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Ticket #8207: 4hhb-max-hemoglobin.pdb

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1	HEADER OXYGEN TRANSPORT 07-MAR-84 4HHB
2	TITLE THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS
3	TITLE 2 RESOLUTION
4	COMPND MOL_ID: 1;
5	COMPND 2 MOLECULE: HEMOGLOBIN (DEOXY) (ALPHA CHAIN);
6	COMPND 3 CHAIN: A, C;
7	COMPND 4 ENGINEERED: YES;
8	COMPND 5 MOL_ID: 2;
9	COMPND 6 MOLECULE: HEMOGLOBIN (DEOXY) (BETA CHAIN);
10	COMPND 7 CHAIN: B, D;
11	COMPND 8 ENGINEERED: YES
12	SOURCE MOL_ID: 1;
13	SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
14	SOURCE 3 ORGANISM_COMMON: HUMAN;
15	SOURCE 4 ORGANISM_TAXID: 9606;
16	SOURCE 5 MOL_ID: 2;
17	SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
18	SOURCE 7 ORGANISM_COMMON: HUMAN;
19	SOURCE 8 ORGANISM_TAXID: 9606
20	KEYWDS OXYGEN TRANSPORT
21	EXPDTA X-RAY DIFFRACTION
22	AUTHOR G.FERMI,M.F.PERUTZ
23	REVDAT 5 13-JUL-11 4HHB 1 VERSN
24	REVDAT 4 24-FEB-09 4HHB 1 VERSN
25	REVDAT 3 01-APR-03 4HHB 1 JRNL
26	REVDAT 2 15-OCT-89 4HHB 3 MTRIX
27	REVDAT 1 17-JUL-84 4HHB 0
28	SPRSDE 17-JUL-84 4HHB 1HHB
29	JRNL AUTH G.FERMI,M.F.PERUTZ,B.SHAANAN,R.FOURME
30	JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 A
31	JRNL TITL 2 RESOLUTION
32	JRNL REF J.MOL.BIOL. V. 175 159 1984
33	JRNL REFN ISSN 0022-2836
34	JRNL PMID 6726807
35	JRNL DOI 10.1016/0022-2836(84)90472-8
36	REMARK 1
37	REMARK 1 REFERENCE 1
38	REMARK 1 AUTH M.F.PERUTZ,S.S.HASNAIN,P.J.DUKE,J.L.SESSLER,J.E.HAHN
39	REMARK 1 TITL STEREOCHEMISTRY OF IRON IN DEOXYHAEMOGLOBIN
40	REMARK 1 REF NATURE V. 295 535 1982
41	REMARK 1 REFN ISSN 0028-0836
42	REMARK 1 REFERENCE 2
43	REMARK 1 AUTH G.FERMI,M.F.PERUTZ
44	REMARK 1 REF HAEMOGLOBIN AND MYOGLOBIN. V. 2 1981
45	REMARK 1 REF 2 ATLAS OF MOLECULAR
46	REMARK 1 REF 3 STRUCTURES IN BIOLOGY
47	REMARK 1 PUBL OXFORD UNIVERSITY PRESS
48	REMARK 1 REFN
49	REMARK 1 REFERENCE 3
50	REMARK 1 AUTH M.F.PERUTZ
51	REMARK 1 TITL REGULATION OF OXYGEN AFFINITY OF HEMOGLOBIN. INFLUENCE OF
52	REMARK 1 TITL 2 STRUCTURE OF THE GLOBIN ON THE HEME IRON
53	REMARK 1 REF ANNU.REV.BIOCHEM. V. 48 327 1979
54	REMARK 1 REFN ISSN 0066-4154
55	REMARK 1 REFERENCE 4
56	REMARK 1 AUTH L.F.TENEYCK,A.ARNONE
57	REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN DEOXYHEMOGLOBIN
58	REMARK 1 TITL 2 AT 2.5 ANGSTROMS RESOLUTION, I.X-RAY ANALYSIS
59	REMARK 1 REF J.MOL.BIOL. V. 100 3 1976
60	REMARK 1 REFN ISSN 0022-2836
61	REMARK 1 REFERENCE 5
62	REMARK 1 AUTH G.FERMI
63	REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
64	REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 2.5 ANGSTROMS RESOLUTION, REFINEMENT OF
65	REMARK 1 TITL 3 THE ATOMIC MODEL
66	REMARK 1 REF J.MOL.BIOL. V. 97 237 1975
67	REMARK 1 REFN ISSN 0022-2836
68	REMARK 1 REFERENCE 6
69	REMARK 1 AUTH H.MUIRHEAD,J.GREER
70	REMARK 1 TITL THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN
71	REMARK 1 TITL 2 DEOXYHAEMOGLOBIN AT 3.5 ANGSTROMS RESOLUTION
72	REMARK 1 REF NATURE V. 228 516 1970
73	REMARK 1 REFN ISSN 0028-0836
74	REMARK 1 REFERENCE 7
75	REMARK 1 EDIT M.O.DAYHOFF
76	REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 56 1972
77	REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
78	REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
79	REMARK 1 REFN
80	REMARK 1 REFERENCE 8
81	REMARK 1 EDIT M.O.DAYHOFF
82	REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 64 1972
83	REMARK 1 REF 2 AND STRUCTURE (DATA SECTION)
84	REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
85	REMARK 1 REFN
86	REMARK 2
87	REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
88	REMARK 3
89	REMARK 3 REFINEMENT.
90	REMARK 3 PROGRAM : NULL
91	REMARK 3 AUTHORS : NULL
92	REMARK 3
93	REMARK 3 DATA USED IN REFINEMENT.
94	REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
95	REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
96	REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
97	REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
98	REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
99	REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
100	REMARK 3 NUMBER OF REFLECTIONS : NULL
101	REMARK 3
102	REMARK 3 FIT TO DATA USED IN REFINEMENT.
103	REMARK 3 CROSS-VALIDATION METHOD : NULL
104	REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
105	REMARK 3 R VALUE (WORKING SET) : 0.135
106	REMARK 3 FREE R VALUE : NULL
107	REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
108	REMARK 3 FREE R VALUE TEST SET COUNT : NULL
109	REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
110	REMARK 3
111	REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
112	REMARK 3 TOTAL NUMBER OF BINS USED : NULL
113	REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
114	REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
115	REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
116	REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
117	REMARK 3 BIN R VALUE (WORKING SET) : NULL
118	REMARK 3 BIN FREE R VALUE : NULL
119	REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
120	REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
121	REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
122	REMARK 3
123	REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
124	REMARK 3 PROTEIN ATOMS : 4384
125	REMARK 3 NUCLEIC ACID ATOMS : 0
126	REMARK 3 HETEROGEN ATOMS : 174
127	REMARK 3 SOLVENT ATOMS : 221
128	REMARK 3
129	REMARK 3 B VALUES.
130	REMARK 3 FROM WILSON PLOT (A**2) : NULL
131	REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
132	REMARK 3 OVERALL ANISOTROPIC B VALUE.
133	REMARK 3 B11 (A**2) : NULL
134	REMARK 3 B22 (A**2) : NULL
135	REMARK 3 B33 (A**2) : NULL
136	REMARK 3 B12 (A**2) : NULL
137	REMARK 3 B13 (A**2) : NULL
138	REMARK 3 B23 (A**2) : NULL
139	REMARK 3
140	REMARK 3 ESTIMATED COORDINATE ERROR.
141	REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
142	REMARK 3 ESD FROM SIGMAA (A) : NULL
143	REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
144	REMARK 3
145	REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
146	REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
147	REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
148	REMARK 3
149	REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
150	REMARK 3 BOND LENGTHS (A) : NULL
151	REMARK 3 BOND ANGLES (DEGREES) : NULL
152	REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
153	REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
154	REMARK 3
155	REMARK 3 ISOTROPIC THERMAL MODEL : NULL
156	REMARK 3
157	REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
158	REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
159	REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
160	REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
161	REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
162	REMARK 3
163	REMARK 3 NCS MODEL : NULL
164	REMARK 3
165	REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
166	REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
167	REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
168	REMARK 3
169	REMARK 3 PARAMETER FILE 1 : NULL
170	REMARK 3 TOPOLOGY FILE 1 : NULL
171	REMARK 3
172	REMARK 3 OTHER REFINEMENT REMARKS:
173	REMARK 3 THE COORDINATES GIVEN HERE ARE IN THE ORTHOGONAL ANGSTROM
174	REMARK 3 SYSTEM STANDARD FOR HEMOGLOBINS. THE Y AXIS IS THE
175	REMARK 3 (NON CRYSTALLOGRAPHIC) MOLECULAR DIAD AND THE X AXIS IS THE
176	REMARK 3 PSEUDO DIAD WHICH RELATES THE ALPHA-1 AND BETA-1 CHAINS.
177	REMARK 3 THE TRANSFORMATION GIVEN IN THE MTRIX RECORDS BELOW
178	REMARK 3 WILL GENERATE COORDINATES FOR THE C AND D CHAINS FROM
179	REMARK 3 THE A AND B CHAINS RESPECTIVELY.
180	REMARK 4
181	REMARK 4 4HHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
182	REMARK 100
183	REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
184	REMARK 200
185	REMARK 200 EXPERIMENTAL DETAILS
186	REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
187	REMARK 200 DATE OF DATA COLLECTION : NULL
188	REMARK 200 TEMPERATURE (KELVIN) : NULL
189	REMARK 200 PH : NULL
190	REMARK 200 NUMBER OF CRYSTALS USED : NULL
191	REMARK 200
192	REMARK 200 SYNCHROTRON (Y/N) : NULL
193	REMARK 200 RADIATION SOURCE : NULL
194	REMARK 200 BEAMLINE : NULL
195	REMARK 200 X-RAY GENERATOR MODEL : NULL
196	REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
197	REMARK 200 WAVELENGTH OR RANGE (A) : NULL
198	REMARK 200 MONOCHROMATOR : NULL
199	REMARK 200 OPTICS : NULL
200	REMARK 200
201	REMARK 200 DETECTOR TYPE : NULL
202	REMARK 200 DETECTOR MANUFACTURER : NULL
203	REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
204	REMARK 200 DATA SCALING SOFTWARE : NULL
205	REMARK 200
206	REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
207	REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
208	REMARK 200 RESOLUTION RANGE LOW (A) : NULL
209	REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
210	REMARK 200
211	REMARK 200 OVERALL.
212	REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
213	REMARK 200 DATA REDUNDANCY : NULL
214	REMARK 200 R MERGE (I) : NULL
215	REMARK 200 R SYM (I) : NULL
216	REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
217	REMARK 200
218	REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
219	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
220	REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
221	REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
222	REMARK 200 DATA REDUNDANCY IN SHELL : NULL
223	REMARK 200 R MERGE FOR SHELL (I) : NULL
224	REMARK 200 R SYM FOR SHELL (I) : NULL
225	REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
226	REMARK 200
227	REMARK 200 DIFFRACTION PROTOCOL: NULL
228	REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
229	REMARK 200 SOFTWARE USED: NULL
230	REMARK 200 STARTING MODEL: NULL
231	REMARK 200
232	REMARK 200 REMARK: NULL
233	REMARK 280
234	REMARK 280 CRYSTAL
235	REMARK 280 SOLVENT CONTENT, VS (%): 45.48
236	REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
237	REMARK 280
238	REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
239	REMARK 285
240	REMARK 285 THE ENTRY COORDINATES
241	REMARK 285 ARE NOT PRESENTED IN THE STANDARD CRYSTAL FRAME.
242	REMARK 290
243	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
244	REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
245	REMARK 290
246	REMARK 290 SYMOP SYMMETRY
247	REMARK 290 NNNMMM OPERATOR
248	REMARK 290 1555 X,Y,Z
249	REMARK 290 2555 -X,Y+1/2,-Z
250	REMARK 290
251	REMARK 290 WHERE NNN -> OPERATOR NUMBER
252	REMARK 290 MMM -> TRANSLATION VECTOR
253	REMARK 290
254	REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
255	REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
256	REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
257	REMARK 290 RELATED MOLECULES.
258	REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
259	REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
260	REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
261	REMARK 290 SMTRY1 2 -0.949456 -0.312801 -0.025883 -6.64347
262	REMARK 290 SMTRY2 2 -0.312858 0.936202 0.160212 41.12228
263	REMARK 290 SMTRY3 2 -0.025884 0.160188 -0.986745 3.40218
264	REMARK 290
265	REMARK 290 REMARK: NULL
266	REMARK 300
267	REMARK 300 BIOMOLECULE: 1
268	REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
269	REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
270	REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
271	REMARK 300 BURIED SURFACE AREA.
272	REMARK 350
273	REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
274	REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
275	REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
276	REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
277	REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
278	REMARK 350
279	REMARK 350 BIOMOLECULE: 1
280	REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
281	REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
282	REMARK 350 SOFTWARE USED: PISA
283	REMARK 350 TOTAL BURIED SURFACE AREA: 11630 ANGSTROM**2
284	REMARK 350 SURFACE AREA OF THE COMPLEX: 24010 ANGSTROM**2
285	REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL
286	REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
287	REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
288	REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
289	REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
290	REMARK 500
291	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
292	REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
293	REMARK 500
294	REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
295	REMARK 500
296	REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
297	REMARK 500 C VAL B 1 CA HIS B 2 1.63
298	REMARK 500 C PHE D 45 CA GLY D 46 1.78
299	REMARK 500 CB THR D 4 OE2 GLU D 6 2.00
300	REMARK 500 NZ LYS D 66 O1A HEM D 148 2.06
301	REMARK 500 OD2 ASP D 73 O HOH D 174 2.10
302	REMARK 500 OG1 THR D 4 OE2 GLU D 6 2.19
303	REMARK 500
304	REMARK 500 REMARK: NULL
305	REMARK 500
306	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
307	REMARK 500 SUBTOPIC: CLOSE CONTACTS
308	REMARK 500
309	REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
310	REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
311	REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
312	REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
313	REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
314	REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
315	REMARK 500
316	REMARK 500 DISTANCE CUTOFF:
317	REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
318	REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
319	REMARK 500
320	REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
321	REMARK 500 OD2 ASP C 85 O HOH B 204 2657 1.41
322	REMARK 500 O HOH B 204 O HOH C 161 2647 2.02
323	REMARK 500
324	REMARK 500 REMARK: NULL
325	REMARK 500
326	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
327	REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
328	REMARK 500
329	REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
330	REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
331	REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
332	REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
333	REMARK 500
334	REMARK 500 STANDARD TABLE:
335	REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
336	REMARK 500
337	REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
338	REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
339	REMARK 500
340	REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
341	REMARK 500 VAL A 1 N VAL A 1 CA -0.295
342	REMARK 500 VAL A 1 CA VAL A 1 CB 0.299
343	REMARK 500 VAL A 1 CB VAL A 1 CG1 -0.206
344	REMARK 500 VAL A 1 CB VAL A 1 CG2 -0.283
345	REMARK 500 LEU A 2 CA LEU A 2 C 0.249
346	REMARK 500 SER A 3 N SER A 3 CA 0.167
347	REMARK 500 SER A 3 CB SER A 3 OG -0.132
348	REMARK 500 LEU A 2 C SER A 3 N -0.320
349	REMARK 500 PRO A 4 N PRO A 4 CA -0.149
350	REMARK 500 PRO A 4 CA PRO A 4 CB 0.202
351	REMARK 500 SER A 3 C PRO A 4 N 0.282
352	REMARK 500 ALA A 5 N ALA A 5 CA -0.130
353	REMARK 500 ALA A 5 CA ALA A 5 CB 0.247
354	REMARK 500 PRO A 4 C ALA A 5 N 0.257
355	REMARK 500 LYS A 7 N LYS A 7 CA 0.157
356	REMARK 500 THR A 8 CA THR A 8 CB 0.178
357	REMARK 500 THR A 8 CB THR A 8 OG1 -0.173
358	REMARK 500 THR A 8 CB THR A 8 CG2 -0.245
359	REMARK 500 THR A 8 CA THR A 8 C -0.174
360	REMARK 500 LYS A 7 C THR A 8 N 0.258
361	REMARK 500 THR A 8 C ASN A 9 N 0.179
362	REMARK 500 VAL A 10 CB VAL A 10 CG2 -0.179
363	REMARK 500 VAL A 10 CA VAL A 10 C 0.160
364	REMARK 500 LYS A 11 N LYS A 11 CA 0.131
365	REMARK 500 LYS A 11 CA LYS A 11 CB -0.137
366	REMARK 500 LYS A 11 CB LYS A 11 CG -0.196
367	REMARK 500 LYS A 11 CG LYS A 11 CD -0.206
368	REMARK 500 LYS A 11 CD LYS A 11 CE 0.454
369	REMARK 500 ALA A 12 N ALA A 12 CA -0.133
370	REMARK 500 ALA A 12 C ALA A 12 O 0.225
371	REMARK 500 ALA A 13 CA ALA A 13 C 0.201
372	REMARK 500 TRP A 14 CA TRP A 14 CB 0.291
373	REMARK 500 TRP A 14 CB TRP A 14 CG -0.274
374	REMARK 500 TRP A 14 CG TRP A 14 CD1 0.306
375	REMARK 500 TRP A 14 CD1 TRP A 14 NE1 0.158
376	REMARK 500 TRP A 14 NE1 TRP A 14 CE2 -0.234
377	REMARK 500 TRP A 14 CE2 TRP A 14 CZ2 -0.243
378	REMARK 500 TRP A 14 CE2 TRP A 14 CD2 0.221
379	REMARK 500 TRP A 14 CH2 TRP A 14 CZ2 -0.217
380	REMARK 500 GLY A 15 CA GLY A 15 C 0.182
381	REMARK 500 GLY A 15 C GLY A 15 O 0.437
382	REMARK 500 LYS A 16 CB LYS A 16 CG 0.164
383	REMARK 500 LYS A 16 CG LYS A 16 CD 0.488
384	REMARK 500 LYS A 16 CD LYS A 16 CE 0.410
385	REMARK 500 LYS A 16 C LYS A 16 O -0.149
386	REMARK 500 GLY A 15 C LYS A 16 N -0.418
387	REMARK 500 VAL A 17 N VAL A 17 CA -0.191
388	REMARK 500 VAL A 17 CA VAL A 17 CB -0.168
389	REMARK 500 VAL A 17 CA VAL A 17 C 0.432
390	REMARK 500 VAL A 17 C VAL A 17 O -0.483
391	REMARK 500
392	REMARK 500 THIS ENTRY HAS 1271 BOND DEVIATIONS.
393	REMARK 500
394	REMARK 500 REMARK: NULL
395	REMARK 500
396	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
397	REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
398	REMARK 500
399	REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
400	REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
401	REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
402	REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
403	REMARK 500
404	REMARK 500 STANDARD TABLE:
405	REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
406	REMARK 500
407	REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
408	REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
409	REMARK 500
410	REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
411	REMARK 500 VAL A 1 CG1 - CB - CG2 ANGL. DEV. = 27.5 DEGREES
412	REMARK 500 VAL A 1 CA - CB - CG2 ANGL. DEV. = -25.9 DEGREES
413	REMARK 500 LEU A 2 N - CA - CB ANGL. DEV. = -17.9 DEGREES
414	REMARK 500 LEU A 2 CB - CG - CD1 ANGL. DEV. = 13.0 DEGREES
415	REMARK 500 LEU A 2 CA - C - O ANGL. DEV. = -21.8 DEGREES
416	REMARK 500 VAL A 1 CA - C - N ANGL. DEV. = -13.3 DEGREES
417	REMARK 500 VAL A 1 O - C - N ANGL. DEV. = 12.7 DEGREES
418	REMARK 500 LEU A 2 C - N - CA ANGL. DEV. = -20.6 DEGREES
419	REMARK 500 SER A 3 N - CA - CB ANGL. DEV. = -9.7 DEGREES
420	REMARK 500 SER A 3 CA - C - O ANGL. DEV. = 15.9 DEGREES
421	REMARK 500 LEU A 2 O - C - N ANGL. DEV. = 30.2 DEGREES
422	REMARK 500 PRO A 4 CB - CA - C ANGL. DEV. = -30.7 DEGREES
423	REMARK 500 PRO A 4 CA - CB - CG ANGL. DEV. = -15.7 DEGREES
424	REMARK 500 PRO A 4 N - CD - CG ANGL. DEV. = -12.4 DEGREES
425	REMARK 500 SER A 3 O - C - N ANGL. DEV. = -14.6 DEGREES
426	REMARK 500 PRO A 4 C - N - CA ANGL. DEV. = -14.1 DEGREES
427	REMARK 500 PRO A 4 C - N - CD ANGL. DEV. = -18.4 DEGREES
428	REMARK 500 ALA A 5 CB - CA - C ANGL. DEV. = -10.8 DEGREES
429	REMARK 500 PRO A 4 O - C - N ANGL. DEV. = -9.9 DEGREES
430	REMARK 500 ASP A 6 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
431	REMARK 500 ASP A 6 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
432	REMARK 500 LYS A 7 N - CA - CB ANGL. DEV. = -13.5 DEGREES
433	REMARK 500 LYS A 7 CD - CE - NZ ANGL. DEV. = -27.4 DEGREES
434	REMARK 500 LYS A 7 N - CA - C ANGL. DEV. = 22.1 DEGREES
435	REMARK 500 ASP A 6 O - C - N ANGL. DEV. = 14.8 DEGREES
436	REMARK 500 LYS A 7 C - N - CA ANGL. DEV. = -20.2 DEGREES
437	REMARK 500 THR A 8 CA - CB - CG2 ANGL. DEV. = -10.7 DEGREES
438	REMARK 500 THR A 8 CA - C - O ANGL. DEV. = 21.3 DEGREES
439	REMARK 500 LYS A 7 CA - C - N ANGL. DEV. = -20.1 DEGREES
440	REMARK 500 THR A 8 C - N - CA ANGL. DEV. = -15.7 DEGREES
441	REMARK 500 VAL A 10 O - C - N ANGL. DEV. = 11.4 DEGREES
442	REMARK 500 ALA A 12 CB - CA - C ANGL. DEV. = -29.5 DEGREES
443	REMARK 500 ALA A 12 N - CA - CB ANGL. DEV. = -14.5 DEGREES
444	REMARK 500 ALA A 12 C - N - CA ANGL. DEV. = -22.9 DEGREES
445	REMARK 500 ALA A 12 O - C - N ANGL. DEV. = -25.9 DEGREES
446	REMARK 500 TRP A 14 CA - CB - CG ANGL. DEV. = -22.4 DEGREES
447	REMARK 500 TRP A 14 CG - CD1 - NE1 ANGL. DEV. = -13.5 DEGREES
448	REMARK 500 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 19.8 DEGREES
449	REMARK 500 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 11.2 DEGREES
450	REMARK 500 TRP A 14 CH2 - CZ2 - CE2 ANGL. DEV. = 13.2 DEGREES
451	REMARK 500 ALA A 13 O - C - N ANGL. DEV. = 13.6 DEGREES
452	REMARK 500 GLY A 15 N - CA - C ANGL. DEV. = -24.3 DEGREES
453	REMARK 500 GLY A 15 CA - C - O ANGL. DEV. = -21.6 DEGREES
454	REMARK 500 GLY A 15 C - N - CA ANGL. DEV. = -19.0 DEGREES
455	REMARK 500 LYS A 16 N - CA - CB ANGL. DEV. = 14.8 DEGREES
456	REMARK 500 LYS A 16 CG - CD - CE ANGL. DEV. = -48.6 DEGREES
457	REMARK 500 LYS A 16 CD - CE - NZ ANGL. DEV. = 17.9 DEGREES
458	REMARK 500 GLY A 15 CA - C - N ANGL. DEV. = 25.6 DEGREES
459	REMARK 500 GLY A 15 O - C - N ANGL. DEV. = -10.0 DEGREES
460	REMARK 500 LYS A 16 C - N - CA ANGL. DEV. = 15.1 DEGREES
461	REMARK 500
462	REMARK 500 THIS ENTRY HAS 1481 ANGLE DEVIATIONS.
463	REMARK 500
464	REMARK 500 REMARK: NULL
465	REMARK 500
466	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
467	REMARK 500 SUBTOPIC: TORSION ANGLES
468	REMARK 500
469	REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
470	REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
471	REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
472	REMARK 500
473	REMARK 500 STANDARD TABLE:
474	REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
475	REMARK 500
476	REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
477	REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
478	REMARK 500
479	REMARK 500 M RES CSSEQI PSI PHI
480	REMARK 500 SER A 3 -176.01 -60.80
481	REMARK 500 LYS A 16 -55.41 -1.55
482	REMARK 500 ALA A 21 -76.55 -47.40
483	REMARK 500 LEU A 48 40.81 -103.90
484	REMARK 500 SER A 52 150.87 -47.80
485	REMARK 500 HIS A 122 -70.12 -41.02
486	REMARK 500 THR B 4 -176.32 -55.07
487	REMARK 500 GLU B 7 -71.39 -64.26
488	REMARK 500 PHE B 45 -9.16 -52.07
489	REMARK 500 ASN B 80 59.72 -142.35
490	REMARK 500 TYR B 145 130.62 -35.71
491	REMARK 500 SER C 3 172.94 -57.29
492	REMARK 500 VAL C 17 -70.34 -65.44
493	REMARK 500 LEU C 48 32.06 -92.63
494	REMARK 500 ASP C 75 72.45 -151.27
495	REMARK 500 LYS C 90 -77.18 -122.52
496	REMARK 500 LEU C 113 71.25 -107.78
497	REMARK 500 LEU D 3 -163.80 -100.24
498	REMARK 500 ASN D 19 94.43 -63.05
499	REMARK 500 GLN D 39 0.49 -67.48
500	REMARK 500 SER D 72 -71.73 -40.75
501	REMARK 500 ASP D 73 -43.09 -22.67
502	REMARK 500 ALA D 76 7.73 -63.28
503	REMARK 500 HIS D 77 62.58 -172.71
504	REMARK 500 LEU D 78 -50.86 -25.69
505	REMARK 500 ASN D 80 85.05 -167.04
506	REMARK 500 HIS D 97 35.26 76.08
507	REMARK 500
508	REMARK 500 REMARK: NULL
509	REMARK 500
510	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
511	REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
512	REMARK 500
513	REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
514	REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
515	REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
516	REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
517	REMARK 500 MODEL OMEGA
518	REMARK 500 GLY A 18 ALA A 19 -145.49
519	REMARK 500 SER B 49 THR B 50 113.74
520	REMARK 500 LEU D 3 THR D 4 148.65
521	REMARK 500 VAL D 18 ASN D 19 148.41
522	REMARK 500 LEU D 48 SER D 49 -144.37
523	REMARK 500 SER D 49 THR D 50 143.57
524	REMARK 500
525	REMARK 500 REMARK: NULL
526	REMARK 500
527	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
528	REMARK 500 SUBTOPIC: PLANAR GROUPS
529	REMARK 500
530	REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
531	REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
532	REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
533	REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
534	REMARK 500 AN RMSD GREATER THAN THIS VALUE
535	REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
536	REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
537	REMARK 500
538	REMARK 500 M RES CSSEQI RMS TYPE
539	REMARK 500 HIS A 20 0.17 SIDE CHAIN
540	REMARK 500 GLU A 23 0.25 SIDE CHAIN
541	REMARK 500 TYR A 24 0.10 SIDE CHAIN
542	REMARK 500 PHE A 36 0.09 SIDE CHAIN
543	REMARK 500 HIS A 45 0.11 SIDE CHAIN
544	REMARK 500 HIS A 50 0.20 SIDE CHAIN
545	REMARK 500 GLN A 54 0.10 SIDE CHAIN
546	REMARK 500 ASP A 64 0.14 SIDE CHAIN
547	REMARK 500 HIS A 72 0.24 SIDE CHAIN
548	REMARK 500 ASN A 78 0.08 SIDE CHAIN
549	REMARK 500 ASP A 85 0.09 SIDE CHAIN
550	REMARK 500 ARG A 92 0.08 SIDE CHAIN
551	REMARK 500 ASP A 126 0.10 SIDE CHAIN
552	REMARK 500 ARG A 141 0.08 SIDE CHAIN
553	REMARK 500 HIS B 2 0.16 SIDE CHAIN
554	REMARK 500 GLU B 6 0.16 SIDE CHAIN
555	REMARK 500 ASN B 19 0.08 SIDE CHAIN
556	REMARK 500 ASP B 21 0.15 SIDE CHAIN
557	REMARK 500 GLU B 22 0.51 SIDE CHAIN
558	REMARK 500 GLU B 26 0.38 SIDE CHAIN
559	REMARK 500 ASP B 47 0.14 SIDE CHAIN
560	REMARK 500 ASP B 52 0.19 SIDE CHAIN
561	REMARK 500 HIS B 63 0.11 SIDE CHAIN
562	REMARK 500 ASP B 79 0.11 SIDE CHAIN
563	REMARK 500 ASN B 80 0.20 SIDE CHAIN
564	REMARK 500 GLU B 90 0.15 SIDE CHAIN
565	REMARK 500 ARG B 104 0.39 SIDE CHAIN
566	REMARK 500 HIS B 117 0.22 SIDE CHAIN
567	REMARK 500 PHE B 118 0.13 SIDE CHAIN
568	REMARK 500 GLU B 121 0.26 SIDE CHAIN
569	REMARK 500 HIS B 143 0.10 SIDE CHAIN
570	REMARK 500 HIS B 146 0.31 SIDE CHAIN
571	REMARK 500 ASN C 9 0.08 SIDE CHAIN
572	REMARK 500 HIS C 20 0.14 SIDE CHAIN
573	REMARK 500 GLU C 23 0.30 SIDE CHAIN
574	REMARK 500 HIS C 45 0.10 SIDE CHAIN
575	REMARK 500 PHE C 46 0.10 SIDE CHAIN
576	REMARK 500 ASP C 47 0.15 SIDE CHAIN
577	REMARK 500 ASP C 64 0.08 SIDE CHAIN
578	REMARK 500 ASP C 75 0.07 SIDE CHAIN
579	REMARK 500 ASN C 78 0.11 SIDE CHAIN
580	REMARK 500 ARG C 92 0.20 SIDE CHAIN
581	REMARK 500 GLU C 116 0.09 SIDE CHAIN
582	REMARK 500 ASP C 126 0.11 SIDE CHAIN
583	REMARK 500 ARG C 141 0.08 SIDE CHAIN
584	REMARK 500 HIS D 2 0.10 SIDE CHAIN
585	REMARK 500 GLU D 6 0.17 SIDE CHAIN
586	REMARK 500 GLU D 7 0.10 SIDE CHAIN
587	REMARK 500 ASN D 19 0.38 SIDE CHAIN
588	REMARK 500 ASP D 21 0.18 SIDE CHAIN
589	REMARK 500
590	REMARK 500 THIS ENTRY HAS 71 PLANE DEVIATIONS.
591	REMARK 500
592	REMARK 500 REMARK: NULL
593	REMARK 500
594	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
595	REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
596	REMARK 500
597	REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
598	REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
599	REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
600	REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
601	REMARK 500 I=INSERTION CODE).
602	REMARK 500
603	REMARK 500 M RES CSSEQI ANGLE
604	REMARK 500 VAL A 1 -12.66
605	REMARK 500 SER A 3 -13.96
606	REMARK 500 PRO A 4 -17.06
607	REMARK 500 ASN A 9 10.02
608	REMARK 500 LYS A 11 -14.58
609	REMARK 500 ALA A 12 -29.94
610	REMARK 500 GLY A 15 25.08
611	REMARK 500 ALA A 19 -16.87
612	REMARK 500 ALA A 21 26.61
613	REMARK 500 GLY A 22 15.67
614	REMARK 500 THR A 41 10.65
615	REMARK 500 PHE A 46 -10.97
616	REMARK 500 LEU A 48 -25.01
617	REMARK 500 SER A 52 -10.23
618	REMARK 500 LYS A 56 14.67
619	REMARK 500 GLY A 59 -10.71
620	REMARK 500 LYS A 61 -11.09
621	REMARK 500 ALA A 63 -17.65
622	REMARK 500 ASP A 74 18.25
623	REMARK 500 ASP A 75 -17.02
624	REMARK 500 MET A 76 -10.23
625	REMARK 500 ASN A 78 -10.93
626	REMARK 500 SER A 81 -10.91
627	REMARK 500 ALA A 82 11.29
628	REMARK 500 LEU A 83 -10.53
629	REMARK 500 ASP A 85 -12.19
630	REMARK 500 ALA A 88 11.87
631	REMARK 500 LYS A 90 -14.75
632	REMARK 500 ASN A 97 -10.48
633	REMARK 500 LYS A 99 -15.40
634	REMARK 500 LEU A 101 -10.99
635	REMARK 500 LEU A 106 -10.02
636	REMARK 500 ALA A 111 10.63
637	REMARK 500 PRO A 114 -12.36
638	REMARK 500 THR A 118 -18.84
639	REMARK 500 HIS A 122 17.52
640	REMARK 500 VAL B 1 34.93
641	REMARK 500 LEU B 3 14.19
642	REMARK 500 THR B 4 -16.98
643	REMARK 500 GLU B 7 12.85
644	REMARK 500 LEU B 14 12.16
645	REMARK 500 ASP B 21 -10.62
646	REMARK 500 THR B 38 14.87
647	REMARK 500 GLU B 43 -24.15
648	REMARK 500 SER B 44 54.71
649	REMARK 500 ASP B 47 16.36
650	REMARK 500 SER B 49 -74.55
651	REMARK 500 GLY B 56 -31.39
652	REMARK 500 LYS B 59 -12.59
653	REMARK 500 VAL B 60 10.98
654	REMARK 500
655	REMARK 500 THIS ENTRY HAS 130 MAIN CHAIN PLANARITY DEVIATIONS.
656	REMARK 500
657	REMARK 500 REMARK: NULL
658	REMARK 500
659	REMARK 500 GEOMETRY AND STEREOCHEMISTRY
660	REMARK 500 SUBTOPIC: CHIRAL CENTERS
661	REMARK 500
662	REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
663	REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
664	REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
665	REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
666	REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
667	REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
668	REMARK 500
669	REMARK 500 STANDARD TABLE:
670	REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
671	REMARK 500
672	REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
673	REMARK 500 SER A 3 47.5 L L OUTSIDE RANGE
674	REMARK 500 LYS A 7 22.9 L L OUTSIDE RANGE
675	REMARK 500 LYS A 16 14.6 L L OUTSIDE RANGE
676	REMARK 500 VAL A 17 18.2 L L OUTSIDE RANGE
677	REMARK 500 ALA A 26 18.6 L L OUTSIDE RANGE
678	REMARK 500 PHE A 33 25.0 L L OUTSIDE RANGE
679	REMARK 500 SER A 49 47.6 L L OUTSIDE RANGE
680	REMARK 500 LYS A 56 14.8 L L OUTSIDE RANGE
681	REMARK 500 LYS A 60 22.7 L L OUTSIDE RANGE
682	REMARK 500 ALA A 71 48.3 L L OUTSIDE RANGE
683	REMARK 500 PRO A 77 16.7 L L OUTSIDE RANGE
684	REMARK 500 SER A 84 23.0 L L OUTSIDE RANGE
685	REMARK 500 HIS A 89 23.9 L L OUTSIDE RANGE
686	REMARK 500 LYS A 90 17.4 L L OUTSIDE RANGE
687	REMARK 500 HIS A 103 22.3 L L OUTSIDE RANGE
688	REMARK 500 ALA A 111 21.3 L L OUTSIDE RANGE
689	REMARK 500 PRO A 114 49.5 L L OUTSIDE RANGE
690	REMARK 500 PHE A 117 21.9 L L OUTSIDE RANGE
691	REMARK 500 ALA A 120 20.3 L L OUTSIDE RANGE
692	REMARK 500 HIS A 122 46.2 L L OUTSIDE RANGE
693	REMARK 500 TYR A 140 23.5 L L OUTSIDE RANGE
694	REMARK 500 PRO B 5 18.3 L L OUTSIDE RANGE
695	REMARK 500 SER B 9 13.0 L L OUTSIDE RANGE
696	REMARK 500 ALA B 13 23.4 L L OUTSIDE RANGE
697	REMARK 500 LEU B 28 16.4 L L OUTSIDE RANGE
698	REMARK 500 THR B 38 24.4 L L OUTSIDE RANGE
699	REMARK 500 GLU B 43 46.6 L L OUTSIDE RANGE
700	REMARK 500 ASP B 47 45.8 L L OUTSIDE RANGE
701	REMARK 500 SER B 49 53.4 L L OUTSIDE RANGE
702	REMARK 500 VAL B 60 24.9 L L OUTSIDE RANGE
703	REMARK 500 LYS B 65 20.6 L L OUTSIDE RANGE
704	REMARK 500 HIS B 77 47.6 L L OUTSIDE RANGE
705	REMARK 500 ASP B 79 51.3 L L OUTSIDE RANGE
706	REMARK 500 ASN B 80 45.3 L L OUTSIDE RANGE
707	REMARK 500 LYS B 82 47.0 L L OUTSIDE RANGE
708	REMARK 500 THR B 84 23.8 L L OUTSIDE RANGE
709	REMARK 500 GLU B 90 11.1 L L OUTSIDE RANGE
710	REMARK 500 LEU B 96 22.2 L L OUTSIDE RANGE
711	REMARK 500 ASP B 99 47.0 L L OUTSIDE RANGE
712	REMARK 500 HIS B 117 22.8 L L OUTSIDE RANGE
713	REMARK 500 GLN B 127 23.5 L L OUTSIDE RANGE
714	REMARK 500 VAL B 134 20.6 L L OUTSIDE RANGE
715	REMARK 500 TYR B 145 13.6 L L OUTSIDE RANGE
716	REMARK 500 VAL C 1 85.9 L L OUTSIDE RANGE
717	REMARK 500 ALA C 5 23.1 L L OUTSIDE RANGE
718	REMARK 500 ALA C 12 13.9 L L OUTSIDE RANGE
719	REMARK 500 LYS C 16 18.8 L L OUTSIDE RANGE
720	REMARK 500 VAL C 17 23.9 L L OUTSIDE RANGE
721	REMARK 500 TYR C 24 23.1 L L OUTSIDE RANGE
722	REMARK 500 ALA C 26 24.5 L L OUTSIDE RANGE
723	REMARK 500
724	REMARK 500 THIS ENTRY HAS 97 CHIRALITY DEVIATIONS.
725	REMARK 500
726	REMARK 500 REMARK: NULL
727	REMARK 610
728	REMARK 610 MISSING HETEROATOM
729	REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
730	REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
731	REMARK 610 I=INSERTION CODE):
732	REMARK 610 M RES C SSEQI
733	REMARK 610 PO4 D 147
734	REMARK 610 PO4 B 147
735	REMARK 620
736	REMARK 620 METAL COORDINATION
737	REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
738	REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
739	REMARK 620
740	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
741	REMARK 620 HEM A 142 FE
742	REMARK 620 N RES CSSEQI ATOM
743	REMARK 620 1 HIS A 87 NE2
744	REMARK 620 2 HEM A 142 NA 100.9
745	REMARK 620 3 HEM A 142 NB 100.3 86.2
746	REMARK 620 4 HEM A 142 NC 104.6 154.5 88.3
747	REMARK 620 5 HEM A 142 ND 106.5 90.3 153.2 83.5
748	REMARK 620 N 1 2 3 4
749	REMARK 620
750	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
751	REMARK 620 HEM B 148 FE
752	REMARK 620 N RES CSSEQI ATOM
753	REMARK 620 1 HIS B 92 NE2
754	REMARK 620 2 HEM B 148 NA 97.7
755	REMARK 620 3 HEM B 148 NB 97.1 88.7
756	REMARK 620 4 HEM B 148 NC 104.0 158.3 90.0
757	REMARK 620 5 HEM B 148 ND 103.6 91.0 159.1 82.6
758	REMARK 620 N 1 2 3 4
759	REMARK 620
760	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
761	REMARK 620 HEM C 142 FE
762	REMARK 620 N RES CSSEQI ATOM
763	REMARK 620 1 HIS C 87 NE2
764	REMARK 620 2 HEM C 142 NA 92.2
765	REMARK 620 3 HEM C 142 NB 93.3 83.8
766	REMARK 620 4 HEM C 142 NC 105.8 162.0 94.8
767	REMARK 620 5 HEM C 142 ND 103.5 88.9 161.9 87.1
768	REMARK 620 N 1 2 3 4
769	REMARK 620
770	REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
771	REMARK 620 HEM D 148 FE
772	REMARK 620 N RES CSSEQI ATOM
773	REMARK 620 1 HIS D 92 NE2
774	REMARK 620 2 HEM D 148 NA 90.2
775	REMARK 620 3 HEM D 148 NB 102.2 88.3
776	REMARK 620 4 HEM D 148 NC 109.1 160.5 84.5
777	REMARK 620 5 HEM D 148 ND 97.7 89.1 159.9 91.4
778	REMARK 620 N 1 2 3 4
779	REMARK 800
780	REMARK 800 SITE
781	REMARK 800 SITE_IDENTIFIER: AC1
782	REMARK 800 EVIDENCE_CODE: SOFTWARE
783	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 147
784	REMARK 800
785	REMARK 800 SITE_IDENTIFIER: AC2
786	REMARK 800 EVIDENCE_CODE: SOFTWARE
787	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 147
788	REMARK 800
789	REMARK 800 SITE_IDENTIFIER: AC3
790	REMARK 800 EVIDENCE_CODE: SOFTWARE
791	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142
792	REMARK 800
793	REMARK 800 SITE_IDENTIFIER: AC4
794	REMARK 800 EVIDENCE_CODE: SOFTWARE
795	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 148
796	REMARK 800
797	REMARK 800 SITE_IDENTIFIER: AC5
798	REMARK 800 EVIDENCE_CODE: SOFTWARE
799	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
800	REMARK 800
801	REMARK 800 SITE_IDENTIFIER: AC6
802	REMARK 800 EVIDENCE_CODE: SOFTWARE
803	REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 148
804	REMARK 900
805	REMARK 900 RELATED ENTRIES
806	REMARK 900 RELATED ID: 2HHB RELATED DB: PDB
807	REMARK 900 REFINED BY THE METHOD OF JACK AND LEVITT. THIS ENTRY
808	REMARK 900 PRESENTS THE BEST ESTIMATE OF THE COORDINATES.
809	REMARK 900 RELATED ID: 3HHB RELATED DB: PDB
810	REMARK 900 SYMMETRY AVERAGED ABOUT THE (NON-CRYSTALLOGRAPHIC)
811	REMARK 900 MOLECULAR AXIS AND THEN RE-REGULARIZED BY THE ENERGY
812	REMARK 900 REFINEMENT METHOD OF LEVITT. THIS ENTRY PRESENTS
813	REMARK 900 COORDINATES THAT ARE ADEQUATE FOR MOST PURPOSES, SUCH AS
814	REMARK 900 COMPARISON WITH OTHER STRUCTURES.
815	REMARK 900 RELATED ID: 1GLI RELATED DB: PDB
816	DBREF 4HHB A 1 141 UNP P69905 HBA_HUMAN 1 141
817	DBREF 4HHB B 1 146 UNP P68871 HBB_HUMAN 1 146
818	DBREF 4HHB C 1 141 UNP P69905 HBA_HUMAN 1 141
819	DBREF 4HHB D 1 146 UNP P68871 HBB_HUMAN 1 146
820	SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
821	SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
822	SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
823	SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
824	SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
825	SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
826	SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
827	SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
828	SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
829	SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
830	SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
831	SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
832	SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
833	SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
834	SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
835	SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
836	SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
837	SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
838	SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
839	SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
840	SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
841	SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
842	SEQRES 12 B 146 LYS TYR HIS
843	SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
844	SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
845	SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
846	SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
847	SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
848	SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
849	SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
850	SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
851	SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
852	SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
853	SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
854	SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
855	SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
856	SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
857	SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
858	SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
859	SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
860	SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
861	SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
862	SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
863	SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
864	SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
865	SEQRES 12 D 146 LYS TYR HIS
866	HET PO4 D 147 1
867	HET PO4 B 147 1
868	HET HEM A 142 43
869	HET HEM B 148 43
870	HET HEM C 142 43
871	HET HEM D 148 43
872	HETNAM PO4 PHOSPHATE ION
873	HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
874	HETSYN HEM HEME
875	FORMUL 5 PO4 2(O4 P 3-)
876	FORMUL 7 HEM 4(C34 H32 FE N4 O4)
877	FORMUL 11 HOH *221(H2 O)
878	HELIX 1 AA SER A 3 GLY A 18 1 16
879	HELIX 2 AB HIS A 20 SER A 35 1 16
880	HELIX 3 AC PHE A 36 TYR A 42 1 7
881	HELIX 4 AD HIS A 50 GLY A 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
882	HELIX 5 AE SER A 52 ALA A 71 1 20
883	HELIX 6 AF LEU A 80 ALA A 88 1 9
884	HELIX 7 AG ASP A 94 HIS A 112 1 19
885	HELIX 8 AH THR A 118 SER A 138 1 21
886	HELIX 9 BA THR B 4 VAL B 18 1 15
887	HELIX 10 BB ASN B 19 VAL B 34 1 16
888	HELIX 11 BC TYR B 35 PHE B 41 1 7
889	HELIX 12 BD THR B 50 GLY B 56 1 7
890	HELIX 13 BE ASN B 57 ALA B 76 1 20
891	HELIX 14 BF PHE B 85 CYS B 93 1 9
892	HELIX 15 BG ASP B 99 HIS B 117 1 19
893	HELIX 16 BH THR B 123 HIS B 143 1 21
894	HELIX 17 CA SER C 3 GLY C 18 1 16
895	HELIX 18 CB HIS C 20 SER C 35 1 16
896	HELIX 19 CC PHE C 36 TYR C 42 1 7
897	HELIX 20 CD HIS C 50 GLY C 51 1DEGEN 2 RES HLX RETAIN HOMOL 2
898	HELIX 21 CE SER C 52 ALA C 71 1 20
899	HELIX 22 CF LEU C 80 ALA C 88 1 9
900	HELIX 23 CG ASP C 94 HIS C 112 1 19
901	HELIX 24 CH THR C 118 SER C 138 1 21
902	HELIX 25 DA THR D 4 VAL D 18 1 15
903	HELIX 26 DB ASN D 19 VAL D 34 1 16
904	HELIX 27 DC TYR D 35 PHE D 41 1 7
905	HELIX 28 DD THR D 50 GLY D 56 1 7
906	HELIX 29 DE ASN D 57 ALA D 76 1 20
907	HELIX 30 DF PHE D 85 CYS D 93 1 9
908	HELIX 31 DG ASP D 99 HIS D 117 1 19
909	HELIX 32 DH THR D 123 HIS D 143 1 21
910	LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.14
911	LINK NE2 HIS B 92 FE HEM B 148 1555 1555 2.22
912	LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.26
913	LINK NE2 HIS D 92 FE HEM D 148 1555 1555 1.98
914	SITE 1 AC1 1 VAL D 1
915	SITE 1 AC2 1 HOH B 197
916	SITE 1 AC3 16 TYR A 42 PHE A 43 HIS A 45 PHE A 46
917	SITE 2 AC3 16 HIS A 58 LYS A 61 LEU A 86 HIS A 87
918	SITE 3 AC3 16 LEU A 91 VAL A 93 ASN A 97 PHE A 98
919	SITE 4 AC3 16 LEU A 101 LEU A 136 HOH A 144 HOH A 159
920	SITE 1 AC4 13 ALA A 53 HOH A 145 PHE B 41 HIS B 63
921	SITE 2 AC4 13 LYS B 66 VAL B 67 HIS B 92 LEU B 96
922	SITE 3 AC4 13 ASN B 102 PHE B 103 LEU B 141 HOH B 175
923	SITE 4 AC4 13 HOH B 193
924	SITE 1 AC5 15 TYR C 42 PHE C 43 HIS C 45 HIS C 58
925	SITE 2 AC5 15 LYS C 61 LEU C 83 LEU C 86 HIS C 87
926	SITE 3 AC5 15 LEU C 91 VAL C 93 ASN C 97 PHE C 98
927	SITE 4 AC5 15 LEU C 136 HOH C 149 HOH C 164
928	SITE 1 AC6 7 HIS D 63 LYS D 66 VAL D 67 HIS D 92
929	SITE 2 AC6 7 LEU D 96 ASN D 102 LEU D 141
930	CRYST1 63.150 83.590 53.800 90.00 99.34 90.00 P 1 21 1 4
931	ORIGX1 0.963457 0.136613 0.230424 16.61000
932	ORIGX2 -0.158977 0.983924 0.081383 13.72000
933	ORIGX3 -0.215598 -0.115048 0.969683 37.65000
934	SCALE1 0.015462 0.002192 0.003698 0.26656
935	SCALE2 -0.001902 0.011771 0.000974 0.16413
936	SCALE3 -0.001062 -0.001721 0.018728 0.75059
937	MTRIX1 1 -1.000000 0.000000 0.000000 0.00001 1
938	MTRIX2 1 0.000000 1.000000 0.000000 0.00002 1
939	MTRIX3 1 0.000000 0.000000 -1.000000 0.00002 1
940	ATOM 1 N VAL A 1 6.204 16.869 4.854 1.00 49.05 N
941	ATOM 2 CA VAL A 1 6.913 17.759 4.607 1.00 43.14 C
942	ATOM 3 C VAL A 1 8.504 17.378 4.797 1.00 24.80 C
943	ATOM 4 O VAL A 1 8.805 17.011 5.943 1.00 37.68 O
944	ATOM 5 CB VAL A 1 6.369 19.044 5.810 1.00 72.12 C
945	ATOM 6 CG1 VAL A 1 7.009 20.127 5.418 1.00 61.79 C
946	ATOM 7 CG2 VAL A 1 5.246 18.533 5.681 1.00 80.12 C
947	ATOM 8 N LEU A 2 9.096 18.040 3.857 1.00 26.44 N
948	ATOM 9 CA LEU A 2 10.600 17.889 4.283 1.00 26.32 C
949	ATOM 10 C LEU A 2 11.265 19.184 5.297 1.00 32.96 C
950	ATOM 11 O LEU A 2 10.813 20.177 4.647 1.00 31.90 O
951	ATOM 12 CB LEU A 2 11.099 18.007 2.815 1.00 29.23 C
952	ATOM 13 CG LEU A 2 11.322 16.956 1.934 1.00 37.71 C
953	ATOM 14 CD1 LEU A 2 11.468 15.596 2.337 1.00 39.10 C
954	ATOM 15 CD2 LEU A 2 11.423 17.268 0.300 1.00 37.47 C
955	ATOM 16 N SER A 3 11.584 18.730 6.148 1.00 28.01 N
956	ATOM 17 CA SER A 3 12.263 19.871 7.087 1.00 26.03 C
957	ATOM 18 C SER A 3 13.304 20.329 6.300 1.00 25.99 C
958	ATOM 19 O SER A 3 14.085 19.818 5.364 1.00 25.98 O
959	ATOM 20 CB SER A 3 12.744 19.045 8.223 1.00 23.41 C
960	ATOM 21 OG SER A 3 13.781 18.286 8.179 1.00 30.00 O
961	ATOM 22 N PRO A 4 14.196 21.422 7.097 1.00 37.49 N
962	ATOM 23 CA PRO A 4 15.048 21.890 6.206 1.00 38.81 C
963	ATOM 24 C PRO A 4 16.464 21.282 6.288 1.00 25.63 C
964	ATOM 25 O PRO A 4 17.212 20.899 5.409 1.00 34.38 O
965	ATOM 26 CB PRO A 4 15.814 23.113 7.166 1.00 50.44 C
966	ATOM 27 CG PRO A 4 14.493 23.536 7.638 1.00 43.42 C
967	ATOM 28 CD PRO A 4 13.298 22.523 7.651 1.00 42.77 C
968	ATOM 29 N ALA A 5 16.399 20.279 7.524 1.00 24.33 N
969	ATOM 30 CA ALA A 5 17.552 19.622 7.588 1.00 24.06 C
970	ATOM 31 C ALA A 5 17.376 18.283 6.601 1.00 20.01 C
971	ATOM 32 O ALA A 5 18.422 17.849 6.010 1.00 24.46 O
972	ATOM 33 CB ALA A 5 17.454 18.830 9.164 1.00 28.15 C
973	ATOM 34 N ASP A 6 16.050 17.799 6.298 1.00 21.19 N
974	ATOM 35 CA ASP A 6 15.881 16.887 5.120 1.00 23.14 C
975	ATOM 36 C ASP A 6 16.573 17.497 3.915 1.00 15.75 C
976	ATOM 37 O ASP A 6 17.240 16.611 3.235 1.00 18.92 O
977	ATOM 38 CB ASP A 6 14.530 16.515 4.983 1.00 18.68 C
978	ATOM 39 CG ASP A 6 13.966 15.638 6.125 1.00 21.70 C
979	ATOM 40 OD1 ASP A 6 14.573 14.751 6.678 1.00 19.76 O
980	ATOM 41 OD2 ASP A 6 12.734 15.931 6.321 1.00 21.26 O
981	ATOM 42 N LYS A 7 16.082 18.800 3.719 1.00 15.62 N
982	ATOM 43 CA LYS A 7 16.897 19.255 2.400 1.00 26.74 C
983	ATOM 44 C LYS A 7 18.354 19.319 2.072 1.00 24.82 C
984	ATOM 45 O LYS A 7 18.858 18.855 1.145 1.00 21.36 O
985	ATOM 46 CB LYS A 7 16.022 20.503 2.054 1.00 28.73 C
986	ATOM 47 CG LYS A 7 14.518 20.443 2.287 1.00 34.11 C
987	ATOM 48 CD LYS A 7 13.833 21.967 2.124 1.00 46.50 C
988	ATOM 49 CE LYS A 7 12.524 21.830 2.733 1.00 40.75 C
989	ATOM 50 NZ LYS A 7 12.310 23.286 2.231 1.00 50.05 N
990	ATOM 51 N THR A 8 18.879 19.583 3.554 1.00 20.80 N
991	ATOM 52 CA THR A 8 20.359 19.452 3.495 1.00 23.21 C
992	ATOM 53 C THR A 8 21.000 18.322 3.125 1.00 17.85 C
993	ATOM 54 O THR A 8 21.907 17.957 2.500 1.00 20.04 O
994	ATOM 55 CB THR A 8 20.762 20.269 4.939 1.00 31.90 C
995	ATOM 56 OG1 THR A 8 20.363 21.458 4.886 1.00 31.01 O
996	ATOM 57 CG2 THR A 8 22.026 20.115 4.978 1.00 43.78 C
997	ATOM 58 N ASN A 9 20.249 17.203 3.818 1.00 16.13 N
998	ATOM 59 CA ASN A 9 20.591 15.889 3.728 1.00 17.84 C
999	ATOM 60 C ASN A 9 20.630 15.286 2.184 1.00 14.45 C
1000	ATOM 61 O ASN A 9 21.319 14.475 1.822 1.00 21.78 O
1001	ATOM 62 CB ASN A 9 19.836 14.946 4.644 1.00 20.10 C
1002	ATOM 63 CG ASN A 9 20.193 15.272 6.089 1.00 34.82 C
1003	ATOM 64 OD1 ASN A 9 21.294 15.680 6.444 1.00 26.93 O
1004	ATOM 65 ND2 ASN A 9 19.527 14.719 6.950 1.00 28.08 N
1005	ATOM 66 N VAL A 10 19.435 15.546 1.583 1.00 19.64 N
1006	ATOM 67 CA VAL A 10 19.157 15.110 0.179 1.00 13.04 C
1007	ATOM 68 C VAL A 10 20.341 15.904 -0.719 1.00 18.71 C
1008	ATOM 69 O VAL A 10 20.832 15.221 -1.618 1.00 22.34 O
1009	ATOM 70 CB VAL A 10 17.776 15.394 -0.119 1.00 19.07 C
1010	ATOM 71 CG1 VAL A 10 17.623 15.138 -1.549 1.00 21.59 C
1011	ATOM 72 CG2 VAL A 10 16.816 14.756 0.575 1.00 22.75 C
1012	ATOM 73 N LYS A 11 20.392 17.201 -0.404 1.00 18.31 N
1013	ATOM 74 CA LYS A 11 21.297 18.030 -1.415 1.00 24.80 C
1014	ATOM 75 C LYS A 11 22.762 17.451 -1.066 1.00 19.51 C
1015	ATOM 76 O LYS A 11 23.584 17.190 -2.069 1.00 22.33 O
1016	ATOM 77 CB LYS A 11 21.334 19.381 -1.059 1.00 39.77 C
1017	ATOM 78 CG LYS A 11 20.229 20.052 -1.350 1.00 34.41 C
1018	ATOM 79 CD LYS A 11 20.256 21.365 -1.389 1.00 46.95 C
1019	ATOM 80 CE LYS A 11 18.633 21.891 -2.358 1.00 49.55 C
1020	ATOM 81 NZ LYS A 11 18.398 23.088 -1.720 1.00 78.67 N
1021	ATOM 82 N ALA A 12 23.031 16.766 0.069 1.00 20.60 N
1022	ATOM 83 CA ALA A 12 24.347 16.671 -0.059 1.00 25.98 C
1023	ATOM 84 C ALA A 12 24.529 15.278 -0.129 1.00 38.04 C
1024	ATOM 85 O ALA A 12 25.505 14.711 -1.045 1.00 31.19 O
1025	ATOM 86 CB ALA A 12 24.641 16.359 1.529 1.00 28.13 C
1026	ATOM 87 N ALA A 13 23.581 14.281 -0.261 1.00 21.69 N
1027	ATOM 88 CA ALA A 13 23.822 13.010 -0.701 1.00 19.11 C
1028	ATOM 89 C ALA A 13 23.807 12.890 -2.423 1.00 22.93 C
1029	ATOM 90 O ALA A 13 24.517 12.116 -2.938 1.00 24.98 O
1030	ATOM 91 CB ALA A 13 22.612 12.109 -0.160 1.00 23.17 C
1031	ATOM 92 N TRP A 14 22.807 13.763 -2.832 1.00 22.14 N
1032	ATOM 93 CA TRP A 14 22.715 13.681 -4.311 1.00 21.27 C
1033	ATOM 94 C TRP A 14 24.007 14.453 -5.015 1.00 28.97 C
1034	ATOM 95 O TRP A 14 24.452 13.999 -6.086 1.00 27.61 O
1035	ATOM 96 CB TRP A 14 21.129 14.484 -4.728 1.00 29.00 C
1036	ATOM 97 CG TRP A 14 21.116 13.951 -5.830 1.00 25.79 C
1037	ATOM 98 CD1 TRP A 14 21.182 14.904 -7.199 1.00 22.38 C
1038	ATOM 99 CD2 TRP A 14 20.358 12.768 -6.306 1.00 20.46 C
1039	ATOM 100 NE1 TRP A 14 20.545 13.886 -8.152 1.00 29.74 N
1040	ATOM 101 CE2 TRP A 14 20.127 12.855 -7.917 1.00 27.75 C
1041	ATOM 102 CE3 TRP A 14 19.993 11.556 -5.760 1.00 34.00 C
1042	ATOM 103 CZ2 TRP A 14 19.685 11.924 -8.428 1.00 34.81 C
1043	ATOM 104 CZ3 TRP A 14 19.443 10.605 -6.677 1.00 42.11 C
1044	ATOM 105 CH2 TRP A 14 19.361 10.910 -7.988 1.00 47.54 C
1045	ATOM 106 N GLY A 15 24.563 15.294 -4.064 1.00 40.92 N
1046	ATOM 107 CA GLY A 15 25.545 16.032 -4.810 1.00 38.97 C
1047	ATOM 108 C GLY A 15 26.606 14.720 -4.643 1.00 34.61 C
1048	ATOM 109 O GLY A 15 27.532 14.956 -6.011 1.00 36.24 O
1049	ATOM 110 N LYS A 16 27.023 14.192 -4.019 1.00 35.37 N
1050	ATOM 111 CA LYS A 16 27.691 12.809 -3.990 1.00 29.09 C
1051	ATOM 112 C LYS A 16 27.692 11.980 -5.322 1.00 27.28 C
1052	ATOM 113 O LYS A 16 28.444 11.335 -5.752 1.00 36.62 O
1053	ATOM 114 CB LYS A 16 27.773 11.881 -2.758 1.00 30.47 C
1054	ATOM 115 CG LYS A 16 29.128 10.897 -2.949 1.00 47.02 C
1055	ATOM 116 CD LYS A 16 30.512 12.265 -2.454 1.00 66.41 C
1056	ATOM 117 CE LYS A 16 31.160 10.590 -3.127 1.00 65.00 C
1057	ATOM 118 NZ LYS A 16 31.293 9.343 -2.468 1.00 69.28 N
1058	ATOM 119 N VAL A 17 26.231 11.894 -5.716 1.00 40.63 N
1059	ATOM 120 CA VAL A 17 25.763 11.093 -6.580 1.00 32.19 C
1060	ATOM 121 C VAL A 17 26.644 11.417 -8.297 1.00 51.53 C
1061	ATOM 122 O VAL A 17 27.090 10.850 -8.486 1.00 36.95 O
1062	ATOM 123 CB VAL A 17 24.455 10.688 -6.704 1.00 24.77 C
1063	ATOM 124 CG1 VAL A 17 24.024 10.418 -8.088 1.00 21.73 C
1064	ATOM 125 CG2 VAL A 17 23.718 9.922 -5.546 1.00 23.90 C
1065	ATOM 126 N GLY A 18 26.340 12.947 -7.963 1.00 36.07 N
1066	ATOM 127 CA GLY A 18 27.063 13.723 -8.931 1.00 37.64 C
1067	ATOM 128 C GLY A 18 26.574 12.969 -10.560 1.00 27.84 C
1068	ATOM 129 O GLY A 18 25.253 13.110 -10.707 1.00 34.16 O
1069	ATOM 130 N ALA A 19 27.657 12.515 -11.022 1.00 35.70 N
1070	ATOM 131 CA ALA A 19 27.728 12.613 -12.429 1.00 37.59 C
1071	ATOM 132 C ALA A 19 27.500 10.976 -12.552 1.00 34.69 C
1072	ATOM 133 O ALA A 19 27.084 10.420 -13.842 1.00 48.59 O
1073	ATOM 134 CB ALA A 19 29.012 12.664 -13.280 1.00 46.19 C
1074	ATOM 135 N HIS A 20 27.156 10.119 -11.606 1.00 20.24 N
1075	ATOM 136 CA HIS A 20 26.883 8.665 -11.713 1.00 19.03 C
1076	ATOM 137 C HIS A 20 25.297 8.749 -11.742 1.00 17.82 C
1077	ATOM 138 O HIS A 20 24.744 7.547 -11.745 1.00 20.59 O
1078	ATOM 139 CB HIS A 20 27.211 8.007 -10.561 1.00 31.92 C
1079	ATOM 140 CG HIS A 20 28.495 7.629 -10.284 1.00 45.35 C
1080	ATOM 141 ND1 HIS A 20 29.488 7.023 -11.531 1.00 52.86 N
1081	ATOM 142 CD2 HIS A 20 29.445 8.698 -9.743 1.00 43.12 C
1082	ATOM 143 CE1 HIS A 20 30.546 7.246 -10.801 1.00 68.75 C
1083	ATOM 144 NE2 HIS A 20 30.729 7.865 -10.003 1.00 55.89 N
1084	ATOM 145 N ALA A 21 24.687 9.784 -11.799 1.00 29.55 N
1085	ATOM 146 CA ALA A 21 23.159 9.917 -11.488 1.00 29.36 C
1086	ATOM 147 C ALA A 21 22.579 8.284 -12.650 1.00 46.23 C
1087	ATOM 148 O ALA A 21 21.659 8.109 -12.129 1.00 27.88 O
1088	ATOM 149 CB ALA A 21 22.561 11.174 -11.335 1.00 28.64 C
1089	ATOM 150 N GLY A 22 22.741 9.029 -13.713 1.00 27.74 N
1090	ATOM 151 CA GLY A 22 22.302 7.955 -14.644 1.00 29.10 C
1091	ATOM 152 C GLY A 22 22.405 6.768 -14.523 1.00 40.30 C
1092	ATOM 153 O GLY A 22 21.884 5.714 -14.971 1.00 33.08 O
1093	ATOM 154 N GLU A 23 23.751 6.163 -14.331 1.00 22.76 N
1094	ATOM 155 CA GLU A 23 24.084 4.748 -14.144 1.00 14.60 C
1095	ATOM 156 C GLU A 23 23.211 4.210 -12.893 1.00 13.41 C
1096	ATOM 157 O GLU A 23 22.937 3.039 -12.842 1.00 16.24 O
1097	ATOM 158 CB GLU A 23 25.664 4.939 -13.797 1.00 20.16 C
1098	ATOM 159 CG GLU A 23 26.201 3.519 -13.776 1.00 40.65 C
1099	ATOM 160 CD GLU A 23 28.243 3.900 -13.483 1.00 70.75 C
1100	ATOM 161 OE1 GLU A 23 27.931 3.380 -11.875 1.00 57.57 O
1101	ATOM 162 OE2 GLU A 23 28.452 5.212 -13.971 1.00 57.46 O
1102	ATOM 163 N TYR A 24 23.179 5.044 -11.863 1.00 18.60 N
1103	ATOM 164 CA TYR A 24 22.505 4.593 -10.679 1.00 26.35 C
1104	ATOM 165 C TYR A 24 21.016 4.562 -11.095 1.00 17.67 C
1105	ATOM 166 O TYR A 24 20.360 3.603 -10.478 1.00 17.15 O
1106	ATOM 167 CB TYR A 24 22.464 5.807 -9.581 1.00 21.47 C
1107	ATOM 168 CG TYR A 24 23.992 5.643 -8.868 1.00 17.94 C
1108	ATOM 169 CD1 TYR A 24 24.282 6.445 -7.897 1.00 25.54 C
1109	ATOM 170 CD2 TYR A 24 24.950 4.858 -9.353 1.00 18.41 C
1110	ATOM 171 CE1 TYR A 24 25.677 6.369 -7.422 1.00 27.77 C
1111	ATOM 172 CE2 TYR A 24 26.305 4.768 -8.960 1.00 24.84 C
1112	ATOM 173 CZ TYR A 24 26.528 5.702 -7.748 1.00 28.92 C
1113	ATOM 174 OH TYR A 24 27.827 5.849 -7.564 1.00 33.79 O
1114	ATOM 175 N GLY A 25 20.378 5.478 -11.759 1.00 17.58 N
1115	ATOM 176 CA GLY A 25 19.016 5.420 -12.390 1.00 16.95 C
1116	ATOM 177 C GLY A 25 18.833 4.130 -12.941 1.00 12.93 C
1117	ATOM 178 O GLY A 25 17.819 3.343 -12.872 1.00 14.53 O
1118	ATOM 179 N ALA A 26 19.615 3.604 -13.915 1.00 15.78 N
1119	ATOM 180 CA ALA A 26 19.582 2.579 -14.539 1.00 18.05 C
1120	ATOM 181 C ALA A 26 19.480 1.089 -13.772 1.00 13.38 C
1121	ATOM 182 O ALA A 26 18.901 0.084 -13.805 1.00 13.68 O
1122	ATOM 183 CB ALA A 26 20.556 2.124 -15.501 1.00 21.17 C
1123	ATOM 184 N GLU A 27 20.535 1.124 -12.715 1.00 13.26 N
1124	ATOM 185 CA GLU A 27 20.575 0.021 -11.753 1.00 15.73 C
1125	ATOM 186 C GLU A 27 19.308 -0.043 -10.886 1.00 9.69 C
1126	ATOM 187 O GLU A 27 18.918 -1.164 -10.735 1.00 13.70 O
1127	ATOM 188 CB GLU A 27 21.903 0.397 -10.962 1.00 17.47 C
1128	ATOM 189 CG GLU A 27 21.998 -0.702 -9.888 1.00 16.72 C
1129	ATOM 190 CD GLU A 27 23.378 -0.554 -8.914 1.00 28.34 C
1130	ATOM 191 OE1 GLU A 27 23.164 -0.938 -7.844 1.00 20.53 O
1131	ATOM 192 OE2 GLU A 27 24.282 0.068 -9.385 1.00 20.32 O
1132	ATOM 193 N ALA A 28 18.802 1.101 -10.459 1.00 11.71 N
1133	ATOM 194 CA ALA A 28 17.589 1.092 -9.707 1.00 14.08 C
1134	ATOM 195 C ALA A 28 16.437 0.281 -10.410 1.00 18.50 C
1135	ATOM 196 O ALA A 28 15.609 -0.358 -10.010 1.00 12.43 O
1136	ATOM 197 CB ALA A 28 17.166 2.432 -9.252 1.00 19.09 C
1137	ATOM 198 N LEU A 29 16.400 0.918 -11.698 1.00 12.19 N
1138	ATOM 199 CA LEU A 29 15.328 0.075 -12.594 1.00 17.48 C
1139	ATOM 200 C LEU A 29 15.559 -1.439 -12.734 1.00 9.74 C
1140	ATOM 201 O LEU A 29 14.606 -2.189 -12.644 1.00 10.80 O
1141	ATOM 202 CB LEU A 29 15.302 0.859 -14.203 1.00 12.13 C
1142	ATOM 203 CG LEU A 29 14.894 2.291 -14.067 1.00 14.66 C
1143	ATOM 204 CD1 LEU A 29 15.261 2.690 -15.515 1.00 16.80 C
1144	ATOM 205 CD2 LEU A 29 13.402 2.225 -13.944 1.00 18.58 C
1145	ATOM 206 N GLU A 30 16.843 -1.859 -13.083 1.00 9.20 N
1146	ATOM 207 CA GLU A 30 17.065 -3.260 -13.067 1.00 11.66 C
1147	ATOM 208 C GLU A 30 16.682 -4.043 -11.806 1.00 13.48 C
1148	ATOM 209 O GLU A 30 16.222 -5.112 -11.842 1.00 17.00 O
1149	ATOM 210 CB GLU A 30 18.445 -3.450 -13.556 1.00 19.11 C
1150	ATOM 211 CG GLU A 30 18.613 -4.789 -13.421 1.00 27.23 C
1151	ATOM 212 CD GLU A 30 20.397 -5.050 -14.290 1.00 43.77 C
1152	ATOM 213 OE1 GLU A 30 21.034 -4.018 -14.191 1.00 45.21 O
1153	ATOM 214 OE2 GLU A 30 20.320 -6.204 -14.925 1.00 45.13 O
1154	ATOM 215 N ARG A 31 17.074 -3.325 -10.709 1.00 11.70 N
1155	ATOM 216 CA ARG A 31 16.706 -3.885 -9.384 1.00 13.69 C
1156	ATOM 217 C ARG A 31 15.116 -4.077 -9.266 1.00 13.95 C
1157	ATOM 218 O ARG A 31 14.772 -5.201 -8.729 1.00 16.42 O
1158	ATOM 219 CB ARG A 31 17.207 -3.143 -8.212 1.00 9.32 C
1159	ATOM 220 CG ARG A 31 18.786 -3.298 -8.162 1.00 14.85 C
1160	ATOM 221 CD ARG A 31 19.223 -2.383 -7.101 1.00 20.12 C
1161	ATOM 222 NE ARG A 31 20.863 -2.372 -6.759 1.00 14.83 N
1162	ATOM 223 CZ ARG A 31 21.361 -3.431 -6.210 1.00 13.22 C
1163	ATOM 224 NH1 ARG A 31 20.746 -4.460 -5.716 1.00 11.40 N
1164	ATOM 225 NH2 ARG A 31 22.719 -3.344 -6.301 1.00 17.34 N
1165	ATOM 226 N MET A 32 14.439 -3.020 -9.681 1.00 11.37 N
1166	ATOM 227 CA MET A 32 13.032 -3.139 -9.600 1.00 10.16 C
1167	ATOM 228 C MET A 32 12.471 -4.206 -10.484 1.00 12.10 C
1168	ATOM 229 O MET A 32 11.562 -5.027 -10.075 1.00 12.78 O
1169	ATOM 230 CB MET A 32 12.387 -1.842 -9.978 1.00 12.48 C
1170	ATOM 231 CG MET A 32 10.889 -1.620 -9.930 1.00 17.73 C
1171	ATOM 232 SD MET A 32 10.285 -0.089 -10.543 1.00 15.12 S
1172	ATOM 233 CE MET A 32 10.633 -0.449 -12.284 1.00 11.32 C
1173	ATOM 234 N PHE A 33 12.859 -4.341 -11.658 1.00 13.98 N
1174	ATOM 235 CA PHE A 33 12.423 -5.476 -12.584 1.00 16.07 C
1175	ATOM 236 C PHE A 33 12.551 -6.737 -12.305 1.00 12.29 C
1176	ATOM 237 O PHE A 33 11.788 -7.686 -12.349 1.00 14.84 O
1177	ATOM 238 CB PHE A 33 12.947 -5.237 -13.990 1.00 11.16 C
1178	ATOM 239 CG PHE A 33 12.536 -3.998 -14.641 1.00 10.01 C
1179	ATOM 240 CD1 PHE A 33 11.466 -3.383 -14.673 1.00 13.62 C
1180	ATOM 241 CD2 PHE A 33 13.679 -3.464 -15.536 1.00 19.46 C
1181	ATOM 242 CE1 PHE A 33 11.074 -2.180 -15.483 1.00 17.65 C
1182	ATOM 243 CE2 PHE A 33 13.177 -2.070 -16.087 1.00 14.83 C
1183	ATOM 244 CZ PHE A 33 12.158 -1.591 -16.095 1.00 12.93 C
1184	ATOM 245 N LEU A 34 13.735 -6.963 -11.432 1.00 16.04 N
1185	ATOM 246 CA LEU A 34 14.079 -8.337 -11.022 1.00 14.57 C
1186	ATOM 247 C LEU A 34 13.293 -8.578 -9.676 1.00 17.64 C
1187	ATOM 248 O LEU A 34 12.997 -9.724 -9.442 1.00 18.98 O
1188	ATOM 249 CB LEU A 34 15.453 -8.526 -10.814 1.00 18.08 C
1189	ATOM 250 CG LEU A 34 16.401 -8.680 -11.761 1.00 28.60 C
1190	ATOM 251 CD1 LEU A 34 17.957 -8.573 -11.703 1.00 25.37 C
1191	ATOM 252 CD2 LEU A 34 15.936 -9.330 -12.871 1.00 34.83 C
1192	ATOM 253 N SER A 35 13.220 -7.510 -8.706 1.00 15.41 N
1193	ATOM 254 CA SER A 35 12.815 -7.908 -7.502 1.00 14.95 C
1194	ATOM 255 C SER A 35 11.238 -7.909 -7.418 1.00 15.69 C
1195	ATOM 256 O SER A 35 10.517 -8.531 -6.585 1.00 14.29 O
1196	ATOM 257 CB SER A 35 13.131 -6.749 -6.442 1.00 13.14 C
1197	ATOM 258 OG SER A 35 14.485 -7.014 -6.085 1.00 17.78 O
1198	ATOM 259 N PHE A 36 10.680 -7.033 -8.262 1.00 13.54 N
1199	ATOM 260 CA PHE A 36 9.195 -6.850 -8.454 1.00 13.46 C
1200	ATOM 261 C PHE A 36 8.843 -6.910 -9.927 1.00 8.62 C
1201	ATOM 262 O PHE A 36 8.478 -5.788 -10.556 1.00 14.12 O
1202	ATOM 263 CB PHE A 36 8.936 -5.457 -7.919 1.00 16.50 C
1203	ATOM 264 CG PHE A 36 9.418 -4.974 -6.493 1.00 13.63 C
1204	ATOM 265 CD1 PHE A 36 10.591 -4.292 -6.329 1.00 11.92 C
1205	ATOM 266 CD2 PHE A 36 8.828 -5.831 -5.362 1.00 19.28 C
1206	ATOM 267 CE1 PHE A 36 11.048 -4.090 -5.054 1.00 15.75 C
1207	ATOM 268 CE2 PHE A 36 9.372 -5.629 -4.112 1.00 13.78 C
1208	ATOM 269 CZ PHE A 36 10.535 -4.872 -4.007 1.00 15.33 C
1209	ATOM 270 N PRO A 37 8.621 -8.156 -10.145 1.00 14.18 N
1210	ATOM 271 CA PRO A 37 8.292 -8.333 -11.715 1.00 17.12 C
1211	ATOM 272 C PRO A 37 7.088 -7.804 -12.224 1.00 17.85 C
1212	ATOM 273 O PRO A 37 6.976 -7.542 -13.453 1.00 18.50 O
1213	ATOM 274 CB PRO A 37 8.433 -9.844 -11.897 1.00 23.37 C
1214	ATOM 275 CG PRO A 37 8.573 -10.410 -10.572 1.00 28.27 C
1215	ATOM 276 CD PRO A 37 8.857 -9.204 -9.532 1.00 20.43 C
1216	ATOM 277 N THR A 38 6.105 -7.481 -11.322 1.00 18.86 N
1217	ATOM 278 CA THR A 38 4.849 -6.949 -11.938 1.00 14.66 C
1218	ATOM 279 C THR A 38 5.134 -5.609 -12.568 1.00 12.72 C
1219	ATOM 280 O THR A 38 4.433 -5.064 -13.326 1.00 15.75 O
1220	ATOM 281 CB THR A 38 3.879 -6.749 -10.732 1.00 19.10 C
1221	ATOM 282 OG1 THR A 38 4.340 -6.112 -9.661 1.00 18.82 O
1222	ATOM 283 CG2 THR A 38 3.543 -8.224 -10.416 1.00 22.69 C
1223	ATOM 284 N THR A 39 6.269 -4.882 -12.154 1.00 14.27 N
1224	ATOM 285 CA THR A 39 6.491 -3.556 -12.776 1.00 10.19 C
1225	ATOM 286 C THR A 39 6.886 -3.690 -14.302 1.00 10.17 C
1226	ATOM 287 O THR A 39 6.836 -2.719 -14.886 1.00 14.01 O
1227	ATOM 288 CB THR A 39 7.510 -2.917 -11.996 1.00 15.56 C
1228	ATOM 289 OG1 THR A 39 8.881 -3.562 -11.937 1.00 14.68 O
1229	ATOM 290 CG2 THR A 39 7.258 -2.652 -10.511 1.00 20.52 C
1230	ATOM 291 N LYS A 40 7.174 -4.831 -14.593 1.00 14.72 N
1231	ATOM 292 CA LYS A 40 7.574 -4.871 -15.954 1.00 15.89 C
1232	ATOM 293 C LYS A 40 6.392 -4.785 -17.012 1.00 21.37 C
1233	ATOM 294 O LYS A 40 6.437 -4.614 -18.103 1.00 15.72 O
1234	ATOM 295 CB LYS A 40 8.145 -6.482 -16.338 1.00 11.64 C
1235	ATOM 296 CG LYS A 40 9.529 -6.584 -15.725 1.00 16.19 C
1236	ATOM 297 CD LYS A 40 10.167 -7.889 -16.138 1.00 23.35 C
1237	ATOM 298 CE LYS A 40 9.677 -9.033 -15.597 1.00 24.42 C
1238	ATOM 299 NZ LYS A 40 10.352 -10.362 -15.922 1.00 19.04 N
1239	ATOM 300 N THR A 41 5.127 -4.865 -16.397 1.00 13.16 N
1240	ATOM 301 CA THR A 41 3.875 -4.707 -17.174 1.00 14.78 C
1241	ATOM 302 C THR A 41 3.932 -3.487 -17.746 1.00 15.32 C
1242	ATOM 303 O THR A 41 3.044 -3.054 -18.672 1.00 15.67 O
1243	ATOM 304 CB THR A 41 2.612 -5.037 -16.228 1.00 15.38 C
1244	ATOM 305 OG1 THR A 41 2.526 -4.071 -15.248 1.00 14.93 O
1245	ATOM 306 CG2 THR A 41 2.578 -6.405 -15.884 1.00 16.57 C
1246	ATOM 307 N TYR A 42 4.610 -2.356 -17.311 1.00 10.46 N
1247	ATOM 308 CA TYR A 42 4.398 -1.015 -17.861 1.00 12.73 C
1248	ATOM 309 C TYR A 42 5.571 -0.792 -19.101 1.00 7.07 C
1249	ATOM 310 O TYR A 42 5.611 0.312 -19.642 1.00 12.11 O
1250	ATOM 311 CB TYR A 42 4.898 -0.049 -16.794 1.00 14.67 C
1251	ATOM 312 CG TYR A 42 3.618 0.026 -15.875 1.00 13.54 C
1252	ATOM 313 CD1 TYR A 42 2.437 0.794 -16.095 1.00 19.68 C
1253	ATOM 314 CD2 TYR A 42 3.661 -0.765 -14.634 1.00 18.38 C
1254	ATOM 315 CE1 TYR A 42 1.433 0.570 -15.142 1.00 23.98 C
1255	ATOM 316 CE2 TYR A 42 2.601 -0.739 -13.758 1.00 13.41 C
1256	ATOM 317 CZ TYR A 42 1.469 -0.048 -14.033 1.00 18.96 C
1257	ATOM 318 OH TYR A 42 0.436 -0.054 -13.115 1.00 19.81 O
1258	ATOM 319 N PHE A 43 6.476 -1.826 -19.154 1.00 17.11 N
1259	ATOM 320 CA PHE A 43 7.621 -1.843 -20.115 1.00 18.18 C
1260	ATOM 321 C PHE A 43 7.472 -2.895 -21.133 1.00 24.86 C
1261	ATOM 322 O PHE A 43 8.506 -3.413 -21.456 1.00 22.13 O
1262	ATOM 323 CB PHE A 43 8.883 -1.731 -19.445 1.00 15.44 C
1263	ATOM 324 CG PHE A 43 9.117 -0.406 -18.576 1.00 14.36 C
1264	ATOM 325 CD1 PHE A 43 8.554 -0.479 -17.198 1.00 14.47 C
1265	ATOM 326 CD2 PHE A 43 9.564 0.739 -18.886 1.00 16.54 C
1266	ATOM 327 CE1 PHE A 43 8.777 0.624 -16.478 1.00 20.56 C
1267	ATOM 328 CE2 PHE A 43 9.747 1.973 -18.107 1.00 17.61 C
1268	ATOM 329 CZ PHE A 43 9.344 1.707 -16.778 1.00 18.88 C
1269	ATOM 330 N PRO A 44 6.315 -3.239 -21.641 1.00 18.09 N
1270	ATOM 331 CA PRO A 44 6.381 -4.414 -22.439 1.00 22.24 C
1271	ATOM 332 C PRO A 44 7.028 -3.933 -24.077 1.00 24.15 C
1272	ATOM 333 O PRO A 44 7.495 -4.754 -24.733 1.00 24.01 O
1273	ATOM 334 CB PRO A 44 5.048 -4.531 -22.752 1.00 28.44 C
1274	ATOM 335 CG PRO A 44 4.370 -3.210 -22.675 1.00 24.77 C
1275	ATOM 336 CD PRO A 44 5.151 -2.594 -21.501 1.00 21.37 C
1276	ATOM 337 N HIS A 45 7.181 -2.759 -24.200 1.00 22.61 N
1277	ATOM 338 CA HIS A 45 7.861 -2.190 -25.416 1.00 32.33 C
1278	ATOM 339 C HIS A 45 9.330 -2.042 -25.421 1.00 27.50 C
1279	ATOM 340 O HIS A 45 9.974 -1.539 -26.257 1.00 22.34 O
1280	ATOM 341 CB HIS A 45 7.358 -0.919 -25.693 1.00 28.91 C
1281	ATOM 342 CG HIS A 45 7.192 0.375 -24.801 1.00 24.48 C
1282	ATOM 343 ND1 HIS A 45 6.886 -0.058 -23.407 1.00 28.61 N
1283	ATOM 344 CD2 HIS A 45 7.956 1.463 -24.795 1.00 25.11 C
1284	ATOM 345 CE1 HIS A 45 7.011 1.085 -22.716 1.00 26.97 C
1285	ATOM 346 NE2 HIS A 45 7.765 2.042 -23.628 1.00 30.40 N
1286	ATOM 347 N PHE A 46 10.122 -2.386 -24.054 1.00 17.28 N
1287	ATOM 348 CA PHE A 46 11.455 -2.262 -23.909 1.00 16.89 C
1288	ATOM 349 C PHE A 46 12.005 -3.636 -24.127 1.00 16.17 C
1289	ATOM 350 O PHE A 46 11.604 -4.686 -23.635 1.00 18.14 O
1290	ATOM 351 CB PHE A 46 11.684 -1.700 -22.434 1.00 19.02 C
1291	ATOM 352 CG PHE A 46 11.699 -0.399 -22.451 1.00 24.73 C
1292	ATOM 353 CD1 PHE A 46 12.430 0.377 -21.434 1.00 19.60 C
1293	ATOM 354 CD2 PHE A 46 11.298 0.412 -23.118 1.00 32.07 C
1294	ATOM 355 CE1 PHE A 46 12.410 1.666 -21.260 1.00 16.62 C
1295	ATOM 356 CE2 PHE A 46 11.265 1.969 -23.113 1.00 32.95 C
1296	ATOM 357 CZ PHE A 46 11.777 2.738 -22.175 1.00 26.82 C
1297	ATOM 358 N ASP A 47 13.392 -3.464 -24.534 1.00 19.28 N
1298	ATOM 359 CA ASP A 47 14.201 -4.676 -24.267 1.00 21.11 C
1299	ATOM 360 C ASP A 47 14.839 -4.498 -22.659 1.00 19.86 C
1300	ATOM 361 O ASP A 47 15.431 -3.489 -22.547 1.00 21.26 O
1301	ATOM 362 CB ASP A 47 15.523 -4.420 -25.240 1.00 18.49 C
1302	ATOM 363 CG ASP A 47 16.401 -5.761 -25.037 1.00 31.25 C
1303	ATOM 364 OD1 ASP A 47 16.311 -6.607 -24.275 1.00 29.75 O
1304	ATOM 365 OD2 ASP A 47 17.439 -5.328 -25.588 1.00 43.41 O
1305	ATOM 366 N LEU A 48 14.368 -5.324 -22.041 1.00 24.03 N
1306	ATOM 367 CA LEU A 48 14.753 -5.341 -20.734 1.00 18.27 C
1307	ATOM 368 C LEU A 48 15.791 -6.404 -20.198 1.00 36.02 C
1308	ATOM 369 O LEU A 48 16.171 -6.209 -19.141 1.00 39.74 O
1309	ATOM 370 CB LEU A 48 13.415 -5.610 -19.721 1.00 19.69 C
1310	ATOM 371 CG LEU A 48 12.489 -4.486 -19.789 1.00 21.82 C
1311	ATOM 372 CD1 LEU A 48 11.174 -5.208 -18.951 1.00 33.27 C
1312	ATOM 373 CD2 LEU A 48 12.620 -3.262 -19.549 1.00 24.10 C
1313	ATOM 374 N SER A 49 16.783 -6.499 -21.225 1.00 29.95 N
1314	ATOM 375 CA SER A 49 18.122 -7.384 -21.060 1.00 36.57 C
1315	ATOM 376 C SER A 49 18.846 -6.374 -20.277 1.00 27.84 C
1316	ATOM 377 O SER A 49 19.000 -5.086 -20.358 1.00 22.88 O
1317	ATOM 378 CB SER A 49 18.154 -8.122 -22.211 1.00 37.22 C
1318	ATOM 379 OG SER A 49 18.651 -7.428 -22.904 1.00 43.53 O
1319	ATOM 380 N HIS A 50 19.910 -7.126 -19.381 1.00 28.70 N
1320	ATOM 381 CA HIS A 50 20.458 -5.929 -18.816 1.00 33.73 C
1321	ATOM 382 C HIS A 50 21.497 -5.179 -19.493 1.00 26.32 C
1322	ATOM 383 O HIS A 50 22.162 -5.918 -20.594 1.00 31.00 O
1323	ATOM 384 CB HIS A 50 21.839 -7.147 -17.996 1.00 52.72 C
1324	ATOM 385 CG HIS A 50 22.748 -6.326 -17.477 1.00 44.40 C
1325	ATOM 386 ND1 HIS A 50 22.626 -5.701 -16.215 1.00 33.80 N
1326	ATOM 387 CD2 HIS A 50 24.218 -6.937 -17.247 1.00 47.43 C
1327	ATOM 388 CE1 HIS A 50 23.812 -5.042 -15.891 1.00 41.56 C
1328	ATOM 389 NE2 HIS A 50 24.721 -5.696 -16.698 1.00 46.05 N
1329	ATOM 390 N GLY A 51 21.750 -4.254 -19.494 1.00 24.77 N
1330	ATOM 391 CA GLY A 51 22.455 -3.151 -20.084 1.00 47.57 C
1331	ATOM 392 C GLY A 51 21.857 -2.536 -21.373 1.00 38.90 C
1332	ATOM 393 O GLY A 51 22.594 -2.038 -22.085 1.00 36.29 O
1333	ATOM 394 N SER A 52 20.675 -3.017 -21.484 1.00 31.32 N
1334	ATOM 395 CA SER A 52 19.963 -2.196 -22.851 1.00 26.23 C
1335	ATOM 396 C SER A 52 20.134 -0.997 -22.782 1.00 16.57 C
1336	ATOM 397 O SER A 52 19.933 -0.129 -21.983 1.00 20.02 O
1337	ATOM 398 CB SER A 52 18.619 -2.881 -22.964 1.00 27.24 C
1338	ATOM 399 OG SER A 52 17.746 -2.046 -22.388 1.00 23.82 O
1339	ATOM 400 N ALA A 53 20.194 -0.382 -24.103 1.00 17.74 N
1340	ATOM 401 CA ALA A 53 20.270 0.998 -24.154 1.00 23.86 C
1341	ATOM 402 C ALA A 53 18.923 1.773 -23.848 1.00 16.18 C
1342	ATOM 403 O ALA A 53 18.953 2.849 -23.330 1.00 19.42 O
1343	ATOM 404 CB ALA A 53 20.303 1.395 -25.787 1.00 25.47 C
1344	ATOM 405 N GLN A 54 17.736 0.981 -23.874 1.00 20.85 N
1345	ATOM 406 CA GLN A 54 16.512 1.657 -23.573 1.00 13.59 C
1346	ATOM 407 C GLN A 54 16.574 1.828 -21.914 1.00 19.26 C
1347	ATOM 408 O GLN A 54 15.942 2.867 -21.609 1.00 20.48 O
1348	ATOM 409 CB GLN A 54 15.353 0.611 -23.904 1.00 15.39 C
1349	ATOM 410 CG GLN A 54 14.983 0.803 -25.364 1.00 20.40 C
1350	ATOM 411 CD GLN A 54 14.209 -0.311 -25.782 1.00 15.48 C
1351	ATOM 412 OE1 GLN A 54 14.579 -1.521 -25.849 1.00 23.45 O
1352	ATOM 413 NE2 GLN A 54 13.268 -0.063 -26.856 1.00 19.86 N
1353	ATOM 414 N VAL A 55 16.964 0.770 -21.300 1.00 16.87 N
1354	ATOM 415 CA VAL A 55 17.057 0.967 -19.825 1.00 16.48 C
1355	ATOM 416 C VAL A 55 17.956 2.003 -19.318 1.00 17.36 C
1356	ATOM 417 O VAL A 55 17.791 2.873 -18.570 1.00 18.40 O
1357	ATOM 418 CB VAL A 55 17.306 -0.514 -19.268 1.00 14.78 C
1358	ATOM 419 CG1 VAL A 55 17.609 -0.401 -17.796 1.00 21.77 C
1359	ATOM 420 CG2 VAL A 55 16.107 -1.297 -19.446 1.00 16.83 C
1360	ATOM 421 N LYS A 56 19.228 1.986 -19.953 1.00 16.43 N
1361	ATOM 422 CA LYS A 56 20.094 3.039 -19.797 1.00 16.52 C
1362	ATOM 423 C LYS A 56 19.566 4.272 -19.699 1.00 21.58 C
1363	ATOM 424 O LYS A 56 19.825 5.350 -19.163 1.00 20.11 O
1364	ATOM 425 CB LYS A 56 21.563 2.786 -20.316 1.00 18.35 C
1365	ATOM 426 CG LYS A 56 21.968 1.412 -19.848 1.00 28.49 C
1366	ATOM 427 CD LYS A 56 23.832 1.798 -20.631 1.00 44.71 C
1367	ATOM 428 CE LYS A 56 24.647 0.185 -20.276 1.00 47.65 C
1368	ATOM 429 NZ LYS A 56 26.042 0.618 -20.926 1.00 52.31 N
1369	ATOM 430 N GLY A 57 19.018 4.549 -21.123 1.00 17.21 N
1370	ATOM 431 CA GLY A 57 18.386 5.829 -21.439 1.00 25.10 C
1371	ATOM 432 C GLY A 57 17.163 6.322 -20.441 1.00 19.44 C
1372	ATOM 433 O GLY A 57 17.339 7.478 -20.078 1.00 20.54 O
1373	ATOM 434 N HIS A 58 16.465 5.322 -20.170 1.00 18.79 N
1374	ATOM 435 CA HIS A 58 15.350 5.701 -19.218 1.00 20.27 C
1375	ATOM 436 C HIS A 58 15.995 6.080 -17.623 1.00 13.51 C
1376	ATOM 437 O HIS A 58 15.432 7.056 -17.182 1.00 17.47 O
1377	ATOM 438 CB HIS A 58 14.449 4.447 -19.262 1.00 17.90 C
1378	ATOM 439 CG HIS A 58 13.058 4.996 -18.478 1.00 15.76 C
1379	ATOM 440 ND1 HIS A 58 12.287 6.114 -18.800 1.00 20.40 N
1380	ATOM 441 CD2 HIS A 58 12.522 4.394 -17.450 1.00 20.31 C
1381	ATOM 442 CE1 HIS A 58 11.473 6.092 -17.719 1.00 20.13 C
1382	ATOM 443 NE2 HIS A 58 11.497 5.103 -17.065 1.00 21.08 N
1383	ATOM 444 N GLY A 59 16.881 5.222 -17.443 1.00 14.95 N
1384	ATOM 445 CA GLY A 59 17.562 5.623 -16.096 1.00 18.11 C
1385	ATOM 446 C GLY A 59 18.124 6.806 -15.942 1.00 19.85 C
1386	ATOM 447 O GLY A 59 17.932 7.718 -15.003 1.00 15.36 O
1387	ATOM 448 N LYS A 60 18.701 7.399 -17.074 1.00 17.17 N
1388	ATOM 449 CA LYS A 60 19.105 8.846 -17.109 1.00 18.34 C
1389	ATOM 450 C LYS A 60 18.266 9.905 -16.940 1.00 18.03 C
1390	ATOM 451 O LYS A 60 18.249 10.847 -16.377 1.00 18.72 O
1391	ATOM 452 CB LYS A 60 20.142 9.096 -18.402 1.00 30.65 C
1392	ATOM 453 CG LYS A 60 20.617 10.355 -18.546 1.00 41.57 C
1393	ATOM 454 CD LYS A 60 21.486 10.272 -19.721 1.00 63.44 C
1394	ATOM 455 CE LYS A 60 22.042 12.123 -19.760 1.00 44.10 C
1395	ATOM 456 NZ LYS A 60 23.253 10.931 -21.838 1.00 49.08 N
1396	ATOM 457 N LYS A 61 17.057 9.480 -17.740 1.00 16.33 N
1397	ATOM 458 CA LYS A 61 15.986 10.442 -17.612 1.00 17.87 C
1398	ATOM 459 C LYS A 61 15.127 10.479 -16.158 1.00 14.89 C
1399	ATOM 460 O LYS A 61 14.981 11.608 -15.829 1.00 19.71 O
1400	ATOM 461 CB LYS A 61 14.717 10.033 -18.529 1.00 25.67 C
1401	ATOM 462 CG LYS A 61 14.971 10.361 -20.143 1.00 41.04 C
1402	ATOM 463 CD LYS A 61 13.959 9.646 -21.043 1.00 54.25 C
1403	ATOM 464 CE LYS A 61 14.061 9.666 -21.851 1.00 78.95 C
1404	ATOM 465 NZ LYS A 61 13.029 9.011 -23.092 1.00 43.58 N
1405	ATOM 466 N VAL A 62 15.316 9.304 -15.709 1.00 15.10 N
1406	ATOM 467 CA VAL A 62 14.699 9.322 -14.234 1.00 16.18 C
1407	ATOM 468 C VAL A 62 15.686 10.200 -13.093 1.00 18.93 C
1408	ATOM 469 O VAL A 62 15.095 11.051 -12.555 1.00 16.64 O
1409	ATOM 470 CB VAL A 62 14.660 7.890 -13.835 1.00 13.59 C
1410	ATOM 471 CG1 VAL A 62 14.141 7.704 -12.419 1.00 20.28 C
1411	ATOM 472 CG2 VAL A 62 13.407 7.365 -14.552 1.00 17.24 C
1412	ATOM 473 N ALA A 63 16.863 9.822 -13.546 1.00 18.60 N
1413	ATOM 474 CA ALA A 63 17.806 10.661 -12.634 1.00 14.91 C
1414	ATOM 475 C ALA A 63 18.050 11.967 -12.922 1.00 18.47 C
1415	ATOM 476 O ALA A 63 17.940 12.889 -11.976 1.00 18.58 O
1416	ATOM 477 CB ALA A 63 19.170 9.768 -12.782 1.00 37.76 C
1417	ATOM 478 N ASP A 64 17.821 12.573 -14.198 1.00 16.80 N
1418	ATOM 479 CA ASP A 64 17.733 13.912 -14.174 1.00 24.74 C
1419	ATOM 480 C ASP A 64 16.549 14.773 -13.697 1.00 17.12 C
1420	ATOM 481 O ASP A 64 16.672 15.717 -13.116 1.00 22.08 O
1421	ATOM 482 CB ASP A 64 17.603 14.212 -15.737 1.00 35.97 C
1422	ATOM 483 CG ASP A 64 19.349 14.293 -16.612 1.00 31.06 C
1423	ATOM 484 OD1 ASP A 64 20.156 13.672 -15.497 1.00 35.72 O
1424	ATOM 485 OD2 ASP A 64 18.977 14.172 -17.839 1.00 43.58 O
1425	ATOM 486 N ALA A 65 15.332 13.912 -13.869 1.00 13.28 N
1426	ATOM 487 CA ALA A 65 14.329 14.415 -13.017 1.00 17.27 C
1427	ATOM 488 C ALA A 65 14.445 14.482 -11.415 1.00 13.03 C
1428	ATOM 489 O ALA A 65 13.989 15.536 -11.013 1.00 17.77 O
1429	ATOM 490 CB ALA A 65 12.982 13.578 -13.361 1.00 23.35 C
1430	ATOM 491 N LEU A 66 15.162 13.498 -11.063 1.00 15.51 N
1431	ATOM 492 CA LEU A 66 15.339 13.706 -9.605 1.00 11.63 C
1432	ATOM 493 C LEU A 66 16.337 14.754 -9.333 1.00 19.15 C
1433	ATOM 494 O LEU A 66 16.146 15.585 -8.334 1.00 19.52 O
1434	ATOM 495 CB LEU A 66 15.829 12.371 -9.144 1.00 13.76 C
1435	ATOM 496 CG LEU A 66 14.823 11.115 -8.963 1.00 19.82 C
1436	ATOM 497 CD1 LEU A 66 15.489 9.880 -8.746 1.00 18.79 C
1437	ATOM 498 CD2 LEU A 66 13.658 11.434 -8.143 1.00 21.54 C
1438	ATOM 499 N THR A 67 17.286 14.890 -10.137 1.00 15.35 N
1439	ATOM 500 CA THR A 67 18.223 15.978 -10.096 1.00 19.22 C
1440	ATOM 501 C THR A 67 17.538 17.420 -10.103 1.00 19.35 C
1441	ATOM 502 O THR A 67 17.647 18.426 -9.135 1.00 25.50 O
1442	ATOM 503 CB THR A 67 19.391 15.815 -10.975 1.00 27.92 C
1443	ATOM 504 OG1 THR A 67 20.048 14.951 -10.890 1.00 31.77 O
1444	ATOM 505 CG2 THR A 67 20.007 17.263 -11.105 1.00 31.55 C
1445	ATOM 506 N ASN A 68 16.575 17.470 -11.016 1.00 18.73 N
1446	ATOM 507 CA ASN A 68 15.744 18.747 -11.028 1.00 18.68 C
1447	ATOM 508 C ASN A 68 14.923 18.912 -9.894 1.00 24.52 C
1448	ATOM 509 O ASN A 68 14.765 20.137 -9.247 1.00 25.75 O
1449	ATOM 510 CB ASN A 68 14.756 18.608 -12.121 1.00 25.79 C
1450	ATOM 511 CG ASN A 68 13.735 19.831 -12.299 1.00 36.65 C
1451	ATOM 512 OD1 ASN A 68 14.126 20.875 -12.151 1.00 38.63 O
1452	ATOM 513 ND2 ASN A 68 12.596 19.698 -13.037 1.00 39.67 N
1453	ATOM 514 N ALA A 69 14.365 17.791 -9.099 1.00 17.85 N
1454	ATOM 515 CA ALA A 69 13.480 18.120 -7.964 1.00 16.12 C
1455	ATOM 516 C ALA A 69 14.454 18.477 -6.733 1.00 15.28 C
1456	ATOM 517 O ALA A 69 14.055 19.178 -5.996 1.00 20.90 O
1457	ATOM 518 CB ALA A 69 13.019 16.796 -7.635 1.00 21.91 C
1458	ATOM 519 N VAL A 70 15.742 17.807 -6.739 1.00 18.42 N
1459	ATOM 520 CA VAL A 70 16.670 18.320 -5.560 1.00 18.79 C
1460	ATOM 521 C VAL A 70 17.052 19.774 -5.743 1.00 21.40 C
1461	ATOM 522 O VAL A 70 16.986 20.472 -4.749 1.00 22.44 O
1462	ATOM 523 CB VAL A 70 17.782 17.521 -5.616 1.00 19.75 C
1463	ATOM 524 CG1 VAL A 70 19.021 17.739 -4.714 1.00 24.49 C
1464	ATOM 525 CG2 VAL A 70 17.476 16.043 -5.206 1.00 30.23 C
1465	ATOM 526 N ALA A 71 17.156 20.293 -6.971 1.00 20.17 N
1466	ATOM 527 CA ALA A 71 17.389 21.815 -7.308 1.00 23.56 C
1467	ATOM 528 C ALA A 71 16.370 22.294 -6.912 1.00 25.98 C
1468	ATOM 529 O ALA A 71 16.635 23.655 -6.511 1.00 33.09 O
1469	ATOM 530 CB ALA A 71 17.654 21.789 -8.655 1.00 32.78 C
1470	ATOM 531 N HIS A 72 15.081 22.080 -6.888 1.00 23.78 N
1471	ATOM 532 CA HIS A 72 13.997 22.837 -6.617 1.00 21.95 C
1472	ATOM 533 C HIS A 72 13.181 22.411 -5.617 1.00 20.17 C
1473	ATOM 534 O HIS A 72 11.897 22.212 -5.613 1.00 23.99 O
1474	ATOM 535 CB HIS A 72 12.821 22.953 -7.947 1.00 35.07 C
1475	ATOM 536 CG HIS A 72 13.866 23.277 -8.689 1.00 34.89 C
1476	ATOM 537 ND1 HIS A 72 13.873 24.932 -9.510 1.00 43.74 N
1477	ATOM 538 CD2 HIS A 72 14.464 23.117 -10.031 1.00 29.96 C
1478	ATOM 539 CE1 HIS A 72 15.153 25.255 -9.959 1.00 41.69 C
1479	ATOM 540 NE2 HIS A 72 15.223 24.225 -10.948 1.00 44.85 N
1480	ATOM 541 N VAL A 73 13.752 21.857 -4.446 1.00 23.31 N
1481	ATOM 542 CA VAL A 73 13.057 21.077 -3.315 1.00 23.32 C
1482	ATOM 543 C VAL A 73 12.075 21.651 -2.904 1.00 32.07 C
1483	ATOM 544 O VAL A 73 10.955 21.485 -2.533 1.00 42.18 O
1484	ATOM 545 CB VAL A 73 13.998 20.556 -2.485 1.00 41.19 C
1485	ATOM 546 CG1 VAL A 73 14.923 21.399 -1.795 1.00 52.76 C
1486	ATOM 547 CG2 VAL A 73 13.799 19.262 -2.036 1.00 47.91 C
1487	ATOM 548 N ASP A 74 12.275 23.065 -2.789 1.00 30.40 N
1488	ATOM 549 CA ASP A 74 11.145 24.002 -2.142 1.00 34.95 C
1489	ATOM 550 C ASP A 74 10.049 24.015 -3.350 1.00 50.97 C
1490	ATOM 551 O ASP A 74 9.132 24.778 -2.717 1.00 49.62 O
1491	ATOM 552 CB ASP A 74 11.678 25.422 -2.020 1.00 42.77 C
1492	ATOM 553 CG ASP A 74 12.830 25.304 -0.645 1.00 52.01 C
1493	ATOM 554 OD1 ASP A 74 12.752 24.865 0.015 1.00 49.67 O
1494	ATOM 555 OD2 ASP A 74 14.337 25.661 -0.918 1.00 51.46 O
1495	ATOM 556 N ASP A 75 9.922 23.915 -4.261 1.00 36.55 N
1496	ATOM 557 CA ASP A 75 8.668 23.936 -5.208 1.00 36.46 C
1497	ATOM 558 C ASP A 75 8.874 22.788 -6.315 1.00 19.07 C
1498	ATOM 559 O ASP A 75 8.567 23.036 -7.581 1.00 22.77 O
1499	ATOM 560 CB ASP A 75 9.451 25.163 -6.540 1.00 64.13 C
1500	ATOM 561 CG ASP A 75 8.868 25.436 -6.330 1.00 74.46 C
1501	ATOM 562 OD1 ASP A 75 7.314 26.337 -6.605 1.00 47.43 O
1502	ATOM 563 OD2 ASP A 75 8.881 25.994 -8.289 1.00 60.83 O
1503	ATOM 564 N MET A 76 8.625 21.775 -5.634 1.00 28.83 N
1504	ATOM 565 CA MET A 76 8.674 20.530 -6.647 1.00 25.75 C
1505	ATOM 566 C MET A 76 7.271 20.288 -7.401 1.00 26.47 C
1506	ATOM 567 O MET A 76 7.358 19.996 -8.579 1.00 25.06 O
1507	ATOM 568 CB MET A 76 8.643 19.305 -5.552 1.00 26.87 C
1508	ATOM 569 CG MET A 76 9.740 19.092 -5.553 1.00 44.91 C
1509	ATOM 570 SD MET A 76 10.207 17.317 -4.716 1.00 43.69 S
1510	ATOM 571 CE MET A 76 10.186 17.272 -3.278 1.00 47.45 C
1511	ATOM 572 N PRO A 77 6.289 20.734 -6.858 1.00 24.72 N
1512	ATOM 573 CA PRO A 77 5.288 21.011 -7.720 1.00 32.25 C
1513	ATOM 574 C PRO A 77 5.404 21.500 -8.895 1.00 33.71 C
1514	ATOM 575 O PRO A 77 4.843 20.983 -10.107 1.00 27.50 O
1515	ATOM 576 CB PRO A 77 3.868 21.504 -6.885 1.00 35.42 C
1516	ATOM 577 CG PRO A 77 4.538 21.027 -5.570 1.00 42.65 C
1517	ATOM 578 CD PRO A 77 5.873 20.979 -5.490 1.00 26.77 C
1518	ATOM 579 N ASN A 78 5.832 22.745 -9.066 1.00 28.71 N
1519	ATOM 580 CA ASN A 78 5.931 23.542 -10.146 1.00 29.25 C
1520	ATOM 581 C ASN A 78 7.105 22.960 -10.923 1.00 25.30 C
1521	ATOM 582 O ASN A 78 7.043 22.562 -12.258 1.00 31.49 O
1522	ATOM 583 CB ASN A 78 6.292 25.075 -10.189 1.00 52.85 C
1523	ATOM 584 CG ASN A 78 5.615 25.627 -10.060 1.00 62.76 C
1524	ATOM 585 OD1 ASN A 78 4.765 26.184 -8.258 1.00 71.55 O
1525	ATOM 586 ND2 ASN A 78 4.594 25.811 -10.486 1.00 72.60 N
1526	ATOM 587 N ALA A 79 8.114 22.456 -10.315 1.00 21.06 N
1527	ATOM 588 CA ALA A 79 9.264 21.897 -10.989 1.00 28.88 C
1528	ATOM 589 C ALA A 79 8.963 20.522 -11.944 1.00 27.69 C
1529	ATOM 590 O ALA A 79 9.465 20.431 -13.022 1.00 25.51 O
1530	ATOM 591 CB ALA A 79 10.294 21.701 -10.105 1.00 35.64 C
1531	ATOM 592 N LEU A 80 8.232 19.781 -11.312 1.00 22.21 N
1532	ATOM 593 CA LEU A 80 7.767 18.341 -11.815 1.00 24.91 C
1533	ATOM 594 C LEU A 80 6.510 18.562 -12.698 1.00 29.49 C
1534	ATOM 595 O LEU A 80 5.875 17.479 -12.950 1.00 21.47 O
1535	ATOM 596 CB LEU A 80 7.734 17.285 -10.765 1.00 17.03 C
1536	ATOM 597 CG LEU A 80 9.126 17.077 -10.078 1.00 26.04 C
1537	ATOM 598 CD1 LEU A 80 8.930 16.109 -9.016 1.00 30.97 C
1538	ATOM 599 CD2 LEU A 80 10.040 16.545 -11.282 1.00 40.31 C
1539	ATOM 600 N SER A 81 5.857 19.827 -12.942 1.00 21.07 N
1540	ATOM 601 CA SER A 81 4.431 19.687 -13.335 1.00 18.09 C
1541	ATOM 602 C SER A 81 4.363 19.087 -14.671 1.00 20.48 C
1542	ATOM 603 O SER A 81 3.314 18.257 -14.890 1.00 25.77 O
1543	ATOM 604 CB SER A 81 4.467 21.619 -13.861 1.00 32.64 C
1544	ATOM 605 OG SER A 81 2.994 21.456 -13.913 1.00 44.30 O
1545	ATOM 606 N ALA A 82 5.219 18.957 -15.594 1.00 23.80 N
1546	ATOM 607 CA ALA A 82 5.295 18.397 -16.849 1.00 21.23 C
1547	ATOM 608 C ALA A 82 5.047 16.984 -16.596 1.00 19.91 C
1548	ATOM 609 O ALA A 82 4.419 16.133 -17.266 1.00 24.36 O
1549	ATOM 610 CB ALA A 82 6.433 18.664 -17.830 1.00 22.94 C
1550	ATOM 611 N LEU A 83 6.039 16.444 -15.755 1.00 18.35 N
1551	ATOM 612 CA LEU A 83 5.983 14.900 -15.664 1.00 19.01 C
1552	ATOM 613 C LEU A 83 4.967 14.491 -14.735 1.00 18.91 C
1553	ATOM 614 O LEU A 83 4.393 13.347 -14.967 1.00 18.17 O
1554	ATOM 615 CB LEU A 83 7.250 14.624 -14.735 1.00 22.27 C
1555	ATOM 616 CG LEU A 83 8.130 13.821 -15.009 1.00 34.66 C
1556	ATOM 617 CD1 LEU A 83 8.449 13.918 -16.558 1.00 28.24 C
1557	ATOM 618 CD2 LEU A 83 9.756 14.153 -14.680 1.00 38.79 C
1558	ATOM 619 N SER A 84 4.321 15.210 -13.869 1.00 13.22 N
1559	ATOM 620 CA SER A 84 3.091 14.769 -13.309 1.00 14.54 C
1560	ATOM 621 C SER A 84 1.806 14.643 -14.240 1.00 13.50 C
1561	ATOM 622 O SER A 84 1.081 13.802 -14.037 1.00 20.19 O
1562	ATOM 623 CB SER A 84 2.316 15.701 -11.953 1.00 25.45 C
1563	ATOM 624 OG SER A 84 3.028 16.684 -12.075 1.00 36.19 O
1564	ATOM 625 N ASP A 85 1.894 15.645 -15.194 1.00 15.99 N
1565	ATOM 626 CA ASP A 85 0.657 15.457 -16.246 1.00 18.10 C
1566	ATOM 627 C ASP A 85 0.872 14.320 -17.117 1.00 20.71 C
1567	ATOM 628 O ASP A 85 0.085 13.524 -17.249 1.00 20.01 O
1568	ATOM 629 CB ASP A 85 0.847 16.636 -17.207 1.00 30.89 C
1569	ATOM 630 CG ASP A 85 0.240 17.791 -16.350 1.00 57.00 C
1570	ATOM 631 OD1 ASP A 85 -0.408 17.890 -15.984 1.00 51.34 O
1571	ATOM 632 OD2 ASP A 85 0.645 19.250 -17.189 1.00 50.68 O
1572	ATOM 633 N LEU A 86 2.217 13.883 -17.444 1.00 20.13 N
1573	ATOM 634 CA LEU A 86 2.516 12.802 -18.225 1.00 17.03 C
1574	ATOM 635 C LEU A 86 2.094 11.499 -17.604 1.00 14.48 C
1575	ATOM 636 O LEU A 86 1.613 10.536 -18.155 1.00 18.46 O
1576	ATOM 637 CB LEU A 86 4.085 12.859 -18.555 1.00 16.01 C
1577	ATOM 638 CG LEU A 86 4.479 11.856 -19.204 1.00 23.66 C
1578	ATOM 639 CD1 LEU A 86 4.217 11.927 -20.682 1.00 40.43 C
1579	ATOM 640 CD2 LEU A 86 6.063 11.399 -19.455 1.00 33.72 C
1580	ATOM 641 N HIS A 87 2.488 11.534 -16.185 1.00 12.17 N
1581	ATOM 642 CA HIS A 87 2.237 10.125 -15.649 1.00 12.85 C
1582	ATOM 643 C HIS A 87 0.524 10.055 -15.280 1.00 15.39 C
1583	ATOM 644 O HIS A 87 0.114 8.957 -15.394 1.00 15.03 O
1584	ATOM 645 CB HIS A 87 2.873 10.043 -14.177 1.00 13.63 C
1585	ATOM 646 CG HIS A 87 4.357 9.531 -14.510 1.00 14.91 C
1586	ATOM 647 ND1 HIS A 87 5.315 10.638 -14.847 1.00 15.35 N
1587	ATOM 648 CD2 HIS A 87 5.128 8.461 -14.450 1.00 17.85 C
1588	ATOM 649 CE1 HIS A 87 6.425 9.938 -15.110 1.00 15.29 C
1589	ATOM 650 NE2 HIS A 87 6.410 8.672 -14.776 1.00 15.64 N
1590	ATOM 651 N ALA A 88 0.070 11.240 -15.092 1.00 19.56 N
1591	ATOM 652 CA ALA A 88 -1.450 11.245 -14.731 1.00 16.45 C
1592	ATOM 653 C ALA A 88 -2.307 10.782 -16.164 1.00 28.29 C
1593	ATOM 654 O ALA A 88 -3.217 10.321 -15.884 1.00 25.27 O
1594	ATOM 655 CB ALA A 88 -1.985 12.408 -13.954 1.00 17.34 C
1595	ATOM 656 N HIS A 89 -1.856 11.542 -17.115 1.00 21.56 N
1596	ATOM 657 CA HIS A 89 -2.652 11.471 -18.284 1.00 29.42 C
1597	ATOM 658 C HIS A 89 -2.430 10.590 -19.375 1.00 27.17 C
1598	ATOM 659 O HIS A 89 -3.237 9.974 -20.183 1.00 22.35 O
1599	ATOM 660 CB HIS A 89 -2.855 12.836 -18.839 1.00 26.26 C
1600	ATOM 661 CG HIS A 89 -3.474 13.775 -17.933 1.00 44.45 C
1601	ATOM 662 ND1 HIS A 89 -4.582 13.545 -17.082 1.00 45.59 N
1602	ATOM 663 CD2 HIS A 89 -3.036 15.133 -17.376 1.00 45.61 C
1603	ATOM 664 CE1 HIS A 89 -4.931 14.373 -15.965 1.00 42.72 C
1604	ATOM 665 NE2 HIS A 89 -3.969 15.212 -16.507 1.00 43.49 N
1605	ATOM 666 N LYS A 90 -1.237 10.085 -19.553 1.00 18.65 N
1606	ATOM 667 CA LYS A 90 -0.701 9.212 -20.311 1.00 28.92 C
1607	ATOM 668 C LYS A 90 -0.235 7.836 -20.094 1.00 28.09 C
1608	ATOM 669 O LYS A 90 -0.814 6.865 -20.213 1.00 25.04 O
1609	ATOM 670 CB LYS A 90 0.483 9.973 -21.248 1.00 32.47 C
1610	ATOM 671 CG LYS A 90 -0.258 11.271 -22.102 1.00 49.97 C
1611	ATOM 672 CD LYS A 90 -1.161 11.150 -22.865 1.00 58.54 C
1612	ATOM 673 CE LYS A 90 -0.717 12.584 -23.928 1.00 66.22 C
1613	ATOM 674 NZ LYS A 90 -3.148 11.648 -24.501 1.00 63.54 N
1614	ATOM 675 N LEU A 91 0.684 7.834 -19.083 1.00 17.50 N
1615	ATOM 676 CA LEU A 91 1.357 6.678 -18.728 1.00 15.47 C
1616	ATOM 677 C LEU A 91 0.469 5.814 -17.729 1.00 18.54 C
1617	ATOM 678 O LEU A 91 0.360 4.623 -17.933 1.00 17.03 O
1618	ATOM 679 CB LEU A 91 2.810 6.867 -17.956 1.00 13.84 C
1619	ATOM 680 CG LEU A 91 3.828 7.564 -18.848 1.00 16.01 C
1620	ATOM 681 CD1 LEU A 91 4.943 7.934 -18.256 1.00 18.27 C
1621	ATOM 682 CD2 LEU A 91 3.998 6.811 -20.081 1.00 22.12 C
1622	ATOM 683 N ARG A 92 -0.013 6.544 -16.785 1.00 18.03 N
1623	ATOM 684 CA ARG A 92 -1.120 5.962 -15.831 1.00 14.41 C
1624	ATOM 685 C ARG A 92 -0.663 4.876 -15.136 1.00 15.84 C
1625	ATOM 686 O ARG A 92 -1.280 3.746 -14.964 1.00 17.92 O
1626	ATOM 687 CB ARG A 92 -2.457 5.762 -16.768 1.00 18.61 C
1627	ATOM 688 CG ARG A 92 -3.108 6.901 -17.068 1.00 25.14 C
1628	ATOM 689 CD ARG A 92 -3.735 6.578 -19.206 1.00 53.25 C
1629	ATOM 690 NE ARG A 92 -4.375 7.010 -18.108 1.00 51.61 N
1630	ATOM 691 CZ ARG A 92 -5.273 6.721 -20.498 1.00 59.18 C
1631	ATOM 692 NH1 ARG A 92 -4.092 6.059 -21.138 1.00 31.30 N
1632	ATOM 693 NH2 ARG A 92 -6.080 6.715 -20.222 1.00 36.70 N
1633	ATOM 694 N VAL A 93 0.444 4.876 -14.510 1.00 14.32 N
1634	ATOM 695 CA VAL A 93 1.119 3.933 -13.665 1.00 16.19 C
1635	ATOM 696 C VAL A 93 0.472 3.844 -12.448 1.00 13.83 C
1636	ATOM 697 O VAL A 93 0.272 4.879 -11.643 1.00 14.88 O
1637	ATOM 698 CB VAL A 93 2.564 4.273 -13.453 1.00 12.60 C
1638	ATOM 699 CG1 VAL A 93 3.153 3.301 -12.513 1.00 15.68 C
1639	ATOM 700 CG2 VAL A 93 3.314 4.342 -14.815 1.00 15.91 C
1640	ATOM 701 N ASP A 94 0.015 2.696 -11.867 1.00 14.66 N
1641	ATOM 702 CA ASP A 94 -0.813 2.633 -10.611 1.00 11.73 C
1642	ATOM 703 C ASP A 94 0.271 3.244 -9.468 1.00 12.54 C
1643	ATOM 704 O ASP A 94 1.339 2.859 -9.516 1.00 16.42 O
1644	ATOM 705 CB ASP A 94 -1.010 1.197 -10.262 1.00 12.92 C
1645	ATOM 706 CG ASP A 94 -1.972 1.228 -9.080 1.00 22.91 C
1646	ATOM 707 OD1 ASP A 94 -3.187 1.146 -9.201 1.00 22.17 O
1647	ATOM 708 OD2 ASP A 94 -1.457 1.316 -7.935 1.00 19.01 O
1648	ATOM 709 N PRO A 95 -0.249 3.901 -8.527 1.00 16.46 N
1649	ATOM 710 CA PRO A 95 0.567 4.636 -7.596 1.00 14.67 C
1650	ATOM 711 C PRO A 95 1.260 3.622 -6.816 1.00 17.74 C
1651	ATOM 712 O PRO A 95 2.400 4.046 -6.219 1.00 22.38 O
1652	ATOM 713 CB PRO A 95 -0.368 5.238 -6.654 1.00 22.16 C
1653	ATOM 714 CG PRO A 95 -1.377 5.777 -7.565 1.00 21.38 C
1654	ATOM 715 CD PRO A 95 -1.576 4.623 -8.536 1.00 20.78 C
1655	ATOM 716 N VAL A 96 0.927 2.374 -6.618 1.00 13.01 N
1656	ATOM 717 CA VAL A 96 1.730 1.539 -5.762 1.00 11.93 C
1657	ATOM 718 C VAL A 96 3.098 1.350 -6.142 1.00 21.27 C
1658	ATOM 719 O VAL A 96 4.069 1.031 -5.537 1.00 16.07 O
1659	ATOM 720 CB VAL A 96 0.857 0.099 -5.620 1.00 29.83 C
1660	ATOM 721 CG1 VAL A 96 0.923 -0.687 -6.401 1.00 48.43 C
1661	ATOM 722 CG2 VAL A 96 1.322 -0.240 -4.779 1.00 70.91 C
1662	ATOM 723 N ASN A 97 3.269 1.470 -7.559 1.00 15.63 N
1663	ATOM 724 CA ASN A 97 4.615 1.047 -8.098 1.00 10.10 C
1664	ATOM 725 C ASN A 97 5.675 2.262 -7.895 1.00 4.91 C
1665	ATOM 726 O ASN A 97 6.828 1.839 -7.860 1.00 9.67 O
1666	ATOM 727 CB ASN A 97 4.581 0.892 -9.670 1.00 13.43 C
1667	ATOM 728 CG ASN A 97 3.716 -0.282 -9.938 1.00 17.91 C
1668	ATOM 729 OD1 ASN A 97 4.086 -1.378 -9.937 1.00 10.92 O
1669	ATOM 730 ND2 ASN A 97 2.339 0.119 -10.294 1.00 21.96 N
1670	ATOM 731 N PHE A 98 5.251 3.390 -7.458 1.00 9.20 N
1671	ATOM 732 CA PHE A 98 6.132 4.482 -7.110 1.00 12.10 C
1672	ATOM 733 C PHE A 98 6.958 4.075 -5.773 1.00 12.02 C
1673	ATOM 734 O PHE A 98 8.240 4.323 -5.676 1.00 11.50 O
1674	ATOM 735 CB PHE A 98 5.590 5.923 -6.936 1.00 16.66 C
1675	ATOM 736 CG PHE A 98 5.051 6.336 -8.208 1.00 14.23 C
1676	ATOM 737 CD1 PHE A 98 5.894 7.220 -8.806 1.00 16.70 C
1677	ATOM 738 CD2 PHE A 98 3.842 5.962 -8.759 1.00 12.76 C
1678	ATOM 739 CE1 PHE A 98 5.529 7.688 -9.904 1.00 23.57 C
1679	ATOM 740 CE2 PHE A 98 3.513 6.440 -10.107 1.00 15.74 C
1680	ATOM 741 CZ PHE A 98 4.374 7.231 -10.516 1.00 17.50 C
1681	ATOM 742 N LYS A 99 6.362 3.356 -4.846 1.00 13.69 N
1682	ATOM 743 CA LYS A 99 7.109 2.770 -3.687 1.00 13.57 C
1683	ATOM 744 C LYS A 99 7.912 1.744 -3.941 1.00 14.35 C
1684	ATOM 745 O LYS A 99 9.044 1.864 -3.350 1.00 13.29 O
1685	ATOM 746 CB LYS A 99 5.909 2.378 -2.665 1.00 22.01 C
1686	ATOM 747 CG LYS A 99 5.016 2.967 -2.454 1.00 54.35 C
1687	ATOM 748 CD LYS A 99 4.488 3.000 -1.609 1.00 72.56 C
1688	ATOM 749 CE LYS A 99 2.959 1.795 -1.600 1.00 73.99 C
1689	ATOM 750 NZ LYS A 99 1.741 2.896 -0.134 1.00 80.12 N
1690	ATOM 751 N LEU A 100 7.785 1.013 -5.037 1.00 9.89 N
1691	ATOM 752 CA LEU A 100 8.665 -0.028 -5.354 1.00 8.80 C
1692	ATOM 753 C LEU A 100 9.884 0.546 -6.019 1.00 9.28 C
1693	ATOM 754 O LEU A 100 11.014 0.165 -5.616 1.00 12.09 O
1694	ATOM 755 CB LEU A 100 8.009 -1.084 -6.185 1.00 11.00 C
1695	ATOM 756 CG LEU A 100 6.724 -1.520 -5.691 1.00 16.83 C
1696	ATOM 757 CD1 LEU A 100 6.069 -2.688 -6.703 1.00 20.94 C
1697	ATOM 758 CD2 LEU A 100 7.065 -2.491 -4.548 1.00 18.49 C
1698	ATOM 759 N LEU A 101 9.812 1.484 -6.927 1.00 8.39 N
1699	ATOM 760 CA LEU A 101 10.986 2.076 -7.511 1.00 10.30 C
1700	ATOM 761 C LEU A 101 11.701 2.979 -6.551 1.00 14.49 C
1701	ATOM 762 O LEU A 101 12.986 2.948 -6.333 1.00 16.14 O
1702	ATOM 763 CB LEU A 101 10.485 2.971 -8.570 1.00 11.44 C
1703	ATOM 764 CG LEU A 101 11.708 3.704 -9.282 1.00 15.06 C
1704	ATOM 765 CD1 LEU A 101 12.805 2.937 -9.771 1.00 17.72 C
1705	ATOM 766 CD2 LEU A 101 11.060 4.651 -10.427 1.00 19.38 C
1706	ATOM 767 N SER A 102 11.019 3.662 -5.475 1.00 15.17 N
1707	ATOM 768 CA SER A 102 11.653 4.426 -4.454 1.00 9.19 C
1708	ATOM 769 C SER A 102 12.577 3.423 -3.620 1.00 9.91 C
1709	ATOM 770 O SER A 102 13.768 3.831 -3.267 1.00 14.07 O
1710	ATOM 771 CB SER A 102 10.597 5.003 -3.570 1.00 12.36 C
1711	ATOM 772 OG SER A 102 9.919 6.079 -4.248 1.00 16.52 O
1712	ATOM 773 N HIS A 103 12.034 2.275 -3.168 1.00 12.27 N
1713	ATOM 774 CA HIS A 103 12.685 1.217 -2.471 1.00 10.16 C
1714	ATOM 775 C HIS A 103 14.063 1.009 -3.068 1.00 13.13 C
1715	ATOM 776 O HIS A 103 15.226 0.862 -2.602 1.00 13.37 O
1716	ATOM 777 CB HIS A 103 11.949 0.073 -2.013 1.00 12.31 C
1717	ATOM 778 CG HIS A 103 12.674 -1.002 -1.380 1.00 10.33 C
1718	ATOM 779 ND1 HIS A 103 12.899 -2.229 -2.007 1.00 10.01 N
1719	ATOM 780 CD2 HIS A 103 13.318 -0.937 -0.179 1.00 9.56 C
1720	ATOM 781 CE1 HIS A 103 13.687 -2.798 -1.043 1.00 12.63 C
1721	ATOM 782 NE2 HIS A 103 14.053 -2.093 0.083 1.00 10.77 N
1722	ATOM 783 N CYS A 104 13.914 0.657 -4.439 1.00 11.06 N
1723	ATOM 784 CA CYS A 104 15.233 0.205 -5.307 1.00 11.72 C
1724	ATOM 785 C CYS A 104 16.049 1.418 -5.518 1.00 9.58 C
1725	ATOM 786 O CYS A 104 17.228 1.081 -5.567 1.00 14.10 O
1726	ATOM 787 CB CYS A 104 14.671 -0.439 -6.552 1.00 16.81 C
1727	ATOM 788 SG CYS A 104 13.797 -1.958 -6.414 1.00 14.76 S
1728	ATOM 789 N LEU A 105 15.618 2.594 -5.516 1.00 7.99 N
1729	ATOM 790 CA LEU A 105 16.723 3.634 -5.593 1.00 10.43 C
1730	ATOM 791 C LEU A 105 17.448 3.890 -4.202 1.00 11.96 C
1731	ATOM 792 O LEU A 105 18.594 3.985 -4.326 1.00 15.19 O
1732	ATOM 793 CB LEU A 105 15.765 4.895 -6.092 1.00 16.93 C
1733	ATOM 794 CG LEU A 105 15.765 5.438 -7.260 1.00 44.57 C
1734	ATOM 795 CD1 LEU A 105 14.641 6.498 -7.442 1.00 40.98 C
1735	ATOM 796 CD2 LEU A 105 16.687 5.564 -8.008 1.00 33.21 C
1736	ATOM 797 N LEU A 106 16.617 3.676 -3.143 1.00 10.40 N
1737	ATOM 798 CA LEU A 106 17.322 3.635 -1.869 1.00 15.02 C
1738	ATOM 799 C LEU A 106 18.190 2.641 -1.668 1.00 13.79 C
1739	ATOM 800 O LEU A 106 19.481 2.857 -1.263 1.00 13.12 O
1740	ATOM 801 CB LEU A 106 16.241 3.634 -0.757 1.00 16.59 C
1741	ATOM 802 CG LEU A 106 15.821 4.348 0.036 1.00 26.87 C
1742	ATOM 803 CD1 LEU A 106 14.832 4.036 0.973 1.00 28.01 C
1743	ATOM 804 CD2 LEU A 106 16.399 5.824 0.153 1.00 18.73 C
1744	ATOM 805 N VAL A 107 18.054 1.391 -2.126 1.00 9.58 N
1745	ATOM 806 CA VAL A 107 18.953 0.372 -2.172 1.00 10.69 C
1746	ATOM 807 C VAL A 107 20.116 0.640 -3.008 1.00 12.39 C
1747	ATOM 808 O VAL A 107 21.316 0.322 -2.651 1.00 13.09 O
1748	ATOM 809 CB VAL A 107 18.301 -0.968 -2.671 1.00 14.48 C
1749	ATOM 810 CG1 VAL A 107 19.286 -1.955 -2.913 1.00 19.64 C
1750	ATOM 811 CG2 VAL A 107 17.236 -1.532 -1.566 1.00 13.81 C
1751	ATOM 812 N THR A 108 19.963 1.288 -4.127 1.00 12.66 N
1752	ATOM 813 CA THR A 108 21.110 1.595 -5.027 1.00 11.04 C
1753	ATOM 814 C THR A 108 21.986 2.516 -4.350 1.00 11.25 C
1754	ATOM 815 O THR A 108 23.209 2.402 -4.407 1.00 13.68 O
1755	ATOM 816 CB THR A 108 20.373 2.089 -6.467 1.00 8.55 C
1756	ATOM 817 OG1 THR A 108 19.740 1.009 -7.110 1.00 9.51 O
1757	ATOM 818 CG2 THR A 108 21.547 2.322 -7.342 1.00 15.85 C
1758	ATOM 819 N LEU A 109 21.371 3.638 -3.771 1.00 11.20 N
1759	ATOM 820 CA LEU A 109 22.189 4.682 -3.080 1.00 12.61 C
1760	ATOM 821 C LEU A 109 23.015 3.976 -1.882 1.00 16.09 C
1761	ATOM 822 O LEU A 109 24.210 4.291 -1.739 1.00 14.60 O
1762	ATOM 823 CB LEU A 109 21.280 5.707 -2.657 1.00 17.08 C
1763	ATOM 824 CG LEU A 109 20.748 6.795 -3.713 1.00 24.50 C
1764	ATOM 825 CD1 LEU A 109 19.679 7.424 -3.306 1.00 22.52 C
1765	ATOM 826 CD2 LEU A 109 21.379 6.943 -4.782 1.00 32.08 C
1766	ATOM 827 N ALA A 110 22.243 3.090 -1.228 1.00 13.55 N
1767	ATOM 828 CA ALA A 110 22.985 2.551 -0.107 1.00 19.86 C
1768	ATOM 829 C ALA A 110 24.128 1.797 -0.396 1.00 18.59 C
1769	ATOM 830 O ALA A 110 25.285 1.654 0.094 1.00 14.76 O
1770	ATOM 831 CB ALA A 110 21.957 1.572 0.573 1.00 17.34 C
1771	ATOM 832 N ALA A 111 24.211 0.998 -1.558 1.00 15.15 N
1772	ATOM 833 CA ALA A 111 25.062 0.161 -2.216 1.00 13.42 C
1773	ATOM 834 C ALA A 111 26.376 1.017 -2.643 1.00 16.84 C
1774	ATOM 835 O ALA A 111 27.331 0.420 -2.883 1.00 21.50 O
1775	ATOM 836 CB ALA A 111 24.726 -0.813 -3.252 1.00 16.85 C
1776	ATOM 837 N HIS A 112 26.089 2.220 -3.063 1.00 17.71 N
1777	ATOM 838 CA HIS A 112 27.174 3.032 -3.686 1.00 25.83 C
1778	ATOM 839 C HIS A 112 27.556 4.174 -2.656 1.00 21.86 C
1779	ATOM 840 O HIS A 112 28.710 4.609 -3.162 1.00 23.07 O
1780	ATOM 841 CB HIS A 112 26.642 3.736 -5.093 1.00 17.12 C
1781	ATOM 842 CG HIS A 112 26.500 2.730 -6.083 1.00 18.91 C
1782	ATOM 843 ND1 HIS A 112 27.696 2.669 -6.792 1.00 20.25 N
1783	ATOM 844 CD2 HIS A 112 25.457 2.082 -6.643 1.00 13.97 C
1784	ATOM 845 CE1 HIS A 112 27.065 1.572 -7.791 1.00 16.16 C
1785	ATOM 846 NE2 HIS A 112 25.728 1.142 -7.624 1.00 16.17 N
1786	ATOM 847 N LEU A 113 26.962 4.473 -1.633 1.00 16.18 N
1787	ATOM 848 CA LEU A 113 27.430 5.708 -0.856 1.00 18.52 C
1788	ATOM 849 C LEU A 113 27.676 5.161 0.490 1.00 15.09 C
1789	ATOM 850 O LEU A 113 26.991 5.652 1.418 1.00 22.00 O
1790	ATOM 851 CB LEU A 113 26.385 6.569 -0.567 1.00 26.60 C
1791	ATOM 852 CG LEU A 113 25.991 7.546 -1.915 1.00 26.91 C
1792	ATOM 853 CD1 LEU A 113 25.025 8.844 -1.799 1.00 38.78 C
1793	ATOM 854 CD2 LEU A 113 27.117 7.882 -2.870 1.00 35.29 C
1794	ATOM 855 N PRO A 114 28.523 4.242 0.795 1.00 18.92 N
1795	ATOM 856 CA PRO A 114 28.714 3.528 2.218 1.00 24.61 C
1796	ATOM 857 C PRO A 114 29.102 4.799 3.218 1.00 23.92 C
1797	ATOM 858 O PRO A 114 28.415 4.826 4.106 1.00 21.99 O
1798	ATOM 859 CB PRO A 114 30.033 2.940 1.849 1.00 23.94 C
1799	ATOM 860 CG PRO A 114 30.698 3.344 0.612 1.00 18.92 C
1800	ATOM 861 CD PRO A 114 29.469 3.904 -0.168 1.00 16.59 C
1801	ATOM 862 N ALA A 115 29.794 5.877 2.767 1.00 18.42 N
1802	ATOM 863 CA ALA A 115 30.159 6.863 3.921 1.00 21.98 C
1803	ATOM 864 C ALA A 115 28.895 7.716 4.285 1.00 22.41 C
1804	ATOM 865 O ALA A 115 28.703 8.192 5.284 1.00 22.94 O
1805	ATOM 866 CB ALA A 115 31.247 7.657 3.369 1.00 30.20 C
1806	ATOM 867 N GLU A 116 28.136 8.035 3.290 1.00 15.58 N
1807	ATOM 868 CA GLU A 116 27.073 9.160 3.429 1.00 17.43 C
1808	ATOM 869 C GLU A 116 25.648 8.548 3.788 1.00 15.97 C
1809	ATOM 870 O GLU A 116 24.768 9.367 4.171 1.00 23.49 O
1810	ATOM 871 CB GLU A 116 26.875 9.750 1.910 1.00 21.21 C
1811	ATOM 872 CG GLU A 116 27.948 10.674 1.482 1.00 24.18 C
1812	ATOM 873 CD GLU A 116 28.950 9.665 0.967 1.00 26.12 C
1813	ATOM 874 OE1 GLU A 116 28.992 8.438 0.543 1.00 28.16 O
1814	ATOM 875 OE2 GLU A 116 30.132 10.301 0.462 1.00 33.82 O
1815	ATOM 876 N PHE A 117 25.414 7.310 3.661 1.00 16.62 N
1816	ATOM 877 CA PHE A 117 24.245 6.614 3.985 1.00 14.17 C
1817	ATOM 878 C PHE A 117 23.918 6.335 5.559 1.00 17.74 C
1818	ATOM 879 O PHE A 117 23.649 5.222 5.819 1.00 19.92 O
1819	ATOM 880 CB PHE A 117 23.936 5.421 3.086 1.00 12.47 C
1820	ATOM 881 CG PHE A 117 22.448 4.906 2.825 1.00 9.61 C
1821	ATOM 882 CD1 PHE A 117 21.681 5.713 2.037 1.00 15.09 C
1822	ATOM 883 CD2 PHE A 117 22.071 3.807 3.568 1.00 15.73 C
1823	ATOM 884 CE1 PHE A 117 20.396 5.197 1.858 1.00 17.90 C
1824	ATOM 885 CE2 PHE A 117 20.593 3.448 3.517 1.00 23.05 C
1825	ATOM 886 CZ PHE A 117 19.914 4.171 2.606 1.00 14.00 C
1826	ATOM 887 N THR A 118 23.856 7.434 6.252 1.00 11.56 N
1827	ATOM 888 CA THR A 118 23.660 7.280 7.655 1.00 10.93 C
1828	ATOM 889 C THR A 118 22.259 6.982 7.820 1.00 15.34 C
1829	ATOM 890 O THR A 118 21.447 7.435 7.051 1.00 14.33 O
1830	ATOM 891 CB THR A 118 23.982 8.621 8.138 1.00 22.78 C
1831	ATOM 892 OG1 THR A 118 23.375 9.780 7.827 1.00 25.00 O
1832	ATOM 893 CG2 THR A 118 25.586 8.842 8.226 1.00 25.00 C
1833	ATOM 894 N PRO A 119 21.833 6.884 9.086 1.00 16.93 N
1834	ATOM 895 CA PRO A 119 20.398 6.708 9.436 1.00 7.97 C
1835	ATOM 896 C PRO A 119 19.633 7.821 9.121 1.00 9.71 C
1836	ATOM 897 O PRO A 119 18.484 7.899 8.632 1.00 13.14 O
1837	ATOM 898 CB PRO A 119 20.352 6.336 10.909 1.00 15.02 C
1838	ATOM 899 CG PRO A 119 21.556 5.500 11.105 1.00 20.08 C
1839	ATOM 900 CD PRO A 119 22.686 6.188 10.125 1.00 23.85 C
1840	ATOM 901 N ALA A 120 20.184 9.026 9.484 1.00 18.30 N
1841	ATOM 902 CA ALA A 120 19.624 10.215 9.304 1.00 20.48 C
1842	ATOM 903 C ALA A 120 19.441 10.650 7.769 1.00 11.11 C
1843	ATOM 904 O ALA A 120 18.342 11.025 7.255 1.00 14.90 O
1844	ATOM 905 CB ALA A 120 20.042 11.527 10.014 1.00 21.25 C
1845	ATOM 906 N VAL A 121 20.278 10.312 7.027 1.00 15.02 N
1846	ATOM 907 CA VAL A 121 20.243 10.488 5.614 1.00 11.64 C
1847	ATOM 908 C VAL A 121 19.214 9.526 4.899 1.00 13.80 C
1848	ATOM 909 O VAL A 121 18.469 9.919 4.066 1.00 15.60 O
1849	ATOM 910 CB VAL A 121 21.606 10.473 4.939 1.00 16.28 C
1850	ATOM 911 CG1 VAL A 121 21.595 10.524 3.309 1.00 17.80 C
1851	ATOM 912 CG2 VAL A 121 22.496 11.659 5.330 1.00 19.30 C
1852	ATOM 913 N HIS A 122 19.312 8.350 5.306 1.00 15.45 N
1853	ATOM 914 CA HIS A 122 18.254 7.136 4.913 1.00 11.57 C
1854	ATOM 915 C HIS A 122 16.950 7.952 5.022 1.00 13.88 C
1855	ATOM 916 O HIS A 122 16.085 7.716 4.230 1.00 13.87 O
1856	ATOM 917 CB HIS A 122 18.754 5.950 5.667 1.00 12.36 C
1857	ATOM 918 CG HIS A 122 17.848 4.887 5.471 1.00 15.49 C
1858	ATOM 919 ND1 HIS A 122 18.318 3.588 6.013 1.00 14.41 N
1859	ATOM 920 CD2 HIS A 122 16.770 4.643 4.716 1.00 16.00 C
1860	ATOM 921 CE1 HIS A 122 17.238 2.617 5.530 1.00 20.76 C
1861	ATOM 922 NE2 HIS A 122 16.304 3.230 4.756 1.00 17.17 N
1862	ATOM 923 N ALA A 123 16.659 8.268 6.248 1.00 12.31 N
1863	ATOM 924 CA ALA A 123 15.409 8.791 6.637 1.00 12.34 C
1864	ATOM 925 C ALA A 123 14.961 9.969 5.694 1.00 12.36 C
1865	ATOM 926 O ALA A 123 13.756 10.012 5.125 1.00 16.22 O
1866	ATOM 927 CB ALA A 123 15.295 9.229 8.074 1.00 18.20 C
1867	ATOM 928 N SER A 124 15.970 10.909 5.411 1.00 11.72 N
1868	ATOM 929 CA SER A 124 15.641 12.024 4.678 1.00 15.71 C
1869	ATOM 930 C SER A 124 15.409 11.594 3.146 1.00 11.97 C
1870	ATOM 931 O SER A 124 14.491 12.176 2.530 1.00 13.78 O
1871	ATOM 932 CB SER A 124 16.719 13.075 4.649 1.00 17.31 C
1872	ATOM 933 OG SER A 124 16.856 13.618 5.975 1.00 19.36 O
1873	ATOM 934 N LEU A 125 16.244 10.663 2.745 1.00 11.45 N
1874	ATOM 935 CA LEU A 125 16.012 10.336 1.348 1.00 9.77 C
1875	ATOM 936 C LEU A 125 14.814 9.607 1.165 1.00 13.87 C
1876	ATOM 937 O LEU A 125 14.134 9.697 0.072 1.00 12.03 O
1877	ATOM 938 CB LEU A 125 17.131 9.446 0.945 1.00 14.61 C
1878	ATOM 939 CG LEU A 125 18.555 9.965 0.565 1.00 15.39 C
1879	ATOM 940 CD1 LEU A 125 19.590 8.976 0.528 1.00 26.84 C
1880	ATOM 941 CD2 LEU A 125 18.455 10.851 -0.577 1.00 19.46 C
1881	ATOM 942 N ASP A 126 14.277 8.735 2.034 1.00 13.89 N
1882	ATOM 943 CA ASP A 126 13.042 7.997 2.040 1.00 14.28 C
1883	ATOM 944 C ASP A 126 11.977 8.930 1.898 1.00 13.60 C
1884	ATOM 945 O ASP A 126 10.911 8.959 1.188 1.00 12.25 O
1885	ATOM 946 CB ASP A 126 12.901 7.025 3.127 1.00 9.77 C
1886	ATOM 947 CG ASP A 126 11.751 5.958 3.086 1.00 17.51 C
1887	ATOM 948 OD1 ASP A 126 11.597 5.517 1.933 1.00 22.67 O
1888	ATOM 949 OD2 ASP A 126 10.812 6.013 3.738 1.00 20.83 O
1889	ATOM 950 N LYS A 127 11.945 10.077 2.732 1.00 11.87 N
1890	ATOM 951 CA LYS A 127 11.051 11.143 2.756 1.00 11.94 C
1891	ATOM 952 C LYS A 127 11.080 11.794 1.382 1.00 16.34 C
1892	ATOM 953 O LYS A 127 9.925 12.173 0.922 1.00 15.26 O
1893	ATOM 954 CB LYS A 127 11.131 11.830 4.210 1.00 27.23 C
1894	ATOM 955 CG LYS A 127 10.719 12.405 4.298 1.00 41.38 C
1895	ATOM 956 CD LYS A 127 10.893 12.716 6.240 1.00 22.35 C
1896	ATOM 957 CE LYS A 127 10.245 13.990 6.093 1.00 24.85 C
1897	ATOM 958 NZ LYS A 127 10.431 14.893 7.319 1.00 27.43 N
1898	ATOM 959 N PHE A 128 12.109 12.155 0.978 1.00 9.60 N
1899	ATOM 960 CA PHE A 128 12.219 12.896 -0.315 1.00 9.45 C
1900	ATOM 961 C PHE A 128 11.648 12.055 -1.437 1.00 11.35 C
1901	ATOM 962 O PHE A 128 10.825 12.624 -2.222 1.00 13.72 O
1902	ATOM 963 CB PHE A 128 13.691 13.118 -0.597 1.00 10.04 C
1903	ATOM 964 CG PHE A 128 13.845 13.645 -2.016 1.00 12.71 C
1904	ATOM 965 CD1 PHE A 128 13.433 15.022 -2.350 1.00 22.47 C
1905	ATOM 966 CD2 PHE A 128 14.442 12.953 -2.821 1.00 15.10 C
1906	ATOM 967 CE1 PHE A 128 13.646 15.369 -3.684 1.00 21.90 C
1907	ATOM 968 CE2 PHE A 128 15.006 13.229 -4.197 1.00 24.41 C
1908	ATOM 969 CZ PHE A 128 14.491 14.511 -4.397 1.00 19.00 C
1909	ATOM 970 N LEU A 129 11.863 10.701 -1.438 1.00 10.92 N
1910	ATOM 971 CA LEU A 129 11.247 9.983 -2.588 1.00 8.59 C
1911	ATOM 972 C LEU A 129 9.888 9.762 -2.445 1.00 15.58 C
1912	ATOM 973 O LEU A 129 9.123 9.780 -3.420 1.00 12.33 O
1913	ATOM 974 CB LEU A 129 11.971 8.639 -2.709 1.00 11.08 C
1914	ATOM 975 CG LEU A 129 13.553 8.574 -3.067 1.00 16.43 C
1915	ATOM 976 CD1 LEU A 129 14.162 7.385 -2.920 1.00 21.21 C
1916	ATOM 977 CD2 LEU A 129 13.509 9.197 -4.648 1.00 24.11 C
1917	ATOM 978 N ALA A 130 9.315 9.777 -1.285 1.00 13.59 N
1918	ATOM 979 CA ALA A 130 7.861 9.751 -0.992 1.00 12.80 C
1919	ATOM 980 C ALA A 130 7.198 11.000 -1.487 1.00 13.10 C
1920	ATOM 981 O ALA A 130 6.124 11.123 -2.087 1.00 16.72 O
1921	ATOM 982 CB ALA A 130 7.566 9.549 0.507 1.00 11.70 C
1922	ATOM 983 N SER A 131 7.929 12.205 -1.316 1.00 12.15 N
1923	ATOM 984 CA SER A 131 7.318 13.421 -1.788 1.00 17.97 C
1924	ATOM 985 C SER A 131 7.403 13.484 -3.383 1.00 14.23 C
1925	ATOM 986 O SER A 131 6.313 14.078 -3.819 1.00 17.89 O
1926	ATOM 987 CB SER A 131 8.230 14.652 -1.217 1.00 19.09 C
1927	ATOM 988 OG SER A 131 7.985 14.599 -0.027 1.00 34.89 O
1928	ATOM 989 N VAL A 132 8.509 13.092 -3.817 1.00 11.02 N
1929	ATOM 990 CA VAL A 132 8.474 13.187 -5.332 1.00 13.44 C
1930	ATOM 991 C VAL A 132 7.379 12.239 -5.739 1.00 13.26 C
1931	ATOM 992 O VAL A 132 6.574 12.766 -6.727 1.00 14.28 O
1932	ATOM 993 CB VAL A 132 9.676 12.669 -5.775 1.00 17.47 C
1933	ATOM 994 CG1 VAL A 132 9.886 12.366 -7.268 1.00 23.96 C
1934	ATOM 995 CG2 VAL A 132 10.893 13.605 -5.556 1.00 15.24 C
1935	ATOM 996 N SER A 133 7.084 11.034 -5.279 1.00 11.44 N
1936	ATOM 997 CA SER A 133 6.003 10.145 -5.616 1.00 14.28 C
1937	ATOM 998 C SER A 133 4.653 10.824 -5.346 1.00 22.70 C
1938	ATOM 999 O SER A 133 3.857 10.661 -6.312 1.00 18.73 O
1939	ATOM 1000 CB SER A 133 6.206 8.913 -4.797 1.00 14.07 C
1940	ATOM 1001 OG SER A 133 7.326 8.157 -5.136 1.00 16.41 O
1941	ATOM 1002 N THR A 134 4.415 11.603 -4.390 1.00 14.75 N
1942	ATOM 1003 CA THR A 134 3.185 12.188 -4.293 1.00 11.93 C
1943	ATOM 1004 C THR A 134 3.018 13.180 -5.135 1.00 12.33 C
1944	ATOM 1005 O THR A 134 1.906 13.411 -5.657 1.00 15.87 O
1945	ATOM 1006 CB THR A 134 3.337 12.691 -2.840 1.00 23.98 C
1946	ATOM 1007 OG1 THR A 134 3.226 11.963 -1.926 1.00 24.65 O
1947	ATOM 1008 CG2 THR A 134 2.127 13.740 -2.527 1.00 35.48 C
1948	ATOM 1009 N VAL A 135 3.914 14.063 -5.633 1.00 16.85 N
1949	ATOM 1010 CA VAL A 135 3.773 15.122 -6.561 1.00 15.02 C
1950	ATOM 1011 C VAL A 135 3.692 14.401 -7.901 1.00 18.49 C
1951	ATOM 1012 O VAL A 135 2.676 14.854 -8.623 1.00 17.84 O
1952	ATOM 1013 CB VAL A 135 5.097 16.044 -6.643 1.00 21.41 C
1953	ATOM 1014 CG1 VAL A 135 5.125 16.829 -7.908 1.00 28.88 C
1954	ATOM 1015 CG2 VAL A 135 5.265 16.767 -5.381 1.00 18.54 C
1955	ATOM 1016 N LEU A 136 4.254 13.322 -8.291 1.00 15.13 N
1956	ATOM 1017 CA LEU A 136 3.951 12.616 -9.538 1.00 14.14 C
1957	ATOM 1018 C LEU A 136 2.480 12.083 -9.717 1.00 16.82 C
1958	ATOM 1019 O LEU A 136 2.071 11.725 -10.914 1.00 16.56 O
1959	ATOM 1020 CB LEU A 136 5.082 11.671 -9.878 1.00 19.05 C
1960	ATOM 1021 CG LEU A 136 6.468 12.174 -10.486 1.00 19.99 C
1961	ATOM 1022 CD1 LEU A 136 7.357 11.046 -10.401 1.00 23.33 C
1962	ATOM 1023 CD2 LEU A 136 6.502 13.371 -11.272 1.00 20.84 C
1963	ATOM 1024 N THR A 137 1.951 11.790 -8.618 1.00 14.14 N
1964	ATOM 1025 CA THR A 137 0.509 10.996 -8.584 1.00 17.11 C
1965	ATOM 1026 C THR A 137 -0.385 12.070 -8.267 1.00 15.43 C
1966	ATOM 1027 O THR A 137 -1.637 11.700 -8.230 1.00 15.99 O
1967	ATOM 1028 CB THR A 137 0.560 9.964 -6.978 1.00 17.27 C
1968	ATOM 1029 OG1 THR A 137 1.278 8.939 -8.074 1.00 28.37 O
1969	ATOM 1030 CG2 THR A 137 1.320 10.263 -6.388 1.00 47.04 C
1970	ATOM 1031 N SER A 138 -0.164 13.266 -8.168 1.00 16.91 N
1971	ATOM 1032 CA SER A 138 -0.947 14.363 -7.753 1.00 23.51 C
1972	ATOM 1033 C SER A 138 -2.266 14.743 -8.597 1.00 23.60 C
1973	ATOM 1034 O SER A 138 -3.250 14.937 -8.017 1.00 27.80 O
1974	ATOM 1035 CB SER A 138 0.046 16.222 -7.976 1.00 22.76 C
1975	ATOM 1036 OG SER A 138 -0.261 15.617 -6.862 1.00 45.85 O
1976	ATOM 1037 N LYS A 139 -2.026 14.453 -9.807 1.00 19.13 N
1977	ATOM 1038 CA LYS A 139 -3.058 14.995 -10.892 1.00 21.43 C
1978	ATOM 1039 C LYS A 139 -3.804 13.721 -11.284 1.00 18.35 C
1979	ATOM 1040 O LYS A 139 -4.384 13.814 -12.266 1.00 22.16 O
1980	ATOM 1041 CB LYS A 139 -2.474 15.794 -11.975 1.00 24.13 C
1981	ATOM 1042 CG LYS A 139 -1.839 16.973 -11.481 1.00 28.98 C
1982	ATOM 1043 CD LYS A 139 -0.886 17.619 -12.549 1.00 33.18 C
1983	ATOM 1044 CE LYS A 139 -0.495 18.885 -12.192 1.00 52.82 C
1984	ATOM 1045 NZ LYS A 139 0.788 19.253 -13.621 1.00 55.02 N
1985	ATOM 1046 N TYR A 140 -3.715 12.530 -10.777 1.00 17.12 N
1986	ATOM 1047 CA TYR A 140 -4.275 11.374 -11.162 1.00 22.48 C
1987	ATOM 1048 C TYR A 140 -5.830 11.291 -11.160 1.00 18.75 C
1988	ATOM 1049 O TYR A 140 -6.423 10.704 -12.162 1.00 22.47 O
1989	ATOM 1050 CB TYR A 140 -3.896 10.028 -10.426 1.00 23.15 C
1990	ATOM 1051 CG TYR A 140 -2.655 9.444 -11.006 1.00 15.57 C
1991	ATOM 1052 CD1 TYR A 140 -2.495 7.940 -11.096 1.00 16.98 C
1992	ATOM 1053 CD2 TYR A 140 -1.471 10.093 -11.392 1.00 18.11 C
1993	ATOM 1054 CE1 TYR A 140 -1.296 7.400 -11.625 1.00 19.97 C
1994	ATOM 1055 CE2 TYR A 140 -0.267 9.379 -11.806 1.00 14.94 C
1995	ATOM 1056 CZ TYR A 140 -0.246 7.948 -11.911 1.00 17.89 C
1996	ATOM 1057 OH TYR A 140 0.808 7.493 -12.283 1.00 18.05 O
1997	ATOM 1058 N ARG A 141 -6.399 12.034 -10.391 1.00 17.59 N
1998	ATOM 1059 CA ARG A 141 -8.000 12.137 -10.191 1.00 24.58 C
1999	ATOM 1060 C ARG A 141 -8.327 13.610 -9.572 1.00 44.44 C
2000	ATOM 1061 O ARG A 141 -7.492 14.016 -8.882 1.00 21.81 O
2001	ATOM 1062 CB ARG A 141 -8.478 10.914 -9.869 1.00 33.40 C
2002	ATOM 1063 CG ARG A 141 -8.068 10.650 -8.145 1.00 17.28 C
2003	ATOM 1064 CD ARG A 141 -9.053 9.446 -7.867 1.00 14.66 C
2004	ATOM 1065 NE ARG A 141 -8.372 9.269 -6.610 1.00 22.73 N
2005	ATOM 1066 CZ ARG A 141 -9.233 8.420 -5.781 1.00 26.88 C
2006	ATOM 1067 NH1 ARG A 141 -10.147 7.455 -6.079 1.00 23.24 N
2007	ATOM 1068 NH2 ARG A 141 -8.672 8.328 -4.506 1.00 33.34 N
2008	ATOM 1069 OXT ARG A 141 -9.474 13.682 -9.742 1.00 31.52 O
2009	TER 1070 ARG A 141
2010	ATOM 1071 N VAL B 1 9.223 -20.614 1.365 1.00 46.08 N
2011	ATOM 1072 CA VAL B 1 8.694 -20.026 -0.123 1.00 70.96 C
2012	ATOM 1073 C VAL B 1 9.668 -21.068 -1.645 1.00 69.74 C
2013	ATOM 1074 O VAL B 1 9.370 -22.612 -0.994 1.00 71.82 O
2014	ATOM 1075 CB VAL B 1 9.283 -18.281 -0.381 1.00 59.18 C
2015	ATOM 1076 CG1 VAL B 1 7.449 -17.518 -0.791 1.00 57.89 C
2016	ATOM 1077 CG2 VAL B 1 10.416 -18.038 0.066 1.00 44.20 C
2017	ATOM 1078 N HIS B 2 9.270 -20.650 -2.180 1.00 53.55 N
2018	ATOM 1079 CA HIS B 2 10.245 -21.378 -3.143 1.00 62.62 C
2019	ATOM 1080 C HIS B 2 11.419 -20.331 -4.099 1.00 51.71 C
2020	ATOM 1081 O HIS B 2 11.252 -19.250 -5.024 1.00 48.42 O
2021	ATOM 1082 CB HIS B 2 9.225 -20.955 -4.825 1.00 62.58 C
2022	ATOM 1083 CG HIS B 2 9.378 -21.082 -5.634 1.00 73.96 C
2023	ATOM 1084 ND1 HIS B 2 9.645 -19.683 -6.869 1.00 80.12 N
2024	ATOM 1085 CD2 HIS B 2 10.077 -22.950 -6.116 1.00 63.02 C
2025	ATOM 1086 CE1 HIS B 2 10.672 -21.165 -8.087 1.00 76.40 C
2026	ATOM 1087 NE2 HIS B 2 11.344 -22.584 -7.734 1.00 62.86 N
2027	ATOM 1088 N LEU B 3 12.365 -20.722 -3.649 1.00 43.89 N
2028	ATOM 1089 CA LEU B 3 13.611 -20.183 -4.477 1.00 43.79 C
2029	ATOM 1090 C LEU B 3 14.557 -21.356 -5.125 1.00 32.77 C
2030	ATOM 1091 O LEU B 3 14.340 -22.536 -4.780 1.00 41.84 O
2031	ATOM 1092 CB LEU B 3 14.522 -19.852 -2.996 1.00 28.80 C
2032	ATOM 1093 CG LEU B 3 13.980 -18.598 -2.183 1.00 28.70 C
2033	ATOM 1094 CD1 LEU B 3 14.846 -18.445 -1.199 1.00 63.39 C
2034	ATOM 1095 CD2 LEU B 3 14.509 -17.517 -3.001 1.00 32.10 C
2035	ATOM 1096 N THR B 4 14.840 -20.756 -6.280 1.00 42.35 N
2036	ATOM 1097 CA THR B 4 15.864 -21.825 -6.744 1.00 41.74 C
2037	ATOM 1098 C THR B 4 16.873 -22.187 -6.071 1.00 36.91 C
2038	ATOM 1099 O THR B 4 17.370 -21.395 -5.237 1.00 31.57 O
2039	ATOM 1100 CB THR B 4 15.949 -21.050 -8.090 1.00 38.91 C
2040	ATOM 1101 OG1 THR B 4 16.952 -20.015 -8.082 1.00 52.85 O
2041	ATOM 1102 CG2 THR B 4 14.967 -20.467 -9.056 1.00 56.94 C
2042	ATOM 1103 N PRO B 5 17.854 -23.111 -6.524 1.00 45.56 N
2043	ATOM 1104 CA PRO B 5 18.731 -23.731 -6.023 1.00 47.54 C
2044	ATOM 1105 C PRO B 5 19.935 -22.444 -5.760 1.00 37.80 C
2045	ATOM 1106 O PRO B 5 20.658 -22.372 -4.793 1.00 33.06 O
2046	ATOM 1107 CB PRO B 5 19.534 -24.900 -6.291 1.00 62.12 C
2047	ATOM 1108 CG PRO B 5 18.296 -25.318 -7.157 1.00 42.55 C
2048	ATOM 1109 CD PRO B 5 17.186 -24.560 -7.385 1.00 48.08 C
2049	ATOM 1110 N GLU B 6 19.819 -21.815 -6.978 1.00 27.00 N
2050	ATOM 1111 CA GLU B 6 20.898 -20.991 -7.230 1.00 34.37 C
2051	ATOM 1112 C GLU B 6 20.521 -19.635 -6.155 1.00 23.02 C
2052	ATOM 1113 O GLU B 6 21.687 -18.920 -5.617 1.00 28.54 O
2053	ATOM 1114 CB GLU B 6 20.842 -20.165 -8.661 1.00 37.20 C
2054	ATOM 1115 CG GLU B 6 20.141 -19.957 -9.396 1.00 66.65 C
2055	ATOM 1116 CD GLU B 6 19.153 -21.597 -10.181 1.00 60.44 C
2056	ATOM 1117 OE1 GLU B 6 20.183 -22.830 -9.731 1.00 63.16 O
2057	ATOM 1118 OE2 GLU B 6 18.299 -21.975 -10.007 1.00 70.62 O
2058	ATOM 1119 N GLU B 7 19.362 -19.413 -5.964 1.00 31.47 N
2059	ATOM 1120 CA GLU B 7 18.560 -18.284 -5.124 1.00 34.08 C
2060	ATOM 1121 C GLU B 7 19.160 -18.789 -3.682 1.00 21.49 C
2061	ATOM 1122 O GLU B 7 19.620 -17.847 -3.008 1.00 27.04 O
2062	ATOM 1123 CB GLU B 7 17.625 -18.097 -5.359 1.00 35.55 C
2063	ATOM 1124 CG GLU B 7 17.103 -17.196 -6.791 1.00 33.74 C
2064	ATOM 1125 CD GLU B 7 15.759 -16.911 -6.659 1.00 31.89 C
2065	ATOM 1126 OE1 GLU B 7 15.476 -15.756 -7.225 1.00 52.51 O
2066	ATOM 1127 OE2 GLU B 7 14.748 -17.803 -6.419 1.00 32.56 O
2067	ATOM 1128 N LYS B 8 18.747 -19.865 -3.237 1.00 26.08 N
2068	ATOM 1129 CA LYS B 8 19.026 -20.305 -2.016 1.00 32.23 C
2069	ATOM 1130 C LYS B 8 20.466 -20.216 -1.796 1.00 26.59 C
2070	ATOM 1131 O LYS B 8 21.162 -19.731 -0.601 1.00 26.11 O
2071	ATOM 1132 CB LYS B 8 18.395 -21.925 -1.875 1.00 36.34 C
2072	ATOM 1133 CG LYS B 8 18.802 -22.252 -1.182 1.00 64.20 C
2073	ATOM 1134 CD LYS B 8 18.769 -23.771 -0.248 1.00 73.64 C
2074	ATOM 1135 CE LYS B 8 19.461 -24.137 0.849 1.00 79.30 C
2075	ATOM 1136 NZ LYS B 8 19.874 -26.365 1.034 1.00 66.73 N
2076	ATOM 1137 N SER B 9 21.467 -20.675 -2.533 1.00 23.88 N
2077	ATOM 1138 CA SER B 9 22.559 -20.677 -2.426 1.00 36.76 C
2078	ATOM 1139 C SER B 9 23.490 -19.070 -2.230 1.00 37.61 C
2079	ATOM 1140 O SER B 9 24.284 -18.831 -1.430 1.00 28.84 O
2080	ATOM 1141 CB SER B 9 23.619 -21.853 -3.256 1.00 36.63 C
2081	ATOM 1142 OG SER B 9 23.958 -20.627 -4.033 1.00 64.02 O
2082	ATOM 1143 N ALA B 10 22.719 -18.196 -3.034 1.00 21.54 N
2083	ATOM 1144 CA ALA B 10 23.262 -17.029 -2.963 1.00 32.77 C
2084	ATOM 1145 C ALA B 10 22.792 -16.202 -1.459 1.00 23.64 C
2085	ATOM 1146 O ALA B 10 23.628 -15.408 -0.898 1.00 26.26 O
2086	ATOM 1147 CB ALA B 10 22.504 -16.176 -3.856 1.00 30.88 C
2087	ATOM 1148 N VAL B 11 21.589 -16.575 -0.940 1.00 22.75 N
2088	ATOM 1149 CA VAL B 11 21.174 -16.108 0.417 1.00 18.12 C
2089	ATOM 1150 C VAL B 11 22.242 -16.512 1.434 1.00 18.13 C
2090	ATOM 1151 O VAL B 11 22.655 -15.680 2.245 1.00 19.40 O
2091	ATOM 1152 CB VAL B 11 19.853 -16.542 0.518 1.00 19.48 C
2092	ATOM 1153 CG1 VAL B 11 19.403 -16.415 1.946 1.00 26.15 C
2093	ATOM 1154 CG2 VAL B 11 18.815 -15.702 -0.276 1.00 23.37 C
2094	ATOM 1155 N THR B 12 22.386 -17.775 1.358 1.00 19.01 N
2095	ATOM 1156 CA THR B 12 23.153 -18.592 2.377 1.00 25.04 C
2096	ATOM 1157 C THR B 12 24.569 -18.098 2.437 1.00 20.68 C
2097	ATOM 1158 O THR B 12 25.254 -17.692 3.335 1.00 23.87 O
2098	ATOM 1159 CB THR B 12 23.196 -20.284 2.185 1.00 42.63 C
2099	ATOM 1160 OG1 THR B 12 22.010 -20.433 2.444 1.00 42.78 O
2100	ATOM 1161 CG2 THR B 12 23.729 -20.348 1.974 1.00 67.38 C
2101	ATOM 1162 N ALA B 13 25.190 -17.913 1.267 1.00 22.79 N
2102	ATOM 1163 CA ALA B 13 26.401 -17.387 1.166 1.00 26.66 C
2103	ATOM 1164 C ALA B 13 26.828 -16.135 1.582 1.00 26.26 C
2104	ATOM 1165 O ALA B 13 27.614 -15.809 2.378 1.00 27.07 O
2105	ATOM 1166 CB ALA B 13 26.857 -17.378 -0.445 1.00 26.35 C
2106	ATOM 1167 N LEU B 14 25.928 -14.999 1.236 1.00 15.70 N
2107	ATOM 1168 CA LEU B 14 26.092 -13.737 1.994 1.00 15.10 C
2108	ATOM 1169 C LEU B 14 25.996 -13.791 3.419 1.00 17.25 C
2109	ATOM 1170 O LEU B 14 26.440 -13.013 4.127 1.00 15.43 O
2110	ATOM 1171 CB LEU B 14 25.023 -12.816 1.145 1.00 16.82 C
2111	ATOM 1172 CG LEU B 14 25.284 -11.388 1.257 1.00 27.27 C
2112	ATOM 1173 CD1 LEU B 14 26.470 -10.984 0.911 1.00 40.43 C
2113	ATOM 1174 CD2 LEU B 14 23.923 -10.655 1.151 1.00 24.81 C
2114	ATOM 1175 N TRP B 15 24.847 -14.542 3.847 1.00 17.75 N
2115	ATOM 1176 CA TRP B 15 24.543 -14.533 5.293 1.00 20.73 C
2116	ATOM 1177 C TRP B 15 25.779 -15.040 6.144 1.00 17.66 C
2117	ATOM 1178 O TRP B 15 25.791 -14.500 7.295 1.00 18.75 O
2118	ATOM 1179 CB TRP B 15 23.337 -15.255 5.477 1.00 17.11 C
2119	ATOM 1180 CG TRP B 15 22.785 -14.972 6.964 1.00 17.91 C
2120	ATOM 1181 CD1 TRP B 15 22.809 -15.647 8.020 1.00 21.87 C
2121	ATOM 1182 CD2 TRP B 15 21.992 -13.854 7.213 1.00 17.58 C
2122	ATOM 1183 NE1 TRP B 15 22.135 -15.153 9.079 1.00 18.04 N
2123	ATOM 1184 CE2 TRP B 15 21.659 -13.824 8.669 1.00 16.29 C
2124	ATOM 1185 CE3 TRP B 15 21.610 -12.684 6.475 1.00 16.29 C
2125	ATOM 1186 CZ2 TRP B 15 20.847 -12.810 9.252 1.00 25.87 C
2126	ATOM 1187 CZ3 TRP B 15 20.839 -11.689 7.176 1.00 17.96 C
2127	ATOM 1188 CH2 TRP B 15 20.450 -11.898 8.453 1.00 24.12 C
2128	ATOM 1189 N GLY B 16 26.491 -15.885 5.456 1.00 18.59 N
2129	ATOM 1190 CA GLY B 16 27.793 -16.367 6.203 1.00 18.72 C
2130	ATOM 1191 C GLY B 16 28.640 -15.293 6.479 1.00 24.14 C
2131	ATOM 1192 O GLY B 16 29.526 -15.462 7.418 1.00 24.08 O
2132	ATOM 1193 N LYS B 17 28.533 -14.214 5.902 1.00 16.20 N
2133	ATOM 1194 CA LYS B 17 29.341 -13.100 6.055 1.00 17.17 C
2134	ATOM 1195 C LYS B 17 28.732 -12.165 6.877 1.00 17.84 C
2135	ATOM 1196 O LYS B 17 29.459 -11.044 7.345 1.00 23.03 O
2136	ATOM 1197 CB LYS B 17 29.636 -12.212 4.866 1.00 27.63 C
2137	ATOM 1198 CG LYS B 17 30.260 -13.332 3.793 1.00 26.84 C
2138	ATOM 1199 CD LYS B 17 30.681 -12.758 2.663 1.00 36.92 C
2139	ATOM 1200 CE LYS B 17 31.201 -13.748 1.394 1.00 48.09 C
2140	ATOM 1201 NZ LYS B 17 31.749 -12.471 0.760 1.00 51.60 N
2141	ATOM 1202 N VAL B 18 27.632 -12.163 7.561 1.00 19.79 N
2142	ATOM 1203 CA VAL B 18 26.839 -11.228 8.296 1.00 15.59 C
2143	ATOM 1204 C VAL B 18 27.221 -11.355 9.806 1.00 24.20 C
2144	ATOM 1205 O VAL B 18 27.181 -12.396 10.461 1.00 22.49 O
2145	ATOM 1206 CB VAL B 18 25.375 -11.611 8.249 1.00 13.43 C
2146	ATOM 1207 CG1 VAL B 18 24.680 -10.797 9.203 1.00 20.38 C
2147	ATOM 1208 CG2 VAL B 18 25.124 -10.816 6.753 1.00 25.54 C
2148	ATOM 1209 N ASN B 19 27.508 -10.243 10.525 1.00 20.52 N
2149	ATOM 1210 CA ASN B 19 27.647 -10.334 12.056 1.00 15.58 C
2150	ATOM 1211 C ASN B 19 26.161 -10.008 12.553 1.00 13.56 C
2151	ATOM 1212 O ASN B 19 25.706 -8.798 12.411 1.00 14.77 O
2152	ATOM 1213 CB ASN B 19 28.532 -9.065 12.579 1.00 26.08 C
2153	ATOM 1214 CG ASN B 19 28.340 -8.916 14.065 1.00 29.11 C
2154	ATOM 1215 OD1 ASN B 19 27.732 -9.412 14.784 1.00 27.77 O
2155	ATOM 1216 ND2 ASN B 19 29.702 -8.401 14.383 1.00 33.88 N
2156	ATOM 1217 N VAL B 20 25.621 -11.024 13.009 1.00 18.83 N
2157	ATOM 1218 CA VAL B 20 24.087 -11.031 13.284 1.00 19.05 C
2158	ATOM 1219 C VAL B 20 23.851 -10.149 14.214 1.00 20.02 C
2159	ATOM 1220 O VAL B 20 22.901 -9.142 14.245 1.00 17.50 O
2160	ATOM 1221 CB VAL B 20 23.694 -12.517 13.598 1.00 25.16 C
2161	ATOM 1222 CG1 VAL B 20 22.215 -12.356 13.912 1.00 29.32 C
2162	ATOM 1223 CG2 VAL B 20 23.748 -13.338 12.333 1.00 21.26 C
2163	ATOM 1224 N ASP B 21 24.547 -9.725 15.239 1.00 19.64 N
2164	ATOM 1225 CA ASP B 21 24.274 -8.816 16.395 1.00 20.67 C
2165	ATOM 1226 C ASP B 21 24.562 -7.492 15.870 1.00 18.97 C
2166	ATOM 1227 O ASP B 21 23.606 -6.622 16.080 1.00 21.29 O
2167	ATOM 1228 CB ASP B 21 25.312 -9.108 17.415 1.00 34.10 C
2168	ATOM 1229 CG ASP B 21 25.029 -10.570 18.492 1.00 53.28 C
2169	ATOM 1230 OD1 ASP B 21 23.848 -10.805 18.323 1.00 40.86 O
2170	ATOM 1231 OD2 ASP B 21 25.861 -10.240 19.644 1.00 50.69 O
2171	ATOM 1232 N GLU B 22 25.464 -7.225 14.999 1.00 17.77 N
2172	ATOM 1233 CA GLU B 22 25.739 -5.702 14.538 1.00 21.32 C
2173	ATOM 1234 C GLU B 22 24.523 -5.287 13.546 1.00 17.53 C
2174	ATOM 1235 O GLU B 22 23.957 -4.290 13.703 1.00 21.51 O
2175	ATOM 1236 CB GLU B 22 27.018 -5.846 13.812 1.00 24.38 C
2176	ATOM 1237 CG GLU B 22 27.214 -4.730 13.144 1.00 38.60 C
2177	ATOM 1238 CD GLU B 22 28.169 -3.862 11.812 1.00 75.75 C
2178	ATOM 1239 OE1 GLU B 22 28.555 -5.400 11.034 1.00 53.89 O
2179	ATOM 1240 OE2 GLU B 22 29.808 -4.745 12.821 1.00 65.14 O
2180	ATOM 1241 N VAL B 23 24.347 -6.274 12.578 1.00 19.15 N
2181	ATOM 1242 CA VAL B 23 23.303 -6.039 11.518 1.00 16.52 C
2182	ATOM 1243 C VAL B 23 21.857 -5.985 12.342 1.00 19.25 C
2183	ATOM 1244 O VAL B 23 20.964 -5.128 11.822 1.00 16.10 O
2184	ATOM 1245 CB VAL B 23 23.294 -7.123 10.403 1.00 21.83 C
2185	ATOM 1246 CG1 VAL B 23 22.065 -7.019 9.672 1.00 26.98 C
2186	ATOM 1247 CG2 VAL B 23 24.689 -6.722 9.825 1.00 24.14 C
2187	ATOM 1248 N GLY B 24 21.684 -6.753 13.284 1.00 11.83 N
2188	ATOM 1249 CA GLY B 24 20.512 -6.666 14.003 1.00 15.96 C
2189	ATOM 1250 C GLY B 24 20.131 -5.391 14.689 1.00 15.32 C
2190	ATOM 1251 O GLY B 24 19.133 -4.694 14.628 1.00 13.59 O
2191	ATOM 1252 N GLY B 25 21.093 -4.853 15.395 1.00 19.52 N
2192	ATOM 1253 CA GLY B 25 21.202 -3.549 15.972 1.00 15.79 C
2193	ATOM 1254 C GLY B 25 20.921 -2.401 14.917 1.00 12.82 C
2194	ATOM 1255 O GLY B 25 20.200 -1.481 15.135 1.00 18.05 O
2195	ATOM 1256 N GLU B 26 21.598 -2.510 13.849 1.00 12.16 N
2196	ATOM 1257 CA GLU B 26 21.567 -1.493 12.736 1.00 11.32 C
2197	ATOM 1258 C GLU B 26 20.042 -1.534 12.176 1.00 13.79 C
2198	ATOM 1259 O GLU B 26 19.605 -0.362 11.944 1.00 14.59 O
2199	ATOM 1260 CB GLU B 26 22.564 -1.757 11.778 1.00 13.18 C
2200	ATOM 1261 CG GLU B 26 23.022 -0.301 10.974 1.00 29.90 C
2201	ATOM 1262 CD GLU B 26 23.535 0.894 10.508 1.00 51.34 C
2202	ATOM 1263 OE1 GLU B 26 23.767 -0.209 7.916 1.00 54.93 O
2203	ATOM 1264 OE2 GLU B 26 24.549 -1.302 10.298 1.00 37.93 O
2204	ATOM 1265 N ALA B 27 19.659 -2.698 11.904 1.00 13.14 N
2205	ATOM 1266 CA ALA B 27 18.339 -2.622 11.197 1.00 9.05 C
2206	ATOM 1267 C ALA B 27 17.188 -2.188 12.064 1.00 10.83 C
2207	ATOM 1268 O ALA B 27 16.247 -1.538 11.698 1.00 11.12 O
2208	ATOM 1269 CB ALA B 27 18.124 -4.039 10.850 1.00 14.07 C
2209	ATOM 1270 N LEU B 28 17.097 -2.654 13.364 1.00 11.19 N
2210	ATOM 1271 CA LEU B 28 16.289 -2.225 14.403 1.00 14.47 C
2211	ATOM 1272 C LEU B 28 16.216 -0.842 14.498 1.00 12.13 C
2212	ATOM 1273 O LEU B 28 15.292 -0.024 14.599 1.00 12.32 O
2213	ATOM 1274 CB LEU B 28 16.089 -3.101 15.599 1.00 9.21 C
2214	ATOM 1275 CG LEU B 28 14.602 -2.613 16.344 1.00 20.67 C
2215	ATOM 1276 CD1 LEU B 28 13.558 -3.287 15.723 1.00 17.60 C
2216	ATOM 1277 CD2 LEU B 28 15.036 -3.349 17.556 1.00 34.99 C
2217	ATOM 1278 N GLY B 29 17.488 -0.244 14.733 1.00 10.00 N
2218	ATOM 1279 CA GLY B 29 17.555 1.107 14.942 1.00 15.27 C
2219	ATOM 1280 C GLY B 29 17.147 1.979 13.686 1.00 10.88 C
2220	ATOM 1281 O GLY B 29 16.406 2.945 13.855 1.00 14.42 O
2221	ATOM 1282 N ARG B 30 17.503 1.503 12.514 1.00 11.39 N
2222	ATOM 1283 CA ARG B 30 17.138 2.392 11.410 1.00 14.49 C
2223	ATOM 1284 C ARG B 30 15.517 2.168 11.180 1.00 10.79 C
2224	ATOM 1285 O ARG B 30 14.997 3.218 10.749 1.00 13.81 O
2225	ATOM 1286 CB ARG B 30 17.883 1.854 10.134 1.00 19.88 C
2226	ATOM 1287 CG ARG B 30 19.264 2.550 9.848 1.00 16.11 C
2227	ATOM 1288 CD ARG B 30 19.816 1.919 8.615 1.00 14.71 C
2228	ATOM 1289 NE ARG B 30 21.229 2.190 8.567 1.00 21.05 N
2229	ATOM 1290 CZ ARG B 30 21.899 3.048 7.943 1.00 18.56 C
2230	ATOM 1291 NH1 ARG B 30 21.169 3.859 7.078 1.00 19.13 N
2231	ATOM 1292 NH2 ARG B 30 23.126 3.441 7.930 1.00 19.91 N
2232	ATOM 1293 N LEU B 31 14.954 1.034 11.546 1.00 12.04 N
2233	ATOM 1294 CA LEU B 31 13.557 0.954 11.581 1.00 10.54 C
2234	ATOM 1295 C LEU B 31 13.079 2.129 12.312 1.00 13.93 C
2235	ATOM 1296 O LEU B 31 12.053 2.837 11.993 1.00 14.67 O
2236	ATOM 1297 CB LEU B 31 12.999 -0.394 11.933 1.00 12.99 C
2237	ATOM 1298 CG LEU B 31 11.476 -0.524 12.150 1.00 10.97 C
2238	ATOM 1299 CD1 LEU B 31 11.036 -0.535 10.722 1.00 19.46 C
2239	ATOM 1300 CD2 LEU B 31 11.106 -1.700 13.040 1.00 13.98 C
2240	ATOM 1301 N LEU B 32 13.531 2.329 13.530 1.00 10.13 N
2241	ATOM 1302 CA LEU B 32 12.882 3.156 14.401 1.00 11.52 C
2242	ATOM 1303 C LEU B 32 13.149 4.616 14.057 1.00 12.11 C
2243	ATOM 1304 O LEU B 32 12.467 5.633 14.438 1.00 15.31 O
2244	ATOM 1305 CB LEU B 32 13.453 3.038 15.919 1.00 11.75 C
2245	ATOM 1306 CG LEU B 32 12.805 1.940 16.581 1.00 16.68 C
2246	ATOM 1307 CD1 LEU B 32 12.104 0.941 16.260 1.00 22.26 C
2247	ATOM 1308 CD2 LEU B 32 13.566 1.603 17.835 1.00 28.90 C
2248	ATOM 1309 N VAL B 33 14.250 4.899 13.351 1.00 10.32 N
2249	ATOM 1310 CA VAL B 33 14.628 6.174 12.868 1.00 11.98 C
2250	ATOM 1311 C VAL B 33 13.704 6.548 11.535 1.00 12.10 C
2251	ATOM 1312 O VAL B 33 13.345 7.771 11.481 1.00 13.28 O
2252	ATOM 1313 CB VAL B 33 16.139 6.304 12.522 1.00 14.87 C
2253	ATOM 1314 CG1 VAL B 33 16.518 7.591 11.880 1.00 11.54 C
2254	ATOM 1315 CG2 VAL B 33 16.745 6.275 13.788 1.00 16.57 C
2255	ATOM 1316 N VAL B 34 13.820 5.650 10.638 1.00 13.66 N
2256	ATOM 1317 CA VAL B 34 13.156 6.096 9.258 1.00 9.59 C
2257	ATOM 1318 C VAL B 34 11.591 6.042 9.368 1.00 8.72 C
2258	ATOM 1319 O VAL B 34 11.052 6.910 8.763 1.00 9.42 O
2259	ATOM 1320 CB VAL B 34 13.681 5.042 8.326 1.00 9.09 C
2260	ATOM 1321 CG1 VAL B 34 13.079 5.328 6.958 1.00 9.82 C
2261	ATOM 1322 CG2 VAL B 34 15.076 5.133 8.253 1.00 17.00 C
2262	ATOM 1323 N TYR B 35 11.088 5.155 10.260 1.00 10.80 N
2263	ATOM 1324 CA TYR B 35 9.613 5.019 10.405 1.00 13.73 C
2264	ATOM 1325 C TYR B 35 9.249 5.241 11.959 1.00 14.87 C
2265	ATOM 1326 O TYR B 35 9.056 4.156 12.514 1.00 16.30 O
2266	ATOM 1327 CB TYR B 35 9.162 3.628 9.962 1.00 14.97 C
2267	ATOM 1328 CG TYR B 35 9.590 3.397 8.554 1.00 16.57 C
2268	ATOM 1329 CD1 TYR B 35 9.059 4.138 7.400 1.00 17.11 C
2269	ATOM 1330 CD2 TYR B 35 10.495 2.446 8.096 1.00 21.02 C
2270	ATOM 1331 CE1 TYR B 35 9.473 3.862 6.085 1.00 16.53 C
2271	ATOM 1332 CE2 TYR B 35 10.987 2.455 6.905 1.00 21.07 C
2272	ATOM 1333 CZ TYR B 35 10.434 2.948 5.860 1.00 16.91 C
2273	ATOM 1334 OH TYR B 35 11.073 2.851 4.537 1.00 21.07 O
2274	ATOM 1335 N PRO B 36 9.337 6.384 12.381 1.00 18.32 N
2275	ATOM 1336 CA PRO B 36 9.299 6.665 13.797 1.00 15.72 C
2276	ATOM 1337 C PRO B 36 8.010 6.232 14.403 1.00 27.07 C
2277	ATOM 1338 O PRO B 36 8.028 5.977 15.694 1.00 15.67 O
2278	ATOM 1339 CB PRO B 36 9.448 8.143 14.056 1.00 16.26 C
2279	ATOM 1340 CG PRO B 36 9.504 8.813 12.839 1.00 21.27 C
2280	ATOM 1341 CD PRO B 36 9.498 7.681 11.841 1.00 25.93 C
2281	ATOM 1342 N TRP B 37 6.917 5.884 13.840 1.00 14.10 N
2282	ATOM 1343 CA TRP B 37 5.821 5.395 14.601 1.00 12.74 C
2283	ATOM 1344 C TRP B 37 5.965 3.976 15.036 1.00 15.06 C
2284	ATOM 1345 O TRP B 37 5.268 3.465 15.926 1.00 15.27 O
2285	ATOM 1346 CB TRP B 37 4.670 5.475 13.490 1.00 19.41 C
2286	ATOM 1347 CG TRP B 37 4.766 4.831 12.253 1.00 14.79 C
2287	ATOM 1348 CD1 TRP B 37 4.298 3.513 11.774 1.00 18.82 C
2288	ATOM 1349 CD2 TRP B 37 5.265 5.442 10.984 1.00 18.23 C
2289	ATOM 1350 NE1 TRP B 37 4.669 3.435 10.535 1.00 23.72 N
2290	ATOM 1351 CE2 TRP B 37 5.184 4.400 9.923 1.00 22.13 C
2291	ATOM 1352 CE3 TRP B 37 5.947 6.691 10.672 1.00 21.52 C
2292	ATOM 1353 CZ2 TRP B 37 5.584 4.556 8.589 1.00 18.19 C
2293	ATOM 1354 CZ3 TRP B 37 6.183 6.773 9.398 1.00 31.71 C
2294	ATOM 1355 CH2 TRP B 37 6.069 5.844 8.520 1.00 14.12 C
2295	ATOM 1356 N THR B 38 7.039 3.221 14.646 1.00 14.17 N
2296	ATOM 1357 CA THR B 38 7.466 1.912 14.979 1.00 13.46 C
2297	ATOM 1358 C THR B 38 7.760 1.960 16.519 1.00 16.65 C
2298	ATOM 1359 O THR B 38 8.073 0.918 17.118 1.00 18.86 O
2299	ATOM 1360 CB THR B 38 8.456 1.107 14.212 1.00 12.74 C
2300	ATOM 1361 OG1 THR B 38 9.507 1.962 14.105 1.00 14.09 O
2301	ATOM 1362 CG2 THR B 38 7.863 1.128 12.798 1.00 15.42 C
2302	ATOM 1363 N GLN B 39 8.203 3.108 16.922 1.00 19.91 N
2303	ATOM 1364 CA GLN B 39 8.656 3.567 18.379 1.00 23.22 C
2304	ATOM 1365 C GLN B 39 7.604 3.201 19.358 1.00 19.19 C
2305	ATOM 1366 O GLN B 39 7.968 2.987 20.495 1.00 19.29 O
2306	ATOM 1367 CB GLN B 39 9.277 4.878 18.529 1.00 24.35 C
2307	ATOM 1368 CG GLN B 39 10.405 5.137 17.759 1.00 25.27 C
2308	ATOM 1369 CD GLN B 39 10.983 6.633 17.918 1.00 24.35 C
2309	ATOM 1370 OE1 GLN B 39 10.480 7.189 18.922 1.00 26.75 O
2310	ATOM 1371 NE2 GLN B 39 11.852 7.006 16.956 1.00 30.18 N
2311	ATOM 1372 N ARG B 40 6.347 3.079 18.900 1.00 20.02 N
2312	ATOM 1373 CA ARG B 40 5.184 2.850 19.816 1.00 21.80 C
2313	ATOM 1374 C ARG B 40 5.511 1.455 20.630 1.00 29.36 C
2314	ATOM 1375 O ARG B 40 4.888 1.619 21.749 1.00 24.42 O
2315	ATOM 1376 CB ARG B 40 3.944 2.700 18.938 1.00 16.52 C
2316	ATOM 1377 CG ARG B 40 3.694 1.420 18.404 1.00 20.34 C
2317	ATOM 1378 CD ARG B 40 2.451 1.519 17.302 1.00 25.31 C
2318	ATOM 1379 NE ARG B 40 1.370 1.856 17.810 1.00 29.70 N
2319	ATOM 1380 CZ ARG B 40 0.400 1.022 18.648 1.00 34.46 C
2320	ATOM 1381 NH1 ARG B 40 0.678 -0.097 18.556 1.00 31.34 N
2321	ATOM 1382 NH2 ARG B 40 -0.783 2.010 18.877 1.00 39.12 N
2322	ATOM 1383 N PHE B 41 6.149 0.541 20.453 1.00 19.21 N
2323	ATOM 1384 CA PHE B 41 6.133 -0.730 21.151 1.00 16.53 C
2324	ATOM 1385 C PHE B 41 7.442 -0.621 22.343 1.00 21.34 C
2325	ATOM 1386 O PHE B 41 7.412 -1.538 22.897 1.00 23.45 O
2326	ATOM 1387 CB PHE B 41 6.675 -1.804 20.080 1.00 10.39 C
2327	ATOM 1388 CG PHE B 41 5.553 -1.984 19.152 1.00 13.84 C
2328	ATOM 1389 CD1 PHE B 41 5.763 -1.448 17.828 1.00 17.38 C
2329	ATOM 1390 CD2 PHE B 41 4.239 -2.655 19.578 1.00 25.55 C
2330	ATOM 1391 CE1 PHE B 41 4.713 -1.720 16.922 1.00 15.72 C
2331	ATOM 1392 CE2 PHE B 41 3.272 -2.680 18.459 1.00 21.40 C
2332	ATOM 1393 CZ PHE B 41 3.586 -2.146 17.207 1.00 13.46 C
2333	ATOM 1394 N PHE B 42 8.072 0.397 22.159 1.00 18.41 N
2334	ATOM 1395 CA PHE B 42 9.433 0.476 22.639 1.00 17.88 C
2335	ATOM 1396 C PHE B 42 9.683 1.552 23.631 1.00 26.28 C
2336	ATOM 1397 O PHE B 42 10.712 1.963 24.025 1.00 30.16 O
2337	ATOM 1398 CB PHE B 42 10.561 0.553 21.602 1.00 16.57 C
2338	ATOM 1399 CG PHE B 42 10.524 -0.621 20.906 1.00 18.87 C
2339	ATOM 1400 CD1 PHE B 42 10.208 -0.431 19.261 1.00 17.08 C
2340	ATOM 1401 CD2 PHE B 42 10.804 -1.937 21.065 1.00 17.75 C
2341	ATOM 1402 CE1 PHE B 42 10.137 -1.716 18.672 1.00 12.34 C
2342	ATOM 1403 CE2 PHE B 42 10.625 -2.998 20.314 1.00 16.32 C
2343	ATOM 1404 CZ PHE B 42 10.370 -2.870 18.826 1.00 14.29 C
2344	ATOM 1405 N GLU B 43 8.703 2.022 24.176 1.00 32.94 N
2345	ATOM 1406 CA GLU B 43 9.021 3.274 25.060 1.00 42.17 C
2346	ATOM 1407 C GLU B 43 9.315 2.924 26.617 1.00 21.09 C
2347	ATOM 1408 O GLU B 43 10.204 3.362 27.291 1.00 37.55 O
2348	ATOM 1409 CB GLU B 43 7.798 3.586 25.059 1.00 73.91 C
2349	ATOM 1410 CG GLU B 43 6.528 3.291 25.915 1.00 61.81 C
2350	ATOM 1411 CD GLU B 43 4.777 4.930 25.558 1.00 78.77 C
2351	ATOM 1412 OE1 GLU B 43 5.276 5.543 25.252 1.00 63.33 O
2352	ATOM 1413 OE2 GLU B 43 4.274 3.783 26.403 1.00 59.41 O
2353	ATOM 1414 N SER B 44 9.424 1.477 26.805 1.00 22.68 N
2354	ATOM 1415 CA SER B 44 10.261 0.951 28.039 1.00 28.45 C
2355	ATOM 1416 C SER B 44 11.527 1.680 27.935 1.00 36.10 C
2356	ATOM 1417 O SER B 44 12.578 0.776 28.511 1.00 25.24 O
2357	ATOM 1418 CB SER B 44 9.957 -0.409 28.119 1.00 27.61 C
2358	ATOM 1419 OG SER B 44 10.204 -1.503 27.766 1.00 37.26 O
2359	ATOM 1420 N PHE B 45 12.292 1.349 26.626 1.00 28.36 N
2360	ATOM 1421 CA PHE B 45 13.648 1.329 26.186 1.00 25.47 C
2361	ATOM 1422 C PHE B 45 14.197 2.590 26.508 1.00 26.28 C
2362	ATOM 1423 O PHE B 45 15.451 2.670 26.190 1.00 31.39 O
2363	ATOM 1424 CB PHE B 45 13.618 0.947 24.623 1.00 22.10 C
2364	ATOM 1425 CG PHE B 45 13.541 -0.652 24.249 1.00 18.85 C
2365	ATOM 1426 CD1 PHE B 45 13.939 -0.880 22.983 1.00 29.27 C
2366	ATOM 1427 CD2 PHE B 45 12.982 -1.450 24.626 1.00 31.57 C
2367	ATOM 1428 CE1 PHE B 45 13.682 -2.441 22.618 1.00 29.02 C
2368	ATOM 1429 CE2 PHE B 45 12.642 -2.810 24.625 1.00 30.34 C
2369	ATOM 1430 CZ PHE B 45 13.202 -2.999 23.312 1.00 36.33 C
2370	ATOM 1431 N GLY B 46 13.772 3.730 26.937 1.00 39.28 N
2371	ATOM 1432 CA GLY B 46 14.529 4.785 27.301 1.00 46.90 C
2372	ATOM 1433 C GLY B 46 14.720 5.977 26.137 1.00 45.06 C
2373	ATOM 1434 O GLY B 46 13.492 6.152 25.410 1.00 36.42 O
2374	ATOM 1435 N ASP B 47 15.717 6.365 26.037 1.00 38.00 N
2375	ATOM 1436 CA ASP B 47 15.729 7.801 25.184 1.00 38.15 C
2376	ATOM 1437 C ASP B 47 16.096 7.362 23.534 1.00 25.86 C
2377	ATOM 1438 O ASP B 47 16.860 6.380 23.281 1.00 25.46 O
2378	ATOM 1439 CB ASP B 47 17.237 8.136 25.516 1.00 44.07 C
2379	ATOM 1440 CG ASP B 47 17.345 9.494 25.209 1.00 52.06 C
2380	ATOM 1441 OD1 ASP B 47 18.506 10.069 24.917 1.00 44.54 O
2381	ATOM 1442 OD2 ASP B 47 16.192 10.248 24.076 1.00 35.33 O
2382	ATOM 1443 N LEU B 48 14.758 7.696 22.981 1.00 25.27 N
2383	ATOM 1444 CA LEU B 48 14.475 7.473 21.435 1.00 28.75 C
2384	ATOM 1445 C LEU B 48 14.468 8.903 20.740 1.00 27.19 C
2385	ATOM 1446 O LEU B 48 13.953 8.921 19.724 1.00 27.20 O
2386	ATOM 1447 CB LEU B 48 13.484 6.505 21.317 1.00 23.96 C
2387	ATOM 1448 CG LEU B 48 13.754 5.148 21.718 1.00 24.35 C
2388	ATOM 1449 CD1 LEU B 48 12.414 4.237 21.541 1.00 34.74 C
2389	ATOM 1450 CD2 LEU B 48 14.775 4.377 21.408 1.00 34.58 C
2390	ATOM 1451 N SER B 49 15.103 9.812 21.342 1.00 41.94 N
2391	ATOM 1452 CA SER B 49 14.421 11.168 20.634 1.00 46.28 C
2392	ATOM 1453 C SER B 49 15.582 11.613 20.219 1.00 38.86 C
2393	ATOM 1454 O SER B 49 14.817 12.605 18.942 1.00 41.94 O
2394	ATOM 1455 CB SER B 49 14.717 12.244 22.089 1.00 37.98 C
2395	ATOM 1456 OG SER B 49 16.403 12.088 22.302 1.00 37.71 O
2396	ATOM 1457 N THR B 50 16.507 11.264 19.343 1.00 28.29 N
2397	ATOM 1458 CA THR B 50 17.236 11.360 18.289 1.00 30.77 C
2398	ATOM 1459 C THR B 50 17.885 10.175 17.455 1.00 28.12 C
2399	ATOM 1460 O THR B 50 17.899 9.107 18.221 1.00 25.38 O
2400	ATOM 1461 CB THR B 50 18.076 12.160 18.824 1.00 33.39 C
2401	ATOM 1462 OG1 THR B 50 19.415 11.795 19.160 1.00 37.96 O
2402	ATOM 1463 CG2 THR B 50 18.083 13.812 19.397 1.00 29.64 C
2403	ATOM 1464 N PRO B 51 18.477 10.443 16.283 1.00 28.96 N
2404	ATOM 1465 CA PRO B 51 18.840 9.268 15.580 1.00 22.25 C
2405	ATOM 1466 C PRO B 51 20.003 8.659 16.259 1.00 19.80 C
2406	ATOM 1467 O PRO B 51 20.229 7.322 16.651 1.00 21.55 O
2407	ATOM 1468 CB PRO B 51 19.279 9.752 14.257 1.00 27.29 C
2408	ATOM 1469 CG PRO B 51 18.236 10.849 14.019 1.00 23.54 C
2409	ATOM 1470 CD PRO B 51 18.120 11.592 15.204 1.00 26.04 C
2410	ATOM 1471 N ASP B 52 20.955 9.490 16.887 1.00 21.99 N
2411	ATOM 1472 CA ASP B 52 22.107 9.063 17.596 1.00 20.50 C
2412	ATOM 1473 C ASP B 52 21.711 8.282 18.816 1.00 16.32 C
2413	ATOM 1474 O ASP B 52 22.264 7.261 19.307 1.00 25.55 O
2414	ATOM 1475 CB ASP B 52 22.971 10.246 17.966 1.00 32.17 C
2415	ATOM 1476 CG ASP B 52 24.234 10.367 16.728 1.00 47.24 C
2416	ATOM 1477 OD1 ASP B 52 24.140 9.731 15.886 1.00 41.78 O
2417	ATOM 1478 OD2 ASP B 52 24.041 11.689 16.359 1.00 62.08 O
2418	ATOM 1479 N ALA B 53 20.654 8.843 19.515 1.00 23.18 N
2419	ATOM 1480 CA ALA B 53 20.143 8.181 20.776 1.00 24.60 C
2420	ATOM 1481 C ALA B 53 19.728 6.737 20.669 1.00 20.91 C
2421	ATOM 1482 O ALA B 53 19.736 5.693 21.187 1.00 20.19 O
2422	ATOM 1483 CB ALA B 53 19.176 8.937 21.371 1.00 23.45 C
2423	ATOM 1484 N VAL B 54 18.925 6.610 19.428 1.00 19.02 N
2424	ATOM 1485 CA VAL B 54 18.396 5.367 18.970 1.00 17.30 C
2425	ATOM 1486 C VAL B 54 19.363 4.542 18.660 1.00 15.03 C
2426	ATOM 1487 O VAL B 54 19.429 3.266 19.120 1.00 19.06 O
2427	ATOM 1488 CB VAL B 54 17.268 5.613 17.733 1.00 27.63 C
2428	ATOM 1489 CG1 VAL B 54 17.019 4.214 17.213 1.00 22.46 C
2429	ATOM 1490 CG2 VAL B 54 16.224 6.564 17.992 1.00 27.27 C
2430	ATOM 1491 N MET B 55 20.370 4.888 17.834 1.00 21.73 N
2431	ATOM 1492 CA MET B 55 21.262 3.920 17.351 1.00 17.86 C
2432	ATOM 1493 C MET B 55 22.215 3.437 18.454 1.00 32.16 C
2433	ATOM 1494 O MET B 55 22.701 2.355 18.174 1.00 26.15 O
2434	ATOM 1495 CB MET B 55 22.167 4.509 16.152 1.00 19.12 C
2435	ATOM 1496 CG MET B 55 21.367 4.924 14.914 1.00 18.10 C
2436	ATOM 1497 SD MET B 55 20.328 3.573 14.221 1.00 21.28 S
2437	ATOM 1498 CE MET B 55 21.373 2.471 13.659 1.00 20.66 C
2438	ATOM 1499 N GLY B 56 22.406 4.339 19.361 1.00 24.42 N
2439	ATOM 1500 CA GLY B 56 23.329 3.841 20.456 1.00 36.79 C
2440	ATOM 1501 C GLY B 56 22.514 3.565 21.746 1.00 33.28 C
2441	ATOM 1502 O GLY B 56 23.093 2.903 22.699 1.00 24.94 O
2442	ATOM 1503 N ASN B 57 21.348 2.997 21.778 1.00 22.01 N
2443	ATOM 1504 CA ASN B 57 20.559 2.685 22.827 1.00 15.71 C
2444	ATOM 1505 C ASN B 57 20.755 1.267 22.976 1.00 17.88 C
2445	ATOM 1506 O ASN B 57 20.502 0.300 22.098 1.00 18.04 O
2446	ATOM 1507 CB ASN B 57 19.144 2.920 22.701 1.00 21.80 C
2447	ATOM 1508 CG ASN B 57 18.247 2.358 23.776 1.00 18.78 C
2448	ATOM 1509 OD1 ASN B 57 18.261 1.376 24.212 1.00 23.41 O
2449	ATOM 1510 ND2 ASN B 57 17.583 3.338 24.270 1.00 26.53 N
2450	ATOM 1511 N PRO B 58 21.174 0.662 24.086 1.00 24.81 N
2451	ATOM 1512 CA PRO B 58 21.379 -0.699 24.384 1.00 24.38 C
2452	ATOM 1513 C PRO B 58 20.320 -1.707 24.238 1.00 16.45 C
2453	ATOM 1514 O PRO B 58 20.621 -2.865 23.942 1.00 22.03 O
2454	ATOM 1515 CB PRO B 58 22.199 -0.585 25.810 1.00 41.00 C
2455	ATOM 1516 CG PRO B 58 21.985 0.546 26.007 1.00 36.46 C
2456	ATOM 1517 CD PRO B 58 21.572 1.751 25.438 1.00 41.75 C
2457	ATOM 1518 N LYS B 59 19.129 -1.092 24.601 1.00 16.03 N
2458	ATOM 1519 CA LYS B 59 17.877 -2.002 24.599 1.00 22.04 C
2459	ATOM 1520 C LYS B 59 17.389 -2.185 23.113 1.00 13.98 C
2460	ATOM 1521 O LYS B 59 17.132 -3.370 22.712 1.00 15.67 O
2461	ATOM 1522 CB LYS B 59 16.893 -1.439 25.346 1.00 22.22 C
2462	ATOM 1523 CG LYS B 59 17.003 -1.840 26.817 1.00 45.70 C
2463	ATOM 1524 CD LYS B 59 17.133 -0.988 27.329 1.00 44.05 C
2464	ATOM 1525 CE LYS B 59 17.311 -2.126 29.392 1.00 71.22 C
2465	ATOM 1526 NZ LYS B 59 16.304 -0.516 29.672 1.00 61.54 N
2466	ATOM 1527 N VAL B 60 17.762 -1.228 22.435 1.00 17.28 N
2467	ATOM 1528 CA VAL B 60 17.489 -1.267 20.987 1.00 18.21 C
2468	ATOM 1529 C VAL B 60 18.198 -2.383 20.467 1.00 17.60 C
2469	ATOM 1530 O VAL B 60 18.065 -3.331 19.597 1.00 19.11 O
2470	ATOM 1531 CB VAL B 60 17.415 0.000 20.196 1.00 19.15 C
2471	ATOM 1532 CG1 VAL B 60 17.700 -0.242 18.743 1.00 20.44 C
2472	ATOM 1533 CG2 VAL B 60 16.452 0.957 20.699 1.00 20.64 C
2473	ATOM 1534 N LYS B 61 19.612 -2.162 20.575 1.00 16.19 N
2474	ATOM 1535 CA LYS B 61 20.529 -3.146 20.062 1.00 15.00 C
2475	ATOM 1536 C LYS B 61 20.399 -4.610 20.622 1.00 17.90 C
2476	ATOM 1537 O LYS B 61 20.213 -5.649 19.890 1.00 20.52 O
2477	ATOM 1538 CB LYS B 61 21.934 -2.794 20.686 1.00 23.50 C
2478	ATOM 1539 CG LYS B 61 22.389 -1.790 20.123 1.00 34.21 C
2479	ATOM 1540 CD LYS B 61 23.914 -1.121 21.095 1.00 48.05 C
2480	ATOM 1541 CE LYS B 61 24.659 -0.514 19.697 1.00 65.12 C
2481	ATOM 1542 NZ LYS B 61 25.928 0.153 20.694 1.00 66.26 N
2482	ATOM 1543 N ALA B 62 19.935 -4.789 21.817 1.00 18.99 N
2483	ATOM 1544 CA ALA B 62 19.613 -6.179 22.281 1.00 20.11 C
2484	ATOM 1545 C ALA B 62 18.327 -6.740 21.532 1.00 23.44 C
2485	ATOM 1546 O ALA B 62 18.260 -7.852 21.400 1.00 21.26 O
2486	ATOM 1547 CB ALA B 62 19.287 -6.023 23.792 1.00 28.90 C
2487	ATOM 1548 N HIS B 63 17.361 -5.800 21.608 1.00 20.40 N
2488	ATOM 1549 CA HIS B 63 16.190 -6.291 20.805 1.00 18.39 C
2489	ATOM 1550 C HIS B 63 16.516 -6.639 19.256 1.00 14.88 C
2490	ATOM 1551 O HIS B 63 16.111 -7.828 18.863 1.00 18.29 O
2491	ATOM 1552 CB HIS B 63 15.116 -5.410 20.859 1.00 22.46 C
2492	ATOM 1553 CG HIS B 63 13.751 -5.776 20.554 1.00 25.19 C
2493	ATOM 1554 ND1 HIS B 63 13.281 -7.248 21.117 1.00 24.68 N
2494	ATOM 1555 CD2 HIS B 63 13.005 -5.716 19.310 1.00 20.46 C
2495	ATOM 1556 CE1 HIS B 63 11.969 -7.447 20.274 1.00 21.48 C
2496	ATOM 1557 NE2 HIS B 63 11.891 -6.627 19.400 1.00 20.00 N
2497	ATOM 1558 N GLY B 64 17.369 -5.912 18.807 1.00 15.81 N
2498	ATOM 1559 CA GLY B 64 17.753 -6.266 17.372 1.00 16.57 C
2499	ATOM 1560 C GLY B 64 18.356 -7.523 17.041 1.00 14.05 C
2500	ATOM 1561 O GLY B 64 18.321 -8.353 16.306 1.00 17.38 O
2501	ATOM 1562 N LYS B 65 19.222 -7.845 18.080 1.00 15.77 N
2502	ATOM 1563 CA LYS B 65 19.749 -9.096 18.187 1.00 17.79 C
2503	ATOM 1564 C LYS B 65 18.945 -10.321 18.319 1.00 18.32 C
2504	ATOM 1565 O LYS B 65 19.205 -11.332 17.796 1.00 19.33 O
2505	ATOM 1566 CB LYS B 65 21.117 -9.195 19.352 1.00 34.65 C
2506	ATOM 1567 CG LYS B 65 20.823 -9.337 19.828 1.00 64.04 C
2507	ATOM 1568 CD LYS B 65 22.866 -9.404 21.254 1.00 58.77 C
2508	ATOM 1569 CE LYS B 65 21.591 -11.376 21.213 1.00 64.47 C
2509	ATOM 1570 NZ LYS B 65 22.762 -11.190 23.512 1.00 67.19 N
2510	ATOM 1571 N LYS B 66 17.979 -10.126 19.094 1.00 17.45 N
2511	ATOM 1572 CA LYS B 66 17.297 -11.071 19.293 1.00 20.10 C
2512	ATOM 1573 C LYS B 66 16.171 -11.403 18.033 1.00 21.06 C
2513	ATOM 1574 O LYS B 66 15.915 -12.596 17.725 1.00 17.84 O
2514	ATOM 1575 CB LYS B 66 16.183 -10.827 20.504 1.00 22.19 C
2515	ATOM 1576 CG LYS B 66 15.115 -11.668 20.860 1.00 40.97 C
2516	ATOM 1577 CD LYS B 66 14.348 -11.289 22.165 1.00 49.22 C
2517	ATOM 1578 CE LYS B 66 14.883 -13.426 23.031 1.00 72.58 C
2518	ATOM 1579 NZ LYS B 66 13.505 -13.329 24.195 1.00 70.66 N
2519	ATOM 1580 N VAL B 67 15.722 -10.213 17.591 1.00 16.93 N
2520	ATOM 1581 CA VAL B 67 14.967 -10.430 16.204 1.00 19.22 C
2521	ATOM 1582 C VAL B 67 15.793 -10.926 15.110 1.00 11.08 C
2522	ATOM 1583 O VAL B 67 15.419 -12.032 14.481 1.00 14.57 O
2523	ATOM 1584 CB VAL B 67 14.239 -9.056 15.913 1.00 21.56 C
2524	ATOM 1585 CG1 VAL B 67 13.929 -8.835 14.427 1.00 18.58 C
2525	ATOM 1586 CG2 VAL B 67 13.400 -8.550 17.010 1.00 21.34 C
2526	ATOM 1587 N LEU B 68 16.954 -10.461 14.916 1.00 11.62 N
2527	ATOM 1588 CA LEU B 68 17.765 -11.045 13.835 1.00 15.23 C
2528	ATOM 1589 C LEU B 68 18.198 -12.546 14.030 1.00 13.22 C
2529	ATOM 1590 O LEU B 68 18.576 -13.320 13.014 1.00 14.49 O
2530	ATOM 1591 CB LEU B 68 18.788 -10.157 13.424 1.00 22.80 C
2531	ATOM 1592 CG LEU B 68 18.947 -9.620 11.990 1.00 26.57 C
2532	ATOM 1593 CD1 LEU B 68 20.192 -10.323 11.868 1.00 62.38 C
2533	ATOM 1594 CD2 LEU B 68 17.922 -9.301 11.306 1.00 35.30 C
2534	ATOM 1595 N GLY B 69 18.512 -12.954 15.230 1.00 14.77 N
2535	ATOM 1596 CA GLY B 69 18.843 -14.169 15.499 1.00 20.29 C
2536	ATOM 1597 C GLY B 69 17.847 -15.440 15.178 1.00 17.59 C
2537	ATOM 1598 O GLY B 69 17.982 -16.324 14.534 1.00 19.02 O
2538	ATOM 1599 N ALA B 70 16.471 -14.870 15.541 1.00 19.76 N
2539	ATOM 1600 CA ALA B 70 15.432 -15.582 15.055 1.00 20.35 C
2540	ATOM 1601 C ALA B 70 15.296 -15.691 13.506 1.00 16.36 C
2541	ATOM 1602 O ALA B 70 14.996 -16.706 12.805 1.00 18.12 O
2542	ATOM 1603 CB ALA B 70 14.137 -15.174 15.556 1.00 18.92 C
2543	ATOM 1604 N PHE B 71 15.441 -14.520 12.868 1.00 14.47 N
2544	ATOM 1605 CA PHE B 71 15.473 -14.523 11.393 1.00 18.37 C
2545	ATOM 1606 C PHE B 71 16.681 -15.484 10.885 1.00 23.80 C
2546	ATOM 1607 O PHE B 71 16.324 -16.238 10.064 1.00 20.23 O
2547	ATOM 1608 CB PHE B 71 15.760 -13.050 11.104 1.00 13.73 C
2548	ATOM 1609 CG PHE B 71 15.796 -12.885 9.606 1.00 18.08 C
2549	ATOM 1610 CD1 PHE B 71 14.729 -12.558 8.930 1.00 25.10 C
2550	ATOM 1611 CD2 PHE B 71 17.072 -12.967 8.830 1.00 17.17 C
2551	ATOM 1612 CE1 PHE B 71 14.623 -12.282 7.460 1.00 19.10 C
2552	ATOM 1613 CE2 PHE B 71 16.901 -12.741 7.550 1.00 22.20 C
2553	ATOM 1614 CZ PHE B 71 15.701 -12.364 6.812 1.00 12.94 C
2554	ATOM 1615 N SER B 72 17.595 -15.502 11.393 1.00 20.10 N
2555	ATOM 1616 CA SER B 72 18.969 -16.288 11.125 1.00 20.52 C
2556	ATOM 1617 C SER B 72 18.446 -17.702 11.027 1.00 24.58 C
2557	ATOM 1618 O SER B 72 18.709 -18.593 10.064 1.00 22.06 O
2558	ATOM 1619 CB SER B 72 20.232 -15.732 11.864 1.00 15.28 C
2559	ATOM 1620 OG SER B 72 21.400 -16.267 11.544 1.00 25.10 O
2560	ATOM 1621 N ASP B 73 17.933 -17.999 12.102 1.00 27.59 N
2561	ATOM 1622 CA ASP B 73 17.456 -19.508 12.282 1.00 37.45 C
2562	ATOM 1623 C ASP B 73 16.631 -19.746 11.447 1.00 25.08 C
2563	ATOM 1624 O ASP B 73 16.306 -20.962 10.848 1.00 31.64 O
2564	ATOM 1625 CB ASP B 73 17.022 -19.613 13.914 1.00 36.32 C
2565	ATOM 1626 CG ASP B 73 18.407 -19.595 14.926 1.00 45.09 C
2566	ATOM 1627 OD1 ASP B 73 19.800 -19.407 14.506 1.00 37.33 O
2567	ATOM 1628 OD2 ASP B 73 18.096 -19.496 15.880 1.00 52.94 O
2568	ATOM 1629 N GLY B 74 15.535 -19.019 10.954 1.00 21.04 N
2569	ATOM 1630 CA GLY B 74 14.735 -19.149 9.973 1.00 15.14 C
2570	ATOM 1631 C GLY B 74 14.988 -19.490 8.722 1.00 22.81 C
2571	ATOM 1632 O GLY B 74 14.637 -20.071 7.621 1.00 25.94 O
2572	ATOM 1633 N LEU B 75 16.509 -18.919 8.215 1.00 20.94 N
2573	ATOM 1634 CA LEU B 75 17.037 -19.090 6.965 1.00 15.84 C
2574	ATOM 1635 C LEU B 75 17.465 -20.570 6.842 1.00 26.11 C
2575	ATOM 1636 O LEU B 75 17.646 -20.979 5.741 1.00 28.14 O
2576	ATOM 1637 CB LEU B 75 18.377 -18.389 6.691 1.00 21.09 C
2577	ATOM 1638 CG LEU B 75 18.160 -17.146 6.885 1.00 27.76 C
2578	ATOM 1639 CD1 LEU B 75 19.415 -16.065 6.621 1.00 33.03 C
2579	ATOM 1640 CD2 LEU B 75 17.192 -16.405 5.891 1.00 30.01 C
2580	ATOM 1641 N ALA B 76 17.528 -21.312 7.923 1.00 21.21 N
2581	ATOM 1642 CA ALA B 76 17.717 -22.609 7.710 1.00 22.79 C
2582	ATOM 1643 C ALA B 76 16.647 -23.681 7.464 1.00 40.88 C
2583	ATOM 1644 O ALA B 76 16.656 -24.527 7.123 1.00 38.44 O
2584	ATOM 1645 CB ALA B 76 18.164 -23.328 9.061 1.00 29.05 C
2585	ATOM 1646 N HIS B 77 15.219 -22.886 7.385 1.00 23.87 N
2586	ATOM 1647 CA HIS B 77 13.929 -23.700 7.284 1.00 21.57 C
2587	ATOM 1648 C HIS B 77 13.284 -22.870 6.150 1.00 18.37 C
2588	ATOM 1649 O HIS B 77 12.059 -22.798 6.220 1.00 23.13 O
2589	ATOM 1650 CB HIS B 77 13.250 -23.395 8.460 1.00 29.02 C
2590	ATOM 1651 CG HIS B 77 14.079 -24.146 9.683 1.00 36.16 C
2591	ATOM 1652 ND1 HIS B 77 14.936 -23.842 10.757 1.00 45.10 N
2592	ATOM 1653 CD2 HIS B 77 14.095 -25.953 9.360 1.00 41.12 C
2593	ATOM 1654 CE1 HIS B 77 15.178 -24.891 11.130 1.00 37.52 C
2594	ATOM 1655 NE2 HIS B 77 14.852 -25.983 10.561 1.00 42.04 N
2595	ATOM 1656 N LEU B 78 13.874 -22.553 5.099 1.00 22.31 N
2596	ATOM 1657 CA LEU B 78 13.302 -21.614 4.148 1.00 20.28 C
2597	ATOM 1658 C LEU B 78 12.283 -22.522 3.216 1.00 31.20 C
2598	ATOM 1659 O LEU B 78 11.288 -21.899 3.087 1.00 34.80 O
2599	ATOM 1660 CB LEU B 78 14.257 -21.383 2.881 1.00 19.92 C
2600	ATOM 1661 CG LEU B 78 14.986 -19.978 3.420 1.00 39.49 C
2601	ATOM 1662 CD1 LEU B 78 16.407 -19.926 2.680 1.00 34.16 C
2602	ATOM 1663 CD2 LEU B 78 14.406 -18.731 3.892 1.00 31.09 C
2603	ATOM 1664 N ASP B 79 12.097 -23.916 3.393 1.00 31.59 N
2604	ATOM 1665 CA ASP B 79 11.104 -24.882 2.602 1.00 37.85 C
2605	ATOM 1666 C ASP B 79 9.843 -24.653 3.569 1.00 38.72 C
2606	ATOM 1667 O ASP B 79 9.096 -25.342 3.631 1.00 37.62 O
2607	ATOM 1668 CB ASP B 79 11.737 -26.234 3.104 1.00 48.10 C
2608	ATOM 1669 CG ASP B 79 12.662 -26.319 2.384 1.00 61.60 C
2609	ATOM 1670 OD1 ASP B 79 13.286 -27.317 2.464 1.00 57.05 O
2610	ATOM 1671 OD2 ASP B 79 12.655 -25.818 0.790 1.00 50.26 O
2611	ATOM 1672 N ASN B 80 10.028 -24.212 4.945 1.00 35.73 N
2612	ATOM 1673 CA ASN B 80 8.836 -24.555 6.146 1.00 42.30 C
2613	ATOM 1674 C ASN B 80 9.062 -22.961 6.944 1.00 30.43 C
2614	ATOM 1675 O ASN B 80 8.998 -23.185 7.997 1.00 27.17 O
2615	ATOM 1676 CB ASN B 80 9.098 -25.723 6.800 1.00 45.64 C
2616	ATOM 1677 CG ASN B 80 7.793 -26.259 7.837 1.00 49.79 C
2617	ATOM 1678 OD1 ASN B 80 6.751 -25.228 7.493 1.00 49.18 O
2618	ATOM 1679 ND2 ASN B 80 8.556 -26.466 8.946 1.00 48.18 N
2619	ATOM 1680 N LEU B 81 8.851 -21.845 6.271 1.00 31.23 N
2620	ATOM 1681 CA LEU B 81 8.683 -20.637 7.429 1.00 24.59 C
2621	ATOM 1682 C LEU B 81 7.679 -20.724 8.281 1.00 25.32 C
2622	ATOM 1683 O LEU B 81 7.523 -20.208 9.309 1.00 23.54 O
2623	ATOM 1684 CB LEU B 81 8.987 -19.631 6.449 1.00 29.09 C
2624	ATOM 1685 CG LEU B 81 10.160 -19.226 5.665 1.00 21.46 C
2625	ATOM 1686 CD1 LEU B 81 10.084 -18.185 4.643 1.00 28.62 C
2626	ATOM 1687 CD2 LEU B 81 11.341 -18.875 6.546 1.00 30.82 C
2627	ATOM 1688 N LYS B 82 6.283 -21.136 7.490 1.00 26.15 N
2628	ATOM 1689 CA LYS B 82 5.156 -20.862 8.452 1.00 24.25 C
2629	ATOM 1690 C LYS B 82 5.202 -21.643 9.461 1.00 23.08 C
2630	ATOM 1691 O LYS B 82 4.869 -21.389 10.597 1.00 24.88 O
2631	ATOM 1692 CB LYS B 82 4.142 -21.433 7.392 1.00 40.41 C
2632	ATOM 1693 CG LYS B 82 3.479 -20.229 6.738 1.00 39.73 C
2633	ATOM 1694 CD LYS B 82 2.160 -20.747 5.755 1.00 66.91 C
2634	ATOM 1695 CE LYS B 82 1.685 -20.767 6.266 1.00 59.33 C
2635	ATOM 1696 NZ LYS B 82 -0.023 -22.087 5.346 1.00 80.12 N
2636	ATOM 1697 N GLY B 83 5.725 -22.942 9.358 1.00 26.18 N
2637	ATOM 1698 CA GLY B 83 5.798 -23.724 10.746 1.00 41.64 C
2638	ATOM 1699 C GLY B 83 6.819 -23.249 11.591 1.00 31.59 C
2639	ATOM 1700 O GLY B 83 6.621 -23.464 12.858 1.00 36.40 O
2640	ATOM 1701 N THR B 84 7.985 -22.864 11.019 1.00 26.72 N
2641	ATOM 1702 CA THR B 84 9.150 -22.242 11.744 1.00 25.47 C
2642	ATOM 1703 C THR B 84 8.609 -21.278 12.796 1.00 33.72 C
2643	ATOM 1704 O THR B 84 8.964 -20.907 13.790 1.00 27.43 O
2644	ATOM 1705 CB THR B 84 10.394 -21.742 11.042 1.00 25.58 C
2645	ATOM 1706 OG1 THR B 84 10.806 -23.108 10.337 1.00 39.04 O
2646	ATOM 1707 CG2 THR B 84 11.362 -21.482 11.789 1.00 30.76 C
2647	ATOM 1708 N PHE B 85 7.740 -20.301 12.125 1.00 23.61 N
2648	ATOM 1709 CA PHE B 85 7.236 -18.963 12.749 1.00 21.59 C
2649	ATOM 1710 C PHE B 85 5.980 -19.056 13.414 1.00 28.51 C
2650	ATOM 1711 O PHE B 85 5.496 -18.006 13.809 1.00 18.85 O
2651	ATOM 1712 CB PHE B 85 7.575 -17.733 11.855 1.00 18.34 C
2652	ATOM 1713 CG PHE B 85 8.914 -17.486 11.587 1.00 13.87 C
2653	ATOM 1714 CD1 PHE B 85 9.583 -17.701 10.358 1.00 16.61 C
2654	ATOM 1715 CD2 PHE B 85 9.616 -17.039 12.693 1.00 18.32 C
2655	ATOM 1716 CE1 PHE B 85 11.009 -17.444 10.305 1.00 27.99 C
2656	ATOM 1717 CE2 PHE B 85 11.013 -16.752 12.253 1.00 21.68 C
2657	ATOM 1718 CZ PHE B 85 11.837 -16.973 11.161 1.00 21.59 C
2658	ATOM 1719 N ALA B 86 5.328 -20.141 13.373 1.00 22.16 N
2659	ATOM 1720 CA ALA B 86 3.899 -20.242 13.948 1.00 23.14 C
2660	ATOM 1721 C ALA B 86 3.715 -19.788 15.246 1.00 20.99 C
2661	ATOM 1722 O ALA B 86 2.881 -18.975 15.595 1.00 20.07 O
2662	ATOM 1723 CB ALA B 86 3.272 -21.660 13.783 1.00 23.69 C
2663	ATOM 1724 N THR B 87 4.501 -20.280 16.157 1.00 14.82 N
2664	ATOM 1725 CA THR B 87 4.271 -19.764 17.443 1.00 18.61 C
2665	ATOM 1726 C THR B 87 4.737 -18.271 17.729 1.00 25.42 C
2666	ATOM 1727 O THR B 87 4.013 -17.569 18.383 1.00 23.63 O
2667	ATOM 1728 CB THR B 87 5.631 -20.439 18.664 1.00 36.27 C
2668	ATOM 1729 OG1 THR B 87 5.010 -21.597 18.659 1.00 56.82 O
2669	ATOM 1730 CG2 THR B 87 4.455 -20.311 20.305 1.00 60.80 C
2670	ATOM 1731 N LEU B 88 5.836 -17.770 16.978 1.00 19.44 N
2671	ATOM 1732 CA LEU B 88 5.984 -16.362 17.087 1.00 17.97 C
2672	ATOM 1733 C LEU B 88 4.882 -15.510 16.526 1.00 11.34 C
2673	ATOM 1734 O LEU B 88 4.682 -14.416 16.964 1.00 17.71 O
2674	ATOM 1735 CB LEU B 88 7.361 -16.058 16.476 1.00 20.20 C
2675	ATOM 1736 CG LEU B 88 8.654 -16.553 17.229 1.00 27.17 C
2676	ATOM 1737 CD1 LEU B 88 9.614 -15.962 16.454 1.00 32.32 C
2677	ATOM 1738 CD2 LEU B 88 8.631 -15.491 18.343 1.00 27.72 C
2678	ATOM 1739 N SER B 89 4.254 -16.087 15.451 1.00 12.58 N
2679	ATOM 1740 CA SER B 89 3.084 -15.313 14.877 1.00 15.21 C
2680	ATOM 1741 C SER B 89 1.999 -14.995 15.898 1.00 14.13 C
2681	ATOM 1742 O SER B 89 1.472 -13.894 16.189 1.00 14.29 O
2682	ATOM 1743 CB SER B 89 2.771 -16.248 13.670 1.00 18.34 C
2683	ATOM 1744 OG SER B 89 1.531 -15.441 13.107 1.00 17.85 O
2684	ATOM 1745 N GLU B 90 1.628 -16.201 16.484 1.00 14.25 N
2685	ATOM 1746 CA GLU B 90 0.931 -16.070 17.617 1.00 20.50 C
2686	ATOM 1747 C GLU B 90 0.876 -15.142 18.820 1.00 13.47 C
2687	ATOM 1748 O GLU B 90 0.179 -14.243 19.122 1.00 16.05 O
2688	ATOM 1749 CB GLU B 90 0.387 -17.706 18.270 1.00 21.76 C
2689	ATOM 1750 CG GLU B 90 0.049 -18.266 17.145 1.00 48.13 C
2690	ATOM 1751 CD GLU B 90 -0.726 -20.095 17.710 1.00 78.64 C
2691	ATOM 1752 OE1 GLU B 90 -1.132 -19.837 18.495 1.00 55.55 O
2692	ATOM 1753 OE2 GLU B 90 0.235 -20.950 17.492 1.00 74.37 O
2693	ATOM 1754 N LEU B 91 2.312 -15.215 19.185 1.00 13.36 N
2694	ATOM 1755 CA LEU B 91 2.718 -14.253 20.128 1.00 14.20 C
2695	ATOM 1756 C LEU B 91 2.527 -12.831 19.767 1.00 8.80 C
2696	ATOM 1757 O LEU B 91 2.160 -11.906 20.481 1.00 10.74 O
2697	ATOM 1758 CB LEU B 91 4.110 -14.807 20.432 1.00 12.00 C
2698	ATOM 1759 CG LEU B 91 4.669 -13.801 21.348 1.00 18.50 C
2699	ATOM 1760 CD1 LEU B 91 4.127 -14.212 22.834 1.00 20.79 C
2700	ATOM 1761 CD2 LEU B 91 5.943 -13.652 21.455 1.00 37.40 C
2701	ATOM 1762 N HIS B 92 3.059 -12.662 18.493 1.00 10.78 N
2702	ATOM 1763 CA HIS B 92 3.032 -11.268 18.253 1.00 11.85 C
2703	ATOM 1764 C HIS B 92 1.536 -10.600 17.895 1.00 11.06 C
2704	ATOM 1765 O HIS B 92 1.291 -9.431 18.158 1.00 13.45 O
2705	ATOM 1766 CB HIS B 92 3.754 -11.078 16.807 1.00 9.95 C
2706	ATOM 1767 CG HIS B 92 5.289 -10.900 17.051 1.00 15.50 C
2707	ATOM 1768 ND1 HIS B 92 6.099 -12.172 17.134 1.00 15.27 N
2708	ATOM 1769 CD2 HIS B 92 6.215 -9.905 16.994 1.00 23.76 C
2709	ATOM 1770 CE1 HIS B 92 7.432 -11.572 17.375 1.00 16.99 C
2710	ATOM 1771 NE2 HIS B 92 7.367 -10.337 17.129 1.00 14.76 N
2711	ATOM 1772 N CYS B 93 0.636 -11.512 17.534 1.00 14.83 N
2712	ATOM 1773 CA CYS B 93 -0.706 -11.057 17.499 1.00 12.23 C
2713	ATOM 1774 C CYS B 93 -1.360 -10.953 18.986 1.00 10.49 C
2714	ATOM 1775 O CYS B 93 -1.843 -9.987 19.222 1.00 18.01 O
2715	ATOM 1776 CB CYS B 93 -1.330 -12.054 16.605 1.00 15.43 C
2716	ATOM 1777 SG CYS B 93 -3.259 -11.741 16.494 1.00 18.37 S
2717	ATOM 1778 N ASP B 94 -1.338 -12.094 19.598 1.00 13.11 N
2718	ATOM 1779 CA ASP B 94 -2.308 -12.076 20.721 1.00 15.32 C
2719	ATOM 1780 C ASP B 94 -1.586 -11.449 21.803 1.00 25.71 C
2720	ATOM 1781 O ASP B 94 -2.319 -10.827 22.800 1.00 21.65 O
2721	ATOM 1782 CB ASP B 94 -2.522 -13.477 21.183 1.00 21.65 C
2722	ATOM 1783 CG ASP B 94 -3.443 -14.553 20.246 1.00 42.42 C
2723	ATOM 1784 OD1 ASP B 94 -3.967 -13.792 19.626 1.00 30.02 O
2724	ATOM 1785 OD2 ASP B 94 -3.094 -15.441 20.443 1.00 43.30 O
2725	ATOM 1786 N LYS B 95 -0.348 -11.361 22.144 1.00 18.55 N
2726	ATOM 1787 CA LYS B 95 0.080 -10.591 23.184 1.00 19.10 C
2727	ATOM 1788 C LYS B 95 0.803 -9.499 23.130 1.00 19.57 C
2728	ATOM 1789 O LYS B 95 0.736 -8.565 23.699 1.00 21.87 O
2729	ATOM 1790 CB LYS B 95 1.151 -11.737 23.890 1.00 25.95 C
2730	ATOM 1791 CG LYS B 95 0.477 -13.054 24.377 1.00 24.86 C
2731	ATOM 1792 CD LYS B 95 -0.659 -12.473 25.407 1.00 36.14 C
2732	ATOM 1793 CE LYS B 95 -1.063 -13.745 26.122 1.00 47.76 C
2733	ATOM 1794 NZ LYS B 95 -2.126 -13.501 26.952 1.00 55.91 N
2734	ATOM 1795 N LEU B 96 1.669 -9.358 21.897 1.00 12.40 N
2735	ATOM 1796 CA LEU B 96 2.264 -8.159 21.581 1.00 11.86 C
2736	ATOM 1797 C LEU B 96 1.626 -7.005 20.824 1.00 15.10 C
2737	ATOM 1798 O LEU B 96 2.002 -5.926 20.849 1.00 17.50 O
2738	ATOM 1799 CB LEU B 96 3.645 -8.491 21.134 1.00 14.08 C
2739	ATOM 1800 CG LEU B 96 4.528 -9.722 21.739 1.00 12.34 C
2740	ATOM 1801 CD1 LEU B 96 5.778 -9.939 20.848 1.00 13.78 C
2741	ATOM 1802 CD2 LEU B 96 4.863 -8.876 23.113 1.00 22.81 C
2742	ATOM 1803 N HIS B 97 0.616 -7.508 20.069 1.00 15.44 N
2743	ATOM 1804 CA HIS B 97 -0.223 -6.510 19.374 1.00 18.15 C
2744	ATOM 1805 C HIS B 97 0.581 -5.736 18.319 1.00 12.24 C
2745	ATOM 1806 O HIS B 97 0.337 -4.532 18.056 1.00 15.82 O
2746	ATOM 1807 CB HIS B 97 -1.053 -5.508 20.203 1.00 17.74 C
2747	ATOM 1808 CG HIS B 97 -1.716 -6.273 21.483 1.00 16.77 C
2748	ATOM 1809 ND1 HIS B 97 -2.602 -7.310 21.250 1.00 19.56 N
2749	ATOM 1810 CD2 HIS B 97 -1.189 -6.197 22.703 1.00 23.33 C
2750	ATOM 1811 CE1 HIS B 97 -2.759 -7.812 22.476 1.00 19.82 C
2751	ATOM 1812 NE2 HIS B 97 -2.056 -7.104 23.341 1.00 20.39 N
2752	ATOM 1813 N VAL B 98 1.359 -6.524 17.506 1.00 13.81 N
2753	ATOM 1814 CA VAL B 98 2.284 -5.763 16.567 1.00 9.22 C
2754	ATOM 1815 C VAL B 98 1.443 -5.905 15.109 1.00 9.86 C
2755	ATOM 1816 O VAL B 98 1.420 -7.012 14.615 1.00 12.90 O
2756	ATOM 1817 CB VAL B 98 3.592 -6.460 16.393 1.00 9.87 C
2757	ATOM 1818 CG1 VAL B 98 4.438 -5.824 15.405 1.00 14.91 C
2758	ATOM 1819 CG2 VAL B 98 4.444 -6.258 17.798 1.00 11.36 C
2759	ATOM 1820 N ASP B 99 1.147 -4.763 14.513 1.00 11.46 N
2760	ATOM 1821 CA ASP B 99 0.360 -4.723 13.272 1.00 9.02 C
2761	ATOM 1822 C ASP B 99 1.555 -5.328 12.375 1.00 15.41 C
2762	ATOM 1823 O ASP B 99 2.744 -4.931 12.235 1.00 10.63 O
2763	ATOM 1824 CB ASP B 99 0.336 -3.327 12.907 1.00 9.79 C
2764	ATOM 1825 CG ASP B 99 -0.231 -3.002 11.431 1.00 10.69 C
2765	ATOM 1826 OD1 ASP B 99 -0.535 -1.748 11.309 1.00 15.04 O
2766	ATOM 1827 OD2 ASP B 99 -0.299 -4.052 10.734 1.00 11.07 O
2767	ATOM 1828 N PRO B 100 1.274 -6.350 11.556 1.00 10.46 N
2768	ATOM 1829 CA PRO B 100 2.264 -7.099 10.669 1.00 11.87 C
2769	ATOM 1830 C PRO B 100 2.744 -6.170 9.522 1.00 13.04 C
2770	ATOM 1831 O PRO B 100 3.883 -6.627 8.995 1.00 13.79 O
2771	ATOM 1832 CB PRO B 100 1.545 -8.233 10.081 1.00 17.03 C
2772	ATOM 1833 CG PRO B 100 0.234 -8.243 10.793 1.00 17.33 C
2773	ATOM 1834 CD PRO B 100 -0.030 -7.028 11.592 1.00 9.97 C
2774	ATOM 1835 N GLU B 101 2.300 -4.973 9.393 1.00 9.66 N
2775	ATOM 1836 CA GLU B 101 2.927 -3.983 8.469 1.00 11.29 C
2776	ATOM 1837 C GLU B 101 4.322 -3.633 8.825 1.00 17.59 C
2777	ATOM 1838 O GLU B 101 5.293 -3.640 8.196 1.00 16.98 O
2778	ATOM 1839 CB GLU B 101 2.178 -2.819 8.156 1.00 18.71 C
2779	ATOM 1840 CG GLU B 101 2.755 -1.760 7.270 1.00 30.25 C
2780	ATOM 1841 CD GLU B 101 2.569 -2.612 5.445 1.00 26.27 C
2781	ATOM 1842 OE1 GLU B 101 1.725 -3.411 5.564 1.00 25.29 O
2782	ATOM 1843 OE2 GLU B 101 3.441 -1.765 5.293 1.00 34.30 O
2783	ATOM 1844 N ASN B 102 4.601 -3.752 10.314 1.00 12.60 N
2784	ATOM 1845 CA ASN B 102 5.969 -3.548 10.721 1.00 9.48 C
2785	ATOM 1846 C ASN B 102 6.861 -4.572 10.309 1.00 8.44 C
2786	ATOM 1847 O ASN B 102 8.118 -4.224 10.106 1.00 13.92 O
2787	ATOM 1848 CB ASN B 102 5.901 -3.665 12.265 1.00 18.27 C
2788	ATOM 1849 CG ASN B 102 5.284 -2.285 12.825 1.00 26.18 C
2789	ATOM 1850 OD1 ASN B 102 5.641 -1.422 12.815 1.00 20.87 O
2790	ATOM 1851 ND2 ASN B 102 4.003 -2.618 13.502 1.00 25.76 N
2791	ATOM 1852 N PHE B 103 6.584 -5.846 10.057 1.00 11.66 N
2792	ATOM 1853 CA PHE B 103 7.332 -6.920 9.605 1.00 11.79 C
2793	ATOM 1854 C PHE B 103 7.931 -6.435 8.177 1.00 19.35 C
2794	ATOM 1855 O PHE B 103 8.997 -6.751 7.762 1.00 16.06 O
2795	ATOM 1856 CB PHE B 103 6.816 -8.253 9.574 1.00 12.75 C
2796	ATOM 1857 CG PHE B 103 6.173 -8.727 10.951 1.00 17.48 C
2797	ATOM 1858 CD1 PHE B 103 6.884 -8.372 12.079 1.00 13.65 C
2798	ATOM 1859 CD2 PHE B 103 5.035 -9.335 10.925 1.00 13.36 C
2799	ATOM 1860 CE1 PHE B 103 6.240 -8.652 13.315 1.00 14.94 C
2800	ATOM 1861 CE2 PHE B 103 4.498 -9.665 12.273 1.00 14.24 C
2801	ATOM 1862 CZ PHE B 103 5.298 -9.364 13.368 1.00 19.61 C
2802	ATOM 1863 N ARG B 104 6.970 -5.873 7.380 1.00 13.60 N
2803	ATOM 1864 CA ARG B 104 7.430 -5.624 6.005 1.00 17.00 C
2804	ATOM 1865 C ARG B 104 8.326 -4.499 5.935 1.00 13.66 C
2805	ATOM 1866 O ARG B 104 9.337 -4.368 5.141 1.00 13.41 O
2806	ATOM 1867 CB ARG B 104 6.018 -5.177 5.223 1.00 18.62 C
2807	ATOM 1868 CG ARG B 104 5.137 -6.280 4.965 1.00 31.60 C
2808	ATOM 1869 CD ARG B 104 3.494 -6.093 4.370 1.00 44.99 C
2809	ATOM 1870 NE ARG B 104 2.810 -7.429 5.065 1.00 53.69 N
2810	ATOM 1871 CZ ARG B 104 1.600 -6.829 3.420 1.00 80.12 C
2811	ATOM 1872 NH1 ARG B 104 0.761 -5.157 3.344 1.00 72.76 N
2812	ATOM 1873 NH2 ARG B 104 1.186 -8.540 2.528 1.00 80.07 N
2813	ATOM 1874 N LEU B 105 8.064 -3.438 6.831 1.00 12.29 N
2814	ATOM 1875 CA LEU B 105 8.899 -2.275 6.982 1.00 11.07 C
2815	ATOM 1876 C LEU B 105 10.327 -2.808 7.482 1.00 13.91 C
2816	ATOM 1877 O LEU B 105 11.317 -2.347 6.887 1.00 14.94 O
2817	ATOM 1878 CB LEU B 105 8.443 -1.409 8.005 1.00 12.50 C
2818	ATOM 1879 CG LEU B 105 7.121 -0.514 7.549 1.00 17.21 C
2819	ATOM 1880 CD1 LEU B 105 6.747 0.236 8.813 1.00 19.52 C
2820	ATOM 1881 CD2 LEU B 105 7.420 0.384 6.353 1.00 25.82 C
2821	ATOM 1882 N LEU B 106 10.302 -3.738 8.415 1.00 16.16 N
2822	ATOM 1883 CA LEU B 106 11.679 -4.227 8.855 1.00 11.19 C
2823	ATOM 1884 C LEU B 106 12.325 -4.914 7.713 1.00 11.49 C
2824	ATOM 1885 O LEU B 106 13.544 -4.734 7.492 1.00 14.59 O
2825	ATOM 1886 CB LEU B 106 11.615 -5.043 10.074 1.00 9.57 C
2826	ATOM 1887 CG LEU B 106 12.904 -5.567 10.740 1.00 14.52 C
2827	ATOM 1888 CD1 LEU B 106 13.738 -4.483 11.015 1.00 20.21 C
2828	ATOM 1889 CD2 LEU B 106 12.609 -6.504 11.567 1.00 25.23 C
2829	ATOM 1890 N GLY B 107 11.728 -5.699 6.854 1.00 8.80 N
2830	ATOM 1891 CA GLY B 107 12.297 -6.476 5.851 1.00 11.35 C
2831	ATOM 1892 C GLY B 107 12.781 -5.426 4.844 1.00 11.83 C
2832	ATOM 1893 O GLY B 107 13.958 -5.700 4.332 1.00 14.42 O
2833	ATOM 1894 N ASN B 108 12.187 -4.243 4.553 1.00 11.55 N
2834	ATOM 1895 CA ASN B 108 12.802 -3.506 3.538 1.00 9.47 C
2835	ATOM 1896 C ASN B 108 14.026 -2.647 4.184 1.00 9.85 C
2836	ATOM 1897 O ASN B 108 14.983 -2.466 3.460 1.00 13.16 O
2837	ATOM 1898 CB ASN B 108 11.824 -2.458 3.182 1.00 16.47 C
2838	ATOM 1899 CG ASN B 108 10.727 -3.234 1.924 1.00 25.36 C
2839	ATOM 1900 OD1 ASN B 108 11.335 -4.320 1.398 1.00 28.00 O
2840	ATOM 1901 ND2 ASN B 108 10.036 -2.270 2.100 1.00 42.45 N
2841	ATOM 1902 N VAL B 109 14.008 -2.327 5.491 1.00 11.97 N
2842	ATOM 1903 CA VAL B 109 15.193 -1.717 6.001 1.00 8.99 C
2843	ATOM 1904 C VAL B 109 16.259 -2.676 6.124 1.00 12.55 C
2844	ATOM 1905 O VAL B 109 17.518 -2.304 5.902 1.00 13.71 O
2845	ATOM 1906 CB VAL B 109 14.853 -1.250 7.488 1.00 15.07 C
2846	ATOM 1907 CG1 VAL B 109 16.100 -0.810 8.069 1.00 19.91 C
2847	ATOM 1908 CG2 VAL B 109 13.852 0.066 7.393 1.00 15.78 C
2848	ATOM 1909 N LEU B 110 16.030 -4.023 6.388 1.00 9.97 N
2849	ATOM 1910 CA LEU B 110 17.059 -5.101 6.357 1.00 9.78 C
2850	ATOM 1911 C LEU B 110 17.764 -5.056 5.040 1.00 13.14 C
2851	ATOM 1912 O LEU B 110 18.980 -5.187 4.895 1.00 11.97 O
2852	ATOM 1913 CB LEU B 110 16.410 -6.369 6.847 1.00 11.11 C
2853	ATOM 1914 CG LEU B 110 17.490 -7.596 6.862 1.00 18.59 C
2854	ATOM 1915 CD1 LEU B 110 18.696 -7.290 7.723 1.00 24.07 C
2855	ATOM 1916 CD2 LEU B 110 17.031 -8.897 7.193 1.00 21.67 C
2856	ATOM 1917 N VAL B 111 17.015 -5.083 3.938 1.00 10.25 N
2857	ATOM 1918 CA VAL B 111 17.517 -5.121 2.535 1.00 8.08 C
2858	ATOM 1919 C VAL B 111 18.459 -3.959 2.465 1.00 10.10 C
2859	ATOM 1920 O VAL B 111 19.605 -3.960 1.822 1.00 14.18 O
2860	ATOM 1921 CB VAL B 111 16.320 -5.216 1.576 1.00 11.95 C
2861	ATOM 1922 CG1 VAL B 111 16.949 -4.942 0.196 1.00 16.64 C
2862	ATOM 1923 CG2 VAL B 111 15.888 -6.643 1.659 1.00 12.92 C
2863	ATOM 1924 N CYS B 112 18.155 -2.685 2.811 1.00 10.01 N
2864	ATOM 1925 CA CYS B 112 18.863 -1.400 2.699 1.00 9.19 C
2865	ATOM 1926 C CYS B 112 20.143 -1.657 3.581 1.00 14.92 C
2866	ATOM 1927 O CYS B 112 21.199 -1.284 3.015 1.00 13.93 O
2867	ATOM 1928 CB CYS B 112 18.369 -0.230 3.207 1.00 15.04 C
2868	ATOM 1929 SG CYS B 112 16.911 0.308 2.042 1.00 18.10 S
2869	ATOM 1930 N VAL B 113 19.969 -2.202 4.651 1.00 9.52 N
2870	ATOM 1931 CA VAL B 113 21.202 -2.512 5.398 1.00 11.92 C
2871	ATOM 1932 C VAL B 113 22.035 -3.532 4.865 1.00 15.57 C
2872	ATOM 1933 O VAL B 113 23.397 -3.138 4.862 1.00 13.38 O
2873	ATOM 1934 CB VAL B 113 20.888 -2.948 6.932 1.00 12.70 C
2874	ATOM 1935 CG1 VAL B 113 22.031 -3.383 7.663 1.00 17.23 C
2875	ATOM 1936 CG2 VAL B 113 20.282 -1.893 7.694 1.00 17.43 C
2876	ATOM 1937 N LEU B 114 21.768 -4.615 4.224 1.00 10.74 N
2877	ATOM 1938 CA LEU B 114 22.632 -5.454 3.485 1.00 10.20 C
2878	ATOM 1939 C LEU B 114 23.346 -4.641 2.455 1.00 10.87 C
2879	ATOM 1940 O LEU B 114 24.522 -5.071 2.156 1.00 12.76 O
2880	ATOM 1941 CB LEU B 114 21.856 -6.600 3.242 1.00 6.84 C
2881	ATOM 1942 CG LEU B 114 21.362 -7.530 4.328 1.00 10.74 C
2882	ATOM 1943 CD1 LEU B 114 20.435 -8.554 3.798 1.00 15.38 C
2883	ATOM 1944 CD2 LEU B 114 22.500 -8.141 5.077 1.00 21.35 C
2884	ATOM 1945 N ALA B 115 22.472 -3.897 1.677 1.00 9.28 N
2885	ATOM 1946 CA ALA B 115 23.134 -3.206 0.546 1.00 9.22 C
2886	ATOM 1947 C ALA B 115 24.284 -2.278 1.091 1.00 9.44 C
2887	ATOM 1948 O ALA B 115 25.320 -2.142 0.446 1.00 12.10 O
2888	ATOM 1949 CB ALA B 115 21.930 -2.539 -0.036 1.00 12.15 C
2889	ATOM 1950 N HIS B 116 23.975 -1.612 2.171 1.00 13.11 N
2890	ATOM 1951 CA HIS B 116 25.023 -0.593 2.641 1.00 12.81 C
2891	ATOM 1952 C HIS B 116 26.176 -1.395 3.061 1.00 18.85 C
2892	ATOM 1953 O HIS B 116 27.357 -0.986 2.878 1.00 16.05 O
2893	ATOM 1954 CB HIS B 116 24.442 0.070 3.767 1.00 17.43 C
2894	ATOM 1955 CG HIS B 116 25.164 1.158 4.279 1.00 27.80 C
2895	ATOM 1956 ND1 HIS B 116 25.567 1.157 5.736 1.00 27.30 N
2896	ATOM 1957 CD2 HIS B 116 25.793 2.195 3.793 1.00 25.62 C
2897	ATOM 1958 CE1 HIS B 116 26.226 2.480 5.818 1.00 29.22 C
2898	ATOM 1959 NE2 HIS B 116 26.570 2.986 4.660 1.00 26.05 N
2899	ATOM 1960 N HIS B 117 26.066 -2.490 3.850 1.00 11.35 N
2900	ATOM 1961 CA HIS B 117 27.064 -3.366 4.194 1.00 18.75 C
2901	ATOM 1962 C HIS B 117 27.881 -3.985 3.242 1.00 20.53 C
2902	ATOM 1963 O HIS B 117 29.104 -4.114 3.403 1.00 17.07 O
2903	ATOM 1964 CB HIS B 117 26.621 -4.637 5.175 1.00 19.57 C
2904	ATOM 1965 CG HIS B 117 27.096 -4.621 6.444 1.00 39.90 C
2905	ATOM 1966 ND1 HIS B 117 26.039 -3.036 6.824 1.00 47.73 N
2906	ATOM 1967 CD2 HIS B 117 28.146 -5.329 7.512 1.00 38.82 C
2907	ATOM 1968 CE1 HIS B 117 26.295 -2.928 8.550 1.00 27.38 C
2908	ATOM 1969 NE2 HIS B 117 26.763 -4.335 8.924 1.00 51.83 N
2909	ATOM 1970 N PHE B 118 27.367 -4.628 2.104 1.00 13.44 N
2910	ATOM 1971 CA PHE B 118 27.888 -5.419 1.096 1.00 13.47 C
2911	ATOM 1972 C PHE B 118 28.280 -4.574 -0.126 1.00 14.52 C
2912	ATOM 1973 O PHE B 118 29.082 -5.219 -0.874 1.00 15.85 O
2913	ATOM 1974 CB PHE B 118 27.174 -6.618 0.947 1.00 14.99 C
2914	ATOM 1975 CG PHE B 118 27.310 -7.470 1.980 1.00 22.65 C
2915	ATOM 1976 CD1 PHE B 118 26.224 -7.666 2.855 1.00 28.61 C
2916	ATOM 1977 CD2 PHE B 118 28.549 -8.159 2.601 1.00 34.26 C
2917	ATOM 1978 CE1 PHE B 118 26.242 -8.675 3.981 1.00 29.50 C
2918	ATOM 1979 CE2 PHE B 118 28.351 -9.080 3.277 1.00 36.60 C
2919	ATOM 1980 CZ PHE B 118 27.627 -9.130 4.417 1.00 30.15 C
2920	ATOM 1981 N GLY B 119 27.701 -3.412 -0.335 1.00 13.81 N
2921	ATOM 1982 CA GLY B 119 28.107 -2.567 -1.533 1.00 14.28 C
2922	ATOM 1983 C GLY B 119 27.814 -3.353 -2.686 1.00 17.07 C
2923	ATOM 1984 O GLY B 119 26.808 -4.212 -2.888 1.00 16.48 O
2924	ATOM 1985 N LYS B 120 28.740 -3.472 -3.465 1.00 19.17 N
2925	ATOM 1986 CA LYS B 120 28.535 -4.059 -4.848 1.00 27.00 C
2926	ATOM 1987 C LYS B 120 28.486 -5.640 -4.886 1.00 25.94 C
2927	ATOM 1988 O LYS B 120 27.868 -6.039 -5.935 1.00 20.66 O
2928	ATOM 1989 CB LYS B 120 29.863 -3.838 -5.852 1.00 31.85 C
2929	ATOM 1990 CG LYS B 120 30.960 -4.510 -5.562 1.00 36.58 C
2930	ATOM 1991 CD LYS B 120 32.161 -4.170 -6.625 1.00 49.76 C
2931	ATOM 1992 CE LYS B 120 33.201 -5.292 -5.966 1.00 55.47 C
2932	ATOM 1993 NZ LYS B 120 34.292 -5.686 -6.589 1.00 71.03 N
2933	ATOM 1994 N GLU B 121 28.720 -6.302 -3.902 1.00 20.26 N
2934	ATOM 1995 CA GLU B 121 28.393 -7.556 -3.778 1.00 15.17 C
2935	ATOM 1996 C GLU B 121 26.786 -7.871 -3.622 1.00 13.63 C
2936	ATOM 1997 O GLU B 121 26.362 -9.055 -3.923 1.00 17.16 O
2937	ATOM 1998 CB GLU B 121 29.233 -8.318 -2.533 1.00 29.40 C
2938	ATOM 1999 CG GLU B 121 29.541 -9.342 -2.700 1.00 50.25 C
2939	ATOM 2000 CD GLU B 121 30.241 -9.882 -0.830 1.00 42.74 C
2940	ATOM 2001 OE1 GLU B 121 29.786 -11.667 -1.141 1.00 47.83 O
2941	ATOM 2002 OE2 GLU B 121 31.217 -9.425 -1.168 1.00 34.52 O
2942	ATOM 2003 N PHE B 122 26.054 -6.831 -3.241 1.00 14.63 N
2943	ATOM 2004 CA PHE B 122 24.581 -7.077 -3.075 1.00 15.34 C
2944	ATOM 2005 C PHE B 122 24.015 -6.737 -4.532 1.00 13.61 C
2945	ATOM 2006 O PHE B 122 23.478 -5.701 -4.760 1.00 14.29 O
2946	ATOM 2007 CB PHE B 122 24.133 -6.005 -1.987 1.00 12.07 C
2947	ATOM 2008 CG PHE B 122 22.750 -6.466 -1.525 1.00 11.02 C
2948	ATOM 2009 CD1 PHE B 122 22.540 -7.652 -0.894 1.00 16.65 C
2949	ATOM 2010 CD2 PHE B 122 21.790 -5.593 -1.747 1.00 10.83 C
2950	ATOM 2011 CE1 PHE B 122 21.288 -8.069 -0.329 1.00 13.73 C
2951	ATOM 2012 CE2 PHE B 122 20.427 -5.937 -1.325 1.00 12.97 C
2952	ATOM 2013 CZ PHE B 122 20.322 -7.247 -0.672 1.00 16.05 C
2953	ATOM 2014 N THR B 123 24.216 -7.664 -5.332 1.00 18.07 N
2954	ATOM 2015 CA THR B 123 23.866 -7.444 -6.796 1.00 21.03 C
2955	ATOM 2016 C THR B 123 22.176 -7.347 -6.888 1.00 27.18 C
2956	ATOM 2017 O THR B 123 21.678 -7.911 -6.078 1.00 14.31 O
2957	ATOM 2018 CB THR B 123 24.352 -8.535 -7.622 1.00 19.82 C
2958	ATOM 2019 OG1 THR B 123 24.030 -9.746 -7.305 1.00 17.47 O
2959	ATOM 2020 CG2 THR B 123 25.945 -8.568 -7.681 1.00 22.67 C
2960	ATOM 2021 N PRO B 124 21.821 -7.033 -7.981 1.00 19.47 N
2961	ATOM 2022 CA PRO B 124 20.309 -7.060 -8.306 1.00 20.19 C
2962	ATOM 2023 C PRO B 124 19.874 -8.457 -8.199 1.00 20.69 C
2963	ATOM 2024 O PRO B 124 18.738 -8.543 -7.455 1.00 13.34 O
2964	ATOM 2025 CB PRO B 124 20.074 -6.480 -9.678 1.00 17.09 C
2965	ATOM 2026 CG PRO B 124 21.308 -5.510 -9.842 1.00 18.87 C
2966	ATOM 2027 CD PRO B 124 22.649 -6.190 -9.202 1.00 24.42 C
2967	ATOM 2028 N PRO B 125 20.354 -9.489 -8.576 1.00 16.20 N
2968	ATOM 2029 CA PRO B 125 19.952 -10.892 -8.433 1.00 16.84 C
2969	ATOM 2030 C PRO B 125 19.925 -11.341 -6.992 1.00 14.92 C
2970	ATOM 2031 O PRO B 125 18.950 -11.983 -6.530 1.00 16.05 O
2971	ATOM 2032 CB PRO B 125 20.675 -11.924 -9.198 1.00 19.48 C
2972	ATOM 2033 CG PRO B 125 21.240 -11.056 -10.143 1.00 21.56 C
2973	ATOM 2034 CD PRO B 125 21.611 -9.723 -9.654 1.00 25.73 C
2974	ATOM 2035 N VAL B 126 20.904 -10.923 -6.329 1.00 13.83 N
2975	ATOM 2036 CA VAL B 126 20.919 -11.183 -4.904 1.00 19.80 C
2976	ATOM 2037 C VAL B 126 20.061 -10.295 -4.143 1.00 14.89 C
2977	ATOM 2038 O VAL B 126 19.229 -10.946 -3.203 1.00 13.92 O
2978	ATOM 2039 CB VAL B 126 22.424 -10.769 -4.382 1.00 19.55 C
2979	ATOM 2040 CG1 VAL B 126 22.408 -11.156 -2.912 1.00 21.55 C
2980	ATOM 2041 CG2 VAL B 126 23.366 -11.841 -4.809 1.00 27.82 C
2981	ATOM 2042 N GLN B 127 19.711 -9.155 -4.321 1.00 13.64 N
2982	ATOM 2043 CA GLN B 127 18.607 -8.382 -3.880 1.00 9.72 C
2983	ATOM 2044 C GLN B 127 17.397 -9.130 -3.899 1.00 16.14 C
2984	ATOM 2045 O GLN B 127 16.431 -9.272 -3.189 1.00 12.24 O
2985	ATOM 2046 CB GLN B 127 18.574 -6.951 -4.292 1.00 13.15 C
2986	ATOM 2047 CG GLN B 127 17.258 -6.340 -3.818 1.00 13.42 C
2987	ATOM 2048 CD GLN B 127 17.180 -5.056 -4.465 1.00 16.28 C
2988	ATOM 2049 OE1 GLN B 127 17.979 -4.488 -5.247 1.00 16.20 O
2989	ATOM 2050 NE2 GLN B 127 16.107 -4.400 -4.118 1.00 19.47 N
2990	ATOM 2051 N ALA B 128 17.014 -9.478 -5.230 1.00 15.15 N
2991	ATOM 2052 CA ALA B 128 15.847 -10.225 -5.543 1.00 15.02 C
2992	ATOM 2053 C ALA B 128 15.496 -11.450 -4.737 1.00 11.97 C
2993	ATOM 2054 O ALA B 128 14.413 -11.642 -4.228 1.00 16.35 O
2994	ATOM 2055 CB ALA B 128 15.759 -10.403 -7.092 1.00 17.08 C
2995	ATOM 2056 N ALA B 129 16.462 -12.287 -4.461 1.00 13.66 N
2996	ATOM 2057 CA ALA B 129 16.408 -13.427 -3.647 1.00 13.76 C
2997	ATOM 2058 C ALA B 129 16.208 -12.966 -2.160 1.00 10.22 C
2998	ATOM 2059 O ALA B 129 15.192 -13.627 -1.584 1.00 10.46 O
2999	ATOM 2060 CB ALA B 129 17.632 -14.165 -3.702 1.00 13.23 C
3000	ATOM 2061 N TYR B 130 16.867 -11.953 -1.693 1.00 10.66 N
3001	ATOM 2062 CA TYR B 130 16.462 -11.629 -0.331 1.00 13.05 C
3002	ATOM 2063 C TYR B 130 15.102 -10.929 -0.163 1.00 11.70 C
3003	ATOM 2064 O TYR B 130 14.473 -11.012 0.813 1.00 11.83 O
3004	ATOM 2065 CB TYR B 130 17.543 -10.575 0.161 1.00 11.97 C
3005	ATOM 2066 CG TYR B 130 18.623 -11.287 0.924 1.00 13.90 C
3006	ATOM 2067 CD1 TYR B 130 18.650 -11.526 2.272 1.00 15.61 C
3007	ATOM 2068 CD2 TYR B 130 19.782 -11.574 0.237 1.00 14.18 C
3008	ATOM 2069 CE1 TYR B 130 19.630 -12.272 2.811 1.00 19.97 C
3009	ATOM 2070 CE2 TYR B 130 20.865 -12.543 0.889 1.00 19.65 C
3010	ATOM 2071 CZ TYR B 130 20.770 -12.571 2.260 1.00 22.28 C
3011	ATOM 2072 OH TYR B 130 21.731 -13.339 2.902 1.00 21.52 O
3012	ATOM 2073 N GLN B 131 14.606 -10.236 -1.202 1.00 12.03 N
3013	ATOM 2074 CA GLN B 131 13.282 -9.830 -1.214 1.00 12.03 C
3014	ATOM 2075 C GLN B 131 12.216 -10.851 -1.125 1.00 12.76 C
3015	ATOM 2076 O GLN B 131 11.369 -10.664 -0.189 1.00 15.09 O
3016	ATOM 2077 CB GLN B 131 12.944 -9.078 -2.464 1.00 14.85 C
3017	ATOM 2078 CG GLN B 131 13.735 -7.716 -2.449 1.00 19.57 C
3018	ATOM 2079 CD GLN B 131 13.251 -6.548 -1.638 1.00 22.82 C
3019	ATOM 2080 OE1 GLN B 131 13.981 -5.553 -1.833 1.00 18.44 O
3020	ATOM 2081 NE2 GLN B 131 12.251 -6.415 -0.990 1.00 16.43 N
3021	ATOM 2082 N LYS B 132 12.503 -11.991 -1.746 1.00 12.50 N
3022	ATOM 2083 CA LYS B 132 11.644 -13.098 -1.708 1.00 14.23 C
3023	ATOM 2084 C LYS B 132 11.592 -13.603 -0.224 1.00 17.46 C
3024	ATOM 2085 O LYS B 132 10.599 -13.851 0.497 1.00 14.87 O
3025	ATOM 2086 CB LYS B 132 11.937 -14.147 -2.452 1.00 19.74 C
3026	ATOM 2087 CG LYS B 132 11.561 -13.879 -3.966 1.00 26.28 C
3027	ATOM 2088 CD LYS B 132 11.989 -15.031 -4.739 1.00 31.58 C
3028	ATOM 2089 CE LYS B 132 11.660 -14.274 -6.180 1.00 32.98 C
3029	ATOM 2090 NZ LYS B 132 12.119 -15.998 -6.779 1.00 37.48 N
3030	ATOM 2091 N VAL B 133 12.856 -13.702 0.483 1.00 17.22 N
3031	ATOM 2092 CA VAL B 133 13.038 -14.205 1.805 1.00 11.45 C
3032	ATOM 2093 C VAL B 133 12.401 -13.319 2.840 1.00 11.90 C
3033	ATOM 2094 O VAL B 133 11.556 -13.799 3.731 1.00 13.71 O
3034	ATOM 2095 CB VAL B 133 14.459 -14.401 2.160 1.00 16.41 C
3035	ATOM 2096 CG1 VAL B 133 14.632 -14.683 3.511 1.00 36.18 C
3036	ATOM 2097 CG2 VAL B 133 15.014 -15.541 1.250 1.00 15.51 C
3037	ATOM 2098 N VAL B 134 12.512 -11.981 2.749 1.00 13.21 N
3038	ATOM 2099 CA VAL B 134 12.091 -11.081 3.574 1.00 12.26 C
3039	ATOM 2100 C VAL B 134 10.632 -11.128 3.483 1.00 16.19 C
3040	ATOM 2101 O VAL B 134 9.763 -10.888 4.517 1.00 17.40 O
3041	ATOM 2102 CB VAL B 134 12.356 -9.643 3.780 1.00 11.96 C
3042	ATOM 2103 CG1 VAL B 134 13.841 -9.777 4.082 1.00 18.38 C
3043	ATOM 2104 CG2 VAL B 134 12.314 -8.873 2.475 1.00 14.78 C
3044	ATOM 2105 N ALA B 135 9.938 -11.113 2.262 1.00 13.32 N
3045	ATOM 2106 CA ALA B 135 8.505 -11.237 2.119 1.00 21.37 C
3046	ATOM 2107 C ALA B 135 7.942 -12.494 2.777 1.00 17.09 C
3047	ATOM 2108 O ALA B 135 6.829 -12.512 3.348 1.00 17.43 O
3048	ATOM 2109 CB ALA B 135 8.135 -10.953 0.769 1.00 28.77 C
3049	ATOM 2110 N GLY B 136 8.572 -13.635 2.636 1.00 18.26 N
3050	ATOM 2111 CA GLY B 136 8.219 -15.058 3.189 1.00 19.82 C
3051	ATOM 2112 C GLY B 136 8.146 -14.912 4.633 1.00 16.67 C
3052	ATOM 2113 O GLY B 136 7.260 -15.405 5.231 1.00 15.34 O
3053	ATOM 2114 N VAL B 137 9.300 -14.354 5.275 1.00 19.06 N
3054	ATOM 2115 CA VAL B 137 9.275 -14.229 6.676 1.00 13.40 C
3055	ATOM 2116 C VAL B 137 8.222 -13.320 7.172 1.00 14.98 C
3056	ATOM 2117 O VAL B 137 7.448 -13.726 8.127 1.00 15.32 O
3057	ATOM 2118 CB VAL B 137 10.681 -13.683 7.141 1.00 12.05 C
3058	ATOM 2119 CG1 VAL B 137 10.587 -13.517 8.589 1.00 24.37 C
3059	ATOM 2120 CG2 VAL B 137 11.663 -14.723 6.701 1.00 11.44 C
3060	ATOM 2121 N ALA B 138 7.830 -12.223 6.567 1.00 14.63 N
3061	ATOM 2122 CA ALA B 138 6.739 -11.343 6.960 1.00 14.97 C
3062	ATOM 2123 C ALA B 138 5.477 -12.035 7.025 1.00 14.00 C
3063	ATOM 2124 O ALA B 138 4.520 -11.965 7.766 1.00 15.18 O
3064	ATOM 2125 CB ALA B 138 6.733 -10.129 6.135 1.00 21.60 C
3065	ATOM 2126 N ASN B 139 5.257 -12.632 5.801 1.00 14.76 N
3066	ATOM 2127 CA ASN B 139 3.965 -13.443 5.693 1.00 19.56 C
3067	ATOM 2128 C ASN B 139 3.788 -14.741 6.508 1.00 16.64 C
3068	ATOM 2129 O ASN B 139 2.773 -14.813 7.122 1.00 15.66 O
3069	ATOM 2130 CB ASN B 139 3.915 -14.281 4.273 1.00 32.30 C
3070	ATOM 2131 CG ASN B 139 3.642 -13.817 3.893 1.00 58.46 C
3071	ATOM 2132 OD1 ASN B 139 3.350 -12.337 3.410 1.00 49.38 O
3072	ATOM 2133 ND2 ASN B 139 4.138 -13.358 1.997 1.00 59.02 N
3073	ATOM 2134 N ALA B 140 4.975 -15.279 6.996 1.00 12.53 N
3074	ATOM 2135 CA ALA B 140 4.880 -16.341 7.880 1.00 19.39 C
3075	ATOM 2136 C ALA B 140 4.686 -15.725 9.225 1.00 15.37 C
3076	ATOM 2137 O ALA B 140 3.890 -16.337 10.107 1.00 15.92 O
3077	ATOM 2138 CB ALA B 140 6.298 -17.186 7.962 1.00 22.20 C
3078	ATOM 2139 N LEU B 141 5.135 -14.663 9.697 1.00 12.47 N
3079	ATOM 2140 CA LEU B 141 4.897 -13.957 10.913 1.00 15.63 C
3080	ATOM 2141 C LEU B 141 3.480 -13.697 11.034 1.00 21.66 C
3081	ATOM 2142 O LEU B 141 2.905 -13.294 12.092 1.00 17.40 O
3082	ATOM 2143 CB LEU B 141 5.926 -12.962 11.275 1.00 15.12 C
3083	ATOM 2144 CG LEU B 141 7.158 -13.407 11.868 1.00 17.02 C
3084	ATOM 2145 CD1 LEU B 141 8.083 -12.226 12.076 1.00 19.94 C
3085	ATOM 2146 CD2 LEU B 141 7.122 -13.935 13.238 1.00 21.74 C
3086	ATOM 2147 N ALA B 142 2.836 -13.244 9.876 1.00 12.86 N
3087	ATOM 2148 CA ALA B 142 1.608 -12.628 9.849 1.00 14.61 C
3088	ATOM 2149 C ALA B 142 0.405 -13.995 9.823 1.00 20.31 C
3089	ATOM 2150 O ALA B 142 -0.813 -13.424 10.022 1.00 18.06 O
3090	ATOM 2151 CB ALA B 142 1.282 -11.676 8.702 1.00 21.40 C
3091	ATOM 2152 N HIS B 143 0.842 -15.030 9.582 1.00 17.95 N
3092	ATOM 2153 CA HIS B 143 0.024 -16.256 9.074 1.00 26.37 C
3093	ATOM 2154 C HIS B 143 -1.200 -16.456 10.329 1.00 19.76 C
3094	ATOM 2155 O HIS B 143 -2.306 -16.886 9.956 1.00 21.59 O
3095	ATOM 2156 CB HIS B 143 0.773 -17.382 8.911 1.00 35.96 C
3096	ATOM 2157 CG HIS B 143 -0.236 -18.629 8.237 1.00 57.59 C
3097	ATOM 2158 ND1 HIS B 143 0.057 -19.594 9.608 1.00 48.44 N
3098	ATOM 2159 CD2 HIS B 143 -0.841 -18.281 7.293 1.00 54.87 C
3099	ATOM 2160 CE1 HIS B 143 -0.983 -20.316 8.077 1.00 74.03 C
3100	ATOM 2161 NE2 HIS B 143 -1.640 -19.381 7.013 1.00 57.99 N
3101	ATOM 2162 N LYS B 144 -0.804 -16.302 11.559 1.00 18.69 N
3102	ATOM 2163 CA LYS B 144 -1.735 -16.737 12.588 1.00 14.86 C
3103	ATOM 2164 C LYS B 144 -2.396 -15.617 12.962 1.00 16.55 C
3104	ATOM 2165 O LYS B 144 -3.129 -15.705 14.113 1.00 18.03 O
3105	ATOM 2166 CB LYS B 144 -0.819 -17.365 13.621 1.00 17.13 C
3106	ATOM 2167 CG LYS B 144 -0.392 -18.897 13.123 1.00 20.99 C
3107	ATOM 2168 CD LYS B 144 -1.238 -19.970 13.316 1.00 34.56 C
3108	ATOM 2169 CE LYS B 144 -2.035 -21.775 13.683 1.00 62.41 C
3109	ATOM 2170 NZ LYS B 144 -0.955 -22.424 15.226 1.00 62.40 N
3110	ATOM 2171 N TYR B 145 -2.408 -14.424 12.668 1.00 19.33 N
3111	ATOM 2172 CA TYR B 145 -3.111 -13.193 12.851 1.00 25.80 C
3112	ATOM 2173 C TYR B 145 -4.833 -13.485 12.942 1.00 37.10 C
3113	ATOM 2174 O TYR B 145 -4.989 -14.273 11.858 1.00 25.59 O
3114	ATOM 2175 CB TYR B 145 -2.815 -11.990 12.502 1.00 20.19 C
3115	ATOM 2176 CG TYR B 145 -1.513 -11.202 13.062 1.00 16.11 C
3116	ATOM 2177 CD1 TYR B 145 -1.713 -10.043 13.732 1.00 13.84 C
3117	ATOM 2178 CD2 TYR B 145 -0.444 -12.052 12.964 1.00 19.35 C
3118	ATOM 2179 CE1 TYR B 145 -0.716 -9.470 14.306 1.00 14.00 C
3119	ATOM 2180 CE2 TYR B 145 0.824 -11.431 13.760 1.00 16.15 C
3120	ATOM 2181 CZ TYR B 145 0.705 -10.123 14.396 1.00 11.23 C
3121	ATOM 2182 OH TYR B 145 1.824 -9.505 14.779 1.00 11.07 O
3122	ATOM 2183 N HIS B 146 -5.455 -13.156 13.610 1.00 22.40 N
3123	ATOM 2184 CA HIS B 146 -7.082 -13.260 13.817 1.00 24.36 C
3124	ATOM 2185 C HIS B 146 -7.642 -12.243 14.547 1.00 19.29 C
3125	ATOM 2186 O HIS B 146 -6.896 -11.423 15.229 1.00 20.20 O
3126	ATOM 2187 CB HIS B 146 -7.319 -14.676 14.251 1.00 17.91 C
3127	ATOM 2188 CG HIS B 146 -7.349 -14.408 16.278 1.00 30.29 C
3128	ATOM 2189 ND1 HIS B 146 -7.504 -15.329 16.577 1.00 56.02 N
3129	ATOM 2190 CD2 HIS B 146 -5.754 -14.700 16.400 1.00 32.02 C
3130	ATOM 2191 CE1 HIS B 146 -6.763 -15.571 18.243 1.00 45.40 C
3131	ATOM 2192 NE2 HIS B 146 -6.023 -14.569 17.782 1.00 35.25 N
3132	ATOM 2193 OXT HIS B 146 -8.867 -12.118 14.478 1.00 28.98 O
3133	TER 2194 HIS B 146
3134	ATOM 2195 N VAL C 1 -6.932 15.801 -4.736 1.00 53.78 N
3135	ATOM 2196 CA VAL C 1 -6.986 18.132 -4.726 1.00 39.83 C
3136	ATOM 2197 C VAL C 1 -8.725 18.013 -5.289 1.00 29.73 C
3137	ATOM 2198 O VAL C 1 -9.322 17.317 -6.202 1.00 31.20 O
3138	ATOM 2199 CB VAL C 1 -6.406 17.702 -5.747 1.00 52.94 C
3139	ATOM 2200 CG1 VAL C 1 -7.045 19.788 -6.149 1.00 47.73 C
3140	ATOM 2201 CG2 VAL C 1 -5.138 19.765 -5.197 1.00 67.01 C
3141	ATOM 2202 N LEU C 2 -9.481 18.489 -4.357 1.00 33.50 N
3142	ATOM 2203 CA LEU C 2 -10.829 18.318 -4.244 1.00 35.54 C
3143	ATOM 2204 C LEU C 2 -11.593 19.461 -5.392 1.00 25.83 C
3144	ATOM 2205 O LEU C 2 -11.224 20.587 -4.763 1.00 37.30 O
3145	ATOM 2206 CB LEU C 2 -11.320 18.570 -2.993 1.00 38.49 C
3146	ATOM 2207 CG LEU C 2 -11.368 17.191 -2.068 1.00 34.89 C
3147	ATOM 2208 CD1 LEU C 2 -11.559 17.406 -0.855 1.00 40.00 C
3148	ATOM 2209 CD2 LEU C 2 -11.556 16.072 -2.571 1.00 36.30 C
3149	ATOM 2210 N SER C 3 -12.051 19.126 -6.445 1.00 20.82 N
3150	ATOM 2211 CA SER C 3 -12.764 20.102 -7.265 1.00 16.99 C
3151	ATOM 2212 C SER C 3 -13.851 20.641 -6.492 1.00 19.86 C
3152	ATOM 2213 O SER C 3 -14.562 20.118 -5.605 1.00 23.30 O
3153	ATOM 2214 CB SER C 3 -12.915 19.412 -8.479 1.00 21.69 C
3154	ATOM 2215 OG SER C 3 -14.045 18.617 -8.438 1.00 24.96 O
3155	ATOM 2216 N PRO C 4 -14.614 21.747 -7.040 1.00 27.73 N
3156	ATOM 2217 CA PRO C 4 -15.686 22.248 -6.606 1.00 18.30 C
3157	ATOM 2218 C PRO C 4 -16.940 21.185 -6.683 1.00 21.79 C
3158	ATOM 2219 O PRO C 4 -17.669 21.118 -5.776 1.00 30.78 O
3159	ATOM 2220 CB PRO C 4 -16.024 23.555 -7.534 1.00 35.17 C
3160	ATOM 2221 CG PRO C 4 -14.548 23.940 -7.997 1.00 39.10 C
3161	ATOM 2222 CD PRO C 4 -13.753 22.599 -7.931 1.00 33.69 C
3162	ATOM 2223 N ALA C 5 -16.700 20.569 -7.707 1.00 20.53 N
3163	ATOM 2224 CA ALA C 5 -17.694 19.448 -7.877 1.00 15.17 C
3164	ATOM 2225 C ALA C 5 -17.668 18.427 -6.566 1.00 17.36 C
3165	ATOM 2226 O ALA C 5 -18.567 17.818 -6.161 1.00 18.86 O
3166	ATOM 2227 CB ALA C 5 -17.845 18.678 -9.144 1.00 14.70 C
3167	ATOM 2228 N ASP C 6 -16.408 17.997 -6.530 1.00 17.28 N
3168	ATOM 2229 CA ASP C 6 -16.090 17.056 -5.440 1.00 13.65 C
3169	ATOM 2230 C ASP C 6 -16.737 17.558 -4.126 1.00 16.19 C
3170	ATOM 2231 O ASP C 6 -17.234 16.746 -3.292 1.00 18.77 O
3171	ATOM 2232 CB ASP C 6 -14.589 16.808 -5.234 1.00 14.90 C
3172	ATOM 2233 CG ASP C 6 -14.039 15.955 -6.391 1.00 15.46 C
3173	ATOM 2234 OD1 ASP C 6 -14.772 14.926 -6.958 1.00 20.59 O
3174	ATOM 2235 OD2 ASP C 6 -12.866 16.168 -6.605 1.00 19.80 O
3175	ATOM 2236 N LYS C 7 -16.400 18.816 -3.902 1.00 17.95 N
3176	ATOM 2237 CA LYS C 7 -17.103 19.561 -2.483 1.00 25.53 C
3177	ATOM 2238 C LYS C 7 -18.248 19.426 -2.208 1.00 19.12 C
3178	ATOM 2239 O LYS C 7 -18.931 19.046 -1.371 1.00 19.71 O
3179	ATOM 2240 CB LYS C 7 -16.318 20.793 -2.391 1.00 27.50 C
3180	ATOM 2241 CG LYS C 7 -14.901 20.741 -2.614 1.00 53.71 C
3181	ATOM 2242 CD LYS C 7 -13.993 22.186 -1.677 1.00 60.72 C
3182	ATOM 2243 CE LYS C 7 -13.186 22.490 -2.528 1.00 63.74 C
3183	ATOM 2244 NZ LYS C 7 -12.305 23.225 -2.858 1.00 80.12 N
3184	ATOM 2245 N THR C 8 -18.940 19.776 -3.501 1.00 18.59 N
3185	ATOM 2246 CA THR C 8 -20.439 19.567 -3.523 1.00 17.68 C
3186	ATOM 2247 C THR C 8 -21.010 18.410 -3.219 1.00 15.92 C
3187	ATOM 2248 O THR C 8 -21.956 18.189 -2.497 1.00 18.11 O
3188	ATOM 2249 CB THR C 8 -21.005 20.281 -5.121 1.00 18.41 C
3189	ATOM 2250 OG1 THR C 8 -20.596 21.570 -4.936 1.00 22.00 O
3190	ATOM 2251 CG2 THR C 8 -22.332 20.382 -5.020 1.00 19.72 C
3191	ATOM 2252 N ASN C 9 -20.389 17.337 -3.881 1.00 14.52 N
3192	ATOM 2253 CA ASN C 9 -20.679 15.854 -3.720 1.00 11.76 C
3193	ATOM 2254 C ASN C 9 -20.524 15.368 -2.372 1.00 13.43 C
3194	ATOM 2255 O ASN C 9 -21.452 14.760 -1.788 1.00 14.77 O
3195	ATOM 2256 CB ASN C 9 -19.952 14.978 -4.802 1.00 15.52 C
3196	ATOM 2257 CG ASN C 9 -20.502 14.902 -6.224 1.00 21.23 C
3197	ATOM 2258 OD1 ASN C 9 -21.551 15.460 -6.366 1.00 17.78 O
3198	ATOM 2259 ND2 ASN C 9 -19.655 14.764 -7.036 1.00 16.93 N
3199	ATOM 2260 N VAL C 10 -19.456 15.819 -1.845 1.00 15.37 N
3200	ATOM 2261 CA VAL C 10 -19.214 15.430 -0.511 1.00 15.09 C
3201	ATOM 2262 C VAL C 10 -20.248 16.151 0.791 1.00 19.82 C
3202	ATOM 2263 O VAL C 10 -20.653 15.344 1.499 1.00 21.55 O
3203	ATOM 2264 CB VAL C 10 -17.776 15.740 -0.056 1.00 23.83 C
3204	ATOM 2265 CG1 VAL C 10 -17.369 15.319 1.491 1.00 26.38 C
3205	ATOM 2266 CG2 VAL C 10 -16.835 14.843 -0.837 1.00 22.96 C
3206	ATOM 2267 N LYS C 11 -20.423 17.395 0.515 1.00 19.06 N
3207	ATOM 2268 CA LYS C 11 -21.545 18.040 1.267 1.00 21.27 C
3208	ATOM 2269 C LYS C 11 -22.705 17.621 1.194 1.00 24.36 C
3209	ATOM 2270 O LYS C 11 -23.497 17.219 2.050 1.00 26.88 O
3210	ATOM 2271 CB LYS C 11 -21.200 19.455 1.180 1.00 24.11 C
3211	ATOM 2272 CG LYS C 11 -19.982 20.187 1.471 1.00 39.96 C
3212	ATOM 2273 CD LYS C 11 -20.184 21.708 1.326 1.00 36.60 C
3213	ATOM 2274 CE LYS C 11 -19.119 22.424 1.599 1.00 40.99 C
3214	ATOM 2275 NZ LYS C 11 -18.303 23.379 0.156 1.00 57.68 N
3215	ATOM 2276 N ALA C 12 -23.071 17.255 -0.098 1.00 26.89 N
3216	ATOM 2277 CA ALA C 12 -24.190 16.574 -0.166 1.00 22.80 C
3217	ATOM 2278 C ALA C 12 -24.709 15.466 0.479 1.00 22.96 C
3218	ATOM 2279 O ALA C 12 -25.641 14.894 1.303 1.00 25.17 O
3219	ATOM 2280 CB ALA C 12 -24.758 16.354 -1.436 1.00 30.68 C
3220	ATOM 2281 N ALA C 13 -23.698 14.326 0.213 1.00 19.81 N
3221	ATOM 2282 CA ALA C 13 -23.581 12.980 0.775 1.00 20.52 C
3222	ATOM 2283 C ALA C 13 -23.620 13.074 2.219 1.00 17.10 C
3223	ATOM 2284 O ALA C 13 -24.459 12.346 2.958 1.00 22.70 O
3224	ATOM 2285 CB ALA C 13 -22.559 12.176 0.137 1.00 20.00 C
3225	ATOM 2286 N TRP C 14 -22.646 13.784 2.878 1.00 18.93 N
3226	ATOM 2287 CA TRP C 14 -22.430 13.732 4.346 1.00 19.61 C
3227	ATOM 2288 C TRP C 14 -23.567 14.473 4.894 1.00 29.50 C
3228	ATOM 2289 O TRP C 14 -24.277 14.100 6.022 1.00 22.89 O
3229	ATOM 2290 CB TRP C 14 -21.334 14.670 4.695 1.00 20.94 C
3230	ATOM 2291 CG TRP C 14 -20.803 14.092 5.924 1.00 20.44 C
3231	ATOM 2292 CD1 TRP C 14 -21.097 15.028 7.151 1.00 25.06 C
3232	ATOM 2293 CD2 TRP C 14 -20.135 12.848 6.216 1.00 19.23 C
3233	ATOM 2294 NE1 TRP C 14 -20.337 14.117 8.027 1.00 26.03 N
3234	ATOM 2295 CE2 TRP C 14 -19.941 12.969 7.773 1.00 27.20 C
3235	ATOM 2296 CE3 TRP C 14 -19.861 11.878 5.555 1.00 24.26 C
3236	ATOM 2297 CZ2 TRP C 14 -19.510 11.822 8.284 1.00 29.42 C
3237	ATOM 2298 CZ3 TRP C 14 -19.277 10.605 6.015 1.00 27.47 C
3238	ATOM 2299 CH2 TRP C 14 -19.230 10.798 7.728 1.00 31.11 C
3239	ATOM 2300 N GLY C 15 -24.359 15.298 4.516 1.00 39.26 N
3240	ATOM 2301 CA GLY C 15 -25.631 16.086 4.525 1.00 27.60 C
3241	ATOM 2302 C GLY C 15 -26.650 15.043 4.748 1.00 35.88 C
3242	ATOM 2303 O GLY C 15 -27.292 14.929 6.180 1.00 44.35 O
3243	ATOM 2304 N LYS C 16 -26.927 14.192 4.125 1.00 34.61 N
3244	ATOM 2305 CA LYS C 16 -27.870 13.141 3.632 1.00 36.98 C
3245	ATOM 2306 C LYS C 16 -27.538 12.020 5.023 1.00 26.09 C
3246	ATOM 2307 O LYS C 16 -28.345 11.313 5.635 1.00 33.01 O
3247	ATOM 2308 CB LYS C 16 -28.251 12.406 2.440 1.00 27.30 C
3248	ATOM 2309 CG LYS C 16 -30.036 12.836 1.831 1.00 50.84 C
3249	ATOM 2310 CD LYS C 16 -30.158 11.081 2.262 1.00 68.28 C
3250	ATOM 2311 CE LYS C 16 -32.371 10.866 2.370 1.00 73.16 C
3251	ATOM 2312 NZ LYS C 16 -32.038 9.453 3.272 1.00 69.52 N
3252	ATOM 2313 N VAL C 17 -26.252 12.133 5.573 1.00 35.88 N
3253	ATOM 2314 CA VAL C 17 -25.770 11.297 6.645 1.00 27.62 C
3254	ATOM 2315 C VAL C 17 -26.612 11.695 7.685 1.00 30.67 C
3255	ATOM 2316 O VAL C 17 -27.281 11.042 8.701 1.00 29.27 O
3256	ATOM 2317 CB VAL C 17 -24.169 10.853 6.795 1.00 24.84 C
3257	ATOM 2318 CG1 VAL C 17 -23.946 10.589 8.064 1.00 24.66 C
3258	ATOM 2319 CG2 VAL C 17 -23.794 9.916 5.483 1.00 36.95 C
3259	ATOM 2320 N GLY C 18 -26.104 13.085 7.958 1.00 37.42 N
3260	ATOM 2321 CA GLY C 18 -26.962 13.614 9.161 1.00 36.79 C
3261	ATOM 2322 C GLY C 18 -26.609 13.344 10.447 1.00 35.54 C
3262	ATOM 2323 O GLY C 18 -25.379 12.833 10.941 1.00 34.05 O
3263	ATOM 2324 N ALA C 19 -27.875 13.044 10.943 1.00 30.07 N
3264	ATOM 2325 CA ALA C 19 -27.686 12.652 12.207 1.00 42.34 C
3265	ATOM 2326 C ALA C 19 -27.441 11.246 12.497 1.00 38.75 C
3266	ATOM 2327 O ALA C 19 -27.016 10.579 13.697 1.00 34.11 O
3267	ATOM 2328 CB ALA C 19 -28.889 12.929 12.875 1.00 49.98 C
3268	ATOM 2329 N HIS C 20 -27.337 10.243 11.555 1.00 27.23 N
3269	ATOM 2330 CA HIS C 20 -26.912 8.767 11.705 1.00 31.96 C
3270	ATOM 2331 C HIS C 20 -25.296 8.716 11.689 1.00 24.34 C
3271	ATOM 2332 O HIS C 20 -24.833 7.499 11.716 1.00 23.07 O
3272	ATOM 2333 CB HIS C 20 -27.281 8.149 10.528 1.00 47.99 C
3273	ATOM 2334 CG HIS C 20 -28.926 8.104 10.076 1.00 49.70 C
3274	ATOM 2335 ND1 HIS C 20 -29.432 7.280 11.405 1.00 46.00 N
3275	ATOM 2336 CD2 HIS C 20 -29.730 9.020 9.630 1.00 46.72 C
3276	ATOM 2337 CE1 HIS C 20 -31.098 7.852 11.111 1.00 49.28 C
3277	ATOM 2338 NE2 HIS C 20 -30.830 8.671 9.800 1.00 51.94 N
3278	ATOM 2339 N ALA C 21 -24.619 9.813 11.399 1.00 28.71 N
3279	ATOM 2340 CA ALA C 21 -23.098 9.802 11.331 1.00 32.59 C
3280	ATOM 2341 C ALA C 21 -22.391 9.015 12.473 1.00 33.22 C
3281	ATOM 2342 O ALA C 21 -21.700 8.030 11.964 1.00 25.05 O
3282	ATOM 2343 CB ALA C 21 -22.805 11.312 11.238 1.00 28.99 C
3283	ATOM 2344 N GLY C 22 -22.670 8.973 13.605 1.00 30.50 N
3284	ATOM 2345 CA GLY C 22 -22.269 8.117 14.625 1.00 25.20 C
3285	ATOM 2346 C GLY C 22 -22.605 6.970 14.498 1.00 28.87 C
3286	ATOM 2347 O GLY C 22 -21.738 5.901 14.583 1.00 21.09 O
3287	ATOM 2348 N GLU C 23 -23.752 6.203 14.168 1.00 19.95 N
3288	ATOM 2349 CA GLU C 23 -24.151 4.976 13.969 1.00 21.38 C
3289	ATOM 2350 C GLU C 23 -23.181 4.329 12.723 1.00 15.02 C
3290	ATOM 2351 O GLU C 23 -22.815 3.097 12.742 1.00 16.54 O
3291	ATOM 2352 CB GLU C 23 -25.689 4.819 13.452 1.00 29.82 C
3292	ATOM 2353 CG GLU C 23 -26.106 3.452 13.736 1.00 36.93 C
3293	ATOM 2354 CD GLU C 23 -28.202 3.924 13.602 1.00 80.12 C
3294	ATOM 2355 OE1 GLU C 23 -27.795 2.922 11.489 1.00 66.02 O
3295	ATOM 2356 OE2 GLU C 23 -27.964 4.694 13.267 1.00 59.79 O
3296	ATOM 2357 N TYR C 24 -23.207 5.173 11.697 1.00 21.28 N
3297	ATOM 2358 CA TYR C 24 -22.418 4.812 10.585 1.00 19.46 C
3298	ATOM 2359 C TYR C 24 -20.849 4.466 10.860 1.00 15.33 C
3299	ATOM 2360 O TYR C 24 -20.148 3.754 10.360 1.00 13.77 O
3300	ATOM 2361 CB TYR C 24 -22.651 5.606 9.406 1.00 16.14 C
3301	ATOM 2362 CG TYR C 24 -24.080 5.727 8.793 1.00 13.71 C
3302	ATOM 2363 CD1 TYR C 24 -24.170 6.732 7.640 1.00 24.76 C
3303	ATOM 2364 CD2 TYR C 24 -25.002 4.824 9.337 1.00 21.84 C
3304	ATOM 2365 CE1 TYR C 24 -25.645 6.832 7.377 1.00 25.66 C
3305	ATOM 2366 CE2 TYR C 24 -26.453 4.934 8.784 1.00 17.49 C
3306	ATOM 2367 CZ TYR C 24 -26.325 5.877 7.791 1.00 27.32 C
3307	ATOM 2368 OH TYR C 24 -27.810 6.069 7.401 1.00 31.23 O
3308	ATOM 2369 N GLY C 25 -20.290 5.421 11.638 1.00 18.29 N
3309	ATOM 2370 CA GLY C 25 -19.027 5.388 12.069 1.00 15.33 C
3310	ATOM 2371 C GLY C 25 -18.807 4.272 12.918 1.00 12.64 C
3311	ATOM 2372 O GLY C 25 -17.733 3.304 12.661 1.00 15.23 O
3312	ATOM 2373 N ALA C 26 -19.542 3.599 13.820 1.00 16.00 N
3313	ATOM 2374 CA ALA C 26 -19.471 2.386 14.471 1.00 11.42 C
3314	ATOM 2375 C ALA C 26 -19.307 1.193 13.564 1.00 10.94 C
3315	ATOM 2376 O ALA C 26 -18.739 0.230 13.578 1.00 13.65 O
3316	ATOM 2377 CB ALA C 26 -20.512 2.232 15.656 1.00 11.99 C
3317	ATOM 2378 N GLU C 27 -20.425 1.260 12.521 1.00 12.87 N
3318	ATOM 2379 CA GLU C 27 -20.638 0.028 11.636 1.00 15.51 C
3319	ATOM 2380 C GLU C 27 -19.412 0.022 10.785 1.00 12.84 C
3320	ATOM 2381 O GLU C 27 -18.849 -1.119 10.534 1.00 15.95 O
3321	ATOM 2382 CB GLU C 27 -21.715 0.427 10.623 1.00 15.50 C
3322	ATOM 2383 CG GLU C 27 -21.926 -0.710 9.772 1.00 17.08 C
3323	ATOM 2384 CD GLU C 27 -23.164 -0.586 8.872 1.00 30.48 C
3324	ATOM 2385 OE1 GLU C 27 -23.095 -0.770 7.588 1.00 18.71 O
3325	ATOM 2386 OE2 GLU C 27 -24.194 0.119 9.312 1.00 24.16 O
3326	ATOM 2387 N ALA C 28 -18.789 1.258 10.332 1.00 11.36 N
3327	ATOM 2388 CA ALA C 28 -17.460 1.158 9.500 1.00 9.58 C
3328	ATOM 2389 C ALA C 28 -16.340 0.418 10.332 1.00 9.29 C
3329	ATOM 2390 O ALA C 28 -15.677 -0.370 9.760 1.00 12.64 O
3330	ATOM 2391 CB ALA C 28 -17.171 2.523 9.159 1.00 13.35 C
3331	ATOM 2392 N LEU C 29 -16.325 0.834 11.666 1.00 12.01 N
3332	ATOM 2393 CA LEU C 29 -15.240 0.036 12.460 1.00 9.42 C
3333	ATOM 2394 C LEU C 29 -15.351 -1.296 12.531 1.00 8.04 C
3334	ATOM 2395 O LEU C 29 -14.557 -2.221 12.462 1.00 11.27 O
3335	ATOM 2396 CB LEU C 29 -15.253 0.792 13.944 1.00 13.39 C
3336	ATOM 2397 CG LEU C 29 -14.671 2.120 14.000 1.00 14.28 C
3337	ATOM 2398 CD1 LEU C 29 -15.060 2.641 15.229 1.00 21.17 C
3338	ATOM 2399 CD2 LEU C 29 -13.328 2.186 13.586 1.00 17.52 C
3339	ATOM 2400 N GLU C 30 -16.582 -1.891 12.768 1.00 12.13 N
3340	ATOM 2401 CA GLU C 30 -17.039 -3.158 12.830 1.00 15.15 C
3341	ATOM 2402 C GLU C 30 -16.575 -3.834 11.597 1.00 15.74 C
3342	ATOM 2403 O GLU C 30 -16.144 -4.973 11.643 1.00 15.15 O
3343	ATOM 2404 CB GLU C 30 -18.512 -3.390 13.241 1.00 16.95 C
3344	ATOM 2405 CG GLU C 30 -18.749 -4.796 13.397 1.00 22.01 C
3345	ATOM 2406 CD GLU C 30 -20.492 -5.310 14.125 1.00 33.25 C
3346	ATOM 2407 OE1 GLU C 30 -20.859 -4.170 14.215 1.00 33.78 O
3347	ATOM 2408 OE2 GLU C 30 -20.298 -6.063 14.309 1.00 40.59 O
3348	ATOM 2409 N ARG C 31 -17.016 -3.172 10.500 1.00 9.68 N
3349	ATOM 2410 CA ARG C 31 -16.706 -3.791 9.173 1.00 8.70 C
3350	ATOM 2411 C ARG C 31 -15.092 -4.029 9.070 1.00 13.62 C
3351	ATOM 2412 O ARG C 31 -14.706 -5.080 8.618 1.00 13.67 O
3352	ATOM 2413 CB ARG C 31 -17.211 -2.898 8.144 1.00 12.42 C
3353	ATOM 2414 CG ARG C 31 -18.743 -3.121 7.942 1.00 11.84 C
3354	ATOM 2415 CD ARG C 31 -19.136 -2.201 6.911 1.00 15.20 C
3355	ATOM 2416 NE ARG C 31 -20.701 -2.256 6.631 1.00 14.19 N
3356	ATOM 2417 CZ ARG C 31 -21.363 -3.224 5.977 1.00 11.42 C
3357	ATOM 2418 NH1 ARG C 31 -20.645 -4.259 5.462 1.00 11.92 N
3358	ATOM 2419 NH2 ARG C 31 -22.607 -3.167 6.110 1.00 15.15 N
3359	ATOM 2420 N MET C 32 -14.391 -2.999 9.390 1.00 10.57 N
3360	ATOM 2421 CA MET C 32 -12.880 -2.985 9.431 1.00 8.16 C
3361	ATOM 2422 C MET C 32 -12.304 -4.106 10.303 1.00 7.80 C
3362	ATOM 2423 O MET C 32 -11.482 -4.880 9.804 1.00 11.64 O
3363	ATOM 2424 CB MET C 32 -12.387 -1.587 9.793 1.00 8.09 C
3364	ATOM 2425 CG MET C 32 -10.949 -1.623 9.744 1.00 11.10 C
3365	ATOM 2426 SD MET C 32 -10.226 -0.081 10.328 1.00 18.02 S
3366	ATOM 2427 CE MET C 32 -10.638 -0.209 12.043 1.00 20.04 C
3367	ATOM 2428 N PHE C 33 -12.802 -4.206 11.603 1.00 13.50 N
3368	ATOM 2429 CA PHE C 33 -12.271 -5.320 12.432 1.00 12.85 C
3369	ATOM 2430 C PHE C 33 -12.547 -6.578 11.951 1.00 15.05 C
3370	ATOM 2431 O PHE C 33 -11.717 -7.551 12.143 1.00 13.38 O
3371	ATOM 2432 CB PHE C 33 -12.756 -5.046 13.817 1.00 12.45 C
3372	ATOM 2433 CG PHE C 33 -12.568 -3.710 14.467 1.00 10.81 C
3373	ATOM 2434 CD1 PHE C 33 -11.266 -3.320 14.428 1.00 14.60 C
3374	ATOM 2435 CD2 PHE C 33 -13.526 -3.151 15.305 1.00 15.15 C
3375	ATOM 2436 CE1 PHE C 33 -10.894 -2.155 15.062 1.00 15.80 C
3376	ATOM 2437 CE2 PHE C 33 -13.010 -1.947 15.768 1.00 13.43 C
3377	ATOM 2438 CZ PHE C 33 -11.786 -1.494 15.661 1.00 22.23 C
3378	ATOM 2439 N LEU C 34 -13.672 -6.909 11.292 1.00 11.85 N
3379	ATOM 2440 CA LEU C 34 -14.025 -8.262 10.744 1.00 12.31 C
3380	ATOM 2441 C LEU C 34 -13.308 -8.546 9.433 1.00 15.72 C
3381	ATOM 2442 O LEU C 34 -12.814 -9.634 9.197 1.00 19.67 O
3382	ATOM 2443 CB LEU C 34 -15.490 -8.519 10.506 1.00 16.89 C
3383	ATOM 2444 CG LEU C 34 -16.308 -8.523 11.809 1.00 26.21 C
3384	ATOM 2445 CD1 LEU C 34 -17.801 -8.703 11.585 1.00 26.59 C
3385	ATOM 2446 CD2 LEU C 34 -15.886 -9.544 12.837 1.00 38.34 C
3386	ATOM 2447 N SER C 35 -13.287 -7.520 8.527 1.00 12.82 N
3387	ATOM 2448 CA SER C 35 -12.594 -7.794 7.329 1.00 10.93 C
3388	ATOM 2449 C SER C 35 -11.162 -7.828 7.166 1.00 14.27 C
3389	ATOM 2450 O SER C 35 -10.505 -8.327 6.376 1.00 16.71 O
3390	ATOM 2451 CB SER C 35 -13.015 -6.732 6.237 1.00 13.98 C
3391	ATOM 2452 OG SER C 35 -14.406 -6.851 5.967 1.00 18.75 O
3392	ATOM 2453 N PHE C 36 -10.441 -6.974 8.104 1.00 11.09 N
3393	ATOM 2454 CA PHE C 36 -9.024 -6.696 8.153 1.00 10.70 C
3394	ATOM 2455 C PHE C 36 -8.606 -6.742 9.707 1.00 13.97 C
3395	ATOM 2456 O PHE C 36 -8.344 -5.778 10.402 1.00 16.32 O
3396	ATOM 2457 CB PHE C 36 -8.759 -5.327 7.682 1.00 12.71 C
3397	ATOM 2458 CG PHE C 36 -9.244 -5.034 6.227 1.00 14.13 C
3398	ATOM 2459 CD1 PHE C 36 -10.405 -4.227 6.071 1.00 14.98 C
3399	ATOM 2460 CD2 PHE C 36 -8.716 -5.826 5.029 1.00 21.47 C
3400	ATOM 2461 CE1 PHE C 36 -10.962 -3.950 4.805 1.00 23.41 C
3401	ATOM 2462 CE2 PHE C 36 -9.304 -5.498 3.966 1.00 24.62 C
3402	ATOM 2463 CZ PHE C 36 -10.428 -4.612 3.839 1.00 15.55 C
3403	ATOM 2464 N PRO C 37 -8.487 -8.050 9.947 1.00 18.65 N
3404	ATOM 2465 CA PRO C 37 -8.320 -8.334 11.359 1.00 17.35 C
3405	ATOM 2466 C PRO C 37 -6.962 -7.708 12.012 1.00 18.35 C
3406	ATOM 2467 O PRO C 37 -6.854 -7.465 13.248 1.00 14.04 O
3407	ATOM 2468 CB PRO C 37 -8.349 -9.870 11.562 1.00 27.87 C
3408	ATOM 2469 CG PRO C 37 -8.429 -10.372 10.373 1.00 37.42 C
3409	ATOM 2470 CD PRO C 37 -8.767 -9.192 9.450 1.00 22.48 C
3410	ATOM 2471 N THR C 38 -6.066 -7.410 11.173 1.00 12.63 N
3411	ATOM 2472 CA THR C 38 -4.834 -6.636 11.753 1.00 17.25 C
3412	ATOM 2473 C THR C 38 -5.049 -5.478 12.414 1.00 15.32 C
3413	ATOM 2474 O THR C 38 -4.264 -5.001 13.219 1.00 11.09 O
3414	ATOM 2475 CB THR C 38 -3.639 -7.011 10.452 1.00 12.40 C
3415	ATOM 2476 OG1 THR C 38 -4.178 -5.757 9.596 1.00 15.33 O
3416	ATOM 2477 CG2 THR C 38 -4.507 -7.126 9.385 1.00 80.12 C
3417	ATOM 2478 N THR C 39 -6.072 -4.797 11.866 1.00 10.35 N
3418	ATOM 2479 CA THR C 39 -6.458 -3.530 12.499 1.00 11.60 C
3419	ATOM 2480 C THR C 39 -6.867 -3.675 13.987 1.00 11.25 C
3420	ATOM 2481 O THR C 39 -6.719 -2.683 14.751 1.00 15.31 O
3421	ATOM 2482 CB THR C 39 -7.618 -2.839 11.782 1.00 10.41 C
3422	ATOM 2483 OG1 THR C 39 -8.902 -3.535 11.780 1.00 8.43 O
3423	ATOM 2484 CG2 THR C 39 -7.110 -2.694 10.278 1.00 7.27 C
3424	ATOM 2485 N LYS C 40 -7.142 -4.800 14.416 1.00 12.10 N
3425	ATOM 2486 CA LYS C 40 -7.571 -4.948 15.946 1.00 12.37 C
3426	ATOM 2487 C LYS C 40 -6.340 -4.815 16.822 1.00 12.69 C
3427	ATOM 2488 O LYS C 40 -6.554 -4.646 17.995 1.00 13.50 O
3428	ATOM 2489 CB LYS C 40 -8.135 -6.441 16.142 1.00 13.01 C
3429	ATOM 2490 CG LYS C 40 -9.508 -6.644 15.446 1.00 16.35 C
3430	ATOM 2491 CD LYS C 40 -9.585 -8.284 15.551 1.00 21.60 C
3431	ATOM 2492 CE LYS C 40 -10.395 -8.518 15.432 1.00 41.58 C
3432	ATOM 2493 NZ LYS C 40 -10.104 -10.161 15.709 1.00 24.62 N
3433	ATOM 2494 N THR C 41 -5.213 -4.883 16.231 1.00 15.39 N
3434	ATOM 2495 CA THR C 41 -3.858 -4.878 17.048 1.00 15.24 C
3435	ATOM 2496 C THR C 41 -3.895 -3.538 17.513 1.00 24.53 C
3436	ATOM 2497 O THR C 41 -3.052 -3.276 18.625 1.00 20.94 O
3437	ATOM 2498 CB THR C 41 -2.611 -5.058 16.204 1.00 10.27 C
3438	ATOM 2499 OG1 THR C 41 -2.473 -4.084 15.265 1.00 10.56 O
3439	ATOM 2500 CG2 THR C 41 -2.649 -6.370 15.637 1.00 13.16 C
3440	ATOM 2501 N TYR C 42 -4.559 -2.347 17.313 1.00 15.74 N
3441	ATOM 2502 CA TYR C 42 -4.420 -1.045 17.757 1.00 10.60 C
3442	ATOM 2503 C TYR C 42 -5.479 -0.829 18.921 1.00 12.75 C
3443	ATOM 2504 O TYR C 42 -5.553 0.201 19.530 1.00 15.68 O
3444	ATOM 2505 CB TYR C 42 -4.800 0.068 16.774 1.00 16.68 C
3445	ATOM 2506 CG TYR C 42 -3.607 -0.087 15.746 1.00 10.99 C
3446	ATOM 2507 CD1 TYR C 42 -2.328 0.661 16.011 1.00 17.16 C
3447	ATOM 2508 CD2 TYR C 42 -3.699 -0.743 14.478 1.00 12.51 C
3448	ATOM 2509 CE1 TYR C 42 -1.337 0.521 15.154 1.00 15.83 C
3449	ATOM 2510 CE2 TYR C 42 -2.696 -0.758 13.617 1.00 12.91 C
3450	ATOM 2511 CZ TYR C 42 -1.386 -0.114 13.943 1.00 12.97 C
3451	ATOM 2512 OH TYR C 42 -0.401 -0.078 12.976 1.00 13.25 O
3452	ATOM 2513 N PHE C 43 -6.271 -1.850 19.113 1.00 15.49 N
3453	ATOM 2514 CA PHE C 43 -7.459 -1.760 20.167 1.00 17.75 C
3454	ATOM 2515 C PHE C 43 -7.514 -3.016 21.053 1.00 20.04 C
3455	ATOM 2516 O PHE C 43 -8.605 -3.535 21.334 1.00 17.05 O
3456	ATOM 2517 CB PHE C 43 -8.817 -1.519 19.333 1.00 26.70 C
3457	ATOM 2518 CG PHE C 43 -8.906 -0.392 18.437 1.00 14.42 C
3458	ATOM 2519 CD1 PHE C 43 -8.473 -0.554 17.054 1.00 15.73 C
3459	ATOM 2520 CD2 PHE C 43 -9.700 0.777 18.998 1.00 15.90 C
3460	ATOM 2521 CE1 PHE C 43 -8.663 0.579 16.317 1.00 16.99 C
3461	ATOM 2522 CE2 PHE C 43 -9.585 1.781 18.059 1.00 19.76 C
3462	ATOM 2523 CZ PHE C 43 -9.193 1.883 16.726 1.00 10.96 C
3463	ATOM 2524 N PRO C 44 -6.303 -3.266 21.758 1.00 17.51 N
3464	ATOM 2525 CA PRO C 44 -6.430 -4.575 22.577 1.00 22.01 C
3465	ATOM 2526 C PRO C 44 -7.021 -4.034 23.952 1.00 23.34 C
3466	ATOM 2527 O PRO C 44 -7.479 -5.004 24.549 1.00 23.67 O
3467	ATOM 2528 CB PRO C 44 -4.725 -4.600 22.823 1.00 28.76 C
3468	ATOM 2529 CG PRO C 44 -4.302 -3.265 22.722 1.00 30.00 C
3469	ATOM 2530 CD PRO C 44 -5.000 -2.496 21.564 1.00 18.17 C
3470	ATOM 2531 N HIS C 45 -7.313 -2.986 24.170 1.00 23.82 N
3471	ATOM 2532 CA HIS C 45 -8.129 -2.454 25.363 1.00 24.33 C
3472	ATOM 2533 C HIS C 45 -9.774 -2.425 25.223 1.00 36.67 C
3473	ATOM 2534 O HIS C 45 -10.201 -1.856 26.159 1.00 32.61 O
3474	ATOM 2535 CB HIS C 45 -7.724 -1.122 25.714 1.00 29.73 C
3475	ATOM 2536 CG HIS C 45 -7.512 0.207 24.830 1.00 29.43 C
3476	ATOM 2537 ND1 HIS C 45 -6.904 -0.240 23.536 1.00 26.84 N
3477	ATOM 2538 CD2 HIS C 45 -8.212 1.313 24.765 1.00 33.54 C
3478	ATOM 2539 CE1 HIS C 45 -7.241 0.770 23.119 1.00 37.75 C
3479	ATOM 2540 NE2 HIS C 45 -7.901 1.880 23.651 1.00 39.11 N
3480	ATOM 2541 N PHE C 46 -10.097 -2.588 23.981 1.00 19.71 N
3481	ATOM 2542 CA PHE C 46 -11.427 -2.447 23.784 1.00 16.71 C
3482	ATOM 2543 C PHE C 46 -11.984 -3.704 23.878 1.00 21.27 C
3483	ATOM 2544 O PHE C 46 -11.601 -4.890 23.408 1.00 23.84 O
3484	ATOM 2545 CB PHE C 46 -11.721 -1.909 22.223 1.00 21.57 C
3485	ATOM 2546 CG PHE C 46 -11.812 -0.571 22.355 1.00 17.89 C
3486	ATOM 2547 CD1 PHE C 46 -12.584 0.134 21.407 1.00 29.22 C
3487	ATOM 2548 CD2 PHE C 46 -11.092 0.466 22.932 1.00 29.35 C
3488	ATOM 2549 CE1 PHE C 46 -12.539 1.579 21.231 1.00 23.51 C
3489	ATOM 2550 CE2 PHE C 46 -11.283 1.342 22.737 1.00 34.19 C
3490	ATOM 2551 CZ PHE C 46 -11.794 2.381 21.680 1.00 30.38 C
3491	ATOM 2552 N ASP C 47 -13.484 -3.924 24.123 1.00 21.22 N
3492	ATOM 2553 CA ASP C 47 -14.200 -5.093 23.710 1.00 21.17 C
3493	ATOM 2554 C ASP C 47 -14.972 -4.945 22.231 1.00 15.44 C
3494	ATOM 2555 O ASP C 47 -15.394 -3.747 22.085 1.00 19.22 O
3495	ATOM 2556 CB ASP C 47 -15.564 -4.912 24.743 1.00 26.87 C
3496	ATOM 2557 CG ASP C 47 -16.291 -6.456 24.524 1.00 44.60 C
3497	ATOM 2558 OD1 ASP C 47 -16.314 -6.539 23.491 1.00 38.14 O
3498	ATOM 2559 OD2 ASP C 47 -17.247 -6.397 25.386 1.00 35.16 O
3499	ATOM 2560 N LEU C 48 -14.283 -5.744 21.445 1.00 20.23 N
3500	ATOM 2561 CA LEU C 48 -14.738 -5.455 19.945 1.00 22.13 C
3501	ATOM 2562 C LEU C 48 -15.716 -6.250 19.550 1.00 26.79 C
3502	ATOM 2563 O LEU C 48 -16.269 -6.380 18.272 1.00 28.79 O
3503	ATOM 2564 CB LEU C 48 -13.468 -5.863 19.207 1.00 20.10 C
3504	ATOM 2565 CG LEU C 48 -12.283 -5.143 19.138 1.00 22.13 C
3505	ATOM 2566 CD1 LEU C 48 -10.976 -5.443 18.455 1.00 30.66 C
3506	ATOM 2567 CD2 LEU C 48 -12.440 -3.412 19.024 1.00 21.27 C
3507	ATOM 2568 N SER C 49 -16.750 -6.795 20.348 1.00 29.67 N
3508	ATOM 2569 CA SER C 49 -17.996 -7.682 20.348 1.00 26.45 C
3509	ATOM 2570 C SER C 49 -18.688 -6.784 19.661 1.00 19.97 C
3510	ATOM 2571 O SER C 49 -18.950 -5.536 19.662 1.00 20.96 O
3511	ATOM 2572 CB SER C 49 -18.391 -8.577 21.574 1.00 26.72 C
3512	ATOM 2573 OG SER C 49 -18.238 -7.994 22.499 1.00 34.29 O
3513	ATOM 2574 N HIS C 50 -19.776 -7.581 18.833 1.00 28.23 N
3514	ATOM 2575 CA HIS C 50 -20.784 -6.859 18.155 1.00 26.06 C
3515	ATOM 2576 C HIS C 50 -21.742 -6.003 19.283 1.00 24.81 C
3516	ATOM 2577 O HIS C 50 -21.976 -6.730 20.143 1.00 27.33 O
3517	ATOM 2578 CB HIS C 50 -21.772 -7.860 17.171 1.00 33.58 C
3518	ATOM 2579 CG HIS C 50 -22.495 -6.997 16.501 1.00 21.75 C
3519	ATOM 2580 ND1 HIS C 50 -24.098 -7.224 16.903 1.00 37.61 N
3520	ATOM 2581 CD2 HIS C 50 -22.721 -6.030 15.749 1.00 24.11 C
3521	ATOM 2582 CE1 HIS C 50 -24.713 -6.289 16.301 1.00 35.12 C
3522	ATOM 2583 NE2 HIS C 50 -23.972 -5.305 15.362 1.00 42.35 N
3523	ATOM 2584 N GLY C 51 -21.911 -4.827 19.019 1.00 24.42 N
3524	ATOM 2585 CA GLY C 51 -22.633 -4.098 19.831 1.00 26.56 C
3525	ATOM 2586 C GLY C 51 -22.082 -3.387 20.930 1.00 23.39 C
3526	ATOM 2587 O GLY C 51 -22.536 -2.501 21.731 1.00 25.53 O
3527	ATOM 2588 N SER C 52 -20.724 -3.498 20.885 1.00 22.06 N
3528	ATOM 2589 CA SER C 52 -19.739 -2.846 21.982 1.00 25.03 C
3529	ATOM 2590 C SER C 52 -19.903 -1.593 22.193 1.00 31.37 C
3530	ATOM 2591 O SER C 52 -19.945 -0.663 21.200 1.00 22.94 O
3531	ATOM 2592 CB SER C 52 -18.376 -3.162 21.704 1.00 30.26 C
3532	ATOM 2593 OG SER C 52 -17.567 -2.497 22.631 1.00 21.66 O
3533	ATOM 2594 N ALA C 53 -20.311 -0.885 23.302 1.00 22.15 N
3534	ATOM 2595 CA ALA C 53 -20.223 0.561 23.639 1.00 29.32 C
3535	ATOM 2596 C ALA C 53 -19.008 1.341 23.195 1.00 23.50 C
3536	ATOM 2597 O ALA C 53 -19.144 2.489 22.964 1.00 19.56 O
3537	ATOM 2598 CB ALA C 53 -21.016 0.770 24.778 1.00 46.37 C
3538	ATOM 2599 N GLN C 54 -18.075 0.456 23.565 1.00 20.69 N
3539	ATOM 2600 CA GLN C 54 -16.671 1.124 23.388 1.00 22.13 C
3540	ATOM 2601 C GLN C 54 -16.498 1.625 21.724 1.00 21.00 C
3541	ATOM 2602 O GLN C 54 -15.986 2.677 21.452 1.00 19.66 O
3542	ATOM 2603 CB GLN C 54 -15.533 0.388 23.780 1.00 23.01 C
3543	ATOM 2604 CG GLN C 54 -15.387 0.264 25.146 1.00 26.98 C
3544	ATOM 2605 CD GLN C 54 -14.244 -0.704 25.751 1.00 17.64 C
3545	ATOM 2606 OE1 GLN C 54 -14.213 -1.867 25.317 1.00 23.97 O
3546	ATOM 2607 NE2 GLN C 54 -13.269 -0.029 26.343 1.00 35.16 N
3547	ATOM 2608 N VAL C 55 -16.998 0.495 20.976 1.00 18.58 N
3548	ATOM 2609 CA VAL C 55 -16.782 0.728 19.397 1.00 18.23 C
3549	ATOM 2610 C VAL C 55 -17.788 1.835 19.121 1.00 15.73 C
3550	ATOM 2611 O VAL C 55 -17.557 2.638 18.250 1.00 16.15 O
3551	ATOM 2612 CB VAL C 55 -17.023 -0.655 18.769 1.00 16.13 C
3552	ATOM 2613 CG1 VAL C 55 -17.141 -0.282 17.289 1.00 22.56 C
3553	ATOM 2614 CG2 VAL C 55 -15.953 -1.526 19.088 1.00 16.34 C
3554	ATOM 2615 N LYS C 56 -19.064 1.844 19.638 1.00 17.00 N
3555	ATOM 2616 CA LYS C 56 -20.011 2.798 19.335 1.00 18.57 C
3556	ATOM 2617 C LYS C 56 -19.657 4.015 19.595 1.00 20.36 C
3557	ATOM 2618 O LYS C 56 -19.638 5.117 18.950 1.00 20.10 O
3558	ATOM 2619 CB LYS C 56 -21.306 2.565 20.099 1.00 27.04 C
3559	ATOM 2620 CG LYS C 56 -22.017 1.239 19.517 1.00 42.35 C
3560	ATOM 2621 CD LYS C 56 -23.983 2.334 19.796 1.00 43.36 C
3561	ATOM 2622 CE LYS C 56 -24.238 -0.016 19.420 1.00 48.38 C
3562	ATOM 2623 NZ LYS C 56 -25.547 0.420 20.454 1.00 67.70 N
3563	ATOM 2624 N GLY C 57 -18.873 4.239 20.758 1.00 16.00 N
3564	ATOM 2625 CA GLY C 57 -18.397 5.432 21.231 1.00 21.54 C
3565	ATOM 2626 C GLY C 57 -17.299 6.086 20.387 1.00 18.61 C
3566	ATOM 2627 O GLY C 57 -17.174 7.416 20.069 1.00 24.59 O
3567	ATOM 2628 N HIS C 58 -16.421 5.133 20.063 1.00 15.81 N
3568	ATOM 2629 CA HIS C 58 -15.259 5.492 19.163 1.00 16.10 C
3569	ATOM 2630 C HIS C 58 -15.968 5.977 17.705 1.00 21.16 C
3570	ATOM 2631 O HIS C 58 -15.334 6.873 17.165 1.00 17.74 O
3571	ATOM 2632 CB HIS C 58 -14.298 4.450 19.037 1.00 15.43 C
3572	ATOM 2633 CG HIS C 58 -13.084 4.816 18.336 1.00 18.98 C
3573	ATOM 2634 ND1 HIS C 58 -12.377 5.886 18.887 1.00 21.14 N
3574	ATOM 2635 CD2 HIS C 58 -12.537 4.339 17.359 1.00 16.95 C
3575	ATOM 2636 CE1 HIS C 58 -11.397 5.896 17.811 1.00 21.77 C
3576	ATOM 2637 NE2 HIS C 58 -11.418 4.951 16.789 1.00 17.45 N
3577	ATOM 2638 N GLY C 59 -16.820 5.155 17.321 1.00 20.04 N
3578	ATOM 2639 CA GLY C 59 -17.341 5.505 16.148 1.00 24.32 C
3579	ATOM 2640 C GLY C 59 -18.005 6.810 15.949 1.00 16.44 C
3580	ATOM 2641 O GLY C 59 -17.768 7.655 14.926 1.00 16.63 O
3581	ATOM 2642 N LYS C 60 -18.641 7.304 17.045 1.00 14.40 N
3582	ATOM 2643 CA LYS C 60 -19.047 8.674 17.195 1.00 14.87 C
3583	ATOM 2644 C LYS C 60 -18.066 9.704 17.103 1.00 17.20 C
3584	ATOM 2645 O LYS C 60 -18.083 10.725 16.452 1.00 19.10 O
3585	ATOM 2646 CB LYS C 60 -20.090 8.722 18.417 1.00 20.14 C
3586	ATOM 2647 CG LYS C 60 -20.474 10.102 18.286 1.00 36.22 C
3587	ATOM 2648 CD LYS C 60 -21.736 10.498 19.120 1.00 67.45 C
3588	ATOM 2649 CE LYS C 60 -22.281 11.583 18.549 1.00 61.41 C
3589	ATOM 2650 NZ LYS C 60 -21.104 12.754 19.691 1.00 67.02 N
3590	ATOM 2651 N LYS C 61 -16.927 9.423 17.774 1.00 17.79 N
3591	ATOM 2652 CA LYS C 61 -15.858 10.357 17.767 1.00 21.13 C
3592	ATOM 2653 C LYS C 61 -15.164 10.595 16.162 1.00 16.24 C
3593	ATOM 2654 O LYS C 61 -14.881 11.695 15.808 1.00 15.80 O
3594	ATOM 2655 CB LYS C 61 -14.696 9.830 18.603 1.00 23.05 C
3595	ATOM 2656 CG LYS C 61 -15.062 10.074 19.860 1.00 29.48 C
3596	ATOM 2657 CD LYS C 61 -14.168 9.693 20.841 1.00 35.76 C
3597	ATOM 2658 CE LYS C 61 -14.859 10.184 22.437 1.00 58.26 C
3598	ATOM 2659 NZ LYS C 61 -13.290 9.055 22.853 1.00 59.87 N
3599	ATOM 2660 N VAL C 62 -15.053 9.278 15.522 1.00 15.31 N
3600	ATOM 2661 CA VAL C 62 -14.623 9.355 14.153 1.00 17.56 C
3601	ATOM 2662 C VAL C 62 -15.371 10.194 13.113 1.00 16.25 C
3602	ATOM 2663 O VAL C 62 -15.014 11.087 12.455 1.00 13.61 O
3603	ATOM 2664 CB VAL C 62 -14.380 7.809 13.720 1.00 18.84 C
3604	ATOM 2665 CG1 VAL C 62 -14.183 7.763 12.290 1.00 17.19 C
3605	ATOM 2666 CG2 VAL C 62 -13.252 7.305 14.521 1.00 18.33 C
3606	ATOM 2667 N ALA C 63 -16.701 9.866 13.495 1.00 13.67 N
3607	ATOM 2668 CA ALA C 63 -17.818 10.501 12.645 1.00 21.56 C
3608	ATOM 2669 C ALA C 63 -17.715 11.855 12.728 1.00 19.04 C
3609	ATOM 2670 O ALA C 63 -17.832 12.775 11.974 1.00 17.01 O
3610	ATOM 2671 CB ALA C 63 -19.206 9.890 12.827 1.00 17.02 C
3611	ATOM 2672 N ASP C 64 -17.653 12.417 13.991 1.00 16.51 N
3612	ATOM 2673 CA ASP C 64 -17.709 13.830 14.243 1.00 19.49 C
3613	ATOM 2674 C ASP C 64 -16.540 14.535 13.748 1.00 14.91 C
3614	ATOM 2675 O ASP C 64 -16.584 15.604 13.224 1.00 19.95 O
3615	ATOM 2676 CB ASP C 64 -17.991 14.096 15.799 1.00 24.76 C
3616	ATOM 2677 CG ASP C 64 -19.393 13.818 16.643 1.00 34.25 C
3617	ATOM 2678 OD1 ASP C 64 -20.152 13.414 15.899 1.00 28.85 O
3618	ATOM 2679 OD2 ASP C 64 -19.056 13.688 17.650 1.00 27.13 O
3619	ATOM 2680 N ALA C 65 -15.369 13.857 13.860 1.00 16.65 N
3620	ATOM 2681 CA ALA C 65 -14.163 14.481 13.291 1.00 16.32 C
3621	ATOM 2682 C ALA C 65 -14.252 14.735 11.694 1.00 13.95 C
3622	ATOM 2683 O ALA C 65 -13.994 15.689 11.048 1.00 16.33 O
3623	ATOM 2684 CB ALA C 65 -13.017 13.593 13.359 1.00 16.15 C
3624	ATOM 2685 N LEU C 66 -15.064 13.712 10.969 1.00 17.13 N
3625	ATOM 2686 CA LEU C 66 -15.337 13.726 9.525 1.00 13.55 C
3626	ATOM 2687 C LEU C 66 -16.272 14.810 9.233 1.00 14.32 C
3627	ATOM 2688 O LEU C 66 -16.159 15.647 8.296 1.00 15.99 O
3628	ATOM 2689 CB LEU C 66 -15.780 12.400 8.970 1.00 12.37 C
3629	ATOM 2690 CG LEU C 66 -14.557 11.353 8.900 1.00 14.22 C
3630	ATOM 2691 CD1 LEU C 66 -15.162 10.177 8.798 1.00 25.53 C
3631	ATOM 2692 CD2 LEU C 66 -13.636 11.641 7.894 1.00 14.43 C
3632	ATOM 2693 N THR C 67 -17.292 14.977 10.145 1.00 14.80 N
3633	ATOM 2694 CA THR C 67 -18.300 16.119 9.983 1.00 15.27 C
3634	ATOM 2695 C THR C 67 -17.479 17.374 10.100 1.00 19.15 C
3635	ATOM 2696 O THR C 67 -17.741 18.262 9.274 1.00 21.53 O
3636	ATOM 2697 CB THR C 67 -19.282 15.886 11.189 1.00 13.22 C
3637	ATOM 2698 OG1 THR C 67 -20.066 14.785 10.961 1.00 17.30 O
3638	ATOM 2699 CG2 THR C 67 -20.207 17.226 11.132 1.00 30.44 C
3639	ATOM 2700 N ASN C 68 -16.541 17.536 11.125 1.00 19.52 N
3640	ATOM 2701 CA ASN C 68 -15.765 18.613 11.088 1.00 21.49 C
3641	ATOM 2702 C ASN C 68 -14.901 18.833 9.858 1.00 19.25 C
3642	ATOM 2703 O ASN C 68 -14.653 20.197 9.353 1.00 22.73 O
3643	ATOM 2704 CB ASN C 68 -14.964 18.621 12.362 1.00 16.47 C
3644	ATOM 2705 CG ASN C 68 -13.974 19.880 12.584 1.00 43.34 C
3645	ATOM 2706 OD1 ASN C 68 -14.128 20.746 12.326 1.00 49.22 O
3646	ATOM 2707 ND2 ASN C 68 -12.524 19.654 13.058 1.00 50.67 N
3647	ATOM 2708 N ALA C 69 -14.378 17.793 9.402 1.00 16.22 N
3648	ATOM 2709 CA ALA C 69 -13.526 17.929 8.006 1.00 15.27 C
3649	ATOM 2710 C ALA C 69 -14.531 18.551 6.897 1.00 20.32 C
3650	ATOM 2711 O ALA C 69 -13.858 19.250 6.103 1.00 22.38 O
3651	ATOM 2712 CB ALA C 69 -12.891 16.615 7.759 1.00 15.52 C
3652	ATOM 2713 N VAL C 70 -15.649 17.853 6.837 1.00 18.62 N
3653	ATOM 2714 CA VAL C 70 -16.708 18.432 5.673 1.00 21.72 C
3654	ATOM 2715 C VAL C 70 -16.947 20.121 6.025 1.00 33.94 C
3655	ATOM 2716 O VAL C 70 -16.795 20.608 4.872 1.00 26.93 O
3656	ATOM 2717 CB VAL C 70 -17.884 17.598 5.765 1.00 16.50 C
3657	ATOM 2718 CG1 VAL C 70 -18.759 18.120 4.709 1.00 19.06 C
3658	ATOM 2719 CG2 VAL C 70 -17.623 16.139 5.358 1.00 16.14 C
3659	ATOM 2720 N ALA C 71 -17.135 20.362 6.965 1.00 27.30 N
3660	ATOM 2721 CA ALA C 71 -17.392 21.922 7.494 1.00 22.92 C
3661	ATOM 2722 C ALA C 71 -16.435 22.534 6.896 1.00 25.79 C
3662	ATOM 2723 O ALA C 71 -16.374 23.836 6.718 1.00 24.88 O
3663	ATOM 2724 CB ALA C 71 -17.865 21.980 8.684 1.00 26.73 C
3664	ATOM 2725 N HIS C 72 -15.134 22.254 6.980 1.00 25.11 N
3665	ATOM 2726 CA HIS C 72 -13.948 22.613 6.662 1.00 31.54 C
3666	ATOM 2727 C HIS C 72 -13.174 22.493 5.762 1.00 23.73 C
3667	ATOM 2728 O HIS C 72 -11.739 22.306 5.638 1.00 26.60 O
3668	ATOM 2729 CB HIS C 72 -12.834 22.798 8.133 1.00 34.18 C
3669	ATOM 2730 CG HIS C 72 -13.458 23.235 9.080 1.00 46.84 C
3670	ATOM 2731 ND1 HIS C 72 -13.546 24.937 9.646 1.00 41.84 N
3671	ATOM 2732 CD2 HIS C 72 -14.636 22.949 10.155 1.00 36.64 C
3672	ATOM 2733 CE1 HIS C 72 -14.088 24.896 10.559 1.00 46.81 C
3673	ATOM 2734 NE2 HIS C 72 -14.920 23.926 11.193 1.00 49.65 N
3674	ATOM 2735 N VAL C 73 -13.783 21.917 4.647 1.00 19.28 N
3675	ATOM 2736 CA VAL C 73 -13.123 21.287 3.673 1.00 19.45 C
3676	ATOM 2737 C VAL C 73 -11.827 22.122 2.987 1.00 29.84 C
3677	ATOM 2738 O VAL C 73 -10.987 21.361 2.509 1.00 35.51 O
3678	ATOM 2739 CB VAL C 73 -14.122 20.427 2.448 1.00 30.11 C
3679	ATOM 2740 CG1 VAL C 73 -14.780 21.629 2.180 1.00 33.72 C
3680	ATOM 2741 CG2 VAL C 73 -13.307 19.397 1.916 1.00 28.74 C
3681	ATOM 2742 N ASP C 74 -12.046 23.454 3.145 1.00 28.51 N
3682	ATOM 2743 CA ASP C 74 -10.850 24.295 2.500 1.00 28.33 C
3683	ATOM 2744 C ASP C 74 -9.537 24.483 3.294 1.00 41.00 C
3684	ATOM 2745 O ASP C 74 -8.999 25.130 2.953 1.00 39.68 O
3685	ATOM 2746 CB ASP C 74 -11.641 25.551 2.038 1.00 34.16 C
3686	ATOM 2747 CG ASP C 74 -12.636 25.691 1.138 1.00 52.11 C
3687	ATOM 2748 OD1 ASP C 74 -12.809 24.845 -0.109 1.00 41.95 O
3688	ATOM 2749 OD2 ASP C 74 -13.725 26.027 1.050 1.00 57.27 O
3689	ATOM 2750 N ASP C 75 -9.900 24.071 4.497 1.00 29.36 N
3690	ATOM 2751 CA ASP C 75 -8.638 24.283 5.628 1.00 35.73 C
3691	ATOM 2752 C ASP C 75 -9.022 23.128 6.558 1.00 33.10 C
3692	ATOM 2753 O ASP C 75 -8.649 23.257 7.697 1.00 33.04 O
3693	ATOM 2754 CB ASP C 75 -9.160 25.604 6.376 1.00 60.97 C
3694	ATOM 2755 CG ASP C 75 -8.310 26.492 7.214 1.00 66.84 C
3695	ATOM 2756 OD1 ASP C 75 -7.090 26.471 6.833 1.00 48.92 O
3696	ATOM 2757 OD2 ASP C 75 -9.269 26.482 8.164 1.00 62.98 O
3697	ATOM 2758 N MET C 76 -8.644 21.799 5.775 1.00 27.58 N
3698	ATOM 2759 CA MET C 76 -8.452 20.656 6.738 1.00 27.89 C
3699	ATOM 2760 C MET C 76 -7.374 20.534 7.506 1.00 27.58 C
3700	ATOM 2761 O MET C 76 -7.529 20.166 8.646 1.00 20.50 O
3701	ATOM 2762 CB MET C 76 -8.792 19.438 5.724 1.00 26.12 C
3702	ATOM 2763 CG MET C 76 -10.257 19.383 5.400 1.00 43.36 C
3703	ATOM 2764 SD MET C 76 -10.271 17.473 4.652 1.00 37.03 S
3704	ATOM 2765 CE MET C 76 -9.415 17.721 3.291 1.00 44.39 C
3705	ATOM 2766 N PRO C 77 -6.212 20.856 6.950 1.00 20.45 N
3706	ATOM 2767 CA PRO C 77 -5.120 20.876 8.013 1.00 25.45 C
3707	ATOM 2768 C PRO C 77 -5.008 21.386 9.255 1.00 36.43 C
3708	ATOM 2769 O PRO C 77 -4.686 20.931 10.357 1.00 30.57 O
3709	ATOM 2770 CB PRO C 77 -3.910 21.274 7.011 1.00 26.13 C
3710	ATOM 2771 CG PRO C 77 -4.232 21.298 5.608 1.00 24.41 C
3711	ATOM 2772 CD PRO C 77 -5.794 21.507 5.765 1.00 18.39 C
3712	ATOM 2773 N ASN C 78 -5.556 22.597 9.438 1.00 27.78 N
3713	ATOM 2774 CA ASN C 78 -6.067 23.245 10.604 1.00 53.47 C
3714	ATOM 2775 C ASN C 78 -6.714 22.831 11.450 1.00 25.06 C
3715	ATOM 2776 O ASN C 78 -6.836 22.551 12.629 1.00 27.11 O
3716	ATOM 2777 CB ASN C 78 -5.848 24.913 10.378 1.00 49.62 C
3717	ATOM 2778 CG ASN C 78 -5.937 25.817 11.891 1.00 27.09 C
3718	ATOM 2779 OD1 ASN C 78 -5.094 25.489 12.673 1.00 25.78 O
3719	ATOM 2780 ND2 ASN C 78 -7.164 26.163 12.327 1.00 30.98 N
3720	ATOM 2781 N ALA C 79 -8.038 22.510 10.822 1.00 21.32 N
3721	ATOM 2782 CA ALA C 79 -9.063 21.943 11.591 1.00 21.47 C
3722	ATOM 2783 C ALA C 79 -8.803 20.510 12.317 1.00 24.81 C
3723	ATOM 2784 O ALA C 79 -9.440 20.242 13.323 1.00 25.13 O
3724	ATOM 2785 CB ALA C 79 -10.333 21.459 10.764 1.00 25.42 C
3725	ATOM 2786 N LEU C 80 -8.034 19.757 11.542 1.00 14.71 N
3726	ATOM 2787 CA LEU C 80 -7.693 18.364 12.080 1.00 14.80 C
3727	ATOM 2788 C LEU C 80 -6.147 18.320 12.632 1.00 13.69 C
3728	ATOM 2789 O LEU C 80 -5.765 17.251 13.012 1.00 17.02 O
3729	ATOM 2790 CB LEU C 80 -7.618 17.425 10.975 1.00 23.31 C
3730	ATOM 2791 CG LEU C 80 -9.017 17.241 10.096 1.00 28.90 C
3731	ATOM 2792 CD1 LEU C 80 -8.888 16.179 9.066 1.00 22.59 C
3732	ATOM 2793 CD2 LEU C 80 -9.912 16.862 11.126 1.00 28.24 C
3733	ATOM 2794 N SER C 81 -5.642 19.595 13.022 1.00 15.20 N
3734	ATOM 2795 CA SER C 81 -4.176 19.598 13.532 1.00 16.69 C
3735	ATOM 2796 C SER C 81 -4.082 18.751 14.821 1.00 15.66 C
3736	ATOM 2797 O SER C 81 -3.121 18.036 14.913 1.00 18.30 O
3737	ATOM 2798 CB SER C 81 -4.200 21.212 13.927 1.00 20.04 C
3738	ATOM 2799 OG SER C 81 -2.662 21.194 13.956 1.00 27.86 O
3739	ATOM 2800 N ALA C 82 -4.975 18.951 15.740 1.00 16.14 N
3740	ATOM 2801 CA ALA C 82 -4.666 18.152 16.940 1.00 27.63 C
3741	ATOM 2802 C ALA C 82 -4.666 16.766 16.844 1.00 26.48 C
3742	ATOM 2803 O ALA C 82 -4.201 15.804 17.443 1.00 22.53 O
3743	ATOM 2804 CB ALA C 82 -5.631 18.625 18.033 1.00 26.01 C
3744	ATOM 2805 N LEU C 83 -5.794 16.171 15.738 1.00 16.69 N
3745	ATOM 2806 CA LEU C 83 -5.833 14.767 15.713 1.00 11.24 C
3746	ATOM 2807 C LEU C 83 -4.721 14.342 14.699 1.00 14.18 C
3747	ATOM 2808 O LEU C 83 -4.218 13.107 15.018 1.00 18.82 O
3748	ATOM 2809 CB LEU C 83 -7.049 14.621 14.641 1.00 19.57 C
3749	ATOM 2810 CG LEU C 83 -8.323 14.343 15.598 1.00 31.08 C
3750	ATOM 2811 CD1 LEU C 83 -9.453 13.945 14.510 1.00 37.56 C
3751	ATOM 2812 CD2 LEU C 83 -8.174 13.408 16.783 1.00 31.25 C
3752	ATOM 2813 N SER C 84 -4.154 15.133 13.918 1.00 17.80 N
3753	ATOM 2814 CA SER C 84 -2.888 14.776 13.267 1.00 16.31 C
3754	ATOM 2815 C SER C 84 -1.740 14.590 14.181 1.00 16.72 C
3755	ATOM 2816 O SER C 84 -0.882 13.728 14.196 1.00 20.08 O
3756	ATOM 2817 CB SER C 84 -1.928 15.701 12.069 1.00 25.74 C
3757	ATOM 2818 OG SER C 84 -2.988 16.059 11.690 1.00 36.74 O
3758	ATOM 2819 N ASP C 85 -1.671 15.596 15.245 1.00 14.56 N
3759	ATOM 2820 CA ASP C 85 -0.682 15.299 16.354 1.00 16.51 C
3760	ATOM 2821 C ASP C 85 -0.794 14.103 17.109 1.00 12.46 C
3761	ATOM 2822 O ASP C 85 0.064 13.405 17.411 1.00 15.88 O
3762	ATOM 2823 CB ASP C 85 -0.758 16.459 17.195 1.00 24.70 C
3763	ATOM 2824 CG ASP C 85 -0.167 17.721 16.629 1.00 34.11 C
3764	ATOM 2825 OD1 ASP C 85 0.446 17.900 15.796 1.00 25.15 O
3765	ATOM 2826 OD2 ASP C 85 -0.625 18.754 17.406 1.00 33.76 O
3766	ATOM 2827 N LEU C 86 -2.190 13.771 17.337 1.00 12.70 N
3767	ATOM 2828 CA LEU C 86 -2.467 12.693 18.111 1.00 16.53 C
3768	ATOM 2829 C LEU C 86 -2.015 11.303 17.695 1.00 14.13 C
3769	ATOM 2830 O LEU C 86 -1.425 10.432 18.116 1.00 17.79 O
3770	ATOM 2831 CB LEU C 86 -3.980 12.638 18.447 1.00 18.93 C
3771	ATOM 2832 CG LEU C 86 -4.506 11.657 19.521 1.00 29.36 C
3772	ATOM 2833 CD1 LEU C 86 -3.802 11.791 20.879 1.00 25.18 C
3773	ATOM 2834 CD2 LEU C 86 -5.938 11.585 19.602 1.00 37.62 C
3774	ATOM 2835 N HIS C 87 -2.350 11.290 16.308 1.00 15.64 N
3775	ATOM 2836 CA HIS C 87 -2.196 9.988 15.684 1.00 15.27 C
3776	ATOM 2837 C HIS C 87 -0.432 9.776 15.294 1.00 11.96 C
3777	ATOM 2838 O HIS C 87 -0.010 8.655 15.509 1.00 15.54 O
3778	ATOM 2839 CB HIS C 87 -2.877 9.761 14.248 1.00 15.31 C
3779	ATOM 2840 CG HIS C 87 -4.370 9.569 14.496 1.00 12.16 C
3780	ATOM 2841 ND1 HIS C 87 -5.204 10.514 14.931 1.00 15.96 N
3781	ATOM 2842 CD2 HIS C 87 -5.162 8.339 14.571 1.00 14.58 C
3782	ATOM 2843 CE1 HIS C 87 -6.508 9.921 15.132 1.00 13.46 C
3783	ATOM 2844 NE2 HIS C 87 -6.403 8.796 14.850 1.00 17.27 N
3784	ATOM 2845 N ALA C 88 0.106 11.030 15.024 1.00 14.25 N
3785	ATOM 2846 CA ALA C 88 1.440 11.027 14.747 1.00 15.37 C
3786	ATOM 2847 C ALA C 88 2.402 10.439 15.994 1.00 19.72 C
3787	ATOM 2848 O ALA C 88 3.419 9.888 15.742 1.00 18.60 O
3788	ATOM 2849 CB ALA C 88 2.009 12.263 14.095 1.00 17.41 C
3789	ATOM 2850 N HIS C 89 2.139 11.270 17.065 1.00 17.52 N
3790	ATOM 2851 CA HIS C 89 2.856 11.246 18.393 1.00 20.01 C
3791	ATOM 2852 C HIS C 89 2.445 10.295 19.376 1.00 19.52 C
3792	ATOM 2853 O HIS C 89 3.400 9.856 20.127 1.00 22.69 O
3793	ATOM 2854 CB HIS C 89 3.204 12.750 18.766 1.00 26.82 C
3794	ATOM 2855 CG HIS C 89 3.898 13.462 17.550 1.00 23.76 C
3795	ATOM 2856 ND1 HIS C 89 5.028 13.110 16.879 1.00 28.14 N
3796	ATOM 2857 CD2 HIS C 89 3.344 14.574 17.213 1.00 25.55 C
3797	ATOM 2858 CE1 HIS C 89 4.845 14.030 16.064 1.00 32.36 C
3798	ATOM 2859 NE2 HIS C 89 4.173 15.010 16.064 1.00 29.26 N
3799	ATOM 2860 N LYS C 90 1.340 9.800 19.443 1.00 16.72 N
3800	ATOM 2861 CA LYS C 90 0.718 9.223 20.440 1.00 20.32 C
3801	ATOM 2862 C LYS C 90 0.299 7.707 20.002 1.00 20.91 C
3802	ATOM 2863 O LYS C 90 0.862 6.631 20.320 1.00 23.22 O
3803	ATOM 2864 CB LYS C 90 -0.138 9.844 21.447 1.00 20.81 C
3804	ATOM 2865 CG LYS C 90 -0.560 8.580 22.285 1.00 29.14 C
3805	ATOM 2866 CD LYS C 90 -1.751 9.734 23.205 1.00 67.74 C
3806	ATOM 2867 CE LYS C 90 -1.793 8.441 24.607 1.00 66.29 C
3807	ATOM 2868 NZ LYS C 90 -1.676 10.047 25.898 1.00 56.99 N
3808	ATOM 2869 N LEU C 91 -0.852 7.689 19.140 1.00 13.37 N
3809	ATOM 2870 CA LEU C 91 -1.388 6.384 18.683 1.00 10.47 C
3810	ATOM 2871 C LEU C 91 -0.395 5.670 17.757 1.00 15.87 C
3811	ATOM 2872 O LEU C 91 -0.337 4.504 17.810 1.00 17.45 O
3812	ATOM 2873 CB LEU C 91 -2.734 6.916 18.060 1.00 11.80 C
3813	ATOM 2874 CG LEU C 91 -3.503 7.677 18.936 1.00 14.59 C
3814	ATOM 2875 CD1 LEU C 91 -4.817 8.063 18.135 1.00 18.31 C
3815	ATOM 2876 CD2 LEU C 91 -3.927 6.656 20.006 1.00 19.42 C
3816	ATOM 2877 N ARG C 92 0.163 6.386 16.757 1.00 17.30 N
3817	ATOM 2878 CA ARG C 92 1.225 5.888 15.973 1.00 16.69 C
3818	ATOM 2879 C ARG C 92 0.801 4.590 15.144 1.00 18.80 C
3819	ATOM 2880 O ARG C 92 1.289 3.690 14.985 1.00 19.26 O
3820	ATOM 2881 CB ARG C 92 2.462 5.556 16.835 1.00 13.64 C
3821	ATOM 2882 CG ARG C 92 3.207 6.871 17.042 1.00 14.42 C
3822	ATOM 2883 CD ARG C 92 4.320 6.680 18.089 1.00 27.16 C
3823	ATOM 2884 NE ARG C 92 4.955 7.507 17.826 1.00 44.94 N
3824	ATOM 2885 CZ ARG C 92 5.808 6.749 20.563 1.00 38.22 C
3825	ATOM 2886 NH1 ARG C 92 4.053 6.376 21.084 1.00 33.94 N
3826	ATOM 2887 NH2 ARG C 92 6.026 7.349 19.817 1.00 48.21 N
3827	ATOM 2888 N VAL C 93 -0.511 4.844 14.546 1.00 13.36 N
3828	ATOM 2889 CA VAL C 93 -1.122 3.790 13.672 1.00 14.31 C
3829	ATOM 2890 C VAL C 93 -0.425 3.861 12.310 1.00 12.63 C
3830	ATOM 2891 O VAL C 93 -0.266 4.875 11.618 1.00 14.78 O
3831	ATOM 2892 CB VAL C 93 -2.622 4.322 13.422 1.00 8.72 C
3832	ATOM 2893 CG1 VAL C 93 -3.298 3.413 12.409 1.00 14.83 C
3833	ATOM 2894 CG2 VAL C 93 -3.256 4.402 14.761 1.00 15.34 C
3834	ATOM 2895 N ASP C 94 -0.069 2.672 11.865 1.00 14.84 N
3835	ATOM 2896 CA ASP C 94 0.516 2.634 10.645 1.00 17.19 C
3836	ATOM 2897 C ASP C 94 -0.337 3.187 9.492 1.00 13.94 C
3837	ATOM 2898 O ASP C 94 -1.496 2.844 9.436 1.00 13.55 O
3838	ATOM 2899 CB ASP C 94 1.001 1.175 10.166 1.00 19.19 C
3839	ATOM 2900 CG ASP C 94 2.066 1.114 9.015 1.00 25.98 C
3840	ATOM 2901 OD1 ASP C 94 3.132 1.101 9.167 1.00 23.44 O
3841	ATOM 2902 OD2 ASP C 94 1.457 1.246 7.818 1.00 20.10 O
3842	ATOM 2903 N PRO C 95 0.336 3.997 8.656 1.00 13.43 N
3843	ATOM 2904 CA PRO C 95 -0.533 4.680 7.482 1.00 16.10 C
3844	ATOM 2905 C PRO C 95 -1.120 3.788 6.667 1.00 11.12 C
3845	ATOM 2906 O PRO C 95 -2.331 4.229 6.243 1.00 14.55 O
3846	ATOM 2907 CB PRO C 95 0.512 5.399 6.750 1.00 19.09 C
3847	ATOM 2908 CG PRO C 95 1.437 5.610 7.677 1.00 18.28 C
3848	ATOM 2909 CD PRO C 95 1.704 4.489 8.616 1.00 15.64 C
3849	ATOM 2910 N VAL C 96 -0.975 2.426 6.418 1.00 15.60 N
3850	ATOM 2911 CA VAL C 96 -1.688 1.553 5.597 1.00 13.24 C
3851	ATOM 2912 C VAL C 96 -3.093 1.373 6.108 1.00 11.50 C
3852	ATOM 2913 O VAL C 96 -4.125 1.168 5.337 1.00 13.19 O
3853	ATOM 2914 CB VAL C 96 -0.963 0.166 5.595 1.00 20.64 C
3854	ATOM 2915 CG1 VAL C 96 0.380 0.545 5.130 1.00 37.75 C
3855	ATOM 2916 CG2 VAL C 96 -0.986 -0.723 6.614 1.00 28.85 C
3856	ATOM 2917 N ASN C 97 -3.362 1.525 7.446 1.00 9.54 N
3857	ATOM 2918 CA ASN C 97 -4.626 1.297 7.971 1.00 11.68 C
3858	ATOM 2919 C ASN C 97 -5.641 2.261 7.562 1.00 9.63 C
3859	ATOM 2920 O ASN C 97 -6.898 1.950 7.745 1.00 9.95 O
3860	ATOM 2921 CB ASN C 97 -4.431 1.174 9.336 1.00 13.42 C
3861	ATOM 2922 CG ASN C 97 -3.599 -0.084 9.836 1.00 14.06 C
3862	ATOM 2923 OD1 ASN C 97 -3.997 -1.327 9.652 1.00 8.45 O
3863	ATOM 2924 ND2 ASN C 97 -2.374 0.157 10.197 1.00 18.92 N
3864	ATOM 2925 N PHE C 98 -5.236 3.438 7.306 1.00 11.20 N
3865	ATOM 2926 CA PHE C 98 -6.082 4.528 6.931 1.00 10.00 C
3866	ATOM 2927 C PHE C 98 -6.998 4.116 5.628 1.00 12.29 C
3867	ATOM 2928 O PHE C 98 -8.203 4.405 5.580 1.00 11.85 O
3868	ATOM 2929 CB PHE C 98 -5.520 5.917 6.784 1.00 11.84 C
3869	ATOM 2930 CG PHE C 98 -4.966 6.392 8.161 1.00 10.85 C
3870	ATOM 2931 CD1 PHE C 98 -5.796 7.234 8.908 1.00 20.50 C
3871	ATOM 2932 CD2 PHE C 98 -3.900 5.913 8.688 1.00 15.66 C
3872	ATOM 2933 CE1 PHE C 98 -5.555 7.714 10.141 1.00 25.62 C
3873	ATOM 2934 CE2 PHE C 98 -3.735 6.528 10.021 1.00 23.17 C
3874	ATOM 2935 CZ PHE C 98 -4.378 7.442 10.790 1.00 16.17 C
3875	ATOM 2936 N LYS C 99 -6.268 3.417 4.783 1.00 12.40 N
3876	ATOM 2937 CA LYS C 99 -6.999 2.958 3.593 1.00 16.89 C
3877	ATOM 2938 C LYS C 99 -8.208 2.150 3.790 1.00 16.36 C
3878	ATOM 2939 O LYS C 99 -9.081 1.954 3.131 1.00 12.00 O
3879	ATOM 2940 CB LYS C 99 -5.965 2.519 2.404 1.00 37.75 C
3880	ATOM 2941 CG LYS C 99 -5.634 1.867 2.299 1.00 60.42 C
3881	ATOM 2942 CD LYS C 99 -4.523 1.328 0.960 1.00 80.12 C
3882	ATOM 2943 CE LYS C 99 -5.145 -0.811 1.345 1.00 54.41 C
3883	ATOM 2944 NZ LYS C 99 -4.072 -1.896 0.975 1.00 73.17 N
3884	ATOM 2945 N LEU C 100 -7.771 1.248 4.812 1.00 11.58 N
3885	ATOM 2946 CA LEU C 100 -8.668 0.083 5.298 1.00 10.08 C
3886	ATOM 2947 C LEU C 100 -9.923 0.739 5.824 1.00 15.81 C
3887	ATOM 2948 O LEU C 100 -11.033 0.328 5.495 1.00 12.64 O
3888	ATOM 2949 CB LEU C 100 -7.919 -0.962 6.095 1.00 11.52 C
3889	ATOM 2950 CG LEU C 100 -6.700 -1.456 5.659 1.00 12.29 C
3890	ATOM 2951 CD1 LEU C 100 -6.140 -2.487 6.602 1.00 13.43 C
3891	ATOM 2952 CD2 LEU C 100 -6.937 -2.037 4.366 1.00 20.82 C
3892	ATOM 2953 N LEU C 101 -9.764 1.698 6.763 1.00 9.97 N
3893	ATOM 2954 CA LEU C 101 -10.983 2.177 7.355 1.00 11.48 C
3894	ATOM 2955 C LEU C 101 -11.756 3.062 6.216 1.00 15.63 C
3895	ATOM 2956 O LEU C 101 -12.976 2.978 6.299 1.00 14.14 O
3896	ATOM 2957 CB LEU C 101 -10.599 3.208 8.498 1.00 14.89 C
3897	ATOM 2958 CG LEU C 101 -11.670 3.902 9.072 1.00 22.22 C
3898	ATOM 2959 CD1 LEU C 101 -12.818 2.883 9.487 1.00 22.49 C
3899	ATOM 2960 CD2 LEU C 101 -11.241 4.642 10.285 1.00 23.89 C
3900	ATOM 2961 N SER C 102 -11.033 3.737 5.313 1.00 13.80 N
3901	ATOM 2962 CA SER C 102 -11.714 4.605 4.376 1.00 7.27 C
3902	ATOM 2963 C SER C 102 -12.532 3.565 3.508 1.00 8.13 C
3903	ATOM 2964 O SER C 102 -13.716 4.048 3.196 1.00 14.48 O
3904	ATOM 2965 CB SER C 102 -10.627 5.223 3.513 1.00 12.53 C
3905	ATOM 2966 OG SER C 102 -9.908 6.246 4.205 1.00 16.99 O
3906	ATOM 2967 N HIS C 103 -12.013 2.448 3.076 1.00 9.47 N
3907	ATOM 2968 CA HIS C 103 -12.856 1.553 2.231 1.00 7.87 C
3908	ATOM 2969 C HIS C 103 -13.969 1.179 3.005 1.00 9.96 C
3909	ATOM 2970 O HIS C 103 -15.145 1.064 2.463 1.00 11.06 O
3910	ATOM 2971 CB HIS C 103 -12.045 0.334 2.007 1.00 13.28 C
3911	ATOM 2972 CG HIS C 103 -12.687 -0.723 1.251 1.00 12.69 C
3912	ATOM 2973 ND1 HIS C 103 -12.940 -2.084 2.021 1.00 13.59 N
3913	ATOM 2974 CD2 HIS C 103 -13.286 -0.768 0.111 1.00 11.80 C
3914	ATOM 2975 CE1 HIS C 103 -13.607 -2.702 0.895 1.00 18.03 C
3915	ATOM 2976 NE2 HIS C 103 -13.846 -2.052 -0.281 1.00 12.75 N
3916	ATOM 2977 N CYS C 104 -13.956 0.809 4.281 1.00 11.32 N
3917	ATOM 2978 CA CYS C 104 -15.102 0.402 5.220 1.00 10.36 C
3918	ATOM 2979 C CYS C 104 -16.128 1.576 5.312 1.00 10.40 C
3919	ATOM 2980 O CYS C 104 -17.326 1.230 5.408 1.00 13.45 O
3920	ATOM 2981 CB CYS C 104 -14.679 -0.210 6.511 1.00 10.60 C
3921	ATOM 2982 SG CYS C 104 -13.758 -1.766 6.256 1.00 14.84 S
3922	ATOM 2983 N LEU C 105 -15.610 2.759 5.400 1.00 7.19 N
3923	ATOM 2984 CA LEU C 105 -16.550 3.718 5.401 1.00 7.94 C
3924	ATOM 2985 C LEU C 105 -17.308 3.811 4.064 1.00 12.20 C
3925	ATOM 2986 O LEU C 105 -18.557 4.127 4.121 1.00 10.34 O
3926	ATOM 2987 CB LEU C 105 -15.878 5.040 5.656 1.00 21.49 C
3927	ATOM 2988 CG LEU C 105 -16.527 6.202 6.207 1.00 44.61 C
3928	ATOM 2989 CD1 LEU C 105 -16.548 5.934 7.976 1.00 29.90 C
3929	ATOM 2990 CD2 LEU C 105 -14.638 7.055 6.645 1.00 67.41 C
3930	ATOM 2991 N LEU C 106 -16.563 3.801 3.055 1.00 12.01 N
3931	ATOM 2992 CA LEU C 106 -17.399 3.653 1.720 1.00 11.59 C
3932	ATOM 2993 C LEU C 106 -18.331 2.701 1.716 1.00 13.18 C
3933	ATOM 2994 O LEU C 106 -19.445 3.007 1.174 1.00 13.67 O
3934	ATOM 2995 CB LEU C 106 -16.393 3.784 0.463 1.00 15.01 C
3935	ATOM 2996 CG LEU C 106 -15.665 4.920 0.043 1.00 26.98 C
3936	ATOM 2997 CD1 LEU C 106 -14.786 4.477 -0.938 1.00 27.15 C
3937	ATOM 2998 CD2 LEU C 106 -16.427 6.222 -0.197 1.00 28.82 C
3938	ATOM 2999 N VAL C 107 -18.135 1.497 2.015 1.00 9.69 N
3939	ATOM 3000 CA VAL C 107 -18.836 0.268 2.127 1.00 13.59 C
3940	ATOM 3001 C VAL C 107 -20.197 0.605 2.883 1.00 17.84 C
3941	ATOM 3002 O VAL C 107 -21.451 0.519 2.577 1.00 16.17 O
3942	ATOM 3003 CB VAL C 107 -18.247 -1.024 2.534 1.00 6.66 C
3943	ATOM 3004 CG1 VAL C 107 -19.313 -1.975 2.757 1.00 10.41 C
3944	ATOM 3005 CG2 VAL C 107 -17.243 -1.377 1.493 1.00 9.95 C
3945	ATOM 3006 N THR C 108 -20.022 1.317 4.069 1.00 12.50 N
3946	ATOM 3007 CA THR C 108 -21.156 1.586 4.961 1.00 12.00 C
3947	ATOM 3008 C THR C 108 -22.004 2.672 4.235 1.00 8.53 C
3948	ATOM 3009 O THR C 108 -23.266 2.600 4.430 1.00 13.95 O
3949	ATOM 3010 CB THR C 108 -20.489 2.175 6.313 1.00 10.15 C
3950	ATOM 3011 OG1 THR C 108 -19.618 1.211 6.782 1.00 10.65 O
3951	ATOM 3012 CG2 THR C 108 -21.574 2.581 7.303 1.00 9.30 C
3952	ATOM 3013 N LEU C 109 -21.432 3.696 3.675 1.00 9.01 N
3953	ATOM 3014 CA LEU C 109 -22.256 4.765 2.941 1.00 9.31 C
3954	ATOM 3015 C LEU C 109 -23.120 4.001 2.078 1.00 15.85 C
3955	ATOM 3016 O LEU C 109 -24.157 4.405 1.752 1.00 14.26 O
3956	ATOM 3017 CB LEU C 109 -21.296 5.848 2.566 1.00 11.02 C
3957	ATOM 3018 CG LEU C 109 -20.716 6.843 3.619 1.00 19.91 C
3958	ATOM 3019 CD1 LEU C 109 -19.558 7.677 2.954 1.00 29.96 C
3959	ATOM 3020 CD2 LEU C 109 -21.630 7.225 4.484 1.00 27.29 C
3960	ATOM 3021 N ALA C 110 -22.355 3.185 1.097 1.00 14.51 N
3961	ATOM 3022 CA ALA C 110 -22.975 2.438 -0.100 1.00 13.69 C
3962	ATOM 3023 C ALA C 110 -24.179 1.916 0.467 1.00 24.66 C
3963	ATOM 3024 O ALA C 110 -25.339 1.691 -0.205 1.00 18.31 O
3964	ATOM 3025 CB ALA C 110 -21.958 1.541 -0.721 1.00 13.14 C
3965	ATOM 3026 N ALA C 111 -24.108 1.069 1.636 1.00 17.30 N
3966	ATOM 3027 CA ALA C 111 -25.131 0.205 2.227 1.00 14.98 C
3967	ATOM 3028 C ALA C 111 -26.406 1.141 2.649 1.00 17.59 C
3968	ATOM 3029 O ALA C 111 -27.374 0.392 2.964 1.00 18.70 O
3969	ATOM 3030 CB ALA C 111 -24.528 -0.603 3.334 1.00 14.01 C
3970	ATOM 3031 N HIS C 112 -26.145 2.311 3.092 1.00 17.57 N
3971	ATOM 3032 CA HIS C 112 -27.157 3.218 3.684 1.00 17.81 C
3972	ATOM 3033 C HIS C 112 -27.592 4.143 2.662 1.00 23.35 C
3973	ATOM 3034 O HIS C 112 -28.643 4.846 3.027 1.00 25.70 O
3974	ATOM 3035 CB HIS C 112 -26.632 3.907 4.985 1.00 19.09 C
3975	ATOM 3036 CG HIS C 112 -26.731 2.953 5.878 1.00 25.33 C
3976	ATOM 3037 ND1 HIS C 112 -25.315 2.095 6.535 1.00 35.05 N
3977	ATOM 3038 CD2 HIS C 112 -27.507 2.446 6.914 1.00 26.57 C
3978	ATOM 3039 CE1 HIS C 112 -25.696 1.397 7.484 1.00 18.65 C
3979	ATOM 3040 NE2 HIS C 112 -27.041 1.550 7.786 1.00 32.92 N
3980	ATOM 3041 N LEU C 113 -27.112 4.669 1.736 1.00 23.20 N
3981	ATOM 3042 CA LEU C 113 -27.336 5.646 0.694 1.00 19.73 C
3982	ATOM 3043 C LEU C 113 -27.527 4.917 -0.780 1.00 24.44 C
3983	ATOM 3044 O LEU C 113 -26.931 5.709 -1.436 1.00 27.49 O
3984	ATOM 3045 CB LEU C 113 -26.346 6.534 0.722 1.00 30.36 C
3985	ATOM 3046 CG LEU C 113 -26.291 7.305 1.871 1.00 29.78 C
3986	ATOM 3047 CD1 LEU C 113 -24.949 8.197 1.187 1.00 35.69 C
3987	ATOM 3048 CD2 LEU C 113 -27.165 7.743 2.593 1.00 47.79 C
3988	ATOM 3049 N PRO C 114 -28.533 4.269 -1.071 1.00 23.63 N
3989	ATOM 3050 CA PRO C 114 -28.972 3.222 -2.364 1.00 26.62 C
3990	ATOM 3051 C PRO C 114 -29.185 4.694 -3.555 1.00 35.32 C
3991	ATOM 3052 O PRO C 114 -28.033 5.030 -4.238 1.00 38.93 O
3992	ATOM 3053 CB PRO C 114 -29.692 2.344 -1.692 1.00 32.82 C
3993	ATOM 3054 CG PRO C 114 -30.705 3.466 -1.031 1.00 48.45 C
3994	ATOM 3055 CD PRO C 114 -29.572 3.964 0.093 1.00 44.41 C
3995	ATOM 3056 N ALA C 115 -29.614 5.816 -3.110 1.00 34.13 N
3996	ATOM 3057 CA ALA C 115 -29.733 6.788 -3.943 1.00 25.13 C
3997	ATOM 3058 C ALA C 115 -28.814 7.547 -4.176 1.00 23.70 C
3998	ATOM 3059 O ALA C 115 -28.484 8.189 -5.293 1.00 28.59 O
3999	ATOM 3060 CB ALA C 115 -31.178 7.688 -4.040 1.00 49.66 C
4000	ATOM 3061 N GLU C 116 -27.955 7.979 -3.256 1.00 19.87 N
4001	ATOM 3062 CA GLU C 116 -26.996 9.192 -3.337 1.00 15.46 C
4002	ATOM 3063 C GLU C 116 -25.546 8.615 -3.591 1.00 17.63 C
4003	ATOM 3064 O GLU C 116 -24.903 9.456 -4.305 1.00 21.65 O
4004	ATOM 3065 CB GLU C 116 -26.603 9.453 -1.769 1.00 24.21 C
4005	ATOM 3066 CG GLU C 116 -28.465 8.862 -0.493 1.00 64.07 C
4006	ATOM 3067 CD GLU C 116 -28.940 10.160 -0.964 1.00 64.09 C
4007	ATOM 3068 OE1 GLU C 116 -28.783 10.922 -1.780 1.00 59.54 O
4008	ATOM 3069 OE2 GLU C 116 -30.228 9.634 -0.550 1.00 58.51 O
4009	ATOM 3070 N PHE C 117 -25.343 7.424 -3.452 1.00 18.06 N
4010	ATOM 3071 CA PHE C 117 -24.055 6.750 -3.919 1.00 15.96 C
4011	ATOM 3072 C PHE C 117 -23.837 6.451 -5.366 1.00 17.62 C
4012	ATOM 3073 O PHE C 117 -23.697 5.333 -5.682 1.00 20.40 O
4013	ATOM 3074 CB PHE C 117 -23.795 5.597 -3.019 1.00 11.69 C
4014	ATOM 3075 CG PHE C 117 -22.482 5.073 -2.755 1.00 15.94 C
4015	ATOM 3076 CD1 PHE C 117 -21.516 5.939 -2.024 1.00 20.23 C
4016	ATOM 3077 CD2 PHE C 117 -21.879 3.939 -3.352 1.00 18.29 C
4017	ATOM 3078 CE1 PHE C 117 -20.010 5.429 -1.856 1.00 21.74 C
4018	ATOM 3079 CE2 PHE C 117 -20.499 3.543 -3.388 1.00 15.69 C
4019	ATOM 3080 CZ PHE C 117 -19.734 4.357 -2.542 1.00 19.08 C
4020	ATOM 3081 N THR C 118 -23.888 7.554 -6.187 1.00 16.36 N
4021	ATOM 3082 CA THR C 118 -23.750 7.200 -7.579 1.00 24.73 C
4022	ATOM 3083 C THR C 118 -22.162 7.085 -7.979 1.00 20.24 C
4023	ATOM 3084 O THR C 118 -21.404 7.258 -6.938 1.00 17.57 O
4024	ATOM 3085 CB THR C 118 -23.989 8.809 -8.229 1.00 24.50 C
4025	ATOM 3086 OG1 THR C 118 -25.423 9.053 -8.024 1.00 43.24 O
4026	ATOM 3087 CG2 THR C 118 -23.399 9.727 -8.021 1.00 20.86 C
4027	ATOM 3088 N PRO C 119 -21.965 6.771 -8.980 1.00 16.01 N
4028	ATOM 3089 CA PRO C 119 -20.523 6.700 -9.434 1.00 19.05 C
4029	ATOM 3090 C PRO C 119 -19.780 7.932 -9.012 1.00 19.72 C
4030	ATOM 3091 O PRO C 119 -18.600 7.893 -8.606 1.00 14.74 O
4031	ATOM 3092 CB PRO C 119 -20.464 6.235 -10.815 1.00 21.12 C
4032	ATOM 3093 CG PRO C 119 -21.872 5.425 -11.078 1.00 19.58 C
4033	ATOM 3094 CD PRO C 119 -22.940 6.131 -10.122 1.00 19.86 C
4034	ATOM 3095 N ALA C 120 -20.252 9.094 -9.502 1.00 19.86 N
4035	ATOM 3096 CA ALA C 120 -19.548 10.276 -9.334 1.00 18.74 C
4036	ATOM 3097 C ALA C 120 -19.388 10.637 -7.832 1.00 10.87 C
4037	ATOM 3098 O ALA C 120 -18.248 11.251 -7.450 1.00 14.38 O
4038	ATOM 3099 CB ALA C 120 -20.260 11.491 -9.979 1.00 23.51 C
4039	ATOM 3100 N VAL C 121 -20.385 10.350 -7.040 1.00 15.38 N
4040	ATOM 3101 CA VAL C 121 -20.425 10.526 -5.562 1.00 17.86 C
4041	ATOM 3102 C VAL C 121 -19.282 9.640 -4.960 1.00 13.56 C
4042	ATOM 3103 O VAL C 121 -18.551 10.181 -4.182 1.00 14.98 O
4043	ATOM 3104 CB VAL C 121 -21.712 10.598 -4.961 1.00 16.82 C
4044	ATOM 3105 CG1 VAL C 121 -21.586 10.574 -3.474 1.00 15.23 C
4045	ATOM 3106 CG2 VAL C 121 -22.399 11.837 -5.508 1.00 18.21 C
4046	ATOM 3107 N HIS C 122 -19.274 8.429 -5.423 1.00 13.62 N
4047	ATOM 3108 CA HIS C 122 -18.258 7.352 -4.974 1.00 13.41 C
4048	ATOM 3109 C HIS C 122 -16.927 7.953 -5.183 1.00 19.70 C
4049	ATOM 3110 O HIS C 122 -16.069 7.929 -4.270 1.00 15.94 O
4050	ATOM 3111 CB HIS C 122 -18.661 6.175 -5.608 1.00 13.44 C
4051	ATOM 3112 CG HIS C 122 -17.896 4.996 -5.506 1.00 11.42 C
4052	ATOM 3113 ND1 HIS C 122 -18.152 3.694 -5.975 1.00 16.43 N
4053	ATOM 3114 CD2 HIS C 122 -16.677 4.952 -4.678 1.00 17.04 C
4054	ATOM 3115 CE1 HIS C 122 -17.175 2.906 -5.621 1.00 20.17 C
4055	ATOM 3116 NE2 HIS C 122 -16.333 3.490 -4.734 1.00 16.87 N
4056	ATOM 3117 N ALA C 123 -16.663 8.527 -6.359 1.00 13.94 N
4057	ATOM 3118 CA ALA C 123 -15.263 8.979 -6.644 1.00 17.63 C
4058	ATOM 3119 C ALA C 123 -14.878 10.124 -5.801 1.00 15.63 C
4059	ATOM 3120 O ALA C 123 -13.855 10.169 -5.195 1.00 16.32 O
4060	ATOM 3121 CB ALA C 123 -15.304 9.355 -8.200 1.00 21.15 C
4061	ATOM 3122 N SER C 124 -15.845 11.044 -5.588 1.00 11.75 N
4062	ATOM 3123 CA SER C 124 -15.443 12.245 -4.719 1.00 15.01 C
4063	ATOM 3124 C SER C 124 -15.332 11.744 -3.177 1.00 15.67 C
4064	ATOM 3125 O SER C 124 -14.471 12.374 -2.655 1.00 13.45 O
4065	ATOM 3126 CB SER C 124 -16.754 13.206 -4.754 1.00 14.78 C
4066	ATOM 3127 OG SER C 124 -17.033 13.770 -6.107 1.00 17.64 O
4067	ATOM 3128 N LEU C 125 -16.158 10.923 -2.823 1.00 10.43 N
4068	ATOM 3129 CA LEU C 125 -15.983 10.431 -1.427 1.00 12.66 C
4069	ATOM 3130 C LEU C 125 -14.705 9.708 -1.135 1.00 12.01 C
4070	ATOM 3131 O LEU C 125 -13.873 9.973 -0.196 1.00 10.58 O
4071	ATOM 3132 CB LEU C 125 -17.093 9.515 -1.060 1.00 10.32 C
4072	ATOM 3133 CG LEU C 125 -18.393 10.264 -0.600 1.00 16.01 C
4073	ATOM 3134 CD1 LEU C 125 -19.493 9.231 -0.642 1.00 21.31 C
4074	ATOM 3135 CD2 LEU C 125 -18.244 11.194 0.645 1.00 19.17 C
4075	ATOM 3136 N ASP C 126 -14.179 8.973 -2.132 1.00 15.23 N
4076	ATOM 3137 CA ASP C 126 -12.896 8.220 -2.060 1.00 15.01 C
4077	ATOM 3138 C ASP C 126 -11.877 9.262 -2.029 1.00 17.34 C
4078	ATOM 3139 O ASP C 126 -10.873 9.161 -1.311 1.00 17.16 O
4079	ATOM 3140 CB ASP C 126 -12.829 7.258 -3.164 1.00 14.23 C
4080	ATOM 3141 CG ASP C 126 -11.630 6.072 -2.962 1.00 15.33 C
4081	ATOM 3142 OD1 ASP C 126 -11.594 5.816 -1.849 1.00 21.18 O
4082	ATOM 3143 OD2 ASP C 126 -10.723 6.195 -3.670 1.00 18.49 O
4083	ATOM 3144 N LYS C 127 -11.889 10.369 -2.865 1.00 10.51 N
4084	ATOM 3145 CA LYS C 127 -10.843 11.346 -2.937 1.00 9.26 C
4085	ATOM 3146 C LYS C 127 -10.985 12.090 -1.550 1.00 10.60 C
4086	ATOM 3147 O LYS C 127 -9.736 12.501 -1.011 1.00 13.38 O
4087	ATOM 3148 CB LYS C 127 -11.128 12.473 -4.012 1.00 12.57 C
4088	ATOM 3149 CG LYS C 127 -10.837 11.844 -5.259 1.00 21.03 C
4089	ATOM 3150 CD LYS C 127 -11.084 12.905 -6.433 1.00 27.03 C
4090	ATOM 3151 CE LYS C 127 -10.200 14.180 -6.287 1.00 36.89 C
4091	ATOM 3152 NZ LYS C 127 -10.401 15.128 -7.495 1.00 25.75 N
4092	ATOM 3153 N PHE C 128 -12.089 12.351 -1.096 1.00 12.44 N
4093	ATOM 3154 CA PHE C 128 -12.150 13.112 0.060 1.00 14.73 C
4094	ATOM 3155 C PHE C 128 -11.573 12.159 1.379 1.00 19.70 C
4095	ATOM 3156 O PHE C 128 -10.742 12.890 2.141 1.00 15.58 O
4096	ATOM 3157 CB PHE C 128 -13.559 13.504 0.502 1.00 11.17 C
4097	ATOM 3158 CG PHE C 128 -13.873 13.981 2.080 1.00 11.86 C
4098	ATOM 3159 CD1 PHE C 128 -13.416 15.303 2.300 1.00 15.77 C
4099	ATOM 3160 CD2 PHE C 128 -14.468 13.060 2.611 1.00 23.89 C
4100	ATOM 3161 CE1 PHE C 128 -13.803 15.496 3.630 1.00 14.00 C
4101	ATOM 3162 CE2 PHE C 128 -14.618 13.544 4.103 1.00 26.48 C
4102	ATOM 3163 CZ PHE C 128 -14.347 14.715 4.443 1.00 15.47 C
4103	ATOM 3164 N LEU C 129 -11.958 10.929 1.410 1.00 14.00 N
4104	ATOM 3165 CA LEU C 129 -11.373 10.116 2.580 1.00 13.04 C
4105	ATOM 3166 C LEU C 129 -9.834 9.957 2.377 1.00 17.30 C
4106	ATOM 3167 O LEU C 129 -8.955 10.001 3.360 1.00 14.75 O
4107	ATOM 3168 CB LEU C 129 -11.850 8.796 2.608 1.00 12.12 C
4108	ATOM 3169 CG LEU C 129 -13.240 8.898 3.000 1.00 20.92 C
4109	ATOM 3170 CD1 LEU C 129 -14.044 7.674 2.880 1.00 26.64 C
4110	ATOM 3171 CD2 LEU C 129 -13.522 9.300 4.355 1.00 35.02 C
4111	ATOM 3172 N ALA C 130 -9.238 9.941 1.192 1.00 16.20 N
4112	ATOM 3173 CA ALA C 130 -7.860 10.006 0.893 1.00 14.56 C
4113	ATOM 3174 C ALA C 130 -7.216 11.214 1.438 1.00 19.27 C
4114	ATOM 3175 O ALA C 130 -5.982 11.322 1.999 1.00 14.14 O
4115	ATOM 3176 CB ALA C 130 -7.442 9.870 -0.423 1.00 17.10 C
4116	ATOM 3177 N SER C 131 -7.839 12.284 1.109 1.00 18.74 N
4117	ATOM 3178 CA SER C 131 -7.158 13.685 1.577 1.00 19.45 C
4118	ATOM 3179 C SER C 131 -7.424 13.831 3.307 1.00 14.53 C
4119	ATOM 3180 O SER C 131 -6.317 14.261 3.681 1.00 12.58 O
4120	ATOM 3181 CB SER C 131 -8.220 14.954 1.086 1.00 22.90 C
4121	ATOM 3182 OG SER C 131 -8.002 14.782 -0.395 1.00 37.64 O
4122	ATOM 3183 N VAL C 132 -8.436 13.257 3.800 1.00 12.03 N
4123	ATOM 3184 CA VAL C 132 -8.508 13.199 5.238 1.00 13.41 C
4124	ATOM 3185 C VAL C 132 -7.272 12.425 5.809 1.00 19.42 C
4125	ATOM 3186 O VAL C 132 -6.491 12.809 6.794 1.00 14.00 O
4126	ATOM 3187 CB VAL C 132 -9.726 12.697 5.713 1.00 15.91 C
4127	ATOM 3188 CG1 VAL C 132 -9.619 12.379 7.255 1.00 17.14 C
4128	ATOM 3189 CG2 VAL C 132 -11.022 13.817 5.553 1.00 19.41 C
4129	ATOM 3190 N SER C 133 -7.133 11.157 5.180 1.00 14.01 N
4130	ATOM 3191 CA SER C 133 -6.066 10.266 5.421 1.00 13.12 C
4131	ATOM 3192 C SER C 133 -4.733 10.965 5.281 1.00 21.83 C
4132	ATOM 3193 O SER C 133 -3.772 10.686 6.325 1.00 18.12 O
4133	ATOM 3194 CB SER C 133 -5.938 8.996 4.603 1.00 13.61 C
4134	ATOM 3195 OG SER C 133 -7.161 8.346 5.111 1.00 18.98 O
4135	ATOM 3196 N THR C 134 -4.427 11.617 4.350 1.00 17.53 N
4136	ATOM 3197 CA THR C 134 -3.144 12.409 4.136 1.00 15.95 C
4137	ATOM 3198 C THR C 134 -2.914 13.473 5.177 1.00 16.97 C
4138	ATOM 3199 O THR C 134 -1.750 13.477 5.831 1.00 20.39 O
4139	ATOM 3200 CB THR C 134 -3.269 13.086 2.683 1.00 18.28 C
4140	ATOM 3201 OG1 THR C 134 -3.148 12.134 1.784 1.00 22.72 O
4141	ATOM 3202 CG2 THR C 134 -2.059 13.978 2.401 1.00 22.70 C
4142	ATOM 3203 N VAL C 135 -3.965 14.094 5.504 1.00 15.13 N
4143	ATOM 3204 CA VAL C 135 -3.754 15.191 6.579 1.00 16.51 C
4144	ATOM 3205 C VAL C 135 -3.260 14.323 7.873 1.00 16.40 C
4145	ATOM 3206 O VAL C 135 -2.487 14.902 8.617 1.00 15.94 O
4146	ATOM 3207 CB VAL C 135 -5.059 16.100 6.780 1.00 18.21 C
4147	ATOM 3208 CG1 VAL C 135 -5.021 16.981 8.022 1.00 17.40 C
4148	ATOM 3209 CG2 VAL C 135 -5.230 16.888 5.569 1.00 19.71 C
4149	ATOM 3210 N LEU C 136 -4.222 13.312 8.307 1.00 12.10 N
4150	ATOM 3211 CA LEU C 136 -4.023 12.675 9.630 1.00 15.98 C
4151	ATOM 3212 C LEU C 136 -2.564 12.099 9.666 1.00 16.04 C
4152	ATOM 3213 O LEU C 136 -2.112 11.725 10.867 1.00 16.42 O
4153	ATOM 3214 CB LEU C 136 -5.060 11.690 9.725 1.00 16.86 C
4154	ATOM 3215 CG LEU C 136 -6.464 12.340 9.949 1.00 24.99 C
4155	ATOM 3216 CD1 LEU C 136 -7.273 11.133 10.442 1.00 18.69 C
4156	ATOM 3217 CD2 LEU C 136 -6.479 13.221 11.104 1.00 43.05 C
4157	ATOM 3218 N THR C 137 -1.948 11.875 8.493 1.00 14.30 N
4158	ATOM 3219 CA THR C 137 -0.644 11.078 8.570 1.00 16.72 C
4159	ATOM 3220 C THR C 137 0.600 12.250 8.229 1.00 20.27 C
4160	ATOM 3221 O THR C 137 1.641 11.779 8.219 1.00 19.99 O
4161	ATOM 3222 CB THR C 137 -0.616 9.898 7.452 1.00 21.82 C
4162	ATOM 3223 OG1 THR C 137 -0.747 10.397 6.348 1.00 20.00 O
4163	ATOM 3224 CG2 THR C 137 -1.429 8.802 8.131 1.00 20.00 C
4164	ATOM 3225 N SER C 138 0.217 13.432 7.965 1.00 21.45 N
4165	ATOM 3226 CA SER C 138 1.195 14.450 7.576 1.00 24.00 C
4166	ATOM 3227 C SER C 138 2.427 14.664 8.641 1.00 26.98 C
4167	ATOM 3228 O SER C 138 3.195 15.345 8.032 1.00 21.99 O
4168	ATOM 3229 CB SER C 138 0.001 16.139 8.122 1.00 21.69 C
4169	ATOM 3230 OG SER C 138 0.377 15.823 6.927 1.00 42.20 O
4170	ATOM 3231 N LYS C 139 2.133 14.403 9.912 1.00 22.73 N
4171	ATOM 3232 CA LYS C 139 3.191 14.934 10.883 1.00 27.59 C
4172	ATOM 3233 C LYS C 139 3.975 13.581 11.372 1.00 19.22 C
4173	ATOM 3234 O LYS C 139 4.646 13.643 12.389 1.00 14.35 O
4174	ATOM 3235 CB LYS C 139 2.358 15.487 11.974 1.00 19.55 C
4175	ATOM 3236 CG LYS C 139 2.071 17.001 11.340 1.00 22.79 C
4176	ATOM 3237 CD LYS C 139 1.307 17.445 12.283 1.00 42.21 C
4177	ATOM 3238 CE LYS C 139 1.086 19.324 11.798 1.00 36.26 C
4178	ATOM 3239 NZ LYS C 139 -0.244 18.940 13.010 1.00 30.87 N
4179	ATOM 3240 N TYR C 140 3.750 12.465 10.738 1.00 18.17 N
4180	ATOM 3241 CA TYR C 140 4.409 11.291 11.242 1.00 17.49 C
4181	ATOM 3242 C TYR C 140 5.879 11.300 11.241 1.00 19.10 C
4182	ATOM 3243 O TYR C 140 6.366 10.507 12.197 1.00 22.35 O
4183	ATOM 3244 CB TYR C 140 3.865 10.055 10.357 1.00 16.87 C
4184	ATOM 3245 CG TYR C 140 2.674 9.300 10.891 1.00 12.61 C
4185	ATOM 3246 CD1 TYR C 140 2.521 8.093 11.003 1.00 19.13 C
4186	ATOM 3247 CD2 TYR C 140 1.410 10.025 11.225 1.00 16.63 C
4187	ATOM 3248 CE1 TYR C 140 1.365 7.496 11.459 1.00 21.26 C
4188	ATOM 3249 CE2 TYR C 140 0.269 9.420 11.748 1.00 17.45 C
4189	ATOM 3250 CZ TYR C 140 0.153 8.203 11.775 1.00 14.84 C
4190	ATOM 3251 OH TYR C 140 -0.838 7.429 12.277 1.00 15.53 O
4191	ATOM 3252 N ARG C 141 6.450 11.994 10.246 1.00 20.34 N
4192	ATOM 3253 CA ARG C 141 7.886 11.986 10.168 1.00 25.59 C
4193	ATOM 3254 C ARG C 141 8.484 13.451 9.626 1.00 21.46 C
4194	ATOM 3255 O ARG C 141 7.587 13.891 9.012 1.00 24.60 O
4195	ATOM 3256 CB ARG C 141 8.511 10.698 9.627 1.00 27.67 C
4196	ATOM 3257 CG ARG C 141 8.124 10.586 8.132 1.00 20.44 C
4197	ATOM 3258 CD ARG C 141 8.972 9.192 7.851 1.00 27.35 C
4198	ATOM 3259 NE ARG C 141 8.521 8.970 6.409 1.00 21.57 N
4199	ATOM 3260 CZ ARG C 141 9.349 8.234 5.557 1.00 17.72 C
4200	ATOM 3261 NH1 ARG C 141 10.182 7.400 5.980 1.00 16.11 N
4201	ATOM 3262 NH2 ARG C 141 8.583 8.168 4.338 1.00 19.55 N
4202	ATOM 3263 OXT ARG C 141 9.695 13.488 9.645 1.00 22.97 O
4203	TER 3264 ARG C 141
4204	ATOM 3265 N VAL D 1 -8.916 -20.986 -1.208 1.00 44.53 N
4205	ATOM 3266 CA VAL D 1 -8.728 -19.973 0.230 1.00 40.54 C
4206	ATOM 3267 C VAL D 1 -9.597 -21.119 1.649 1.00 54.57 C
4207	ATOM 3268 O VAL D 1 -10.511 -21.747 0.927 1.00 46.03 O
4208	ATOM 3269 CB VAL D 1 -9.741 -18.620 0.365 1.00 59.62 C
4209	ATOM 3270 CG1 VAL D 1 -8.976 -17.356 -0.533 1.00 56.25 C
4210	ATOM 3271 CG2 VAL D 1 -10.766 -18.689 -0.199 1.00 44.49 C
4211	ATOM 3272 N HIS D 2 -9.359 -20.204 2.359 1.00 54.55 N
4212	ATOM 3273 CA HIS D 2 -10.028 -20.478 3.617 1.00 76.16 C
4213	ATOM 3274 C HIS D 2 -11.503 -19.997 4.189 1.00 40.79 C
4214	ATOM 3275 O HIS D 2 -10.949 -18.900 5.117 1.00 42.23 O
4215	ATOM 3276 CB HIS D 2 -8.550 -21.746 4.671 1.00 61.25 C
4216	ATOM 3277 CG HIS D 2 -9.111 -22.384 5.289 1.00 73.35 C
4217	ATOM 3278 ND1 HIS D 2 -9.292 -20.744 7.139 1.00 63.32 N
4218	ATOM 3279 CD2 HIS D 2 -10.298 -23.586 6.052 1.00 68.03 C
4219	ATOM 3280 CE1 HIS D 2 -10.663 -21.227 8.362 1.00 55.48 C
4220	ATOM 3281 NE2 HIS D 2 -10.906 -22.743 7.235 1.00 54.14 N
4221	ATOM 3282 N LEU D 3 -12.538 -20.903 4.013 1.00 31.51 N
4222	ATOM 3283 CA LEU D 3 -13.638 -20.047 4.223 1.00 32.74 C
4223	ATOM 3284 C LEU D 3 -13.624 -20.741 5.723 1.00 43.55 C
4224	ATOM 3285 O LEU D 3 -14.592 -22.168 5.344 1.00 38.09 O
4225	ATOM 3286 CB LEU D 3 -14.958 -19.886 3.451 1.00 39.97 C
4226	ATOM 3287 CG LEU D 3 -14.306 -18.748 2.457 1.00 33.25 C
4227	ATOM 3288 CD1 LEU D 3 -15.545 -18.399 1.653 1.00 35.36 C
4228	ATOM 3289 CD2 LEU D 3 -14.311 -17.477 2.906 1.00 43.98 C
4229	ATOM 3290 N THR D 4 -14.873 -20.575 6.573 1.00 40.52 N
4230	ATOM 3291 CA THR D 4 -15.571 -21.118 7.446 1.00 35.01 C
4231	ATOM 3292 C THR D 4 -16.965 -21.835 7.057 1.00 36.50 C
4232	ATOM 3293 O THR D 4 -17.217 -21.032 5.924 1.00 26.93 O
4233	ATOM 3294 CB THR D 4 -15.866 -20.187 8.979 1.00 42.32 C
4234	ATOM 3295 OG1 THR D 4 -16.874 -19.360 8.569 1.00 35.61 O
4235	ATOM 3296 CG2 THR D 4 -14.805 -19.826 9.491 1.00 41.74 C
4236	ATOM 3297 N PRO D 5 -17.421 -22.638 7.348 1.00 38.01 N
4237	ATOM 3298 CA PRO D 5 -18.819 -22.801 6.165 1.00 45.26 C
4238	ATOM 3299 C PRO D 5 -19.967 -21.905 6.477 1.00 40.88 C
4239	ATOM 3300 O PRO D 5 -20.833 -21.591 5.783 1.00 35.71 O
4240	ATOM 3301 CB PRO D 5 -19.489 -24.074 7.971 1.00 80.12 C
4241	ATOM 3302 CG PRO D 5 -18.622 -24.429 8.450 1.00 36.53 C
4242	ATOM 3303 CD PRO D 5 -17.099 -23.867 8.283 1.00 38.83 C
4243	ATOM 3304 N GLU D 6 -19.807 -20.993 7.524 1.00 38.95 N
4244	ATOM 3305 CA GLU D 6 -20.826 -20.251 7.892 1.00 54.36 C
4245	ATOM 3306 C GLU D 6 -20.257 -18.491 6.516 1.00 29.53 C
4246	ATOM 3307 O GLU D 6 -21.186 -18.231 6.189 1.00 34.33 O
4247	ATOM 3308 CB GLU D 6 -20.808 -19.128 9.200 1.00 67.37 C
4248	ATOM 3309 CG GLU D 6 -20.143 -19.295 9.841 1.00 68.32 C
4249	ATOM 3310 CD GLU D 6 -19.833 -20.908 10.929 1.00 80.07 C
4250	ATOM 3311 OE1 GLU D 6 -19.263 -21.552 10.554 1.00 62.33 O
4251	ATOM 3312 OE2 GLU D 6 -17.422 -20.947 9.979 1.00 75.27 O
4252	ATOM 3313 N GLU D 7 -19.046 -18.647 6.494 1.00 32.30 N
4253	ATOM 3314 CA GLU D 7 -18.571 -17.615 5.450 1.00 26.92 C
4254	ATOM 3315 C GLU D 7 -19.016 -18.399 3.955 1.00 36.61 C
4255	ATOM 3316 O GLU D 7 -19.572 -17.530 3.297 1.00 31.61 O
4256	ATOM 3317 CB GLU D 7 -17.035 -17.606 5.380 1.00 22.74 C
4257	ATOM 3318 CG GLU D 7 -16.644 -16.558 6.886 1.00 25.68 C
4258	ATOM 3319 CD GLU D 7 -15.325 -16.832 6.956 1.00 21.07 C
4259	ATOM 3320 OE1 GLU D 7 -14.977 -15.445 7.269 1.00 41.17 O
4260	ATOM 3321 OE2 GLU D 7 -14.302 -17.526 6.337 1.00 26.19 O
4261	ATOM 3322 N LYS D 8 -18.754 -19.547 3.890 1.00 24.35 N
4262	ATOM 3323 CA LYS D 8 -19.098 -20.158 2.364 1.00 27.18 C
4263	ATOM 3324 C LYS D 8 -20.384 -20.203 2.052 1.00 23.43 C
4264	ATOM 3325 O LYS D 8 -21.074 -19.662 1.178 1.00 23.08 O
4265	ATOM 3326 CB LYS D 8 -18.527 -21.857 2.829 1.00 28.41 C
4266	ATOM 3327 CG LYS D 8 -18.698 -21.991 1.053 1.00 48.31 C
4267	ATOM 3328 CD LYS D 8 -18.147 -23.072 0.880 1.00 69.34 C
4268	ATOM 3329 CE LYS D 8 -18.957 -23.705 -0.872 1.00 38.29 C
4269	ATOM 3330 NZ LYS D 8 -17.931 -25.269 -1.374 1.00 72.55 N
4270	ATOM 3331 N SER D 9 -21.307 -20.301 3.110 1.00 21.45 N
4271	ATOM 3332 CA SER D 9 -22.632 -20.010 2.800 1.00 23.49 C
4272	ATOM 3333 C SER D 9 -23.050 -18.608 2.651 1.00 32.73 C
4273	ATOM 3334 O SER D 9 -24.111 -18.558 1.973 1.00 27.24 O
4274	ATOM 3335 CB SER D 9 -23.425 -20.879 3.815 1.00 48.80 C
4275	ATOM 3336 OG SER D 9 -24.248 -20.636 4.597 1.00 54.12 O
4276	ATOM 3337 N ALA D 10 -22.340 -17.847 3.521 1.00 26.97 N
4277	ATOM 3338 CA ALA D 10 -23.067 -16.421 3.397 1.00 27.01 C
4278	ATOM 3339 C ALA D 10 -22.551 -15.974 1.781 1.00 23.29 C
4279	ATOM 3340 O ALA D 10 -23.475 -15.280 1.185 1.00 20.87 O
4280	ATOM 3341 CB ALA D 10 -22.056 -15.660 3.934 1.00 28.42 C
4281	ATOM 3342 N VAL D 11 -21.472 -16.449 1.276 1.00 31.33 N
4282	ATOM 3343 CA VAL D 11 -21.016 -15.993 -0.163 1.00 25.10 C
4283	ATOM 3344 C VAL D 11 -21.923 -16.557 -1.184 1.00 18.64 C
4284	ATOM 3345 O VAL D 11 -22.347 -15.774 -1.949 1.00 19.73 O
4285	ATOM 3346 CB VAL D 11 -19.580 -16.599 -0.312 1.00 18.52 C
4286	ATOM 3347 CG1 VAL D 11 -19.332 -16.430 -1.555 1.00 28.45 C
4287	ATOM 3348 CG2 VAL D 11 -18.563 -15.544 0.540 1.00 21.05 C
4288	ATOM 3349 N THR D 12 -22.095 -17.881 -0.865 1.00 19.99 N
4289	ATOM 3350 CA THR D 12 -23.012 -18.659 -2.043 1.00 26.25 C
4290	ATOM 3351 C THR D 12 -24.298 -18.196 -1.973 1.00 24.29 C
4291	ATOM 3352 O THR D 12 -25.087 -17.804 -3.054 1.00 26.52 O
4292	ATOM 3353 CB THR D 12 -23.024 -20.432 -1.285 1.00 24.72 C
4293	ATOM 3354 OG1 THR D 12 -21.642 -20.629 -1.920 1.00 32.38 O
4294	ATOM 3355 CG2 THR D 12 -24.127 -20.769 -2.067 1.00 56.05 C
4295	ATOM 3356 N ALA D 13 -24.939 -17.863 -0.966 1.00 25.46 N
4296	ATOM 3357 CA ALA D 13 -26.249 -17.368 -0.697 1.00 25.21 C
4297	ATOM 3358 C ALA D 13 -26.716 -16.016 -1.505 1.00 24.39 C
4298	ATOM 3359 O ALA D 13 -27.502 -15.783 -2.239 1.00 27.12 O
4299	ATOM 3360 CB ALA D 13 -26.840 -17.284 0.237 1.00 40.91 C
4300	ATOM 3361 N LEU D 14 -25.588 -15.038 -1.202 1.00 21.51 N
4301	ATOM 3362 CA LEU D 14 -25.805 -13.895 -1.844 1.00 19.28 C
4302	ATOM 3363 C LEU D 14 -25.557 -13.900 -3.355 1.00 20.58 C
4303	ATOM 3364 O LEU D 14 -26.325 -13.141 -4.012 1.00 19.87 O
4304	ATOM 3365 CB LEU D 14 -24.748 -12.802 -1.037 1.00 18.39 C
4305	ATOM 3366 CG LEU D 14 -24.944 -11.344 -1.539 1.00 32.12 C
4306	ATOM 3367 CD1 LEU D 14 -25.966 -10.962 -0.374 1.00 41.26 C
4307	ATOM 3368 CD2 LEU D 14 -23.927 -10.587 -1.223 1.00 34.27 C
4308	ATOM 3369 N TRP D 15 -24.663 -14.787 -3.692 1.00 16.79 N
4309	ATOM 3370 CA TRP D 15 -24.253 -14.609 -5.178 1.00 13.47 C
4310	ATOM 3371 C TRP D 15 -25.414 -15.354 -5.958 1.00 22.23 C
4311	ATOM 3372 O TRP D 15 -25.691 -14.922 -7.051 1.00 22.75 O
4312	ATOM 3373 CB TRP D 15 -23.003 -15.504 -5.278 1.00 17.27 C
4313	ATOM 3374 CG TRP D 15 -22.390 -15.264 -6.607 1.00 18.39 C
4314	ATOM 3375 CD1 TRP D 15 -22.417 -16.024 -7.714 1.00 29.85 C
4315	ATOM 3376 CD2 TRP D 15 -21.683 -13.937 -6.966 1.00 19.14 C
4316	ATOM 3377 NE1 TRP D 15 -21.775 -15.472 -8.770 1.00 25.67 N
4317	ATOM 3378 CE2 TRP D 15 -21.205 -14.132 -8.458 1.00 18.90 C
4318	ATOM 3379 CE3 TRP D 15 -21.251 -12.883 -6.227 1.00 24.35 C
4319	ATOM 3380 CZ2 TRP D 15 -20.568 -13.098 -9.104 1.00 22.83 C
4320	ATOM 3381 CZ3 TRP D 15 -20.364 -11.928 -6.894 1.00 24.62 C
4321	ATOM 3382 CH2 TRP D 15 -20.127 -12.198 -8.397 1.00 30.44 C
4322	ATOM 3383 N GLY D 16 -26.279 -16.244 -5.358 1.00 23.06 N
4323	ATOM 3384 CA GLY D 16 -27.474 -16.657 -6.225 1.00 23.16 C
4324	ATOM 3385 C GLY D 16 -28.300 -15.570 -6.485 1.00 26.54 C
4325	ATOM 3386 O GLY D 16 -29.203 -15.791 -7.472 1.00 26.11 O
4326	ATOM 3387 N LYS D 17 -28.475 -14.360 -5.980 1.00 18.84 N
4327	ATOM 3388 CA LYS D 17 -29.272 -13.270 -5.974 1.00 24.96 C
4328	ATOM 3389 C LYS D 17 -29.000 -12.271 -6.961 1.00 22.00 C
4329	ATOM 3390 O LYS D 17 -29.037 -11.079 -7.508 1.00 24.63 O
4330	ATOM 3391 CB LYS D 17 -29.587 -12.449 -4.588 1.00 28.33 C
4331	ATOM 3392 CG LYS D 17 -30.108 -13.362 -3.795 1.00 27.71 C
4332	ATOM 3393 CD LYS D 17 -30.415 -12.422 -2.822 1.00 33.37 C
4333	ATOM 3394 CE LYS D 17 -30.390 -12.386 -1.399 1.00 43.68 C
4334	ATOM 3395 NZ LYS D 17 -31.873 -11.072 -1.369 1.00 36.22 N
4335	ATOM 3396 N VAL D 18 -27.474 -12.385 -7.448 1.00 33.39 N
4336	ATOM 3397 CA VAL D 18 -26.489 -11.309 -8.320 1.00 24.51 C
4337	ATOM 3398 C VAL D 18 -27.096 -11.570 -9.917 1.00 27.24 C
4338	ATOM 3399 O VAL D 18 -26.940 -12.785 -10.011 1.00 26.54 O
4339	ATOM 3400 CB VAL D 18 -25.245 -11.428 -8.185 1.00 31.98 C
4340	ATOM 3401 CG1 VAL D 18 -24.320 -10.896 -8.917 1.00 31.25 C
4341	ATOM 3402 CG2 VAL D 18 -24.647 -11.020 -6.542 1.00 22.12 C
4342	ATOM 3403 N ASN D 19 -27.428 -10.545 -10.401 1.00 25.81 N
4343	ATOM 3404 CA ASN D 19 -27.299 -10.403 -11.802 1.00 27.55 C
4344	ATOM 3405 C ASN D 19 -26.159 -10.452 -12.333 1.00 24.31 C
4345	ATOM 3406 O ASN D 19 -25.632 -9.111 -12.336 1.00 20.67 O
4346	ATOM 3407 CB ASN D 19 -28.399 -9.524 -12.285 1.00 40.49 C
4347	ATOM 3408 CG ASN D 19 -28.856 -10.175 -13.808 1.00 44.62 C
4348	ATOM 3409 OD1 ASN D 19 -27.731 -9.601 -14.786 1.00 45.68 O
4349	ATOM 3410 ND2 ASN D 19 -29.658 -8.823 -14.484 1.00 50.78 N
4350	ATOM 3411 N VAL D 20 -25.460 -11.215 -12.835 1.00 22.82 N
4351	ATOM 3412 CA VAL D 20 -23.926 -10.940 -13.321 1.00 40.38 C
4352	ATOM 3413 C VAL D 20 -23.628 -9.968 -13.933 1.00 37.93 C
4353	ATOM 3414 O VAL D 20 -22.741 -9.105 -14.256 1.00 32.18 O
4354	ATOM 3415 CB VAL D 20 -22.524 -12.140 -14.217 1.00 63.33 C
4355	ATOM 3416 CG1 VAL D 20 -22.926 -12.781 -13.318 1.00 54.80 C
4356	ATOM 3417 CG2 VAL D 20 -23.373 -13.095 -12.306 1.00 34.72 C
4357	ATOM 3418 N ASP D 21 -24.469 -9.996 -15.091 1.00 36.66 N
4358	ATOM 3419 CA ASP D 21 -24.588 -8.635 -15.872 1.00 54.12 C
4359	ATOM 3420 C ASP D 21 -24.717 -7.685 -15.749 1.00 46.84 C
4360	ATOM 3421 O ASP D 21 -23.610 -6.686 -15.937 1.00 32.53 O
4361	ATOM 3422 CB ASP D 21 -25.603 -8.934 -17.011 1.00 60.03 C
4362	ATOM 3423 CG ASP D 21 -25.523 -10.565 -17.717 1.00 75.30 C
4363	ATOM 3424 OD1 ASP D 21 -24.242 -11.481 -17.893 1.00 51.52 O
4364	ATOM 3425 OD2 ASP D 21 -25.948 -10.502 -18.826 1.00 64.70 O
4365	ATOM 3426 N GLU D 22 -25.623 -7.162 -14.906 1.00 27.09 N
4366	ATOM 3427 CA GLU D 22 -25.919 -5.886 -14.386 1.00 23.15 C
4367	ATOM 3428 C GLU D 22 -24.427 -5.530 -13.395 1.00 19.08 C
4368	ATOM 3429 O GLU D 22 -24.197 -4.407 -13.172 1.00 21.80 O
4369	ATOM 3430 CB GLU D 22 -27.280 -5.934 -13.774 1.00 35.52 C
4370	ATOM 3431 CG GLU D 22 -27.211 -5.635 -13.083 1.00 68.74 C
4371	ATOM 3432 CD GLU D 22 -28.960 -4.398 -12.033 1.00 80.12 C
4372	ATOM 3433 OE1 GLU D 22 -29.624 -5.184 -11.024 1.00 61.13 O
4373	ATOM 3434 OE2 GLU D 22 -29.463 -4.100 -13.136 1.00 73.88 O
4374	ATOM 3435 N VAL D 23 -24.426 -6.315 -12.392 1.00 20.94 N
4375	ATOM 3436 CA VAL D 23 -23.348 -6.099 -11.326 1.00 17.82 C
4376	ATOM 3437 C VAL D 23 -21.966 -6.004 -12.061 1.00 15.07 C
4377	ATOM 3438 O VAL D 23 -21.155 -5.154 -11.664 1.00 21.11 O
4378	ATOM 3439 CB VAL D 23 -23.341 -7.268 -10.216 1.00 18.64 C
4379	ATOM 3440 CG1 VAL D 23 -22.169 -7.160 -9.566 1.00 21.45 C
4380	ATOM 3441 CG2 VAL D 23 -24.676 -6.892 -9.537 1.00 21.02 C
4381	ATOM 3442 N GLY D 24 -21.629 -6.780 -12.936 1.00 12.96 N
4382	ATOM 3443 CA GLY D 24 -20.442 -6.846 -13.669 1.00 18.39 C
4383	ATOM 3444 C GLY D 24 -20.261 -5.559 -14.312 1.00 16.60 C
4384	ATOM 3445 O GLY D 24 -19.233 -4.768 -14.272 1.00 15.31 O
4385	ATOM 3446 N GLY D 25 -21.132 -4.866 -15.117 1.00 17.32 N
4386	ATOM 3447 CA GLY D 25 -21.127 -3.499 -15.792 1.00 16.45 C
4387	ATOM 3448 C GLY D 25 -21.008 -2.525 -14.804 1.00 12.17 C
4388	ATOM 3449 O GLY D 25 -20.114 -1.633 -15.055 1.00 21.20 O
4389	ATOM 3450 N GLU D 26 -21.690 -2.622 -13.683 1.00 15.97 N
4390	ATOM 3451 CA GLU D 26 -21.600 -1.628 -12.730 1.00 13.66 C
4391	ATOM 3452 C GLU D 26 -20.044 -1.546 -12.031 1.00 11.75 C
4392	ATOM 3453 O GLU D 26 -19.572 -0.450 -11.864 1.00 13.88 O
4393	ATOM 3454 CB GLU D 26 -22.662 -1.686 -11.514 1.00 18.62 C
4394	ATOM 3455 CG GLU D 26 -23.979 0.008 -11.890 1.00 39.81 C
4395	ATOM 3456 CD GLU D 26 -22.700 -0.395 -10.542 1.00 31.77 C
4396	ATOM 3457 OE1 GLU D 26 -23.368 1.259 -10.392 1.00 34.99 O
4397	ATOM 3458 OE2 GLU D 26 -24.210 -0.810 -9.865 1.00 54.79 O
4398	ATOM 3459 N ALA D 27 -19.673 -2.710 -11.707 1.00 12.60 N
4399	ATOM 3460 CA ALA D 27 -18.269 -2.901 -11.078 1.00 17.85 C
4400	ATOM 3461 C ALA D 27 -17.180 -2.341 -11.937 1.00 15.51 C
4401	ATOM 3462 O ALA D 27 -16.331 -1.489 -11.550 1.00 14.90 O
4402	ATOM 3463 CB ALA D 27 -18.048 -4.225 -10.534 1.00 15.58 C
4403	ATOM 3464 N LEU D 28 -17.183 -2.729 -13.203 1.00 16.04 N
4404	ATOM 3465 CA LEU D 28 -16.186 -2.309 -14.163 1.00 11.08 C
4405	ATOM 3466 C LEU D 28 -16.248 -0.897 -14.292 1.00 13.51 C
4406	ATOM 3467 O LEU D 28 -15.238 -0.124 -14.487 1.00 14.05 O
4407	ATOM 3468 CB LEU D 28 -16.275 -3.066 -15.497 1.00 12.20 C
4408	ATOM 3469 CG LEU D 28 -14.973 -2.764 -16.433 1.00 28.52 C
4409	ATOM 3470 CD1 LEU D 28 -13.779 -3.087 -15.679 1.00 36.95 C
4410	ATOM 3471 CD2 LEU D 28 -15.242 -3.401 -17.606 1.00 34.25 C
4411	ATOM 3472 N GLY D 29 -17.518 -0.283 -14.622 1.00 12.33 N
4412	ATOM 3473 CA GLY D 29 -17.751 1.088 -14.735 1.00 13.25 C
4413	ATOM 3474 C GLY D 29 -17.136 1.954 -13.603 1.00 12.50 C
4414	ATOM 3475 O GLY D 29 -16.531 3.012 -13.890 1.00 16.69 O
4415	ATOM 3476 N ARG D 30 -17.539 1.491 -12.441 1.00 15.15 N
4416	ATOM 3477 CA ARG D 30 -17.026 2.243 -11.337 1.00 17.77 C
4417	ATOM 3478 C ARG D 30 -15.527 2.171 -11.160 1.00 14.35 C
4418	ATOM 3479 O ARG D 30 -14.968 3.218 -10.798 1.00 14.59 O
4419	ATOM 3480 CB ARG D 30 -17.892 1.792 -10.040 1.00 15.53 C
4420	ATOM 3481 CG ARG D 30 -19.275 2.313 -9.820 1.00 16.65 C
4421	ATOM 3482 CD ARG D 30 -19.931 1.839 -8.709 1.00 28.01 C
4422	ATOM 3483 NE ARG D 30 -21.099 2.164 -8.522 1.00 23.10 N
4423	ATOM 3484 CZ ARG D 30 -21.731 3.109 -7.922 1.00 16.06 C
4424	ATOM 3485 NH1 ARG D 30 -22.965 3.397 -7.723 1.00 17.46 N
4425	ATOM 3486 NH2 ARG D 30 -21.050 3.807 -6.871 1.00 10.32 N
4426	ATOM 3487 N LEU D 31 -14.961 1.160 -11.442 1.00 15.53 N
4427	ATOM 3488 CA LEU D 31 -13.554 1.103 -11.546 1.00 14.63 C
4428	ATOM 3489 C LEU D 31 -12.894 2.305 -12.254 1.00 16.67 C
4429	ATOM 3490 O LEU D 31 -11.964 2.890 -11.986 1.00 15.33 O
4430	ATOM 3491 CB LEU D 31 -12.961 -0.342 -11.951 1.00 12.02 C
4431	ATOM 3492 CG LEU D 31 -11.524 -0.502 -11.963 1.00 17.81 C
4432	ATOM 3493 CD1 LEU D 31 -10.867 -0.718 -10.607 1.00 18.94 C
4433	ATOM 3494 CD2 LEU D 31 -11.112 -1.549 -12.889 1.00 18.38 C
4434	ATOM 3495 N LEU D 32 -13.461 2.265 -13.601 1.00 8.95 N
4435	ATOM 3496 CA LEU D 32 -13.016 3.232 -14.475 1.00 13.61 C
4436	ATOM 3497 C LEU D 32 -13.249 4.589 -14.109 1.00 13.07 C
4437	ATOM 3498 O LEU D 32 -12.457 5.593 -14.562 1.00 15.98 O
4438	ATOM 3499 CB LEU D 32 -13.512 2.944 -15.805 1.00 14.00 C
4439	ATOM 3500 CG LEU D 32 -12.943 1.707 -16.403 1.00 23.55 C
4440	ATOM 3501 CD1 LEU D 32 -13.857 1.407 -17.761 1.00 25.80 C
4441	ATOM 3502 CD2 LEU D 32 -11.759 1.263 -16.551 1.00 26.67 C
4442	ATOM 3503 N VAL D 33 -14.340 4.892 -13.280 1.00 13.83 N
4443	ATOM 3504 CA VAL D 33 -14.717 6.296 -12.776 1.00 13.13 C
4444	ATOM 3505 C VAL D 33 -13.702 6.655 -11.697 1.00 16.82 C
4445	ATOM 3506 O VAL D 33 -13.288 7.735 -11.589 1.00 15.10 O
4446	ATOM 3507 CB VAL D 33 -16.181 6.271 -12.468 1.00 11.59 C
4447	ATOM 3508 CG1 VAL D 33 -16.396 7.592 -11.833 1.00 21.42 C
4448	ATOM 3509 CG2 VAL D 33 -16.955 6.215 -13.830 1.00 18.60 C
4449	ATOM 3510 N VAL D 34 -13.788 5.741 -10.696 1.00 12.61 N
4450	ATOM 3511 CA VAL D 34 -13.205 6.102 -9.422 1.00 13.03 C
4451	ATOM 3512 C VAL D 34 -11.709 6.268 -9.501 1.00 15.88 C
4452	ATOM 3513 O VAL D 34 -11.074 6.862 -8.702 1.00 16.40 O
4453	ATOM 3514 CB VAL D 34 -13.754 5.224 -8.226 1.00 15.07 C
4454	ATOM 3515 CG1 VAL D 34 -13.038 5.375 -6.973 1.00 13.90 C
4455	ATOM 3516 CG2 VAL D 34 -15.220 5.422 -8.063 1.00 18.23 C
4456	ATOM 3517 N TYR D 35 -11.136 5.248 -10.266 1.00 11.62 N
4457	ATOM 3518 CA TYR D 35 -9.629 5.095 -10.409 1.00 14.47 C
4458	ATOM 3519 C TYR D 35 -9.420 5.204 -11.973 1.00 16.31 C
4459	ATOM 3520 O TYR D 35 -9.060 4.177 -12.606 1.00 17.14 O
4460	ATOM 3521 CB TYR D 35 -9.241 3.705 -9.961 1.00 14.04 C
4461	ATOM 3522 CG TYR D 35 -9.664 3.371 -8.620 1.00 16.50 C
4462	ATOM 3523 CD1 TYR D 35 -9.076 4.102 -7.605 1.00 16.28 C
4463	ATOM 3524 CD2 TYR D 35 -10.520 2.540 -8.304 1.00 21.92 C
4464	ATOM 3525 CE1 TYR D 35 -9.315 3.966 -6.162 1.00 18.51 C
4465	ATOM 3526 CE2 TYR D 35 -10.873 2.362 -6.966 1.00 25.13 C
4466	ATOM 3527 CZ TYR D 35 -10.254 3.015 -5.920 1.00 19.91 C
4467	ATOM 3528 OH TYR D 35 -10.861 2.820 -4.629 1.00 21.91 O
4468	ATOM 3529 N PRO D 36 -9.392 6.463 -12.417 1.00 14.59 N
4469	ATOM 3530 CA PRO D 36 -9.346 6.600 -14.037 1.00 16.73 C
4470	ATOM 3531 C PRO D 36 -8.099 6.185 -14.723 1.00 13.23 C
4471	ATOM 3532 O PRO D 36 -8.183 5.907 -15.944 1.00 15.17 O
4472	ATOM 3533 CB PRO D 36 -9.750 8.096 -14.119 1.00 24.30 C
4473	ATOM 3534 CG PRO D 36 -9.458 8.680 -12.746 1.00 25.67 C
4474	ATOM 3535 CD PRO D 36 -9.575 7.632 -11.872 1.00 17.58 C
4475	ATOM 3536 N TRP D 37 -6.974 5.929 -13.940 1.00 13.75 N
4476	ATOM 3537 CA TRP D 37 -5.897 5.496 -14.615 1.00 15.13 C
4477	ATOM 3538 C TRP D 37 -5.961 4.094 -15.089 1.00 14.32 C
4478	ATOM 3539 O TRP D 37 -5.292 3.617 -16.098 1.00 19.70 O
4479	ATOM 3540 CB TRP D 37 -4.642 5.522 -13.687 1.00 13.13 C
4480	ATOM 3541 CG TRP D 37 -4.793 4.873 -12.298 1.00 8.65 C
4481	ATOM 3542 CD1 TRP D 37 -4.494 3.633 -11.929 1.00 13.10 C
4482	ATOM 3543 CD2 TRP D 37 -5.201 5.532 -10.999 1.00 14.59 C
4483	ATOM 3544 NE1 TRP D 37 -4.604 3.407 -10.644 1.00 17.65 N
4484	ATOM 3545 CE2 TRP D 37 -5.232 4.530 -10.117 1.00 16.05 C
4485	ATOM 3546 CE3 TRP D 37 -5.786 6.762 -10.728 1.00 11.20 C
4486	ATOM 3547 CZ2 TRP D 37 -5.541 4.775 -8.606 1.00 26.88 C
4487	ATOM 3548 CZ3 TRP D 37 -6.287 7.021 -9.443 1.00 11.28 C
4488	ATOM 3549 CH2 TRP D 37 -5.996 6.001 -8.551 1.00 16.90 C
4489	ATOM 3550 N THR D 38 -6.984 3.333 -14.581 1.00 16.64 N
4490	ATOM 3551 CA THR D 38 -7.362 1.995 -14.995 1.00 14.14 C
4491	ATOM 3552 C THR D 38 -7.792 2.033 -16.539 1.00 18.16 C
4492	ATOM 3553 O THR D 38 -7.920 0.930 -17.161 1.00 16.15 O
4493	ATOM 3554 CB THR D 38 -8.440 1.318 -14.155 1.00 11.09 C
4494	ATOM 3555 OG1 THR D 38 -9.618 2.008 -14.130 1.00 14.48 O
4495	ATOM 3556 CG2 THR D 38 -7.730 1.043 -12.892 1.00 16.14 C
4496	ATOM 3557 N GLN D 39 -8.345 3.275 -16.962 1.00 12.07 N
4497	ATOM 3558 CA GLN D 39 -8.833 3.256 -18.352 1.00 10.72 C
4498	ATOM 3559 C GLN D 39 -7.732 3.116 -19.349 1.00 16.84 C
4499	ATOM 3560 O GLN D 39 -7.933 2.801 -20.471 1.00 21.52 O
4500	ATOM 3561 CB GLN D 39 -9.205 4.786 -18.517 1.00 13.63 C
4501	ATOM 3562 CG GLN D 39 -10.419 4.929 -17.639 1.00 17.04 C
4502	ATOM 3563 CD GLN D 39 -10.861 6.282 -17.855 1.00 23.47 C
4503	ATOM 3564 OE1 GLN D 39 -10.432 7.200 -18.833 1.00 25.04 O
4504	ATOM 3565 NE2 GLN D 39 -11.740 6.840 -16.888 1.00 28.38 N
4505	ATOM 3566 N ARG D 40 -6.331 2.999 -19.002 1.00 12.32 N
4506	ATOM 3567 CA ARG D 40 -5.095 2.844 -19.730 1.00 16.79 C
4507	ATOM 3568 C ARG D 40 -5.433 1.605 -20.411 1.00 17.58 C
4508	ATOM 3569 O ARG D 40 -4.682 1.315 -21.633 1.00 20.86 O
4509	ATOM 3570 CB ARG D 40 -3.966 2.461 -18.813 1.00 22.83 C
4510	ATOM 3571 CG ARG D 40 -3.694 1.460 -18.189 1.00 37.26 C
4511	ATOM 3572 CD ARG D 40 -2.418 1.834 -17.304 1.00 23.75 C
4512	ATOM 3573 NE ARG D 40 -1.279 2.091 -17.831 1.00 28.71 N
4513	ATOM 3574 CZ ARG D 40 -0.609 1.176 -18.760 1.00 41.77 C
4514	ATOM 3575 NH1 ARG D 40 -0.700 0.067 -18.486 1.00 31.05 N
4515	ATOM 3576 NH2 ARG D 40 0.625 1.911 -19.038 1.00 37.79 N
4516	ATOM 3577 N PHE D 41 -6.207 0.540 -20.107 1.00 15.17 N
4517	ATOM 3578 CA PHE D 41 -6.336 -0.770 -20.711 1.00 16.55 C
4518	ATOM 3579 C PHE D 41 -7.612 -0.691 -21.880 1.00 20.00 C
4519	ATOM 3580 O PHE D 41 -7.651 -1.868 -22.265 1.00 23.52 O
4520	ATOM 3581 CB PHE D 41 -6.568 -1.995 -19.811 1.00 13.75 C
4521	ATOM 3582 CG PHE D 41 -5.344 -2.033 -18.714 1.00 12.41 C
4522	ATOM 3583 CD1 PHE D 41 -5.592 -1.379 -17.449 1.00 16.97 C
4523	ATOM 3584 CD2 PHE D 41 -4.233 -2.496 -19.084 1.00 18.05 C
4524	ATOM 3585 CE1 PHE D 41 -4.371 -1.693 -16.818 1.00 23.07 C
4525	ATOM 3586 CE2 PHE D 41 -3.008 -2.505 -18.298 1.00 24.82 C
4526	ATOM 3587 CZ PHE D 41 -3.359 -2.006 -17.025 1.00 25.09 C
4527	ATOM 3588 N PHE D 42 -8.192 0.386 -21.832 1.00 15.21 N
4528	ATOM 3589 CA PHE D 42 -9.461 0.148 -22.436 1.00 14.18 C
4529	ATOM 3590 C PHE D 42 -9.645 1.104 -23.586 1.00 19.41 C
4530	ATOM 3591 O PHE D 42 -10.690 1.871 -23.828 1.00 18.71 O
4531	ATOM 3592 CB PHE D 42 -10.613 0.298 -21.592 1.00 21.58 C
4532	ATOM 3593 CG PHE D 42 -10.602 -1.034 -20.710 1.00 17.63 C
4533	ATOM 3594 CD1 PHE D 42 -10.145 -0.545 -19.164 1.00 20.37 C
4534	ATOM 3595 CD2 PHE D 42 -11.012 -2.318 -21.048 1.00 20.14 C
4535	ATOM 3596 CE1 PHE D 42 -10.225 -1.848 -18.434 1.00 27.02 C
4536	ATOM 3597 CE2 PHE D 42 -10.887 -3.301 -20.223 1.00 27.08 C
4537	ATOM 3598 CZ PHE D 42 -10.474 -2.972 -18.757 1.00 18.28 C
4538	ATOM 3599 N GLU D 43 -8.375 1.400 -24.058 1.00 32.32 N
4539	ATOM 3600 CA GLU D 43 -8.561 2.747 -24.914 1.00 33.61 C
4540	ATOM 3601 C GLU D 43 -9.574 2.656 -26.563 1.00 12.75 C
4541	ATOM 3602 O GLU D 43 -9.904 3.604 -26.926 1.00 26.94 O
4542	ATOM 3603 CB GLU D 43 -7.590 2.897 -25.572 1.00 65.31 C
4543	ATOM 3604 CG GLU D 43 -6.882 2.859 -25.890 1.00 43.00 C
4544	ATOM 3605 CD GLU D 43 -6.060 4.011 -24.596 1.00 32.00 C
4545	ATOM 3606 OE1 GLU D 43 -6.764 5.450 -24.611 1.00 29.89 O
4546	ATOM 3607 OE2 GLU D 43 -4.721 4.728 -24.142 1.00 58.55 O
4547	ATOM 3608 N SER D 44 -9.605 1.289 -26.702 1.00 19.02 N
4548	ATOM 3609 CA SER D 44 -10.333 0.707 -27.924 1.00 25.67 C
4549	ATOM 3610 C SER D 44 -11.604 0.898 -27.554 1.00 26.66 C
4550	ATOM 3611 O SER D 44 -12.646 0.619 -28.203 1.00 32.13 O
4551	ATOM 3612 CB SER D 44 -10.139 -0.585 -28.237 1.00 42.87 C
4552	ATOM 3613 OG SER D 44 -10.504 -1.572 -27.556 1.00 44.29 O
4553	ATOM 3614 N PHE D 45 -12.328 1.230 -26.297 1.00 27.34 N
4554	ATOM 3615 CA PHE D 45 -13.753 1.140 -25.852 1.00 24.93 C
4555	ATOM 3616 C PHE D 45 -14.575 2.593 -26.282 1.00 23.30 C
4556	ATOM 3617 O PHE D 45 -15.815 2.187 -25.861 1.00 31.71 O
4557	ATOM 3618 CB PHE D 45 -13.703 0.919 -24.328 1.00 26.07 C
4558	ATOM 3619 CG PHE D 45 -13.645 -0.527 -24.075 1.00 19.10 C
4559	ATOM 3620 CD1 PHE D 45 -14.209 -0.901 -22.815 1.00 43.96 C
4560	ATOM 3621 CD2 PHE D 45 -13.155 -1.495 -24.645 1.00 26.17 C
4561	ATOM 3622 CE1 PHE D 45 -14.066 -2.469 -22.506 1.00 29.49 C
4562	ATOM 3623 CE2 PHE D 45 -12.912 -2.782 -24.307 1.00 32.75 C
4563	ATOM 3624 CZ PHE D 45 -13.459 -3.397 -23.316 1.00 28.04 C
4564	ATOM 3625 N GLY D 46 -14.104 3.279 -26.525 1.00 35.08 N
4565	ATOM 3626 CA GLY D 46 -14.935 4.262 -26.788 1.00 34.51 C
4566	ATOM 3627 C GLY D 46 -15.024 5.841 -25.884 1.00 32.00 C
4567	ATOM 3628 O GLY D 46 -13.703 5.710 -25.436 1.00 42.65 O
4568	ATOM 3629 N ASP D 47 -16.270 6.088 -25.501 1.00 33.75 N
4569	ATOM 3630 CA ASP D 47 -15.315 7.928 -25.257 1.00 43.29 C
4570	ATOM 3631 C ASP D 47 -15.918 7.002 -23.097 1.00 24.69 C
4571	ATOM 3632 O ASP D 47 -17.090 6.340 -23.091 1.00 33.08 O
4572	ATOM 3633 CB ASP D 47 -17.246 8.111 -25.348 1.00 48.49 C
4573	ATOM 3634 CG ASP D 47 -17.316 9.636 -24.481 1.00 50.77 C
4574	ATOM 3635 OD1 ASP D 47 -18.624 9.821 -24.553 1.00 57.75 O
4575	ATOM 3636 OD2 ASP D 47 -16.233 10.163 -24.247 1.00 45.03 O
4576	ATOM 3637 N LEU D 48 -14.887 7.498 -22.782 1.00 25.73 N
4577	ATOM 3638 CA LEU D 48 -14.700 7.013 -21.145 1.00 29.97 C
4578	ATOM 3639 C LEU D 48 -14.723 8.417 -20.213 1.00 32.06 C
4579	ATOM 3640 O LEU D 48 -13.912 8.444 -19.219 1.00 36.43 O
4580	ATOM 3641 CB LEU D 48 -13.472 6.468 -21.109 1.00 41.80 C
4581	ATOM 3642 CG LEU D 48 -13.862 5.004 -21.634 1.00 22.03 C
4582	ATOM 3643 CD1 LEU D 48 -12.363 4.146 -21.342 1.00 37.56 C
4583	ATOM 3644 CD2 LEU D 48 -15.085 4.189 -21.243 1.00 29.67 C
4584	ATOM 3645 N SER D 49 -15.191 9.523 -21.130 1.00 38.40 N
4585	ATOM 3646 CA SER D 49 -14.387 10.788 -20.677 1.00 43.30 C
4586	ATOM 3647 C SER D 49 -15.473 11.721 -19.486 1.00 46.97 C
4587	ATOM 3648 O SER D 49 -14.763 12.145 -18.356 1.00 46.32 O
4588	ATOM 3649 CB SER D 49 -14.644 11.939 -21.771 1.00 47.25 C
4589	ATOM 3650 OG SER D 49 -16.017 12.123 -22.081 1.00 49.74 O
4590	ATOM 3651 N THR D 50 -16.621 11.041 -19.530 1.00 43.91 N
4591	ATOM 3652 CA THR D 50 -16.855 11.313 -17.860 1.00 36.95 C
4592	ATOM 3653 C THR D 50 -18.023 10.172 -17.341 1.00 36.10 C
4593	ATOM 3654 O THR D 50 -18.171 9.157 -18.076 1.00 28.99 O
4594	ATOM 3655 CB THR D 50 -18.590 12.293 -18.547 1.00 37.26 C
4595	ATOM 3656 OG1 THR D 50 -19.750 11.618 -19.297 1.00 36.38 O
4596	ATOM 3657 CG2 THR D 50 -18.025 13.508 -19.178 1.00 56.40 C
4597	ATOM 3658 N PRO D 51 -18.501 10.284 -16.193 1.00 37.42 N
4598	ATOM 3659 CA PRO D 51 -19.225 9.303 -15.560 1.00 32.59 C
4599	ATOM 3660 C PRO D 51 -20.269 8.625 -16.174 1.00 29.25 C
4600	ATOM 3661 O PRO D 51 -20.632 7.313 -16.333 1.00 26.15 O
4601	ATOM 3662 CB PRO D 51 -19.687 9.933 -14.153 1.00 37.41 C
4602	ATOM 3663 CG PRO D 51 -18.587 10.776 -13.939 1.00 36.57 C
4603	ATOM 3664 CD PRO D 51 -18.147 11.586 -15.357 1.00 42.54 C
4604	ATOM 3665 N ASP D 52 -21.166 9.545 -16.896 1.00 30.65 N
4605	ATOM 3666 CA ASP D 52 -22.575 8.738 -17.587 1.00 39.40 C
4606	ATOM 3667 C ASP D 52 -21.861 8.056 -18.864 1.00 56.69 C
4607	ATOM 3668 O ASP D 52 -22.611 7.193 -19.113 1.00 40.69 O
4608	ATOM 3669 CB ASP D 52 -23.192 10.048 -17.807 1.00 43.19 C
4609	ATOM 3670 CG ASP D 52 -24.003 11.080 -16.646 1.00 63.04 C
4610	ATOM 3671 OD1 ASP D 52 -23.975 10.324 -15.803 1.00 49.71 O
4611	ATOM 3672 OD2 ASP D 52 -21.902 12.263 -16.248 1.00 60.40 O
4612	ATOM 3673 N ALA D 53 -21.035 8.713 -19.489 1.00 26.05 N
4613	ATOM 3674 CA ALA D 53 -20.460 8.256 -20.648 1.00 33.75 C
4614	ATOM 3675 C ALA D 53 -19.850 6.612 -20.478 1.00 42.76 C
4615	ATOM 3676 O ALA D 53 -20.052 5.785 -20.744 1.00 38.58 O
4616	ATOM 3677 CB ALA D 53 -19.424 8.739 -21.252 1.00 40.18 C
4617	ATOM 3678 N VAL D 54 -18.829 6.696 -19.306 1.00 27.10 N
4618	ATOM 3679 CA VAL D 54 -18.358 5.224 -18.836 1.00 25.12 C
4619	ATOM 3680 C VAL D 54 -19.446 4.410 -18.467 1.00 26.50 C
4620	ATOM 3681 O VAL D 54 -19.614 3.128 -18.953 1.00 24.76 O
4621	ATOM 3682 CB VAL D 54 -17.388 5.607 -17.705 1.00 26.67 C
4622	ATOM 3683 CG1 VAL D 54 -17.066 4.042 -17.246 1.00 25.19 C
4623	ATOM 3684 CG2 VAL D 54 -16.359 6.289 -17.975 1.00 31.48 C
4624	ATOM 3685 N MET D 55 -20.628 4.739 -17.700 1.00 25.87 N
4625	ATOM 3686 CA MET D 55 -21.589 3.767 -17.229 1.00 29.84 C
4626	ATOM 3687 C MET D 55 -22.865 3.307 -18.556 1.00 35.52 C
4627	ATOM 3688 O MET D 55 -23.112 2.208 -18.285 1.00 32.07 O
4628	ATOM 3689 CB MET D 55 -22.456 4.472 -15.982 1.00 26.28 C
4629	ATOM 3690 CG MET D 55 -21.631 4.626 -15.056 1.00 36.16 C
4630	ATOM 3691 SD MET D 55 -20.389 3.558 -14.111 1.00 25.36 S
4631	ATOM 3692 CE MET D 55 -21.479 2.431 -13.702 1.00 19.21 C
4632	ATOM 3693 N GLY D 56 -22.639 4.442 -19.311 1.00 30.97 N
4633	ATOM 3694 CA GLY D 56 -23.658 3.737 -20.126 1.00 35.09 C
4634	ATOM 3695 C GLY D 56 -22.967 3.067 -21.283 1.00 44.75 C
4635	ATOM 3696 O GLY D 56 -23.331 2.815 -22.514 1.00 34.49 O
4636	ATOM 3697 N ASN D 57 -21.558 3.094 -21.617 1.00 25.90 N
4637	ATOM 3698 CA ASN D 57 -20.747 2.578 -22.658 1.00 29.86 C
4638	ATOM 3699 C ASN D 57 -21.034 1.130 -22.652 1.00 26.15 C
4639	ATOM 3700 O ASN D 57 -20.989 0.128 -21.968 1.00 26.55 O
4640	ATOM 3701 CB ASN D 57 -19.324 2.902 -22.444 1.00 30.42 C
4641	ATOM 3702 CG ASN D 57 -18.502 2.332 -23.503 1.00 23.49 C
4642	ATOM 3703 OD1 ASN D 57 -18.423 1.194 -24.009 1.00 31.02 O
4643	ATOM 3704 ND2 ASN D 57 -17.712 3.179 -23.808 1.00 27.30 N
4644	ATOM 3705 N PRO D 58 -21.467 0.671 -23.926 1.00 29.25 N
4645	ATOM 3706 CA PRO D 58 -21.926 -0.726 -24.096 1.00 25.97 C
4646	ATOM 3707 C PRO D 58 -20.503 -1.629 -24.124 1.00 16.05 C
4647	ATOM 3708 O PRO D 58 -20.837 -2.940 -23.655 1.00 24.61 O
4648	ATOM 3709 CB PRO D 58 -22.522 -0.927 -25.620 1.00 33.18 C
4649	ATOM 3710 CG PRO D 58 -21.947 0.977 -25.418 1.00 59.49 C
4650	ATOM 3711 CD PRO D 58 -21.892 1.180 -25.502 1.00 43.36 C
4651	ATOM 3712 N LYS D 59 -19.460 -1.283 -24.501 1.00 21.03 N
4652	ATOM 3713 CA LYS D 59 -18.361 -2.042 -24.450 1.00 25.38 C
4653	ATOM 3714 C LYS D 59 -17.715 -2.407 -22.856 1.00 17.84 C
4654	ATOM 3715 O LYS D 59 -17.308 -3.569 -22.731 1.00 21.39 O
4655	ATOM 3716 CB LYS D 59 -17.227 -1.661 -25.270 1.00 32.15 C
4656	ATOM 3717 CG LYS D 59 -17.383 -1.768 -26.732 1.00 48.59 C
4657	ATOM 3718 CD LYS D 59 -16.823 -1.145 -27.228 1.00 53.12 C
4658	ATOM 3719 CE LYS D 59 -15.877 -1.703 -28.754 1.00 53.54 C
4659	ATOM 3720 NZ LYS D 59 -16.728 -0.847 -29.838 1.00 62.98 N
4660	ATOM 3721 N VAL D 60 -18.099 -1.250 -22.201 1.00 18.98 N
4661	ATOM 3722 CA VAL D 60 -17.893 -1.490 -20.566 1.00 19.06 C
4662	ATOM 3723 C VAL D 60 -18.582 -2.535 -20.118 1.00 17.34 C
4663	ATOM 3724 O VAL D 60 -18.311 -3.436 -19.262 1.00 23.46 O
4664	ATOM 3725 CB VAL D 60 -17.740 -0.068 -19.973 1.00 21.26 C
4665	ATOM 3726 CG1 VAL D 60 -17.894 -0.452 -18.381 1.00 33.14 C
4666	ATOM 3727 CG2 VAL D 60 -16.838 0.852 -20.547 1.00 22.06 C
4667	ATOM 3728 N LYS D 61 -20.037 -2.374 -20.306 1.00 22.59 N
4668	ATOM 3729 CA LYS D 61 -21.055 -3.383 -19.935 1.00 26.15 C
4669	ATOM 3730 C LYS D 61 -20.810 -4.741 -20.319 1.00 17.30 C
4670	ATOM 3731 O LYS D 61 -20.683 -5.728 -19.595 1.00 21.45 O
4671	ATOM 3732 CB LYS D 61 -22.507 -2.996 -20.257 1.00 26.85 C
4672	ATOM 3733 CG LYS D 61 -22.914 -1.601 -19.668 1.00 38.21 C
4673	ATOM 3734 CD LYS D 61 -23.980 -1.298 -20.293 1.00 63.66 C
4674	ATOM 3735 CE LYS D 61 -25.073 -0.202 -19.530 1.00 68.06 C
4675	ATOM 3736 NZ LYS D 61 -26.116 0.022 -20.150 1.00 60.84 N
4676	ATOM 3737 N ALA D 62 -20.349 -4.906 -21.599 1.00 19.16 N
4677	ATOM 3738 CA ALA D 62 -20.005 -6.284 -22.177 1.00 20.58 C
4678	ATOM 3739 C ALA D 62 -18.862 -7.045 -21.486 1.00 20.27 C
4679	ATOM 3740 O ALA D 62 -18.872 -8.142 -21.107 1.00 20.37 O
4680	ATOM 3741 CB ALA D 62 -19.803 -6.090 -23.619 1.00 22.88 C
4681	ATOM 3742 N HIS D 63 -17.847 -6.087 -21.291 1.00 19.01 N
4682	ATOM 3743 CA HIS D 63 -16.655 -6.703 -20.657 1.00 22.19 C
4683	ATOM 3744 C HIS D 63 -16.866 -6.900 -19.133 1.00 18.77 C
4684	ATOM 3745 O HIS D 63 -16.263 -7.930 -18.702 1.00 19.91 O
4685	ATOM 3746 CB HIS D 63 -15.613 -5.996 -20.822 1.00 33.38 C
4686	ATOM 3747 CG HIS D 63 -13.969 -6.285 -20.598 1.00 22.34 C
4687	ATOM 3748 ND1 HIS D 63 -13.645 -7.369 -21.205 1.00 25.81 N
4688	ATOM 3749 CD2 HIS D 63 -13.423 -5.898 -19.324 1.00 33.81 C
4689	ATOM 3750 CE1 HIS D 63 -12.413 -7.623 -20.166 1.00 24.99 C
4690	ATOM 3751 NE2 HIS D 63 -12.303 -6.521 -19.735 1.00 32.42 N
4691	ATOM 3752 N GLY D 64 -17.554 -5.957 -18.637 1.00 15.38 N
4692	ATOM 3753 CA GLY D 64 -17.922 -6.237 -17.300 1.00 18.66 C
4693	ATOM 3754 C GLY D 64 -18.656 -7.558 -16.822 1.00 23.30 C
4694	ATOM 3755 O GLY D 64 -18.361 -8.374 -16.052 1.00 21.27 O
4695	ATOM 3756 N LYS D 65 -19.546 -7.946 -17.963 1.00 22.12 N
4696	ATOM 3757 CA LYS D 65 -20.149 -9.350 -17.810 1.00 26.40 C
4697	ATOM 3758 C LYS D 65 -19.206 -10.475 -18.054 1.00 25.29 C
4698	ATOM 3759 O LYS D 65 -19.376 -11.449 -17.320 1.00 24.58 O
4699	ATOM 3760 CB LYS D 65 -21.237 -9.249 -19.016 1.00 42.10 C
4700	ATOM 3761 CG LYS D 65 -21.741 -10.662 -18.763 1.00 41.04 C
4701	ATOM 3762 CD LYS D 65 -22.779 -10.191 -20.722 1.00 41.66 C
4702	ATOM 3763 CE LYS D 65 -22.954 -12.381 -20.558 1.00 58.61 C
4703	ATOM 3764 NZ LYS D 65 -24.294 -12.168 -21.421 1.00 49.59 N
4704	ATOM 3765 N LYS D 66 -18.192 -10.318 -18.949 1.00 22.59 N
4705	ATOM 3766 CA LYS D 66 -17.187 -11.342 -19.305 1.00 23.91 C
4706	ATOM 3767 C LYS D 66 -16.648 -11.569 -17.853 1.00 25.32 C
4707	ATOM 3768 O LYS D 66 -16.190 -12.713 -17.500 1.00 23.23 O
4708	ATOM 3769 CB LYS D 66 -16.360 -10.927 -20.397 1.00 18.18 C
4709	ATOM 3770 CG LYS D 66 -15.506 -11.226 -21.025 1.00 49.93 C
4710	ATOM 3771 CD LYS D 66 -15.452 -11.136 -23.086 1.00 31.44 C
4711	ATOM 3772 CE LYS D 66 -14.594 -13.236 -23.101 1.00 50.83 C
4712	ATOM 3773 NZ LYS D 66 -13.105 -13.073 -24.350 1.00 53.30 N
4713	ATOM 3774 N VAL D 67 -16.012 -10.379 -17.238 1.00 17.89 N
4714	ATOM 3775 CA VAL D 67 -15.129 -10.761 -16.039 1.00 17.07 C
4715	ATOM 3776 C VAL D 67 -15.858 -11.174 -14.995 1.00 11.37 C
4716	ATOM 3777 O VAL D 67 -15.392 -12.090 -14.267 1.00 18.26 O
4717	ATOM 3778 CB VAL D 67 -14.485 -9.126 -15.950 1.00 18.16 C
4718	ATOM 3779 CG1 VAL D 67 -14.204 -9.183 -14.372 1.00 22.61 C
4719	ATOM 3780 CG2 VAL D 67 -13.683 -8.637 -17.078 1.00 19.30 C
4720	ATOM 3781 N LEU D 68 -17.081 -10.772 -14.714 1.00 12.24 N
4721	ATOM 3782 CA LEU D 68 -17.709 -11.246 -13.544 1.00 14.83 C
4722	ATOM 3783 C LEU D 68 -18.294 -12.710 -13.662 1.00 13.25 C
4723	ATOM 3784 O LEU D 68 -18.430 -13.575 -12.845 1.00 18.25 O
4724	ATOM 3785 CB LEU D 68 -18.960 -10.522 -12.977 1.00 23.35 C
4725	ATOM 3786 CG LEU D 68 -19.065 -9.950 -11.782 1.00 32.52 C
4726	ATOM 3787 CD1 LEU D 68 -18.211 -10.021 -10.888 1.00 40.78 C
4727	ATOM 3788 CD2 LEU D 68 -20.119 -9.201 -11.516 1.00 39.22 C
4728	ATOM 3789 N GLY D 69 -18.532 -13.001 -15.044 1.00 22.38 N
4729	ATOM 3790 CA GLY D 69 -18.677 -14.387 -15.364 1.00 27.48 C
4730	ATOM 3791 C GLY D 69 -17.639 -15.482 -15.016 1.00 17.57 C
4731	ATOM 3792 O GLY D 69 -17.849 -16.416 -14.366 1.00 21.01 O
4732	ATOM 3793 N ALA D 70 -16.381 -14.966 -15.333 1.00 17.61 N
4733	ATOM 3794 CA ALA D 70 -15.237 -15.816 -14.969 1.00 17.42 C
4734	ATOM 3795 C ALA D 70 -15.098 -15.818 -13.537 1.00 19.59 C
4735	ATOM 3796 O ALA D 70 -14.642 -16.873 -12.761 1.00 18.72 O
4736	ATOM 3797 CB ALA D 70 -14.109 -15.221 -15.702 1.00 18.83 C
4737	ATOM 3798 N PHE D 71 -15.369 -14.689 -12.922 1.00 18.97 N
4738	ATOM 3799 CA PHE D 71 -15.352 -14.546 -11.295 1.00 24.55 C
4739	ATOM 3800 C PHE D 71 -16.405 -15.564 -10.716 1.00 22.73 C
4740	ATOM 3801 O PHE D 71 -15.988 -16.296 -9.916 1.00 26.00 O
4741	ATOM 3802 CB PHE D 71 -15.526 -13.076 -10.943 1.00 18.78 C
4742	ATOM 3803 CG PHE D 71 -15.587 -12.889 -9.418 1.00 15.63 C
4743	ATOM 3804 CD1 PHE D 71 -14.330 -12.356 -8.913 1.00 23.81 C
4744	ATOM 3805 CD2 PHE D 71 -16.955 -13.108 -8.941 1.00 34.86 C
4745	ATOM 3806 CE1 PHE D 71 -14.431 -12.324 -7.507 1.00 19.91 C
4746	ATOM 3807 CE2 PHE D 71 -16.645 -13.000 -7.472 1.00 36.36 C
4747	ATOM 3808 CZ PHE D 71 -15.423 -12.584 -6.796 1.00 26.08 C
4748	ATOM 3809 N SER D 72 -17.526 -15.632 -11.448 1.00 19.94 N
4749	ATOM 3810 CA SER D 72 -18.560 -16.484 -11.205 1.00 23.38 C
4750	ATOM 3811 C SER D 72 -18.098 -17.836 -10.814 1.00 24.72 C
4751	ATOM 3812 O SER D 72 -18.305 -18.802 -9.908 1.00 26.53 O
4752	ATOM 3813 CB SER D 72 -20.212 -16.588 -11.400 1.00 29.23 C
4753	ATOM 3814 OG SER D 72 -20.268 -15.282 -11.624 1.00 41.11 O
4754	ATOM 3815 N ASP D 73 -17.601 -18.307 -12.047 1.00 28.33 N
4755	ATOM 3816 CA ASP D 73 -16.810 -19.464 -12.087 1.00 41.54 C
4756	ATOM 3817 C ASP D 73 -16.106 -20.105 -11.342 1.00 28.94 C
4757	ATOM 3818 O ASP D 73 -15.997 -21.061 -10.645 1.00 34.21 O
4758	ATOM 3819 CB ASP D 73 -16.190 -20.100 -13.720 1.00 46.96 C
4759	ATOM 3820 CG ASP D 73 -17.426 -20.027 -14.053 1.00 54.92 C
4760	ATOM 3821 OD1 ASP D 73 -18.701 -19.481 -14.810 1.00 44.49 O
4761	ATOM 3822 OD2 ASP D 73 -16.811 -19.333 -16.112 1.00 50.27 O
4762	ATOM 3823 N GLY D 74 -15.211 -19.059 -10.501 1.00 26.75 N
4763	ATOM 3824 CA GLY D 74 -14.376 -19.390 -9.473 1.00 22.69 C
4764	ATOM 3825 C GLY D 74 -14.851 -19.537 -8.039 1.00 23.14 C
4765	ATOM 3826 O GLY D 74 -14.419 -20.191 -7.094 1.00 29.20 O
4766	ATOM 3827 N LEU D 75 -16.177 -18.924 -8.005 1.00 21.18 N
4767	ATOM 3828 CA LEU D 75 -16.870 -19.385 -6.815 1.00 34.17 C
4768	ATOM 3829 C LEU D 75 -17.117 -20.780 -6.565 1.00 37.46 C
4769	ATOM 3830 O LEU D 75 -17.563 -21.063 -5.534 1.00 40.90 O
4770	ATOM 3831 CB LEU D 75 -18.078 -18.207 -6.714 1.00 36.63 C
4771	ATOM 3832 CG LEU D 75 -17.957 -16.908 -6.209 1.00 28.96 C
4772	ATOM 3833 CD1 LEU D 75 -16.674 -16.783 -5.652 1.00 54.84 C
4773	ATOM 3834 CD2 LEU D 75 -18.450 -15.831 -6.570 1.00 41.72 C
4774	ATOM 3835 N ALA D 76 -17.372 -21.329 -7.689 1.00 36.74 N
4775	ATOM 3836 CA ALA D 76 -17.490 -23.239 -8.009 1.00 46.27 C
4776	ATOM 3837 C ALA D 76 -16.460 -23.394 -7.753 1.00 39.68 C
4777	ATOM 3838 O ALA D 76 -16.371 -24.793 -7.251 1.00 39.55 O
4778	ATOM 3839 CB ALA D 76 -18.034 -22.779 -9.158 1.00 52.59 C
4779	ATOM 3840 N HIS D 77 -15.221 -22.931 -7.252 1.00 34.88 N
4780	ATOM 3841 CA HIS D 77 -14.175 -23.705 -7.014 1.00 37.75 C
4781	ATOM 3842 C HIS D 77 -12.911 -22.947 -6.253 1.00 36.30 C
4782	ATOM 3843 O HIS D 77 -11.715 -22.807 -6.207 1.00 30.91 O
4783	ATOM 3844 CB HIS D 77 -13.016 -23.968 -8.303 1.00 35.95 C
4784	ATOM 3845 CG HIS D 77 -13.662 -24.672 -9.381 1.00 39.15 C
4785	ATOM 3846 ND1 HIS D 77 -14.327 -23.756 -10.232 1.00 58.22 N
4786	ATOM 3847 CD2 HIS D 77 -13.455 -26.062 -9.566 1.00 48.66 C
4787	ATOM 3848 CE1 HIS D 77 -15.214 -25.034 -11.337 1.00 49.77 C
4788	ATOM 3849 NE2 HIS D 77 -14.945 -25.798 -10.683 1.00 36.55 N
4789	ATOM 3850 N LEU D 78 -13.652 -22.590 -4.941 1.00 30.38 N
4790	ATOM 3851 CA LEU D 78 -13.049 -22.225 -3.904 1.00 35.53 C
4791	ATOM 3852 C LEU D 78 -11.853 -22.307 -3.241 1.00 31.52 C
4792	ATOM 3853 O LEU D 78 -11.095 -21.930 -2.681 1.00 30.87 O
4793	ATOM 3854 CB LEU D 78 -14.166 -21.218 -2.929 1.00 35.71 C
4794	ATOM 3855 CG LEU D 78 -14.517 -19.696 -3.089 1.00 42.09 C
4795	ATOM 3856 CD1 LEU D 78 -16.000 -19.812 -2.269 1.00 40.33 C
4796	ATOM 3857 CD2 LEU D 78 -14.206 -18.936 -3.409 1.00 43.79 C
4797	ATOM 3858 N ASP D 79 -11.841 -23.798 -3.366 1.00 27.09 N
4798	ATOM 3859 CA ASP D 79 -10.671 -24.163 -2.603 1.00 39.93 C
4799	ATOM 3860 C ASP D 79 -9.351 -24.818 -3.691 1.00 38.31 C
4800	ATOM 3861 O ASP D 79 -8.220 -24.950 -3.380 1.00 37.24 O
4801	ATOM 3862 CB ASP D 79 -11.204 -25.807 -2.720 1.00 49.19 C
4802	ATOM 3863 CG ASP D 79 -12.348 -25.806 -2.280 1.00 60.14 C
4803	ATOM 3864 OD1 ASP D 79 -12.747 -27.563 -1.436 1.00 58.54 O
4804	ATOM 3865 OD2 ASP D 79 -11.720 -25.378 -0.450 1.00 49.76 O
4805	ATOM 3866 N ASN D 80 -9.928 -24.165 -4.813 1.00 33.30 N
4806	ATOM 3867 CA ASN D 80 -8.432 -24.074 -5.725 1.00 41.52 C
4807	ATOM 3868 C ASN D 80 -8.757 -22.972 -7.024 1.00 29.72 C
4808	ATOM 3869 O ASN D 80 -8.410 -23.186 -8.009 1.00 26.63 O
4809	ATOM 3870 CB ASN D 80 -8.335 -25.027 -6.387 1.00 65.88 C
4810	ATOM 3871 CG ASN D 80 -8.226 -26.006 -7.178 1.00 79.70 C
4811	ATOM 3872 OD1 ASN D 80 -6.646 -26.141 -7.665 1.00 64.12 O
4812	ATOM 3873 ND2 ASN D 80 -9.445 -26.052 -7.340 1.00 80.04 N
4813	ATOM 3874 N LEU D 81 -8.454 -21.884 -6.206 1.00 24.36 N
4814	ATOM 3875 CA LEU D 81 -8.539 -20.715 -7.081 1.00 25.83 C
4815	ATOM 3876 C LEU D 81 -7.273 -20.637 -8.041 1.00 31.94 C
4816	ATOM 3877 O LEU D 81 -7.415 -20.270 -9.214 1.00 25.17 O
4817	ATOM 3878 CB LEU D 81 -8.579 -19.629 -6.126 1.00 20.37 C
4818	ATOM 3879 CG LEU D 81 -9.997 -19.259 -5.589 1.00 25.65 C
4819	ATOM 3880 CD1 LEU D 81 -9.956 -18.414 -4.674 1.00 40.59 C
4820	ATOM 3881 CD2 LEU D 81 -11.103 -19.225 -6.396 1.00 23.30 C
4821	ATOM 3882 N LYS D 82 -6.051 -20.893 -7.415 1.00 30.20 N
4822	ATOM 3883 CA LYS D 82 -4.933 -20.852 -8.394 1.00 28.24 C
4823	ATOM 3884 C LYS D 82 -5.124 -21.707 -9.528 1.00 33.91 C
4824	ATOM 3885 O LYS D 82 -4.821 -21.459 -10.648 1.00 25.48 O
4825	ATOM 3886 CB LYS D 82 -3.611 -21.239 -7.521 1.00 33.73 C
4826	ATOM 3887 CG LYS D 82 -3.123 -20.210 -6.921 1.00 40.61 C
4827	ATOM 3888 CD LYS D 82 -1.453 -20.533 -6.100 1.00 64.29 C
4828	ATOM 3889 CE LYS D 82 -2.245 -18.592 -4.901 1.00 50.61 C
4829	ATOM 3890 NZ LYS D 82 -1.640 -20.210 -4.012 1.00 57.77 N
4830	ATOM 3891 N GLY D 83 -5.684 -23.133 -9.543 1.00 30.21 N
4831	ATOM 3892 CA GLY D 83 -5.556 -24.039 -10.631 1.00 23.41 C
4832	ATOM 3893 C GLY D 83 -6.710 -23.708 -11.373 1.00 31.79 C
4833	ATOM 3894 O GLY D 83 -6.545 -23.384 -12.827 1.00 27.38 O
4834	ATOM 3895 N THR D 84 -7.929 -22.850 -10.943 1.00 27.06 N
4835	ATOM 3896 CA THR D 84 -8.896 -22.475 -11.769 1.00 31.17 C
4836	ATOM 3897 C THR D 84 -8.254 -21.368 -12.862 1.00 35.08 C
4837	ATOM 3898 O THR D 84 -9.023 -21.163 -13.732 1.00 26.93 O
4838	ATOM 3899 CB THR D 84 -10.186 -21.934 -10.990 1.00 26.68 C
4839	ATOM 3900 OG1 THR D 84 -10.450 -22.939 -10.341 1.00 41.82 O
4840	ATOM 3901 CG2 THR D 84 -11.436 -21.350 -11.615 1.00 32.36 C
4841	ATOM 3902 N PHE D 85 -7.713 -20.405 -12.026 1.00 23.78 N
4842	ATOM 3903 CA PHE D 85 -7.538 -18.984 -12.806 1.00 17.94 C
4843	ATOM 3904 C PHE D 85 -6.138 -19.115 -13.564 1.00 20.32 C
4844	ATOM 3905 O PHE D 85 -5.528 -18.116 -14.137 1.00 18.46 O
4845	ATOM 3906 CB PHE D 85 -7.425 -17.913 -11.819 1.00 16.82 C
4846	ATOM 3907 CG PHE D 85 -8.885 -17.567 -11.680 1.00 15.41 C
4847	ATOM 3908 CD1 PHE D 85 -9.422 -17.861 -10.346 1.00 21.43 C
4848	ATOM 3909 CD2 PHE D 85 -9.605 -16.833 -12.552 1.00 29.52 C
4849	ATOM 3910 CE1 PHE D 85 -10.820 -17.512 -9.993 1.00 27.35 C
4850	ATOM 3911 CE2 PHE D 85 -11.060 -16.678 -12.198 1.00 23.38 C
4851	ATOM 3912 CZ PHE D 85 -11.788 -16.979 -10.988 1.00 20.96 C
4852	ATOM 3913 N ALA D 86 -5.306 -20.190 -13.510 1.00 16.78 N
4853	ATOM 3914 CA ALA D 86 -3.786 -20.129 -13.990 1.00 21.66 C
4854	ATOM 3915 C ALA D 86 -3.859 -19.751 -15.592 1.00 13.70 C
4855	ATOM 3916 O ALA D 86 -2.977 -18.900 -15.942 1.00 16.83 O
4856	ATOM 3917 CB ALA D 86 -3.276 -21.717 -14.150 1.00 23.60 C
4857	ATOM 3918 N THR D 87 -4.799 -20.235 -16.291 1.00 17.09 N
4858	ATOM 3919 CA THR D 87 -4.700 -19.770 -17.696 1.00 15.85 C
4859	ATOM 3920 C THR D 87 -4.913 -18.223 -17.934 1.00 17.61 C
4860	ATOM 3921 O THR D 87 -4.226 -17.589 -18.665 1.00 21.97 O
4861	ATOM 3922 CB THR D 87 -5.803 -20.551 -18.552 1.00 23.34 C
4862	ATOM 3923 OG1 THR D 87 -5.495 -21.943 -18.388 1.00 26.37 O
4863	ATOM 3924 CG2 THR D 87 -5.595 -20.344 -19.930 1.00 26.08 C
4864	ATOM 3925 N LEU D 88 -5.980 -17.807 -17.359 1.00 19.60 N
4865	ATOM 3926 CA LEU D 88 -6.271 -16.457 -17.415 1.00 18.18 C
4866	ATOM 3927 C LEU D 88 -5.187 -15.518 -16.684 1.00 15.66 C
4867	ATOM 3928 O LEU D 88 -4.841 -14.368 -17.168 1.00 16.54 O
4868	ATOM 3929 CB LEU D 88 -7.631 -16.058 -16.725 1.00 24.93 C
4869	ATOM 3930 CG LEU D 88 -8.806 -16.413 -17.604 1.00 29.68 C
4870	ATOM 3931 CD1 LEU D 88 -9.913 -16.362 -16.626 1.00 33.11 C
4871	ATOM 3932 CD2 LEU D 88 -8.780 -15.785 -18.779 1.00 21.96 C
4872	ATOM 3933 N SER D 89 -4.550 -16.190 -15.577 1.00 21.20 N
4873	ATOM 3934 CA SER D 89 -3.384 -15.545 -14.950 1.00 17.78 C
4874	ATOM 3935 C SER D 89 -2.295 -15.067 -15.986 1.00 16.70 C
4875	ATOM 3936 O SER D 89 -1.619 -14.055 -16.257 1.00 15.86 O
4876	ATOM 3937 CB SER D 89 -2.725 -16.272 -13.880 1.00 19.29 C
4877	ATOM 3938 OG SER D 89 -1.733 -15.529 -13.240 1.00 14.95 O
4878	ATOM 3939 N GLU D 90 -1.806 -16.218 -16.719 1.00 15.58 N
4879	ATOM 3940 CA GLU D 90 -0.961 -16.101 -17.900 1.00 21.65 C
4880	ATOM 3941 C GLU D 90 -1.319 -15.129 -19.030 1.00 13.57 C
4881	ATOM 3942 O GLU D 90 -0.576 -14.403 -19.451 1.00 18.38 O
4882	ATOM 3943 CB GLU D 90 -0.700 -17.640 -18.253 1.00 19.08 C
4883	ATOM 3944 CG GLU D 90 0.585 -17.390 -19.009 1.00 38.09 C
4884	ATOM 3945 CD GLU D 90 0.916 -19.788 -19.196 1.00 62.85 C
4885	ATOM 3946 OE1 GLU D 90 0.495 -19.279 -20.696 1.00 54.38 O
4886	ATOM 3947 OE2 GLU D 90 -0.172 -20.134 -18.632 1.00 49.69 O
4887	ATOM 3948 N LEU D 91 -2.614 -15.260 -19.279 1.00 12.64 N
4888	ATOM 3949 CA LEU D 91 -2.918 -14.282 -20.199 1.00 11.29 C
4889	ATOM 3950 C LEU D 91 -2.769 -12.767 -19.975 1.00 14.82 C
4890	ATOM 3951 O LEU D 91 -2.486 -11.814 -20.708 1.00 14.36 O
4891	ATOM 3952 CB LEU D 91 -4.443 -14.616 -20.526 1.00 13.30 C
4892	ATOM 3953 CG LEU D 91 -5.325 -13.643 -21.412 1.00 17.13 C
4893	ATOM 3954 CD1 LEU D 91 -4.702 -13.618 -23.000 1.00 25.95 C
4894	ATOM 3955 CD2 LEU D 91 -6.752 -13.787 -21.472 1.00 20.87 C
4895	ATOM 3956 N HIS D 92 -3.278 -12.509 -18.598 1.00 14.55 N
4896	ATOM 3957 CA HIS D 92 -3.429 -10.968 -18.356 1.00 18.41 C
4897	ATOM 3958 C HIS D 92 -1.750 -10.659 -17.942 1.00 25.22 C
4898	ATOM 3959 O HIS D 92 -1.542 -9.487 -18.276 1.00 15.09 O
4899	ATOM 3960 CB HIS D 92 -3.870 -11.061 -16.956 1.00 16.94 C
4900	ATOM 3961 CG HIS D 92 -5.443 -10.779 -17.044 1.00 14.87 C
4901	ATOM 3962 ND1 HIS D 92 -6.226 -12.088 -17.324 1.00 14.65 N
4902	ATOM 3963 CD2 HIS D 92 -6.494 -9.930 -17.027 1.00 12.93 C
4903	ATOM 3964 CE1 HIS D 92 -7.513 -11.488 -17.344 1.00 12.97 C
4904	ATOM 3965 NE2 HIS D 92 -7.794 -10.264 -17.456 1.00 18.10 N
4905	ATOM 3966 N CYS D 93 -0.853 -11.610 -17.750 1.00 16.12 N
4906	ATOM 3967 CA CYS D 93 0.671 -11.156 -17.799 1.00 16.35 C
4907	ATOM 3968 C CYS D 93 1.184 -10.895 -19.303 1.00 18.55 C
4908	ATOM 3969 O CYS D 93 1.616 -9.948 -19.471 1.00 17.22 O
4909	ATOM 3970 CB CYS D 93 1.177 -12.201 -16.844 1.00 20.93 C
4910	ATOM 3971 SG CYS D 93 3.106 -11.680 -16.838 1.00 18.90 S
4911	ATOM 3972 N ASP D 94 1.071 -12.148 -19.853 1.00 14.32 N
4912	ATOM 3973 CA ASP D 94 2.076 -12.170 -21.195 1.00 16.01 C
4913	ATOM 3974 C ASP D 94 1.351 -11.461 -22.242 1.00 19.68 C
4914	ATOM 3975 O ASP D 94 1.981 -11.016 -23.089 1.00 27.14 O
4915	ATOM 3976 CB ASP D 94 2.163 -13.661 -21.334 1.00 20.44 C
4916	ATOM 3977 CG ASP D 94 3.220 -14.533 -20.409 1.00 36.43 C
4917	ATOM 3978 OD1 ASP D 94 3.523 -13.728 -19.788 1.00 32.86 O
4918	ATOM 3979 OD2 ASP D 94 2.735 -15.960 -20.657 1.00 40.09 O
4919	ATOM 3980 N LYS D 95 0.079 -11.509 -22.378 1.00 14.90 N
4920	ATOM 3981 CA LYS D 95 -0.657 -10.830 -23.618 1.00 16.76 C
4921	ATOM 3982 C LYS D 95 -1.037 -9.542 -23.369 1.00 18.82 C
4922	ATOM 3983 O LYS D 95 -1.025 -8.517 -23.887 1.00 19.72 O
4923	ATOM 3984 CB LYS D 95 -1.739 -11.719 -24.171 1.00 24.57 C
4924	ATOM 3985 CG LYS D 95 -1.405 -13.254 -24.270 1.00 49.61 C
4925	ATOM 3986 CD LYS D 95 0.033 -12.822 -25.830 1.00 60.17 C
4926	ATOM 3987 CE LYS D 95 0.875 -13.698 -26.541 1.00 57.82 C
4927	ATOM 3988 NZ LYS D 95 1.951 -12.652 -27.842 1.00 59.53 N
4928	ATOM 3989 N LEU D 96 -1.816 -9.347 -21.943 1.00 16.80 N
4929	ATOM 3990 CA LEU D 96 -2.489 -8.095 -21.711 1.00 16.58 C
4930	ATOM 3991 C LEU D 96 -1.557 -6.998 -20.981 1.00 16.01 C
4931	ATOM 3992 O LEU D 96 -2.025 -5.870 -20.986 1.00 15.73 O
4932	ATOM 3993 CB LEU D 96 -3.813 -8.447 -21.040 1.00 21.01 C
4933	ATOM 3994 CG LEU D 96 -4.799 -9.421 -21.657 1.00 22.06 C
4934	ATOM 3995 CD1 LEU D 96 -6.039 -9.748 -20.763 1.00 15.50 C
4935	ATOM 3996 CD2 LEU D 96 -5.152 -8.823 -22.921 1.00 34.04 C
4936	ATOM 3997 N HIS D 97 -0.781 -7.579 -20.217 1.00 18.03 N
4937	ATOM 3998 CA HIS D 97 0.244 -6.637 -19.580 1.00 18.48 C
4938	ATOM 3999 C HIS D 97 -0.432 -5.796 -18.443 1.00 13.60 C
4939	ATOM 4000 O HIS D 97 -0.253 -4.620 -18.215 1.00 15.07 O
4940	ATOM 4001 CB HIS D 97 0.990 -5.653 -20.400 1.00 24.24 C
4941	ATOM 4002 CG HIS D 97 1.776 -6.391 -21.656 1.00 28.24 C
4942	ATOM 4003 ND1 HIS D 97 2.554 -7.432 -21.385 1.00 26.25 N
4943	ATOM 4004 CD2 HIS D 97 1.271 -6.244 -22.910 1.00 35.10 C
4944	ATOM 4005 CE1 HIS D 97 3.136 -7.961 -22.703 1.00 25.85 C
4945	ATOM 4006 NE2 HIS D 97 2.325 -7.208 -23.322 1.00 28.28 N
4946	ATOM 4007 N VAL D 98 -1.455 -6.545 -17.703 1.00 15.21 N
4947	ATOM 4008 CA VAL D 98 -2.210 -5.794 -16.736 1.00 14.55 C
4948	ATOM 4009 C VAL D 98 -1.489 -5.841 -15.285 1.00 10.52 C
4949	ATOM 4010 O VAL D 98 -1.368 -7.002 -14.827 1.00 11.77 O
4950	ATOM 4011 CB VAL D 98 -3.549 -6.468 -16.502 1.00 15.30 C
4951	ATOM 4012 CG1 VAL D 98 -4.339 -5.933 -15.325 1.00 15.30 C
4952	ATOM 4013 CG2 VAL D 98 -4.285 -6.152 -17.968 1.00 17.14 C
4953	ATOM 4014 N ASP D 99 -1.167 -4.730 -14.701 1.00 9.86 N
4954	ATOM 4015 CA ASP D 99 -0.610 -4.765 -13.282 1.00 10.99 C
4955	ATOM 4016 C ASP D 99 -1.652 -5.465 -12.445 1.00 12.34 C
4956	ATOM 4017 O ASP D 99 -2.837 -4.921 -12.433 1.00 15.90 O
4957	ATOM 4018 CB ASP D 99 -0.421 -3.334 -12.976 1.00 12.59 C
4958	ATOM 4019 CG ASP D 99 0.231 -3.018 -11.481 1.00 12.64 C
4959	ATOM 4020 OD1 ASP D 99 0.529 -1.770 -11.464 1.00 11.35 O
4960	ATOM 4021 OD2 ASP D 99 0.421 -4.097 -10.818 1.00 14.04 O
4961	ATOM 4022 N PRO D 100 -1.293 -6.422 -11.755 1.00 16.57 N
4962	ATOM 4023 CA PRO D 100 -2.075 -7.130 -10.712 1.00 11.14 C
4963	ATOM 4024 C PRO D 100 -2.767 -6.164 -9.672 1.00 11.03 C
4964	ATOM 4025 O PRO D 100 -3.730 -6.728 -9.131 1.00 12.40 O
4965	ATOM 4026 CB PRO D 100 -1.455 -8.509 -10.454 1.00 18.57 C
4966	ATOM 4027 CG PRO D 100 -0.120 -8.351 -10.644 1.00 16.52 C
4967	ATOM 4028 CD PRO D 100 0.008 -7.085 -11.678 1.00 15.61 C
4968	ATOM 4029 N GLU D 101 -2.120 -5.022 -9.432 1.00 9.29 N
4969	ATOM 4030 CA GLU D 101 -2.721 -4.184 -8.535 1.00 12.45 C
4970	ATOM 4031 C GLU D 101 -4.150 -3.766 -8.894 1.00 20.07 C
4971	ATOM 4032 O GLU D 101 -5.139 -3.640 -8.044 1.00 15.47 O
4972	ATOM 4033 CB GLU D 101 -1.898 -2.971 -8.352 1.00 18.48 C
4973	ATOM 4034 CG GLU D 101 -2.751 -1.912 -7.301 1.00 30.49 C
4974	ATOM 4035 CD GLU D 101 -2.928 -2.595 -5.361 1.00 32.99 C
4975	ATOM 4036 OE1 GLU D 101 -1.814 -3.251 -5.501 1.00 22.72 O
4976	ATOM 4037 OE2 GLU D 101 -3.790 -1.433 -5.275 1.00 37.16 O
4977	ATOM 4038 N ASN D 102 -4.416 -3.866 -10.222 1.00 14.86 N
4978	ATOM 4039 CA ASN D 102 -5.827 -3.553 -10.820 1.00 14.38 C
4979	ATOM 4040 C ASN D 102 -6.730 -4.706 -10.375 1.00 12.83 C
4980	ATOM 4041 O ASN D 102 -8.073 -4.305 -10.051 1.00 15.98 O
4981	ATOM 4042 CB ASN D 102 -5.825 -3.726 -12.202 1.00 15.85 C
4982	ATOM 4043 CG ASN D 102 -5.178 -2.418 -12.728 1.00 20.86 C
4983	ATOM 4044 OD1 ASN D 102 -5.594 -1.386 -12.707 1.00 17.49 O
4984	ATOM 4045 ND2 ASN D 102 -3.900 -2.610 -13.401 1.00 22.52 N
4985	ATOM 4046 N PHE D 103 -6.450 -5.902 -10.088 1.00 11.06 N
4986	ATOM 4047 CA PHE D 103 -7.223 -7.062 -9.594 1.00 11.10 C
4987	ATOM 4048 C PHE D 103 -7.838 -6.627 -8.138 1.00 14.83 C
4988	ATOM 4049 O PHE D 103 -9.038 -6.926 -7.755 1.00 12.07 O
4989	ATOM 4050 CB PHE D 103 -6.641 -8.378 -9.453 1.00 14.26 C
4990	ATOM 4051 CG PHE D 103 -5.978 -8.685 -10.884 1.00 14.43 C
4991	ATOM 4052 CD1 PHE D 103 -6.722 -8.442 -12.150 1.00 22.91 C
4992	ATOM 4053 CD2 PHE D 103 -4.777 -9.418 -10.920 1.00 19.84 C
4993	ATOM 4054 CE1 PHE D 103 -6.285 -8.812 -13.376 1.00 22.48 C
4994	ATOM 4055 CE2 PHE D 103 -4.350 -9.752 -12.200 1.00 13.44 C
4995	ATOM 4056 CZ PHE D 103 -4.988 -9.426 -13.435 1.00 16.91 C
4996	ATOM 4057 N ARG D 104 -6.979 -6.041 -7.313 1.00 14.96 N
4997	ATOM 4058 CA ARG D 104 -7.236 -5.640 -5.946 1.00 18.64 C
4998	ATOM 4059 C ARG D 104 -8.352 -4.439 -5.984 1.00 17.76 C
4999	ATOM 4060 O ARG D 104 -9.251 -4.482 -5.206 1.00 14.29 O
5000	ATOM 4061 CB ARG D 104 -5.925 -5.205 -5.097 1.00 19.67 C
5001	ATOM 4062 CG ARG D 104 -5.188 -6.366 -5.055 1.00 39.66 C
5002	ATOM 4063 CD ARG D 104 -3.686 -6.042 -4.324 1.00 67.99 C
5003	ATOM 4064 NE ARG D 104 -3.285 -7.833 -4.405 1.00 67.11 N
5004	ATOM 4065 CZ ARG D 104 -0.829 -7.130 -4.074 1.00 80.12 C
5005	ATOM 4066 NH1 ARG D 104 -1.228 -5.714 -3.904 1.00 77.56 N
5006	ATOM 4067 NH2 ARG D 104 -1.024 -7.904 -3.149 1.00 80.12 N
5007	ATOM 4068 N LEU D 105 -8.019 -3.490 -6.857 1.00 14.78 N
5008	ATOM 4069 CA LEU D 105 -8.933 -2.377 -6.997 1.00 11.66 C
5009	ATOM 4070 C LEU D 105 -10.366 -2.815 -7.384 1.00 13.52 C
5010	ATOM 4071 O LEU D 105 -11.325 -2.484 -6.781 1.00 12.56 O
5011	ATOM 4072 CB LEU D 105 -8.385 -1.463 -7.865 1.00 16.32 C
5012	ATOM 4073 CG LEU D 105 -7.155 -0.533 -7.691 1.00 23.61 C
5013	ATOM 4074 CD1 LEU D 105 -6.564 0.347 -8.601 1.00 25.65 C
5014	ATOM 4075 CD2 LEU D 105 -7.175 -0.008 -6.272 1.00 30.28 C
5015	ATOM 4076 N LEU D 106 -10.388 -3.731 -8.359 1.00 11.11 N
5016	ATOM 4077 CA LEU D 106 -11.776 -4.169 -8.774 1.00 10.81 C
5017	ATOM 4078 C LEU D 106 -12.425 -4.909 -7.735 1.00 7.04 C
5018	ATOM 4079 O LEU D 106 -13.596 -4.860 -7.508 1.00 8.65 O
5019	ATOM 4080 CB LEU D 106 -11.565 -5.136 -9.996 1.00 12.84 C
5020	ATOM 4081 CG LEU D 106 -12.908 -5.591 -10.559 1.00 16.25 C
5021	ATOM 4082 CD1 LEU D 106 -13.855 -4.506 -11.046 1.00 16.77 C
5022	ATOM 4083 CD2 LEU D 106 -12.516 -6.548 -11.540 1.00 20.04 C
5023	ATOM 4084 N GLY D 107 -11.735 -5.688 -6.939 1.00 12.52 N
5024	ATOM 4085 CA GLY D 107 -12.179 -6.516 -5.777 1.00 16.15 C
5025	ATOM 4086 C GLY D 107 -12.899 -5.574 -4.792 1.00 14.99 C
5026	ATOM 4087 O GLY D 107 -14.015 -5.773 -4.332 1.00 12.81 O
5027	ATOM 4088 N ASN D 108 -12.285 -4.436 -4.514 1.00 12.36 N
5028	ATOM 4089 CA ASN D 108 -12.802 -3.491 -3.621 1.00 14.00 C
5029	ATOM 4090 C ASN D 108 -13.963 -2.724 -4.098 1.00 11.43 C
5030	ATOM 4091 O ASN D 108 -15.056 -2.507 -3.385 1.00 12.39 O
5031	ATOM 4092 CB ASN D 108 -11.844 -2.454 -3.053 1.00 18.57 C
5032	ATOM 4093 CG ASN D 108 -10.617 -3.293 -1.988 1.00 22.26 C
5033	ATOM 4094 OD1 ASN D 108 -11.199 -4.293 -1.311 1.00 22.78 O
5034	ATOM 4095 ND2 ASN D 108 -9.853 -2.344 -1.843 1.00 30.03 N
5035	ATOM 4096 N VAL D 109 -13.924 -2.387 -5.385 1.00 10.09 N
5036	ATOM 4097 CA VAL D 109 -15.064 -1.848 -6.032 1.00 8.21 C
5037	ATOM 4098 C VAL D 109 -16.234 -2.783 -6.101 1.00 9.89 C
5038	ATOM 4099 O VAL D 109 -17.335 -2.321 -5.728 1.00 11.76 O
5039	ATOM 4100 CB VAL D 109 -14.656 -1.351 -7.492 1.00 11.59 C
5040	ATOM 4101 CG1 VAL D 109 -15.861 -0.846 -8.320 1.00 17.96 C
5041	ATOM 4102 CG2 VAL D 109 -13.771 -0.178 -7.377 1.00 17.98 C
5042	ATOM 4103 N LEU D 110 -15.952 -4.083 -6.403 1.00 9.62 N
5043	ATOM 4104 CA LEU D 110 -17.024 -5.059 -6.369 1.00 14.08 C
5044	ATOM 4105 C LEU D 110 -17.831 -5.035 -5.141 1.00 11.97 C
5045	ATOM 4106 O LEU D 110 -19.008 -5.257 -4.826 1.00 10.97 O
5046	ATOM 4107 CB LEU D 110 -16.600 -6.309 -6.770 1.00 15.34 C
5047	ATOM 4108 CG LEU D 110 -17.478 -7.458 -6.761 1.00 14.97 C
5048	ATOM 4109 CD1 LEU D 110 -18.670 -7.282 -7.592 1.00 23.21 C
5049	ATOM 4110 CD2 LEU D 110 -16.862 -8.829 -7.132 1.00 26.92 C
5050	ATOM 4111 N VAL D 111 -16.932 -5.013 -3.909 1.00 14.50 N
5051	ATOM 4112 CA VAL D 111 -17.557 -5.003 -2.482 1.00 11.82 C
5052	ATOM 4113 C VAL D 111 -18.496 -3.835 -2.339 1.00 14.01 C
5053	ATOM 4114 O VAL D 111 -19.560 -3.938 -1.746 1.00 12.03 O
5054	ATOM 4115 CB VAL D 111 -16.468 -5.174 -1.423 1.00 12.62 C
5055	ATOM 4116 CG1 VAL D 111 -17.105 -4.887 -0.077 1.00 15.85 C
5056	ATOM 4117 CG2 VAL D 111 -15.845 -6.615 -1.505 1.00 10.77 C
5057	ATOM 4118 N CYS D 112 -17.954 -2.598 -2.876 1.00 13.62 N
5058	ATOM 4119 CA CYS D 112 -18.674 -1.428 -2.875 1.00 13.72 C
5059	ATOM 4120 C CYS D 112 -20.245 -1.545 -3.397 1.00 20.10 C
5060	ATOM 4121 O CYS D 112 -21.199 -1.153 -2.984 1.00 16.56 O
5061	ATOM 4122 CB CYS D 112 -18.077 -0.213 -3.441 1.00 12.95 C
5062	ATOM 4123 SG CYS D 112 -16.890 0.371 -2.238 1.00 15.21 S
5063	ATOM 4124 N VAL D 113 -20.090 -2.259 -4.565 1.00 17.02 N
5064	ATOM 4125 CA VAL D 113 -21.229 -2.476 -5.537 1.00 12.28 C
5065	ATOM 4126 C VAL D 113 -22.216 -3.415 -4.943 1.00 12.56 C
5066	ATOM 4127 O VAL D 113 -23.393 -3.166 -4.833 1.00 15.84 O
5067	ATOM 4128 CB VAL D 113 -20.819 -3.012 -6.914 1.00 17.85 C
5068	ATOM 4129 CG1 VAL D 113 -22.007 -3.440 -7.657 1.00 18.74 C
5069	ATOM 4130 CG2 VAL D 113 -20.123 -1.688 -7.807 1.00 21.41 C
5070	ATOM 4131 N LEU D 114 -21.799 -4.480 -4.273 1.00 10.75 N
5071	ATOM 4132 CA LEU D 114 -22.611 -5.453 -3.526 1.00 10.78 C
5072	ATOM 4133 C LEU D 114 -23.336 -4.689 -2.455 1.00 19.00 C
5073	ATOM 4134 O LEU D 114 -24.454 -4.811 -2.196 1.00 11.46 O
5074	ATOM 4135 CB LEU D 114 -21.815 -6.582 -3.114 1.00 14.56 C
5075	ATOM 4136 CG LEU D 114 -21.183 -7.401 -4.241 1.00 17.11 C
5076	ATOM 4137 CD1 LEU D 114 -20.368 -8.591 -3.652 1.00 17.06 C
5077	ATOM 4138 CD2 LEU D 114 -22.473 -8.135 -5.021 1.00 20.86 C
5078	ATOM 4139 N ALA D 115 -22.573 -3.965 -1.677 1.00 11.71 N
5079	ATOM 4140 CA ALA D 115 -23.177 -3.124 -0.512 1.00 11.69 C
5080	ATOM 4141 C ALA D 115 -24.286 -2.193 -1.056 1.00 15.12 C
5081	ATOM 4142 O ALA D 115 -25.190 -2.078 -0.405 1.00 15.47 O
5082	ATOM 4143 CB ALA D 115 -22.014 -2.336 0.283 1.00 12.28 C
5083	ATOM 4144 N HIS D 116 -23.996 -1.420 -2.116 1.00 15.03 N
5084	ATOM 4145 CA HIS D 116 -24.955 -0.497 -2.730 1.00 12.09 C
5085	ATOM 4146 C HIS D 116 -26.163 -1.244 -3.183 1.00 12.50 C
5086	ATOM 4147 O HIS D 116 -27.367 -0.733 -2.977 1.00 15.93 O
5087	ATOM 4148 CB HIS D 116 -24.260 0.137 -3.930 1.00 20.66 C
5088	ATOM 4149 CG HIS D 116 -25.177 1.236 -4.511 1.00 27.72 C
5089	ATOM 4150 ND1 HIS D 116 -25.302 1.194 -5.752 1.00 29.99 N
5090	ATOM 4151 CD2 HIS D 116 -25.633 2.207 -3.823 1.00 30.96 C
5091	ATOM 4152 CE1 HIS D 116 -26.002 2.415 -6.103 1.00 27.26 C
5092	ATOM 4153 NE2 HIS D 116 -26.344 3.000 -4.762 1.00 28.89 N
5093	ATOM 4154 N HIS D 117 -26.018 -2.363 -3.828 1.00 13.33 N
5094	ATOM 4155 CA HIS D 117 -27.076 -3.136 -4.425 1.00 15.24 C
5095	ATOM 4156 C HIS D 117 -27.870 -3.712 -3.255 1.00 17.50 C
5096	ATOM 4157 O HIS D 117 -29.133 -3.855 -3.315 1.00 16.06 O
5097	ATOM 4158 CB HIS D 117 -26.496 -4.135 -5.434 1.00 17.22 C
5098	ATOM 4159 CG HIS D 117 -27.385 -4.774 -6.024 1.00 54.91 C
5099	ATOM 4160 ND1 HIS D 117 -28.250 -3.991 -7.312 1.00 47.40 N
5100	ATOM 4161 CD2 HIS D 117 -28.517 -5.901 -5.930 1.00 49.34 C
5101	ATOM 4162 CE1 HIS D 117 -29.253 -5.278 -7.522 1.00 48.36 C
5102	ATOM 4163 NE2 HIS D 117 -29.230 -6.041 -6.924 1.00 37.10 N
5103	ATOM 4164 N PHE D 118 -27.360 -4.464 -2.297 1.00 14.50 N
5104	ATOM 4165 CA PHE D 118 -28.031 -5.299 -1.218 1.00 19.30 C
5105	ATOM 4166 C PHE D 118 -28.313 -4.501 -0.028 1.00 20.52 C
5106	ATOM 4167 O PHE D 118 -29.066 -5.081 0.915 1.00 18.09 O
5107	ATOM 4168 CB PHE D 118 -27.213 -6.481 -0.908 1.00 18.97 C
5108	ATOM 4169 CG PHE D 118 -27.223 -7.413 -2.204 1.00 18.93 C
5109	ATOM 4170 CD1 PHE D 118 -26.304 -7.801 -3.109 1.00 24.34 C
5110	ATOM 4171 CD2 PHE D 118 -28.509 -8.118 -2.367 1.00 26.48 C
5111	ATOM 4172 CE1 PHE D 118 -26.170 -8.548 -4.227 1.00 20.81 C
5112	ATOM 4173 CE2 PHE D 118 -28.524 -8.992 -3.636 1.00 22.90 C
5113	ATOM 4174 CZ PHE D 118 -27.563 -8.928 -4.575 1.00 38.52 C
5114	ATOM 4175 N GLY D 119 -27.754 -3.376 0.316 1.00 12.95 N
5115	ATOM 4176 CA GLY D 119 -28.196 -2.563 1.458 1.00 17.60 C
5116	ATOM 4177 C GLY D 119 -27.642 -3.404 2.740 1.00 22.58 C
5117	ATOM 4178 O GLY D 119 -26.745 -4.123 2.946 1.00 17.60 O
5118	ATOM 4179 N LYS D 120 -28.738 -3.418 3.697 1.00 21.46 N
5119	ATOM 4180 CA LYS D 120 -28.403 -3.844 5.025 1.00 20.05 C
5120	ATOM 4181 C LYS D 120 -28.472 -5.257 5.045 1.00 21.98 C
5121	ATOM 4182 O LYS D 120 -27.730 -5.889 5.925 1.00 18.57 O
5122	ATOM 4183 CB LYS D 120 -29.674 -3.273 5.899 1.00 27.28 C
5123	ATOM 4184 CG LYS D 120 -30.525 -4.321 5.995 1.00 44.07 C
5124	ATOM 4185 CD LYS D 120 -31.907 -4.631 6.867 1.00 48.21 C
5125	ATOM 4186 CE LYS D 120 -33.041 -5.118 5.873 1.00 53.23 C
5126	ATOM 4187 NZ LYS D 120 -34.578 -6.152 7.224 1.00 62.54 N
5127	ATOM 4188 N GLU D 121 -28.504 -6.080 4.008 1.00 25.88 N
5128	ATOM 4189 CA GLU D 121 -28.273 -7.343 3.934 1.00 20.02 C
5129	ATOM 4190 C GLU D 121 -26.675 -7.822 3.749 1.00 18.96 C
5130	ATOM 4191 O GLU D 121 -26.335 -8.975 4.074 1.00 16.05 O
5131	ATOM 4192 CB GLU D 121 -29.032 -8.153 2.527 1.00 28.13 C
5132	ATOM 4193 CG GLU D 121 -28.995 -9.238 2.561 1.00 40.20 C
5133	ATOM 4194 CD GLU D 121 -30.346 -10.237 1.461 1.00 49.97 C
5134	ATOM 4195 OE1 GLU D 121 -29.357 -11.293 1.004 1.00 36.73 O
5135	ATOM 4196 OE2 GLU D 121 -30.336 -9.346 0.552 1.00 38.86 O
5136	ATOM 4197 N PHE D 122 -26.073 -6.783 3.271 1.00 14.83 N
5137	ATOM 4198 CA PHE D 122 -24.573 -7.060 3.133 1.00 20.37 C
5138	ATOM 4199 C PHE D 122 -23.961 -6.641 4.530 1.00 15.94 C
5139	ATOM 4200 O PHE D 122 -23.307 -5.592 4.698 1.00 17.73 O
5140	ATOM 4201 CB PHE D 122 -24.256 -6.093 2.128 1.00 14.63 C
5141	ATOM 4202 CG PHE D 122 -22.862 -6.484 1.494 1.00 12.39 C
5142	ATOM 4203 CD1 PHE D 122 -22.569 -7.575 0.927 1.00 14.73 C
5143	ATOM 4204 CD2 PHE D 122 -21.593 -5.712 1.717 1.00 15.96 C
5144	ATOM 4205 CE1 PHE D 122 -21.227 -8.021 0.354 1.00 19.03 C
5145	ATOM 4206 CE2 PHE D 122 -20.268 -6.011 1.383 1.00 16.31 C
5146	ATOM 4207 CZ PHE D 122 -20.290 -7.145 0.714 1.00 19.86 C
5147	ATOM 4208 N THR D 123 -24.154 -7.525 5.413 1.00 12.54 N
5148	ATOM 4209 CA THR D 123 -23.654 -7.132 6.808 1.00 13.34 C
5149	ATOM 4210 C THR D 123 -22.221 -7.283 6.854 1.00 15.73 C
5150	ATOM 4211 O THR D 123 -21.546 -7.802 6.060 1.00 13.84 O
5151	ATOM 4212 CB THR D 123 -24.160 -8.212 7.778 1.00 17.72 C
5152	ATOM 4213 OG1 THR D 123 -23.892 -9.520 7.414 1.00 19.04 O
5153	ATOM 4214 CG2 THR D 123 -25.951 -8.264 7.657 1.00 20.06 C
5154	ATOM 4215 N PRO D 124 -21.722 -6.789 8.010 1.00 17.46 N
5155	ATOM 4216 CA PRO D 124 -20.251 -6.940 8.311 1.00 14.41 C
5156	ATOM 4217 C PRO D 124 -19.706 -8.259 8.132 1.00 12.05 C
5157	ATOM 4218 O PRO D 124 -18.668 -8.405 7.486 1.00 13.28 O
5158	ATOM 4219 CB PRO D 124 -20.088 -6.243 9.615 1.00 14.54 C
5159	ATOM 4220 CG PRO D 124 -21.223 -5.227 9.715 1.00 15.93 C
5160	ATOM 4221 CD PRO D 124 -22.358 -6.045 9.113 1.00 14.57 C
5161	ATOM 4222 N PRO D 125 -20.257 -9.372 8.599 1.00 11.40 N
5162	ATOM 4223 CA PRO D 125 -19.807 -10.596 8.366 1.00 17.87 C
5163	ATOM 4224 C PRO D 125 -19.690 -11.236 6.993 1.00 15.21 C
5164	ATOM 4225 O PRO D 125 -18.781 -11.857 6.488 1.00 14.41 O
5165	ATOM 4226 CB PRO D 125 -20.651 -11.465 9.240 1.00 23.30 C
5166	ATOM 4227 CG PRO D 125 -21.148 -10.683 10.183 1.00 26.37 C
5167	ATOM 4228 CD PRO D 125 -21.413 -9.462 9.802 1.00 17.49 C
5168	ATOM 4229 N VAL D 126 -20.833 -10.714 6.263 1.00 17.66 N
5169	ATOM 4230 CA VAL D 126 -20.828 -11.114 4.812 1.00 21.55 C
5170	ATOM 4231 C VAL D 126 -19.574 -10.424 3.938 1.00 16.49 C
5171	ATOM 4232 O VAL D 126 -19.053 -10.988 3.156 1.00 13.46 O
5172	ATOM 4233 CB VAL D 126 -22.452 -10.640 4.161 1.00 13.98 C
5173	ATOM 4234 CG1 VAL D 126 -22.335 -11.055 2.842 1.00 20.70 C
5174	ATOM 4235 CG2 VAL D 126 -23.218 -11.661 4.994 1.00 18.54 C
5175	ATOM 4236 N GLN D 127 -19.567 -8.990 4.377 1.00 10.60 N
5176	ATOM 4237 CA GLN D 127 -18.404 -8.336 3.872 1.00 12.83 C
5177	ATOM 4238 C GLN D 127 -17.168 -9.034 3.964 1.00 13.74 C
5178	ATOM 4239 O GLN D 127 -16.333 -9.154 3.044 1.00 12.71 O
5179	ATOM 4240 CB GLN D 127 -18.494 -6.875 4.230 1.00 11.73 C
5180	ATOM 4241 CG GLN D 127 -17.167 -6.142 3.667 1.00 13.68 C
5181	ATOM 4242 CD GLN D 127 -16.957 -4.845 4.400 1.00 11.81 C
5182	ATOM 4243 OE1 GLN D 127 -17.847 -4.243 5.015 1.00 13.99 O
5183	ATOM 4244 NE2 GLN D 127 -15.920 -4.250 3.871 1.00 15.96 N
5184	ATOM 4245 N ALA D 128 -16.860 -9.470 5.254 1.00 12.61 N
5185	ATOM 4246 CA ALA D 128 -15.629 -10.118 5.636 1.00 9.64 C
5186	ATOM 4247 C ALA D 128 -15.294 -11.332 4.779 1.00 7.66 C
5187	ATOM 4248 O ALA D 128 -14.216 -11.498 4.302 1.00 11.68 O
5188	ATOM 4249 CB ALA D 128 -15.618 -10.468 7.105 1.00 13.80 C
5189	ATOM 4250 N ALA D 129 -16.442 -11.965 4.516 1.00 13.18 N
5190	ATOM 4251 CA ALA D 129 -16.351 -13.231 3.750 1.00 11.17 C
5191	ATOM 4252 C ALA D 129 -15.929 -12.840 2.277 1.00 11.52 C
5192	ATOM 4253 O ALA D 129 -15.098 -13.537 1.657 1.00 13.56 O
5193	ATOM 4254 CB ALA D 129 -17.591 -14.039 3.811 1.00 14.35 C
5194	ATOM 4255 N TYR D 130 -16.661 -11.959 1.697 1.00 13.36 N
5195	ATOM 4256 CA TYR D 130 -16.475 -11.445 0.343 1.00 13.72 C
5196	ATOM 4257 C TYR D 130 -15.053 -10.791 0.256 1.00 15.10 C
5197	ATOM 4258 O TYR D 130 -14.355 -11.020 -0.750 1.00 13.21 O
5198	ATOM 4259 CB TYR D 130 -17.422 -10.440 -0.057 1.00 13.30 C
5199	ATOM 4260 CG TYR D 130 -18.539 -11.158 -0.682 1.00 15.19 C
5200	ATOM 4261 CD1 TYR D 130 -18.456 -11.539 -1.989 1.00 16.58 C
5201	ATOM 4262 CD2 TYR D 130 -19.661 -11.646 -0.093 1.00 11.73 C
5202	ATOM 4263 CE1 TYR D 130 -19.348 -12.381 -2.950 1.00 20.28 C
5203	ATOM 4264 CE2 TYR D 130 -20.692 -12.412 -0.867 1.00 14.90 C
5204	ATOM 4265 CZ TYR D 130 -20.584 -12.824 -2.071 1.00 22.05 C
5205	ATOM 4266 OH TYR D 130 -21.522 -13.470 -2.725 1.00 20.92 O
5206	ATOM 4267 N GLN D 131 -14.583 -10.235 1.300 1.00 12.24 N
5207	ATOM 4268 CA GLN D 131 -13.174 -9.715 1.275 1.00 13.72 C
5208	ATOM 4269 C GLN D 131 -12.128 -10.656 1.064 1.00 20.69 C
5209	ATOM 4270 O GLN D 131 -11.251 -10.668 0.401 1.00 17.83 O
5210	ATOM 4271 CB GLN D 131 -12.830 -8.708 2.421 1.00 13.45 C
5211	ATOM 4272 CG GLN D 131 -13.616 -7.579 2.534 1.00 20.19 C
5212	ATOM 4273 CD GLN D 131 -13.161 -6.166 1.573 1.00 18.43 C
5213	ATOM 4274 OE1 GLN D 131 -14.035 -5.385 1.692 1.00 14.48 O
5214	ATOM 4275 NE2 GLN D 131 -12.233 -6.377 0.841 1.00 16.06 N
5215	ATOM 4276 N LYS D 132 -12.389 -11.876 1.744 1.00 12.67 N
5216	ATOM 4277 CA LYS D 132 -11.377 -12.991 1.725 1.00 15.63 C
5217	ATOM 4278 C LYS D 132 -11.407 -13.587 0.293 1.00 18.80 C
5218	ATOM 4279 O LYS D 132 -10.481 -13.843 -0.328 1.00 14.05 O
5219	ATOM 4280 CB LYS D 132 -11.780 -14.083 2.621 1.00 24.81 C
5220	ATOM 4281 CG LYS D 132 -11.356 -13.759 4.081 1.00 25.97 C
5221	ATOM 4282 CD LYS D 132 -11.952 -14.985 5.007 1.00 26.81 C
5222	ATOM 4283 CE LYS D 132 -12.396 -14.023 6.345 1.00 50.23 C
5223	ATOM 4284 NZ LYS D 132 -12.099 -16.364 7.125 1.00 63.38 N
5224	ATOM 4285 N VAL D 133 -12.646 -13.574 -0.320 1.00 13.42 N
5225	ATOM 4286 CA VAL D 133 -12.819 -14.186 -1.656 1.00 18.27 C
5226	ATOM 4287 C VAL D 133 -12.113 -13.235 -2.641 1.00 19.39 C
5227	ATOM 4288 O VAL D 133 -11.376 -13.757 -3.529 1.00 15.06 O
5228	ATOM 4289 CB VAL D 133 -14.347 -14.459 -2.009 1.00 17.40 C
5229	ATOM 4290 CG1 VAL D 133 -14.482 -14.527 -3.527 1.00 22.79 C
5230	ATOM 4291 CG2 VAL D 133 -14.897 -15.429 -1.020 1.00 19.90 C
5231	ATOM 4292 N VAL D 134 -12.419 -12.044 -2.631 1.00 14.66 N
5232	ATOM 4293 CA VAL D 134 -11.817 -11.184 -3.697 1.00 17.41 C
5233	ATOM 4294 C VAL D 134 -10.205 -10.998 -3.622 1.00 17.93 C
5234	ATOM 4295 O VAL D 134 -9.555 -11.088 -4.632 1.00 17.13 O
5235	ATOM 4296 CB VAL D 134 -12.523 -9.795 -3.826 1.00 16.69 C
5236	ATOM 4297 CG1 VAL D 134 -13.942 -9.809 -3.996 1.00 22.42 C
5237	ATOM 4298 CG2 VAL D 134 -12.135 -9.012 -2.596 1.00 16.30 C
5238	ATOM 4299 N ALA D 135 -9.754 -11.116 -2.425 1.00 16.25 N
5239	ATOM 4300 CA ALA D 135 -8.338 -11.031 -2.088 1.00 14.79 C
5240	ATOM 4301 C ALA D 135 -7.743 -12.494 -2.790 1.00 21.70 C
5241	ATOM 4302 O ALA D 135 -6.667 -12.571 -3.342 1.00 16.89 O
5242	ATOM 4303 CB ALA D 135 -7.946 -11.087 -0.719 1.00 18.34 C
5243	ATOM 4304 N GLY D 136 -8.430 -13.631 -2.593 1.00 17.40 N
5244	ATOM 4305 CA GLY D 136 -8.238 -14.854 -2.994 1.00 16.77 C
5245	ATOM 4306 C GLY D 136 -8.046 -14.863 -4.547 1.00 21.35 C
5246	ATOM 4307 O GLY D 136 -7.103 -15.386 -5.248 1.00 16.80 O
5247	ATOM 4308 N VAL D 137 -9.061 -14.287 -5.106 1.00 23.70 N
5248	ATOM 4309 CA VAL D 137 -9.117 -14.207 -6.516 1.00 26.49 C
5249	ATOM 4310 C VAL D 137 -8.271 -13.386 -7.311 1.00 33.07 C
5250	ATOM 4311 O VAL D 137 -7.434 -13.729 -8.023 1.00 30.90 O
5251	ATOM 4312 CB VAL D 137 -10.635 -13.731 -7.203 1.00 15.94 C
5252	ATOM 4313 CG1 VAL D 137 -10.606 -13.355 -8.722 1.00 21.57 C
5253	ATOM 4314 CG2 VAL D 137 -11.540 -14.757 -6.690 1.00 21.46 C
5254	ATOM 4315 N ALA D 138 -7.804 -12.254 -6.635 1.00 14.66 N
5255	ATOM 4316 CA ALA D 138 -6.688 -11.339 -7.074 1.00 18.95 C
5256	ATOM 4317 C ALA D 138 -5.417 -12.079 -7.070 1.00 18.17 C
5257	ATOM 4318 O ALA D 138 -4.593 -11.997 -7.851 1.00 14.81 O
5258	ATOM 4319 CB ALA D 138 -6.540 -10.040 -6.183 1.00 19.78 C
5259	ATOM 4320 N ASN D 139 -5.187 -12.811 -5.928 1.00 15.30 N
5260	ATOM 4321 CA ASN D 139 -3.937 -13.374 -5.586 1.00 18.41 C
5261	ATOM 4322 C ASN D 139 -3.703 -14.483 -6.697 1.00 25.63 C
5262	ATOM 4323 O ASN D 139 -2.635 -14.913 -7.329 1.00 23.38 O
5263	ATOM 4324 CB ASN D 139 -3.989 -14.050 -4.592 1.00 50.89 C
5264	ATOM 4325 CG ASN D 139 -3.194 -13.790 -3.503 1.00 63.06 C
5265	ATOM 4326 OD1 ASN D 139 -2.135 -15.017 -3.938 1.00 52.41 O
5266	ATOM 4327 ND2 ASN D 139 -3.072 -12.228 -3.482 1.00 29.84 N
5267	ATOM 4328 N ALA D 140 -4.873 -15.260 -6.949 1.00 19.40 N
5268	ATOM 4329 CA ALA D 140 -5.005 -16.402 -7.986 1.00 23.09 C
5269	ATOM 4330 C ALA D 140 -4.740 -15.710 -9.403 1.00 18.16 C
5270	ATOM 4331 O ALA D 140 -3.930 -16.420 -10.089 1.00 16.51 O
5271	ATOM 4332 CB ALA D 140 -6.303 -16.997 -8.071 1.00 18.14 C
5272	ATOM 4333 N LEU D 141 -5.172 -14.659 -9.775 1.00 14.97 N
5273	ATOM 4334 CA LEU D 141 -4.899 -14.068 -11.011 1.00 14.94 C
5274	ATOM 4335 C LEU D 141 -3.434 -13.602 -11.198 1.00 11.73 C
5275	ATOM 4336 O LEU D 141 -2.840 -13.285 -12.242 1.00 15.21 O
5276	ATOM 4337 CB LEU D 141 -6.006 -12.939 -11.311 1.00 15.16 C
5277	ATOM 4338 CG LEU D 141 -7.325 -13.394 -11.757 1.00 17.87 C
5278	ATOM 4339 CD1 LEU D 141 -7.836 -12.121 -12.278 1.00 24.86 C
5279	ATOM 4340 CD2 LEU D 141 -6.860 -13.940 -13.382 1.00 16.07 C
5280	ATOM 4341 N ALA D 142 -2.826 -13.097 -10.036 1.00 14.26 N
5281	ATOM 4342 CA ALA D 142 -1.439 -12.718 -10.054 1.00 17.21 C
5282	ATOM 4343 C ALA D 142 -0.379 -13.783 -9.991 1.00 18.46 C
5283	ATOM 4344 O ALA D 142 0.751 -13.412 -10.228 1.00 18.92 O
5284	ATOM 4345 CB ALA D 142 -1.279 -11.774 -8.892 1.00 19.11 C
5285	ATOM 4346 N HIS D 143 -0.748 -15.020 -9.767 1.00 19.75 N
5286	ATOM 4347 CA HIS D 143 0.079 -16.200 -9.518 1.00 26.63 C
5287	ATOM 4348 C HIS D 143 1.176 -16.436 -10.670 1.00 23.72 C
5288	ATOM 4349 O HIS D 143 2.224 -16.803 -10.136 1.00 24.41 O
5289	ATOM 4350 CB HIS D 143 -0.669 -17.339 -8.942 1.00 25.89 C
5290	ATOM 4351 CG HIS D 143 0.097 -18.406 -8.683 1.00 56.45 C
5291	ATOM 4352 ND1 HIS D 143 0.122 -19.475 -9.292 1.00 44.25 N
5292	ATOM 4353 CD2 HIS D 143 1.035 -18.261 -7.098 1.00 48.81 C
5293	ATOM 4354 CE1 HIS D 143 1.293 -20.089 -8.356 1.00 56.93 C
5294	ATOM 4355 NE2 HIS D 143 1.407 -19.517 -7.123 1.00 49.27 N
5295	ATOM 4356 N LYS D 144 0.773 -16.313 -11.824 1.00 19.26 N
5296	ATOM 4357 CA LYS D 144 1.442 -16.574 -13.172 1.00 33.94 C
5297	ATOM 4358 C LYS D 144 2.421 -15.633 -13.479 1.00 32.28 C
5298	ATOM 4359 O LYS D 144 2.996 -15.637 -14.654 1.00 23.60 O
5299	ATOM 4360 CB LYS D 144 1.055 -17.526 -13.968 1.00 31.20 C
5300	ATOM 4361 CG LYS D 144 0.220 -18.870 -13.388 1.00 40.85 C
5301	ATOM 4362 CD LYS D 144 1.002 -19.972 -13.512 1.00 59.03 C
5302	ATOM 4363 CE LYS D 144 0.888 -21.048 -13.306 1.00 56.19 C
5303	ATOM 4364 NZ LYS D 144 1.510 -22.846 -14.338 1.00 70.96 N
5304	ATOM 4365 N TYR D 145 2.435 -14.424 -12.946 1.00 24.92 N
5305	ATOM 4366 CA TYR D 145 3.207 -13.372 -13.244 1.00 29.13 C
5306	ATOM 4367 C TYR D 145 4.717 -13.524 -13.102 1.00 38.17 C
5307	ATOM 4368 O TYR D 145 5.061 -14.114 -12.139 1.00 27.99 O
5308	ATOM 4369 CB TYR D 145 2.744 -12.016 -12.590 1.00 17.99 C
5309	ATOM 4370 CG TYR D 145 1.621 -11.268 -13.262 1.00 17.42 C
5310	ATOM 4371 CD1 TYR D 145 1.523 -10.110 -13.925 1.00 16.93 C
5311	ATOM 4372 CD2 TYR D 145 0.375 -12.020 -13.134 1.00 18.60 C
5312	ATOM 4373 CE1 TYR D 145 0.498 -9.521 -14.492 1.00 17.99 C
5313	ATOM 4374 CE2 TYR D 145 -0.813 -11.356 -13.802 1.00 14.96 C
5314	ATOM 4375 CZ TYR D 145 -0.763 -10.275 -14.381 1.00 12.85 C
5315	ATOM 4376 OH TYR D 145 -1.813 -9.580 -14.987 1.00 13.31 O
5316	ATOM 4377 N HIS D 146 5.428 -13.165 -14.072 1.00 26.11 N
5317	ATOM 4378 CA HIS D 146 7.054 -13.167 -14.050 1.00 31.89 C
5318	ATOM 4379 C HIS D 146 7.429 -12.153 -15.048 1.00 21.33 C
5319	ATOM 4380 O HIS D 146 6.931 -11.249 -15.530 1.00 27.92 O
5320	ATOM 4381 CB HIS D 146 7.223 -14.769 -14.665 1.00 30.13 C
5321	ATOM 4382 CG HIS D 146 6.497 -14.789 -15.882 1.00 40.51 C
5322	ATOM 4383 ND1 HIS D 146 7.552 -14.702 -17.398 1.00 47.51 N
5323	ATOM 4384 CD2 HIS D 146 5.784 -14.325 -16.776 1.00 45.49 C
5324	ATOM 4385 CE1 HIS D 146 7.188 -14.800 -17.949 1.00 56.67 C
5325	ATOM 4386 NE2 HIS D 146 5.714 -14.339 -18.353 1.00 37.33 N
5326	ATOM 4387 OXT HIS D 146 8.812 -12.134 -14.847 1.00 21.61 O
5327	TER 4388 HIS D 146
5328	HETATM 4389 CHA HEM A 142 8.585 7.902 -18.282 1.00 16.31 C
5329	HETATM 4390 CHB HEM A 142 10.355 9.805 -14.208 1.00 26.27 C
5330	HETATM 4391 CHC HEM A 142 8.341 6.363 -11.589 1.00 13.23 C
5331	HETATM 4392 CHD HEM A 142 6.988 4.088 -15.744 1.00 14.77 C
5332	HETATM 4393 C1A HEM A 142 9.141 8.725 -17.504 1.00 17.40 C
5333	HETATM 4394 C2A HEM A 142 10.098 9.952 -17.887 1.00 18.53 C
5334	HETATM 4395 C3A HEM A 142 10.636 10.499 -16.796 1.00 18.36 C
5335	HETATM 4396 C4A HEM A 142 10.137 9.679 -15.611 1.00 16.88 C
5336	HETATM 4397 CMA HEM A 142 11.613 11.590 -16.732 1.00 21.20 C
5337	HETATM 4398 CAA HEM A 142 10.403 10.367 -19.312 1.00 25.54 C
5338	HETATM 4399 CBA HEM A 142 9.552 11.270 -19.659 1.00 31.38 C
5339	HETATM 4400 CGA HEM A 142 10.793 12.286 -21.342 1.00 44.82 C
5340	HETATM 4401 O1A HEM A 142 9.887 11.345 -21.943 1.00 39.10 O
5341	HETATM 4402 O2A HEM A 142 9.308 12.698 -21.487 1.00 54.71 O
5342	HETATM 4403 C1B HEM A 142 9.938 9.271 -13.145 1.00 23.63 C
5343	HETATM 4404 C2B HEM A 142 10.318 9.380 -11.838 1.00 11.67 C
5344	HETATM 4405 C3B HEM A 142 9.660 8.341 -11.052 1.00 17.41 C
5345	HETATM 4406 C4B HEM A 142 9.028 7.467 -11.975 1.00 14.84 C
5346	HETATM 4407 CMB HEM A 142 11.048 10.634 -11.389 1.00 12.32 C
5347	HETATM 4408 CAB HEM A 142 9.567 8.336 -9.634 1.00 24.30 C
5348	HETATM 4409 CBB HEM A 142 10.576 8.441 -8.785 1.00 28.40 C
5349	HETATM 4410 C1C HEM A 142 7.680 5.498 -12.499 1.00 13.39 C
5350	HETATM 4411 C2C HEM A 142 7.270 4.198 -12.170 1.00 11.20 C
5351	HETATM 4412 C3C HEM A 142 6.975 3.441 -13.304 1.00 8.94 C
5352	HETATM 4413 C4C HEM A 142 7.207 4.445 -14.517 1.00 10.29 C
5353	HETATM 4414 CMC HEM A 142 7.098 3.618 -10.845 1.00 13.77 C
5354	HETATM 4415 CAC HEM A 142 6.342 2.184 -13.525 1.00 13.45 C
5355	HETATM 4416 CBC HEM A 142 6.722 1.153 -12.766 1.00 11.27 C
5356	HETATM 4417 C1D HEM A 142 7.302 4.989 -16.733 1.00 11.32 C
5357	HETATM 4418 C2D HEM A 142 7.141 4.644 -18.240 1.00 16.69 C
5358	HETATM 4419 C3D HEM A 142 7.540 5.718 -18.887 1.00 20.49 C
5359	HETATM 4420 C4D HEM A 142 8.172 6.582 -18.158 1.00 16.46 C
5360	HETATM 4421 CMD HEM A 142 6.354 3.385 -18.817 1.00 19.45 C
5361	HETATM 4422 CAD HEM A 142 7.621 5.740 -20.408 1.00 21.31 C
5362	HETATM 4423 CBD HEM A 142 8.764 5.354 -20.767 1.00 38.22 C
5363	HETATM 4424 CGD HEM A 142 9.138 5.049 -22.798 1.00 41.21 C
5364	HETATM 4425 O1D HEM A 142 9.998 5.836 -22.703 1.00 42.81 O
5365	HETATM 4426 O2D HEM A 142 8.349 4.920 -23.144 1.00 40.12 O
5366	HETATM 4427 NA HEM A 142 9.397 8.686 -16.211 1.00 16.46 N
5367	HETATM 4428 NB HEM A 142 9.343 8.012 -13.298 1.00 12.29 N
5368	HETATM 4429 NC HEM A 142 7.604 5.533 -13.949 1.00 15.07 N
5369	HETATM 4430 ND HEM A 142 7.715 6.202 -16.788 1.00 13.07 N
5370	HETATM 4431 FE HEM A 142 8.116 7.403 -15.045 1.00 18.07 FE
5371	HETATM 4432 P PO4 B 147 5.931 -21.573 3.319 1.00 32.97 P
5372	HETATM 4433 CHA HEM B 148 9.659 -10.155 20.773 1.00 21.59 C
5373	HETATM 4434 CHB HEM B 148 11.121 -12.190 16.575 1.00 16.50 C
5374	HETATM 4435 CHC HEM B 148 9.762 -8.175 14.122 1.00 16.82 C
5375	HETATM 4436 CHD HEM B 148 8.223 -6.187 18.294 1.00 16.19 C
5376	HETATM 4437 C1A HEM B 148 10.199 -10.977 19.856 1.00 24.57 C
5377	HETATM 4438 C2A HEM B 148 10.940 -12.186 20.114 1.00 17.10 C
5378	HETATM 4439 C3A HEM B 148 11.529 -12.852 19.028 1.00 13.46 C
5379	HETATM 4440 C4A HEM B 148 10.911 -11.942 17.916 1.00 18.78 C
5380	HETATM 4441 CMA HEM B 148 12.211 -14.084 18.855 1.00 20.21 C
5381	HETATM 4442 CAA HEM B 148 11.171 -12.750 21.554 1.00 21.16 C
5382	HETATM 4443 CBA HEM B 148 10.089 -13.674 21.941 1.00 27.78 C
5383	HETATM 4444 CGA HEM B 148 9.936 -14.643 23.585 1.00 59.12 C
5384	HETATM 4445 O1A HEM B 148 10.040 -13.299 24.151 1.00 44.32 O
5385	HETATM 4446 O2A HEM B 148 9.582 -15.171 23.405 1.00 46.16 O
5386	HETATM 4447 C1B HEM B 148 10.820 -11.284 15.524 1.00 10.36 C
5387	HETATM 4448 C2B HEM B 148 11.247 -11.528 14.048 1.00 7.33 C
5388	HETATM 4449 C3B HEM B 148 10.827 -10.448 13.495 1.00 15.63 C
5389	HETATM 4450 C4B HEM B 148 10.176 -9.458 14.534 1.00 15.33 C
5390	HETATM 4451 CMB HEM B 148 11.793 -12.748 13.802 1.00 14.96 C
5391	HETATM 4452 CAB HEM B 148 10.965 -10.083 11.934 1.00 19.63 C
5392	HETATM 4453 CBB HEM B 148 12.063 -10.466 11.288 1.00 39.39 C
5393	HETATM 4454 C1C HEM B 148 9.223 -7.280 15.193 1.00 14.39 C
5394	HETATM 4455 C2C HEM B 148 8.943 -5.947 14.698 1.00 10.78 C
5395	HETATM 4456 C3C HEM B 148 8.461 -5.188 15.934 1.00 10.68 C
5396	HETATM 4457 C4C HEM B 148 8.575 -6.422 16.809 1.00 8.70 C
5397	HETATM 4458 CMC HEM B 148 9.067 -5.306 13.381 1.00 13.95 C
5398	HETATM 4459 CAC HEM B 148 7.915 -3.899 16.132 1.00 11.87 C
5399	HETATM 4460 CBC HEM B 148 8.359 -2.863 15.599 1.00 12.63 C
5400	HETATM 4461 C1D HEM B 148 8.576 -7.046 19.346 1.00 18.32 C
5401	HETATM 4462 C2D HEM B 148 8.195 -6.791 20.753 1.00 15.48 C
5402	HETATM 4463 C3D HEM B 148 8.512 -8.051 21.256 1.00 14.57 C
5403	HETATM 4464 C4D HEM B 148 9.290 -8.905 20.340 1.00 20.76 C
5404	HETATM 4465 CMD HEM B 148 7.722 -5.449 21.269 1.00 27.50 C
5405	HETATM 4466 CAD HEM B 148 8.696 -7.989 22.865 1.00 13.85 C
5406	HETATM 4467 CBD HEM B 148 10.051 -7.739 23.453 1.00 17.11 C
5407	HETATM 4468 CGD HEM B 148 10.333 -8.222 25.219 1.00 27.09 C
5408	HETATM 4469 O1D HEM B 148 11.372 -7.572 25.386 1.00 27.49 O
5409	HETATM 4470 O2D HEM B 148 9.169 -8.132 25.625 1.00 23.65 O
5410	HETATM 4471 NA HEM B 148 10.260 -10.823 18.453 1.00 15.64 N
5411	HETATM 4472 NB HEM B 148 10.199 -10.051 15.722 1.00 12.71 N
5412	HETATM 4473 NC HEM B 148 9.104 -7.643 16.544 1.00 11.22 N
5413	HETATM 4474 ND HEM B 148 9.090 -8.239 19.067 1.00 16.72 N
5414	HETATM 4475 FE HEM B 148 9.333 -9.335 17.389 1.00 15.00 FE
5415	HETATM 4476 CHA HEM C 142 -8.630 7.776 18.352 1.00 18.96 C
5416	HETATM 4477 CHB HEM C 142 -10.320 10.048 14.384 1.00 20.49 C
5417	HETATM 4478 CHC HEM C 142 -8.304 6.446 11.794 1.00 15.25 C
5418	HETATM 4479 CHD HEM C 142 -6.900 4.052 15.698 1.00 14.70 C
5419	HETATM 4480 C1A HEM C 142 -9.195 8.664 17.417 1.00 16.72 C
5420	HETATM 4481 C2A HEM C 142 -10.045 9.791 17.916 1.00 15.73 C
5421	HETATM 4482 C3A HEM C 142 -10.613 10.462 16.942 1.00 17.27 C
5422	HETATM 4483 C4A HEM C 142 -10.077 9.749 15.710 1.00 12.07 C
5423	HETATM 4484 CMA HEM C 142 -11.422 11.658 16.756 1.00 31.88 C
5424	HETATM 4485 CAA HEM C 142 -10.321 10.351 19.308 1.00 24.60 C
5425	HETATM 4486 CBA HEM C 142 -9.201 11.341 19.696 1.00 36.28 C
5426	HETATM 4487 CGA HEM C 142 -10.014 12.024 21.724 1.00 43.70 C
5427	HETATM 4488 O1A HEM C 142 -9.511 10.786 22.089 1.00 38.93 O
5428	HETATM 4489 O2A HEM C 142 -9.503 12.583 21.415 1.00 46.28 O
5429	HETATM 4490 C1B HEM C 142 -9.882 9.419 13.260 1.00 18.45 C
5430	HETATM 4491 C2B HEM C 142 -10.342 9.474 11.782 1.00 12.95 C
5431	HETATM 4492 C3B HEM C 142 -9.631 8.558 11.160 1.00 12.49 C
5432	HETATM 4493 C4B HEM C 142 -8.945 7.665 12.157 1.00 8.33 C
5433	HETATM 4494 CMB HEM C 142 -11.015 10.631 11.441 1.00 15.16 C
5434	HETATM 4495 CAB HEM C 142 -9.701 8.335 9.552 1.00 21.83 C
5435	HETATM 4496 CBB HEM C 142 -10.742 8.875 9.052 1.00 33.11 C
5436	HETATM 4497 C1C HEM C 142 -7.751 5.629 12.596 1.00 15.97 C
5437	HETATM 4498 C2C HEM C 142 -7.320 4.232 12.130 1.00 9.41 C
5438	HETATM 4499 C3C HEM C 142 -6.879 3.543 13.304 1.00 11.73 C
5439	HETATM 4500 C4C HEM C 142 -7.009 4.441 14.484 1.00 15.36 C
5440	HETATM 4501 CMC HEM C 142 -7.210 3.774 10.722 1.00 13.23 C
5441	HETATM 4502 CAC HEM C 142 -6.459 2.233 13.437 1.00 19.55 C
5442	HETATM 4503 CBC HEM C 142 -6.761 1.082 12.572 1.00 14.52 C
5443	HETATM 4504 C1D HEM C 142 -7.305 4.996 16.751 1.00 11.54 C
5444	HETATM 4505 C2D HEM C 142 -6.959 4.620 18.250 1.00 12.94 C
5445	HETATM 4506 C3D HEM C 142 -7.527 5.654 18.907 1.00 11.38 C
5446	HETATM 4507 C4D HEM C 142 -7.947 6.663 18.081 1.00 11.29 C
5447	HETATM 4508 CMD HEM C 142 -6.299 3.375 18.648 1.00 13.29 C
5448	HETATM 4509 CAD HEM C 142 -7.594 5.618 20.504 1.00 15.84 C
5449	HETATM 4510 CBD HEM C 142 -8.833 5.076 20.877 1.00 21.27 C
5450	HETATM 4511 CGD HEM C 142 -9.085 5.314 22.774 1.00 26.94 C
5451	HETATM 4512 O1D HEM C 142 -10.036 5.486 22.824 1.00 30.21 O
5452	HETATM 4513 O2D HEM C 142 -8.326 4.541 23.113 1.00 25.95 O
5453	HETATM 4514 NA HEM C 142 -9.276 8.702 16.089 1.00 16.55 N
5454	HETATM 4515 NB HEM C 142 -9.138 8.185 13.333 1.00 12.79 N
5455	HETATM 4516 NC HEM C 142 -7.518 5.627 13.990 1.00 12.28 N
5456	HETATM 4517 ND HEM C 142 -7.740 6.303 16.793 1.00 12.30 N
5457	HETATM 4518 FE HEM C 142 -8.129 7.348 15.002 1.00 16.89 FE
5458	HETATM 4519 P PO4 D 147 -6.147 -21.111 -3.332 1.00 31.17 P
5459	HETATM 4520 CHA HEM D 148 -9.813 -9.884 -20.599 1.00 19.84 C
5460	HETATM 4521 CHB HEM D 148 -11.252 -11.989 -16.610 1.00 16.61 C
5461	HETATM 4522 CHC HEM D 148 -9.951 -8.302 -14.119 1.00 13.93 C
5462	HETATM 4523 CHD HEM D 148 -8.200 -5.985 -18.127 1.00 15.88 C
5463	HETATM 4524 C1A HEM D 148 -10.428 -10.865 -19.783 1.00 28.09 C
5464	HETATM 4525 C2A HEM D 148 -11.318 -12.071 -20.258 1.00 22.30 C
5465	HETATM 4526 C3A HEM D 148 -11.693 -12.664 -19.188 1.00 22.59 C
5466	HETATM 4527 C4A HEM D 148 -11.051 -11.756 -18.004 1.00 25.38 C
5467	HETATM 4528 CMA HEM D 148 -12.566 -13.772 -18.973 1.00 20.23 C
5468	HETATM 4529 CAA HEM D 148 -11.486 -12.464 -21.884 1.00 19.24 C
5469	HETATM 4530 CBA HEM D 148 -10.405 -12.971 -22.194 1.00 50.08 C
5470	HETATM 4531 CGA HEM D 148 -9.805 -13.296 -24.484 1.00 47.00 C
5471	HETATM 4532 O1A HEM D 148 -11.117 -13.581 -24.158 1.00 49.99 O
5472	HETATM 4533 O2A HEM D 148 -9.172 -14.946 -24.346 1.00 55.24 O
5473	HETATM 4534 C1B HEM D 148 -10.937 -11.332 -15.462 1.00 14.32 C
5474	HETATM 4535 C2B HEM D 148 -11.232 -11.509 -14.176 1.00 15.75 C
5475	HETATM 4536 C3B HEM D 148 -10.801 -10.525 -13.479 1.00 14.95 C
5476	HETATM 4537 C4B HEM D 148 -10.217 -9.585 -14.421 1.00 12.78 C
5477	HETATM 4538 CMB HEM D 148 -11.799 -12.726 -13.757 1.00 18.74 C
5478	HETATM 4539 CAB HEM D 148 -10.869 -10.291 -11.895 1.00 16.19 C
5479	HETATM 4540 CBB HEM D 148 -11.756 -10.396 -11.494 1.00 34.22 C
5480	HETATM 4541 C1C HEM D 148 -9.469 -7.417 -14.891 1.00 14.15 C
5481	HETATM 4542 C2C HEM D 148 -8.915 -5.898 -14.609 1.00 16.84 C
5482	HETATM 4543 C3C HEM D 148 -8.353 -5.322 -15.741 1.00 13.21 C
5483	HETATM 4544 C4C HEM D 148 -8.605 -6.360 -16.751 1.00 15.07 C
5484	HETATM 4545 CMC HEM D 148 -9.128 -5.229 -13.166 1.00 18.77 C
5485	HETATM 4546 CAC HEM D 148 -7.843 -4.077 -15.916 1.00 13.84 C
5486	HETATM 4547 CBC HEM D 148 -8.331 -3.032 -15.408 1.00 20.77 C
5487	HETATM 4548 C1D HEM D 148 -8.465 -7.065 -19.281 1.00 18.28 C
5488	HETATM 4549 C2D HEM D 148 -8.394 -6.595 -20.574 1.00 20.40 C
5489	HETATM 4550 C3D HEM D 148 -8.861 -7.841 -21.341 1.00 19.16 C
5490	HETATM 4551 C4D HEM D 148 -9.573 -8.702 -20.531 1.00 19.80 C
5491	HETATM 4552 CMD HEM D 148 -7.686 -5.397 -21.106 1.00 25.65 C
5492	HETATM 4553 CAD HEM D 148 -8.956 -7.733 -22.890 1.00 23.94 C
5493	HETATM 4554 CBD HEM D 148 -10.040 -6.949 -23.304 1.00 45.78 C
5494	HETATM 4555 CGD HEM D 148 -10.579 -7.365 -25.200 1.00 48.49 C
5495	HETATM 4556 O1D HEM D 148 -9.907 -5.916 -25.395 1.00 40.71 O
5496	HETATM 4557 O2D HEM D 148 -9.982 -7.978 -25.490 1.00 45.79 O
5497	HETATM 4558 NA HEM D 148 -10.454 -10.804 -18.459 1.00 15.98 N
5498	HETATM 4559 NB HEM D 148 -10.364 -9.999 -15.688 1.00 14.27 N
5499	HETATM 4560 NC HEM D 148 -9.228 -7.489 -16.235 1.00 12.21 N
5500	HETATM 4561 ND HEM D 148 -9.282 -8.209 -19.162 1.00 12.94 N
5501	HETATM 4562 FE HEM D 148 -9.504 -9.265 -17.387 1.00 15.46 FE
5502	HETATM 4563 O HOH A 143 27.864 0.667 0.584 1.00 21.15 O
5503	HETATM 4564 O HOH A 144 10.459 5.072 -14.201 1.00 29.96 O
5504	HETATM 4565 O HOH A 145 17.782 -1.325 -26.109 1.00 23.65 O
5505	HETATM 4566 O HOH A 146 13.825 2.114 3.861 1.00 23.17 O
5506	HETATM 4567 O HOH A 147 16.741 12.813 9.083 1.00 26.86 O
5507	HETATM 4568 O HOH A 148 22.374 9.235 11.515 1.00 30.53 O
5508	HETATM 4569 O HOH A 149 25.903 -1.921 -7.245 1.00 27.68 O
5509	HETATM 4570 O HOH A 150 11.472 3.167 0.508 1.00 27.27 O
5510	HETATM 4571 O HOH A 151 30.661 6.822 -0.101 1.00 29.31 O
5511	HETATM 4572 O HOH A 152 -3.585 1.717 -5.969 1.00 29.54 O
5512	HETATM 4573 O HOH A 153 32.341 10.298 6.014 1.00 35.74 O
5513	HETATM 4574 O HOH A 154 34.406 10.442 4.080 1.00 31.58 O
5514	HETATM 4575 O HOH A 155 30.017 0.297 -1.177 1.00 37.73 O
5515	HETATM 4576 O HOH A 156 21.428 14.396 -13.024 1.00 37.58 O
5516	HETATM 4577 O HOH A 157 10.103 6.463 -0.224 1.00 29.83 O
5517	HETATM 4578 O HOH A 158 28.011 -0.672 -5.493 1.00 34.75 O
5518	HETATM 4579 O HOH A 159 12.221 6.676 -21.742 1.00 35.95 O
5519	HETATM 4580 O HOH A 160 0.070 13.369 -11.506 1.00 27.36 O
5520	HETATM 4581 O HOH A 161 6.073 -7.542 -8.224 1.00 27.80 O
5521	HETATM 4582 O HOH A 162 0.959 -1.910 -19.919 1.00 29.65 O
5522	HETATM 4583 O HOH A 163 -5.435 9.067 -14.288 1.00 30.27 O
5523	HETATM 4584 O HOH A 164 3.108 18.897 -10.351 1.00 37.13 O
5524	HETATM 4585 O HOH A 165 9.253 2.690 -0.595 1.00 31.92 O
5525	HETATM 4586 O HOH A 166 3.509 1.516 -20.390 1.00 30.86 O
5526	HETATM 4587 O HOH A 167 7.323 6.472 -2.528 1.00 34.91 O
5527	HETATM 4588 O HOH A 168 8.069 21.100 -2.836 1.00 34.13 O
5528	HETATM 4589 O HOH A 169 22.069 5.076 -17.599 1.00 36.10 O
5529	HETATM 4590 O HOH A 170 12.511 23.031 -13.238 1.00 37.77 O
5530	HETATM 4591 O HOH A 171 27.846 5.439 7.283 1.00 39.01 O
5531	HETATM 4592 O HOH A 172 16.593 -6.697 -7.432 1.00 35.74 O
5532	HETATM 4593 O HOH A 173 19.969 -3.554 -17.319 1.00 36.03 O
5533	HETATM 4594 O HOH A 174 14.440 13.918 -17.292 1.00 34.06 O
5534	HETATM 4595 O HOH A 175 30.151 3.417 -5.741 1.00 35.04 O
5535	HETATM 4596 O HOH A 176 8.360 5.321 2.557 1.00 38.02 O
5536	HETATM 4597 O HOH A 177 -6.479 11.748 -17.967 1.00 39.72 O
5537	HETATM 4598 O HOH A 178 8.608 18.432 -15.341 1.00 36.40 O
5538	HETATM 4599 O HOH A 179 13.827 13.620 8.994 1.00 37.52 O
5539	HETATM 4600 O HOH A 180 16.070 12.039 11.262 1.00 38.53 O
5540	HETATM 4601 O HOH A 181 2.747 5.937 -4.128 1.00 42.85 O
5541	HETATM 4602 O HOH A 182 7.523 20.881 -15.648 1.00 39.27 O
5542	HETATM 4603 O HOH A 183 11.712 -10.960 -5.769 1.00 38.61 O
5543	HETATM 4604 O HOH A 184 30.119 4.139 -8.587 1.00 34.80 O
5544	HETATM 4605 O HOH A 185 25.533 1.205 -11.184 1.00 42.30 O
5545	HETATM 4606 O HOH A 186 -4.812 12.384 -7.265 1.00 38.29 O
5546	HETATM 4607 O HOH A 187 23.809 19.925 1.758 1.00 39.37 O
5547	HETATM 4608 O HOH A 188 26.015 11.766 5.159 1.00 40.95 O
5548	HETATM 4609 O HOH A 189 14.639 24.823 -4.300 1.00 41.35 O
5549	HETATM 4610 O HOH A 190 14.903 5.393 -23.047 1.00 37.45 O
5550	HETATM 4611 O HOH A 191 16.650 -5.137 -16.717 1.00 39.12 O
5551	HETATM 4612 O HOH A 192 7.424 -6.700 -20.085 1.00 38.62 O
5552	HETATM 4613 O HOH A 193 23.120 -3.118 -12.992 1.00 37.05 O
5553	HETATM 4614 O HOH A 194 23.664 0.968 -14.389 1.00 36.25 O
5554	HETATM 4615 O HOH A 195 25.698 7.981 -15.362 1.00 35.85 O
5555	HETATM 4616 O HOH A 196 30.009 16.347 -6.794 1.00 37.62 O
5556	HETATM 4617 O HOH A 197 27.728 16.677 -1.376 1.00 42.54 O
5557	HETATM 4618 O HOH A 198 8.142 18.836 1.041 1.00 39.90 O
5558	HETATM 4619 O HOH B 149 0.093 -2.470 16.222 1.00 21.64 O
5559	HETATM 4620 O HOH B 150 -5.404 -9.289 14.863 1.00 29.94 O
5560	HETATM 4621 O HOH B 151 17.543 -13.863 -8.044 1.00 26.33 O
5561	HETATM 4622 O HOH B 152 10.126 -8.396 -0.639 1.00 27.87 O
5562	HETATM 4623 O HOH B 153 25.765 -4.888 -7.482 1.00 33.60 O
5563	HETATM 4624 O HOH B 154 31.028 -6.924 -0.005 1.00 27.86 O
5564	HETATM 4625 O HOH B 155 10.572 -9.505 7.329 1.00 34.89 O
5565	HETATM 4626 O HOH B 156 2.908 -19.221 10.523 1.00 29.82 O
5566	HETATM 4627 O HOH B 157 27.245 -11.383 -5.263 1.00 34.30 O
5567	HETATM 4628 O HOH B 158 5.726 -17.664 4.076 1.00 29.36 O
5568	HETATM 4629 O HOH B 159 30.677 -1.382 -3.264 1.00 34.23 O
5569	HETATM 4630 O HOH B 160 21.396 -19.202 9.299 1.00 34.06 O
5570	HETATM 4631 O HOH B 161 3.400 -4.625 22.878 1.00 34.98 O
5571	HETATM 4632 O HOH B 162 23.029 7.858 13.868 1.00 34.02 O
5572	HETATM 4633 O HOH B 163 10.054 0.537 2.970 1.00 33.29 O
5573	HETATM 4634 O HOH B 164 16.523 -14.815 19.144 1.00 32.12 O
5574	HETATM 4635 O HOH B 165 -3.521 -7.996 18.788 1.00 35.56 O
5575	HETATM 4636 O HOH B 166 9.429 -6.067 3.140 1.00 34.98 O
5576	HETATM 4637 O HOH B 167 25.800 -14.208 -2.740 1.00 37.65 O
5577	HETATM 4638 O HOH B 168 0.313 -14.430 5.859 1.00 34.45 O
5578	HETATM 4639 O HOH B 169 25.879 -15.224 10.033 1.00 33.37 O
5579	HETATM 4640 O HOH B 170 35.602 -4.153 -9.289 1.00 35.71 O
5580	HETATM 4641 O HOH B 171 20.781 6.254 23.632 1.00 38.68 O
5581	HETATM 4642 O HOH B 172 21.800 -18.543 12.994 1.00 40.56 O
5582	HETATM 4643 O HOH B 173 7.807 -19.735 16.230 1.00 34.56 O
5583	HETATM 4644 O HOH B 174 -2.047 -12.487 30.048 1.00 36.28 O
5584	HETATM 4645 O HOH B 175 13.681 -7.349 23.790 1.00 31.60 O
5585	HETATM 4646 O HOH B 176 24.831 -18.968 5.896 1.00 34.00 O
5586	HETATM 4647 O HOH B 177 5.475 -5.297 23.977 1.00 36.71 O
5587	HETATM 4648 O HOH B 178 15.904 -5.466 24.689 1.00 34.84 O
5588	HETATM 4649 O HOH B 179 22.123 0.182 16.584 1.00 33.20 O
5589	HETATM 4650 O HOH B 180 19.207 -15.705 -9.408 1.00 37.19 O
5590	HETATM 4651 O HOH B 181 25.174 -12.029 -8.381 1.00 35.87 O
5591	HETATM 4652 O HOH B 182 -10.362 -13.333 12.465 1.00 36.08 O
5592	HETATM 4653 O HOH B 183 12.092 8.997 23.297 1.00 38.22 O
5593	HETATM 4654 O HOH B 184 7.727 5.204 22.116 1.00 43.17 O
5594	HETATM 4655 O HOH B 185 30.137 -14.006 10.129 1.00 36.03 O
5595	HETATM 4656 O HOH B 186 13.730 -18.833 14.202 1.00 39.57 O
5596	HETATM 4657 O HOH B 187 22.379 8.870 23.585 1.00 37.45 O
5597	HETATM 4658 O HOH B 188 -4.205 -14.646 8.671 1.00 38.65 O
5598	HETATM 4659 O HOH B 189 12.589 14.261 19.653 1.00 36.93 O
5599	HETATM 4660 O HOH B 190 24.652 6.230 17.996 1.00 42.01 O
5600	HETATM 4661 O HOH B 191 8.775 -23.438 16.055 1.00 42.33 O
5601	HETATM 4662 O HOH B 192 -7.480 -10.898 17.998 1.00 38.06 O
5602	HETATM 4663 O HOH B 193 11.388 -11.044 24.763 1.00 39.34 O
5603	HETATM 4664 O HOH B 194 3.735 -3.643 2.734 1.00 42.17 O
5604	HETATM 4665 O HOH B 195 3.149 -0.692 2.083 1.00 41.40 O
5605	HETATM 4666 O HOH B 196 4.511 -25.886 13.006 1.00 39.83 O
5606	HETATM 4667 O HOH B 197 8.712 -21.655 3.577 1.00 43.08 O
5607	HETATM 4668 O HOH B 198 22.926 -4.304 24.079 1.00 38.10 O
5608	HETATM 4669 O HOH B 199 11.435 9.654 20.618 1.00 40.23 O
5609	HETATM 4670 O HOH B 200 18.099 5.542 27.744 1.00 39.03 O
5610	HETATM 4671 O HOH B 201 12.174 9.951 9.804 1.00 44.34 O
5611	HETATM 4672 O HOH B 202 24.745 -2.501 15.270 1.00 39.78 O
5612	HETATM 4673 O HOH B 203 24.231 0.100 14.764 1.00 42.94 O
5613	HETATM 4674 O HOH B 204 23.324 -18.136 10.981 1.00 53.60 O
5614	HETATM 4675 O HOH B 205 25.576 -22.211 6.309 1.00 45.18 O
5615	HETATM 4676 O HOH C 143 -2.661 -3.608 9.261 1.00 21.26 O
5616	HETATM 4677 O HOH C 144 0.111 13.200 11.373 1.00 21.54 O
5617	HETATM 4678 O HOH C 145 -16.704 12.691 -9.201 1.00 23.30 O
5618	HETATM 4679 O HOH C 146 -13.774 2.466 -4.032 1.00 22.15 O
5619	HETATM 4680 O HOH C 147 5.273 9.077 14.193 1.00 28.02 O
5620	HETATM 4681 O HOH C 148 -11.466 3.494 -0.405 1.00 32.97 O
5621	HETATM 4682 O HOH C 149 -10.454 4.898 14.327 1.00 33.04 O
5622	HETATM 4683 O HOH C 150 -7.824 6.701 2.273 1.00 27.40 O
5623	HETATM 4684 O HOH C 151 -1.248 -1.596 20.098 1.00 29.84 O
5624	HETATM 4685 O HOH C 152 2.150 -0.244 14.446 1.00 30.74 O
5625	HETATM 4686 O HOH C 153 -2.060 18.771 19.773 1.00 29.22 O
5626	HETATM 4687 O HOH C 154 -21.154 14.002 13.362 1.00 32.40 O
5627	HETATM 4688 O HOH C 155 -9.105 3.030 0.663 1.00 28.46 O
5628	HETATM 4689 O HOH C 156 0.739 12.802 4.676 1.00 38.51 O
5629	HETATM 4690 O HOH C 157 -8.549 18.107 15.436 1.00 35.20 O
5630	HETATM 4691 O HOH C 158 -3.358 1.489 20.400 1.00 39.88 O
5631	HETATM 4692 O HOH C 159 -2.351 -4.643 6.766 1.00 36.39 O
5632	HETATM 4693 O HOH C 160 -9.995 6.820 0.255 1.00 29.81 O
5633	HETATM 4694 O HOH C 161 -1.621 21.259 16.530 1.00 33.74 O
5634	HETATM 4695 O HOH C 162 -5.469 23.850 15.062 1.00 31.03 O
5635	HETATM 4696 O HOH C 163 3.572 1.751 6.044 1.00 29.72 O
5636	HETATM 4697 O HOH C 164 -12.295 6.520 21.611 1.00 31.11 O
5637	HETATM 4698 O HOH C 165 -14.251 13.845 17.234 1.00 30.77 O
5638	HETATM 4699 O HOH C 166 -17.414 -5.952 27.962 1.00 34.94 O
5639	HETATM 4700 O HOH C 167 -3.547 16.435 20.027 1.00 34.58 O
5640	HETATM 4701 O HOH C 168 -16.355 -6.652 7.174 1.00 37.69 O
5641	HETATM 4702 O HOH C 169 -7.541 12.855 -2.773 1.00 34.39 O
5642	HETATM 4703 O HOH C 170 -4.225 9.070 1.455 1.00 35.72 O
5643	HETATM 4704 O HOH C 171 -25.974 -1.828 7.173 1.00 32.50 O
5644	HETATM 4705 O HOH C 172 -9.581 -6.364 21.942 1.00 37.91 O
5645	HETATM 4706 O HOH C 173 -14.874 4.521 23.126 1.00 36.81 O
5646	HETATM 4707 O HOH C 174 -15.534 20.875 -10.339 1.00 37.83 O
5647	HETATM 4708 O HOH C 175 -8.242 21.385 2.969 1.00 35.70 O
5648	HETATM 4709 O HOH C 176 -5.634 24.523 6.954 1.00 37.22 O
5649	HETATM 4710 O HOH C 177 -22.981 14.501 -8.660 1.00 34.30 O
5650	HETATM 4711 O HOH C 178 -13.871 16.688 -10.143 1.00 36.92 O
5651	HETATM 4712 O HOH C 179 -20.275 19.235 8.097 1.00 34.30 O
5652	HETATM 4713 O HOH C 180 1.720 15.273 3.670 1.00 39.46 O
5653	HETATM 4714 O HOH C 181 -2.824 18.993 10.315 1.00 37.49 O
5654	HETATM 4715 O HOH C 182 -2.160 0.091 22.111 1.00 39.39 O
5655	HETATM 4716 O HOH C 183 7.922 12.037 14.216 1.00 34.40 O
5656	HETATM 4717 O HOH C 184 -2.698 5.986 4.174 1.00 37.01 O
5657	HETATM 4718 O HOH C 185 6.321 10.115 3.931 1.00 35.17 O
5658	HETATM 4719 O HOH C 186 -7.096 21.140 15.539 1.00 35.39 O
5659	HETATM 4720 O HOH C 187 -10.581 17.364 16.459 1.00 39.95 O
5660	HETATM 4721 O HOH C 188 -4.668 13.050 -0.747 1.00 39.36 O
5661	HETATM 4722 O HOH C 189 -4.764 -6.228 5.515 1.00 40.89 O
5662	HETATM 4723 O HOH C 190 4.693 12.083 7.558 1.00 40.24 O
5663	HETATM 4724 O HOH C 191 -4.731 16.453 2.295 1.00 36.37 O
5664	HETATM 4725 O HOH C 192 -1.055 11.866 -0.448 1.00 43.19 O
5665	HETATM 4726 O HOH C 193 -18.517 -8.355 15.267 1.00 35.55 O
5666	HETATM 4727 O HOH C 194 6.547 9.706 16.296 1.00 41.86 O
5667	HETATM 4728 O HOH C 195 0.029 22.606 14.164 1.00 43.02 O
5668	HETATM 4729 O HOH C 196 -11.367 0.306 28.463 1.00 44.30 O
5669	HETATM 4730 O HOH C 197 -19.950 -10.635 14.301 1.00 40.17 O
5670	HETATM 4731 O HOH C 198 -7.047 -6.324 20.098 1.00 36.98 O
5671	HETATM 4732 O HOH C 199 -23.876 1.108 14.102 1.00 33.31 O
5672	HETATM 4733 O HOH C 200 -34.199 8.033 11.037 1.00 40.72 O
5673	HETATM 4734 O HOH C 201 -14.173 13.393 -8.778 1.00 43.21 O
5674	HETATM 4735 O HOH D 149 0.061 -2.494 -16.397 1.00 18.64 O
5675	HETATM 4736 O HOH D 150 -8.041 -19.581 -16.153 1.00 26.28 O
5676	HETATM 4737 O HOH D 151 2.825 -3.769 -9.602 1.00 23.08 O
5677	HETATM 4738 O HOH D 152 -2.494 -0.118 -14.151 1.00 25.33 O
5678	HETATM 4739 O HOH D 153 -9.792 -8.060 0.750 1.00 30.48 O
5679	HETATM 4740 O HOH D 154 -6.518 -22.534 -15.665 1.00 34.60 O
5680	HETATM 4741 O HOH D 155 -17.398 -13.549 8.357 1.00 35.82 O
5681	HETATM 4742 O HOH D 156 5.350 -9.378 -15.018 1.00 27.68 O
5682	HETATM 4743 O HOH D 157 -6.300 -24.347 -19.100 1.00 35.93 O
5683	HETATM 4744 O HOH D 158 -9.520 7.447 -21.130 1.00 40.04 O
5684	HETATM 4745 O HOH D 159 -16.425 -5.250 -24.764 1.00 32.57 O
5685	HETATM 4746 O HOH D 160 -7.987 -14.493 1.146 1.00 34.30 O
5686	HETATM 4747 O HOH D 161 -3.890 0.572 -11.856 1.00 34.78 O
5687	HETATM 4748 O HOH D 162 -29.504 -0.198 -4.474 1.00 38.63 O
5688	HETATM 4749 O HOH D 163 -25.631 -15.732 -9.906 1.00 33.22 O
5689	HETATM 4750 O HOH D 164 -2.623 -18.453 -21.128 1.00 35.47 O
5690	HETATM 4751 O HOH D 165 -2.780 -19.130 -10.800 1.00 30.23 O
5691	HETATM 4752 O HOH D 166 -25.734 -4.456 7.605 1.00 34.33 O
5692	HETATM 4753 O HOH D 167 -11.771 -10.816 5.496 1.00 38.68 O
5693	HETATM 4754 O HOH D 168 -9.924 0.291 -2.970 1.00 38.71 O
5694	HETATM 4755 O HOH D 169 -25.514 -14.066 2.449 1.00 36.60 O
5695	HETATM 4756 O HOH D 170 -5.455 -17.392 -4.316 1.00 34.43 O
5696	HETATM 4757 O HOH D 171 2.688 -11.418 -8.564 1.00 35.73 O
5697	HETATM 4758 O HOH D 172 7.091 -10.993 -18.224 1.00 32.39 O
5698	HETATM 4759 O HOH D 173 -9.377 -6.399 -3.029 1.00 35.44 O
5699	HETATM 4760 O HOH D 174 -16.565 -17.782 -17.506 1.00 41.02 O
5700	HETATM 4761 O HOH D 175 -8.141 -3.463 -24.390 1.00 37.14 O
5701	HETATM 4762 O HOH D 176 -16.560 -15.177 -19.016 1.00 34.89 O
5702	HETATM 4763 O HOH D 177 3.477 -8.048 -19.033 1.00 35.94 O
5703	HETATM 4764 O HOH D 178 -24.698 -11.573 8.724 1.00 38.01 O
5704	HETATM 4765 O HOH D 179 2.193 -4.435 -6.557 1.00 38.51 O
5705	HETATM 4766 O HOH D 180 -29.898 -16.926 -2.135 1.00 36.37 O
5706	HETATM 4767 O HOH D 181 -7.374 8.034 -17.831 1.00 34.05 O
5707	HETATM 4768 O HOH D 182 -24.015 0.401 -15.301 1.00 39.14 O
5708	HETATM 4769 O HOH D 183 -12.141 9.790 -10.238 1.00 38.30 O
5709	HETATM 4770 O HOH D 184 -5.765 -3.569 -23.682 1.00 36.68 O
5710	HETATM 4771 O HOH D 185 -4.860 -9.811 -2.967 1.00 37.10 O
5711	HETATM 4772 O HOH D 186 -23.107 -4.490 -24.359 1.00 37.97 O
5712	HETATM 4773 O HOH D 187 -10.377 -9.632 -7.043 1.00 38.85 O
5713	HETATM 4774 O HOH D 188 -7.871 -9.078 2.406 1.00 43.37 O
5714	HETATM 4775 O HOH D 189 -27.610 -10.991 5.353 1.00 43.46 O
5715	HETATM 4776 O HOH D 190 -14.034 2.806 -30.367 1.00 41.77 O
5716	HETATM 4777 O HOH D 191 -32.905 -9.033 0.480 1.00 43.68 O
5717	HETATM 4778 O HOH D 192 -28.749 -13.315 1.938 1.00 45.36 O
5718	HETATM 4779 O HOH D 193 0.516 -8.074 -26.354 1.00 41.53 O
5719	HETATM 4780 O HOH D 194 -20.080 -9.873 -22.862 1.00 36.25 O
5720	HETATM 4781 O HOH D 195 -13.442 9.778 -13.572 1.00 39.70 O
5721	HETATM 4782 O HOH D 196 -24.804 -2.608 -15.488 1.00 37.79 O
5722	HETATM 4783 O HOH D 197 -1.263 -2.837 -21.251 1.00 45.10 O
5723	CONECT 650 4431
5724	CONECT 1771 4475
5725	CONECT 2844 4518
5726	CONECT 3965 4562
5727	CONECT 4389 4393 4420
5728	CONECT 4390 4396 4403
5729	CONECT 4391 4406 4410
5730	CONECT 4392 4413 4417
5731	CONECT 4393 4389 4394 4427
5732	CONECT 4394 4393 4395 4398
5733	CONECT 4395 4394 4396 4397
5734	CONECT 4396 4390 4395 4427
5735	CONECT 4397 4395
5736	CONECT 4398 4394 4399
5737	CONECT 4399 4398 4400
5738	CONECT 4400 4399 4401 4402
5739	CONECT 4401 4400
5740	CONECT 4402 4400
5741	CONECT 4403 4390 4404 4428
5742	CONECT 4404 4403 4405 4407
5743	CONECT 4405 4404 4406 4408
5744	CONECT 4406 4391 4405 4428
5745	CONECT 4407 4404
5746	CONECT 4408 4405 4409
5747	CONECT 4409 4408
5748	CONECT 4410 4391 4411 4429
5749	CONECT 4411 4410 4412 4414
5750	CONECT 4412 4411 4413 4415
5751	CONECT 4413 4392 4412 4429
5752	CONECT 4414 4411
5753	CONECT 4415 4412 4416
5754	CONECT 4416 4415
5755	CONECT 4417 4392 4418 4430
5756	CONECT 4418 4417 4419 4421
5757	CONECT 4419 4418 4420 4422
5758	CONECT 4420 4389 4419 4430
5759	CONECT 4421 4418
5760	CONECT 4422 4419 4423
5761	CONECT 4423 4422 4424
5762	CONECT 4424 4423 4425 4426
5763	CONECT 4425 4424
5764	CONECT 4426 4424
5765	CONECT 4427 4393 4396 4431
5766	CONECT 4428 4403 4406 4431
5767	CONECT 4429 4410 4413 4431
5768	CONECT 4430 4417 4420 4431
5769	CONECT 4431 650 4427 4428 4429
5770	CONECT 4431 4430
5771	CONECT 4433 4437 4464
5772	CONECT 4434 4440 4447
5773	CONECT 4435 4450 4454
5774	CONECT 4436 4457 4461
5775	CONECT 4437 4433 4438 4471
5776	CONECT 4438 4437 4439 4442
5777	CONECT 4439 4438 4440 4441
5778	CONECT 4440 4434 4439 4471
5779	CONECT 4441 4439
5780	CONECT 4442 4438 4443
5781	CONECT 4443 4442 4444
5782	CONECT 4444 4443 4445 4446
5783	CONECT 4445 4444
5784	CONECT 4446 4444
5785	CONECT 4447 4434 4448 4472
5786	CONECT 4448 4447 4449 4451
5787	CONECT 4449 4448 4450 4452
5788	CONECT 4450 4435 4449 4472
5789	CONECT 4451 4448
5790	CONECT 4452 4449 4453
5791	CONECT 4453 4452
5792	CONECT 4454 4435 4455 4473
5793	CONECT 4455 4454 4456 4458
5794	CONECT 4456 4455 4457 4459
5795	CONECT 4457 4436 4456 4473
5796	CONECT 4458 4455
5797	CONECT 4459 4456 4460
5798	CONECT 4460 4459
5799	CONECT 4461 4436 4462 4474
5800	CONECT 4462 4461 4463 4465
5801	CONECT 4463 4462 4464 4466
5802	CONECT 4464 4433 4463 4474
5803	CONECT 4465 4462
5804	CONECT 4466 4463 4467
5805	CONECT 4467 4466 4468
5806	CONECT 4468 4467 4469 4470
5807	CONECT 4469 4468
5808	CONECT 4470 4468
5809	CONECT 4471 4437 4440 4475
5810	CONECT 4472 4447 4450 4475
5811	CONECT 4473 4454 4457 4475
5812	CONECT 4474 4461 4464 4475
5813	CONECT 4475 1771 4471 4472 4473
5814	CONECT 4475 4474
5815	CONECT 4476 4480 4507
5816	CONECT 4477 4483 4490
5817	CONECT 4478 4493 4497
5818	CONECT 4479 4500 4504
5819	CONECT 4480 4476 4481 4514
5820	CONECT 4481 4480 4482 4485
5821	CONECT 4482 4481 4483 4484
5822	CONECT 4483 4477 4482 4514
5823	CONECT 4484 4482
5824	CONECT 4485 4481 4486
5825	CONECT 4486 4485 4487
5826	CONECT 4487 4486 4488 4489
5827	CONECT 4488 4487
5828	CONECT 4489 4487
5829	CONECT 4490 4477 4491 4515
5830	CONECT 4491 4490 4492 4494
5831	CONECT 4492 4491 4493 4495
5832	CONECT 4493 4478 4492 4515
5833	CONECT 4494 4491
5834	CONECT 4495 4492 4496
5835	CONECT 4496 4495
5836	CONECT 4497 4478 4498 4516
5837	CONECT 4498 4497 4499 4501
5838	CONECT 4499 4498 4500 4502
5839	CONECT 4500 4479 4499 4516
5840	CONECT 4501 4498
5841	CONECT 4502 4499 4503
5842	CONECT 4503 4502
5843	CONECT 4504 4479 4505 4517
5844	CONECT 4505 4504 4506 4508
5845	CONECT 4506 4505 4507 4509
5846	CONECT 4507 4476 4506 4517
5847	CONECT 4508 4505
5848	CONECT 4509 4506 4510
5849	CONECT 4510 4509 4511
5850	CONECT 4511 4510 4512 4513
5851	CONECT 4512 4511
5852	CONECT 4513 4511
5853	CONECT 4514 4480 4483 4518
5854	CONECT 4515 4490 4493 4518
5855	CONECT 4516 4497 4500 4518
5856	CONECT 4517 4504 4507 4518
5857	CONECT 4518 2844 4514 4515 4516
5858	CONECT 4518 4517
5859	CONECT 4520 4524 4551
5860	CONECT 4521 4527 4534
5861	CONECT 4522 4537 4541
5862	CONECT 4523 4544 4548
5863	CONECT 4524 4520 4525 4558
5864	CONECT 4525 4524 4526 4529
5865	CONECT 4526 4525 4527 4528
5866	CONECT 4527 4521 4526 4558
5867	CONECT 4528 4526
5868	CONECT 4529 4525 4530
5869	CONECT 4530 4529 4531
5870	CONECT 4531 4530 4532 4533
5871	CONECT 4532 4531
5872	CONECT 4533 4531
5873	CONECT 4534 4521 4535 4559
5874	CONECT 4535 4534 4536 4538
5875	CONECT 4536 4535 4537 4539
5876	CONECT 4537 4522 4536 4559
5877	CONECT 4538 4535
5878	CONECT 4539 4536 4540
5879	CONECT 4540 4539
5880	CONECT 4541 4522 4542 4560
5881	CONECT 4542 4541 4543 4545
5882	CONECT 4543 4542 4544 4546
5883	CONECT 4544 4523 4543 4560
5884	CONECT 4545 4542
5885	CONECT 4546 4543 4547
5886	CONECT 4547 4546
5887	CONECT 4548 4523 4549 4561
5888	CONECT 4549 4548 4550 4552
5889	CONECT 4550 4549 4551 4553
5890	CONECT 4551 4520 4550 4561
5891	CONECT 4552 4549
5892	CONECT 4553 4550 4554
5893	CONECT 4554 4553 4555
5894	CONECT 4555 4554 4556 4557
5895	CONECT 4556 4555
5896	CONECT 4557 4555
5897	CONECT 4558 4524 4527 4562
5898	CONECT 4559 4534 4537 4562
5899	CONECT 4560 4541 4544 4562
5900	CONECT 4561 4548 4551 4562
5901	CONECT 4562 3965 4558 4559 4560
5902	CONECT 4562 4561
5903	MASTER 780 1 6 32 0 0 16 9 4779 4 180 46
5904	END

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