
137	REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
138	REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
139	REMARK 3
140	REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
141	REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
142	REMARK 3 PARAMETER FILE 3 : NULL
143	REMARK 3 PARAMETER FILE 4 : NULL
144	REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
145	REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
146	REMARK 3 TOPOLOGY FILE 3 : TOPH19.PEP
147	REMARK 3 TOPOLOGY FILE 4 : NULL
148	REMARK 3
149	REMARK 3 OTHER REFINEMENT REMARKS: NULL
150	REMARK 4
151	REMARK 4 1AV7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
152	REMARK 100
153	REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
154	REMARK 200
155	REMARK 200 EXPERIMENTAL DETAILS
156	REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
157	REMARK 200 DATE OF DATA COLLECTION : AUG-96
158	REMARK 200 TEMPERATURE (KELVIN) : 287
159	REMARK 200 PH : 7.0
160	REMARK 200 NUMBER OF CRYSTALS USED : 1
161	REMARK 200
162	REMARK 200 SYNCHROTRON (Y/N) : N
163	REMARK 200 RADIATION SOURCE : ROTATING ANODE
164	REMARK 200 BEAMLINE : NULL
165	REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
166	REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
167	REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
168	REMARK 200 MONOCHROMATOR : NI FILTER
169	REMARK 200 OPTICS : FRANKS MIRRORS
170	REMARK 200
171	REMARK 200 DETECTOR TYPE : AREA DETECTOR
172	REMARK 200 DETECTOR MANUFACTURER : SIEMENS
173	REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
174	REMARK 200 DATA SCALING SOFTWARE : XSCALE
175	REMARK 200
176	REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6080
177	REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
178	REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
179	REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
180	REMARK 200
181	REMARK 200 OVERALL.
182	REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
183	REMARK 200 DATA REDUNDANCY : 5.800
184	REMARK 200 R MERGE (I) : NULL
185	REMARK 200 R SYM (I) : 0.12000
186	REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
187	REMARK 200
188	REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
189	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
190	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
191	REMARK 200 COMPLETENESS FOR SHELL (%) : 58.9
192	REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
193	REMARK 200 R MERGE FOR SHELL (I) : NULL
194	REMARK 200 R SYM FOR SHELL (I) : 0.21000
195	REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
196	REMARK 200
197	REMARK 200 DIFFRACTION PROTOCOL: NULL
198	REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOSTRUCTURAL TO 1SCA
199	REMARK 200 SOFTWARE USED: X-PLOR 3.1
200	REMARK 200 STARTING MODEL: PDB ENTRY 1SCA
201	REMARK 200
202	REMARK 200 REMARK: STARTING MODEL WAS RE-INDEXED TO CONFORM TO AXIS
203	REMARK 200 LABELING CONVENTION A<B<C.
204	REMARK 280
205	REMARK 280 CRYSTAL
206	REMARK 280 SOLVENT CONTENT, VS (%): 41.50
207	REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
208	REMARK 280
209	REMARK 280 CRYSTALLIZATION CONDITIONS: AS GIVEN IN REFERENCE 4, PH 7.0
210	REMARK 290
211	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
212	REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
213	REMARK 290
214	REMARK 290 SYMOP SYMMETRY
215	REMARK 290 NNNMMM OPERATOR
216	REMARK 290 1555 X,Y,Z
217	REMARK 290 2555 -X+1/2,-Y,Z+1/2
218	REMARK 290 3555 -X,Y+1/2,-Z+1/2
219	REMARK 290 4555 X+1/2,-Y+1/2,-Z
220	REMARK 290
221	REMARK 290 WHERE NNN -> OPERATOR NUMBER
222	REMARK 290 MMM -> TRANSLATION VECTOR
223	REMARK 290
224	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
225	REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
226	REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
227	REMARK 290 RELATED MOLECULES.
228	REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
229	REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
230	REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
231	REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.50000
232	REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
233	REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.30000
234	REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
235	REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.70000
236	REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.30000
237	REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.50000
238	REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.70000
239	REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
240	REMARK 290
241	REMARK 290 REMARK: NULL
242	REMARK 300
243	REMARK 300 BIOMOLECULE: 1
244	REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
245	REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
246	REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
247	REMARK 300 BURIED SURFACE AREA.
248	REMARK 350
249	REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
250	REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
251	REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
252	REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
253	REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
254	REMARK 350
255	REMARK 350 BIOMOLECULE: 1
256	REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
257	REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
258	REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
259	REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
260	REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
261	REMARK 500
262	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
263	REMARK 500 SUBTOPIC: TORSION ANGLES
264	REMARK 500
265	REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
266	REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
267	REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
268	REMARK 500
269	REMARK 500 STANDARD TABLE:
270	REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
271	REMARK 500
272	REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
273	REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
274	REMARK 500
275	REMARK 500 M RES CSSEQI PSI PHI
276	REMARK 500 TYR A 6 -30.31 -39.24
277	REMARK 500 ASP A 32 -141.21 -151.04
278	REMARK 500 GLN A 36 72.73 -65.32
279	REMARK 500 ASN A 58 44.34 -107.17
280	REMARK 500 ASN A 77 -144.95 -152.18
281	REMARK 500 VAL A 81 -166.95 -113.36
282	REMARK 500 SER A 159 51.46 -111.76
283	REMARK 500 GLU A 195 31.28 -84.20
284	REMARK 500 THR A 211 51.59 75.83
285	REMARK 500
286	REMARK 500 REMARK: NULL
287	REMARK 500
288	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
289	REMARK 500 SUBTOPIC: PLANAR GROUPS
290	REMARK 500
291	REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
292	REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
293	REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
294	REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
295	REMARK 500 AN RMSD GREATER THAN THIS VALUE
296	REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
297	REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
298	REMARK 500
299	REMARK 500 M RES CSSEQI RMS TYPE
300	REMARK 500 TYR A 104 0.08 SIDE_CHAIN
301	REMARK 500
302	REMARK 500 REMARK: NULL
303	REMARK 525
304	REMARK 525 SOLVENT
305	REMARK 525
306	REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
307	REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
308	REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
309	REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
310	REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
311	REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
312	REMARK 525 NUMBER; I=INSERTION CODE):
313	REMARK 525
314	REMARK 525 M RES CSSEQI
315	REMARK 525 HOH A 309 DISTANCE = 5.32 ANGSTROMS
316	REMARK 620
317	REMARK 620 METAL COORDINATION
318	REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
319	REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
320	REMARK 620
321	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
322	REMARK 620 NA A 301 NA
323	REMARK 620 N RES CSSEQI ATOM
324	REMARK 620 1 GLN A 2 NE2
325	REMARK 620 2 ASP A 41 OD1 159.9
326	REMARK 620 3 LEU A 75 O 84.2 82.1
327	REMARK 620 4 ASN A 77 OD1 89.2 75.7 87.8
328	REMARK 620 5 VAL A 81 O 74.5 123.3 104.6 158.1
329	REMARK 620 6 THR A 79 O 87.5 100.5 159.8 73.6 90.8
330	REMARK 620 7 ASP A 41 OD2 147.3 52.7 119.5 112.3 77.5 76.1
331	REMARK 620 N 1 2 3 4 5 6
332	REMARK 620
333	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
334	REMARK 620 NA A 300 NA
335	REMARK 620 N RES CSSEQI ATOM
336	REMARK 620 1 VAL A 174 O
337	REMARK 620 2 ALA A 169 O 85.2
338	REMARK 620 3 TYR A 171 O 72.5 71.4
339	REMARK 620 N 1 2
340	REMARK 800
341	REMARK 800 SITE
342	REMARK 800 SITE_IDENTIFIER: ACT
343	REMARK 800 EVIDENCE_CODE: UNKNOWN
344	REMARK 800 SITE_DESCRIPTION: SERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY
345	REMARK 800 MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE
346	REMARK 800 INHIBITOR.
347	REMARK 800 SITE_IDENTIFIER: M1
348	REMARK 800 EVIDENCE_CODE: UNKNOWN
349	REMARK 800 SITE_DESCRIPTION: SODIUM METAL BINDING SITE 1.
350	REMARK 800 SITE_IDENTIFIER: M2
351	REMARK 800 EVIDENCE_CODE: UNKNOWN
352	REMARK 800 SITE_DESCRIPTION: SODIUM METAL BINDING SITE 2.
353	REMARK 800 SITE_IDENTIFIER: AC1
354	REMARK 800 EVIDENCE_CODE: SOFTWARE
355	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 300
356	REMARK 800 SITE_IDENTIFIER: AC2
357	REMARK 800 EVIDENCE_CODE: SOFTWARE
358	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 301
359	REMARK 999
360	REMARK 999 SEQUENCE
361	REMARK 999
362	REMARK 999 THE 274 RESIDUES ARE NUMBERED 1 - 275 WITH RESIDUE 56
363	REMARK 999 DELETED TO CONFORM TO SEQUENCE NUMBERING IN SUBTILISIN
364	REMARK 999 BPN'.
365	DBREF 1AV7 A 1 275 UNP P00780 SUBT_BACLI 106 379
366	SEQADV 1AV7 SER A 103 UNP P00780 THR 207 CONFLICT
367	SEQADV 1AV7 ALA A 129 UNP P00780 PRO 233 CONFLICT
368	SEQADV 1AV7 ASN A 158 UNP P00780 SER 262 CONFLICT
369	SEQADV 1AV7 SER A 161 UNP P00780 ASN 265 CONFLICT
370	SEQADV 1AV7 ASN A 212 UNP P00780 SER 316 CONFLICT
371	SEQADV 1AV7 SBL A 221 UNP P00780 SER 325 MODIFIED RESIDUE
372	SEQRES 1 A 274 ALA GLN THR VAL PRO TYR GLY ILE PRO LEU ILE LYS ALA
373	SEQRES 2 A 274 ASP LYS VAL GLN ALA GLN GLY PHE LYS GLY ALA ASN VAL
374	SEQRES 3 A 274 LYS VAL ALA VAL LEU ASP THR GLY ILE GLN ALA SER HIS
375	SEQRES 4 A 274 PRO ASP LEU ASN VAL VAL GLY GLY ALA SER PHE VAL ALA
376	SEQRES 5 A 274 GLY GLU ALA TYR ASN THR ASP GLY ASN GLY HIS GLY THR
377	SEQRES 6 A 274 HIS VAL ALA GLY THR VAL ALA ALA LEU ASP ASN THR THR
378	SEQRES 7 A 274 GLY VAL LEU GLY VAL ALA PRO SER VAL SER LEU TYR ALA
379	SEQRES 8 A 274 VAL LYS VAL LEU ASN SER SER GLY SER GLY SER TYR SER
380	SEQRES 9 A 274 GLY ILE VAL SER GLY ILE GLU TRP ALA THR THR ASN GLY
381	SEQRES 10 A 274 MET ASP VAL ILE ASN MET SER LEU GLY GLY ALA SER GLY
382	SEQRES 11 A 274 SER THR ALA MET LYS GLN ALA VAL ASP ASN ALA TYR ALA
383	SEQRES 12 A 274 ARG GLY VAL VAL VAL VAL ALA ALA ALA GLY ASN SER GLY
384	SEQRES 13 A 274 ASN SER GLY SER THR ASN THR ILE GLY TYR PRO ALA LYS
385	SEQRES 14 A 274 TYR ASP SER VAL ILE ALA VAL GLY ALA VAL ASP SER ASN
386	SEQRES 15 A 274 SER ASN ARG ALA SER PHE SER SER VAL GLY ALA GLU LEU
387	SEQRES 16 A 274 GLU VAL MET ALA PRO GLY ALA GLY VAL TYR SER THR TYR
388	SEQRES 17 A 274 PRO THR ASN THR TYR ALA THR LEU ASN GLY THR SBL MET
389	SEQRES 18 A 274 ALA SER PRO HIS VAL ALA GLY ALA ALA ALA LEU ILE LEU
390	SEQRES 19 A 274 SER LYS HIS PRO ASN LEU SER ALA SER GLN VAL ARG ASN
391	SEQRES 20 A 274 ARG LEU SER SER THR ALA THR TYR LEU GLY SER SER PHE
392	SEQRES 21 A 274 TYR TYR GLY LYS GLY LEU ILE ASN VAL GLU ALA ALA ALA
393	SEQRES 22 A 274 GLN
394	MODRES 1AV7 SBL A 221 SER
395	HET SBL A 221 25
396	HET NA A 300 1
397	HET NA A 301 1
398	HETNAM SBL L-NAPHTHYL-1-ACETAMIDO BORONIC ACID ALANINE
399	HETNAM NA SODIUM ION
400	FORMUL 1 SBL C17 H22 B N2 O6 1-
401	FORMUL 2 NA 2(NA 1+)
402	FORMUL 4 HOH *27(H2 O)
403	HELIX 1 1 TYR A 6 ILE A 11 1 6
404	HELIX 2 2 LYS A 12 GLN A 19 1 8
405	HELIX 3 3 GLY A 63 ALA A 74 1 12
406	HELIX 4 4 SER A 103 ASN A 117 1 15
407	HELIX 5 5 SER A 132 GLY A 146 1 15
408	HELIX 6 6 THR A 220 HIS A 238 1 19
409	HELIX 7 7 SER A 242 THR A 253 1 12
410	HELIX 8 8 ASN A 269 ALA A 274 1 6
411	SHEET 1 SH1 8 ASN A 43 PHE A 50 0
412	SHEET 2 SH1 8 SER A 89 VAL A 95 1 O LEU A 90 N VAL A 45
413	SHEET 3 SH1 8 VAL A 26 ASP A 32 1 O VAL A 28 N TYR A 91
414	SHEET 4 SH1 8 ASP A 120 MET A 124 1 N ASP A 120 O LYS A 27
415	SHEET 5 SH1 8 VAL A 148 ALA A 153 1 N VAL A 150 O ILE A 122
416	SHEET 6 SH1 8 ILE A 175 VAL A 180 1 N ILE A 175 O VAL A 149
417	SHEET 7 SH1 8 GLU A 197 GLY A 202 1 N GLY A 202 O VAL A 180
418	SHEET 8 SH1 8 LYS A 265 ILE A 268 1 O GLY A 266 N MET A 199
419	LINK N SBL A 221 C THR A 220 1555 1555 1.33
420	LINK C SBL A 221 N MET A 222 1555 1555 1.33
421	LINK NA NA A 301 NE2 GLN A 2 1555 1555 2.25
422	LINK NA NA A 301 OD1 ASP A 41 1555 1555 2.38
423	LINK NA NA A 301 O LEU A 75 1555 1555 2.23
424	LINK NA NA A 301 OD1 ASN A 77 1555 1555 2.38
425	LINK NA NA A 301 O VAL A 81 1555 1555 2.35
426	LINK NA NA A 300 O VAL A 174 1555 1555 2.41
427	LINK NA NA A 301 O THR A 79 1555 1555 2.50
428	LINK NA NA A 301 OD2 ASP A 41 1555 1555 2.51
429	LINK O ALA A 169 NA NA A 300 1555 1555 2.85
430	LINK O TYR A 171 NA NA A 300 1555 1555 2.78
431	CISPEP 1 TYR A 167 PRO A 168 0 0.18
432	SITE 1 ACT 3 ASP A 32 HIS A 64 SBL A 221
433	SITE 1 M1 4 LEU A 75 ASN A 77 THR A 79 VAL A 81
434	SITE 1 M2 2 ALA A 169 VAL A 174
435	SITE 1 AC1 3 ALA A 169 TYR A 171 VAL A 174
436	SITE 1 AC2 6 GLN A 2 ASP A 41 LEU A 75 ASN A 77
437	SITE 2 AC2 6 THR A 79 VAL A 81
438	CRYST1 53.000 55.400 76.600 90.00 90.00 90.00 P 21 21 21 4
439	ORIGX1 1.000000 0.000000 0.000000 0.00000
440	ORIGX2 0.000000 1.000000 0.000000 0.00000
441	ORIGX3 0.000000 0.000000 1.000000 0.00000
442	SCALE1 0.018868 0.000000 0.000000 0.00000
443	SCALE2 0.000000 0.018051 0.000000 0.00000
444	SCALE3 0.000000 0.000000 0.013055 0.00000
445	ATOM 1 N ALA A 1 41.473 11.812 34.360 1.00 10.25 N
446	ATOM 2 CA ALA A 1 41.788 10.771 33.341 1.00 11.52 C
447	ATOM 3 C ALA A 1 40.517 9.954 33.100 1.00 9.31 C
448	ATOM 4 O ALA A 1 40.123 9.767 31.953 1.00 5.00 O
449	ATOM 5 CB ALA A 1 42.975 9.898 33.797 1.00 5.00 C
450	ATOM 6 N GLN A 2 39.829 9.552 34.169 1.00 5.00 N
451	ATOM 7 CA GLN A 2 38.570 8.821 34.005 1.00 9.19 C
452	ATOM 8 C GLN A 2 37.354 9.745 34.282 1.00 5.00 C
453	ATOM 9 O GLN A 2 37.360 10.536 35.235 1.00 5.00 O
454	ATOM 10 CB GLN A 2 38.522 7.554 34.878 1.00 5.41 C
455	ATOM 11 CG GLN A 2 37.165 6.842 34.819 1.00 5.00 C
456	ATOM 12 CD GLN A 2 37.118 5.576 35.644 1.00 6.87 C
457	ATOM 13 OE1 GLN A 2 37.078 5.626 36.869 1.00 9.45 O
458	ATOM 14 NE2 GLN A 2 37.106 4.430 34.972 1.00 7.03 N
459	ATOM 15 N THR A 3 36.338 9.668 33.434 1.00 5.00 N
460	ATOM 16 CA THR A 3 35.166 10.509 33.588 1.00 5.00 C
461	ATOM 17 C THR A 3 34.075 9.779 34.334 1.00 5.00 C
462	ATOM 18 O THR A 3 33.863 8.595 34.115 1.00 5.33 O
463	ATOM 19 CB THR A 3 34.647 10.971 32.227 1.00 5.07 C
464	ATOM 20 OG1 THR A 3 35.575 11.899 31.663 1.00 8.39 O
465	ATOM 21 CG2 THR A 3 33.295 11.646 32.356 1.00 8.89 C
466	ATOM 22 N VAL A 4 33.434 10.479 35.258 1.00 5.00 N
467	ATOM 23 CA VAL A 4 32.351 9.926 36.053 1.00 5.00 C
468	ATOM 24 C VAL A 4 31.044 10.520 35.504 1.00 5.00 C
469	ATOM 25 O VAL A 4 30.656 11.652 35.828 1.00 6.45 O
470	ATOM 26 CB VAL A 4 32.533 10.284 37.519 1.00 5.00 C
471	ATOM 27 CG1 VAL A 4 31.578 9.512 38.372 1.00 7.58 C
472	ATOM 28 CG2 VAL A 4 33.921 9.964 37.930 1.00 8.23 C
473	ATOM 29 N PRO A 5 30.371 9.775 34.618 1.00 8.11 N
474	ATOM 30 CA PRO A 5 29.113 10.217 34.004 1.00 8.49 C
475	ATOM 31 C PRO A 5 28.095 10.603 35.069 1.00 10.65 C
476	ATOM 32 O PRO A 5 27.817 9.808 35.974 1.00 10.75 O
477	ATOM 33 CB PRO A 5 28.681 8.983 33.202 1.00 10.14 C
478	ATOM 34 CG PRO A 5 30.008 8.338 32.859 1.00 6.27 C
479	ATOM 35 CD PRO A 5 30.719 8.412 34.178 1.00 5.02 C
480	ATOM 36 N TYR A 6 27.480 11.777 34.915 1.00 10.68 N
481	ATOM 37 CA TYR A 6 26.535 12.275 35.912 1.00 9.20 C
482	ATOM 38 C TYR A 6 25.612 11.222 36.528 1.00 8.22 C
483	ATOM 39 O TYR A 6 25.252 11.315 37.705 1.00 10.21 O
484	ATOM 40 CB TYR A 6 25.761 13.504 35.386 1.00 8.10 C
485	ATOM 41 CG TYR A 6 24.444 13.222 34.708 1.00 6.91 C
486	ATOM 42 CD1 TYR A 6 23.339 12.770 35.436 1.00 11.44 C
487	ATOM 43 CD2 TYR A 6 24.313 13.348 33.333 1.00 8.56 C
488	ATOM 44 CE1 TYR A 6 22.147 12.435 34.800 1.00 11.39 C
489	ATOM 45 CE2 TYR A 6 23.128 13.021 32.692 1.00 7.58 C
490	ATOM 46 CZ TYR A 6 22.058 12.561 33.429 1.00 6.99 C
491	ATOM 47 OH TYR A 6 20.912 12.180 32.792 1.00 11.65 O
492	ATOM 48 N GLY A 7 25.298 10.195 35.746 1.00 7.60 N
493	ATOM 49 CA GLY A 7 24.418 9.143 36.199 1.00 5.00 C
494	ATOM 50 C GLY A 7 24.835 8.428 37.463 1.00 8.20 C
495	ATOM 51 O GLY A 7 24.022 8.261 38.368 1.00 11.71 O
496	ATOM 52 N ILE A 8 26.101 8.029 37.545 1.00 8.30 N
497	ATOM 53 CA ILE A 8 26.613 7.289 38.705 1.00 5.00 C
498	ATOM 54 C ILE A 8 26.306 8.003 40.019 1.00 5.00 C
499	ATOM 55 O ILE A 8 25.734 7.412 40.925 1.00 5.00 O
500	ATOM 56 CB ILE A 8 28.136 6.933 38.518 1.00 5.00 C
501	ATOM 57 CG1 ILE A 8 28.279 5.862 37.450 1.00 5.00 C
502	ATOM 58 CG2 ILE A 8 28.768 6.398 39.788 1.00 5.00 C
503	ATOM 59 CD1 ILE A 8 27.860 6.313 36.084 1.00 5.00 C
504	ATOM 60 N PRO A 9 26.688 9.276 40.148 1.00 16.99 N
505	ATOM 61 CA PRO A 9 26.371 9.941 41.409 1.00 20.21 C
506	ATOM 62 C PRO A 9 24.861 10.135 41.593 1.00 22.89 C
507	ATOM 63 O PRO A 9 24.334 9.967 42.704 1.00 14.02 O
508	ATOM 64 CB PRO A 9 27.071 11.289 41.259 1.00 9.19 C
509	ATOM 65 CG PRO A 9 28.245 10.947 40.446 1.00 10.86 C
510	ATOM 66 CD PRO A 9 27.650 10.081 39.380 1.00 10.43 C
511	ATOM 67 N LEU A 10 24.160 10.435 40.497 1.00 12.21 N
512	ATOM 68 CA LEU A 10 22.727 10.700 40.578 1.00 6.99 C
513	ATOM 69 C LEU A 10 21.876 9.589 41.204 1.00 5.00 C
514	ATOM 70 O LEU A 10 20.866 9.885 41.822 1.00 5.00 O
515	ATOM 71 CB LEU A 10 22.172 11.163 39.214 1.00 5.00 C
516	ATOM 72 CG LEU A 10 20.706 11.655 39.155 1.00 6.24 C
517	ATOM 73 CD1 LEU A 10 20.472 12.798 40.106 1.00 5.00 C
518	ATOM 74 CD2 LEU A 10 20.334 12.090 37.741 1.00 7.32 C
519	ATOM 75 N ILE A 11 22.319 8.333 41.099 1.00 5.00 N
520	ATOM 76 CA ILE A 11 21.593 7.169 41.644 1.00 5.00 C
521	ATOM 77 C ILE A 11 22.314 6.591 42.863 1.00 5.00 C
522	ATOM 78 O ILE A 11 21.902 5.567 43.424 1.00 6.19 O
523	ATOM 79 CB ILE A 11 21.407 6.045 40.593 1.00 5.00 C
524	ATOM 80 CG1 ILE A 11 22.773 5.425 40.223 1.00 8.10 C
525	ATOM 81 CG2 ILE A 11 20.686 6.592 39.376 1.00 5.00 C
526	ATOM 82 CD1 ILE A 11 22.749 4.288 39.207 1.00 5.00 C
527	ATOM 83 N LYS A 12 23.380 7.274 43.276 1.00 5.00 N
528	ATOM 84 CA LYS A 12 24.170 6.881 44.429 1.00 6.86 C
529	ATOM 85 C LYS A 12 24.918 5.563 44.277 1.00 8.24 C
530	ATOM 86 O LYS A 12 25.131 4.857 45.254 1.00 9.30 O
531	ATOM 87 CB LYS A 12 23.313 6.895 45.694 1.00 5.17 C
532	ATOM 88 CG LYS A 12 23.173 8.277 46.281 1.00 7.91 C
533	ATOM 89 CD LYS A 12 21.838 8.505 46.967 1.00 7.91 C
534	ATOM 90 CE LYS A 12 21.678 9.987 47.361 1.00 12.58 C
535	ATOM 91 NZ LYS A 12 20.240 10.457 47.372 1.00 7.49 N
536	ATOM 92 N ALA A 13 25.353 5.267 43.052 1.00 14.31 N
537	ATOM 93 CA ALA A 13 26.135 4.061 42.749 1.00 13.17 C
538	ATOM 94 C ALA A 13 27.512 4.219 43.408 1.00 15.29 C
539	ATOM 95 O ALA A 13 28.077 3.268 43.944 1.00 14.30 O
540	ATOM 96 CB ALA A 13 26.301 3.902 41.231 1.00 5.00 C
541	ATOM 97 N ASP A 14 28.044 5.436 43.384 1.00 5.00 N
542	ATOM 98 CA ASP A 14 29.336 5.700 43.986 1.00 5.00 C
543	ATOM 99 C ASP A 14 29.348 5.361 45.479 1.00 7.11 C
544	ATOM 100 O ASP A 14 30.349 4.893 46.012 1.00 12.80 O
545	ATOM 101 CB ASP A 14 29.794 7.149 43.714 1.00 8.80 C
546	ATOM 102 CG ASP A 14 28.748 8.209 44.080 1.00 12.05 C
547	ATOM 103 OD1 ASP A 14 27.533 7.926 44.052 1.00 17.61 O
548	ATOM 104 OD2 ASP A 14 29.145 9.362 44.363 1.00 11.28 O
549	ATOM 105 N LYS A 15 28.206 5.525 46.134 1.00 20.37 N
550	ATOM 106 CA LYS A 15 28.095 5.230 47.560 1.00 18.31 C
551	ATOM 107 C LYS A 15 28.335 3.758 47.815 1.00 15.05 C
552	ATOM 108 O LYS A 15 29.225 3.394 48.571 1.00 8.61 O
553	ATOM 109 CB LYS A 15 26.724 5.642 48.079 1.00 13.98 C
554	ATOM 110 CG LYS A 15 26.482 7.126 47.980 1.00 14.56 C
555	ATOM 111 CD LYS A 15 27.582 7.897 48.666 1.00 17.44 C
556	ATOM 112 CE LYS A 15 26.987 8.926 49.608 1.00 24.72 C
557	ATOM 113 NZ LYS A 15 26.113 9.912 48.893 1.00 31.71 N
558	ATOM 114 N VAL A 16 27.547 2.917 47.161 1.00 7.73 N
559	ATOM 115 CA VAL A 16 27.685 1.471 47.281 1.00 7.04 C
560	ATOM 116 C VAL A 16 29.055 0.974 46.812 1.00 5.17 C
561	ATOM 117 O VAL A 16 29.624 0.052 47.406 1.00 5.00 O
562	ATOM 118 CB VAL A 16 26.598 0.771 46.473 1.00 7.40 C
563	ATOM 119 CG1 VAL A 16 26.795 -0.736 46.498 1.00 8.76 C
564	ATOM 120 CG2 VAL A 16 25.230 1.160 47.015 1.00 5.13 C
565	ATOM 121 N GLN A 17 29.587 1.575 45.754 1.00 5.00 N
566	ATOM 122 CA GLN A 17 30.892 1.164 45.239 1.00 6.30 C
567	ATOM 123 C GLN A 17 31.935 1.484 46.293 1.00 6.30 C
568	ATOM 124 O GLN A 17 32.914 0.762 46.437 1.00 15.18 O
569	ATOM 125 CB GLN A 17 31.252 1.907 43.954 1.00 9.90 C
570	ATOM 126 CG GLN A 17 30.683 1.345 42.664 1.00 10.41 C
571	ATOM 127 CD GLN A 17 31.095 2.188 41.461 1.00 11.08 C
572	ATOM 128 OE1 GLN A 17 32.198 2.726 41.432 1.00 9.06 O
573	ATOM 129 NE2 GLN A 17 30.195 2.336 40.483 1.00 12.50 N
574	ATOM 130 N ALA A 18 31.721 2.563 47.040 1.00 15.13 N
575	ATOM 131 CA ALA A 18 32.666 2.958 48.090 1.00 14.38 C
576	ATOM 132 C ALA A 18 32.562 1.973 49.232 1.00 13.51 C
577	ATOM 133 O ALA A 18 33.453 1.892 50.060 1.00 15.10 O
578	ATOM 134 CB ALA A 18 32.379 4.362 48.579 1.00 11.37 C
579	ATOM 135 N GLN A 19 31.446 1.246 49.276 1.00 27.29 N
580	ATOM 136 CA GLN A 19 31.180 0.225 50.290 1.00 23.94 C
581	ATOM 137 C GLN A 19 31.959 -1.001 49.893 1.00 20.81 C
582	ATOM 138 O GLN A 19 32.129 -1.912 50.684 1.00 19.63 O
583	ATOM 139 CB GLN A 19 29.688 -0.120 50.331 1.00 24.53 C
584	ATOM 140 CG GLN A 19 28.796 1.036 50.797 1.00 27.66 C
585	ATOM 141 CD GLN A 19 27.304 0.729 50.710 1.00 28.60 C
586	ATOM 142 OE1 GLN A 19 26.892 -0.436 50.742 1.00 24.67 O
587	ATOM 143 NE2 GLN A 19 26.482 1.788 50.596 1.00 30.67 N
588	ATOM 144 N GLY A 20 32.439 -1.008 48.655 1.00 10.23 N
589	ATOM 145 CA GLY A 20 33.206 -2.131 48.161 1.00 6.28 C
590	ATOM 146 C GLY A 20 32.392 -3.056 47.281 1.00 6.78 C
591	ATOM 147 O GLY A 20 32.855 -4.130 46.916 1.00 16.87 O
592	ATOM 148 N PHE A 21 31.186 -2.640 46.901 1.00 25.25 N
593	ATOM 149 CA PHE A 21 30.332 -3.485 46.068 1.00 19.64 C
594	ATOM 150 C PHE A 21 30.283 -2.964 44.620 1.00 23.53 C
595	ATOM 151 O PHE A 21 29.792 -1.853 44.347 1.00 5.00 O
596	ATOM 152 CB PHE A 21 28.970 -3.600 46.724 1.00 5.00 C
597	ATOM 153 CG PHE A 21 29.036 -4.091 48.149 1.00 5.00 C
598	ATOM 154 CD1 PHE A 21 29.521 -5.371 48.438 1.00 5.00 C
599	ATOM 155 CD2 PHE A 21 28.660 -3.273 49.203 1.00 5.00 C
600	ATOM 156 CE1 PHE A 21 29.636 -5.830 49.754 1.00 5.00 C
601	ATOM 157 CE2 PHE A 21 28.774 -3.725 50.528 1.00 5.00 C
602	ATOM 158 CZ PHE A 21 29.265 -5.008 50.798 1.00 5.00 C
603	ATOM 159 N LYS A 22 30.920 -3.730 43.722 1.00 10.62 N
604	ATOM 160 CA LYS A 22 31.020 -3.363 42.314 1.00 5.05 C
605	ATOM 161 C LYS A 22 30.418 -4.334 41.301 1.00 5.00 C
606	ATOM 162 O LYS A 22 30.760 -4.300 40.132 1.00 5.00 O
607	ATOM 163 CB LYS A 22 32.476 -3.090 41.968 1.00 6.89 C
608	ATOM 164 CG LYS A 22 33.131 -1.998 42.794 1.00 7.70 C
609	ATOM 165 CD LYS A 22 34.631 -2.059 42.615 1.00 14.09 C
610	ATOM 166 CE LYS A 22 35.340 -0.828 43.160 1.00 20.78 C
611	ATOM 167 NZ LYS A 22 34.988 0.413 42.401 1.00 19.14 N
612	ATOM 168 N GLY A 23 29.545 -5.220 41.747 1.00 5.00 N
613	ATOM 169 CA GLY A 23 28.892 -6.123 40.823 1.00 5.00 C
614	ATOM 170 C GLY A 23 29.724 -7.311 40.427 1.00 5.00 C
615	ATOM 171 O GLY A 23 29.311 -8.100 39.580 1.00 5.00 O
616	ATOM 172 N ALA A 24 30.865 -7.469 41.087 1.00 5.00 N
617	ATOM 173 CA ALA A 24 31.769 -8.574 40.799 1.00 5.00 C
618	ATOM 174 C ALA A 24 31.092 -9.932 40.874 1.00 5.00 C
619	ATOM 175 O ALA A 24 30.272 -10.180 41.752 1.00 10.08 O
620	ATOM 176 CB ALA A 24 32.966 -8.536 41.728 1.00 5.65 C
621	ATOM 177 N ASN A 25 31.458 -10.800 39.934 1.00 15.21 N
622	ATOM 178 CA ASN A 25 30.948 -12.172 39.812 1.00 16.53 C
623	ATOM 179 C ASN A 25 29.451 -12.274 39.576 1.00 16.28 C
624	ATOM 180 O ASN A 25 28.845 -13.319 39.820 1.00 18.48 O
625	ATOM 181 CB ASN A 25 31.386 -13.074 40.987 1.00 13.01 C
626	ATOM 182 CG ASN A 25 31.410 -14.572 40.613 1.00 15.48 C
627	ATOM 183 OD1 ASN A 25 32.090 -14.991 39.662 1.00 13.68 O
628	ATOM 184 ND2 ASN A 25 30.666 -15.377 41.370 1.00 17.51 N
629	ATOM 185 N VAL A 26 28.846 -11.195 39.106 1.00 8.96 N
630	ATOM 186 CA VAL A 26 27.426 -11.224 38.794 1.00 5.03 C
631	ATOM 187 C VAL A 26 27.449 -11.202 37.266 1.00 5.00 C
632	ATOM 188 O VAL A 26 28.319 -10.566 36.691 1.00 5.00 O
633	ATOM 189 CB VAL A 26 26.697 -10.043 39.456 1.00 5.00 C
634	ATOM 190 CG1 VAL A 26 25.232 -10.020 39.077 1.00 5.00 C
635	ATOM 191 CG2 VAL A 26 26.847 -10.148 40.982 1.00 5.00 C
636	ATOM 192 N LYS A 27 26.657 -12.076 36.643 1.00 5.00 N
637	ATOM 193 CA LYS A 27 26.572 -12.215 35.186 1.00 5.00 C
638	ATOM 194 C LYS A 27 25.497 -11.308 34.612 1.00 5.00 C
639	ATOM 195 O LYS A 27 24.348 -11.369 35.028 1.00 5.00 O
640	ATOM 196 CB LYS A 27 26.250 -13.657 34.813 1.00 11.28 C
641	ATOM 197 CG LYS A 27 27.384 -14.668 34.948 1.00 13.93 C
642	ATOM 198 CD LYS A 27 27.847 -14.857 36.393 1.00 23.75 C
643	ATOM 199 CE LYS A 27 26.762 -15.438 37.312 1.00 26.37 C
644	ATOM 200 NZ LYS A 27 27.066 -15.283 38.799 1.00 21.93 N
645	ATOM 201 N VAL A 28 25.871 -10.494 33.629 1.00 14.33 N
646	ATOM 202 CA VAL A 28 24.970 -9.533 32.994 1.00 12.52 C
647	ATOM 203 C VAL A 28 25.020 -9.615 31.462 1.00 16.00 C
648	ATOM 204 O VAL A 28 26.073 -9.360 30.850 1.00 12.01 O
649	ATOM 205 CB VAL A 28 25.354 -8.076 33.435 1.00 12.02 C
650	ATOM 206 CG1 VAL A 28 24.481 -7.000 32.734 1.00 5.27 C
651	ATOM 207 CG2 VAL A 28 25.242 -7.950 34.956 1.00 8.92 C
652	ATOM 208 N ALA A 29 23.891 -9.973 30.848 1.00 5.00 N
653	ATOM 209 CA ALA A 29 23.813 -10.038 29.399 1.00 5.00 C
654	ATOM 210 C ALA A 29 23.194 -8.745 28.895 1.00 5.00 C
655	ATOM 211 O ALA A 29 22.291 -8.204 29.526 1.00 8.76 O
656	ATOM 212 CB ALA A 29 22.962 -11.223 28.944 1.00 5.00 C
657	ATOM 213 N VAL A 30 23.684 -8.246 27.766 1.00 5.07 N
658	ATOM 214 CA VAL A 30 23.145 -7.045 27.146 1.00 6.31 C
659	ATOM 215 C VAL A 30 22.600 -7.417 25.733 1.00 8.67 C
660	ATOM 216 O VAL A 30 23.373 -7.635 24.785 1.00 8.10 O
661	ATOM 217 CB VAL A 30 24.230 -5.895 27.058 1.00 10.70 C
662	ATOM 218 CG1 VAL A 30 23.611 -4.601 26.558 1.00 5.08 C
663	ATOM 219 CG2 VAL A 30 24.913 -5.666 28.424 1.00 10.72 C
664	ATOM 220 N LEU A 31 21.277 -7.567 25.612 1.00 11.61 N
665	ATOM 221 CA LEU A 31 20.657 -7.889 24.323 1.00 8.35 C
666	ATOM 222 C LEU A 31 20.575 -6.593 23.517 1.00 9.46 C
667	ATOM 223 O LEU A 31 19.679 -5.771 23.711 1.00 5.00 O
668	ATOM 224 CB LEU A 31 19.270 -8.480 24.530 1.00 5.00 C
669	ATOM 225 CG LEU A 31 19.138 -9.914 25.040 1.00 5.00 C
670	ATOM 226 CD1 LEU A 31 19.989 -10.140 26.259 1.00 5.00 C
671	ATOM 227 CD2 LEU A 31 17.671 -10.181 25.352 1.00 5.00 C
672	ATOM 228 N ASP A 32 21.492 -6.440 22.573 1.00 5.00 N
673	ATOM 229 CA ASP A 32 21.555 -5.218 21.804 1.00 5.00 C
674	ATOM 230 C ASP A 32 22.109 -5.410 20.391 1.00 5.00 C
675	ATOM 231 O ASP A 32 21.806 -6.399 19.740 1.00 7.68 O
676	ATOM 232 CB ASP A 32 22.412 -4.244 22.600 1.00 13.89 C
677	ATOM 233 CG ASP A 32 21.895 -2.840 22.551 1.00 16.40 C
678	ATOM 234 OD1 ASP A 32 22.227 -2.167 21.554 1.00 17.35 O
679	ATOM 235 OD2 ASP A 32 21.192 -2.416 23.508 1.00 20.84 O
680	ATOM 236 N THR A 33 22.913 -4.459 19.921 1.00 5.00 N
681	ATOM 237 CA THR A 33 23.508 -4.484 18.578 1.00 5.00 C
682	ATOM 238 C THR A 33 24.941 -5.035 18.541 1.00 5.00 C
683	ATOM 239 O THR A 33 25.617 -4.963 17.505 1.00 6.09 O
684	ATOM 240 CB THR A 33 23.535 -3.063 17.957 1.00 5.51 C
685	ATOM 241 OG1 THR A 33 24.356 -2.199 18.765 1.00 8.86 O
686	ATOM 242 CG2 THR A 33 22.125 -2.493 17.864 1.00 5.00 C
687	ATOM 243 N GLY A 34 25.382 -5.587 19.667 1.00 5.00 N
688	ATOM 244 CA GLY A 34 26.724 -6.129 19.787 1.00 5.00 C
689	ATOM 245 C GLY A 34 27.503 -5.254 20.757 1.00 5.00 C
690	ATOM 246 O GLY A 34 26.906 -4.378 21.377 1.00 8.37 O
691	ATOM 247 N ILE A 35 28.791 -5.540 20.957 1.00 6.93 N
692	ATOM 248 CA ILE A 35 29.639 -4.743 21.832 1.00 5.16 C
693	ATOM 249 C ILE A 35 31.049 -4.717 21.268 1.00 10.75 C
694	ATOM 250 O ILE A 35 31.636 -5.765 21.026 1.00 12.15 O
695	ATOM 251 CB ILE A 35 29.736 -5.296 23.276 1.00 5.00 C
696	ATOM 252 CG1 ILE A 35 28.355 -5.489 23.891 1.00 5.00 C
697	ATOM 253 CG2 ILE A 35 30.490 -4.296 24.175 1.00 5.00 C
698	ATOM 254 CD1 ILE A 35 28.380 -5.643 25.408 1.00 5.00 C
699	ATOM 255 N GLN A 36 31.588 -3.519 21.047 1.00 30.00 N
700	ATOM 256 CA GLN A 36 32.958 -3.343 20.540 1.00 30.48 C
701	ATOM 257 C GLN A 36 33.884 -3.888 21.655 1.00 31.53 C
702	ATOM 258 O GLN A 36 34.575 -3.124 22.342 1.00 14.07 O
703	ATOM 259 CB GLN A 36 33.224 -1.843 20.314 1.00 11.40 C
704	ATOM 260 CG GLN A 36 34.355 -1.524 19.324 1.00 11.71 C
705	ATOM 261 CD GLN A 36 35.483 -0.664 19.918 1.00 11.23 C
706	ATOM 262 OE1 GLN A 36 36.661 -0.924 19.675 1.00 12.49 O
707	ATOM 263 NE2 GLN A 36 35.125 0.359 20.692 1.00 10.57 N
708	ATOM 264 N ALA A 37 33.916 -5.209 21.810 1.00 19.19 N
709	ATOM 265 CA ALA A 37 34.692 -5.843 22.877 1.00 17.70 C
710	ATOM 266 C ALA A 37 36.155 -5.427 23.025 1.00 15.95 C
711	ATOM 267 O ALA A 37 36.726 -5.514 24.115 1.00 9.85 O
712	ATOM 268 CB ALA A 37 34.571 -7.342 22.773 1.00 15.30 C
713	ATOM 269 N SER A 38 36.748 -4.968 21.929 1.00 5.00 N
714	ATOM 270 CA SER A 38 38.132 -4.537 21.920 1.00 5.00 C
715	ATOM 271 C SER A 38 38.337 -3.167 22.537 1.00 5.00 C
716	ATOM 272 O SER A 38 39.469 -2.703 22.645 1.00 20.20 O
717	ATOM 273 CB SER A 38 38.671 -4.537 20.494 1.00 26.33 C
718	ATOM 274 OG SER A 38 37.772 -3.887 19.617 1.00 32.46 O
719	ATOM 275 N HIS A 39 37.238 -2.514 22.911 1.00 15.72 N
720	ATOM 276 CA HIS A 39 37.267 -1.193 23.525 1.00 9.33 C
721	ATOM 277 C HIS A 39 37.995 -1.351 24.867 1.00 10.94 C
722	ATOM 278 O HIS A 39 37.694 -2.269 25.635 1.00 10.13 O
723	ATOM 279 CB HIS A 39 35.832 -0.693 23.713 1.00 5.00 C
724	ATOM 280 CG HIS A 39 35.731 0.773 23.986 1.00 5.00 C
725	ATOM 281 ND1 HIS A 39 36.276 1.363 25.103 1.00 5.00 N
726	ATOM 282 CD2 HIS A 39 35.128 1.767 23.292 1.00 5.00 C
727	ATOM 283 CE1 HIS A 39 36.014 2.655 25.091 1.00 5.00 C
728	ATOM 284 NE2 HIS A 39 35.317 2.928 24.003 1.00 5.46 N
729	ATOM 285 N PRO A 40 38.985 -0.477 25.156 1.00 6.72 N
730	ATOM 286 CA PRO A 40 39.734 -0.573 26.413 1.00 5.00 C
731	ATOM 287 C PRO A 40 39.007 -0.344 27.721 1.00 5.00 C
732	ATOM 288 O PRO A 40 39.489 -0.729 28.770 1.00 10.89 O
733	ATOM 289 CB PRO A 40 40.907 0.369 26.196 1.00 8.31 C
734	ATOM 290 CG PRO A 40 40.361 1.377 25.215 1.00 12.99 C
735	ATOM 291 CD PRO A 40 39.620 0.498 24.253 1.00 11.26 C
736	ATOM 292 N ASP A 41 37.838 0.254 27.696 1.00 5.00 N
737	ATOM 293 CA ASP A 41 37.143 0.417 28.963 1.00 5.00 C
738	ATOM 294 C ASP A 41 36.074 -0.677 29.206 1.00 5.00 C
739	ATOM 295 O ASP A 41 35.379 -0.659 30.210 1.00 5.00 O
740	ATOM 296 CB ASP A 41 36.545 1.813 29.050 1.00 5.00 C
741	ATOM 297 CG ASP A 41 36.883 2.503 30.347 1.00 7.24 C
742	ATOM 298 OD1 ASP A 41 37.588 1.923 31.198 1.00 8.11 O
743	ATOM 299 OD2 ASP A 41 36.455 3.651 30.518 1.00 9.57 O
744	ATOM 300 N LEU A 42 36.008 -1.666 28.320 1.00 5.00 N
745	ATOM 301 CA LEU A 42 35.014 -2.732 28.403 1.00 5.00 C
746	ATOM 302 C LEU A 42 35.639 -4.114 28.442 1.00 5.00 C
747	ATOM 303 O LEU A 42 36.696 -4.355 27.874 1.00 7.89 O
748	ATOM 304 CB LEU A 42 34.042 -2.641 27.221 1.00 5.00 C
749	ATOM 305 CG LEU A 42 33.163 -1.389 27.235 1.00 5.87 C
750	ATOM 306 CD1 LEU A 42 32.757 -0.978 25.847 1.00 5.00 C
751	ATOM 307 CD2 LEU A 42 31.947 -1.643 28.110 1.00 5.00 C
752	ATOM 308 N ASN A 43 34.952 -5.032 29.096 1.00 13.46 N
753	ATOM 309 CA ASN A 43 35.435 -6.389 29.244 1.00 17.28 C
754	ATOM 310 C ASN A 43 34.260 -7.336 28.992 1.00 14.49 C
755	ATOM 311 O ASN A 43 33.484 -7.633 29.909 1.00 15.75 O
756	ATOM 312 CB ASN A 43 35.981 -6.559 30.670 1.00 29.89 C
757	ATOM 313 CG ASN A 43 36.755 -7.853 30.874 1.00 35.54 C
758	ATOM 314 OD1 ASN A 43 36.335 -8.931 30.451 1.00 41.05 O
759	ATOM 315 ND2 ASN A 43 37.864 -7.756 31.594 1.00 39.92 N
760	ATOM 316 N VAL A 44 34.082 -7.718 27.729 1.00 6.39 N
761	ATOM 317 CA VAL A 44 33.028 -8.655 27.334 1.00 8.29 C
762	ATOM 318 C VAL A 44 33.606 -10.074 27.468 1.00 8.34 C
763	ATOM 319 O VAL A 44 34.491 -10.477 26.717 1.00 8.40 O
764	ATOM 320 CB VAL A 44 32.547 -8.416 25.877 1.00 7.65 C
765	ATOM 321 CG1 VAL A 44 31.447 -9.385 25.514 1.00 5.00 C
766	ATOM 322 CG2 VAL A 44 32.050 -6.980 25.719 1.00 10.57 C
767	ATOM 323 N VAL A 45 33.128 -10.806 28.461 1.00 11.01 N
768	ATOM 324 CA VAL A 45 33.607 -12.149 28.709 1.00 13.65 C
769	ATOM 325 C VAL A 45 33.128 -13.147 27.648 1.00 16.39 C
770	ATOM 326 O VAL A 45 33.870 -14.060 27.245 1.00 18.39 O
771	ATOM 327 CB VAL A 45 33.200 -12.597 30.131 1.00 14.56 C
772	ATOM 328 CG1 VAL A 45 33.605 -14.056 30.380 1.00 13.39 C
773	ATOM 329 CG2 VAL A 45 33.863 -11.665 31.165 1.00 13.82 C
774	ATOM 330 N GLY A 46 31.912 -12.939 27.155 1.00 13.03 N
775	ATOM 331 CA GLY A 46 31.366 -13.832 26.151 1.00 7.52 C
776	ATOM 332 C GLY A 46 30.009 -13.371 25.674 1.00 5.00 C
777	ATOM 333 O GLY A 46 29.614 -12.247 25.945 1.00 6.50 O
778	ATOM 334 N GLY A 47 29.304 -14.240 24.960 1.00 7.08 N
779	ATOM 335 CA GLY A 47 27.995 -13.907 24.450 1.00 8.06 C
780	ATOM 336 C GLY A 47 27.626 -14.769 23.260 1.00 6.21 C
781	ATOM 337 O GLY A 47 28.281 -15.776 23.010 1.00 5.00 O
782	ATOM 338 N ALA A 48 26.574 -14.376 22.545 1.00 5.00 N
783	ATOM 339 CA ALA A 48 26.098 -15.097 21.372 1.00 5.00 C
784	ATOM 340 C ALA A 48 25.571 -14.119 20.324 1.00 5.00 C
785	ATOM 341 O ALA A 48 25.330 -12.957 20.617 1.00 5.00 O
786	ATOM 342 CB ALA A 48 25.019 -16.064 21.766 1.00 5.00 C
787	ATOM 343 N SER A 49 25.471 -14.555 19.081 1.00 5.00 N
788	ATOM 344 CA SER A 49 24.930 -13.672 18.063 1.00 5.00 C
789	ATOM 345 C SER A 49 23.787 -14.358 17.361 1.00 5.00 C
790	ATOM 346 O SER A 49 23.917 -15.505 16.925 1.00 5.00 O
791	ATOM 347 CB SER A 49 25.986 -13.249 17.050 1.00 5.00 C
792	ATOM 348 OG SER A 49 25.437 -12.283 16.170 1.00 5.00 O
793	ATOM 349 N PHE A 50 22.651 -13.677 17.305 1.00 5.78 N
794	ATOM 350 CA PHE A 50 21.444 -14.207 16.652 1.00 10.56 C
795	ATOM 351 C PHE A 50 21.037 -13.396 15.431 1.00 8.22 C
796	ATOM 352 O PHE A 50 19.887 -13.441 14.985 1.00 14.30 O
797	ATOM 353 CB PHE A 50 20.288 -14.308 17.664 1.00 6.81 C
798	ATOM 354 CG PHE A 50 20.559 -15.297 18.742 1.00 6.41 C
799	ATOM 355 CD1 PHE A 50 20.642 -16.654 18.438 1.00 6.44 C
800	ATOM 356 CD2 PHE A 50 20.868 -14.880 20.022 1.00 6.41 C
801	ATOM 357 CE1 PHE A 50 21.041 -17.578 19.388 1.00 6.41 C
802	ATOM 358 CE2 PHE A 50 21.270 -15.803 20.985 1.00 11.51 C
803	ATOM 359 CZ PHE A 50 21.359 -17.160 20.660 1.00 6.41 C
804	ATOM 360 N VAL A 51 21.986 -12.622 14.923 1.00 5.00 N
805	ATOM 361 CA VAL A 51 21.761 -11.798 13.754 1.00 5.00 C
806	ATOM 362 C VAL A 51 22.714 -12.384 12.738 1.00 5.00 C
807	ATOM 363 O VAL A 51 23.851 -12.686 13.064 1.00 8.41 O
808	ATOM 364 CB VAL A 51 22.124 -10.334 14.014 1.00 5.00 C
809	ATOM 365 CG1 VAL A 51 21.649 -9.479 12.876 1.00 5.00 C
810	ATOM 366 CG2 VAL A 51 21.497 -9.863 15.301 1.00 7.90 C
811	ATOM 367 N ALA A 52 22.243 -12.577 11.518 1.00 5.00 N
812	ATOM 368 CA ALA A 52 23.054 -13.159 10.472 1.00 5.00 C
813	ATOM 369 C ALA A 52 24.233 -12.315 10.079 1.00 5.00 C
814	ATOM 370 O ALA A 52 24.158 -11.107 10.129 1.00 14.31 O
815	ATOM 371 CB ALA A 52 22.205 -13.403 9.278 1.00 13.19 C
816	ATOM 372 N GLY A 53 25.323 -12.956 9.691 1.00 5.00 N
817	ATOM 373 CA GLY A 53 26.485 -12.218 9.236 1.00 5.00 C
818	ATOM 374 C GLY A 53 27.289 -11.404 10.232 1.00 5.00 C
819	ATOM 375 O GLY A 53 28.399 -10.968 9.911 1.00 5.00 O
820	ATOM 376 N GLU A 54 26.775 -11.216 11.441 1.00 9.52 N
821	ATOM 377 CA GLU A 54 27.497 -10.436 12.439 1.00 14.57 C
822	ATOM 378 C GLU A 54 27.870 -11.231 13.688 1.00 16.80 C
823	ATOM 379 O GLU A 54 27.019 -11.897 14.288 1.00 9.02 O
824	ATOM 380 CB GLU A 54 26.673 -9.208 12.858 1.00 10.86 C
825	ATOM 381 CG GLU A 54 26.336 -8.272 11.719 1.00 13.18 C
826	ATOM 382 CD GLU A 54 25.734 -6.989 12.198 1.00 12.82 C
827	ATOM 383 OE1 GLU A 54 26.314 -6.380 13.115 1.00 19.35 O
828	ATOM 384 OE2 GLU A 54 24.679 -6.589 11.669 1.00 16.53 O
829	ATOM 385 N ALA A 55 29.133 -11.127 14.098 1.00 5.00 N
830	ATOM 386 CA ALA A 55 29.583 -11.818 15.299 1.00 5.00 C
831	ATOM 387 C ALA A 55 28.967 -11.080 16.470 1.00 5.00 C
832	ATOM 388 O ALA A 55 28.370 -10.048 16.277 1.00 27.47 O
833	ATOM 389 CB ALA A 55 31.098 -11.774 15.393 1.00 32.25 C
834	ATOM 390 N TYR A 57 29.149 -11.563 17.689 1.00 8.93 N
835	ATOM 391 CA TYR A 57 28.569 -10.892 18.848 1.00 7.81 C
836	ATOM 392 C TYR A 57 29.509 -9.842 19.446 1.00 6.74 C
837	ATOM 393 O TYR A 57 29.102 -9.048 20.303 1.00 6.41 O
838	ATOM 394 CB TYR A 57 28.165 -11.915 19.925 1.00 6.71 C
839	ATOM 395 CG TYR A 57 29.340 -12.433 20.719 1.00 9.18 C
840	ATOM 396 CD1 TYR A 57 30.081 -13.544 20.282 1.00 7.81 C
841	ATOM 397 CD2 TYR A 57 29.766 -11.770 21.871 1.00 8.20 C
842	ATOM 398 CE1 TYR A 57 31.211 -13.966 20.973 1.00 6.31 C
843	ATOM 399 CE2 TYR A 57 30.896 -12.185 22.564 1.00 6.76 C
844	ATOM 400 CZ TYR A 57 31.610 -13.275 22.112 1.00 5.87 C
845	ATOM 401 OH TYR A 57 32.740 -13.649 22.793 1.00 12.50 O
846	ATOM 402 N ASN A 58 30.778 -9.862 19.043 1.00 5.00 N
847	ATOM 403 CA ASN A 58 31.719 -8.885 19.598 1.00 7.40 C
848	ATOM 404 C ASN A 58 32.166 -7.764 18.695 1.00 5.99 C
849	ATOM 405 O ASN A 58 33.337 -7.385 18.655 1.00 19.93 O
850	ATOM 406 CB ASN A 58 32.912 -9.524 20.340 1.00 21.04 C
851	ATOM 407 CG ASN A 58 33.677 -10.550 19.515 1.00 23.63 C
852	ATOM 408 OD1 ASN A 58 34.499 -11.277 20.073 1.00 25.83 O
853	ATOM 409 ND2 ASN A 58 33.423 -10.621 18.201 1.00 22.36 N
854	ATOM 410 N THR A 59 31.189 -7.205 18.001 1.00 11.16 N
855	ATOM 411 CA THR A 59 31.385 -6.079 17.121 1.00 5.96 C
856	ATOM 412 C THR A 59 30.115 -5.289 17.267 1.00 5.00 C
857	ATOM 413 O THR A 59 29.053 -5.847 17.499 1.00 5.00 O
858	ATOM 414 CB THR A 59 31.548 -6.481 15.668 1.00 5.00 C
859	ATOM 415 OG1 THR A 59 30.456 -7.317 15.279 1.00 9.69 O
860	ATOM 416 CG2 THR A 59 32.848 -7.190 15.456 1.00 5.00 C
861	ATOM 417 N ASP A 60 30.237 -3.982 17.150 1.00 11.09 N
862	ATOM 418 CA ASP A 60 29.093 -3.108 17.256 1.00 12.98 C
863	ATOM 419 C ASP A 60 29.081 -2.249 16.019 1.00 18.08 C
864	ATOM 420 O ASP A 60 29.810 -1.252 15.946 1.00 9.38 O
865	ATOM 421 CB ASP A 60 29.223 -2.207 18.465 1.00 5.15 C
866	ATOM 422 CG ASP A 60 27.940 -1.596 18.854 1.00 5.00 C
867	ATOM 423 OD1 ASP A 60 26.968 -1.607 18.088 1.00 5.00 O
868	ATOM 424 OD2 ASP A 60 27.893 -1.108 19.963 1.00 5.00 O
869	ATOM 425 N GLY A 61 28.270 -2.650 15.040 1.00 26.84 N
870	ATOM 426 CA GLY A 61 28.171 -1.888 13.807 1.00 24.67 C
871	ATOM 427 C GLY A 61 27.370 -0.599 13.937 1.00 24.97 C
872	ATOM 428 O GLY A 61 27.535 0.311 13.117 1.00 29.94 O
873	ATOM 429 N ASN A 62 26.512 -0.525 14.959 1.00 13.46 N
874	ATOM 430 CA ASN A 62 25.657 0.636 15.211 1.00 12.46 C
875	ATOM 431 C ASN A 62 26.218 1.634 16.260 1.00 9.59 C
876	ATOM 432 O ASN A 62 26.247 2.845 16.026 1.00 11.61 O
877	ATOM 433 CB ASN A 62 24.260 0.144 15.627 1.00 17.52 C
878	ATOM 434 CG ASN A 62 23.249 1.266 15.769 1.00 14.87 C
879	ATOM 435 OD1 ASN A 62 22.250 1.291 15.066 1.00 18.81 O
880	ATOM 436 ND2 ASN A 62 23.482 2.177 16.706 1.00 16.26 N
881	ATOM 437 N GLY A 63 26.617 1.135 17.425 1.00 5.00 N
882	ATOM 438 CA GLY A 63 27.136 2.011 18.464 1.00 5.00 C
883	ATOM 439 C GLY A 63 26.285 1.938 19.719 1.00 5.00 C
884	ATOM 440 O GLY A 63 26.774 2.037 20.846 1.00 9.50 O
885	ATOM 441 N HIS A 64 24.993 1.727 19.516 1.00 5.00 N
886	ATOM 442 CA HIS A 64 24.045 1.626 20.605 1.00 5.00 C
887	ATOM 443 C HIS A 64 24.502 0.581 21.645 1.00 5.00 C
888	ATOM 444 O HIS A 64 24.520 0.874 22.835 1.00 10.02 O
889	ATOM 445 CB HIS A 64 22.659 1.289 20.014 1.00 5.00 C
890	ATOM 446 CG HIS A 64 21.538 1.316 21.009 1.00 6.06 C
891	ATOM 447 ND1 HIS A 64 21.017 0.174 21.577 1.00 10.24 N
892	ATOM 448 CD2 HIS A 64 20.816 2.340 21.514 1.00 7.31 C
893	ATOM 449 CE1 HIS A 64 20.029 0.488 22.392 1.00 5.22 C
894	ATOM 450 NE2 HIS A 64 19.883 1.797 22.368 1.00 6.31 N
895	ATOM 451 N GLY A 65 24.941 -0.596 21.190 1.00 5.00 N
896	ATOM 452 CA GLY A 65 25.355 -1.651 22.104 1.00 5.00 C
897	ATOM 453 C GLY A 65 26.509 -1.356 23.048 1.00 5.00 C
898	ATOM 454 O GLY A 65 26.436 -1.617 24.239 1.00 5.00 O
899	ATOM 455 N THR A 66 27.582 -0.798 22.519 1.00 5.00 N
900	ATOM 456 CA THR A 66 28.745 -0.478 23.315 1.00 5.00 C
901	ATOM 457 C THR A 66 28.345 0.605 24.310 1.00 5.00 C
902	ATOM 458 O THR A 66 28.719 0.532 25.466 1.00 9.77 O
903	ATOM 459 CB THR A 66 29.903 -0.007 22.419 1.00 8.49 C
904	ATOM 460 OG1 THR A 66 30.032 -0.905 21.312 1.00 12.69 O
905	ATOM 461 CG2 THR A 66 31.203 -0.033 23.170 1.00 8.15 C
906	ATOM 462 N HIS A 67 27.534 1.568 23.877 1.00 5.00 N
907	ATOM 463 CA HIS A 67 27.065 2.642 24.759 1.00 5.00 C
908	ATOM 464 C HIS A 67 26.355 2.103 26.004 1.00 5.00 C
909	ATOM 465 O HIS A 67 26.698 2.469 27.127 1.00 9.09 O
910	ATOM 466 CB HIS A 67 26.133 3.600 24.008 1.00 6.92 C
911	ATOM 467 CG HIS A 67 26.192 5.004 24.521 1.00 5.28 C
912	ATOM 468 ND1 HIS A 67 25.605 5.386 25.710 1.00 5.00 N
913	ATOM 469 CD2 HIS A 67 26.889 6.079 24.083 1.00 5.00 C
914	ATOM 470 CE1 HIS A 67 25.953 6.627 25.989 1.00 6.87 C
915	ATOM 471 NE2 HIS A 67 26.733 7.069 25.019 1.00 5.00 N
916	ATOM 472 N VAL A 68 25.356 1.250 25.792 1.00 5.00 N
917	ATOM 473 CA VAL A 68 24.572 0.623 26.865 1.00 5.00 C
918	ATOM 474 C VAL A 68 25.432 -0.318 27.736 1.00 5.00 C
919	ATOM 475 O VAL A 68 25.200 -0.453 28.941 1.00 5.00 O
920	ATOM 476 CB VAL A 68 23.373 -0.160 26.256 1.00 5.00 C
921	ATOM 477 CG1 VAL A 68 22.472 -0.772 27.339 1.00 5.00 C
922	ATOM 478 CG2 VAL A 68 22.605 0.748 25.367 1.00 5.00 C
923	ATOM 479 N ALA A 69 26.409 -0.987 27.134 1.00 5.00 N
924	ATOM 480 CA ALA A 69 27.270 -1.863 27.915 1.00 5.00 C
925	ATOM 481 C ALA A 69 28.052 -0.965 28.840 1.00 5.00 C
926	ATOM 482 O ALA A 69 28.070 -1.165 30.043 1.00 8.24 O
927	ATOM 483 CB ALA A 69 28.195 -2.611 27.026 1.00 5.00 C
928	ATOM 484 N GLY A 70 28.603 0.093 28.262 1.00 10.77 N
929	ATOM 485 CA GLY A 70 29.386 1.070 28.997 1.00 14.56 C
930	ATOM 486 C GLY A 70 28.704 1.633 30.225 1.00 15.17 C
931	ATOM 487 O GLY A 70 29.355 1.857 31.248 1.00 19.75 O
932	ATOM 488 N THR A 71 27.411 1.903 30.129 1.00 6.20 N
933	ATOM 489 CA THR A 71 26.702 2.418 31.284 1.00 8.43 C
934	ATOM 490 C THR A 71 26.711 1.385 32.419 1.00 9.80 C
935	ATOM 491 O THR A 71 26.931 1.745 33.587 1.00 10.39 O
936	ATOM 492 CB THR A 71 25.254 2.788 30.943 1.00 8.24 C
937	ATOM 493 OG1 THR A 71 25.253 3.898 30.037 1.00 9.10 O
938	ATOM 494 CG2 THR A 71 24.476 3.141 32.214 1.00 5.69 C
939	ATOM 495 N VAL A 72 26.523 0.107 32.077 1.00 5.59 N
940	ATOM 496 CA VAL A 72 26.505 -0.928 33.096 1.00 5.00 C
941	ATOM 497 C VAL A 72 27.840 -1.268 33.698 1.00 7.11 C
942	ATOM 498 O VAL A 72 27.958 -1.292 34.931 1.00 6.85 O
943	ATOM 499 CB VAL A 72 25.948 -2.259 32.616 1.00 5.50 C
944	ATOM 500 CG1 VAL A 72 25.941 -3.246 33.787 1.00 5.00 C
945	ATOM 501 CG2 VAL A 72 24.557 -2.086 32.048 1.00 7.48 C
946	ATOM 502 N ALA A 73 28.838 -1.536 32.852 1.00 7.67 N
947	ATOM 503 CA ALA A 73 30.140 -1.953 33.364 1.00 8.77 C
948	ATOM 504 C ALA A 73 31.434 -1.419 32.781 1.00 10.89 C
949	ATOM 505 O ALA A 73 32.436 -2.155 32.781 1.00 15.46 O
950	ATOM 506 CB ALA A 73 30.211 -3.470 33.362 1.00 19.18 C
951	ATOM 507 N ALA A 74 31.464 -0.189 32.274 1.00 5.00 N
952	ATOM 508 CA ALA A 74 32.735 0.289 31.760 1.00 5.00 C
953	ATOM 509 C ALA A 74 33.727 0.251 32.952 1.00 5.00 C
954	ATOM 510 O ALA A 74 33.417 0.676 34.075 1.00 5.00 O
955	ATOM 511 CB ALA A 74 32.609 1.673 31.161 1.00 5.00 C
956	ATOM 512 N LEU A 75 34.834 -0.434 32.720 1.00 5.00 N
957	ATOM 513 CA LEU A 75 35.909 -0.639 33.666 1.00 5.00 C
958	ATOM 514 C LEU A 75 36.322 0.522 34.545 1.00 5.00 C
959	ATOM 515 O LEU A 75 36.658 1.602 34.061 1.00 5.55 O
960	ATOM 516 CB LEU A 75 37.142 -1.121 32.905 1.00 5.00 C
961	ATOM 517 CG LEU A 75 36.980 -2.399 32.085 1.00 5.00 C
962	ATOM 518 CD1 LEU A 75 38.181 -2.590 31.213 1.00 5.00 C
963	ATOM 519 CD2 LEU A 75 36.772 -3.593 32.993 1.00 5.00 C
964	ATOM 520 N ASP A 76 36.370 0.260 35.845 1.00 5.00 N
965	ATOM 521 CA ASP A 76 36.793 1.249 36.834 1.00 5.00 C
966	ATOM 522 C ASP A 76 38.310 1.312 36.736 1.00 5.00 C
967	ATOM 523 O ASP A 76 39.000 0.404 37.203 1.00 5.00 O
968	ATOM 524 CB ASP A 76 36.399 0.780 38.236 1.00 5.00 C
969	ATOM 525 CG ASP A 76 36.752 1.782 39.331 1.00 9.25 C
970	ATOM 526 OD1 ASP A 76 37.622 2.649 39.152 1.00 8.72 O
971	ATOM 527 OD2 ASP A 76 36.144 1.693 40.412 1.00 18.39 O
972	ATOM 528 N ASN A 77 38.821 2.360 36.098 1.00 5.00 N
973	ATOM 529 CA ASN A 77 40.269 2.548 35.924 1.00 5.00 C
974	ATOM 530 C ASN A 77 40.618 4.035 35.810 1.00 5.00 C
975	ATOM 531 O ASN A 77 39.978 4.867 36.443 1.00 5.00 O
976	ATOM 532 CB ASN A 77 40.820 1.723 34.728 1.00 5.00 C
977	ATOM 533 CG ASN A 77 40.028 1.928 33.429 1.00 5.00 C
978	ATOM 534 OD1 ASN A 77 39.418 2.976 33.213 1.00 5.00 O
979	ATOM 535 ND2 ASN A 77 40.065 0.935 32.553 1.00 5.00 N
980	ATOM 536 N THR A 78 41.615 4.367 34.997 1.00 12.18 N
981	ATOM 537 CA THR A 78 42.077 5.755 34.824 1.00 12.48 C
982	ATOM 538 C THR A 78 41.850 6.226 33.379 1.00 14.37 C
983	ATOM 539 O THR A 78 42.548 7.086 32.853 1.00 5.22 O
984	ATOM 540 CB THR A 78 43.578 5.834 35.179 1.00 11.37 C
985	ATOM 541 OG1 THR A 78 44.092 7.147 34.919 1.00 18.40 O
986	ATOM 542 CG2 THR A 78 44.352 4.800 34.373 1.00 12.95 C
987	ATOM 543 N THR A 79 40.845 5.660 32.737 1.00 8.22 N
988	ATOM 544 CA THR A 79 40.562 6.027 31.380 1.00 5.16 C
989	ATOM 545 C THR A 79 39.067 5.932 31.209 1.00 5.86 C
990	ATOM 546 O THR A 79 38.363 5.473 32.121 1.00 8.13 O
991	ATOM 547 CB THR A 79 41.279 5.090 30.398 1.00 13.43 C
992	ATOM 548 OG1 THR A 79 40.823 5.349 29.066 1.00 19.64 O
993	ATOM 549 CG2 THR A 79 41.006 3.615 30.738 1.00 17.54 C
994	ATOM 550 N GLY A 80 38.606 6.458 30.073 1.00 9.49 N
995	ATOM 551 CA GLY A 80 37.209 6.462 29.698 1.00 5.34 C
996	ATOM 552 C GLY A 80 36.231 6.981 30.720 1.00 5.33 C
997	ATOM 553 O GLY A 80 36.410 8.042 31.302 1.00 8.99 O
998	ATOM 554 N VAL A 81 35.166 6.218 30.898 1.00 5.00 N
999	ATOM 555 CA VAL A 81 34.097 6.526 31.826 1.00 5.00 C
1000	ATOM 556 C VAL A 81 34.138 5.458 32.924 1.00 5.00 C
1001	ATOM 557 O VAL A 81 35.123 4.722 33.039 1.00 5.00 O
1002	ATOM 558 CB VAL A 81 32.713 6.562 31.085 1.00 5.00 C
1003	ATOM 559 CG1 VAL A 81 32.760 7.542 29.945 1.00 5.00 C
1004	ATOM 560 CG2 VAL A 81 32.341 5.213 30.534 1.00 5.00 C
1005	ATOM 561 N LEU A 82 33.092 5.383 33.735 1.00 5.00 N
1006	ATOM 562 CA LEU A 82 33.025 4.421 34.817 1.00 5.00 C
1007	ATOM 563 C LEU A 82 31.621 3.888 34.817 1.00 5.00 C
1008	ATOM 564 O LEU A 82 30.684 4.652 34.627 1.00 13.85 O
1009	ATOM 565 CB LEU A 82 33.313 5.109 36.142 1.00 5.25 C
1010	ATOM 566 CG LEU A 82 32.856 4.452 37.439 1.00 5.25 C
1011	ATOM 567 CD1 LEU A 82 33.367 3.041 37.591 1.00 5.34 C
1012	ATOM 568 CD2 LEU A 82 33.358 5.295 38.561 1.00 8.59 C
1013	ATOM 569 N GLY A 83 31.468 2.588 35.019 1.00 5.00 N
1014	ATOM 570 CA GLY A 83 30.144 2.016 35.009 1.00 5.00 C
1015	ATOM 571 C GLY A 83 29.494 1.905 36.365 1.00 5.00 C
1016	ATOM 572 O GLY A 83 30.145 1.974 37.400 1.00 5.00 O
1017	ATOM 573 N VAL A 84 28.185 1.702 36.342 1.00 5.08 N
1018	ATOM 574 CA VAL A 84 27.398 1.535 37.551 1.00 7.72 C
1019	ATOM 575 C VAL A 84 27.943 0.355 38.390 1.00 12.00 C
1020	ATOM 576 O VAL A 84 28.178 0.497 39.591 1.00 16.86 O
1021	ATOM 577 CB VAL A 84 25.906 1.361 37.183 1.00 5.00 C
1022	ATOM 578 CG1 VAL A 84 25.067 1.126 38.412 1.00 5.00 C
1023	ATOM 579 CG2 VAL A 84 25.425 2.620 36.447 1.00 5.00 C
1024	ATOM 580 N ALA A 85 28.184 -0.790 37.757 1.00 5.00 N
1025	ATOM 581 CA ALA A 85 28.728 -1.962 38.442 1.00 5.00 C
1026	ATOM 582 C ALA A 85 29.963 -2.389 37.643 1.00 5.00 C
1027	ATOM 583 O ALA A 85 29.941 -3.404 36.964 1.00 5.00 O
1028	ATOM 584 CB ALA A 85 27.688 -3.066 38.447 1.00 16.36 C
1029	ATOM 585 N PRO A 86 31.092 -1.671 37.811 1.00 23.65 N
1030	ATOM 586 CA PRO A 86 32.346 -1.939 37.097 1.00 20.91 C
1031	ATOM 587 C PRO A 86 33.015 -3.324 37.154 1.00 24.63 C
1032	ATOM 588 O PRO A 86 33.904 -3.599 36.340 1.00 11.44 O
1033	ATOM 589 CB PRO A 86 33.250 -0.820 37.592 1.00 5.84 C
1034	ATOM 590 CG PRO A 86 32.823 -0.672 39.002 1.00 9.76 C
1035	ATOM 591 CD PRO A 86 31.317 -0.684 38.889 1.00 9.19 C
1036	ATOM 592 N SER A 87 32.600 -4.199 38.076 1.00 18.00 N
1037	ATOM 593 CA SER A 87 33.196 -5.550 38.170 1.00 13.27 C
1038	ATOM 594 C SER A 87 32.285 -6.699 37.705 1.00 11.94 C
1039	ATOM 595 O SER A 87 32.604 -7.878 37.885 1.00 18.18 O
1040	ATOM 596 CB SER A 87 33.702 -5.829 39.582 1.00 14.17 C
1041	ATOM 597 OG SER A 87 34.685 -4.890 39.960 1.00 18.24 O
1042	ATOM 598 N VAL A 88 31.152 -6.346 37.110 1.00 8.13 N
1043	ATOM 599 CA VAL A 88 30.195 -7.305 36.594 1.00 5.00 C
1044	ATOM 600 C VAL A 88 30.814 -8.146 35.469 1.00 6.58 C
1045	ATOM 601 O VAL A 88 31.841 -7.775 34.911 1.00 8.16 O
1046	ATOM 602 CB VAL A 88 28.946 -6.555 36.070 1.00 5.00 C
1047	ATOM 603 CG1 VAL A 88 28.948 -6.445 34.532 1.00 5.00 C
1048	ATOM 604 CG2 VAL A 88 27.687 -7.212 36.613 1.00 5.80 C
1049	ATOM 605 N SER A 89 30.204 -9.291 35.167 1.00 8.99 N
1050	ATOM 606 CA SER A 89 30.654 -10.172 34.086 1.00 8.95 C
1051	ATOM 607 C SER A 89 29.780 -9.820 32.885 1.00 7.86 C
1052	ATOM 608 O SER A 89 28.618 -10.207 32.829 1.00 5.20 O
1053	ATOM 609 CB SER A 89 30.442 -11.636 34.469 1.00 10.15 C
1054	ATOM 610 OG SER A 89 31.054 -11.905 35.712 1.00 15.72 O
1055	ATOM 611 N LEU A 90 30.338 -9.095 31.923 1.00 7.19 N
1056	ATOM 612 CA LEU A 90 29.564 -8.646 30.776 1.00 5.24 C
1057	ATOM 613 C LEU A 90 29.396 -9.664 29.682 1.00 5.00 C
1058	ATOM 614 O LEU A 90 30.357 -10.278 29.250 1.00 5.35 O
1059	ATOM 615 CB LEU A 90 30.189 -7.381 30.202 1.00 7.44 C
1060	ATOM 616 CG LEU A 90 29.361 -6.522 29.253 1.00 6.76 C
1061	ATOM 617 CD1 LEU A 90 28.196 -5.959 30.038 1.00 8.43 C
1062	ATOM 618 CD2 LEU A 90 30.213 -5.420 28.688 1.00 5.00 C
1063	ATOM 619 N TYR A 91 28.174 -9.782 29.188 1.00 5.00 N
1064	ATOM 620 CA TYR A 91 27.856 -10.713 28.115 1.00 5.00 C
1065	ATOM 621 C TYR A 91 27.131 -9.969 27.006 1.00 5.00 C
1066	ATOM 622 O TYR A 91 26.204 -9.207 27.241 1.00 5.00 O
1067	ATOM 623 CB TYR A 91 27.019 -11.907 28.625 1.00 5.00 C
1068	ATOM 624 CG TYR A 91 27.802 -12.863 29.510 1.00 5.00 C
1069	ATOM 625 CD1 TYR A 91 28.019 -12.594 30.860 1.00 5.00 C
1070	ATOM 626 CD2 TYR A 91 28.338 -14.039 28.986 1.00 8.70 C
1071	ATOM 627 CE1 TYR A 91 28.755 -13.486 31.671 1.00 7.32 C
1072	ATOM 628 CE2 TYR A 91 29.072 -14.934 29.771 1.00 7.65 C
1073	ATOM 629 CZ TYR A 91 29.279 -14.661 31.108 1.00 11.69 C
1074	ATOM 630 OH TYR A 91 30.004 -15.569 31.865 1.00 9.64 O
1075	ATOM 631 N ALA A 92 27.650 -10.141 25.804 1.00 5.00 N
1076	ATOM 632 CA ALA A 92 27.134 -9.522 24.609 1.00 5.00 C
1077	ATOM 633 C ALA A 92 26.220 -10.518 23.898 1.00 5.00 C
1078	ATOM 634 O ALA A 92 26.636 -11.585 23.462 1.00 5.00 O
1079	ATOM 635 CB ALA A 92 28.289 -9.111 23.721 1.00 5.00 C
1080	ATOM 636 N VAL A 93 24.946 -10.178 23.839 1.00 9.92 N
1081	ATOM 637 CA VAL A 93 23.968 -11.025 23.201 1.00 5.45 C
1082	ATOM 638 C VAL A 93 23.379 -10.160 22.084 1.00 5.45 C
1083	ATOM 639 O VAL A 93 22.497 -9.343 22.316 1.00 5.00 O
1084	ATOM 640 CB VAL A 93 22.943 -11.485 24.263 1.00 5.00 C
1085	ATOM 641 CG1 VAL A 93 21.736 -12.078 23.623 1.00 7.16 C
1086	ATOM 642 CG2 VAL A 93 23.575 -12.502 25.184 1.00 5.00 C
1087	ATOM 643 N LYS A 94 23.940 -10.297 20.884 1.00 5.00 N
1088	ATOM 644 CA LYS A 94 23.538 -9.513 19.709 1.00 5.00 C
1089	ATOM 645 C LYS A 94 22.214 -9.950 19.122 1.00 5.00 C
1090	ATOM 646 O LYS A 94 22.105 -11.023 18.545 1.00 5.00 O
1091	ATOM 647 CB LYS A 94 24.627 -9.557 18.625 1.00 5.00 C
1092	ATOM 648 CG LYS A 94 24.285 -8.789 17.361 1.00 5.00 C
1093	ATOM 649 CD LYS A 94 25.400 -8.807 16.315 1.00 5.00 C
1094	ATOM 650 CE LYS A 94 26.507 -7.790 16.622 1.00 5.00 C
1095	ATOM 651 NZ LYS A 94 27.374 -7.511 15.435 1.00 5.00 N
1096	ATOM 652 N VAL A 95 21.227 -9.069 19.213 1.00 10.36 N
1097	ATOM 653 CA VAL A 95 19.889 -9.358 18.721 1.00 7.97 C
1098	ATOM 654 C VAL A 95 19.355 -8.295 17.776 1.00 7.71 C
1099	ATOM 655 O VAL A 95 18.350 -8.491 17.110 1.00 5.00 O
1100	ATOM 656 CB VAL A 95 18.944 -9.528 19.890 1.00 5.00 C
1101	ATOM 657 CG1 VAL A 95 19.205 -10.865 20.568 1.00 5.00 C
1102	ATOM 658 CG2 VAL A 95 19.159 -8.410 20.865 1.00 5.00 C
1103	ATOM 659 N LEU A 96 20.022 -7.152 17.745 1.00 15.78 N
1104	ATOM 660 CA LEU A 96 19.638 -6.055 16.872 1.00 11.78 C
1105	ATOM 661 C LEU A 96 20.824 -5.938 15.931 1.00 12.76 C
1106	ATOM 662 O LEU A 96 21.964 -6.250 16.296 1.00 5.00 O
1107	ATOM 663 CB LEU A 96 19.454 -4.756 17.660 1.00 5.00 C
1108	ATOM 664 CG LEU A 96 18.568 -4.756 18.902 1.00 5.00 C
1109	ATOM 665 CD1 LEU A 96 18.693 -3.405 19.532 1.00 5.00 C
1110	ATOM 666 CD2 LEU A 96 17.119 -5.051 18.590 1.00 5.00 C
1111	ATOM 667 N ASN A 97 20.542 -5.624 14.685 1.00 5.00 N
1112	ATOM 668 CA ASN A 97 21.606 -5.497 13.727 1.00 6.96 C
1113	ATOM 669 C ASN A 97 22.099 -4.063 13.812 1.00 9.72 C
1114	ATOM 670 O ASN A 97 21.624 -3.291 14.656 1.00 7.29 O
1115	ATOM 671 CB ASN A 97 21.099 -5.839 12.333 1.00 5.15 C
1116	ATOM 672 CG ASN A 97 19.930 -4.970 11.897 1.00 12.13 C
1117	ATOM 673 OD1 ASN A 97 19.443 -5.113 10.784 1.00 17.50 O
1118	ATOM 674 ND2 ASN A 97 19.493 -4.050 12.750 1.00 14.04 N
1119	ATOM 675 N SER A 98 22.983 -3.698 12.890 1.00 21.41 N
1120	ATOM 676 CA SER A 98 23.567 -2.363 12.830 1.00 22.74 C
1121	ATOM 677 C SER A 98 22.608 -1.190 12.520 1.00 22.27 C
1122	ATOM 678 O SER A 98 23.048 -0.028 12.456 1.00 15.66 O
1123	ATOM 679 CB SER A 98 24.758 -2.370 11.864 1.00 11.03 C
1124	ATOM 680 OG SER A 98 24.384 -2.899 10.602 1.00 13.26 O
1125	ATOM 681 N SER A 99 21.332 -1.493 12.263 1.00 7.22 N
1126	ATOM 682 CA SER A 99 20.327 -0.443 12.011 1.00 8.05 C
1127	ATOM 683 C SER A 99 19.506 -0.278 13.273 1.00 9.26 C
1128	ATOM 684 O SER A 99 18.665 0.625 13.389 1.00 11.95 O
1129	ATOM 685 CB SER A 99 19.387 -0.806 10.866 1.00 5.00 C
1130	ATOM 686 OG SER A 99 19.965 -0.475 9.624 1.00 7.66 O
1131	ATOM 687 N GLY A 100 19.738 -1.190 14.209 1.00 9.66 N
1132	ATOM 688 CA GLY A 100 19.040 -1.149 15.472 1.00 10.03 C
1133	ATOM 689 C GLY A 100 17.728 -1.855 15.342 1.00 5.22 C
1134	ATOM 690 O GLY A 100 16.794 -1.566 16.080 1.00 5.00 O
1135	ATOM 691 N SER A 101 17.671 -2.813 14.429 1.00 5.00 N
1136	ATOM 692 CA SER A 101 16.444 -3.566 14.214 1.00 11.83 C
1137	ATOM 693 C SER A 101 16.715 -5.048 14.372 1.00 8.45 C
1138	ATOM 694 O SER A 101 17.827 -5.504 14.136 1.00 21.28 O
1139	ATOM 695 CB SER A 101 15.869 -3.262 12.826 1.00 24.36 C
1140	ATOM 696 OG SER A 101 14.555 -3.776 12.688 1.00 29.43 O
1141	ATOM 697 N GLY A 102 15.710 -5.781 14.831 1.00 20.46 N
1142	ATOM 698 CA GLY A 102 15.835 -7.220 15.019 1.00 25.14 C
1143	ATOM 699 C GLY A 102 14.447 -7.835 14.920 1.00 25.69 C
1144	ATOM 700 O GLY A 102 13.453 -7.098 14.918 1.00 28.63 O
1145	ATOM 701 N SER A 103 14.362 -9.162 14.837 1.00 17.11 N
1146	ATOM 702 CA SER A 103 13.071 -9.858 14.730 1.00 13.11 C
1147	ATOM 703 C SER A 103 12.630 -10.436 16.063 1.00 11.30 C
1148	ATOM 704 O SER A 103 13.451 -10.609 16.975 1.00 15.04 O
1149	ATOM 705 CB SER A 103 13.141 -10.966 13.670 1.00 25.33 C
1150	ATOM 706 OG SER A 103 14.233 -11.856 13.899 1.00 32.62 O
1151	ATOM 707 N TYR A 104 11.344 -10.747 16.189 1.00 17.02 N
1152	ATOM 708 CA TYR A 104 10.875 -11.303 17.443 1.00 18.20 C
1153	ATOM 709 C TYR A 104 11.649 -12.545 17.823 1.00 19.55 C
1154	ATOM 710 O TYR A 104 11.898 -12.775 19.010 1.00 29.18 O
1155	ATOM 711 CB TYR A 104 9.371 -11.541 17.441 1.00 35.12 C
1156	ATOM 712 CG TYR A 104 8.649 -10.298 17.883 1.00 36.18 C
1157	ATOM 713 CD1 TYR A 104 8.376 -9.295 16.969 1.00 39.33 C
1158	ATOM 714 CD2 TYR A 104 8.407 -10.045 19.231 1.00 36.73 C
1159	ATOM 715 CE1 TYR A 104 7.909 -8.066 17.370 1.00 39.80 C
1160	ATOM 716 CE2 TYR A 104 7.936 -8.808 19.648 1.00 41.73 C
1161	ATOM 717 CZ TYR A 104 7.700 -7.812 18.704 1.00 41.83 C
1162	ATOM 718 OH TYR A 104 7.344 -6.526 19.068 1.00 42.25 O
1163	ATOM 719 N SER A 105 12.112 -13.294 16.823 1.00 10.50 N
1164	ATOM 720 CA SER A 105 12.892 -14.496 17.100 1.00 9.82 C
1165	ATOM 721 C SER A 105 14.354 -14.252 17.484 1.00 10.54 C
1166	ATOM 722 O SER A 105 14.951 -15.039 18.214 1.00 9.23 O
1167	ATOM 723 CB SER A 105 12.794 -15.469 15.951 1.00 12.55 C
1168	ATOM 724 OG SER A 105 11.606 -16.220 16.111 1.00 24.18 O
1169	ATOM 725 N GLY A 106 14.941 -13.173 16.989 1.00 10.77 N
1170	ATOM 726 CA GLY A 106 16.304 -12.899 17.375 1.00 12.20 C
1171	ATOM 727 C GLY A 106 16.241 -12.618 18.866 1.00 10.63 C
1172	ATOM 728 O GLY A 106 16.878 -13.309 19.663 1.00 16.91 O
1173	ATOM 729 N ILE A 107 15.389 -11.663 19.238 1.00 5.00 N
1174	ATOM 730 CA ILE A 107 15.206 -11.255 20.627 1.00 5.00 C
1175	ATOM 731 C ILE A 107 14.809 -12.407 21.540 1.00 5.00 C
1176	ATOM 732 O ILE A 107 15.407 -12.596 22.603 1.00 5.00 O
1177	ATOM 733 CB ILE A 107 14.169 -10.111 20.747 1.00 9.38 C
1178	ATOM 734 CG1 ILE A 107 14.604 -8.925 19.876 1.00 7.68 C
1179	ATOM 735 CG2 ILE A 107 14.063 -9.648 22.188 1.00 13.84 C
1180	ATOM 736 CD1 ILE A 107 13.648 -7.753 19.864 1.00 5.06 C
1181	ATOM 737 N VAL A 108 13.821 -13.193 21.124 1.00 6.17 N
1182	ATOM 738 CA VAL A 108 13.380 -14.328 21.931 1.00 5.00 C
1183	ATOM 739 C VAL A 108 14.550 -15.320 22.126 1.00 5.96 C
1184	ATOM 740 O VAL A 108 14.844 -15.742 23.256 1.00 5.11 O
1185	ATOM 741 CB VAL A 108 12.115 -14.981 21.319 1.00 5.00 C
1186	ATOM 742 CG1 VAL A 108 11.720 -16.228 22.087 1.00 6.82 C
1187	ATOM 743 CG2 VAL A 108 10.939 -13.991 21.365 1.00 5.00 C
1188	ATOM 744 N SER A 109 15.276 -15.609 21.045 1.00 15.85 N
1189	ATOM 745 CA SER A 109 16.436 -16.504 21.103 1.00 12.60 C
1190	ATOM 746 C SER A 109 17.492 -15.966 22.052 1.00 12.62 C
1191	ATOM 747 O SER A 109 18.101 -16.737 22.798 1.00 7.69 O
1192	ATOM 748 CB SER A 109 17.046 -16.704 19.721 1.00 5.00 C
1193	ATOM 749 OG SER A 109 16.144 -17.411 18.894 1.00 8.64 O
1194	ATOM 750 N GLY A 110 17.677 -14.644 22.035 1.00 5.00 N
1195	ATOM 751 CA GLY A 110 18.642 -13.990 22.911 1.00 5.00 C
1196	ATOM 752 C GLY A 110 18.299 -14.107 24.391 1.00 5.00 C
1197	ATOM 753 O GLY A 110 19.187 -14.259 25.227 1.00 8.90 O
1198	ATOM 754 N ILE A 111 17.012 -14.018 24.723 1.00 6.55 N
1199	ATOM 755 CA ILE A 111 16.559 -14.150 26.101 1.00 5.84 C
1200	ATOM 756 C ILE A 111 16.692 -15.620 26.524 1.00 8.74 C
1201	ATOM 757 O ILE A 111 17.196 -15.940 27.610 1.00 5.00 O
1202	ATOM 758 CB ILE A 111 15.085 -13.736 26.247 1.00 5.00 C
1203	ATOM 759 CG1 ILE A 111 14.881 -12.297 25.789 1.00 5.00 C
1204	ATOM 760 CG2 ILE A 111 14.679 -13.814 27.691 1.00 5.00 C
1205	ATOM 761 CD1 ILE A 111 13.458 -11.845 25.855 1.00 5.00 C
1206	ATOM 762 N GLU A 112 16.236 -16.514 25.650 1.00 13.76 N
1207	ATOM 763 CA GLU A 112 16.301 -17.954 25.898 1.00 13.31 C
1208	ATOM 764 C GLU A 112 17.726 -18.408 26.210 1.00 12.61 C
1209	ATOM 765 O GLU A 112 17.900 -19.318 27.004 1.00 17.13 O
1210	ATOM 766 CB GLU A 112 15.806 -18.730 24.678 1.00 25.64 C
1211	ATOM 767 CG GLU A 112 14.308 -18.730 24.421 1.00 31.30 C
1212	ATOM 768 CD GLU A 112 13.915 -19.731 23.323 1.00 38.96 C
1213	ATOM 769 OE1 GLU A 112 14.429 -19.605 22.179 1.00 42.10 O
1214	ATOM 770 OE2 GLU A 112 13.107 -20.652 23.607 1.00 38.52 O
1215	ATOM 771 N TRP A 113 18.719 -17.786 25.557 1.00 8.25 N
1216	ATOM 772 CA TRP A 113 20.143 -18.077 25.735 1.00 5.00 C
1217	ATOM 773 C TRP A 113 20.635 -17.602 27.082 1.00 5.00 C
1218	ATOM 774 O TRP A 113 21.431 -18.262 27.731 1.00 5.00 O
1219	ATOM 775 CB TRP A 113 20.977 -17.349 24.674 1.00 5.11 C
1220	ATOM 776 CG TRP A 113 22.488 -17.606 24.755 1.00 10.24 C
1221	ATOM 777 CD1 TRP A 113 23.188 -18.574 24.080 1.00 10.08 C
1222	ATOM 778 CD2 TRP A 113 23.472 -16.893 25.544 1.00 13.29 C
1223	ATOM 779 NE1 TRP A 113 24.518 -18.512 24.393 1.00 11.14 N
1224	ATOM 780 CE2 TRP A 113 24.729 -17.491 25.287 1.00 14.26 C
1225	ATOM 781 CE3 TRP A 113 23.412 -15.811 26.443 1.00 11.66 C
1226	ATOM 782 CZ2 TRP A 113 25.928 -17.038 25.895 1.00 12.42 C
1227	ATOM 783 CZ3 TRP A 113 24.610 -15.364 27.048 1.00 10.17 C
1228	ATOM 784 CH2 TRP A 113 25.843 -15.980 26.768 1.00 6.17 C
1229	ATOM 785 N ALA A 114 20.244 -16.391 27.443 1.00 5.00 N
1230	ATOM 786 CA ALA A 114 20.664 -15.786 28.698 1.00 5.00 C
1231	ATOM 787 C ALA A 114 20.122 -16.561 29.877 1.00 7.16 C
1232	ATOM 788 O ALA A 114 20.837 -16.772 30.858 1.00 18.34 O
1233	ATOM 789 CB ALA A 114 20.224 -14.327 28.763 1.00 17.63 C
1234	ATOM 790 N THR A 115 18.869 -16.992 29.784 1.00 5.00 N
1235	ATOM 791 CA THR A 115 18.266 -17.781 30.853 1.00 7.45 C
1236	ATOM 792 C THR A 115 19.002 -19.133 30.987 1.00 5.34 C
1237	ATOM 793 O THR A 115 19.343 -19.568 32.096 1.00 5.00 O
1238	ATOM 794 CB THR A 115 16.766 -18.017 30.580 1.00 5.00 C
1239	ATOM 795 OG1 THR A 115 16.091 -16.764 30.505 1.00 5.00 O
1240	ATOM 796 CG2 THR A 115 16.162 -18.813 31.651 1.00 5.00 C
1241	ATOM 797 N THR A 116 19.237 -19.788 29.849 1.00 10.37 N
1242	ATOM 798 CA THR A 116 19.943 -21.085 29.812 1.00 12.90 C
1243	ATOM 799 C THR A 116 21.358 -20.946 30.386 1.00 13.26 C
1244	ATOM 800 O THR A 116 21.770 -21.745 31.226 1.00 13.88 O
1245	ATOM 801 CB THR A 116 20.105 -21.639 28.341 1.00 11.94 C
1246	ATOM 802 OG1 THR A 116 18.854 -21.607 27.655 1.00 18.71 O
1247	ATOM 803 CG2 THR A 116 20.571 -23.068 28.348 1.00 12.68 C
1248	ATOM 804 N ASN A 117 22.080 -19.915 29.933 1.00 5.00 N
1249	ATOM 805 CA ASN A 117 23.451 -19.655 30.349 1.00 5.00 C
1250	ATOM 806 C ASN A 117 23.723 -19.034 31.710 1.00 5.00 C
1251	ATOM 807 O ASN A 117 24.863 -18.657 32.005 1.00 13.20 O
1252	ATOM 808 CB ASN A 117 24.180 -18.877 29.276 1.00 11.79 C
1253	ATOM 809 CG ASN A 117 24.495 -19.722 28.086 1.00 13.58 C
1254	ATOM 810 OD1 ASN A 117 25.658 -20.036 27.818 1.00 18.69 O
1255	ATOM 811 ND2 ASN A 117 23.458 -20.118 27.360 1.00 15.09 N
1256	ATOM 812 N GLY A 118 22.694 -18.906 32.533 1.00 5.00 N
1257	ATOM 813 CA GLY A 118 22.900 -18.382 33.872 1.00 6.80 C
1258	ATOM 814 C GLY A 118 23.008 -16.896 34.150 1.00 8.21 C
1259	ATOM 815 O GLY A 118 23.568 -16.522 35.183 1.00 20.87 O
1260	ATOM 816 N MET A 119 22.494 -16.048 33.263 1.00 8.25 N
1261	ATOM 817 CA MET A 119 22.538 -14.610 33.490 1.00 8.63 C
1262	ATOM 818 C MET A 119 21.668 -14.211 34.686 1.00 10.48 C
1263	ATOM 819 O MET A 119 20.553 -14.701 34.855 1.00 17.39 O
1264	ATOM 820 CB MET A 119 22.086 -13.847 32.251 1.00 8.98 C
1265	ATOM 821 CG MET A 119 23.005 -14.030 31.069 1.00 13.14 C
1266	ATOM 822 SD MET A 119 24.737 -13.830 31.529 1.00 14.82 S
1267	ATOM 823 CE MET A 119 25.413 -15.360 30.769 1.00 14.08 C
1268	ATOM 824 N ASP A 120 22.188 -13.319 35.516 1.00 24.74 N
1269	ATOM 825 CA ASP A 120 21.464 -12.861 36.686 1.00 22.62 C
1270	ATOM 826 C ASP A 120 20.559 -11.710 36.307 1.00 18.54 C
1271	ATOM 827 O ASP A 120 19.405 -11.659 36.722 1.00 13.97 O
1272	ATOM 828 CB ASP A 120 22.446 -12.436 37.781 1.00 13.06 C
1273	ATOM 829 CG ASP A 120 23.394 -13.553 38.169 1.00 13.06 C
1274	ATOM 830 OD1 ASP A 120 22.938 -14.544 38.759 1.00 21.12 O
1275	ATOM 831 OD2 ASP A 120 24.596 -13.455 37.881 1.00 11.89 O
1276	ATOM 832 N VAL A 121 21.092 -10.793 35.510 1.00 5.00 N
1277	ATOM 833 CA VAL A 121 20.360 -9.624 35.067 1.00 5.00 C
1278	ATOM 834 C VAL A 121 20.356 -9.694 33.543 1.00 5.00 C
1279	ATOM 835 O VAL A 121 21.287 -10.246 32.944 1.00 10.25 O
1280	ATOM 836 CB VAL A 121 21.099 -8.325 35.492 1.00 5.00 C
1281	ATOM 837 CG1 VAL A 121 20.211 -7.132 35.337 1.00 6.27 C
1282	ATOM 838 CG2 VAL A 121 21.595 -8.406 36.906 1.00 5.00 C
1283	ATOM 839 N ILE A 122 19.279 -9.236 32.918 1.00 5.38 N
1284	ATOM 840 CA ILE A 122 19.184 -9.178 31.455 1.00 5.00 C
1285	ATOM 841 C ILE A 122 18.753 -7.742 31.224 1.00 9.64 C
1286	ATOM 842 O ILE A 122 17.814 -7.254 31.883 1.00 5.00 O
1287	ATOM 843 CB ILE A 122 18.049 -10.048 30.858 1.00 5.00 C
1288	ATOM 844 CG1 ILE A 122 18.399 -11.522 30.867 1.00 5.00 C
1289	ATOM 845 CG2 ILE A 122 17.749 -9.629 29.433 1.00 5.00 C
1290	ATOM 846 CD1 ILE A 122 17.248 -12.357 30.372 1.00 5.00 C
1291	ATOM 847 N ASN A 123 19.456 -7.054 30.331 1.00 17.50 N
1292	ATOM 848 CA ASN A 123 19.114 -5.681 30.001 1.00 14.83 C
1293	ATOM 849 C ASN A 123 18.665 -5.634 28.557 1.00 15.12 C
1294	ATOM 850 O ASN A 123 19.296 -6.226 27.671 1.00 5.00 O
1295	ATOM 851 CB ASN A 123 20.298 -4.744 30.189 1.00 5.00 C
1296	ATOM 852 CG ASN A 123 19.953 -3.316 29.845 1.00 5.00 C
1297	ATOM 853 OD1 ASN A 123 19.358 -2.615 30.642 1.00 6.78 O
1298	ATOM 854 ND2 ASN A 123 20.295 -2.888 28.634 1.00 5.00 N
1299	ATOM 855 N MET A 124 17.563 -4.934 28.330 1.00 7.02 N
1300	ATOM 856 CA MET A 124 17.005 -4.781 26.998 1.00 5.00 C
1301	ATOM 857 C MET A 124 16.666 -3.317 26.665 1.00 5.00 C
1302	ATOM 858 O MET A 124 15.608 -2.802 27.043 1.00 5.00 O
1303	ATOM 859 CB MET A 124 15.766 -5.651 26.869 1.00 5.00 C
1304	ATOM 860 CG MET A 124 16.004 -7.102 27.227 1.00 5.00 C
1305	ATOM 861 SD MET A 124 14.703 -8.152 26.581 1.00 5.00 S
1306	ATOM 862 CE MET A 124 13.541 -8.028 27.886 1.00 5.00 C
1307	ATOM 863 N SER A 125 17.604 -2.624 26.031 1.00 5.00 N
1308	ATOM 864 CA SER A 125 17.382 -1.237 25.634 1.00 5.00 C
1309	ATOM 865 C SER A 125 16.879 -1.325 24.184 1.00 5.00 C
1310	ATOM 866 O SER A 125 17.531 -0.920 23.227 1.00 5.00 O
1311	ATOM 867 CB SER A 125 18.689 -0.438 25.736 1.00 7.03 C
1312	ATOM 868 OG SER A 125 19.105 -0.254 27.083 1.00 5.00 O
1313	ATOM 869 N LEU A 126 15.713 -1.924 24.044 1.00 12.02 N
1314	ATOM 870 CA LEU A 126 15.094 -2.126 22.749 1.00 13.21 C
1315	ATOM 871 C LEU A 126 13.618 -2.334 23.027 1.00 15.46 C
1316	ATOM 872 O LEU A 126 13.235 -2.741 24.136 1.00 10.39 O
1317	ATOM 873 CB LEU A 126 15.689 -3.376 22.088 1.00 9.18 C
1318	ATOM 874 CG LEU A 126 15.778 -4.647 22.940 1.00 7.52 C
1319	ATOM 875 CD1 LEU A 126 14.415 -5.336 23.064 1.00 5.00 C
1320	ATOM 876 CD2 LEU A 126 16.829 -5.570 22.321 1.00 6.70 C
1321	ATOM 877 N GLY A 127 12.775 -2.083 22.037 1.00 23.05 N
1322	ATOM 878 CA GLY A 127 11.362 -2.279 22.291 1.00 22.99 C
1323	ATOM 879 C GLY A 127 10.570 -2.311 21.018 1.00 22.33 C
1324	ATOM 880 O GLY A 127 11.155 -2.329 19.925 1.00 25.24 O
1325	ATOM 881 N GLY A 128 9.249 -2.330 21.165 1.00 5.00 N
1326	ATOM 882 CA GLY A 128 8.376 -2.346 20.021 1.00 5.00 C
1327	ATOM 883 C GLY A 128 6.959 -2.070 20.444 1.00 5.00 C
1328	ATOM 884 O GLY A 128 6.635 -2.193 21.627 1.00 9.24 O
1329	ATOM 885 N ALA A 129 6.118 -1.703 19.479 1.00 10.86 N
1330	ATOM 886 CA ALA A 129 4.703 -1.399 19.726 1.00 12.16 C
1331	ATOM 887 C ALA A 129 3.866 -2.602 20.142 1.00 12.52 C
1332	ATOM 888 O ALA A 129 2.872 -2.460 20.869 1.00 15.71 O
1333	ATOM 889 CB ALA A 129 4.079 -0.759 18.486 1.00 15.75 C
1334	ATOM 890 N SER A 130 4.219 -3.774 19.628 1.00 9.80 N
1335	ATOM 891 CA SER A 130 3.473 -4.974 19.947 1.00 8.56 C
1336	ATOM 892 C SER A 130 4.422 -6.016 20.497 1.00 10.66 C
1337	ATOM 893 O SER A 130 5.629 -5.894 20.343 1.00 17.69 O
1338	ATOM 894 CB SER A 130 2.771 -5.491 18.700 1.00 18.98 C
1339	ATOM 895 OG SER A 130 1.890 -4.504 18.190 1.00 22.17 O
1340	ATOM 896 N GLY A 131 3.882 -6.974 21.240 1.00 27.20 N
1341	ATOM 897 CA GLY A 131 4.725 -8.014 21.793 1.00 29.15 C
1342	ATOM 898 C GLY A 131 4.595 -9.291 20.990 1.00 26.18 C
1343	ATOM 899 O GLY A 131 4.594 -9.280 19.758 1.00 5.00 O
1344	ATOM 900 N SER A 132 4.545 -10.404 21.703 1.00 21.32 N
1345	ATOM 901 CA SER A 132 4.369 -11.701 21.083 1.00 20.92 C
1346	ATOM 902 C SER A 132 4.269 -12.710 22.201 1.00 22.83 C
1347	ATOM 903 O SER A 132 4.813 -12.512 23.302 1.00 8.85 O
1348	ATOM 904 CB SER A 132 5.522 -12.058 20.153 1.00 7.59 C
1349	ATOM 905 OG SER A 132 6.621 -12.502 20.897 1.00 13.84 O
1350	ATOM 906 N THR A 133 3.544 -13.782 21.922 1.00 23.44 N
1351	ATOM 907 CA THR A 133 3.367 -14.837 22.895 1.00 25.97 C
1352	ATOM 908 C THR A 133 4.740 -15.424 23.244 1.00 23.08 C
1353	ATOM 909 O THR A 133 5.030 -15.705 24.408 1.00 28.67 O
1354	ATOM 910 CB THR A 133 2.427 -15.925 22.336 1.00 34.03 C
1355	ATOM 911 OG1 THR A 133 1.301 -15.291 21.708 1.00 37.53 O
1356	ATOM 912 CG2 THR A 133 1.927 -16.830 23.472 1.00 35.04 C
1357	ATOM 913 N ALA A 134 5.601 -15.532 22.234 1.00 12.94 N
1358	ATOM 914 CA ALA A 134 6.942 -16.067 22.399 1.00 5.71 C
1359	ATOM 915 C ALA A 134 7.766 -15.200 23.354 1.00 5.36 C
1360	ATOM 916 O ALA A 134 8.401 -15.707 24.279 1.00 5.00 O
1361	ATOM 917 CB ALA A 134 7.610 -16.148 21.056 1.00 14.09 C
1362	ATOM 918 N MET A 135 7.733 -13.889 23.133 1.00 5.00 N
1363	ATOM 919 CA MET A 135 8.461 -12.939 23.965 1.00 7.44 C
1364	ATOM 920 C MET A 135 7.916 -12.900 25.396 1.00 8.04 C
1365	ATOM 921 O MET A 135 8.683 -12.898 26.370 1.00 5.00 O
1366	ATOM 922 CB MET A 135 8.364 -11.554 23.340 1.00 9.93 C
1367	ATOM 923 CG MET A 135 9.112 -10.444 24.051 1.00 11.57 C
1368	ATOM 924 SD MET A 135 9.341 -9.114 22.839 1.00 12.94 S
1369	ATOM 925 CE MET A 135 10.525 -9.884 21.805 1.00 14.40 C
1370	ATOM 926 N LYS A 136 6.593 -12.873 25.530 1.00 5.00 N
1371	ATOM 927 CA LYS A 136 6.013 -12.825 26.855 1.00 5.00 C
1372	ATOM 928 C LYS A 136 6.383 -14.062 27.670 1.00 7.27 C
1373	ATOM 929 O LYS A 136 6.803 -13.950 28.814 1.00 5.00 O
1374	ATOM 930 CB LYS A 136 4.505 -12.656 26.787 1.00 5.00 C
1375	ATOM 931 CG LYS A 136 3.898 -12.584 28.153 1.00 5.00 C
1376	ATOM 932 CD LYS A 136 2.408 -12.360 28.123 1.00 9.11 C
1377	ATOM 933 CE LYS A 136 1.850 -12.486 29.532 1.00 9.58 C
1378	ATOM 934 NZ LYS A 136 2.002 -13.886 30.013 1.00 12.82 N
1379	ATOM 935 N GLN A 137 6.255 -15.245 27.073 1.00 10.52 N
1380	ATOM 936 CA GLN A 137 6.592 -16.474 27.778 1.00 9.09 C
1381	ATOM 937 C GLN A 137 8.095 -16.473 28.079 1.00 8.59 C
1382	ATOM 938 O GLN A 137 8.531 -16.879 29.167 1.00 17.92 O
1383	ATOM 939 CB GLN A 137 6.152 -17.709 26.970 1.00 21.00 C
1384	ATOM 940 CG GLN A 137 4.906 -18.469 27.528 1.00 29.72 C
1385	ATOM 941 CD GLN A 137 3.613 -17.614 27.618 1.00 35.98 C
1386	ATOM 942 OE1 GLN A 137 3.498 -16.693 28.455 1.00 35.87 O
1387	ATOM 943 NE2 GLN A 137 2.624 -17.946 26.781 1.00 34.24 N
1388	ATOM 944 N ALA A 138 8.878 -15.910 27.162 1.00 10.78 N
1389	ATOM 945 CA ALA A 138 10.337 -15.834 27.337 1.00 10.32 C
1390	ATOM 946 C ALA A 138 10.753 -15.069 28.592 1.00 5.47 C
1391	ATOM 947 O ALA A 138 11.518 -15.575 29.405 1.00 5.03 O
1392	ATOM 948 CB ALA A 138 11.001 -15.204 26.106 1.00 10.79 C
1393	ATOM 949 N VAL A 139 10.268 -13.840 28.718 1.00 5.00 N
1394	ATOM 950 CA VAL A 139 10.584 -12.993 29.852 1.00 5.00 C
1395	ATOM 951 C VAL A 139 9.958 -13.515 31.137 1.00 5.00 C
1396	ATOM 952 O VAL A 139 10.570 -13.428 32.205 1.00 5.00 O
1397	ATOM 953 CB VAL A 139 10.258 -11.502 29.549 1.00 5.00 C
1398	ATOM 954 CG1 VAL A 139 10.962 -11.120 28.268 1.00 5.00 C
1399	ATOM 955 CG2 VAL A 139 8.764 -11.250 29.379 1.00 5.00 C
1400	ATOM 956 N ASP A 140 8.799 -14.164 31.014 1.00 5.00 N
1401	ATOM 957 CA ASP A 140 8.114 -14.749 32.166 1.00 5.00 C
1402	ATOM 958 C ASP A 140 8.966 -15.864 32.779 1.00 5.00 C
1403	ATOM 959 O ASP A 140 9.049 -15.973 34.000 1.00 20.98 O
1404	ATOM 960 CB ASP A 140 6.751 -15.309 31.766 1.00 22.28 C
1405	ATOM 961 CG ASP A 140 5.625 -14.264 31.821 1.00 25.79 C
1406	ATOM 962 OD1 ASP A 140 5.859 -13.116 32.276 1.00 24.48 O
1407	ATOM 963 OD2 ASP A 140 4.488 -14.622 31.415 1.00 25.16 O
1408	ATOM 964 N ASN A 141 9.575 -16.710 31.943 1.00 7.06 N
1409	ATOM 965 CA ASN A 141 10.439 -17.785 32.443 1.00 9.95 C
1410	ATOM 966 C ASN A 141 11.741 -17.226 33.017 1.00 11.62 C
1411	ATOM 967 O ASN A 141 12.152 -17.609 34.113 1.00 23.01 O
1412	ATOM 968 CB ASN A 141 10.821 -18.766 31.342 1.00 26.49 C
1413	ATOM 969 CG ASN A 141 9.644 -19.466 30.760 1.00 28.64 C
1414	ATOM 970 OD1 ASN A 141 9.565 -19.673 29.541 1.00 29.41 O
1415	ATOM 971 ND2 ASN A 141 8.722 -19.870 31.623 1.00 32.67 N
1416	ATOM 972 N ALA A 142 12.438 -16.398 32.239 1.00 5.00 N
1417	ATOM 973 CA ALA A 142 13.677 -15.804 32.701 1.00 5.00 C
1418	ATOM 974 C ALA A 142 13.468 -15.200 34.089 1.00 5.00 C
1419	ATOM 975 O ALA A 142 14.296 -15.331 34.972 1.00 8.46 O
1420	ATOM 976 CB ALA A 142 14.113 -14.747 31.752 1.00 10.47 C
1421	ATOM 977 N TYR A 143 12.321 -14.580 34.291 1.00 5.00 N
1422	ATOM 978 CA TYR A 143 12.014 -13.952 35.557 1.00 5.00 C
1423	ATOM 979 C TYR A 143 11.762 -14.988 36.657 1.00 5.00 C
1424	ATOM 980 O TYR A 143 12.332 -14.902 37.746 1.00 5.70 O
1425	ATOM 981 CB TYR A 143 10.808 -13.042 35.359 1.00 8.77 C
1426	ATOM 982 CG TYR A 143 10.545 -12.177 36.533 1.00 11.41 C
1427	ATOM 983 CD1 TYR A 143 11.601 -11.568 37.206 1.00 13.10 C
1428	ATOM 984 CD2 TYR A 143 9.252 -12.015 37.022 1.00 12.31 C
1429	ATOM 985 CE1 TYR A 143 11.383 -10.830 38.342 1.00 13.88 C
1430	ATOM 986 CE2 TYR A 143 9.020 -11.274 38.152 1.00 10.72 C
1431	ATOM 987 CZ TYR A 143 10.092 -10.696 38.817 1.00 12.23 C
1432	ATOM 988 OH TYR A 143 9.893 -10.055 40.012 1.00 15.49 O
1433	ATOM 989 N ALA A 144 10.938 -15.991 36.338 1.00 14.63 N
1434	ATOM 990 CA ALA A 144 10.566 -17.088 37.254 1.00 9.58 C
1435	ATOM 991 C ALA A 144 11.770 -17.944 37.621 1.00 7.94 C
1436	ATOM 992 O ALA A 144 11.801 -18.619 38.644 1.00 5.00 O
1437	ATOM 993 CB ALA A 144 9.501 -17.956 36.600 1.00 5.00 C
1438	ATOM 994 N ARG A 145 12.766 -17.906 36.760 1.00 5.02 N
1439	ATOM 995 CA ARG A 145 13.962 -18.671 36.952 1.00 6.77 C
1440	ATOM 996 C ARG A 145 15.026 -17.938 37.736 1.00 5.23 C
1441	ATOM 997 O ARG A 145 16.075 -18.508 38.019 1.00 28.18 O
1442	ATOM 998 CB ARG A 145 14.486 -19.148 35.600 1.00 26.85 C
1443	ATOM 999 CG ARG A 145 13.599 -20.247 34.975 1.00 33.57 C
1444	ATOM 1000 CD ARG A 145 14.275 -20.890 33.775 1.00 36.88 C
1445	ATOM 1001 NE ARG A 145 15.732 -20.890 33.941 1.00 41.44 N
1446	ATOM 1002 CZ ARG A 145 16.509 -21.962 33.839 1.00 42.99 C
1447	ATOM 1003 NH1 ARG A 145 15.973 -23.137 33.560 1.00 45.73 N
1448	ATOM 1004 NH2 ARG A 145 17.823 -21.856 34.030 1.00 46.93 N
1449	ATOM 1005 N GLY A 146 14.773 -16.686 38.094 1.00 5.00 N
1450	ATOM 1006 CA GLY A 146 15.758 -15.967 38.879 1.00 5.02 C
1451	ATOM 1007 C GLY A 146 16.398 -14.734 38.263 1.00 8.81 C
1452	ATOM 1008 O GLY A 146 17.072 -13.979 38.973 1.00 19.03 O
1453	ATOM 1009 N VAL A 147 16.227 -14.553 36.954 1.00 15.08 N
1454	ATOM 1010 CA VAL A 147 16.772 -13.407 36.231 1.00 13.46 C
1455	ATOM 1011 C VAL A 147 15.997 -12.116 36.552 1.00 13.89 C
1456	ATOM 1012 O VAL A 147 14.808 -12.130 36.891 1.00 5.00 O
1457	ATOM 1013 CB VAL A 147 16.700 -13.614 34.679 1.00 5.30 C
1458	ATOM 1014 CG1 VAL A 147 17.284 -12.416 33.956 1.00 7.25 C
1459	ATOM 1015 CG2 VAL A 147 17.441 -14.868 34.258 1.00 5.00 C
1460	ATOM 1016 N VAL A 148 16.709 -11.003 36.480 1.00 9.21 N
1461	ATOM 1017 CA VAL A 148 16.127 -9.698 36.677 1.00 6.50 C
1462	ATOM 1018 C VAL A 148 16.091 -9.170 35.260 1.00 7.29 C
1463	ATOM 1019 O VAL A 148 17.149 -8.926 34.675 1.00 10.49 O
1464	ATOM 1020 CB VAL A 148 17.052 -8.806 37.500 1.00 9.21 C
1465	ATOM 1021 CG1 VAL A 148 16.439 -7.430 37.653 1.00 5.46 C
1466	ATOM 1022 CG2 VAL A 148 17.341 -9.458 38.870 1.00 10.43 C
1467	ATOM 1023 N VAL A 149 14.905 -9.108 34.660 1.00 9.51 N
1468	ATOM 1024 CA VAL A 149 14.793 -8.593 33.290 1.00 11.83 C
1469	ATOM 1025 C VAL A 149 14.452 -7.090 33.330 1.00 13.39 C
1470	ATOM 1026 O VAL A 149 13.434 -6.679 33.893 1.00 8.35 O
1471	ATOM 1027 CB VAL A 149 13.760 -9.373 32.421 1.00 5.92 C
1472	ATOM 1028 CG1 VAL A 149 14.382 -9.695 31.063 1.00 5.00 C
1473	ATOM 1029 CG2 VAL A 149 13.290 -10.669 33.118 1.00 5.00 C
1474	ATOM 1030 N VAL A 150 15.335 -6.267 32.777 1.00 5.00 N
1475	ATOM 1031 CA VAL A 150 15.136 -4.833 32.786 1.00 5.00 C
1476	ATOM 1032 C VAL A 150 15.019 -4.365 31.356 1.00 5.00 C
1477	ATOM 1033 O VAL A 150 15.845 -4.733 30.532 1.00 5.00 O
1478	ATOM 1034 CB VAL A 150 16.330 -4.147 33.457 1.00 5.00 C
1479	ATOM 1035 CG1 VAL A 150 16.262 -2.668 33.272 1.00 5.00 C
1480	ATOM 1036 CG2 VAL A 150 16.377 -4.489 34.928 1.00 5.00 C
1481	ATOM 1037 N ALA A 151 13.978 -3.591 31.051 1.00 5.00 N
1482	ATOM 1038 CA ALA A 151 13.762 -3.075 29.695 1.00 5.00 C
1483	ATOM 1039 C ALA A 151 13.388 -1.601 29.618 1.00 5.00 C
1484	ATOM 1040 O ALA A 151 12.742 -1.052 30.503 1.00 5.00 O
1485	ATOM 1041 CB ALA A 151 12.723 -3.896 28.964 1.00 5.00 C
1486	ATOM 1042 N ALA A 152 13.863 -0.958 28.564 1.00 7.04 N
1487	ATOM 1043 CA ALA A 152 13.578 0.437 28.295 1.00 5.00 C
1488	ATOM 1044 C ALA A 152 12.049 0.578 28.095 1.00 9.71 C
1489	ATOM 1045 O ALA A 152 11.418 -0.265 27.441 1.00 6.96 O
1490	ATOM 1046 CB ALA A 152 14.317 0.849 27.047 1.00 5.00 C
1491	ATOM 1047 N ALA A 153 11.457 1.626 28.677 1.00 7.91 N
1492	ATOM 1048 CA ALA A 153 10.016 1.882 28.564 1.00 5.00 C
1493	ATOM 1049 C ALA A 153 9.622 2.374 27.190 1.00 5.00 C
1494	ATOM 1050 O ALA A 153 8.577 1.989 26.659 1.00 5.00 O
1495	ATOM 1051 CB ALA A 153 9.578 2.893 29.599 1.00 5.00 C
1496	ATOM 1052 N GLY A 154 10.440 3.258 26.633 1.00 5.00 N
1497	ATOM 1053 CA GLY A 154 10.147 3.801 25.323 1.00 5.80 C
1498	ATOM 1054 C GLY A 154 10.451 5.284 25.252 1.00 10.27 C
1499	ATOM 1055 O GLY A 154 10.628 5.959 26.276 1.00 5.00 O
1500	ATOM 1056 N ASN A 155 10.443 5.813 24.036 1.00 8.07 N
1501	ATOM 1057 CA ASN A 155 10.765 7.213 23.830 1.00 8.04 C
1502	ATOM 1058 C ASN A 155 9.672 7.924 23.035 1.00 6.47 C
1503	ATOM 1059 O ASN A 155 9.948 8.701 22.134 1.00 6.30 O
1504	ATOM 1060 CB ASN A 155 12.125 7.305 23.131 1.00 14.19 C
1505	ATOM 1061 CG ASN A 155 13.236 6.578 23.904 1.00 14.63 C
1506	ATOM 1062 OD1 ASN A 155 13.373 6.724 25.124 1.00 12.59 O
1507	ATOM 1063 ND2 ASN A 155 14.029 5.792 23.190 1.00 13.70 N
1508	ATOM 1064 N SER A 156 8.431 7.746 23.476 1.00 18.21 N
1509	ATOM 1065 CA SER A 156 7.280 8.304 22.780 1.00 22.69 C
1510	ATOM 1066 C SER A 156 6.545 9.449 23.507 1.00 24.84 C
1511	ATOM 1067 O SER A 156 5.455 9.876 23.084 1.00 18.76 O
1512	ATOM 1068 CB SER A 156 6.297 7.162 22.453 1.00 16.31 C
1513	ATOM 1069 OG SER A 156 6.970 5.979 22.027 1.00 13.38 O
1514	ATOM 1070 N GLY A 157 7.144 9.955 24.577 1.00 5.00 N
1515	ATOM 1071 CA GLY A 157 6.522 11.028 25.319 1.00 5.00 C
1516	ATOM 1072 C GLY A 157 5.173 10.609 25.873 1.00 7.06 C
1517	ATOM 1073 O GLY A 157 4.922 9.435 26.125 1.00 22.07 O
1518	ATOM 1074 N ASN A 158 4.303 11.583 26.077 1.00 20.53 N
1519	ATOM 1075 CA ASN A 158 2.972 11.332 26.587 1.00 24.94 C
1520	ATOM 1076 C ASN A 158 1.995 11.900 25.574 1.00 25.76 C
1521	ATOM 1077 O ASN A 158 2.181 13.016 25.086 1.00 41.59 O
1522	ATOM 1078 CB ASN A 158 2.789 11.980 27.969 1.00 45.16 C
1523	ATOM 1079 CG ASN A 158 3.170 13.465 28.006 1.00 45.15 C
1524	ATOM 1080 OD1 ASN A 158 2.414 14.286 28.529 1.00 49.47 O
1525	ATOM 1081 ND2 ASN A 158 4.359 13.802 27.510 1.00 43.80 N
1526	ATOM 1082 N SER A 159 1.027 11.092 25.167 1.00 29.11 N
1527	ATOM 1083 CA SER A 159 0.023 11.533 24.201 1.00 32.44 C
1528	ATOM 1084 C SER A 159 -1.243 11.579 25.031 1.00 32.87 C
1529	ATOM 1085 O SER A 159 -2.272 10.986 24.671 1.00 46.59 O
1530	ATOM 1086 CB SER A 159 -0.142 10.507 23.060 1.00 50.62 C
1531	ATOM 1087 OG SER A 159 1.075 10.240 22.365 1.00 50.49 O
1532	ATOM 1088 N GLY A 160 -1.151 12.266 26.166 1.00 37.78 N
1533	ATOM 1089 CA GLY A 160 -2.281 12.338 27.070 1.00 35.54 C
1534	ATOM 1090 C GLY A 160 -2.460 10.962 27.697 1.00 38.24 C
1535	ATOM 1091 O GLY A 160 -1.475 10.196 27.799 1.00 28.43 O
1536	ATOM 1092 N SER A 161 -3.713 10.623 28.028 1.00 35.61 N
1537	ATOM 1093 CA SER A 161 -4.083 9.348 28.664 1.00 33.66 C
1538	ATOM 1094 C SER A 161 -3.344 8.151 28.095 1.00 30.46 C
1539	ATOM 1095 O SER A 161 -3.120 7.162 28.792 1.00 26.28 O
1540	ATOM 1096 CB SER A 161 -5.584 9.102 28.508 1.00 36.47 C
1541	ATOM 1097 OG SER A 161 -6.339 10.160 29.073 1.00 39.87 O
1542	ATOM 1098 N THR A 162 -2.976 8.279 26.821 1.00 27.20 N
1543	ATOM 1099 CA THR A 162 -2.278 7.271 26.059 1.00 23.08 C
1544	ATOM 1100 C THR A 162 -1.054 6.677 26.762 1.00 23.16 C
1545	ATOM 1101 O THR A 162 -0.132 7.396 27.207 1.00 10.84 O
1546	ATOM 1102 CB THR A 162 -1.833 7.858 24.689 1.00 20.25 C
1547	ATOM 1103 OG1 THR A 162 -2.924 8.565 24.090 1.00 22.05 O
1548	ATOM 1104 CG2 THR A 162 -1.397 6.758 23.738 1.00 19.62 C
1549	ATOM 1105 N ASN A 163 -1.084 5.347 26.856 1.00 26.80 N
1550	ATOM 1106 CA ASN A 163 -0.004 4.548 27.424 1.00 23.45 C
1551	ATOM 1107 C ASN A 163 0.964 4.347 26.259 1.00 26.97 C
1552	ATOM 1108 O ASN A 163 0.642 3.648 25.285 1.00 12.51 O
1553	ATOM 1109 CB ASN A 163 -0.548 3.204 27.878 1.00 6.68 C
1554	ATOM 1110 CG ASN A 163 0.524 2.278 28.398 1.00 5.00 C
1555	ATOM 1111 OD1 ASN A 163 0.528 1.935 29.577 1.00 5.00 O
1556	ATOM 1112 ND2 ASN A 163 1.388 1.799 27.508 1.00 5.00 N
1557	ATOM 1113 N THR A 164 2.101 5.039 26.327 1.00 24.77 N
1558	ATOM 1114 CA THR A 164 3.139 4.975 25.298 1.00 20.06 C
1559	ATOM 1115 C THR A 164 4.239 3.952 25.627 1.00 20.91 C
1560	ATOM 1116 O THR A 164 5.267 3.866 24.922 1.00 5.75 O
1561	ATOM 1117 CB THR A 164 3.772 6.349 25.114 1.00 9.06 C
1562	ATOM 1118 OG1 THR A 164 4.170 6.849 26.391 1.00 6.93 O
1563	ATOM 1119 CG2 THR A 164 2.780 7.312 24.489 1.00 8.73 C
1564	ATOM 1120 N ILE A 165 4.027 3.206 26.712 1.00 12.33 N
1565	ATOM 1121 CA ILE A 165 4.974 2.184 27.144 1.00 15.56 C
1566	ATOM 1122 C ILE A 165 4.861 0.998 26.162 1.00 16.27 C
1567	ATOM 1123 O ILE A 165 3.779 0.730 25.631 1.00 13.54 O
1568	ATOM 1124 CB ILE A 165 4.687 1.707 28.620 1.00 6.60 C
1569	ATOM 1125 CG1 ILE A 165 4.505 2.900 29.556 1.00 5.00 C
1570	ATOM 1126 CG2 ILE A 165 5.861 0.869 29.143 1.00 5.00 C
1571	ATOM 1127 CD1 ILE A 165 5.805 3.564 29.977 1.00 5.00 C
1572	ATOM 1128 N GLY A 166 5.960 0.289 25.923 1.00 11.94 N
1573	ATOM 1129 CA GLY A 166 5.893 -0.819 24.990 1.00 14.63 C
1574	ATOM 1130 C GLY A 166 6.582 -2.092 25.422 1.00 15.29 C
1575	ATOM 1131 O GLY A 166 7.175 -2.154 26.500 1.00 17.40 O
1576	ATOM 1132 N TYR A 167 6.478 -3.112 24.575 1.00 12.79 N
1577	ATOM 1133 CA TYR A 167 7.083 -4.418 24.815 1.00 14.34 C
1578	ATOM 1134 C TYR A 167 8.536 -4.354 24.397 1.00 15.45 C
1579	ATOM 1135 O TYR A 167 8.877 -3.705 23.396 1.00 14.23 O
1580	ATOM 1136 CB TYR A 167 6.351 -5.479 24.006 1.00 11.24 C
1581	ATOM 1137 CG TYR A 167 4.886 -5.323 24.215 1.00 13.46 C
1582	ATOM 1138 CD1 TYR A 167 4.171 -4.369 23.494 1.00 12.98 C
1583	ATOM 1139 CD2 TYR A 167 4.233 -6.016 25.231 1.00 10.85 C
1584	ATOM 1140 CE1 TYR A 167 2.848 -4.090 23.779 1.00 12.99 C
1585	ATOM 1141 CE2 TYR A 167 2.907 -5.744 25.530 1.00 14.78 C
1586	ATOM 1142 CZ TYR A 167 2.219 -4.774 24.800 1.00 12.82 C
1587	ATOM 1143 OH TYR A 167 0.925 -4.456 25.120 1.00 13.22 O
1588	ATOM 1144 N PRO A 168 9.406 -5.082 25.107 1.00 5.00 N
1589	ATOM 1145 CA PRO A 168 9.102 -5.945 26.253 1.00 5.00 C
1590	ATOM 1146 C PRO A 168 8.763 -5.295 27.582 1.00 5.00 C
1591	ATOM 1147 O PRO A 168 8.248 -5.963 28.479 1.00 5.00 O
1592	ATOM 1148 CB PRO A 168 10.363 -6.782 26.376 1.00 6.13 C
1593	ATOM 1149 CG PRO A 168 11.433 -5.813 25.920 1.00 6.06 C
1594	ATOM 1150 CD PRO A 168 10.825 -5.181 24.723 1.00 5.17 C
1595	ATOM 1151 N ALA A 169 9.035 -4.006 27.708 1.00 5.00 N
1596	ATOM 1152 CA ALA A 169 8.778 -3.271 28.948 1.00 5.00 C
1597	ATOM 1153 C ALA A 169 7.349 -3.359 29.527 1.00 5.00 C
1598	ATOM 1154 O ALA A 169 7.177 -3.399 30.747 1.00 5.00 O
1599	ATOM 1155 CB ALA A 169 9.188 -1.825 28.769 1.00 5.00 C
1600	ATOM 1156 N LYS A 170 6.331 -3.399 28.666 1.00 5.16 N
1601	ATOM 1157 CA LYS A 170 4.936 -3.471 29.121 1.00 8.24 C
1602	ATOM 1158 C LYS A 170 4.604 -4.652 30.050 1.00 8.26 C
1603	ATOM 1159 O LYS A 170 3.889 -4.485 31.041 1.00 7.45 O
1604	ATOM 1160 CB LYS A 170 3.998 -3.474 27.921 1.00 15.60 C
1605	ATOM 1161 CG LYS A 170 2.825 -2.526 28.105 1.00 24.36 C
1606	ATOM 1162 CD LYS A 170 2.070 -2.257 26.803 1.00 28.37 C
1607	ATOM 1163 CE LYS A 170 0.915 -1.294 27.029 1.00 30.67 C
1608	ATOM 1164 NZ LYS A 170 0.049 -1.801 28.151 1.00 34.41 N
1609	ATOM 1165 N TYR A 171 5.127 -5.834 29.719 1.00 9.02 N
1610	ATOM 1166 CA TYR A 171 4.935 -7.066 30.501 1.00 11.77 C
1611	ATOM 1167 C TYR A 171 5.301 -6.895 32.002 1.00 9.66 C
1612	ATOM 1168 O TYR A 171 6.195 -6.104 32.331 1.00 12.23 O
1613	ATOM 1169 CB TYR A 171 5.800 -8.189 29.898 1.00 21.48 C
1614	ATOM 1170 CG TYR A 171 5.511 -8.540 28.448 1.00 23.21 C
1615	ATOM 1171 CD1 TYR A 171 4.206 -8.635 27.983 1.00 25.70 C
1616	ATOM 1172 CD2 TYR A 171 6.545 -8.801 27.551 1.00 23.24 C
1617	ATOM 1173 CE1 TYR A 171 3.934 -8.977 26.671 1.00 26.90 C
1618	ATOM 1174 CE2 TYR A 171 6.281 -9.148 26.232 1.00 22.78 C
1619	ATOM 1175 CZ TYR A 171 4.970 -9.234 25.801 1.00 25.00 C
1620	ATOM 1176 OH TYR A 171 4.674 -9.581 24.499 1.00 27.55 O
1621	ATOM 1177 N ASP A 172 4.681 -7.678 32.899 1.00 15.37 N
1622	ATOM 1178 CA ASP A 172 4.980 -7.539 34.338 1.00 17.27 C
1623	ATOM 1179 C ASP A 172 6.101 -8.391 34.937 1.00 15.84 C
1624	ATOM 1180 O ASP A 172 6.259 -8.483 36.148 1.00 25.92 O
1625	ATOM 1181 CB ASP A 172 3.705 -7.518 35.233 1.00 27.85 C
1626	ATOM 1182 CG ASP A 172 2.932 -8.824 35.232 1.00 31.69 C
1627	ATOM 1183 OD1 ASP A 172 3.217 -9.679 36.100 1.00 36.61 O
1628	ATOM 1184 OD2 ASP A 172 1.995 -8.977 34.409 1.00 36.25 O
1629	ATOM 1185 N SER A 173 6.914 -8.976 34.079 1.00 10.93 N
1630	ATOM 1186 CA SER A 173 8.052 -9.749 34.529 1.00 5.00 C
1631	ATOM 1187 C SER A 173 9.279 -8.901 34.192 1.00 5.00 C
1632	ATOM 1188 O SER A 173 10.374 -9.135 34.696 1.00 9.75 O
1633	ATOM 1189 CB SER A 173 8.088 -11.081 33.797 1.00 9.10 C
1634	ATOM 1190 OG SER A 173 7.484 -10.954 32.516 1.00 11.65 O
1635	ATOM 1191 N VAL A 174 9.047 -7.847 33.411 1.00 5.00 N
1636	ATOM 1192 CA VAL A 174 10.082 -6.923 32.949 1.00 5.00 C
1637	ATOM 1193 C VAL A 174 9.895 -5.535 33.541 1.00 5.00 C
1638	ATOM 1194 O VAL A 174 8.809 -4.974 33.505 1.00 5.00 O
1639	ATOM 1195 CB VAL A 174 10.063 -6.776 31.413 1.00 5.00 C
1640	ATOM 1196 CG1 VAL A 174 11.181 -5.829 30.977 1.00 8.75 C
1641	ATOM 1197 CG2 VAL A 174 10.172 -8.138 30.727 1.00 5.00 C
1642	ATOM 1198 N ILE A 175 10.982 -4.983 34.052 1.00 5.00 N
1643	ATOM 1199 CA ILE A 175 10.995 -3.676 34.679 1.00 5.00 C
1644	ATOM 1200 C ILE A 175 11.075 -2.635 33.568 1.00 5.00 C
1645	ATOM 1201 O ILE A 175 11.988 -2.680 32.751 1.00 13.27 O
1646	ATOM 1202 CB ILE A 175 12.223 -3.591 35.628 1.00 5.00 C
1647	ATOM 1203 CG1 ILE A 175 12.130 -4.685 36.710 1.00 6.84 C
1648	ATOM 1204 CG2 ILE A 175 12.372 -2.211 36.210 1.00 5.00 C
1649	ATOM 1205 CD1 ILE A 175 13.376 -4.832 37.594 1.00 6.56 C
1650	ATOM 1206 N ALA A 176 10.079 -1.762 33.471 1.00 5.00 N
1651	ATOM 1207 CA ALA A 176 10.093 -0.730 32.447 1.00 5.00 C
1652	ATOM 1208 C ALA A 176 10.763 0.494 33.054 1.00 7.72 C
1653	ATOM 1209 O ALA A 176 10.318 1.030 34.074 1.00 5.72 O
1654	ATOM 1210 CB ALA A 176 8.692 -0.403 31.999 1.00 7.80 C
1655	ATOM 1211 N VAL A 177 11.871 0.899 32.448 1.00 21.86 N
1656	ATOM 1212 CA VAL A 177 12.654 2.031 32.930 1.00 18.53 C
1657	ATOM 1213 C VAL A 177 12.421 3.305 32.110 1.00 19.11 C
1658	ATOM 1214 O VAL A 177 12.293 3.256 30.879 1.00 8.01 O
1659	ATOM 1215 CB VAL A 177 14.136 1.662 32.938 1.00 8.90 C
1660	ATOM 1216 CG1 VAL A 177 14.956 2.731 33.657 1.00 5.26 C
1661	ATOM 1217 CG2 VAL A 177 14.314 0.282 33.575 1.00 5.00 C
1662	ATOM 1218 N GLY A 178 12.306 4.432 32.814 1.00 9.56 N
1663	ATOM 1219 CA GLY A 178 12.080 5.717 32.178 1.00 6.11 C
1664	ATOM 1220 C GLY A 178 13.300 6.602 32.356 1.00 11.30 C
1665	ATOM 1221 O GLY A 178 14.127 6.377 33.266 1.00 8.42 O
1666	ATOM 1222 N ALA A 179 13.365 7.665 31.554 1.00 17.28 N
1667	ATOM 1223 CA ALA A 179 14.506 8.575 31.571 1.00 15.73 C
1668	ATOM 1224 C ALA A 179 14.338 9.974 32.174 1.00 13.74 C
1669	ATOM 1225 O ALA A 179 13.413 10.708 31.817 1.00 5.00 O
1670	ATOM 1226 CB ALA A 179 15.048 8.694 30.168 1.00 13.36 C
1671	ATOM 1227 N VAL A 180 15.253 10.322 33.079 1.00 5.00 N
1672	ATOM 1228 CA VAL A 180 15.303 11.647 33.704 1.00 5.00 C
1673	ATOM 1229 C VAL A 180 16.618 12.307 33.242 1.00 5.00 C
1674	ATOM 1230 O VAL A 180 17.519 11.622 32.747 1.00 6.85 O
1675	ATOM 1231 CB VAL A 180 15.240 11.604 35.269 1.00 5.00 C
1676	ATOM 1232 CG1 VAL A 180 13.999 10.910 35.730 1.00 5.00 C
1677	ATOM 1233 CG2 VAL A 180 16.432 10.954 35.847 1.00 5.00 C
1678	ATOM 1234 N ASP A 181 16.682 13.631 33.266 1.00 5.00 N
1679	ATOM 1235 CA ASP A 181 17.900 14.331 32.868 1.00 5.00 C
1680	ATOM 1236 C ASP A 181 18.749 14.481 34.116 1.00 5.00 C
1681	ATOM 1237 O ASP A 181 18.446 13.850 35.134 1.00 13.59 O
1682	ATOM 1238 CB ASP A 181 17.599 15.707 32.243 1.00 14.13 C
1683	ATOM 1239 CG ASP A 181 16.825 16.660 33.172 1.00 13.84 C
1684	ATOM 1240 OD1 ASP A 181 16.890 16.549 34.409 1.00 15.08 O
1685	ATOM 1241 OD2 ASP A 181 16.146 17.560 32.640 1.00 18.41 O
1686	ATOM 1242 N SER A 182 19.742 15.369 34.092 1.00 8.77 N
1687	ATOM 1243 CA SER A 182 20.601 15.550 35.265 1.00 10.32 C
1688	ATOM 1244 C SER A 182 19.976 16.342 36.408 1.00 9.58 C
1689	ATOM 1245 O SER A 182 20.399 16.207 37.562 1.00 16.17 O
1690	ATOM 1246 CB SER A 182 21.951 16.150 34.889 1.00 16.18 C
1691	ATOM 1247 OG SER A 182 21.803 17.355 34.167 1.00 17.56 O
1692	ATOM 1248 N ASN A 183 18.978 17.164 36.099 1.00 5.00 N
1693	ATOM 1249 CA ASN A 183 18.301 17.950 37.125 1.00 5.05 C
1694	ATOM 1250 C ASN A 183 17.298 17.085 37.869 1.00 7.32 C
1695	ATOM 1251 O ASN A 183 16.570 17.585 38.746 1.00 10.94 O
1696	ATOM 1252 CB ASN A 183 17.556 19.121 36.493 1.00 12.28 C
1697	ATOM 1253 CG ASN A 183 18.471 20.257 36.119 1.00 14.99 C
1698	ATOM 1254 OD1 ASN A 183 19.075 20.880 36.989 1.00 15.79 O
1699	ATOM 1255 ND2 ASN A 183 18.576 20.542 34.817 1.00 14.60 N
1700	ATOM 1256 N SER A 184 17.279 15.792 37.519 1.00 7.15 N
1701	ATOM 1257 CA SER A 184 16.358 14.799 38.082 1.00 5.63 C
1702	ATOM 1258 C SER A 184 14.946 14.997 37.549 1.00 5.00 C
1703	ATOM 1259 O SER A 184 14.006 14.554 38.183 1.00 9.71 O
1704	ATOM 1260 CB SER A 184 16.301 14.853 39.610 1.00 6.28 C
1705	ATOM 1261 OG SER A 184 17.453 14.323 40.239 1.00 14.76 O
1706	ATOM 1262 N ASN A 185 14.790 15.644 36.397 1.00 5.00 N
1707	ATOM 1263 CA ASN A 185 13.465 15.870 35.828 1.00 5.00 C
1708	ATOM 1264 C ASN A 185 13.237 14.842 34.737 1.00 5.00 C
1709	ATOM 1265 O ASN A 185 14.188 14.382 34.125 1.00 8.25 O
1710	ATOM 1266 CB ASN A 185 13.330 17.272 35.187 1.00 14.21 C
1711	ATOM 1267 CG ASN A 185 13.633 18.427 36.150 1.00 16.88 C
1712	ATOM 1268 OD1 ASN A 185 14.370 19.362 35.795 1.00 18.31 O
1713	ATOM 1269 ND2 ASN A 185 13.052 18.386 37.351 1.00 18.38 N
1714	ATOM 1270 N ARG A 186 11.977 14.495 34.491 1.00 5.00 N
1715	ATOM 1271 CA ARG A 186 11.622 13.542 33.448 1.00 5.00 C
1716	ATOM 1272 C ARG A 186 11.996 14.095 32.090 1.00 5.82 C
1717	ATOM 1273 O ARG A 186 11.991 15.307 31.888 1.00 16.37 O
1718	ATOM 1274 CB ARG A 186 10.125 13.253 33.464 1.00 6.18 C
1719	ATOM 1275 CG ARG A 186 9.575 12.818 32.126 1.00 7.60 C
1720	ATOM 1276 CD ARG A 186 8.171 12.239 32.223 1.00 11.70 C
1721	ATOM 1277 NE ARG A 186 7.721 11.785 30.912 1.00 13.75 N
1722	ATOM 1278 CZ ARG A 186 7.105 12.569 30.040 1.00 15.19 C
1723	ATOM 1279 NH1 ARG A 186 6.850 13.824 30.363 1.00 18.29 N
1724	ATOM 1280 NH2 ARG A 186 6.868 12.152 28.807 1.00 17.42 N
1725	ATOM 1281 N ALA A 187 12.281 13.202 31.151 1.00 13.40 N
1726	ATOM 1282 CA ALA A 187 12.657 13.595 29.796 1.00 12.23 C
1727	ATOM 1283 C ALA A 187 11.435 13.537 28.845 1.00 13.20 C
1728	ATOM 1284 O ALA A 187 10.672 12.576 28.862 1.00 21.67 O
1729	ATOM 1285 CB ALA A 187 13.796 12.696 29.307 1.00 17.68 C
1730	ATOM 1286 N SER A 188 11.251 14.572 28.029 1.00 10.43 N
1731	ATOM 1287 CA SER A 188 10.121 14.675 27.093 1.00 9.82 C
1732	ATOM 1288 C SER A 188 9.839 13.425 26.293 1.00 8.42 C
1733	ATOM 1289 O SER A 188 8.698 13.165 25.934 1.00 19.82 O
1734	ATOM 1290 CB SER A 188 10.359 15.816 26.116 1.00 14.75 C
1735	ATOM 1291 OG SER A 188 11.306 16.725 26.647 1.00 20.66 O
1736	ATOM 1292 N PHE A 189 10.898 12.696 25.965 1.00 10.09 N
1737	ATOM 1293 CA PHE A 189 10.795 11.468 25.191 1.00 9.78 C
1738	ATOM 1294 C PHE A 189 10.358 10.271 26.019 1.00 6.73 C
1739	ATOM 1295 O PHE A 189 9.786 9.342 25.485 1.00 9.95 O
1740	ATOM 1296 CB PHE A 189 12.118 11.164 24.459 1.00 8.53 C
1741	ATOM 1297 CG PHE A 189 13.351 11.122 25.359 1.00 8.49 C
1742	ATOM 1298 CD1 PHE A 189 13.652 9.991 26.118 1.00 10.21 C
1743	ATOM 1299 CD2 PHE A 189 14.229 12.197 25.410 1.00 5.00 C
1744	ATOM 1300 CE1 PHE A 189 14.809 9.941 26.910 1.00 8.61 C
1745	ATOM 1301 CE2 PHE A 189 15.380 12.152 26.197 1.00 5.22 C
1746	ATOM 1302 CZ PHE A 189 15.669 11.027 26.946 1.00 8.95 C
1747	ATOM 1303 N SER A 190 10.597 10.314 27.324 1.00 12.67 N
1748	ATOM 1304 CA SER A 190 10.251 9.221 28.224 1.00 11.78 C
1749	ATOM 1305 C SER A 190 8.779 8.802 28.073 1.00 13.90 C
1750	ATOM 1306 O SER A 190 7.874 9.612 28.274 1.00 5.00 O
1751	ATOM 1307 CB SER A 190 10.572 9.619 29.671 1.00 5.00 C
1752	ATOM 1308 OG SER A 190 10.441 8.529 30.565 1.00 5.00 O
1753	ATOM 1309 N SER A 191 8.556 7.552 27.662 1.00 5.00 N
1754	ATOM 1310 CA SER A 191 7.209 7.036 27.493 1.00 5.00 C
1755	ATOM 1311 C SER A 191 6.484 6.979 28.821 1.00 5.00 C
1756	ATOM 1312 O SER A 191 7.091 6.694 29.856 1.00 7.76 O
1757	ATOM 1313 CB SER A 191 7.245 5.635 26.886 1.00 5.00 C
1758	ATOM 1314 OG SER A 191 7.574 5.674 25.507 1.00 13.18 O
1759	ATOM 1315 N VAL A 192 5.182 7.246 28.782 1.00 5.00 N
1760	ATOM 1316 CA VAL A 192 4.328 7.229 29.970 1.00 5.00 C
1761	ATOM 1317 C VAL A 192 3.327 6.081 29.915 1.00 5.00 C
1762	ATOM 1318 O VAL A 192 2.961 5.612 28.844 1.00 5.00 O
1763	ATOM 1319 CB VAL A 192 3.546 8.546 30.120 1.00 5.00 C
1764	ATOM 1320 CG1 VAL A 192 4.485 9.691 30.278 1.00 5.00 C
1765	ATOM 1321 CG2 VAL A 192 2.665 8.774 28.915 1.00 5.00 C
1766	ATOM 1322 N GLY A 193 2.897 5.620 31.080 1.00 5.00 N
1767	ATOM 1323 CA GLY A 193 1.933 4.544 31.149 1.00 5.00 C
1768	ATOM 1324 C GLY A 193 1.858 3.971 32.542 1.00 5.00 C
1769	ATOM 1325 O GLY A 193 2.742 4.215 33.343 1.00 5.00 O
1770	ATOM 1326 N ALA A 194 0.825 3.175 32.813 1.00 20.87 N
1771	ATOM 1327 CA ALA A 194 0.623 2.557 34.131 1.00 24.91 C
1772	ATOM 1328 C ALA A 194 1.752 1.620 34.523 1.00 26.85 C
1773	ATOM 1329 O ALA A 194 2.111 1.556 35.704 1.00 31.32 O
1774	ATOM 1330 CB ALA A 194 -0.722 1.806 34.188 1.00 17.24 C
1775	ATOM 1331 N GLU A 195 2.304 0.886 33.552 1.00 15.52 N
1776	ATOM 1332 CA GLU A 195 3.402 -0.040 33.850 1.00 13.17 C
1777	ATOM 1333 C GLU A 195 4.766 0.602 33.871 1.00 7.71 C
1778	ATOM 1334 O GLU A 195 5.725 -0.050 33.487 1.00 12.97 O
1779	ATOM 1335 CB GLU A 195 3.465 -1.208 32.862 1.00 20.41 C
1780	ATOM 1336 CG GLU A 195 2.137 -1.832 32.515 1.00 23.59 C
1781	ATOM 1337 CD GLU A 195 1.437 -1.078 31.419 1.00 22.79 C
1782	ATOM 1338 OE1 GLU A 195 2.084 -0.192 30.808 1.00 20.02 O
1783	ATOM 1339 OE2 GLU A 195 0.246 -1.371 31.167 1.00 23.36 O
1784	ATOM 1340 N LEU A 196 4.855 1.874 34.258 1.00 5.00 N
1785	ATOM 1341 CA LEU A 196 6.135 2.568 34.325 1.00 5.00 C
1786	ATOM 1342 C LEU A 196 6.649 2.306 35.731 1.00 5.00 C
1787	ATOM 1343 O LEU A 196 5.949 2.606 36.688 1.00 25.60 O
1788	ATOM 1344 CB LEU A 196 5.913 4.042 34.102 1.00 15.98 C
1789	ATOM 1345 CG LEU A 196 7.122 4.954 34.010 1.00 15.07 C
1790	ATOM 1346 CD1 LEU A 196 8.072 4.400 32.987 1.00 14.61 C
1791	ATOM 1347 CD2 LEU A 196 6.630 6.338 33.617 1.00 14.33 C
1792	ATOM 1348 N GLU A 197 7.868 1.785 35.869 1.00 7.49 N
1793	ATOM 1349 CA GLU A 197 8.381 1.401 37.187 1.00 5.95 C
1794	ATOM 1350 C GLU A 197 9.374 2.275 37.929 1.00 9.30 C
1795	ATOM 1351 O GLU A 197 9.245 2.472 39.148 1.00 10.87 O
1796	ATOM 1352 CB GLU A 197 8.923 -0.020 37.135 1.00 8.02 C
1797	ATOM 1353 CG GLU A 197 8.520 -0.864 38.338 1.00 9.25 C
1798	ATOM 1354 CD GLU A 197 8.936 -2.300 38.204 1.00 10.70 C
1799	ATOM 1355 OE1 GLU A 197 8.280 -3.057 37.435 1.00 10.67 O
1800	ATOM 1356 OE2 GLU A 197 9.935 -2.658 38.858 1.00 13.32 O
1801	ATOM 1357 N VAL A 198 10.437 2.679 37.254 1.00 7.86 N
1802	ATOM 1358 CA VAL A 198 11.416 3.547 37.889 1.00 5.00 C
1803	ATOM 1359 C VAL A 198 11.995 4.474 36.872 1.00 6.40 C
1804	ATOM 1360 O VAL A 198 11.738 4.331 35.681 1.00 11.47 O
1805	ATOM 1361 CB VAL A 198 12.572 2.794 38.583 1.00 5.00 C
1806	ATOM 1362 CG1 VAL A 198 12.184 2.465 39.987 1.00 6.36 C
1807	ATOM 1363 CG2 VAL A 198 12.976 1.559 37.813 1.00 5.00 C
1808	ATOM 1364 N MET A 199 12.752 5.451 37.349 1.00 12.03 N
1809	ATOM 1365 CA MET A 199 13.389 6.416 36.479 1.00 5.28 C
1810	ATOM 1366 C MET A 199 14.867 6.295 36.755 1.00 5.00 C
1811	ATOM 1367 O MET A 199 15.279 6.098 37.906 1.00 5.00 O
1812	ATOM 1368 CB MET A 199 12.901 7.836 36.786 1.00 6.43 C
1813	ATOM 1369 CG MET A 199 11.409 8.040 36.626 1.00 5.92 C
1814	ATOM 1370 SD MET A 199 10.774 7.735 34.967 1.00 10.99 S
1815	ATOM 1371 CE MET A 199 10.938 9.410 34.240 1.00 6.84 C
1816	ATOM 1372 N ALA A 200 15.641 6.307 35.677 1.00 5.00 N
1817	ATOM 1373 CA ALA A 200 17.085 6.219 35.754 1.00 5.00 C
1818	ATOM 1374 C ALA A 200 17.566 7.274 34.763 1.00 5.00 C
1819	ATOM 1375 O ALA A 200 16.813 7.637 33.844 1.00 9.08 O
1820	ATOM 1376 CB ALA A 200 17.536 4.844 35.352 1.00 5.00 C
1821	ATOM 1377 N PRO A 201 18.773 7.848 34.977 1.00 5.00 N
1822	ATOM 1378 CA PRO A 201 19.342 8.881 34.091 1.00 5.00 C
1823	ATOM 1379 C PRO A 201 19.094 8.525 32.636 1.00 5.00 C
1824	ATOM 1380 O PRO A 201 19.175 7.349 32.262 1.00 5.00 O
1825	ATOM 1381 CB PRO A 201 20.839 8.831 34.429 1.00 5.00 C
1826	ATOM 1382 CG PRO A 201 20.846 8.510 35.879 1.00 5.00 C
1827	ATOM 1383 CD PRO A 201 19.738 7.466 36.026 1.00 5.00 C
1828	ATOM 1384 N GLY A 202 18.820 9.521 31.802 1.00 5.00 N
1829	ATOM 1385 CA GLY A 202 18.545 9.202 30.415 1.00 5.00 C
1830	ATOM 1386 C GLY A 202 18.922 10.218 29.382 1.00 5.00 C
1831	ATOM 1387 O GLY A 202 19.122 9.866 28.225 1.00 5.00 O
1832	ATOM 1388 N ALA A 203 18.997 11.482 29.776 1.00 5.00 N
1833	ATOM 1389 CA ALA A 203 19.355 12.545 28.834 1.00 5.00 C
1834	ATOM 1390 C ALA A 203 20.829 12.833 29.012 1.00 5.00 C
1835	ATOM 1391 O ALA A 203 21.347 12.701 30.109 1.00 5.00 O
1836	ATOM 1392 CB ALA A 203 18.526 13.796 29.096 1.00 5.00 C
1837	ATOM 1393 N GLY A 204 21.509 13.169 27.922 1.00 5.00 N
1838	ATOM 1394 CA GLY A 204 22.926 13.465 27.973 1.00 5.00 C
1839	ATOM 1395 C GLY A 204 23.816 12.402 28.579 1.00 5.00 C
1840	ATOM 1396 O GLY A 204 24.809 12.737 29.227 1.00 5.00 O
1841	ATOM 1397 N VAL A 205 23.499 11.130 28.342 1.00 9.23 N
1842	ATOM 1398 CA VAL A 205 24.297 10.021 28.879 1.00 7.30 C
1843	ATOM 1399 C VAL A 205 25.538 9.773 28.046 1.00 6.01 C
1844	ATOM 1400 O VAL A 205 25.457 9.410 26.874 1.00 5.05 O
1845	ATOM 1401 CB VAL A 205 23.499 8.719 28.974 1.00 5.00 C
1846	ATOM 1402 CG1 VAL A 205 24.188 7.764 29.943 1.00 5.00 C
1847	ATOM 1403 CG2 VAL A 205 22.111 9.021 29.444 1.00 5.71 C
1848	ATOM 1404 N TYR A 206 26.682 10.000 28.673 1.00 5.00 N
1849	ATOM 1405 CA TYR A 206 28.000 9.843 28.061 1.00 5.00 C
1850	ATOM 1406 C TYR A 206 28.541 8.437 28.342 1.00 5.00 C
1851	ATOM 1407 O TYR A 206 28.644 8.037 29.503 1.00 7.81 O
1852	ATOM 1408 CB TYR A 206 28.927 10.892 28.683 1.00 7.69 C
1853	ATOM 1409 CG TYR A 206 30.319 10.972 28.103 1.00 11.19 C
1854	ATOM 1410 CD1 TYR A 206 30.528 11.350 26.768 1.00 12.97 C
1855	ATOM 1411 CD2 TYR A 206 31.436 10.705 28.899 1.00 9.65 C
1856	ATOM 1412 CE1 TYR A 206 31.817 11.461 26.247 1.00 11.85 C
1857	ATOM 1413 CE2 TYR A 206 32.715 10.805 28.397 1.00 10.88 C
1858	ATOM 1414 CZ TYR A 206 32.907 11.181 27.069 1.00 12.92 C
1859	ATOM 1415 OH TYR A 206 34.186 11.234 26.563 1.00 13.53 O
1860	ATOM 1416 N SER A 207 28.836 7.660 27.306 1.00 14.54 N
1861	ATOM 1417 CA SER A 207 29.372 6.318 27.544 1.00 15.87 C
1862	ATOM 1418 C SER A 207 30.328 5.842 26.450 1.00 17.86 C
1863	ATOM 1419 O SER A 207 30.730 6.618 25.561 1.00 6.92 O
1864	ATOM 1420 CB SER A 207 28.243 5.304 27.778 1.00 5.00 C
1865	ATOM 1421 OG SER A 207 28.729 4.010 28.075 1.00 5.00 O
1866	ATOM 1422 N THR A 208 30.770 4.592 26.584 1.00 5.00 N
1867	ATOM 1423 CA THR A 208 31.674 3.986 25.632 1.00 5.00 C
1868	ATOM 1424 C THR A 208 31.001 3.960 24.254 1.00 5.00 C
1869	ATOM 1425 O THR A 208 29.795 3.781 24.168 1.00 10.45 O
1870	ATOM 1426 CB THR A 208 32.040 2.567 26.094 1.00 8.73 C
1871	ATOM 1427 OG1 THR A 208 30.870 1.917 26.591 1.00 11.23 O
1872	ATOM 1428 CG2 THR A 208 33.048 2.612 27.220 1.00 6.64 C
1873	ATOM 1429 N TYR A 209 31.754 4.233 23.194 1.00 22.17 N
1874	ATOM 1430 CA TYR A 209 31.207 4.210 21.828 1.00 24.44 C
1875	ATOM 1431 C TYR A 209 32.211 3.541 20.903 1.00 22.98 C
1876	ATOM 1432 O TYR A 209 33.421 3.714 21.056 1.00 13.86 O
1877	ATOM 1433 CB TYR A 209 30.903 5.618 21.305 1.00 15.20 C
1878	ATOM 1434 CG TYR A 209 29.740 5.678 20.327 1.00 10.71 C
1879	ATOM 1435 CD1 TYR A 209 28.488 5.198 20.681 1.00 6.88 C
1880	ATOM 1436 CD2 TYR A 209 29.882 6.274 19.076 1.00 11.30 C
1881	ATOM 1437 CE1 TYR A 209 27.406 5.320 19.822 1.00 8.50 C
1882	ATOM 1438 CE2 TYR A 209 28.806 6.397 18.204 1.00 5.33 C
1883	ATOM 1439 CZ TYR A 209 27.567 5.922 18.584 1.00 7.97 C
1884	ATOM 1440 OH TYR A 209 26.474 6.068 17.742 1.00 10.73 O
1885	ATOM 1441 N PRO A 210 31.722 2.744 19.950 1.00 14.66 N
1886	ATOM 1442 CA PRO A 210 32.587 2.048 19.012 1.00 15.98 C
1887	ATOM 1443 C PRO A 210 33.704 2.880 18.397 1.00 22.37 C
1888	ATOM 1444 O PRO A 210 33.551 4.082 18.084 1.00 6.78 O
1889	ATOM 1445 CB PRO A 210 31.614 1.519 17.974 1.00 11.52 C
1890	ATOM 1446 CG PRO A 210 30.483 1.136 18.811 1.00 16.60 C
1891	ATOM 1447 CD PRO A 210 30.325 2.346 19.734 1.00 15.72 C
1892	ATOM 1448 N THR A 211 34.815 2.153 18.225 1.00 43.76 N
1893	ATOM 1449 CA THR A 211 36.084 2.604 17.693 1.00 39.64 C
1894	ATOM 1450 C THR A 211 36.838 3.431 18.744 1.00 35.25 C
1895	ATOM 1451 O THR A 211 37.295 4.559 18.560 1.00 12.77 O
1896	ATOM 1452 CB THR A 211 35.944 3.106 16.220 1.00 25.79 C
1897	ATOM 1453 OG1 THR A 211 36.636 2.174 15.364 1.00 25.82 O
1898	ATOM 1454 CG2 THR A 211 36.440 4.548 16.001 1.00 27.30 C
1899	ATOM 1455 N ASN A 212 36.912 2.769 19.891 1.00 12.26 N
1900	ATOM 1456 CA ASN A 212 37.585 3.224 21.081 1.00 7.72 C
1901	ATOM 1457 C ASN A 212 37.437 4.690 21.436 1.00 6.46 C
1902	ATOM 1458 O ASN A 212 38.407 5.415 21.574 1.00 10.35 O
1903	ATOM 1459 CB ASN A 212 39.040 2.778 21.020 1.00 8.23 C
1904	ATOM 1460 CG ASN A 212 39.166 1.297 20.715 1.00 11.03 C
1905	ATOM 1461 OD1 ASN A 212 39.879 0.887 19.801 1.00 15.56 O
1906	ATOM 1462 ND2 ASN A 212 38.417 0.487 21.445 1.00 8.52 N
1907	ATOM 1463 N THR A 213 36.200 5.110 21.631 1.00 9.02 N
1908	ATOM 1464 CA THR A 213 35.932 6.478 22.017 1.00 5.07 C
1909	ATOM 1465 C THR A 213 34.647 6.536 22.842 1.00 5.00 C
1910	ATOM 1466 O THR A 213 34.111 5.491 23.235 1.00 5.24 O
1911	ATOM 1467 CB THR A 213 35.920 7.426 20.804 1.00 7.94 C
1912	ATOM 1468 OG1 THR A 213 35.863 8.779 21.269 1.00 13.38 O
1913	ATOM 1469 CG2 THR A 213 34.754 7.123 19.862 1.00 5.24 C
1914	ATOM 1470 N TYR A 214 34.214 7.745 23.188 1.00 8.84 N
1915	ATOM 1471 CA TYR A 214 33.022 7.932 24.017 1.00 11.33 C
1916	ATOM 1472 C TYR A 214 32.132 8.996 23.410 1.00 14.15 C
1917	ATOM 1473 O TYR A 214 32.618 10.006 22.870 1.00 11.63 O
1918	ATOM 1474 CB TYR A 214 33.414 8.309 25.465 1.00 5.41 C
1919	ATOM 1475 CG TYR A 214 34.591 7.512 25.954 1.00 6.68 C
1920	ATOM 1476 CD1 TYR A 214 35.893 7.870 25.577 1.00 5.51 C
1921	ATOM 1477 CD2 TYR A 214 34.413 6.317 26.650 1.00 5.38 C
1922	ATOM 1478 CE1 TYR A 214 36.993 7.052 25.865 1.00 5.32 C
1923	ATOM 1479 CE2 TYR A 214 35.510 5.488 26.939 1.00 6.83 C
1924	ATOM 1480 CZ TYR A 214 36.796 5.871 26.538 1.00 7.75 C
1925	ATOM 1481 OH TYR A 214 37.881 5.081 26.806 1.00 5.34 O
1926	ATOM 1482 N ALA A 215 30.824 8.765 23.512 1.00 11.92 N
1927	ATOM 1483 CA ALA A 215 29.836 9.673 22.961 1.00 8.08 C
1928	ATOM 1484 C ALA A 215 28.689 9.907 23.923 1.00 11.01 C
1929	ATOM 1485 O ALA A 215 28.509 9.175 24.900 1.00 7.24 O
1930	ATOM 1486 CB ALA A 215 29.317 9.123 21.660 1.00 5.00 C
1931	ATOM 1487 N THR A 216 27.918 10.952 23.646 1.00 14.26 N
1932	ATOM 1488 CA THR A 216 26.776 11.284 24.459 1.00 10.47 C
1933	ATOM 1489 C THR A 216 25.521 10.957 23.670 1.00 12.67 C
1934	ATOM 1490 O THR A 216 25.391 11.361 22.506 1.00 7.74 O
1935	ATOM 1491 CB THR A 216 26.817 12.746 24.877 1.00 5.00 C
1936	ATOM 1492 OG1 THR A 216 27.988 12.954 25.667 1.00 5.66 O
1937	ATOM 1493 CG2 THR A 216 25.612 13.094 25.736 1.00 5.64 C
1938	ATOM 1494 N LEU A 217 24.643 10.168 24.297 1.00 5.00 N
1939	ATOM 1495 CA LEU A 217 23.388 9.735 23.713 1.00 5.00 C
1940	ATOM 1496 C LEU A 217 22.203 10.099 24.610 1.00 5.00 C
1941	ATOM 1497 O LEU A 217 22.376 10.424 25.777 1.00 10.15 O
1942	ATOM 1498 CB LEU A 217 23.424 8.216 23.496 1.00 12.10 C
1943	ATOM 1499 CG LEU A 217 23.551 7.615 22.084 1.00 13.92 C
1944	ATOM 1500 CD1 LEU A 217 24.746 8.212 21.345 1.00 18.12 C
1945	ATOM 1501 CD2 LEU A 217 23.679 6.090 22.149 1.00 16.69 C
1946	ATOM 1502 N ASN A 218 21.002 10.019 24.049 1.00 5.00 N
1947	ATOM 1503 CA ASN A 218 19.748 10.309 24.730 1.00 5.00 C
1948	ATOM 1504 C ASN A 218 18.784 9.150 24.456 1.00 5.00 C
1949	ATOM 1505 O ASN A 218 18.696 8.682 23.322 1.00 5.00 O
1950	ATOM 1506 CB ASN A 218 19.079 11.544 24.108 1.00 5.22 C
1951	ATOM 1507 CG ASN A 218 19.577 12.852 24.665 1.00 5.58 C
1952	ATOM 1508 OD1 ASN A 218 20.565 12.915 25.375 1.00 7.64 O
1953	ATOM 1509 ND2 ASN A 218 18.881 13.922 24.322 1.00 10.86 N
1954	ATOM 1510 N GLY A 219 18.026 8.737 25.469 1.00 8.22 N
1955	ATOM 1511 CA GLY A 219 17.035 7.682 25.304 1.00 8.63 C
1956	ATOM 1512 C GLY A 219 16.754 6.929 26.585 1.00 6.66 C
1957	ATOM 1513 O GLY A 219 17.491 7.092 27.554 1.00 8.84 O
1958	ATOM 1514 N THR A 220 15.662 6.170 26.645 1.00 5.00 N
1959	ATOM 1515 CA THR A 220 15.424 5.371 27.845 1.00 5.00 C
1960	ATOM 1516 C THR A 220 16.331 4.156 27.685 1.00 5.00 C
1961	ATOM 1517 O THR A 220 16.440 3.324 28.583 1.00 5.00 O
1962	ATOM 1518 CB THR A 220 13.990 4.921 28.021 1.00 5.00 C
1963	ATOM 1519 OG1 THR A 220 13.581 4.155 26.894 1.00 5.00 O
1964	ATOM 1520 CG2 THR A 220 13.095 6.106 28.181 1.00 5.00 C
1965	HETATM 1521 N SBL A 221 16.957 4.059 26.515 1.00 5.00 N
1966	HETATM 1522 CA SBL A 221 17.920 3.013 26.231 1.00 7.24 C
1967	HETATM 1523 CB SBL A 221 18.462 3.158 24.806 1.00 9.77 C
1968	HETATM 1524 O3 SBL A 221 17.585 2.590 23.843 1.00 11.00 O
1969	HETATM 1525 C SBL A 221 19.065 3.223 27.226 1.00 9.78 C
1970	HETATM 1526 O SBL A 221 19.729 2.270 27.664 1.00 8.72 O
1971	HETATM 1527 N13 SBL A 221 16.674 2.294 20.610 1.00 22.71 N
1972	HETATM 1528 C12 SBL A 221 15.903 2.888 21.717 1.00 17.36 C
1973	HETATM 1529 C11 SBL A 221 14.941 2.057 22.572 1.00 17.97 C
1974	HETATM 1530 C1 SBL A 221 13.614 1.802 21.895 1.00 22.41 C
1975	HETATM 1531 C10 SBL A 221 12.486 1.378 22.624 1.00 25.51 C
1976	HETATM 1532 C5 SBL A 221 11.226 1.206 21.974 1.00 25.37 C
1977	HETATM 1533 C2 SBL A 221 13.460 2.042 20.526 1.00 24.01 C
1978	HETATM 1534 C3 SBL A 221 12.232 1.874 19.887 1.00 24.64 C
1979	HETATM 1535 C4 SBL A 221 11.112 1.462 20.610 1.00 26.46 C
1980	HETATM 1536 O1 SBL A 221 18.252 4.316 22.027 1.00 13.11 O
1981	HETATM 1537 O2 SBL A 221 16.322 4.806 23.611 1.00 10.96 O
1982	HETATM 1538 B SBL A 221 17.055 3.677 22.840 1.00 13.61 B
1983	HETATM 1539 C14 SBL A 221 16.706 0.988 20.328 1.00 27.08 C
1984	HETATM 1540 O15 SBL A 221 15.715 0.269 20.402 1.00 32.84 O
1985	HETATM 1541 C16 SBL A 221 17.993 0.354 19.857 1.00 31.47 C
1986	HETATM 1542 C9 SBL A 221 12.591 1.072 23.981 1.00 27.78 C
1987	HETATM 1543 C8 SBL A 221 11.471 0.603 24.685 1.00 28.33 C
1988	HETATM 1544 C7 SBL A 221 10.236 0.443 24.034 1.00 27.18 C
1989	HETATM 1545 C6 SBL A 221 10.115 0.750 22.685 1.00 23.21 C
1990	ATOM 1546 N MET A 222 19.266 4.494 27.574 1.00 10.30 N
1991	ATOM 1547 CA MET A 222 20.298 4.923 28.506 1.00 9.25 C
1992	ATOM 1548 C MET A 222 19.848 4.812 29.976 1.00 6.65 C
1993	ATOM 1549 O MET A 222 20.663 4.649 30.873 1.00 5.16 O
1994	ATOM 1550 CB MET A 222 20.722 6.367 28.181 1.00 5.00 C
1995	ATOM 1551 CG MET A 222 21.653 6.536 27.004 1.00 5.00 C
1996	ATOM 1552 SD MET A 222 20.962 6.039 25.437 1.00 7.19 S
1997	ATOM 1553 CE MET A 222 22.009 4.617 24.996 1.00 5.00 C
1998	ATOM 1554 N ALA A 223 18.557 4.912 30.226 1.00 5.00 N
1999	ATOM 1555 CA ALA A 223 18.063 4.806 31.586 1.00 5.00 C
2000	ATOM 1556 C ALA A 223 18.218 3.370 32.059 1.00 7.14 C
2001	ATOM 1557 O ALA A 223 18.805 3.107 33.116 1.00 5.00 O
2002	ATOM 1558 CB ALA A 223 16.603 5.217 31.641 1.00 5.00 C
2003	ATOM 1559 N SER A 224 17.762 2.450 31.211 1.00 12.77 N
2004	ATOM 1560 CA SER A 224 17.766 1.009 31.459 1.00 11.96 C
2005	ATOM 1561 C SER A 224 19.031 0.349 32.084 1.00 11.75 C
2006	ATOM 1562 O SER A 224 18.943 -0.304 33.144 1.00 5.00 O
2007	ATOM 1563 CB SER A 224 17.330 0.303 30.177 1.00 5.00 C
2008	ATOM 1564 OG SER A 224 16.974 -1.038 30.424 1.00 7.01 O
2009	ATOM 1565 N PRO A 225 20.219 0.536 31.465 1.00 5.00 N
2010	ATOM 1566 CA PRO A 225 21.449 -0.054 31.999 1.00 5.00 C
2011	ATOM 1567 C PRO A 225 21.816 0.458 33.378 1.00 5.00 C
2012	ATOM 1568 O PRO A 225 22.623 -0.153 34.073 1.00 9.03 O
2013	ATOM 1569 CB PRO A 225 22.505 0.288 30.933 1.00 5.00 C
2014	ATOM 1570 CG PRO A 225 22.002 1.489 30.294 1.00 5.43 C
2015	ATOM 1571 CD PRO A 225 20.502 1.256 30.212 1.00 7.78 C
2016	ATOM 1572 N HIS A 226 21.230 1.576 33.787 1.00 5.00 N
2017	ATOM 1573 CA HIS A 226 21.499 2.110 35.117 1.00 5.00 C
2018	ATOM 1574 C HIS A 226 20.880 1.222 36.155 1.00 5.00 C
2019	ATOM 1575 O HIS A 226 21.396 1.092 37.246 1.00 5.00 O
2020	ATOM 1576 CB HIS A 226 20.920 3.499 35.275 1.00 5.00 C
2021	ATOM 1577 CG HIS A 226 21.721 4.544 34.597 1.00 5.00 C
2022	ATOM 1578 ND1 HIS A 226 21.520 4.894 33.283 1.00 10.88 N
2023	ATOM 1579 CD2 HIS A 226 22.751 5.299 35.037 1.00 5.00 C
2024	ATOM 1580 CE1 HIS A 226 22.391 5.823 32.937 1.00 7.46 C
2025	ATOM 1581 NE2 HIS A 226 23.150 6.085 33.985 1.00 6.05 N
2026	ATOM 1582 N VAL A 227 19.737 0.650 35.805 1.00 14.66 N
2027	ATOM 1583 CA VAL A 227 19.005 -0.237 36.694 1.00 16.43 C
2028	ATOM 1584 C VAL A 227 19.553 -1.687 36.581 1.00 17.55 C
2029	ATOM 1585 O VAL A 227 19.758 -2.363 37.597 1.00 5.00 O
2030	ATOM 1586 CB VAL A 227 17.481 -0.071 36.454 1.00 7.92 C
2031	ATOM 1587 CG1 VAL A 227 16.679 -1.080 37.254 1.00 5.00 C
2032	ATOM 1588 CG2 VAL A 227 17.069 1.370 36.838 1.00 5.00 C
2033	ATOM 1589 N ALA A 228 19.857 -2.125 35.359 1.00 5.00 N
2034	ATOM 1590 CA ALA A 228 20.466 -3.423 35.144 1.00 5.00 C
2035	ATOM 1591 C ALA A 228 21.740 -3.363 35.967 1.00 5.00 C
2036	ATOM 1592 O ALA A 228 22.117 -4.329 36.628 1.00 8.01 O
2037	ATOM 1593 CB ALA A 228 20.815 -3.588 33.710 1.00 5.00 C
2038	ATOM 1594 N GLY A 229 22.378 -2.196 35.959 1.00 5.00 N
2039	ATOM 1595 CA GLY A 229 23.598 -2.001 36.719 1.00 5.00 C
2040	ATOM 1596 C GLY A 229 23.362 -2.094 38.218 1.00 5.00 C
2041	ATOM 1597 O GLY A 229 24.062 -2.831 38.921 1.00 5.00 O
2042	ATOM 1598 N ALA A 230 22.365 -1.352 38.697 1.00 5.00 N
2043	ATOM 1599 CA ALA A 230 21.988 -1.303 40.116 1.00 5.00 C
2044	ATOM 1600 C ALA A 230 21.567 -2.664 40.677 1.00 5.00 C
2045	ATOM 1601 O ALA A 230 21.809 -2.960 41.851 1.00 5.00 O
2046	ATOM 1602 CB ALA A 230 20.890 -0.269 40.338 1.00 5.00 C
2047	ATOM 1603 N ALA A 231 20.912 -3.475 39.851 1.00 5.00 N
2048	ATOM 1604 CA ALA A 231 20.528 -4.824 40.248 1.00 5.00 C
2049	ATOM 1605 C ALA A 231 21.823 -5.599 40.540 1.00 5.00 C
2050	ATOM 1606 O ALA A 231 21.894 -6.324 41.531 1.00 9.04 O
2051	ATOM 1607 CB ALA A 231 19.763 -5.506 39.134 1.00 5.00 C
2052	ATOM 1608 N ALA A 232 22.872 -5.376 39.738 1.00 5.00 N
2053	ATOM 1609 CA ALA A 232 24.137 -6.089 39.920 1.00 5.00 C
2054	ATOM 1610 C ALA A 232 24.829 -5.756 41.220 1.00 5.00 C
2055	ATOM 1611 O ALA A 232 25.423 -6.637 41.847 1.00 8.55 O
2056	ATOM 1612 CB ALA A 232 25.058 -5.855 38.770 1.00 5.00 C
2057	ATOM 1613 N LEU A 233 24.811 -4.480 41.597 1.00 8.79 N
2058	ATOM 1614 CA LEU A 233 25.429 -4.035 42.852 1.00 5.76 C
2059	ATOM 1615 C LEU A 233 24.579 -4.621 43.975 1.00 5.07 C
2060	ATOM 1616 O LEU A 233 25.095 -5.013 45.011 1.00 18.87 O
2061	ATOM 1617 CB LEU A 233 25.441 -2.492 42.967 1.00 17.43 C
2062	ATOM 1618 CG LEU A 233 26.130 -1.551 41.951 1.00 15.43 C
2063	ATOM 1619 CD1 LEU A 233 25.410 -0.241 41.883 1.00 14.54 C
2064	ATOM 1620 CD2 LEU A 233 27.559 -1.298 42.306 1.00 17.86 C
2065	ATOM 1621 N ILE A 234 23.271 -4.711 43.776 1.00 12.31 N
2066	ATOM 1622 CA ILE A 234 22.419 -5.270 44.828 1.00 12.14 C
2067	ATOM 1623 C ILE A 234 22.725 -6.759 45.016 1.00 12.13 C
2068	ATOM 1624 O ILE A 234 22.883 -7.227 46.149 1.00 11.79 O
2069	ATOM 1625 CB ILE A 234 20.903 -5.013 44.551 1.00 8.06 C
2070	ATOM 1626 CG1 ILE A 234 20.631 -3.502 44.578 1.00 6.79 C
2071	ATOM 1627 CG2 ILE A 234 20.036 -5.699 45.591 1.00 5.00 C
2072	ATOM 1628 CD1 ILE A 234 19.196 -3.133 44.333 1.00 6.85 C
2073	ATOM 1629 N LEU A 235 22.903 -7.472 43.907 1.00 5.00 N
2074	ATOM 1630 CA LEU A 235 23.202 -8.890 43.954 1.00 5.00 C
2075	ATOM 1631 C LEU A 235 24.584 -9.207 44.482 1.00 5.00 C
2076	ATOM 1632 O LEU A 235 24.769 -10.228 45.123 1.00 5.00 O
2077	ATOM 1633 CB LEU A 235 23.022 -9.519 42.583 1.00 5.00 C
2078	ATOM 1634 CG LEU A 235 21.558 -9.743 42.203 1.00 5.00 C
2079	ATOM 1635 CD1 LEU A 235 21.415 -9.932 40.721 1.00 5.00 C
2080	ATOM 1636 CD2 LEU A 235 20.975 -10.912 42.985 1.00 5.00 C
2081	ATOM 1637 N SER A 236 25.568 -8.350 44.238 1.00 5.00 N
2082	ATOM 1638 CA SER A 236 26.908 -8.648 44.718 1.00 5.00 C
2083	ATOM 1639 C SER A 236 26.903 -8.521 46.224 1.00 6.36 C
2084	ATOM 1640 O SER A 236 27.319 -9.443 46.935 1.00 13.77 O
2085	ATOM 1641 CB SER A 236 27.955 -7.743 44.075 1.00 5.50 C
2086	ATOM 1642 OG SER A 236 27.996 -6.489 44.701 1.00 7.87 O
2087	ATOM 1643 N LYS A 237 26.348 -7.414 46.708 1.00 5.00 N
2088	ATOM 1644 CA LYS A 237 26.241 -7.163 48.142 1.00 5.56 C
2089	ATOM 1645 C LYS A 237 25.342 -8.161 48.887 1.00 7.68 C
2090	ATOM 1646 O LYS A 237 25.629 -8.480 50.045 1.00 13.54 O
2091	ATOM 1647 CB LYS A 237 25.715 -5.755 48.387 1.00 12.71 C
2092	ATOM 1648 CG LYS A 237 25.618 -5.397 49.849 1.00 12.86 C
2093	ATOM 1649 CD LYS A 237 25.202 -3.962 49.999 1.00 12.82 C
2094	ATOM 1650 CE LYS A 237 25.550 -3.439 51.355 1.00 6.37 C
2095	ATOM 1651 NZ LYS A 237 25.137 -2.033 51.339 1.00 11.47 N
2096	ATOM 1652 N HIS A 238 24.204 -8.545 48.283 1.00 10.75 N
2097	ATOM 1653 CA HIS A 238 23.257 -9.527 48.869 1.00 11.34 C
2098	ATOM 1654 C HIS A 238 22.935 -10.537 47.791 1.00 14.68 C
2099	ATOM 1655 O HIS A 238 21.852 -10.486 47.183 1.00 9.31 O
2100	ATOM 1656 CB HIS A 238 21.908 -8.935 49.285 1.00 10.15 C
2101	ATOM 1657 CG HIS A 238 21.983 -7.909 50.360 1.00 5.53 C
2102	ATOM 1658 ND1 HIS A 238 21.620 -6.597 50.154 1.00 8.91 N
2103	ATOM 1659 CD2 HIS A 238 22.352 -8.000 51.656 1.00 6.91 C
2104	ATOM 1660 CE1 HIS A 238 21.759 -5.919 51.278 1.00 8.00 C
2105	ATOM 1661 NE2 HIS A 238 22.201 -6.748 52.207 1.00 9.68 N
2106	ATOM 1662 N PRO A 239 23.849 -11.500 47.574 1.00 14.24 N
2107	ATOM 1663 CA PRO A 239 23.683 -12.543 46.565 1.00 9.65 C
2108	ATOM 1664 C PRO A 239 22.587 -13.536 46.852 1.00 8.23 C
2109	ATOM 1665 O PRO A 239 22.287 -14.358 45.997 1.00 22.63 O
2110	ATOM 1666 CB PRO A 239 25.050 -13.209 46.548 1.00 20.01 C
2111	ATOM 1667 CG PRO A 239 25.518 -13.045 47.956 1.00 22.07 C
2112	ATOM 1668 CD PRO A 239 25.155 -11.635 48.254 1.00 20.98 C
2113	ATOM 1669 N ASN A 240 22.020 -13.500 48.057 1.00 15.36 N
2114	ATOM 1670 CA ASN A 240 20.937 -14.435 48.442 1.00 20.24 C
2115	ATOM 1671 C ASN A 240 19.529 -13.967 48.043 1.00 19.14 C
2116	ATOM 1672 O ASN A 240 18.560 -14.718 48.169 1.00 36.69 O
2117	ATOM 1673 CB ASN A 240 20.985 -14.757 49.953 1.00 38.59 C
2118	ATOM 1674 CG ASN A 240 21.684 -13.661 50.778 1.00 41.77 C
2119	ATOM 1675 OD1 ASN A 240 21.046 -12.733 51.307 1.00 40.90 O
2120	ATOM 1676 ND2 ASN A 240 23.012 -13.765 50.876 1.00 40.44 N
2121	ATOM 1677 N LEU A 241 19.441 -12.721 47.575 1.00 14.24 N
2122	ATOM 1678 CA LEU A 241 18.204 -12.098 47.136 1.00 5.00 C
2123	ATOM 1679 C LEU A 241 17.691 -12.735 45.875 1.00 5.01 C
2124	ATOM 1680 O LEU A 241 18.464 -13.193 45.031 1.00 5.00 O
2125	ATOM 1681 CB LEU A 241 18.448 -10.624 46.816 1.00 9.97 C
2126	ATOM 1682 CG LEU A 241 18.134 -9.631 47.907 1.00 8.72 C
2127	ATOM 1683 CD1 LEU A 241 18.736 -10.151 49.179 1.00 10.47 C
2128	ATOM 1684 CD2 LEU A 241 18.651 -8.262 47.537 1.00 6.94 C
2129	ATOM 1685 N SER A 242 16.379 -12.626 45.697 1.00 5.00 N
2130	ATOM 1686 CA SER A 242 15.689 -13.164 44.531 1.00 5.00 C
2131	ATOM 1687 C SER A 242 15.469 -11.997 43.603 1.00 5.00 C
2132	ATOM 1688 O SER A 242 15.666 -10.857 44.004 1.00 15.14 O
2133	ATOM 1689 CB SER A 242 14.345 -13.723 44.955 1.00 5.54 C
2134	ATOM 1690 OG SER A 242 13.645 -12.749 45.694 1.00 5.54 O
2135	ATOM 1691 N ALA A 243 15.015 -12.266 42.387 1.00 8.51 N
2136	ATOM 1692 CA ALA A 243 14.776 -11.194 41.422 1.00 10.95 C
2137	ATOM 1693 C ALA A 243 13.661 -10.281 41.901 1.00 9.56 C
2138	ATOM 1694 O ALA A 243 13.706 -9.071 41.686 1.00 6.25 O
2139	ATOM 1695 CB ALA A 243 14.440 -11.768 40.026 1.00 8.87 C
2140	ATOM 1696 N SER A 244 12.677 -10.869 42.577 1.00 5.20 N
2141	ATOM 1697 CA SER A 244 11.545 -10.107 43.082 1.00 8.74 C
2142	ATOM 1698 C SER A 244 11.976 -9.268 44.276 1.00 8.95 C
2143	ATOM 1699 O SER A 244 11.466 -8.165 44.502 1.00 7.88 O
2144	ATOM 1700 CB SER A 244 10.368 -11.027 43.444 1.00 7.05 C
2145	ATOM 1701 OG SER A 244 10.689 -11.914 44.497 1.00 11.21 O
2146	ATOM 1702 N GLN A 245 12.952 -9.782 45.009 1.00 5.13 N
2147	ATOM 1703 CA GLN A 245 13.458 -9.072 46.147 1.00 5.81 C
2148	ATOM 1704 C GLN A 245 14.314 -7.905 45.710 1.00 7.67 C
2149	ATOM 1705 O GLN A 245 14.310 -6.862 46.369 1.00 17.53 O
2150	ATOM 1706 CB GLN A 245 14.202 -10.006 47.076 1.00 13.59 C
2151	ATOM 1707 CG GLN A 245 13.358 -10.383 48.292 1.00 12.31 C
2152	ATOM 1708 CD GLN A 245 13.811 -11.659 48.962 1.00 11.89 C
2153	ATOM 1709 OE1 GLN A 245 12.998 -12.356 49.552 1.00 16.50 O
2154	ATOM 1710 NE2 GLN A 245 15.103 -11.985 48.860 1.00 10.33 N
2155	ATOM 1711 N VAL A 246 15.022 -8.057 44.592 1.00 5.00 N
2156	ATOM 1712 CA VAL A 246 15.846 -6.967 44.081 1.00 5.00 C
2157	ATOM 1713 C VAL A 246 14.878 -5.935 43.525 1.00 5.00 C
2158	ATOM 1714 O VAL A 246 14.814 -4.817 44.012 1.00 5.00 O
2159	ATOM 1715 CB VAL A 246 16.802 -7.450 42.988 1.00 5.00 C
2160	ATOM 1716 CG1 VAL A 246 17.312 -6.272 42.149 1.00 5.00 C
2161	ATOM 1717 CG2 VAL A 246 17.942 -8.249 43.616 1.00 5.00 C
2162	ATOM 1718 N ARG A 247 14.067 -6.359 42.560 1.00 6.44 N
2163	ATOM 1719 CA ARG A 247 13.046 -5.521 41.931 1.00 8.26 C
2164	ATOM 1720 C ARG A 247 12.326 -4.669 42.974 1.00 5.94 C
2165	ATOM 1721 O ARG A 247 12.218 -3.458 42.838 1.00 5.90 O
2166	ATOM 1722 CB ARG A 247 12.033 -6.423 41.231 1.00 10.37 C
2167	ATOM 1723 CG ARG A 247 10.898 -5.708 40.570 1.00 11.30 C
2168	ATOM 1724 CD ARG A 247 10.474 -6.467 39.329 1.00 9.42 C
2169	ATOM 1725 NE ARG A 247 9.354 -5.833 38.656 1.00 10.95 N
2170	ATOM 1726 CZ ARG A 247 8.567 -6.452 37.783 1.00 13.00 C
2171	ATOM 1727 NH1 ARG A 247 8.806 -7.715 37.484 1.00 18.57 N
2172	ATOM 1728 NH2 ARG A 247 7.527 -5.834 37.231 1.00 11.80 N
2173	ATOM 1729 N ASN A 248 11.866 -5.309 44.034 1.00 5.89 N
2174	ATOM 1730 CA ASN A 248 11.173 -4.603 45.108 1.00 9.22 C
2175	ATOM 1731 C ASN A 248 12.038 -3.517 45.786 1.00 9.83 C
2176	ATOM 1732 O ASN A 248 11.571 -2.412 46.104 1.00 5.00 O
2177	ATOM 1733 CB ASN A 248 10.700 -5.607 46.152 1.00 14.18 C
2178	ATOM 1734 CG ASN A 248 9.769 -4.988 47.146 1.00 17.32 C
2179	ATOM 1735 OD1 ASN A 248 8.593 -4.751 46.841 1.00 19.07 O
2180	ATOM 1736 ND2 ASN A 248 10.283 -4.690 48.339 1.00 15.52 N
2181	ATOM 1737 N ARG A 249 13.304 -3.840 46.020 1.00 19.09 N
2182	ATOM 1738 CA ARG A 249 14.214 -2.889 46.637 1.00 17.55 C
2183	ATOM 1739 C ARG A 249 14.407 -1.681 45.714 1.00 14.64 C
2184	ATOM 1740 O ARG A 249 14.314 -0.552 46.159 1.00 20.75 O
2185	ATOM 1741 CB ARG A 249 15.528 -3.584 47.002 1.00 21.39 C
2186	ATOM 1742 CG ARG A 249 15.286 -4.688 48.038 1.00 27.46 C
2187	ATOM 1743 CD ARG A 249 16.516 -5.518 48.396 1.00 31.88 C
2188	ATOM 1744 NE ARG A 249 17.351 -4.881 49.417 1.00 33.99 N
2189	ATOM 1745 CZ ARG A 249 17.527 -5.345 50.652 1.00 33.86 C
2190	ATOM 1746 NH1 ARG A 249 16.933 -6.467 51.050 1.00 34.91 N
2191	ATOM 1747 NH2 ARG A 249 18.280 -4.661 51.502 1.00 35.98 N
2192	ATOM 1748 N LEU A 250 14.567 -1.913 44.419 1.00 7.14 N
2193	ATOM 1749 CA LEU A 250 14.739 -0.813 43.470 1.00 11.99 C
2194	ATOM 1750 C LEU A 250 13.559 0.137 43.510 1.00 10.37 C
2195	ATOM 1751 O LEU A 250 13.737 1.333 43.726 1.00 23.28 O
2196	ATOM 1752 CB LEU A 250 14.930 -1.336 42.029 1.00 18.75 C
2197	ATOM 1753 CG LEU A 250 16.316 -1.915 41.690 1.00 15.72 C
2198	ATOM 1754 CD1 LEU A 250 16.357 -2.409 40.257 1.00 11.23 C
2199	ATOM 1755 CD2 LEU A 250 17.374 -0.832 41.922 1.00 12.44 C
2200	ATOM 1756 N SER A 251 12.361 -0.421 43.362 1.00 20.49 N
2201	ATOM 1757 CA SER A 251 11.110 0.341 43.343 1.00 19.98 C
2202	ATOM 1758 C SER A 251 10.664 0.944 44.666 1.00 21.47 C
2203	ATOM 1759 O SER A 251 10.154 2.076 44.690 1.00 12.97 O
2204	ATOM 1760 CB SER A 251 9.988 -0.531 42.795 1.00 10.08 C
2205	ATOM 1761 OG SER A 251 9.976 -1.770 43.470 1.00 10.29 O
2206	ATOM 1762 N SER A 252 10.808 0.176 45.746 1.00 9.01 N
2207	ATOM 1763 CA SER A 252 10.422 0.617 47.087 1.00 5.92 C
2208	ATOM 1764 C SER A 252 11.225 1.769 47.673 1.00 5.42 C
2209	ATOM 1765 O SER A 252 10.661 2.610 48.353 1.00 14.55 O
2210	ATOM 1766 CB SER A 252 10.481 -0.551 48.070 1.00 14.92 C
2211	ATOM 1767 OG SER A 252 9.459 -1.485 47.796 1.00 21.28 O
2212	ATOM 1768 N THR A 253 12.540 1.779 47.451 1.00 8.73 N
2213	ATOM 1769 CA THR A 253 13.414 2.819 47.988 1.00 7.37 C
2214	ATOM 1770 C THR A 253 13.594 4.008 47.082 1.00 8.27 C
2215	ATOM 1771 O THR A 253 14.268 4.976 47.458 1.00 14.30 O
2216	ATOM 1772 CB THR A 253 14.822 2.296 48.294 1.00 9.60 C
2217	ATOM 1773 OG1 THR A 253 15.399 1.728 47.109 1.00 13.78 O
2218	ATOM 1774 CG2 THR A 253 14.790 1.288 49.407 1.00 5.00 C
2219	ATOM 1775 N ALA A 254 13.040 3.919 45.878 1.00 5.97 N
2220	ATOM 1776 CA ALA A 254 13.152 4.986 44.903 1.00 5.00 C
2221	ATOM 1777 C ALA A 254 12.752 6.318 45.509 1.00 8.21 C
2222	ATOM 1778 O ALA A 254 11.953 6.365 46.441 1.00 21.48 O
2223	ATOM 1779 CB ALA A 254 12.283 4.677 43.726 1.00 6.28 C
2224	ATOM 1780 N THR A 255 13.335 7.397 44.994 1.00 15.74 N
2225	ATOM 1781 CA THR A 255 13.029 8.765 45.430 1.00 12.75 C
2226	ATOM 1782 C THR A 255 11.860 9.387 44.627 1.00 11.02 C
2227	ATOM 1783 O THR A 255 11.951 9.606 43.411 1.00 7.69 O
2228	ATOM 1784 CB THR A 255 14.270 9.662 45.309 1.00 9.19 C
2229	ATOM 1785 OG1 THR A 255 15.243 9.234 46.267 1.00 13.76 O
2230	ATOM 1786 CG2 THR A 255 13.915 11.124 45.561 1.00 8.53 C
2231	ATOM 1787 N TYR A 256 10.774 9.686 45.329 1.00 5.00 N
2232	ATOM 1788 CA TYR A 256 9.593 10.261 44.721 1.00 5.00 C
2233	ATOM 1789 C TYR A 256 9.821 11.583 43.975 1.00 5.00 C
2234	ATOM 1790 O TYR A 256 10.353 12.547 44.520 1.00 5.00 O
2235	ATOM 1791 CB TYR A 256 8.518 10.439 45.793 1.00 6.77 C
2236	ATOM 1792 CG TYR A 256 7.163 10.855 45.250 1.00 10.12 C
2237	ATOM 1793 CD1 TYR A 256 6.249 9.904 44.791 1.00 7.92 C
2238	ATOM 1794 CD2 TYR A 256 6.805 12.204 45.182 1.00 13.82 C
2239	ATOM 1795 CE1 TYR A 256 5.019 10.277 44.277 1.00 9.82 C
2240	ATOM 1796 CE2 TYR A 256 5.578 12.592 44.672 1.00 17.28 C
2241	ATOM 1797 CZ TYR A 256 4.686 11.623 44.218 1.00 16.90 C
2242	ATOM 1798 OH TYR A 256 3.469 12.025 43.705 1.00 20.48 O
2243	ATOM 1799 N LEU A 257 9.377 11.624 42.725 1.00 13.08 N
2244	ATOM 1800 CA LEU A 257 9.488 12.815 41.897 1.00 14.41 C
2245	ATOM 1801 C LEU A 257 8.098 13.388 41.579 1.00 14.18 C
2246	ATOM 1802 O LEU A 257 7.915 14.597 41.589 1.00 25.55 O
2247	ATOM 1803 CB LEU A 257 10.223 12.488 40.597 1.00 24.00 C
2248	ATOM 1804 CG LEU A 257 11.725 12.192 40.680 1.00 28.23 C
2249	ATOM 1805 CD1 LEU A 257 12.233 11.620 39.362 1.00 27.62 C
2250	ATOM 1806 CD2 LEU A 257 12.474 13.464 41.030 1.00 27.28 C
2251	ATOM 1807 N GLY A 258 7.133 12.520 41.289 1.00 5.00 N
2252	ATOM 1808 CA GLY A 258 5.785 12.956 40.972 1.00 5.00 C
2253	ATOM 1809 C GLY A 258 4.919 11.785 40.535 1.00 5.00 C
2254	ATOM 1810 O GLY A 258 5.296 10.622 40.718 1.00 5.00 O
2255	ATOM 1811 N SER A 259 3.791 12.093 39.896 1.00 5.00 N
2256	ATOM 1812 CA SER A 259 2.830 11.088 39.420 1.00 5.00 C
2257	ATOM 1813 C SER A 259 3.482 9.867 38.768 1.00 5.00 C
2258	ATOM 1814 O SER A 259 4.321 10.003 37.872 1.00 14.66 O
2259	ATOM 1815 CB SER A 259 1.848 11.747 38.439 1.00 10.89 C
2260	ATOM 1816 OG SER A 259 0.886 10.826 37.935 1.00 13.88 O
2261	ATOM 1817 N SER A 260 3.067 8.675 39.178 1.00 5.00 N
2262	ATOM 1818 CA SER A 260 3.640 7.441 38.616 1.00 5.00 C
2263	ATOM 1819 C SER A 260 3.390 7.221 37.119 1.00 5.00 C
2264	ATOM 1820 O SER A 260 4.154 6.540 36.451 1.00 13.52 O
2265	ATOM 1821 CB SER A 260 3.182 6.214 39.401 1.00 10.17 C
2266	ATOM 1822 OG SER A 260 1.766 6.164 39.508 1.00 14.46 O
2267	ATOM 1823 N PHE A 261 2.317 7.792 36.589 1.00 14.61 N
2268	ATOM 1824 CA PHE A 261 2.018 7.643 35.171 1.00 12.47 C
2269	ATOM 1825 C PHE A 261 3.145 8.337 34.386 1.00 13.05 C
2270	ATOM 1826 O PHE A 261 3.272 8.173 33.175 1.00 10.33 O
2271	ATOM 1827 CB PHE A 261 0.655 8.276 34.861 1.00 5.00 C
2272	ATOM 1828 CG PHE A 261 0.271 8.228 33.405 1.00 5.00 C
2273	ATOM 1829 CD1 PHE A 261 0.678 9.216 32.533 1.00 5.00 C
2274	ATOM 1830 CD2 PHE A 261 -0.480 7.178 32.906 1.00 5.66 C
2275	ATOM 1831 CE1 PHE A 261 0.353 9.158 31.199 1.00 5.00 C
2276	ATOM 1832 CE2 PHE A 261 -0.809 7.119 31.553 1.00 6.86 C
2277	ATOM 1833 CZ PHE A 261 -0.387 8.111 30.705 1.00 6.11 C
2278	ATOM 1834 N TYR A 262 3.934 9.149 35.082 1.00 5.00 N
2279	ATOM 1835 CA TYR A 262 5.029 9.848 34.445 1.00 5.00 C
2280	ATOM 1836 C TYR A 262 6.366 9.432 35.027 1.00 5.00 C
2281	ATOM 1837 O TYR A 262 7.329 9.346 34.291 1.00 10.73 O
2282	ATOM 1838 CB TYR A 262 4.855 11.351 34.594 1.00 8.05 C
2283	ATOM 1839 CG TYR A 262 3.631 11.914 33.923 1.00 12.70 C
2284	ATOM 1840 CD1 TYR A 262 3.549 12.011 32.533 1.00 18.98 C
2285	ATOM 1841 CD2 TYR A 262 2.560 12.374 34.670 1.00 14.82 C
2286	ATOM 1842 CE1 TYR A 262 2.428 12.556 31.902 1.00 17.07 C
2287	ATOM 1843 CE2 TYR A 262 1.426 12.925 34.051 1.00 19.38 C
2288	ATOM 1844 CZ TYR A 262 1.364 13.011 32.667 1.00 19.13 C
2289	ATOM 1845 OH TYR A 262 0.221 13.520 32.062 1.00 22.41 O
2290	ATOM 1846 N TYR A 263 6.405 9.117 36.325 1.00 5.00 N
2291	ATOM 1847 CA TYR A 263 7.645 8.737 37.017 1.00 5.00 C
2292	ATOM 1848 C TYR A 263 7.736 7.367 37.671 1.00 5.00 C
2293	ATOM 1849 O TYR A 263 8.764 7.049 38.288 1.00 7.77 O
2294	ATOM 1850 CB TYR A 263 7.939 9.720 38.132 1.00 5.00 C
2295	ATOM 1851 CG TYR A 263 7.904 11.137 37.693 1.00 8.29 C
2296	ATOM 1852 CD1 TYR A 263 9.049 11.760 37.213 1.00 5.00 C
2297	ATOM 1853 CD2 TYR A 263 6.726 11.874 37.776 1.00 5.00 C
2298	ATOM 1854 CE1 TYR A 263 9.015 13.074 36.835 1.00 5.00 C
2299	ATOM 1855 CE2 TYR A 263 6.689 13.191 37.394 1.00 5.00 C
2300	ATOM 1856 CZ TYR A 263 7.836 13.785 36.926 1.00 5.00 C
2301	ATOM 1857 OH TYR A 263 7.814 15.103 36.550 1.00 7.05 O
2302	ATOM 1858 N GLY A 264 6.707 6.546 37.543 1.00 5.00 N
2303	ATOM 1859 CA GLY A 264 6.733 5.275 38.226 1.00 5.00 C
2304	ATOM 1860 C GLY A 264 6.848 5.575 39.720 1.00 5.00 C
2305	ATOM 1861 O GLY A 264 6.323 6.567 40.242 1.00 5.00 O
2306	ATOM 1862 N LYS A 265 7.574 4.725 40.421 1.00 16.12 N
2307	ATOM 1863 CA LYS A 265 7.775 4.909 41.852 1.00 18.56 C
2308	ATOM 1864 C LYS A 265 8.785 6.027 42.191 1.00 16.31 C
2309	ATOM 1865 O LYS A 265 8.838 6.499 43.329 1.00 15.33 O
2310	ATOM 1866 CB LYS A 265 8.170 3.567 42.466 1.00 10.28 C
2311	ATOM 1867 CG LYS A 265 7.045 2.562 42.371 1.00 11.27 C
2312	ATOM 1868 CD LYS A 265 5.861 2.996 43.248 1.00 14.72 C
2313	ATOM 1869 CE LYS A 265 6.163 2.800 44.764 1.00 20.83 C
2314	ATOM 1870 NZ LYS A 265 7.458 3.393 45.274 1.00 18.45 N
2315	ATOM 1871 N GLY A 266 9.568 6.433 41.190 1.00 13.02 N
2316	ATOM 1872 CA GLY A 266 10.553 7.489 41.347 1.00 10.31 C
2317	ATOM 1873 C GLY A 266 11.914 7.184 40.733 1.00 9.18 C
2318	ATOM 1874 O GLY A 266 12.112 6.150 40.085 1.00 5.00 O
2319	ATOM 1875 N LEU A 267 12.845 8.116 40.919 1.00 5.00 N
2320	ATOM 1876 CA LEU A 267 14.221 7.974 40.462 1.00 5.00 C
2321	ATOM 1877 C LEU A 267 14.850 6.923 41.395 1.00 5.00 C
2322	ATOM 1878 O LEU A 267 14.590 6.942 42.594 1.00 5.00 O
2323	ATOM 1879 CB LEU A 267 14.931 9.320 40.620 1.00 5.00 C
2324	ATOM 1880 CG LEU A 267 16.427 9.466 40.347 1.00 5.00 C
2325	ATOM 1881 CD1 LEU A 267 16.697 9.182 38.873 1.00 5.00 C
2326	ATOM 1882 CD2 LEU A 267 16.862 10.880 40.725 1.00 5.00 C
2327	ATOM 1883 N ILE A 268 15.671 6.017 40.868 1.00 8.96 N
2328	ATOM 1884 CA ILE A 268 16.261 4.968 41.700 1.00 5.00 C
2329	ATOM 1885 C ILE A 268 17.353 5.412 42.643 1.00 6.07 C
2330	ATOM 1886 O ILE A 268 17.985 6.444 42.436 1.00 5.00 O
2331	ATOM 1887 CB ILE A 268 16.793 3.812 40.876 1.00 5.00 C
2332	ATOM 1888 CG1 ILE A 268 17.929 4.280 39.974 1.00 6.22 C
2333	ATOM 1889 CG2 ILE A 268 15.676 3.219 40.070 1.00 8.05 C
2334	ATOM 1890 CD1 ILE A 268 18.885 3.175 39.593 1.00 6.31 C
2335	ATOM 1891 N ASN A 269 17.570 4.601 43.680 1.00 24.64 N
2336	ATOM 1892 CA ASN A 269 18.587 4.862 44.699 1.00 24.15 C
2337	ATOM 1893 C ASN A 269 19.254 3.551 45.148 1.00 25.42 C
2338	ATOM 1894 O ASN A 269 18.826 2.914 46.127 1.00 10.66 O
2339	ATOM 1895 CB ASN A 269 17.969 5.580 45.905 1.00 5.00 C
2340	ATOM 1896 CG ASN A 269 19.020 6.062 46.883 1.00 5.95 C
2341	ATOM 1897 OD1 ASN A 269 20.200 5.773 46.722 1.00 10.27 O
2342	ATOM 1898 ND2 ASN A 269 18.606 6.815 47.884 1.00 9.73 N
2343	ATOM 1899 N VAL A 270 20.349 3.192 44.485 1.00 7.19 N
2344	ATOM 1900 CA VAL A 270 21.041 1.946 44.803 1.00 9.68 C
2345	ATOM 1901 C VAL A 270 21.590 1.838 46.237 1.00 6.42 C
2346	ATOM 1902 O VAL A 270 21.870 0.728 46.722 1.00 5.99 O
2347	ATOM 1903 CB VAL A 270 22.171 1.603 43.762 1.00 10.12 C
2348	ATOM 1904 CG1 VAL A 270 21.855 2.189 42.405 1.00 12.64 C
2349	ATOM 1905 CG2 VAL A 270 23.505 2.084 44.237 1.00 15.33 C
2350	ATOM 1906 N GLU A 271 21.749 2.971 46.911 1.00 5.00 N
2351	ATOM 1907 CA GLU A 271 22.270 2.954 48.271 1.00 5.00 C
2352	ATOM 1908 C GLU A 271 21.208 2.504 49.242 1.00 5.00 C
2353	ATOM 1909 O GLU A 271 21.450 1.645 50.081 1.00 10.64 O
2354	ATOM 1910 CB GLU A 271 22.798 4.312 48.680 1.00 5.04 C
2355	ATOM 1911 CG GLU A 271 23.194 4.377 50.137 1.00 12.81 C
2356	ATOM 1912 CD GLU A 271 23.704 5.744 50.527 1.00 15.06 C
2357	ATOM 1913 OE1 GLU A 271 23.061 6.745 50.113 1.00 17.39 O
2358	ATOM 1914 OE2 GLU A 271 24.744 5.817 51.235 1.00 14.97 O
2359	ATOM 1915 N ALA A 272 20.014 3.057 49.092 1.00 5.00 N
2360	ATOM 1916 CA ALA A 272 18.900 2.700 49.948 1.00 5.00 C
2361	ATOM 1917 C ALA A 272 18.443 1.293 49.567 1.00 5.00 C
2362	ATOM 1918 O ALA A 272 18.107 0.495 50.424 1.00 10.96 O
2363	ATOM 1919 CB ALA A 272 17.770 3.701 49.771 1.00 5.00 C
2364	ATOM 1920 N ALA A 273 18.445 0.992 48.274 1.00 5.00 N
2365	ATOM 1921 CA ALA A 273 18.039 -0.317 47.791 1.00 5.00 C
2366	ATOM 1922 C ALA A 273 18.929 -1.420 48.350 1.00 5.00 C
2367	ATOM 1923 O ALA A 273 18.440 -2.343 49.001 1.00 9.03 O
2368	ATOM 1924 CB ALA A 273 18.077 -0.338 46.277 1.00 5.00 C
2369	ATOM 1925 N ALA A 274 20.238 -1.294 48.139 1.00 5.00 N
2370	ATOM 1926 CA ALA A 274 21.206 -2.292 48.585 1.00 5.00 C
2371	ATOM 1927 C ALA A 274 21.494 -2.295 50.080 1.00 5.00 C
2372	ATOM 1928 O ALA A 274 22.397 -2.994 50.528 1.00 5.00 O
2373	ATOM 1929 CB ALA A 274 22.486 -2.139 47.810 1.00 5.00 C
2374	ATOM 1930 N GLN A 275 20.704 -1.530 50.833 1.00 12.78 N
2375	ATOM 1931 CA GLN A 275 20.806 -1.391 52.289 1.00 15.94 C
2376	ATOM 1932 C GLN A 275 20.957 -2.702 53.053 1.00 18.48 C
2377	ATOM 1933 O GLN A 275 20.092 -3.582 52.894 1.00 36.46 O
2378	ATOM 1934 CB GLN A 275 19.563 -0.672 52.832 1.00 32.71 C
2379	ATOM 1935 CG GLN A 275 19.753 0.787 53.251 1.00 37.98 C
2380	ATOM 1936 CD GLN A 275 18.510 1.369 53.926 1.00 42.93 C
2381	ATOM 1937 OE1 GLN A 275 17.604 0.628 54.326 1.00 43.46 O
2382	ATOM 1938 NE2 GLN A 275 18.463 2.706 54.061 1.00 47.13 N
2383	ATOM 1939 OXT GLN A 275 21.893 -2.810 53.868 1.00 33.61 O
2384	TER 1940 GLN A 275
2385	HETATM 1941 NA NA A 300 6.785 -3.676 33.554 1.00 30.19 NA
2386	HETATM 1942 NA NA A 301 37.110 3.474 32.936 1.00 13.75 NA
2387	HETATM 1943 O HOH A 302 14.794 -2.431 17.539 1.00 15.53 O
2388	HETATM 1944 O HOH A 303 10.787 -2.643 26.039 1.00 9.34 O
2389	HETATM 1945 O HOH A 304 12.464 -8.086 36.394 1.00 2.00 O
2390	HETATM 1946 O HOH A 305 11.441 -14.344 45.629 1.00 3.79 O
2391	HETATM 1947 O HOH A 306 11.092 -21.963 38.600 1.00 24.92 O
2392	HETATM 1948 O HOH A 307 23.764 0.353 50.817 1.00 7.62 O
2393	HETATM 1949 O HOH A 308 30.056 12.829 38.678 1.00 7.90 O
2394	HETATM 1950 O HOH A 309 38.164 13.761 39.395 1.00 26.58 O
2395	HETATM 1951 O HOH A 310 33.087 -5.807 33.781 1.00 6.37 O
2396	HETATM 1952 O HOH A 311 29.697 -14.561 16.654 1.00 3.02 O
2397	HETATM 1953 O HOH A 312 24.757 -6.850 22.543 1.00 3.86 O
2398	HETATM 1954 O HOH A 313 23.582 4.099 27.740 1.00 2.00 O
2399	HETATM 1955 O HOH A 314 19.949 13.722 20.923 1.00 35.73 O
2400	HETATM 1956 O HOH A 315 21.118 15.660 31.717 1.00 19.08 O
2401	HETATM 1957 O HOH A 316 10.448 15.873 38.715 1.00 2.00 O
2402	HETATM 1958 O HOH A 317 7.602 9.548 40.991 1.00 9.64 O
2403	HETATM 1959 O HOH A 318 1.063 7.941 41.731 1.00 4.22 O
2404	HETATM 1960 O HOH A 319 7.813 8.698 31.675 1.00 2.00 O
2405	HETATM 1961 O HOH A 320 17.861 -11.642 13.641 1.00 12.20 O
2406	HETATM 1962 O HOH A 321 25.943 -15.272 7.056 1.00 9.12 O
2407	HETATM 1963 O HOH A 322 33.292 -8.612 32.261 1.00 11.59 O
2408	HETATM 1964 O HOH A 323 33.775 -4.702 31.450 1.00 20.59 O
2409	HETATM 1965 O HOH A 324 36.780 -2.386 37.030 1.00 5.06 O
2410	HETATM 1966 O HOH A 325 40.265 5.020 26.524 1.00 5.67 O
2411	HETATM 1967 O HOH A 326 40.979 -1.162 17.058 1.00 12.51 O
2412	HETATM 1968 O HOH A 327 9.810 16.340 36.229 1.00 5.50 O
2413	HETATM 1969 O HOH A 328 10.299 4.151 21.365 1.00 8.67 O
2414	CONECT 14 1942
2415	CONECT 298 1942
2416	CONECT 299 1942
2417	CONECT 515 1942
2418	CONECT 534 1942
2419	CONECT 546 1942
2420	CONECT 557 1942
2421	CONECT 1154 1941
2422	CONECT 1168 1941
2423	CONECT 1194 1941
2424	CONECT 1516 1521
2425	CONECT 1521 1516 1522
2426	CONECT 1522 1521 1523 1525
2427	CONECT 1523 1522 1524
2428	CONECT 1524 1523 1538
2429	CONECT 1525 1522 1526 1546
2430	CONECT 1526 1525
2431	CONECT 1527 1528 1539
2432	CONECT 1528 1527 1529 1538
2433	CONECT 1529 1528 1530
2434	CONECT 1530 1529 1531 1533
2435	CONECT 1531 1530 1532 1542
2436	CONECT 1532 1531 1535 1545
2437	CONECT 1533 1530 1534
2438	CONECT 1534 1533 1535
2439	CONECT 1535 1532 1534
2440	CONECT 1536 1538
2441	CONECT 1537 1538
2442	CONECT 1538 1524 1528 1536 1537
2443	CONECT 1539 1527 1540 1541
2444	CONECT 1540 1539
2445	CONECT 1541 1539
2446	CONECT 1542 1531 1543
2447	CONECT 1543 1542 1544
2448	CONECT 1544 1543 1545
2449	CONECT 1545 1532 1544
2450	CONECT 1546 1525
2451	CONECT 1941 1154 1168 1194
2452	CONECT 1942 14 298 299 515
2453	CONECT 1942 534 546 557
2454	MASTER 336 0 3 8 8 0 6 6 1968 1 40 22
2455	END

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