*** Oligopeptidase B de Trypanosoma cruzi ***
Job options:
ID = 21032523153321012
JOBID = Oligopeptidase B de Trypanosoma cruzi
USERID = unknown
PRIVAT = 0
NMODES = 10
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER Oligopeptidase B de Trypanosoma cruzi
HEADER HYDROLASE 23-MAY-13 4BP9
TITLE OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI WITH COVALENTLY BOUND
TITLE 2 ANTIPAIN - CLOSED FORM
CAVEAT 4BP9 OAR G 4 HAS WRONG CHIRALITY AT ATOM CA OAR H 4 HAS WRONG
CAVEAT 2 4BP9 CHIRALITY AT ATOM CA OAR I 4 HAS WRONG CHIRALITY AT ATOM CA
CAVEAT 3 4BP9 OAR J 4 HAS WRONG CHIRALITY AT ATOM CA OAR K 4 HAS WRONG
CAVEAT 4 4BP9 CHIRALITY AT ATOM CA OAR L 4 HAS WRONG CHIRALITY AT ATOM CA
CAVEAT 5 4BP9 OAR G 4 CA HAS THE WRONG CHIRALITY OAR H 4 CA HAS THE WRONG
CAVEAT 6 4BP9 CHIRALITY OAR I 4 CA HAS THE WRONG CHIRALITY OAR J 4 CA HAS
CAVEAT 7 4BP9 THE WRONG CHIRALITY OAR K 4 CA HAS THE WRONG CHIRALITY OAR
CAVEAT 8 4BP9 L 4 CA HAS THE WRONG CHIRALITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASSE B;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.4.21.83;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANTIPAIN;
COMPND 8 CHAIN: G, H, I, J, K, L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PRARE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ACTINOBACTERIA;
SOURCE 11 ORGANISM_TAXID: 1760
KEYWDS HYDROLASE, PROLYL OLIGOPEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CANNING,D.REA,R.MORTY,V.FULOP
REVDAT 6 10-JUL-19 4BP9 1 REMARK
REVDAT 5 15-MAY-19 4BP9 1 CAVEAT REMARK SEQRES LINK
REVDAT 4 13-SEP-17 4BP9 1 REMARK
REVDAT 3 18-JUN-14 4BP9 1 HETATM
REVDAT 2 19-MAR-14 4BP9 1 JRNL HETATM
REVDAT 1 12-FEB-14 4BP9 0
JRNL AUTH P.CANNING,D.REA,R.E.MORTY,V.FULOP
JRNL TITL CRYSTAL STRUCTURES OF TRYPANOSOMA BRUCEI OLIGOPEPTIDASE B
JRNL TITL 2 BROADEN THE PARADIGM OF CATALYTIC REGULATION IN PROLYL
JRNL TITL 3 OLIGOPEPTIDASE FAMILY ENZYMES.
JRNL REF PLOS ONE V. 8 79349 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 24265767
JRNL DOI 10.1371/JOURNAL.PONE.0079349
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 121891
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5162
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8894
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 379
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 34062
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 344
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.97000
REMARK 3 B22 (A**2) : 1.49000
REMARK 3 B33 (A**2) : 0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.69000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.436
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.381
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.636
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.882
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 34896 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47322 ; 1.697 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4254 ; 8.110 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1614 ;35.788 ;23.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5814 ;20.883 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 276 ;20.513 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5136 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26730 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 21210 ; 0.392 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34344 ; 0.774 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13686 ; 1.381 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12978 ; 2.302 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5900 121.8250 223.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.4167 T22: 0.6717
REMARK 3 T33: 0.3381 T12: 0.1220
REMARK 3 T13: 0.1576 T23: 0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 1.6990 L22: 2.1497
REMARK 3 L33: 2.5552 L12: 0.6199
REMARK 3 L13: -0.2926 L23: -0.7631
REMARK 3 S TENSOR
REMARK 3 S11: 0.1958 S12: 0.1253 S13: 0.4175
REMARK 3 S21: 0.3655 S22: 0.1841 S23: 0.5994
REMARK 3 S31: -0.5691 S32: -0.5266 S33: -0.3799
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 87 A 441
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7330 106.1900 248.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.4345 T22: 0.5750
REMARK 3 T33: 0.1617 T12: 0.0175
REMARK 3 T13: 0.0165 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 0.7974 L22: 0.9615
REMARK 3 L33: 1.3416 L12: 0.0510
REMARK 3 L13: 0.0312 L23: -0.1461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: -0.1981 S13: 0.0613
REMARK 3 S21: 0.2644 S22: 0.0492 S23: 0.0167
REMARK 3 S31: 0.0564 S32: 0.1057 S33: -0.0728
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 442 A 714
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6600 109.6620 220.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.3974 T22: 0.5619
REMARK 3 T33: 0.2233 T12: -0.0135
REMARK 3 T13: 0.0302 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.6979 L22: 1.3464
REMARK 3 L33: 1.2312 L12: 0.2719
REMARK 3 L13: -0.1035 L23: -0.0608
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: 0.0166 S13: 0.0967
REMARK 3 S21: 0.1000 S22: 0.0223 S23: 0.0333
REMARK 3 S31: 0.1256 S32: -0.0731 S33: -0.0654
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3490 140.4630 194.0850
REMARK 3 T TENSOR
REMARK 3 T11: 0.5018 T22: 0.5705
REMARK 3 T33: 0.1958 T12: 0.0926
REMARK 3 T13: 0.0635 T23: 0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 1.7073 L22: 2.2222
REMARK 3 L33: 1.7304 L12: 0.8004
REMARK 3 L13: -0.1787 L23: -0.3574
REMARK 3 S TENSOR
REMARK 3 S11: 0.1091 S12: 0.1983 S13: 0.2519
REMARK 3 S21: -0.0253 S22: -0.0500 S23: 0.3722
REMARK 3 S31: -0.5191 S32: -0.2990 S33: -0.0591
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2030 124.7900 182.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2849 T22: 0.9500
REMARK 3 T33: 0.1952 T12: -0.0171
REMARK 3 T13: 0.0462 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.6099 L22: 0.6688
REMARK 3 L33: 2.0683 L12: 0.1180
REMARK 3 L13: -0.1344 L23: 0.0305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0452 S12: 0.1562 S13: -0.0498
REMARK 3 S21: -0.0502 S22: -0.0286 S23: -0.0325
REMARK 3 S31: 0.0113 S32: 0.7632 S33: -0.0166
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 442 B 714
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7200 136.6320 204.7970
REMARK 3 T TENSOR
REMARK 3 T11: 0.5128 T22: 0.6435
REMARK 3 T33: 0.2551 T12: -0.0916
REMARK 3 T13: 0.0492 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.9062 L22: 0.6838
REMARK 3 L33: 1.5649 L12: 0.3395
REMARK 3 L13: 0.0004 L23: -0.0698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.0404 S13: 0.0281
REMARK 3 S21: 0.0167 S22: 0.0346 S23: 0.0325
REMARK 3 S31: -0.4014 S32: 0.2819 S33: -0.0665
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 86
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7850 42.3530 216.1690
REMARK 3 T TENSOR
REMARK 3 T11: 0.7079 T22: 0.7692
REMARK 3 T33: 0.3170 T12: -0.0160
REMARK 3 T13: 0.1993 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 2.9413 L22: 0.9072
REMARK 3 L33: 3.3626 L12: 0.4730
REMARK 3 L13: 1.5078 L23: 0.1774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 0.0353 S13: -0.5749
REMARK 3 S21: -0.1498 S22: -0.2024 S23: -0.1314
REMARK 3 S31: 0.7459 S32: -0.4066 S33: 0.1321
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 87 C 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3880 72.6490 198.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.8187 T22: 0.8194
REMARK 3 T33: 0.2041 T12: 0.2483
REMARK 3 T13: 0.0521 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.9881 L22: 0.6715
REMARK 3 L33: 1.8239 L12: 0.2944
REMARK 3 L13: -0.3279 L23: -0.1156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.3042 S13: 0.0102
REMARK 3 S21: -0.1385 S22: -0.0436 S23: 0.0142
REMARK 3 S31: -0.4683 S32: -0.5338 S33: 0.0241
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 442 C 714
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1420 57.7610 221.1940
REMARK 3 T TENSOR
REMARK 3 T11: 0.6350 T22: 0.9659
REMARK 3 T33: 0.2986 T12: 0.1006
REMARK 3 T13: 0.0615 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 0.8321 L22: 0.5125
REMARK 3 L33: 1.7825 L12: 0.1390
REMARK 3 L13: -0.3256 L23: 0.2134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0449 S12: 0.2659 S13: -0.0686
REMARK 3 S21: -0.1575 S22: -0.1292 S23: -0.0214
REMARK 3 S31: -0.0504 S32: -0.6442 S33: 0.0843
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 5 D 86
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6170 42.5170 255.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.6980 T22: 0.6300
REMARK 3 T33: 0.2937 T12: 0.1245
REMARK 3 T13: 0.2327 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 3.6422 L22: 1.1404
REMARK 3 L33: 3.2490 L12: 0.4076
REMARK 3 L13: 1.2411 L23: 0.1890
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.1410 S13: -0.4821
REMARK 3 S21: 0.1323 S22: -0.2149 S23: 0.1114
REMARK 3 S31: 0.9723 S32: 0.0914 S33: 0.2078
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 87 D 441
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0250 72.8510 272.8470
REMARK 3 T TENSOR
REMARK 3 T11: 0.5627 T22: 0.6474
REMARK 3 T33: 0.1901 T12: -0.0724
REMARK 3 T13: 0.0417 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.9444 L22: 0.9860
REMARK 3 L33: 1.8714 L12: -0.0542
REMARK 3 L13: -0.3010 L23: -0.1905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: -0.2001 S13: 0.0299
REMARK 3 S21: 0.1758 S22: -0.0754 S23: 0.0910
REMARK 3 S31: -0.3145 S32: 0.2250 S33: 0.0485
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 442 D 714
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2920 57.8150 250.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5541 T22: 0.7766
REMARK 3 T33: 0.3074 T12: 0.0411
REMARK 3 T13: 0.1055 T23: 0.1021
REMARK 3 L TENSOR
REMARK 3 L11: 0.6143 L22: 0.5319
REMARK 3 L33: 2.1111 L12: 0.1707
REMARK 3 L13: -0.5368 L23: 0.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.0999 S13: -0.0787
REMARK 3 S21: 0.0000 S22: -0.1351 S23: 0.0047
REMARK 3 S31: 0.0555 S32: 0.3940 S33: 0.1272
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 5 E 86
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0760 47.4680 159.1150
REMARK 3 T TENSOR
REMARK 3 T11: 0.3635 T22: 1.2215
REMARK 3 T33: 0.2785 T12: 0.1284
REMARK 3 T13: 0.0073 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 1.2776 L22: 0.9642
REMARK 3 L33: 6.0542 L12: 0.0100
REMARK 3 L13: -1.2905 L23: -0.2890
REMARK 3 S TENSOR
REMARK 3 S11: 0.1614 S12: 0.1644 S13: 0.0061
REMARK 3 S21: 0.1345 S22: 0.0118 S23: 0.3237
REMARK 3 S31: -0.5452 S32: -1.9389 S33: -0.1732
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 87 E 441
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4720 31.2900 183.9780
REMARK 3 T TENSOR
REMARK 3 T11: 0.7986 T22: 0.6169
REMARK 3 T33: 0.2453 T12: 0.1113
REMARK 3 T13: 0.0987 T23: 0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 1.1442 L22: 0.6682
REMARK 3 L33: 4.7127 L12: -0.0342
REMARK 3 L13: -1.0401 L23: -0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.2468 S12: -0.3082 S13: -0.1246
REMARK 3 S21: 0.2348 S22: 0.0687 S23: -0.0271
REMARK 3 S31: 1.0113 S32: 0.4200 S33: 0.1781
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 442 E 714
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8330 35.1570 155.3530
REMARK 3 T TENSOR
REMARK 3 T11: 0.6198 T22: 0.6742
REMARK 3 T33: 0.2601 T12: -0.1532
REMARK 3 T13: 0.1086 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.0216 L22: 0.6808
REMARK 3 L33: 5.1965 L12: 0.1705
REMARK 3 L13: -1.1195 L23: -0.2129
REMARK 3 S TENSOR
REMARK 3 S11: -0.2581 S12: 0.1592 S13: -0.0979
REMARK 3 S21: 0.0656 S22: 0.0642 S23: 0.0201
REMARK 3 S31: 0.8737 S32: -0.6651 S33: 0.1939
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 5 F 86
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4370 65.9230 129.6430
REMARK 3 T TENSOR
REMARK 3 T11: 0.8811 T22: 0.6564
REMARK 3 T33: 0.2072 T12: 0.1066
REMARK 3 T13: 0.0490 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 2.1089 L22: 2.5497
REMARK 3 L33: 4.8052 L12: 0.1485
REMARK 3 L13: -0.7594 L23: -0.0812
REMARK 3 S TENSOR
REMARK 3 S11: 0.1890 S12: 0.4240 S13: 0.2735
REMARK 3 S21: -0.0147 S22: -0.0471 S23: 0.2624
REMARK 3 S31: -1.5659 S32: -0.5421 S33: -0.1419
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 87 F 441
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9830 49.4520 118.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2921 T22: 1.4549
REMARK 3 T33: 0.2573 T12: -0.1609
REMARK 3 T13: 0.0550 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 0.5034 L22: 0.8560
REMARK 3 L33: 4.5782 L12: -0.0053
REMARK 3 L13: -0.2308 L23: -0.1363
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.0150 S13: -0.0005
REMARK 3 S21: -0.0182 S22: 0.0026 S23: -0.0323
REMARK 3 S31: -0.1926 S32: 1.8657 S33: 0.0046
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 442 F 714
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6280 61.7550 140.3490
REMARK 3 T TENSOR
REMARK 3 T11: 0.7467 T22: 0.7807
REMARK 3 T33: 0.2763 T12: -0.2802
REMARK 3 T13: 0.0675 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 0.8171 L22: 0.6648
REMARK 3 L33: 4.4124 L12: 0.0084
REMARK 3 L13: -0.4684 L23: -0.2158
REMARK 3 S TENSOR
REMARK 3 S11: 0.1334 S12: -0.0515 S13: 0.0705
REMARK 3 S21: 0.0852 S22: 0.0178 S23: -0.0570
REMARK 3 S31: -1.1722 S32: 0.8420 S33: -0.1512
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4BP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1290056998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127053
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 59.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.22000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 1.12000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: STARTING MODEL IS ALSO BEING CURRENTLY DEPOSITED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 4000, 0.2 M CALCIUM ACETATE,
REMARK 280 0.1 M SODIUM ACETATE PH 5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.40000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ANTIPAIN HYDROCHLORIDE IS A REVERSIBLE INHIBITOR OF SERINE/CYSTEINE
REMARK 400 PROTEASES AND SOME TRYPSIN-LIKE SERINE PROTEASES. ITS ACTION
REMARK 400 RESEMBLES LEUPEPTIN; HOWEVER, ITS PLASMIN INHIBITION IS LESS AND
REMARK 400 ITS CATHEPSIN A INHIBITION IS MORE THAN THAT OBSERVED WITH
REMARK 400 LEUPEPTIN. IT IS AN INHIBITOR OF TRYPSIN-LIKE PROTEASES
REMARK 400 (E.G. TRYPSIN, PAPAIN, CATHEPSIN B); CATHEPSIN A, A CARBOXYPEPTIDASE
REMARK 400 IS INHIBITED TOO, WHICH IS NOT TRUE FOR OTHER INHIBITORS FROM
REMARK 400 ACTINOMYCES.THE NAME IS DERIVED FROM ANTI-PAPAIN.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ANTIPAIN
REMARK 400 CHAIN: G, H, I, J, K, L
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 4
REMARK 400 DESCRIPTION: ANTIPAIN FORMS A COVALENT LINKAGE BETWEEN THE ARGINAL
REMARK 400 RESIDUE OF THE INHIBITOR AND SER RESIDUE OF THE
REMARK 400 PROTEIN.THE PROTEASE INHIBITOR ANTIPAIN INCREASES THE
REMARK 400 EFFECTIVENESSOF UV IRRADIATION ON CESSATION OF
REMARK 400 RESPIRATION AND CELL KILLING IN ESCHERICHIA COLI B/R
REMARK 400 CULTURES WITHOUT AFFECTING EXCISION OF PYRIMIDINE
REMARK 400 DIMERS. THE ACTIONS ARE SIMILAR TO THOSE CAUSED BY
REMARK 400 CYCLIC AMP IN IRRADIATED CULTURES.
REMARK 400
REMARK 400 THE ANTIPAIN IS OLIGOPEPTIDE, A MEMBER OF ENZYME INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ANTIPAIN
REMARK 400 CHAIN: G, H, I, J, K, L
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_2: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_3: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_4: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_5: PEPTIDE LIKE POLYMER
REMARK 400 COMPONENT_6: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 LYS A 715
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 LYS B 715
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 THR C 3
REMARK 465 GLU C 4
REMARK 465 LYS C 715
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 THR D 3
REMARK 465 GLU D 4
REMARK 465 LYS D 715
REMARK 465 MET E 1
REMARK 465 GLN E 2
REMARK 465 THR E 3
REMARK 465 GLU E 4
REMARK 465 LYS E 715
REMARK 465 MET F 1
REMARK 465 GLN F 2
REMARK 465 THR F 3
REMARK 465 GLU F 4
REMARK 465 LYS F 715
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 563 C OAR G 4 1.35
REMARK 500 OG SER D 563 C OAR J 4 1.35
REMARK 500 OG SER C 563 C OAR I 4 1.35
REMARK 500 OG SER F 563 C OAR L 4 1.35
REMARK 500 OG SER B 563 C OAR H 4 1.36
REMARK 500 OG SER E 563 C OAR K 4 1.38
REMARK 500 OH TYR E 444 OD1 ASP E 502 2.06
REMARK 500 OG SER C 563 O OAR I 4 2.06
REMARK 500 OG SER A 563 O OAR G 4 2.07
REMARK 500 OD1 ASP D 455 OG1 THR D 457 2.11
REMARK 500 OG SER D 563 O OAR J 4 2.11
REMARK 500 O GLY C 367 N ASP C 369 2.13
REMARK 500 NH2 ARG F 664 O VAL F 673 2.14
REMARK 500 ND2 ASN C 312 OG1 THR C 338 2.15
REMARK 500 O HIS B 381 NH2 ARG B 427 2.15
REMARK 500 OG SER F 563 O OAR L 4 2.16
REMARK 500 OG1 THR B 477 OG1 THR B 552 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO A 157 C - N - CD ANGL. DEV. = -17.3 DEGREES
REMARK 500 VAL A 350 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 TYR A 482 CA - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 GLY A 483 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG A 496 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 664 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 PRO B 157 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO B 157 C - N - CD ANGL. DEV. = -18.5 DEGREES
REMARK 500 LEU B 463 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 GLY B 483 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 ARG B 533 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 PRO C 157 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO C 157 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO D 156 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO D 157 C - N - CD ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO E 157 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU E 279 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 32 112.98 -160.89
REMARK 500 GLU A 88 89.02 60.71
REMARK 500 ASP A 99 -129.36 60.90
REMARK 500 ALA A 121 -57.64 -27.72
REMARK 500 GLU A 142 101.87 -27.60
REMARK 500 PRO A 156 162.68 -26.97
REMARK 500 PRO A 157 -74.67 29.46
REMARK 500 ARG A 180 26.25 38.32
REMARK 500 ASN A 199 39.26 37.94
REMARK 500 LYS A 208 -165.38 -67.25
REMARK 500 ALA A 210 126.45 -37.14
REMARK 500 MET A 281 140.22 -38.27
REMARK 500 VAL A 282 -76.17 -100.86
REMARK 500 PHE A 348 178.26 177.18
REMARK 500 PRO A 368 -32.80 -38.50
REMARK 500 SER A 394 8.46 -66.86
REMARK 500 MET A 411 -9.00 -50.75
REMARK 500 THR A 467 -10.40 -48.05
REMARK 500 TYR A 482 -91.72 -107.00
REMARK 500 TYR A 485 -14.94 63.44
REMARK 500 HIS A 511 59.36 -93.69
REMARK 500 TYR A 529 -136.05 44.47
REMARK 500 LEU A 530 22.77 -74.12
REMARK 500 SER A 563 -122.95 61.27
REMARK 500 VAL A 587 56.74 30.30
REMARK 500 ASP A 591 62.18 -102.00
REMARK 500 GLU A 610 -70.23 -125.56
REMARK 500 PHE A 620 -74.01 -37.44
REMARK 500 ALA A 634 96.84 -63.11
REMARK 500 HIS A 647 34.05 -97.82
REMARK 500 SER A 685 -91.55 -59.83
REMARK 500 ALA A 686 -69.42 65.62
REMARK 500 SER A 687 -174.41 -170.70
REMARK 500 ARG A 689 -150.04 -134.92
REMARK 500 ASN A 708 47.73 75.38
REMARK 500 ASN B 29 58.07 -153.34
REMARK 500 GLU B 88 87.23 56.32
REMARK 500 SER B 93 179.22 -52.68
REMARK 500 ASP B 99 -127.54 42.38
REMARK 500 ALA B 121 90.29 -59.18
REMARK 500 GLU B 142 96.10 -27.81
REMARK 500 CYS B 147 100.38 -160.06
REMARK 500 PRO B 156 180.00 -54.85
REMARK 500 PRO B 157 -75.21 29.55
REMARK 500 ASN B 199 55.26 27.68
REMARK 500 ASP B 214 96.23 -66.14
REMARK 500 ILE B 222 132.67 -39.56
REMARK 500 VAL B 274 -20.01 -33.66
REMARK 500 VAL B 282 -74.63 -95.28
REMARK 500 ASP B 308 32.17 72.67
REMARK 500
REMARK 500 THIS ENTRY HAS 263 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 156 PRO A 157 -129.12
REMARK 500 SER A 685 ALA A 686 -137.48
REMARK 500 PRO B 156 PRO B 157 -129.96
REMARK 500 TYR B 482 GLY B 483 -48.31
REMARK 500 SER B 685 ALA B 686 -135.86
REMARK 500 ASP B 688 ARG B 689 -147.02
REMARK 500 GLY C 110 LEU C 111 -149.94
REMARK 500 PRO C 156 PRO C 157 -126.69
REMARK 500 TYR C 482 GLY C 483 -30.80
REMARK 500 SER C 685 ALA C 686 -145.30
REMARK 500 PRO D 156 PRO D 157 -122.91
REMARK 500 TYR D 482 GLY D 483 -39.14
REMARK 500 PHE D 684 SER D 685 -148.12
REMARK 500 SER D 685 ALA D 686 -142.45
REMARK 500 PRO E 156 PRO E 157 -126.69
REMARK 500 SER E 685 ALA E 686 -134.11
REMARK 500 PRO F 156 PRO F 157 -132.58
REMARK 500 SER F 685 ALA F 686 -131.61
REMARK 500 ARG G 2 VAL G 3 -132.88
REMARK 500 ARG L 2 VAL L 3 -146.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG G 2 0.25 SIDE CHAIN
REMARK 500 ARG H 2 0.29 SIDE CHAIN
REMARK 500 ARG I 2 0.12 SIDE CHAIN
REMARK 500 ARG J 2 0.15 SIDE CHAIN
REMARK 500 ARG K 2 0.27 SIDE CHAIN
REMARK 500 ARG L 2 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ANTIPAIN: COVALENTLY BOUND TO THE CATALYTIC SER563
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN H OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN J OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN K OF ANTIPAIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN L OF ANTIPAIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BP8 RELATED DB: PDB
REMARK 900 OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI - OPEN FORM
DBREF 4BP9 A 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 B 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 C 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 D 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 E 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 F 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP9 G 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 H 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 I 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 J 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 K 1 4 NOR NOR00664 NOR00664 1 4
DBREF 4BP9 L 1 4 NOR NOR00664 NOR00664 1 4
SEQADV 4BP9 OAR G 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR H 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR I 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR J 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR K 4 NOR NOR00664 RGL 4 CONFLICT
SEQADV 4BP9 OAR L 4 NOR NOR00664 RGL 4 CONFLICT
SEQRES 1 A 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 A 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 A 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 A 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 A 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 A 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 A 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 A 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 A 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 A 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 A 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 A 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 A 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 A 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 A 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 A 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 A 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 A 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 A 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 A 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 A 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 A 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 A 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 A 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 A 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 A 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 A 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 A 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 A 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 A 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 A 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 A 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 A 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 A 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 A 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 A 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 A 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 A 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 A 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 A 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 A 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 A 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 A 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 A 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 A 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 A 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 A 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 A 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 A 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 A 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 A 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 A 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 A 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 A 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 A 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 B 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 B 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 B 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 B 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 B 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 B 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 B 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 B 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 B 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 B 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 B 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 B 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 B 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 B 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 B 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 B 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 B 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 B 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 B 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 B 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 B 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 B 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 B 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 B 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 B 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 B 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 B 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 B 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 B 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 B 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 B 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 B 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 B 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 B 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 B 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 B 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 B 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 B 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 B 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 B 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 B 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 B 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 B 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 B 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 B 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 B 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 B 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 B 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 B 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 B 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 B 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 B 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 B 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 B 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 B 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 C 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 C 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 C 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 C 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 C 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 C 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 C 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 C 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 C 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 C 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 C 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 C 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 C 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 C 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 C 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 C 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 C 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 C 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 C 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 C 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 C 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 C 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 C 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 C 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 C 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 C 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 C 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 C 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 C 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 C 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 C 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 C 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 C 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 C 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 C 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 C 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 C 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 C 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 C 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 C 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 C 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 C 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 C 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 C 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 C 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 C 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 C 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 C 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 C 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 C 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 C 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 C 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 C 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 C 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 C 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 D 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 D 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 D 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 D 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 D 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 D 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 D 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 D 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 D 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 D 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 D 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 D 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 D 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 D 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 D 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 D 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 D 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 D 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 D 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 D 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 D 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 D 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 D 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 D 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 D 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 D 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 D 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 D 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 D 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 D 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 D 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 D 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 D 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 D 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 D 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 D 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 D 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 D 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 D 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 D 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 D 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 D 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 D 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 D 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 D 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 D 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 D 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 D 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 D 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 D 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 D 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 D 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 D 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 D 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 D 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 E 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 E 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 E 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 E 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 E 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 E 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 E 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 E 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 E 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 E 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 E 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 E 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 E 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 E 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 E 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 E 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 E 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 E 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 E 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 E 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 E 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 E 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 E 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 E 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 E 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 E 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 E 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 E 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 E 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 E 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 E 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 E 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 E 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 E 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 E 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 E 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 E 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 E 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 E 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 E 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 E 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 E 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 E 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 E 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 E 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 E 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 E 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 E 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 E 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 E 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 E 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 E 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 E 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 E 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 E 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 F 715 MET GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 F 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 F 715 GLY ALA ASN PRO MET ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 F 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 F 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 F 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 F 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 F 715 MET SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 F 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 F 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 F 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 F 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 F 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 F 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 F 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 F 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 F 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 F 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 F 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 F 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MET SER SER
SEQRES 21 F 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 F 715 VAL LYS HIS ASN THR LEU GLU MET VAL ARG PRO ARG GLU
SEQRES 23 F 715 LYS GLY VAL ARG TYR THR VAL GLU MET HIS GLY THR ASP
SEQRES 24 F 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 F 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 F 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 F 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 F 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 F 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 F 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 F 715 VAL VAL CYS SER GLN MET LYS THR TYR ASP ALA SER LEU
SEQRES 32 F 715 LEU ARG LEU ARG TYR SER SER MET THR THR PRO THR VAL
SEQRES 33 F 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 F 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 F 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 F 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 F 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MET LEU TYR GLY
SEQRES 38 F 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 F 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MET ILE TYR
SEQRES 40 F 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MET GLY ARG
SEQRES 41 F 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 F 715 ASN THR PHE MET ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 F 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 F 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 F 715 LEU ASN MET ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 F 715 GLY VAL PRO PHE VAL ASP VAL MET THR THR MET CYS ASP
SEQRES 47 F 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 F 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MET ASN
SEQRES 49 F 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 F 715 PRO HIS LEU MET ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 F 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 F 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 F 715 MET ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 F 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 F 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 G 4 FC0 ARG VAL OAR
SEQRES 1 H 4 FC0 ARG VAL OAR
SEQRES 1 I 4 FC0 ARG VAL OAR
SEQRES 1 J 4 FC0 ARG VAL OAR
SEQRES 1 K 4 FC0 ARG VAL OAR
SEQRES 1 L 4 FC0 ARG VAL OAR
MODRES 4BP9 FC0 G 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR G 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
MODRES 4BP9 FC0 H 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR H 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
MODRES 4BP9 FC0 I 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR I 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
MODRES 4BP9 FC0 J 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR J 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
MODRES 4BP9 FC0 K 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR K 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
MODRES 4BP9 FC0 L 1 PHE N-CARBOXY-L-PHENYLALANINE
MODRES 4BP9 OAR L 4 ARG N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
HET FC0 G 1 14
HET OAR G 4 11
HET FC0 H 1 14
HET OAR H 4 11
HET FC0 I 1 14
HET OAR I 4 11
HET FC0 J 1 14
HET OAR J 4 11
HET FC0 K 1 14
HET OAR K 4 11
HET FC0 L 1 14
HET OAR L 4 11
HETNAM FC0 N-CARBOXY-L-PHENYLALANINE
HETNAM OAR N-(4-AMINO-5-HYDROXY-PENTYL)-GUANIDINE
FORMUL 7 FC0 6(C10 H11 N O4)
FORMUL 7 OAR 6(C6 H16 N4 O)
FORMUL 13 HOH *344(H2 O)
HELIX 1 1 LEU A 41 ARG A 45 5 5
HELIX 2 2 ASP A 51 ALA A 69 1 19
HELIX 3 3 ILE A 72 HIS A 86 1 15
HELIX 4 4 GLU A 137 GLU A 142 1 6
HELIX 5 5 ARG A 180 VAL A 182 5 3
HELIX 6 6 PRO A 198 ALA A 200 5 3
HELIX 7 7 ASP A 209 ARG A 213 5 5
HELIX 8 8 PRO A 225 ASP A 229 5 5
HELIX 9 9 ARG A 271 GLY A 273 5 3
HELIX 10 10 SER A 373 LEU A 377 5 5
HELIX 11 11 CYS A 393 MET A 396 5 4
HELIX 12 12 GLU A 440 LYS A 442 5 3
HELIX 13 13 ASN A 494 ARG A 496 5 3
HELIX 14 14 PHE A 497 ASP A 502 1 6
HELIX 15 15 ARG A 520 VAL A 525 1 6
HELIX 16 16 LYS A 528 THR A 531 5 4
HELIX 17 17 LYS A 532 SER A 549 1 18
HELIX 18 18 THR A 553 ALA A 555 5 3
HELIX 19 19 SER A 563 ARG A 576 1 14
HELIX 20 20 PRO A 577 PHE A 580 5 4
HELIX 21 21 ASP A 591 ASP A 598 1 8
HELIX 22 22 THR A 605 GLU A 610 5 6
HELIX 23 23 PHE A 619 SER A 625 1 7
HELIX 24 24 SER A 627 VAL A 632 1 6
HELIX 25 25 TYR A 653 LYS A 667 1 15
HELIX 26 26 TYR A 690 ASN A 708 1 19
HELIX 27 27 LEU B 41 ARG B 45 5 5
HELIX 28 28 ASP B 51 VAL B 70 1 20
HELIX 29 29 ILE B 72 GLU B 88 1 17
HELIX 30 30 GLU B 137 GLU B 142 1 6
HELIX 31 31 ARG B 180 VAL B 182 5 3
HELIX 32 32 PRO B 198 ALA B 200 5 3
HELIX 33 33 ALA B 210 LYS B 212 5 3
HELIX 34 34 PRO B 225 ASP B 229 5 5
HELIX 35 35 CYS B 393 MET B 396 5 4
HELIX 36 36 GLU B 440 LYS B 442 5 3
HELIX 37 37 ASN B 494 ARG B 496 5 3
HELIX 38 38 PHE B 497 ASP B 502 1 6
HELIX 39 39 ARG B 520 VAL B 525 1 6
HELIX 40 40 LYS B 528 LYS B 532 5 5
HELIX 41 41 ARG B 533 SER B 549 1 17
HELIX 42 42 THR B 553 ALA B 555 5 3
HELIX 43 43 ALA B 564 ARG B 576 1 13
HELIX 44 44 PRO B 577 PHE B 580 5 4
HELIX 45 45 ASP B 591 CYS B 597 1 7
HELIX 46 46 THR B 604 GLU B 609 5 6
HELIX 47 47 PHE B 619 SER B 625 1 7
HELIX 48 48 PRO B 628 VAL B 632 5 5
HELIX 49 49 TYR B 653 LYS B 667 1 15
HELIX 50 50 TYR B 690 LEU B 707 1 18
HELIX 51 51 LEU C 41 ARG C 45 5 5
HELIX 52 52 ASP C 51 VAL C 70 1 20
HELIX 53 53 ASP C 71 LYS C 73 5 3
HELIX 54 54 ASP C 74 GLU C 88 1 15
HELIX 55 55 GLU C 137 GLU C 142 1 6
HELIX 56 56 ARG C 180 VAL C 182 5 3
HELIX 57 57 PRO C 198 ALA C 200 5 3
HELIX 58 58 ASP C 209 ARG C 213 5 5
HELIX 59 59 PRO C 225 ASP C 229 5 5
HELIX 60 60 ARG C 271 GLY C 273 5 3
HELIX 61 61 CYS C 393 MET C 396 5 4
HELIX 62 62 GLU C 440 LYS C 442 5 3
HELIX 63 63 ASN C 494 ARG C 496 5 3
HELIX 64 64 PHE C 497 ASP C 502 1 6
HELIX 65 65 ARG C 520 VAL C 525 1 6
HELIX 66 66 LYS C 528 THR C 531 5 4
HELIX 67 67 LYS C 532 SER C 549 1 18
HELIX 68 68 THR C 553 ALA C 555 5 3
HELIX 69 69 SER C 563 ARG C 576 1 14
HELIX 70 70 PRO C 577 PHE C 580 5 4
HELIX 71 71 ASP C 591 ASP C 598 1 8
HELIX 72 72 LEU C 603 GLU C 610 5 8
HELIX 73 73 GLU C 616 SER C 627 1 12
HELIX 74 74 PRO C 628 VAL C 632 5 5
HELIX 75 75 TYR C 653 LYS C 667 1 15
HELIX 76 76 LYS C 691 ASN C 708 1 18
HELIX 77 77 LEU D 41 ARG D 45 5 5
HELIX 78 78 ASP D 51 ALA D 69 1 19
HELIX 79 79 ILE D 72 HIS D 86 1 15
HELIX 80 80 GLU D 137 ALA D 141 1 5
HELIX 81 81 ARG D 180 VAL D 182 5 3
HELIX 82 82 ALA D 210 LYS D 212 5 3
HELIX 83 83 PRO D 225 ASP D 229 5 5
HELIX 84 84 ARG D 271 GLY D 273 5 3
HELIX 85 85 SER D 373 LEU D 377 5 5
HELIX 86 86 CYS D 393 MET D 396 5 4
HELIX 87 87 GLU D 440 LYS D 442 5 3
HELIX 88 88 ASN D 494 ARG D 496 5 3
HELIX 89 89 PHE D 497 ASP D 502 1 6
HELIX 90 90 ARG D 520 VAL D 525 1 6
HELIX 91 91 LYS D 528 THR D 531 5 4
HELIX 92 92 LYS D 532 SER D 549 1 18
HELIX 93 93 THR D 553 ALA D 555 5 3
HELIX 94 94 SER D 563 ARG D 576 1 14
HELIX 95 95 PRO D 577 PHE D 580 5 4
HELIX 96 96 ASP D 591 CYS D 597 1 7
HELIX 97 97 THR D 605 GLU D 610 5 6
HELIX 98 98 PHE D 619 SER D 625 1 7
HELIX 99 99 PRO D 628 VAL D 632 5 5
HELIX 100 100 TYR D 653 LYS D 667 1 15
HELIX 101 101 TYR D 690 ASN D 708 1 19
HELIX 102 102 LEU E 41 ARG E 45 5 5
HELIX 103 103 ASP E 51 VAL E 70 1 20
HELIX 104 104 ILE E 72 GLU E 88 1 17
HELIX 105 105 GLU E 137 GLU E 142 1 6
HELIX 106 106 ARG E 180 VAL E 182 5 3
HELIX 107 107 PRO E 198 ALA E 200 5 3
HELIX 108 108 ASP E 209 ARG E 213 5 5
HELIX 109 109 PRO E 225 ASP E 229 5 5
HELIX 110 110 CYS E 393 MET E 396 5 4
HELIX 111 111 GLU E 440 LYS E 442 5 3
HELIX 112 112 ASN E 494 ARG E 496 5 3
HELIX 113 113 PHE E 497 ASP E 502 1 6
HELIX 114 114 ARG E 520 VAL E 525 1 6
HELIX 115 115 LYS E 528 THR E 531 5 4
HELIX 116 116 LYS E 532 SER E 549 1 18
HELIX 117 117 THR E 553 ALA E 555 5 3
HELIX 118 118 ALA E 564 ARG E 576 1 13
HELIX 119 119 PRO E 577 PHE E 580 5 4
HELIX 120 120 ASP E 591 ASP E 598 1 8
HELIX 121 121 LEU E 603 TRP E 608 1 6
HELIX 122 122 GLU E 616 SER E 625 1 10
HELIX 123 123 PRO E 628 VAL E 632 5 5
HELIX 124 124 TYR E 653 LYS E 667 1 15
HELIX 125 125 TYR E 690 ASN E 708 1 19
HELIX 126 126 LEU F 41 ARG F 45 5 5
HELIX 127 127 ASP F 51 VAL F 70 1 20
HELIX 128 128 ILE F 72 SER F 85 1 14
HELIX 129 129 GLU F 137 ALA F 141 1 5
HELIX 130 130 ARG F 180 VAL F 182 5 3
HELIX 131 131 PRO F 198 ALA F 200 5 3
HELIX 132 132 ALA F 210 LYS F 212 5 3
HELIX 133 133 PRO F 225 ASP F 229 5 5
HELIX 134 134 CYS F 393 MET F 396 5 4
HELIX 135 135 GLU F 440 LYS F 442 5 3
HELIX 136 136 ASN F 494 ARG F 496 5 3
HELIX 137 137 PHE F 497 ASP F 502 1 6
HELIX 138 138 ARG F 520 VAL F 525 1 6
HELIX 139 139 LYS F 528 THR F 531 5 4
HELIX 140 140 LYS F 532 SER F 549 1 18
HELIX 141 141 THR F 553 ALA F 555 5 3
HELIX 142 142 SER F 563 ARG F 576 1 14
HELIX 143 143 PRO F 577 PHE F 580 5 4
HELIX 144 144 ASP F 591 CYS F 597 1 7
HELIX 145 145 LEU F 603 TRP F 608 1 6
HELIX 146 146 PHE F 619 SER F 625 1 7
HELIX 147 147 PRO F 628 VAL F 632 5 5
HELIX 148 148 TYR F 653 LYS F 667 1 15
HELIX 149 149 TYR F 690 LEU F 707 1 18
SHEET 1 AA 2 GLU A 15 PHE A 18 0
SHEET 2 AA 2 ARG A 35 VAL A 38 -1 O ARG A 35 N PHE A 18
SHEET 1 AB 2 ASP A 91 MET A 92 0
SHEET 2 AB 2 PHE A 101 ASP A 107 -1 O ASP A 107 N ASP A 91
SHEET 1 AC 2 TYR A 96 TYR A 98 0
SHEET 2 AC 2 PHE A 101 ASP A 107 -1 O PHE A 101 N TYR A 98
SHEET 1 AD 4 GLU A 132 ASP A 136 0
SHEET 2 AD 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AD 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AD 4 TYR A 96 TYR A 98 -1 O TYR A 96 N TYR A 103
SHEET 1 AE 4 GLU A 132 ASP A 136 0
SHEET 2 AE 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AE 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AE 4 ASP A 91 MET A 92 -1 O ASP A 91 N ASP A 107
SHEET 1 AF 4 VAL A 148 PRO A 154 0
SHEET 2 AF 4 VAL A 162 ASP A 167 -1 O ALA A 163 N ALA A 153
SHEET 3 AF 4 TYR A 174 PHE A 178 -1 O SER A 175 N VAL A 166
SHEET 4 AF 4 VAL A 187 THR A 190 -1 O VAL A 187 N ILE A 176
SHEET 1 AG 4 VAL A 195 TRP A 196 0
SHEET 2 AG 4 CYS A 202 THR A 207 -1 O PHE A 204 N VAL A 195
SHEET 3 AG 4 LYS A 216 ILE A 221 -1 O LYS A 216 N THR A 207
SHEET 4 AG 4 VAL A 230 THR A 234 -1 O VAL A 230 N ARG A 219
SHEET 1 AH 4 SER A 241 ARG A 246 0
SHEET 2 AH 4 THR A 252 SER A 259 -1 O ILE A 254 N GLY A 245
SHEET 3 AH 4 THR A 262 ASP A 269 -1 O THR A 262 N SER A 259
SHEET 4 AH 4 GLU A 280 MET A 281 -1 O GLU A 280 N LEU A 267
SHEET 1 AI 4 TYR A 291 HIS A 296 0
SHEET 2 AI 4 THR A 300 THR A 305 -1 O THR A 300 N HIS A 296
SHEET 3 AI 4 LYS A 314 LYS A 319 -1 O LYS A 314 N THR A 305
SHEET 4 AI 4 THR A 328 ILE A 331 -1 O THR A 328 N LEU A 317
SHEET 1 AJ 4 THR A 338 VAL A 344 0
SHEET 2 AJ 4 PHE A 348 ARG A 355 -1 O VAL A 350 N ALA A 343
SHEET 3 AJ 4 LEU A 358 ARG A 365 -1 O LEU A 358 N ARG A 355
SHEET 4 AJ 4 LYS A 378 GLU A 379 -1 O LYS A 378 N THR A 363
SHEET 1 AK 4 THR A 388 VAL A 391 0
SHEET 2 AK 4 LEU A 403 SER A 409 -1 O ARG A 407 N HIS A 390
SHEET 3 AK 4 VAL A 416 ASP A 421 -1 O VAL A 416 N TYR A 408
SHEET 4 AK 4 ARG A 427 ALA A 432 -1 O LYS A 428 N ASP A 419
SHEET 1 AL 8 TYR A 444 THR A 452 0
SHEET 2 AL 8 LYS A 458 ASP A 466 -1 O VAL A 459 N ALA A 451
SHEET 3 AL 8 ILE A 506 ALA A 510 -1 O TYR A 507 N VAL A 464
SHEET 4 AL 8 THR A 477 TYR A 480 1 O MET A 478 N ALA A 508
SHEET 5 AL 8 LEU A 557 ARG A 562 1 O SER A 558 N LEU A 479
SHEET 6 AL 8 VAL A 582 GLY A 586 1 O VAL A 582 N CYS A 559
SHEET 7 AL 8 HIS A 639 GLY A 645 1 O HIS A 639 N ALA A 583
SHEET 8 AL 8 VAL A 673 ASP A 678 1 O LEU A 674 N ILE A 642
SHEET 1 BA 2 GLU B 15 PHE B 18 0
SHEET 2 BA 2 ARG B 35 VAL B 38 -1 O ARG B 35 N PHE B 18
SHEET 1 BB 2 ASP B 91 MET B 92 0
SHEET 2 BB 2 PHE B 101 ASP B 107 -1 O ASP B 107 N ASP B 91
SHEET 1 BC 2 TYR B 96 TYR B 98 0
SHEET 2 BC 2 PHE B 101 ASP B 107 -1 O PHE B 101 N TYR B 98
SHEET 1 BD 4 GLU B 132 ASP B 136 0
SHEET 2 BD 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BD 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BD 4 TYR B 96 TYR B 98 -1 O TYR B 96 N TYR B 103
SHEET 1 BE 4 GLU B 132 ASP B 136 0
SHEET 2 BE 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BE 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BE 4 ASP B 91 MET B 92 -1 O ASP B 91 N ASP B 107
SHEET 1 BF 4 VAL B 148 PRO B 154 0
SHEET 2 BF 4 VAL B 162 ASP B 167 -1 O ALA B 163 N ALA B 153
SHEET 3 BF 4 TYR B 174 PHE B 178 -1 O SER B 175 N VAL B 166
SHEET 4 BF 4 VAL B 187 THR B 190 -1 O VAL B 187 N ILE B 176
SHEET 1 BG 4 VAL B 195 TRP B 196 0
SHEET 2 BG 4 CYS B 202 LYS B 208 -1 O PHE B 204 N VAL B 195
SHEET 3 BG 4 ASP B 214 ILE B 221 -1 O LYS B 216 N THR B 207
SHEET 4 BG 4 VAL B 230 THR B 234 -1 O VAL B 230 N ARG B 219
SHEET 1 BH 4 SER B 241 ARG B 246 0
SHEET 2 BH 4 THR B 252 MET B 258 -1 O ILE B 254 N GLY B 245
SHEET 3 BH 4 SER B 263 ASP B 269 -1 O GLU B 264 N SER B 257
SHEET 4 BH 4 GLU B 280 MET B 281 -1 O GLU B 280 N LEU B 267
SHEET 1 BI 3 TYR B 291 HIS B 296 0
SHEET 2 BI 3 THR B 300 THR B 305 -1 O THR B 300 N HIS B 296
SHEET 3 BI 3 LYS B 314 LYS B 319 -1 O LYS B 314 N THR B 305
SHEET 1 BJ 4 THR B 338 VAL B 344 0
SHEET 2 BJ 4 PHE B 348 ARG B 355 -1 O VAL B 350 N ALA B 343
SHEET 3 BJ 4 LEU B 358 LEU B 366 -1 O LEU B 358 N ARG B 355
SHEET 4 BJ 4 PHE B 372 GLU B 379 -1 N SER B 373 O ARG B 365
SHEET 1 BK 4 THR B 388 VAL B 391 0
SHEET 2 BK 4 LEU B 403 SER B 409 -1 O ARG B 407 N HIS B 390
SHEET 3 BK 4 VAL B 416 ASP B 421 -1 O VAL B 416 N TYR B 408
SHEET 4 BK 4 ARG B 427 ALA B 432 -1 O LYS B 428 N ASP B 419
SHEET 1 BL 8 TYR B 444 THR B 452 0
SHEET 2 BL 8 LYS B 458 ASP B 466 -1 O VAL B 459 N ALA B 451
SHEET 3 BL 8 ILE B 506 ALA B 510 -1 O TYR B 507 N VAL B 464
SHEET 4 BL 8 THR B 477 GLY B 481 1 O MET B 478 N ALA B 508
SHEET 5 BL 8 LEU B 557 ARG B 562 1 O SER B 558 N LEU B 479
SHEET 6 BL 8 VAL B 582 GLY B 586 1 O VAL B 582 N CYS B 559
SHEET 7 BL 8 HIS B 639 GLY B 645 1 O HIS B 639 N ALA B 583
SHEET 8 BL 8 VAL B 673 ASP B 678 1 O LEU B 674 N ILE B 642
SHEET 1 CA 2 GLU C 15 PHE C 18 0
SHEET 2 CA 2 ARG C 35 VAL C 38 -1 O ARG C 35 N PHE C 18
SHEET 1 CB 4 TYR C 96 TYR C 98 0
SHEET 2 CB 4 PHE C 101 ARG C 106 -1 O PHE C 101 N TYR C 98
SHEET 3 CB 4 LEU C 115 PRO C 120 -1 O LEU C 115 N ARG C 106
SHEET 4 CB 4 GLU C 132 ASP C 136 -1 O GLU C 132 N ARG C 118
SHEET 1 CC 4 VAL C 148 PRO C 154 0
SHEET 2 CC 4 VAL C 162 ASP C 167 -1 O ALA C 163 N ALA C 153
SHEET 3 CC 4 TYR C 174 PHE C 178 -1 O SER C 175 N VAL C 166
SHEET 4 CC 4 VAL C 187 THR C 190 -1 O VAL C 187 N ILE C 176
SHEET 1 CD 4 VAL C 195 TRP C 196 0
SHEET 2 CD 4 CYS C 202 THR C 207 -1 O PHE C 204 N VAL C 195
SHEET 3 CD 4 LYS C 216 ILE C 221 -1 O LYS C 216 N THR C 207
SHEET 4 CD 4 VAL C 230 THR C 234 -1 O VAL C 230 N ARG C 219
SHEET 1 CE 4 SER C 241 ARG C 246 0
SHEET 2 CE 4 THR C 252 SER C 259 -1 O ILE C 254 N GLY C 245
SHEET 3 CE 4 THR C 262 ASP C 269 -1 O THR C 262 N SER C 259
SHEET 4 CE 4 GLU C 280 MET C 281 -1 O GLU C 280 N LEU C 267
SHEET 1 CF 4 TYR C 291 HIS C 296 0
SHEET 2 CF 4 THR C 300 THR C 305 -1 O THR C 300 N HIS C 296
SHEET 3 CF 4 LYS C 314 LYS C 319 -1 O LYS C 314 N THR C 305
SHEET 4 CF 4 THR C 328 ILE C 331 -1 O THR C 328 N LEU C 317
SHEET 1 CG 4 VAL C 337 VAL C 344 0
SHEET 2 CG 4 PHE C 348 ARG C 355 -1 O VAL C 350 N ALA C 343
SHEET 3 CG 4 LEU C 358 GLY C 367 -1 O LEU C 358 N ARG C 355
SHEET 4 CG 4 LEU C 371 PHE C 372 1 O LEU C 371 N GLY C 367
SHEET 1 CH 4 VAL C 337 VAL C 344 0
SHEET 2 CH 4 PHE C 348 ARG C 355 -1 O VAL C 350 N ALA C 343
SHEET 3 CH 4 LEU C 358 GLY C 367 -1 O LEU C 358 N ARG C 355
SHEET 4 CH 4 LYS C 378 GLU C 379 -1 O LYS C 378 N THR C 363
SHEET 1 CI 2 LEU C 371 PHE C 372 0
SHEET 2 CI 2 LEU C 358 GLY C 367 1 N GLY C 367 O LEU C 371
SHEET 1 CJ 4 PHE C 387 VAL C 391 0
SHEET 2 CJ 4 ARG C 405 SER C 410 -1 O ARG C 407 N HIS C 390
SHEET 3 CJ 4 VAL C 416 GLU C 420 -1 O VAL C 416 N TYR C 408
SHEET 4 CJ 4 ARG C 427 ALA C 432 -1 O LYS C 428 N ASP C 419
SHEET 1 CK 8 TYR C 444 THR C 452 0
SHEET 2 CK 8 LYS C 458 ASP C 466 -1 O VAL C 459 N ALA C 451
SHEET 3 CK 8 ILE C 506 ALA C 510 -1 O TYR C 507 N VAL C 464
SHEET 4 CK 8 THR C 477 GLY C 481 1 O MET C 478 N ALA C 508
SHEET 5 CK 8 LEU C 557 ARG C 562 1 O SER C 558 N LEU C 479
SHEET 6 CK 8 VAL C 582 GLY C 586 1 O VAL C 582 N CYS C 559
SHEET 7 CK 8 HIS C 639 GLY C 645 1 O HIS C 639 N ALA C 583
SHEET 8 CK 8 VAL C 673 ASP C 678 1 O LEU C 674 N ILE C 642
SHEET 1 DA 2 GLU D 15 PHE D 18 0
SHEET 2 DA 2 ARG D 35 VAL D 38 -1 O ARG D 35 N PHE D 18
SHEET 1 DB 2 ASP D 91 MET D 92 0
SHEET 2 DB 2 PHE D 101 ASP D 107 -1 O ASP D 107 N ASP D 91
SHEET 1 DC 2 TYR D 96 TYR D 98 0
SHEET 2 DC 2 PHE D 101 ASP D 107 1 O PHE D 101 N TYR D 98
SHEET 1 DD 4 GLU D 132 ASP D 136 0
SHEET 2 DD 4 LEU D 115 PRO D 120 -1 O HIS D 116 N VAL D 134
SHEET 3 DD 4 PHE D 101 ASP D 107 -1 O LEU D 102 N VAL D 119
SHEET 4 DD 4 TYR D 96 TYR D 98 1 O TYR D 96 N TYR D 103
SHEET 1 DE 4 GLU D 132 ASP D 136 0
SHEET 2 DE 4 LEU D 115 PRO D 120 -1 O HIS D 116 N VAL D 134
SHEET 3 DE 4 PHE D 101 ASP D 107 -1 O LEU D 102 N VAL D 119
SHEET 4 DE 4 ASP D 91 MET D 92 -1 O ASP D 91 N ASP D 107
SHEET 1 DF 4 VAL D 148 PRO D 154 0
SHEET 2 DF 4 VAL D 162 ASP D 167 -1 O ALA D 163 N ALA D 153
SHEET 3 DF 4 TYR D 174 PHE D 178 -1 O SER D 175 N VAL D 166
SHEET 4 DF 4 VAL D 187 THR D 190 -1 O VAL D 187 N ILE D 176
SHEET 1 DG 4 VAL D 195 TRP D 196 0
SHEET 2 DG 4 CYS D 202 LYS D 208 -1 O PHE D 204 N VAL D 195
SHEET 3 DG 4 ASP D 214 ILE D 221 -1 N ASN D 215 O THR D 207
SHEET 4 DG 4 VAL D 230 THR D 234 -1 O VAL D 230 N ARG D 219
SHEET 1 DH 4 SER D 241 ARG D 246 0
SHEET 2 DH 4 THR D 252 SER D 259 -1 O ILE D 254 N GLY D 245
SHEET 3 DH 4 THR D 262 ASP D 269 -1 O THR D 262 N SER D 259
SHEET 4 DH 4 GLU D 280 MET D 281 -1 O GLU D 280 N LEU D 267
SHEET 1 DI 4 TYR D 291 HIS D 296 0
SHEET 2 DI 4 THR D 300 THR D 305 -1 O THR D 300 N HIS D 296
SHEET 3 DI 4 LYS D 314 LYS D 319 -1 O LYS D 314 N THR D 305
SHEET 4 DI 4 THR D 328 ILE D 331 -1 O THR D 328 N LEU D 317
SHEET 1 DJ 4 VAL D 337 VAL D 344 0
SHEET 2 DJ 4 PHE D 348 ARG D 355 -1 O VAL D 350 N ALA D 343
SHEET 3 DJ 4 LEU D 358 ARG D 365 -1 O LEU D 358 N ARG D 355
SHEET 4 DJ 4 LYS D 378 GLU D 379 -1 O LYS D 378 N THR D 363
SHEET 1 DK 4 THR D 388 VAL D 391 0
SHEET 2 DK 4 LEU D 403 SER D 409 -1 O ARG D 407 N HIS D 390
SHEET 3 DK 4 VAL D 416 ASP D 421 -1 O VAL D 416 N TYR D 408
SHEET 4 DK 4 ARG D 427 ALA D 432 -1 O LYS D 428 N ASP D 419
SHEET 1 DL 8 TYR D 444 THR D 452 0
SHEET 2 DL 8 LYS D 458 ASP D 466 -1 O VAL D 459 N ALA D 451
SHEET 3 DL 8 ILE D 506 ALA D 510 -1 O TYR D 507 N VAL D 464
SHEET 4 DL 8 THR D 477 GLY D 481 1 O MET D 478 N ALA D 508
SHEET 5 DL 8 LEU D 557 ARG D 562 1 O SER D 558 N LEU D 479
SHEET 6 DL 8 VAL D 582 GLY D 586 1 O VAL D 582 N CYS D 559
SHEET 7 DL 8 HIS D 639 GLY D 645 1 O HIS D 639 N ALA D 583
SHEET 8 DL 8 VAL D 673 ASP D 678 1 O LEU D 674 N ILE D 642
SHEET 1 EA 2 GLU E 15 PHE E 18 0
SHEET 2 EA 2 ARG E 35 VAL E 38 -1 O ARG E 35 N PHE E 18
SHEET 1 EB 2 ASP E 91 MET E 92 0
SHEET 2 EB 2 PHE E 101 VAL E 108 -1 O ASP E 107 N ASP E 91
SHEET 1 EC 2 TYR E 96 TYR E 98 0
SHEET 2 EC 2 PHE E 101 VAL E 108 1 O PHE E 101 N TYR E 98
SHEET 1 ED 4 GLU E 132 ASP E 136 0
SHEET 2 ED 4 LEU E 111 PRO E 120 -1 O HIS E 116 N LEU E 135
SHEET 3 ED 4 PHE E 101 VAL E 108 -1 O LEU E 102 N VAL E 119
SHEET 4 ED 4 TYR E 96 TYR E 98 1 O TYR E 96 N TYR E 103
SHEET 1 EE 4 GLU E 132 ASP E 136 0
SHEET 2 EE 4 LEU E 111 PRO E 120 -1 O HIS E 116 N LEU E 135
SHEET 3 EE 4 PHE E 101 VAL E 108 -1 O LEU E 102 N VAL E 119
SHEET 4 EE 4 ASP E 91 MET E 92 -1 O ASP E 91 N ASP E 107
SHEET 1 EF 4 VAL E 148 PRO E 154 0
SHEET 2 EF 4 VAL E 162 ASP E 167 -1 O ALA E 163 N ALA E 153
SHEET 3 EF 4 TYR E 174 PHE E 178 -1 O SER E 175 N VAL E 166
SHEET 4 EF 4 VAL E 187 THR E 190 -1 O VAL E 187 N ILE E 176
SHEET 1 EG 4 VAL E 195 TRP E 196 0
SHEET 2 EG 4 CYS E 202 THR E 207 -1 O PHE E 204 N VAL E 195
SHEET 3 EG 4 LYS E 216 ILE E 221 -1 O LYS E 216 N THR E 207
SHEET 4 EG 4 VAL E 230 THR E 234 -1 O VAL E 230 N ARG E 219
SHEET 1 EH 4 SER E 241 ARG E 246 0
SHEET 2 EH 4 THR E 252 MET E 258 -1 O ILE E 254 N GLY E 245
SHEET 3 EH 4 SER E 263 ASP E 269 -1 O GLU E 264 N SER E 257
SHEET 4 EH 4 GLU E 280 MET E 281 -1 O GLU E 280 N LEU E 267
SHEET 1 EI 4 TYR E 291 HIS E 296 0
SHEET 2 EI 4 THR E 300 THR E 305 -1 O THR E 300 N HIS E 296
SHEET 3 EI 4 LYS E 314 LYS E 319 -1 O LYS E 314 N THR E 305
SHEET 4 EI 4 THR E 328 ILE E 331 -1 O THR E 328 N LEU E 317
SHEET 1 EJ 4 VAL E 337 PHE E 345 0
SHEET 2 EJ 4 PHE E 348 ARG E 355 -1 O PHE E 348 N PHE E 345
SHEET 3 EJ 4 LEU E 358 LEU E 366 -1 O LEU E 358 N ARG E 355
SHEET 4 EJ 4 PHE E 372 GLU E 379 -1 N SER E 373 O ARG E 365
SHEET 1 EK 4 THR E 388 VAL E 391 0
SHEET 2 EK 4 LEU E 406 SER E 409 -1 O ARG E 407 N HIS E 390
SHEET 3 EK 4 VAL E 416 GLU E 420 -1 O VAL E 416 N TYR E 408
SHEET 4 EK 4 ARG E 427 ALA E 432 -1 O LYS E 428 N ASP E 419
SHEET 1 EL 8 TYR E 444 THR E 452 0
SHEET 2 EL 8 LYS E 458 ASP E 466 -1 O VAL E 459 N ALA E 451
SHEET 3 EL 8 ILE E 506 ALA E 510 -1 O TYR E 507 N VAL E 464
SHEET 4 EL 8 THR E 477 GLY E 481 1 O MET E 478 N ALA E 508
SHEET 5 EL 8 LEU E 557 ARG E 562 1 O SER E 558 N LEU E 479
SHEET 6 EL 8 VAL E 582 GLY E 586 1 O VAL E 582 N CYS E 559
SHEET 7 EL 8 HIS E 639 GLY E 645 1 O HIS E 639 N ALA E 583
SHEET 8 EL 8 VAL E 673 ASP E 678 1 O LEU E 674 N ILE E 642
SHEET 1 FA 2 HIS F 14 PHE F 18 0
SHEET 2 FA 2 ARG F 35 ASP F 39 -1 O ARG F 35 N PHE F 18
SHEET 1 FB 2 ASP F 91 MET F 92 0
SHEET 2 FB 2 PHE F 101 ASP F 107 -1 O ASP F 107 N ASP F 91
SHEET 1 FC 2 TYR F 96 TYR F 98 0
SHEET 2 FC 2 PHE F 101 ASP F 107 1 O PHE F 101 N TYR F 98
SHEET 1 FD 4 GLU F 132 ASP F 136 0
SHEET 2 FD 4 LEU F 115 ARG F 118 -1 O HIS F 116 N VAL F 134
SHEET 3 FD 4 PHE F 101 ASP F 107 -1 O TYR F 104 N CYS F 117
SHEET 4 FD 4 TYR F 96 TYR F 98 1 O TYR F 96 N TYR F 103
SHEET 1 FE 4 GLU F 132 ASP F 136 0
SHEET 2 FE 4 LEU F 115 ARG F 118 -1 O HIS F 116 N VAL F 134
SHEET 3 FE 4 PHE F 101 ASP F 107 -1 O TYR F 104 N CYS F 117
SHEET 4 FE 4 ASP F 91 MET F 92 -1 O ASP F 91 N ASP F 107
SHEET 1 FF 4 VAL F 148 PRO F 154 0
SHEET 2 FF 4 VAL F 162 ASP F 167 -1 O ALA F 163 N ALA F 153
SHEET 3 FF 4 TYR F 174 PHE F 178 -1 O SER F 175 N VAL F 166
SHEET 4 FF 4 VAL F 187 THR F 190 -1 O VAL F 187 N ILE F 176
SHEET 1 FG 4 VAL F 195 TRP F 196 0
SHEET 2 FG 4 CYS F 202 LYS F 208 -1 O PHE F 204 N VAL F 195
SHEET 3 FG 4 ASP F 214 ILE F 221 -1 O LYS F 216 N THR F 207
SHEET 4 FG 4 VAL F 230 THR F 234 -1 O VAL F 230 N ARG F 219
SHEET 1 FH 4 SER F 241 ARG F 246 0
SHEET 2 FH 4 THR F 252 SER F 259 -1 O ILE F 254 N GLY F 245
SHEET 3 FH 4 THR F 262 ASP F 269 -1 O THR F 262 N SER F 259
SHEET 4 FH 4 GLU F 280 MET F 281 -1 O GLU F 280 N LEU F 267
SHEET 1 FI 4 TYR F 291 HIS F 296 0
SHEET 2 FI 4 THR F 300 THR F 305 -1 O THR F 300 N HIS F 296
SHEET 3 FI 4 LYS F 314 LYS F 319 -1 O LYS F 314 N THR F 305
SHEET 4 FI 4 VAL F 329 ILE F 331 -1 N LEU F 330 O VAL F 315
SHEET 1 FJ 4 THR F 338 VAL F 344 0
SHEET 2 FJ 4 PHE F 348 ARG F 355 -1 O VAL F 350 N ALA F 343
SHEET 3 FJ 4 LEU F 358 ARG F 365 -1 O LEU F 358 N ARG F 355
SHEET 4 FJ 4 LYS F 378 GLU F 379 -1 O LYS F 378 N THR F 363
SHEET 1 FK 4 PHE F 387 VAL F 391 0
SHEET 2 FK 4 LEU F 406 SER F 410 -1 O ARG F 407 N HIS F 390
SHEET 3 FK 4 VAL F 416 GLU F 420 -1 O VAL F 416 N TYR F 408
SHEET 4 FK 4 ARG F 427 ALA F 432 -1 O LYS F 428 N ASP F 419
SHEET 1 FL 8 TYR F 444 THR F 452 0
SHEET 2 FL 8 LYS F 458 ASP F 466 -1 O VAL F 459 N ALA F 451
SHEET 3 FL 8 ILE F 506 ALA F 510 -1 O TYR F 507 N VAL F 464
SHEET 4 FL 8 THR F 477 TYR F 480 1 O MET F 478 N ALA F 508
SHEET 5 FL 8 LEU F 557 ARG F 562 1 O SER F 558 N LEU F 479
SHEET 6 FL 8 VAL F 582 GLY F 586 1 O VAL F 582 N CYS F 559
SHEET 7 FL 8 HIS F 639 GLY F 645 1 O HIS F 639 N ALA F 583
SHEET 8 FL 8 VAL F 673 ASP F 678 1 O LEU F 674 N ILE F 642
LINK C1 FC0 G 1 N ARG G 2 1555 1555 1.37
LINK N1 OAR G 4 C VAL G 3 1555 1555 1.34
LINK C1 FC0 H 1 N ARG H 2 1555 1555 1.34
LINK N1 OAR H 4 C VAL H 3 1555 1555 1.33
LINK C1 FC0 I 1 N ARG I 2 1555 1555 1.34
LINK N1 OAR I 4 C VAL I 3 1555 1555 1.34
LINK C1 FC0 J 1 N ARG J 2 1555 1555 1.34
LINK N1 OAR J 4 C VAL J 3 1555 1555 1.35
LINK C1 FC0 K 1 N ARG K 2 1555 1555 1.36
LINK N1 OAR K 4 C VAL K 3 1555 1555 1.35
LINK C1 FC0 L 1 N ARG L 2 1555 1555 1.32
LINK N1 OAR L 4 C VAL L 3 1555 1555 1.32
CISPEP 1 ASP A 32 PRO A 33 0 2.50
CISPEP 2 TYR A 482 GLY A 483 0 -15.32
CISPEP 3 ASP B 32 PRO B 33 0 1.67
CISPEP 4 ASP C 32 PRO C 33 0 -0.74
CISPEP 5 ASP D 32 PRO D 33 0 -1.21
CISPEP 6 ASP E 32 PRO E 33 0 2.44
CISPEP 7 TYR E 482 GLY E 483 0 -22.05
CISPEP 8 ASP F 32 PRO F 33 0 -4.87
CISPEP 9 TYR F 482 GLY F 483 0 -23.29
SITE 1 AC1 14 ASN A 191 LYS A 208 LYS A 212 ASP A 214
SITE 2 AC1 14 TYR A 482 TYR A 485 SER A 563 ALA A 564
SITE 3 AC1 14 PHE A 589 GLU A 607 ARG A 650 VAL A 651
SITE 4 AC1 14 HOH A2039 HOH A2105
SITE 1 AC2 13 GLU B 172 LYS B 208 ASP B 214 TYR B 482
SITE 2 AC2 13 TYR B 485 SER B 563 ALA B 564 PHE B 589
SITE 3 AC2 13 LEU B 603 GLU B 607 ARG B 650 VAL B 651
SITE 4 AC2 13 GLU B 655
SITE 1 AC3 14 GLU C 172 ASN C 191 LYS C 208 ASP C 214
SITE 2 AC3 14 TYR C 482 TYR C 485 SER C 563 ALA C 564
SITE 3 AC3 14 PHE C 589 GLU C 607 ARG C 650 VAL C 651
SITE 4 AC3 14 GLU C 655 HOH C2008
SITE 1 AC4 12 GLU D 172 LYS D 208 ASP D 214 TYR D 482
SITE 2 AC4 12 TYR D 485 SER D 563 ALA D 564 PHE D 589
SITE 3 AC4 12 LEU D 603 GLU D 607 ARG D 650 VAL D 651
SITE 1 AC5 13 ASN E 191 LYS E 208 LYS E 212 ASP E 214
SITE 2 AC5 13 TYR E 482 TYR E 485 SER E 563 ALA E 564
SITE 3 AC5 13 PHE E 589 GLU E 607 ARG E 650 VAL E 651
SITE 4 AC5 13 HOH E2015
SITE 1 AC6 13 GLU F 172 LYS F 208 LYS F 212 ASP F 214
SITE 2 AC6 13 TYR F 482 TYR F 485 SER F 563 ALA F 564
SITE 3 AC6 13 PHE F 589 GLU F 607 ARG F 650 HOH F2013
SITE 4 AC6 13 HOH F2039
CRYST1 71.800 148.800 268.000 90.00 91.00 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013928 0.000000 0.000243 0.00000
SCALE2 0.000000 0.006720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003732 0.00000
ATOM 1 N ARG A 5 0.375 116.084 208.516 1.00 55.86 N
ANISOU 1 N ARG A 5 3628 11937 5657 387 -935 2668 N
ATOM 2 CA ARG A 5 1.671 116.647 209.047 1.00 53.85 C
ANISOU 2 CA ARG A 5 3662 11416 5382 504 -741 2480 C
ATOM 3 C ARG A 5 1.747 116.484 210.544 1.00 53.32 C
ANISOU 3 C ARG A 5 3633 11184 5441 589 -523 2357 C
ATOM 4 O ARG A 5 1.183 115.539 211.079 1.00 54.70 O
ANISOU 4 O ARG A 5 3703 11428 5652 477 -543 2323 O
ATOM 5 CB ARG A 5 1.767 118.116 208.753 1.00 54.33 C
ANISOU 5 CB ARG A 5 3734 11404 5506 734 -658 2642 C
ATOM 6 CG ARG A 5 3.158 118.672 208.673 1.00 51.51 C
ANISOU 6 CG ARG A 5 3674 10843 5054 770 -562 2482 C
ATOM 7 CD ARG A 5 3.024 120.008 207.934 1.00 54.14 C
ANISOU 7 CD ARG A 5 3980 11173 5417 939 -566 2705 C
ATOM 8 NE ARG A 5 4.278 120.701 207.670 1.00 51.99 N
ANISOU 8 NE ARG A 5 3973 10729 5055 967 -490 2602 N
ATOM 9 CZ ARG A 5 4.365 122.005 207.406 1.00 52.86 C
ANISOU 9 CZ ARG A 5 4123 10738 5221 1144 -416 2757 C
ATOM 10 NH1 ARG A 5 3.270 122.771 207.364 1.00 55.29 N
ANISOU 10 NH1 ARG A 5 4227 11097 5685 1335 -404 3024 N
ATOM 11 NH2 ARG A 5 5.556 122.548 207.192 1.00 51.62 N
ANISOU 11 NH2 ARG A 5 4212 10428 4975 1134 -349 2650 N
ATOM 12 N GLY A 6 2.439 117.409 211.224 1.00 52.19 N
ANISOU 12 N GLY A 6 3652 10824 5356 773 -317 2294 N
ATOM 13 CA GLY A 6 2.657 117.357 212.696 1.00 49.26 C
ANISOU 13 CA GLY A 6 3366 10274 5075 853 -97 2160 C
ATOM 14 C GLY A 6 2.513 118.742 213.332 1.00 49.58 C
ANISOU 14 C GLY A 6 3417 10162 5257 1126 123 2257 C
ATOM 15 O GLY A 6 2.373 119.745 212.625 1.00 50.86 O
ANISOU 15 O GLY A 6 3545 10330 5450 1256 107 2418 O
ATOM 16 N PRO A 7 2.504 118.808 214.671 1.00 49.01 N
ANISOU 16 N PRO A 7 3402 9950 5270 1213 332 2167 N
ATOM 17 CA PRO A 7 2.406 120.086 215.361 1.00 49.81 C
ANISOU 17 CA PRO A 7 3555 9878 5494 1464 564 2225 C
ATOM 18 C PRO A 7 3.615 120.986 215.088 1.00 48.65 C
ANISOU 18 C PRO A 7 3677 9534 5272 1510 607 2134 C
ATOM 19 O PRO A 7 4.759 120.544 215.118 1.00 46.51 O
ANISOU 19 O PRO A 7 3615 9187 4871 1365 565 1934 O
ATOM 20 CB PRO A 7 2.365 119.683 216.853 1.00 49.09 C
ANISOU 20 CB PRO A 7 3526 9683 5443 1473 754 2087 C
ATOM 21 CG PRO A 7 1.849 118.338 216.868 1.00 48.99 C
ANISOU 21 CG PRO A 7 3362 9850 5403 1285 625 2073 C
ATOM 22 CD PRO A 7 2.371 117.683 215.612 1.00 48.13 C
ANISOU 22 CD PRO A 7 3283 9852 5153 1087 366 2037 C
ATOM 23 N ILE A 8 3.345 122.252 214.847 1.00 50.25 N
ANISOU 23 N ILE A 8 3870 9654 5569 1716 698 2289 N
ATOM 24 CA ILE A 8 4.375 123.250 214.692 1.00 49.59 C
ANISOU 24 CA ILE A 8 4038 9363 5439 1773 769 2226 C
ATOM 25 C ILE A 8 3.956 124.394 215.631 1.00 51.08 C
ANISOU 25 C ILE A 8 4275 9352 5783 2025 1032 2281 C
ATOM 26 O ILE A 8 2.847 124.914 215.501 1.00 53.50 O
ANISOU 26 O ILE A 8 4377 9715 6237 2213 1084 2498 O
ATOM 27 CB ILE A 8 4.394 123.712 213.226 1.00 50.59 C
ANISOU 27 CB ILE A 8 4114 9589 5520 1769 597 2396 C
ATOM 28 CG1 ILE A 8 4.853 122.553 212.333 1.00 49.25 C
ANISOU 28 CG1 ILE A 8 3931 9605 5175 1511 359 2310 C
ATOM 29 CG2 ILE A 8 5.229 124.962 213.046 1.00 50.63 C
ANISOU 29 CG2 ILE A 8 4348 9375 5516 1864 694 2393 C
ATOM 30 CD1 ILE A 8 4.544 122.720 210.859 1.00 50.69 C
ANISOU 30 CD1 ILE A 8 4002 9965 5294 1475 156 2502 C
ATOM 31 N ALA A 9 4.789 124.768 216.596 1.00 49.93 N
ANISOU 31 N ALA A 9 4388 8975 5607 2033 1201 2091 N
ATOM 32 CA ALA A 9 4.425 125.889 217.464 1.00 51.58 C
ANISOU 32 CA ALA A 9 4682 8971 5945 2265 1462 2124 C
ATOM 33 C ALA A 9 4.512 127.268 216.779 1.00 53.23 C
ANISOU 33 C ALA A 9 4973 9032 6219 2433 1506 2273 C
ATOM 34 O ALA A 9 5.183 127.439 215.781 1.00 52.61 O
ANISOU 34 O ALA A 9 4963 8972 6053 2338 1355 2299 O
ATOM 35 CB ALA A 9 5.225 125.859 218.728 1.00 50.17 C
ANISOU 35 CB ALA A 9 4763 8599 5699 2205 1620 1878 C
ATOM 36 N ALA A 10 3.821 128.248 217.338 1.00 55.51 N
ANISOU 36 N ALA A 10 5263 9165 6664 2686 1727 2371 N
ATOM 37 CA ALA A 10 3.729 129.569 216.732 1.00 57.57 C
ANISOU 37 CA ALA A 10 5586 9270 7018 2878 1785 2543 C
ATOM 38 C ALA A 10 4.885 130.449 217.133 1.00 56.91 C
ANISOU 38 C ALA A 10 5874 8879 6869 2851 1910 2377 C
ATOM 39 O ALA A 10 5.364 130.388 218.243 1.00 55.97 O
ANISOU 39 O ALA A 10 5951 8614 6703 2799 2056 2163 O
ATOM 40 CB ALA A 10 2.425 130.228 217.118 1.00 60.70 C
ANISOU 40 CB ALA A 10 5807 9629 7628 3185 1977 2737 C
ATOM 41 N HIS A 11 5.281 131.311 216.226 1.00 57.70 N
ANISOU 41 N HIS A 11 6070 8884 6968 2885 1852 2493 N
ATOM 42 CA HIS A 11 6.403 132.190 216.423 1.00 57.31 C
ANISOU 42 CA HIS A 11 6364 8554 6856 2831 1941 2363 C
ATOM 43 C HIS A 11 6.007 133.430 217.142 1.00 59.82 C
ANISOU 43 C HIS A 11 6842 8569 7320 3080 2214 2398 C
ATOM 44 O HIS A 11 5.143 134.127 216.695 1.00 62.39 O
ANISOU 44 O HIS A 11 7047 8862 7797 3317 2265 2632 O
ATOM 45 CB HIS A 11 6.932 132.563 215.057 1.00 57.35 C
ANISOU 45 CB HIS A 11 6391 8602 6797 2755 1760 2498 C
ATOM 46 CG HIS A 11 7.490 131.392 214.323 1.00 54.95 C
ANISOU 46 CG HIS A 11 5984 8568 6326 2496 1510 2431 C
ATOM 47 ND1 HIS A 11 8.529 131.499 213.427 1.00 53.94 N
ANISOU 47 ND1 HIS A 11 5980 8453 6063 2322 1375 2410 N
ATOM 48 CD2 HIS A 11 7.189 130.073 214.408 1.00 53.46 C
ANISOU 48 CD2 HIS A 11 5602 8631 6082 2377 1389 2364 C
ATOM 49 CE1 HIS A 11 8.828 130.296 212.974 1.00 52.00 C
ANISOU 49 CE1 HIS A 11 5618 8455 5686 2123 1189 2330 C
ATOM 50 NE2 HIS A 11 8.031 129.414 213.555 1.00 51.67 N
ANISOU 50 NE2 HIS A 11 5391 8552 5690 2149 1189 2299 N
ATOM 51 N ARG A 12 6.629 133.690 218.277 1.00 59.28 N
ANISOU 51 N ARG A 12 7048 8274 7201 3028 2389 2165 N
ATOM 52 CA ARG A 12 6.476 134.945 218.975 1.00 61.70 C
ANISOU 52 CA ARG A 12 7591 8240 7613 3229 2659 2151 C
ATOM 53 C ARG A 12 7.871 135.536 219.105 1.00 60.75 C
ANISOU 53 C ARG A 12 7835 7884 7364 3035 2664 1972 C
ATOM 54 O ARG A 12 8.779 134.860 219.625 1.00 58.36 O
ANISOU 54 O ARG A 12 7642 7628 6903 2787 2599 1747 O
ATOM 55 CB ARG A 12 5.850 134.718 220.335 1.00 62.37 C
ANISOU 55 CB ARG A 12 7684 8272 7743 3336 2887 2025 C
ATOM 56 CG ARG A 12 4.644 133.807 220.305 1.00 62.67 C
ANISOU 56 CG ARG A 12 7338 8605 7868 3437 2849 2159 C
ATOM 57 CD ARG A 12 3.532 134.374 221.144 1.00 65.64 C
ANISOU 57 CD ARG A 12 7670 8854 8416 3740 3145 2221 C
ATOM 58 NE ARG A 12 2.467 133.407 221.383 1.00 65.82 N
ANISOU 58 NE ARG A 12 7344 9160 8503 3795 3137 2303 N
ATOM 59 CZ ARG A 12 2.308 132.735 222.523 1.00 65.16 C
ANISOU 59 CZ ARG A 12 7274 9120 8364 3734 3262 2134 C
ATOM 60 NH1 ARG A 12 3.152 132.916 223.535 1.00 64.27 N
ANISOU 60 NH1 ARG A 12 7509 8792 8117 3618 3396 1870 N
ATOM 61 NH2 ARG A 12 1.299 131.881 222.659 1.00 65.57 N
ANISOU 61 NH2 ARG A 12 6992 9436 8485 3778 3250 2235 N
ATOM 62 N PRO A 13 8.073 136.781 218.605 1.00 62.73 N
ANISOU 62 N PRO A 13 8267 7887 7682 3135 2729 2085 N
ATOM 63 CA PRO A 13 9.435 137.348 218.580 1.00 61.97 C
ANISOU 63 CA PRO A 13 8497 7587 7462 2917 2707 1939 C
ATOM 64 C PRO A 13 9.939 137.657 219.995 1.00 62.09 C
ANISOU 64 C PRO A 13 8824 7351 7417 2848 2908 1670 C
ATOM 65 O PRO A 13 9.210 138.205 220.836 1.00 64.28 O
ANISOU 65 O PRO A 13 9193 7432 7797 3062 3153 1650 O
ATOM 66 CB PRO A 13 9.273 138.623 217.762 1.00 64.62 C
ANISOU 66 CB PRO A 13 8933 7708 7913 3081 2755 2158 C
ATOM 67 CG PRO A 13 7.873 139.073 218.074 1.00 67.48 C
ANISOU 67 CG PRO A 13 9169 7990 8481 3440 2947 2319 C
ATOM 68 CD PRO A 13 7.061 137.783 218.221 1.00 66.10 C
ANISOU 68 CD PRO A 13 8633 8172 8311 3460 2860 2337 C
ATOM 69 N HIS A 14 11.168 137.238 220.252 1.00 59.84 N
ANISOU 69 N HIS A 14 8685 7095 6958 2547 2800 1466 N
ATOM 70 CA HIS A 14 11.816 137.431 221.527 1.00 59.77 C
ANISOU 70 CA HIS A 14 8971 6887 6850 2418 2934 1206 C
ATOM 71 C HIS A 14 13.270 137.537 221.179 1.00 58.35 C
ANISOU 71 C HIS A 14 8959 6681 6529 2117 2784 1105 C
ATOM 72 O HIS A 14 13.779 136.729 220.400 1.00 56.15 O
ANISOU 72 O HIS A 14 8495 6663 6176 1960 2562 1137 O
ATOM 73 CB HIS A 14 11.585 136.229 222.427 1.00 58.00 C
ANISOU 73 CB HIS A 14 8617 6871 6551 2355 2922 1061 C
ATOM 74 CG HIS A 14 12.433 136.224 223.661 1.00 57.51 C
ANISOU 74 CG HIS A 14 8840 6670 6342 2159 2995 792 C
ATOM 75 ND1 HIS A 14 11.948 136.579 224.901 1.00 59.23 N
ANISOU 75 ND1 HIS A 14 9240 6700 6563 2266 3238 669 N
ATOM 76 CD2 HIS A 14 13.733 135.896 223.848 1.00 55.69 C
ANISOU 76 CD2 HIS A 14 8739 6473 5950 1859 2853 629 C
ATOM 77 CE1 HIS A 14 12.913 136.475 225.797 1.00 58.47 C
ANISOU 77 CE1 HIS A 14 9387 6530 6301 2026 3229 440 C
ATOM 78 NE2 HIS A 14 14.006 136.057 225.185 1.00 56.33 N
ANISOU 78 NE2 HIS A 14 9075 6394 5935 1779 2992 419 N
ATOM 79 N GLU A 15 13.961 138.535 221.714 1.00 59.77 N
ANISOU 79 N GLU A 15 9488 6549 6671 2028 2904 985 N
ATOM 80 CA GLU A 15 15.401 138.558 221.477 1.00 58.44 C
ANISOU 80 CA GLU A 15 9457 6384 6363 1711 2755 879 C
ATOM 81 C GLU A 15 16.146 137.919 222.639 1.00 56.97 C
ANISOU 81 C GLU A 15 9381 6242 6022 1486 2733 621 C
ATOM 82 O GLU A 15 15.784 138.068 223.817 1.00 58.02 O
ANISOU 82 O GLU A 15 9675 6230 6138 1544 2903 484 O
ATOM 83 CB GLU A 15 15.941 139.945 221.067 1.00 60.66 C
ANISOU 83 CB GLU A 15 10021 6351 6676 1672 2825 934 C
ATOM 84 CG GLU A 15 16.293 140.909 222.194 1.00 62.76 C
ANISOU 84 CG GLU A 15 10688 6250 6909 1611 3021 750 C
ATOM 85 CD GLU A 15 16.580 142.321 221.672 1.00 68.65 C
ANISOU 85 CD GLU A 15 11700 6661 7724 1621 3106 847 C
ATOM 86 OE1 GLU A 15 17.106 142.460 220.531 1.00 67.64 O
ANISOU 86 OE1 GLU A 15 11490 6615 7594 1522 2957 993 O
ATOM 87 OE2 GLU A 15 16.265 143.295 222.411 1.00 74.09 O
ANISOU 87 OE2 GLU A 15 12693 6994 8465 1729 3334 776 O
ATOM 88 N VAL A 16 17.159 137.153 222.267 1.00 54.63 N
ANISOU 88 N VAL A 16 8979 6167 5612 1239 2521 567 N
ATOM 89 CA VAL A 16 18.026 136.514 223.233 1.00 53.23 C
ANISOU 89 CA VAL A 16 8882 6058 5285 1003 2457 350 C
ATOM 90 C VAL A 16 19.378 137.182 223.061 1.00 53.62 C
ANISOU 90 C VAL A 16 9136 5985 5250 739 2388 283 C
ATOM 91 O VAL A 16 19.785 137.468 221.961 1.00 53.54 O
ANISOU 91 O VAL A 16 9061 6013 5267 691 2299 409 O
ATOM 92 CB VAL A 16 18.013 134.977 223.073 1.00 50.46 C
ANISOU 92 CB VAL A 16 8220 6065 4885 957 2281 342 C
ATOM 93 CG1 VAL A 16 17.951 134.600 221.607 1.00 49.39 C
ANISOU 93 CG1 VAL A 16 7828 6139 4800 992 2129 523 C
ATOM 94 CG2 VAL A 16 19.191 134.351 223.745 1.00 48.99 C
ANISOU 94 CG2 VAL A 16 8094 5971 4550 685 2161 161 C
ATOM 95 N VAL A 17 20.019 137.520 224.166 1.00 54.40 N
ANISOU 95 N VAL A 17 9501 5923 5247 565 2444 93 N
ATOM 96 CA VAL A 17 21.242 138.316 224.138 1.00 55.38 C
ANISOU 96 CA VAL A 17 9853 5891 5296 302 2401 26 C
ATOM 97 C VAL A 17 22.431 137.426 224.471 1.00 53.45 C
ANISOU 97 C VAL A 17 9522 5875 4911 16 2206 -99 C
ATOM 98 O VAL A 17 22.290 136.513 225.251 1.00 52.22 O
ANISOU 98 O VAL A 17 9285 5864 4691 12 2171 -198 O
ATOM 99 CB VAL A 17 21.154 139.483 225.158 1.00 58.25 C
ANISOU 99 CB VAL A 17 10620 5874 5637 287 2605 -102 C
ATOM 100 CG1 VAL A 17 22.406 140.302 225.120 1.00 59.44 C
ANISOU 100 CG1 VAL A 17 11009 5866 5711 -12 2549 -168 C
ATOM 101 CG2 VAL A 17 19.914 140.340 224.911 1.00 60.44 C
ANISOU 101 CG2 VAL A 17 10980 5912 6073 611 2822 23 C
ATOM 102 N PHE A 18 23.584 137.691 223.868 1.00 53.35 N
ANISOU 102 N PHE A 18 9517 5898 4858 -214 2083 -80 N
ATOM 103 CA PHE A 18 24.840 136.941 224.081 1.00 51.88 C
ANISOU 103 CA PHE A 18 9229 5929 4554 -490 1895 -176 C
ATOM 104 C PHE A 18 25.954 137.923 224.384 1.00 53.75 C
ANISOU 104 C PHE A 18 9726 5977 4719 -775 1885 -255 C
ATOM 105 O PHE A 18 26.268 138.799 223.555 1.00 54.97 O
ANISOU 105 O PHE A 18 9956 6008 4923 -828 1907 -153 O
ATOM 106 CB PHE A 18 25.228 136.164 222.818 1.00 49.92 C
ANISOU 106 CB PHE A 18 8659 5974 4336 -497 1738 -48 C
ATOM 107 CG PHE A 18 24.488 134.898 222.649 1.00 47.80 C
ANISOU 107 CG PHE A 18 8115 5952 4095 -317 1684 -14 C
ATOM 108 CD1 PHE A 18 23.249 134.890 222.039 1.00 47.79 C
ANISOU 108 CD1 PHE A 18 8010 5950 4198 -49 1761 120 C
ATOM 109 CD2 PHE A 18 25.031 133.718 223.091 1.00 46.02 C
ANISOU 109 CD2 PHE A 18 7733 5958 3795 -420 1549 -105 C
ATOM 110 CE1 PHE A 18 22.561 133.733 221.876 1.00 46.04 C
ANISOU 110 CE1 PHE A 18 7540 5954 3999 91 1703 153 C
ATOM 111 CE2 PHE A 18 24.351 132.538 222.947 1.00 44.23 C
ANISOU 111 CE2 PHE A 18 7272 5939 3594 -268 1500 -76 C
ATOM 112 CZ PHE A 18 23.109 132.541 222.346 1.00 44.22 C
ANISOU 112 CZ PHE A 18 7176 5936 3691 -23 1576 48 C
ATOM 113 N GLY A 19 26.554 137.787 225.553 1.00 54.14 N
ANISOU 113 N GLY A 19 9916 6008 4645 -973 1845 -425 N
ATOM 114 CA GLY A 19 27.498 138.794 226.003 1.00 56.36 C
ANISOU 114 CA GLY A 19 10486 6081 4848 -1257 1846 -516 C
ATOM 115 C GLY A 19 27.071 139.458 227.288 1.00 58.50 C
ANISOU 115 C GLY A 19 11118 6065 5046 -1267 1999 -676 C
ATOM 116 O GLY A 19 26.297 138.894 228.048 1.00 57.93 O
ANISOU 116 O GLY A 19 11039 6026 4946 -1111 2065 -745 O
ATOM 117 N LYS A 20 27.572 140.671 227.517 1.00 61.16 N
ANISOU 117 N LYS A 20 11782 6111 5346 -1458 2063 -735 N
ATOM 118 CA LYS A 20 27.382 141.373 228.802 1.00 63.64 C
ANISOU 118 CA LYS A 20 12494 6134 5554 -1535 2200 -921 C
ATOM 119 C LYS A 20 25.951 141.857 229.014 1.00 64.86 C
ANISOU 119 C LYS A 20 12811 6033 5800 -1190 2464 -914 C
ATOM 120 O LYS A 20 25.348 142.458 228.115 1.00 65.49 O
ANISOU 120 O LYS A 20 12879 5970 6033 -981 2576 -766 O
ATOM 121 CB LYS A 20 28.346 142.549 228.908 1.00 66.37 C
ANISOU 121 CB LYS A 20 13154 6228 5837 -1856 2190 -984 C
ATOM 122 CG LYS A 20 28.461 143.152 230.263 1.00 68.97 C
ANISOU 122 CG LYS A 20 13892 6303 6009 -2033 2275 -1201 C
ATOM 123 CD LYS A 20 29.479 144.276 230.269 1.00 71.72 C
ANISOU 123 CD LYS A 20 14533 6419 6298 -2386 2238 -1254 C
ATOM 124 CE LYS A 20 29.737 144.714 231.706 1.00 74.27 C
ANISOU 124 CE LYS A 20 15257 6542 6421 -2623 2277 -1494 C
ATOM 125 NZ LYS A 20 30.648 145.889 231.806 1.00 77.43 N
ANISOU 125 NZ LYS A 20 15996 6672 6753 -2986 2256 -1564 N
ATOM 126 N VAL A 21 25.415 141.572 230.200 1.00 65.32 N
ANISOU 126 N VAL A 21 13008 6050 5762 -1129 2562 -1064 N
ATOM 127 CA VAL A 21 24.088 142.042 230.610 1.00 66.92 C
ANISOU 127 CA VAL A 21 13386 6006 6034 -814 2839 -1086 C
ATOM 128 C VAL A 21 24.127 142.486 232.072 1.00 69.36 C
ANISOU 128 C VAL A 21 14098 6091 6166 -950 2966 -1324 C
ATOM 129 O VAL A 21 24.335 141.666 232.984 1.00 68.45 O
ANISOU 129 O VAL A 21 13949 6163 5895 -1066 2881 -1442 O
ATOM 130 CB VAL A 21 22.967 140.975 230.395 1.00 64.62 C
ANISOU 130 CB VAL A 21 12749 5963 5841 -482 2872 -980 C
ATOM 131 CG1 VAL A 21 21.595 141.545 230.759 1.00 66.64 C
ANISOU 131 CG1 VAL A 21 13164 5966 6192 -146 3174 -981 C
ATOM 132 CG2 VAL A 21 22.959 140.465 228.949 1.00 62.28 C
ANISOU 132 CG2 VAL A 21 12064 5909 5692 -375 2728 -757 C
ATOM 133 N GLU A 22 23.942 143.791 232.273 1.00 72.65 N
ANISOU 133 N GLU A 22 14908 6097 6599 -940 3169 -1391 N
ATOM 134 CA GLU A 22 23.906 144.392 233.598 1.00 75.57 C
ANISOU 134 CA GLU A 22 15723 6192 6799 -1056 3329 -1628 C
ATOM 135 C GLU A 22 22.962 143.654 234.530 1.00 75.11 C
ANISOU 135 C GLU A 22 15625 6238 6675 -849 3464 -1712 C
ATOM 136 O GLU A 22 21.806 143.434 234.188 1.00 74.54 O
ANISOU 136 O GLU A 22 15372 6188 6762 -478 3622 -1597 O
ATOM 137 CB GLU A 22 23.472 145.844 233.495 1.00 79.16 C
ANISOU 137 CB GLU A 22 16565 6168 7343 -943 3590 -1650 C
ATOM 138 CG GLU A 22 24.506 146.736 232.846 1.00 80.46 C
ANISOU 138 CG GLU A 22 16885 6161 7524 -1225 3478 -1613 C
ATOM 139 CD GLU A 22 25.525 147.317 233.838 1.00 82.98 C
ANISOU 139 CD GLU A 22 17619 6299 7611 -1657 3423 -1847 C
ATOM 140 OE1 GLU A 22 25.113 148.035 234.789 1.00 86.12 O
ANISOU 140 OE1 GLU A 22 18450 6358 7914 -1640 3651 -2036 O
ATOM 141 OE2 GLU A 22 26.743 147.072 233.645 1.00 82.03 O
ANISOU 141 OE2 GLU A 22 17390 6374 7401 -2019 3154 -1840 O
ATOM 142 N GLY A 23 23.480 143.276 235.701 1.00 75.52 N
ANISOU 142 N GLY A 23 15842 6366 6489 -1103 3391 -1902 N
ATOM 143 CA GLY A 23 22.693 142.667 236.790 1.00 75.68 C
ANISOU 143 CA GLY A 23 15907 6455 6394 -968 3531 -2015 C
ATOM 144 C GLY A 23 22.853 141.162 236.810 1.00 72.19 C
ANISOU 144 C GLY A 23 15055 6462 5911 -994 3302 -1940 C
ATOM 145 O GLY A 23 22.666 140.511 237.837 1.00 72.14 O
ANISOU 145 O GLY A 23 15094 6576 5741 -1033 3315 -2048 O
ATOM 146 N GLU A 24 23.202 140.624 235.645 1.00 69.43 N
ANISOU 146 N GLU A 24 14318 6350 5710 -972 3098 -1751 N
ATOM 147 CA GLU A 24 23.400 139.193 235.451 1.00 66.07 C
ANISOU 147 CA GLU A 24 13483 6338 5281 -982 2872 -1659 C
ATOM 148 C GLU A 24 24.874 138.849 235.421 1.00 65.12 C
ANISOU 148 C GLU A 24 13294 6405 5044 -1354 2565 -1681 C
ATOM 149 O GLU A 24 25.738 139.727 235.351 1.00 66.83 O
ANISOU 149 O GLU A 24 13729 6455 5211 -1603 2512 -1736 O
ATOM 150 CB GLU A 24 22.780 138.720 234.136 1.00 63.69 C
ANISOU 150 CB GLU A 24 12780 6200 5219 -700 2850 -1434 C
ATOM 151 CG GLU A 24 21.299 139.001 233.988 1.00 64.54 C
ANISOU 151 CG GLU A 24 12873 6169 5480 -312 3127 -1364 C
ATOM 152 CD GLU A 24 20.621 138.061 232.995 1.00 61.80 C
ANISOU 152 CD GLU A 24 12072 6100 5310 -67 3054 -1159 C
ATOM 153 OE1 GLU A 24 21.067 136.889 232.855 1.00 59.17 O
ANISOU 153 OE1 GLU A 24 11461 6087 4935 -170 2831 -1122 O
ATOM 154 OE2 GLU A 24 19.625 138.502 232.373 1.00 62.51 O
ANISOU 154 OE2 GLU A 24 12093 6080 5579 229 3222 -1034 O
ATOM 155 N ASP A 25 25.148 137.555 235.452 1.00 62.53 N
ANISOU 155 N ASP A 25 12649 6425 4684 -1387 2365 -1626 N
ATOM 156 CA ASP A 25 26.492 137.079 235.546 1.00 61.73 C
ANISOU 156 CA ASP A 25 12447 6534 4474 -1710 2078 -1640 C
ATOM 157 C ASP A 25 26.685 136.177 234.367 1.00 58.68 C
ANISOU 157 C ASP A 25 11612 6434 4248 -1607 1913 -1458 C
ATOM 158 O ASP A 25 26.120 135.094 234.303 1.00 56.60 O
ANISOU 158 O ASP A 25 11091 6382 4031 -1427 1887 -1391 O
ATOM 159 CB ASP A 25 26.703 136.353 236.886 1.00 62.01 C
ANISOU 159 CB ASP A 25 12572 6702 4289 -1863 1996 -1762 C
ATOM 160 CG ASP A 25 27.906 135.415 236.865 1.00 60.42 C
ANISOU 160 CG ASP A 25 12116 6819 4022 -2101 1673 -1714 C
ATOM 161 OD1 ASP A 25 29.059 135.868 236.583 1.00 61.17 O
ANISOU 161 OD1 ASP A 25 12229 6921 4091 -2371 1511 -1714 O
ATOM 162 OD2 ASP A 25 27.679 134.206 237.111 1.00 58.54 O
ANISOU 162 OD2 ASP A 25 11647 6825 3770 -2009 1587 -1666 O
ATOM 163 N ARG A 26 27.470 136.657 233.415 1.00 58.62 N
ANISOU 163 N ARG A 26 11528 6420 4323 -1728 1813 -1380 N
ATOM 164 CA ARG A 26 27.664 135.991 232.127 1.00 56.11 C
ANISOU 164 CA ARG A 26 10818 6339 4161 -1628 1687 -1208 C
ATOM 165 C ARG A 26 29.110 135.586 231.988 1.00 55.55 C
ANISOU 165 C ARG A 26 10593 6484 4028 -1922 1429 -1196 C
ATOM 166 O ARG A 26 29.590 135.380 230.895 1.00 54.30 O
ANISOU 166 O ARG A 26 10185 6469 3977 -1923 1332 -1076 O
ATOM 167 CB ARG A 26 27.272 136.920 231.000 1.00 56.69 C
ANISOU 167 CB ARG A 26 10915 6229 4394 -1487 1815 -1099 C
ATOM 168 CG ARG A 26 25.833 137.322 230.992 1.00 57.36 C
ANISOU 168 CG ARG A 26 11101 6117 4576 -1164 2066 -1075 C
ATOM 169 CD ARG A 26 24.941 136.155 230.717 1.00 54.97 C
ANISOU 169 CD ARG A 26 10482 6050 4355 -902 2061 -983 C
ATOM 170 NE ARG A 26 23.558 136.605 230.608 1.00 55.87 N
ANISOU 170 NE ARG A 26 10656 5988 4583 -588 2301 -932 N
ATOM 171 CZ ARG A 26 22.826 136.669 229.487 1.00 55.20 C
ANISOU 171 CZ ARG A 26 10376 5924 4672 -345 2353 -762 C
ATOM 172 NH1 ARG A 26 23.286 136.290 228.307 1.00 53.50 N
ANISOU 172 NH1 ARG A 26 9898 5898 4531 -371 2192 -629 N
ATOM 173 NH2 ARG A 26 21.586 137.109 229.556 1.00 56.43 N
ANISOU 173 NH2 ARG A 26 10596 5918 4927 -67 2573 -720 N
ATOM 174 N GLY A 27 29.809 135.491 233.115 1.00 56.72 N
ANISOU 174 N GLY A 27 10893 6661 3998 -2176 1321 -1319 N
ATOM 175 CA GLY A 27 31.165 134.976 233.151 1.00 56.38 C
ANISOU 175 CA GLY A 27 10672 6857 3891 -2448 1062 -1301 C
ATOM 176 C GLY A 27 32.194 136.067 233.299 1.00 58.91 C
ANISOU 176 C GLY A 27 11215 7036 4134 -2785 1001 -1361 C
ATOM 177 O GLY A 27 31.866 137.258 233.306 1.00 60.93 O
ANISOU 177 O GLY A 27 11781 6982 4389 -2807 1167 -1418 O
ATOM 178 N ALA A 28 33.446 135.638 233.396 1.00 58.95 N
ANISOU 178 N ALA A 28 11048 7269 4081 -3045 763 -1338 N
ATOM 179 CA ALA A 28 34.554 136.509 233.688 1.00 61.51 C
ANISOU 179 CA ALA A 28 11546 7517 4308 -3419 658 -1393 C
ATOM 180 C ALA A 28 34.848 137.493 232.564 1.00 62.27 C
ANISOU 180 C ALA A 28 11658 7472 4531 -3472 726 -1315 C
ATOM 181 O ALA A 28 35.307 138.595 232.819 1.00 64.93 O
ANISOU 181 O ALA A 28 12281 7593 4797 -3730 745 -1385 O
ATOM 182 CB ALA A 28 35.776 135.685 234.002 1.00 61.30 C
ANISOU 182 CB ALA A 28 11263 7813 4214 -3650 379 -1355 C
ATOM 183 N ASN A 29 34.608 137.115 231.319 1.00 60.16 N
ANISOU 183 N ASN A 29 11099 7320 4438 -3249 760 -1169 N
ATOM 184 CA ASN A 29 34.981 137.993 230.222 1.00 60.97 C
ANISOU 184 CA ASN A 29 11198 7320 4647 -3320 807 -1076 C
ATOM 185 C ASN A 29 34.000 137.956 229.020 1.00 59.22 C
ANISOU 185 C ASN A 29 10848 7056 4596 -2970 965 -950 C
ATOM 186 O ASN A 29 34.292 137.371 227.982 1.00 57.50 O
ANISOU 186 O ASN A 29 10304 7065 4479 -2891 899 -821 O
ATOM 187 CB ASN A 29 36.444 137.717 229.861 1.00 61.20 C
ANISOU 187 CB ASN A 29 10965 7616 4673 -3603 589 -1005 C
ATOM 188 CG ASN A 29 36.847 138.249 228.492 1.00 61.31 C
ANISOU 188 CG ASN A 29 10846 7631 4816 -3628 624 -866 C
ATOM 189 OD1 ASN A 29 36.526 139.374 228.093 1.00 62.82 O
ANISOU 189 OD1 ASN A 29 11285 7538 5045 -3642 768 -854 O
ATOM 190 ND2 ASN A 29 37.587 137.431 227.774 1.00 59.89 N
ANISOU 190 ND2 ASN A 29 10279 7774 4702 -3636 496 -757 N
ATOM 191 N PRO A 30 32.821 138.600 229.176 1.00 59.91 N
ANISOU 191 N PRO A 30 11198 6851 4712 -2760 1179 -988 N
ATOM 192 CA PRO A 30 31.738 138.487 228.211 1.00 58.40 C
ANISOU 192 CA PRO A 30 10886 6633 4672 -2408 1319 -867 C
ATOM 193 C PRO A 30 31.772 139.598 227.154 1.00 59.74 C
ANISOU 193 C PRO A 30 11152 6603 4944 -2416 1416 -756 C
ATOM 194 O PRO A 30 32.405 140.626 227.382 1.00 62.22 O
ANISOU 194 O PRO A 30 11724 6709 5207 -2673 1426 -806 O
ATOM 195 CB PRO A 30 30.495 138.596 229.108 1.00 58.88 C
ANISOU 195 CB PRO A 30 11178 6491 4703 -2191 1497 -966 C
ATOM 196 CG PRO A 30 30.923 139.440 230.270 1.00 61.69 C
ANISOU 196 CG PRO A 30 11923 6611 4908 -2455 1523 -1136 C
ATOM 197 CD PRO A 30 32.424 139.444 230.326 1.00 62.37 C
ANISOU 197 CD PRO A 30 11941 6848 4909 -2838 1304 -1149 C
ATOM 198 N MET A 31 31.093 139.373 226.020 1.00 58.26 N
ANISOU 198 N MET A 31 10766 6481 4889 -2148 1477 -604 N
ATOM 199 CA MET A 31 31.150 140.249 224.821 1.00 59.23 C
ANISOU 199 CA MET A 31 10915 6479 5112 -2137 1542 -456 C
ATOM 200 C MET A 31 30.422 141.578 224.991 1.00 61.80 C
ANISOU 200 C MET A 31 11619 6383 5479 -2055 1746 -466 C
ATOM 201 O MET A 31 29.340 141.616 225.589 1.00 62.01 O
ANISOU 201 O MET A 31 11780 6257 5523 -1821 1887 -523 O
ATOM 202 CB MET A 31 30.561 139.537 223.615 1.00 57.00 C
ANISOU 202 CB MET A 31 10313 6407 4936 -1868 1537 -292 C
ATOM 203 CG MET A 31 31.307 138.323 223.191 1.00 54.77 C
ANISOU 203 CG MET A 31 9667 6511 4632 -1934 1360 -262 C
ATOM 204 SD MET A 31 30.610 137.584 221.699 1.00 52.59 S
ANISOU 204 SD MET A 31 9066 6454 4461 -1645 1363 -80 S
ATOM 205 CE MET A 31 29.315 136.536 222.368 1.00 50.68 C
ANISOU 205 CE MET A 31 8735 6287 4236 -1344 1397 -139 C
ATOM 206 N ASP A 32 30.998 142.647 224.436 1.00 63.87 N
ANISOU 206 N ASP A 32 12044 6458 5765 -2235 1770 -401 N
ATOM 207 CA ASP A 32 30.596 144.032 224.738 1.00 66.96 C
ANISOU 207 CA ASP A 32 12858 6405 6180 -2240 1951 -435 C
ATOM 208 C ASP A 32 31.093 144.980 223.620 1.00 68.56 C
ANISOU 208 C ASP A 32 13118 6476 6454 -2361 1965 -275 C
ATOM 209 O ASP A 32 32.302 145.193 223.449 1.00 69.33 O
ANISOU 209 O ASP A 32 13198 6652 6494 -2702 1843 -274 O
ATOM 210 CB ASP A 32 31.103 144.446 226.146 1.00 69.00 C
ANISOU 210 CB ASP A 32 13442 6484 6290 -2513 1947 -660 C
ATOM 211 CG ASP A 32 30.725 145.899 226.561 1.00 72.59 C
ANISOU 211 CG ASP A 32 14386 6440 6754 -2537 2148 -729 C
ATOM 212 OD1 ASP A 32 29.826 146.538 225.969 1.00 73.48 O
ANISOU 212 OD1 ASP A 32 14602 6317 7000 -2267 2323 -616 O
ATOM 213 OD2 ASP A 32 31.341 146.408 227.535 1.00 74.77 O
ANISOU 213 OD2 ASP A 32 14961 6550 6896 -2836 2130 -903 O
ATOM 214 N PRO A 33 30.148 145.557 222.861 1.00 69.23 N
ANISOU 214 N PRO A 33 13269 6368 6668 -2082 2113 -125 N
ATOM 215 CA PRO A 33 28.709 145.391 223.054 1.00 68.74 C
ANISOU 215 CA PRO A 33 13219 6209 6689 -1681 2264 -109 C
ATOM 216 C PRO A 33 28.227 143.991 222.689 1.00 65.32 C
ANISOU 216 C PRO A 33 12369 6173 6278 -1462 2169 -50 C
ATOM 217 O PRO A 33 28.731 143.390 221.731 1.00 63.60 O
ANISOU 217 O PRO A 33 11852 6248 6066 -1514 2032 68 O
ATOM 218 CB PRO A 33 28.109 146.419 222.104 1.00 70.63 C
ANISOU 218 CB PRO A 33 13591 6179 7066 -1501 2401 84 C
ATOM 219 CG PRO A 33 29.131 146.571 221.042 1.00 70.58 C
ANISOU 219 CG PRO A 33 13454 6312 7049 -1739 2273 221 C
ATOM 220 CD PRO A 33 30.445 146.476 221.753 1.00 70.88 C
ANISOU 220 CD PRO A 33 13548 6432 6951 -2152 2144 55 C
ATOM 221 N PRO A 34 27.236 143.485 223.433 1.00 64.55 N
ANISOU 221 N PRO A 34 12260 6076 6189 -1219 2252 -130 N
ATOM 222 CA PRO A 34 26.676 142.144 223.227 1.00 61.54 C
ANISOU 222 CA PRO A 34 11515 6041 5827 -1014 2173 -90 C
ATOM 223 C PRO A 34 26.102 141.886 221.815 1.00 60.38 C
ANISOU 223 C PRO A 34 11098 6049 5796 -789 2151 141 C
ATOM 224 O PRO A 34 25.940 142.825 221.011 1.00 62.08 O
ANISOU 224 O PRO A 34 11421 6075 6091 -734 2223 290 O
ATOM 225 CB PRO A 34 25.583 142.039 224.310 1.00 61.96 C
ANISOU 225 CB PRO A 34 11699 5958 5885 -791 2327 -203 C
ATOM 226 CG PRO A 34 25.280 143.401 224.678 1.00 65.20 C
ANISOU 226 CG PRO A 34 12501 5940 6330 -765 2522 -237 C
ATOM 227 CD PRO A 34 26.521 144.216 224.486 1.00 66.81 C
ANISOU 227 CD PRO A 34 12899 6011 6474 -1114 2451 -259 C
ATOM 228 N ARG A 35 25.834 140.614 221.522 1.00 57.68 N
ANISOU 228 N ARG A 35 10419 6047 5450 -676 2043 171 N
ATOM 229 CA ARG A 35 25.238 140.241 220.242 1.00 56.58 C
ANISOU 229 CA ARG A 35 10019 6084 5395 -474 2007 373 C
ATOM 230 C ARG A 35 23.821 139.784 220.527 1.00 56.02 C
ANISOU 230 C ARG A 35 9854 6030 5401 -148 2095 400 C
ATOM 231 O ARG A 35 23.545 139.285 221.617 1.00 55.46 O
ANISOU 231 O ARG A 35 9812 5971 5291 -122 2128 252 O
ATOM 232 CB ARG A 35 26.035 139.121 219.542 1.00 54.17 C
ANISOU 232 CB ARG A 35 9396 6159 5025 -605 1816 394 C
ATOM 233 CG ARG A 35 27.451 139.505 219.118 1.00 54.78 C
ANISOU 233 CG ARG A 35 9506 6270 5037 -919 1730 395 C
ATOM 234 CD ARG A 35 28.302 138.288 218.762 1.00 52.53 C
ANISOU 234 CD ARG A 35 8919 6358 4683 -1047 1562 365 C
ATOM 235 NE ARG A 35 29.682 138.660 218.397 1.00 53.36 N
ANISOU 235 NE ARG A 35 9031 6511 4733 -1348 1492 371 N
ATOM 236 CZ ARG A 35 30.606 137.806 217.935 1.00 52.02 C
ANISOU 236 CZ ARG A 35 8606 6645 4513 -1480 1367 367 C
ATOM 237 NH1 ARG A 35 30.317 136.512 217.773 1.00 49.74 N
ANISOU 237 NH1 ARG A 35 8058 6623 4218 -1340 1293 348 N
ATOM 238 NH2 ARG A 35 31.827 138.231 217.637 1.00 53.12 N
ANISOU 238 NH2 ARG A 35 8749 6820 4612 -1752 1322 382 N
ATOM 239 N ARG A 36 22.917 139.967 219.564 1.00 56.37 N
ANISOU 239 N ARG A 36 9784 6082 5553 91 2132 599 N
ATOM 240 CA ARG A 36 21.507 139.589 219.733 1.00 56.17 C
ANISOU 240 CA ARG A 36 9637 6085 5620 407 2215 659 C
ATOM 241 C ARG A 36 21.060 138.699 218.573 1.00 54.43 C
ANISOU 241 C ARG A 36 9071 6183 5427 524 2082 824 C
ATOM 242 O ARG A 36 21.630 138.733 217.472 1.00 54.13 O
ANISOU 242 O ARG A 36 8944 6262 5361 422 1976 937 O
ATOM 243 CB ARG A 36 20.613 140.835 219.852 1.00 59.10 C
ANISOU 243 CB ARG A 36 10236 6102 6116 630 2420 750 C
ATOM 244 CG ARG A 36 21.350 142.079 220.356 1.00 61.50 C
ANISOU 244 CG ARG A 36 10926 6048 6393 454 2524 657 C
ATOM 245 CD ARG A 36 20.497 143.326 220.472 1.00 64.67 C
ANISOU 245 CD ARG A 36 11579 6066 6926 685 2743 741 C
ATOM 246 NE ARG A 36 19.856 143.427 221.794 1.00 65.71 N
ANISOU 246 NE ARG A 36 11884 6018 7065 810 2924 574 N
ATOM 247 CZ ARG A 36 20.355 144.069 222.856 1.00 67.37 C
ANISOU 247 CZ ARG A 36 12447 5952 7198 650 3035 371 C
ATOM 248 NH1 ARG A 36 21.524 144.697 222.803 1.00 68.24 N
ANISOU 248 NH1 ARG A 36 12778 5925 7226 342 2975 307 N
ATOM 249 NH2 ARG A 36 19.667 144.094 223.982 1.00 68.37 N
ANISOU 249 NH2 ARG A 36 12713 5942 7323 790 3211 232 N
ATOM 250 N ARG A 37 20.066 137.869 218.845 1.00 53.39 N
ANISOU 250 N ARG A 37 8751 6199 5336 717 2089 829 N
ATOM 251 CA ARG A 37 19.377 137.118 217.810 1.00 52.28 C
ANISOU 251 CA ARG A 37 8307 6323 5233 857 1983 993 C
ATOM 252 C ARG A 37 17.969 136.749 218.248 1.00 52.50 C
ANISOU 252 C ARG A 37 8209 6380 5359 1125 2067 1038 C
ATOM 253 O ARG A 37 17.640 136.852 219.436 1.00 53.05 O
ANISOU 253 O ARG A 37 8406 6307 5443 1181 2200 908 O
ATOM 254 CB ARG A 37 20.159 135.889 217.395 1.00 49.71 C
ANISOU 254 CB ARG A 37 7771 6321 4797 675 1794 928 C
ATOM 255 CG ARG A 37 20.996 135.334 218.465 1.00 48.48 C
ANISOU 255 CG ARG A 37 7678 6194 4548 487 1766 706 C
ATOM 256 CD ARG A 37 21.173 133.886 218.243 1.00 46.07 C
ANISOU 256 CD ARG A 37 7115 6207 4182 436 1615 660 C
ATOM 257 NE ARG A 37 22.170 133.660 217.227 1.00 45.34 N
ANISOU 257 NE ARG A 37 6931 6274 4022 271 1490 696 N
ATOM 258 CZ ARG A 37 22.626 132.461 216.887 1.00 43.45 C
ANISOU 258 CZ ARG A 37 6491 6300 3717 190 1357 646 C
ATOM 259 NH1 ARG A 37 22.166 131.342 217.474 1.00 42.00 N
ANISOU 259 NH1 ARG A 37 6178 6251 3529 251 1316 564 N
ATOM 260 NH2 ARG A 37 23.557 132.394 215.945 1.00 43.19 N
ANISOU 260 NH2 ARG A 37 6395 6391 3623 49 1275 682 N
ATOM 261 N VAL A 38 17.125 136.367 217.286 1.00 52.35 N
ANISOU 261 N VAL A 38 7946 6544 5401 1285 1994 1227 N
ATOM 262 CA VAL A 38 15.705 136.088 217.566 1.00 52.96 C
ANISOU 262 CA VAL A 38 7867 6665 5591 1548 2070 1312 C
ATOM 263 C VAL A 38 15.538 134.598 217.758 1.00 50.57 C
ANISOU 263 C VAL A 38 7322 6665 5227 1493 1947 1228 C
ATOM 264 O VAL A 38 16.114 133.796 217.014 1.00 48.82 O
ANISOU 264 O VAL A 38 6959 6676 4915 1343 1770 1226 O
ATOM 265 CB VAL A 38 14.688 136.663 216.473 1.00 54.87 C
ANISOU 265 CB VAL A 38 7979 6909 5959 1783 2070 1600 C
ATOM 266 CG1 VAL A 38 14.554 138.188 216.594 1.00 57.79 C
ANISOU 266 CG1 VAL A 38 8612 6913 6433 1913 2250 1683 C
ATOM 267 CG2 VAL A 38 15.074 136.265 215.010 1.00 53.94 C
ANISOU 267 CG2 VAL A 38 7695 7035 5767 1673 1861 1740 C
ATOM 268 N ASP A 39 14.812 134.237 218.807 1.00 50.63 N
ANISOU 268 N ASP A 39 7306 6655 5276 1601 2054 1148 N
ATOM 269 CA ASP A 39 14.386 132.876 219.001 1.00 48.83 C
ANISOU 269 CA ASP A 39 6842 6694 5019 1588 1959 1105 C
ATOM 270 C ASP A 39 12.875 132.954 219.035 1.00 50.38 C
ANISOU 270 C ASP A 39 6873 6910 5357 1857 2057 1261 C
ATOM 271 O ASP A 39 12.296 133.328 220.059 1.00 51.66 O
ANISOU 271 O ASP A 39 7131 6915 5584 1990 2248 1208 O
ATOM 272 CB ASP A 39 14.924 132.283 220.301 1.00 47.59 C
ANISOU 272 CB ASP A 39 6794 6520 4769 1451 1993 872 C
ATOM 273 CG ASP A 39 14.423 130.858 220.535 1.00 45.93 C
ANISOU 273 CG ASP A 39 6348 6566 4536 1443 1902 840 C
ATOM 274 OD1 ASP A 39 13.345 130.514 219.998 1.00 48.27 O
ANISOU 274 OD1 ASP A 39 6419 7002 4920 1593 1879 993 O
ATOM 275 OD2 ASP A 39 15.097 130.064 221.239 1.00 44.76 O
ANISOU 275 OD2 ASP A 39 6235 6485 4287 1280 1846 674 O
ATOM 276 N PRO A 40 12.223 132.581 217.916 1.00 50.43 N
ANISOU 276 N PRO A 40 6625 7125 5410 1934 1927 1455 N
ATOM 277 CA PRO A 40 10.764 132.762 217.843 1.00 52.32 C
ANISOU 277 CA PRO A 40 6679 7396 5804 2197 2009 1642 C
ATOM 278 C PRO A 40 9.997 131.809 218.780 1.00 51.75 C
ANISOU 278 C PRO A 40 6456 7451 5754 2242 2062 1565 C
ATOM 279 O PRO A 40 8.813 132.020 219.051 1.00 53.56 O
ANISOU 279 O PRO A 40 6555 7675 6119 2464 2186 1686 O
ATOM 280 CB PRO A 40 10.448 132.465 216.377 1.00 52.33 C
ANISOU 280 CB PRO A 40 6451 7626 5806 2200 1808 1852 C
ATOM 281 CG PRO A 40 11.729 131.785 215.785 1.00 49.93 C
ANISOU 281 CG PRO A 40 6188 7456 5327 1919 1620 1730 C
ATOM 282 CD PRO A 40 12.740 131.671 216.867 1.00 48.57 C
ANISOU 282 CD PRO A 40 6232 7152 5071 1764 1693 1477 C
ATOM 283 N LEU A 41 10.677 130.784 219.288 1.00 49.43 N
ANISOU 283 N LEU A 41 6179 7269 5334 2035 1978 1375 N
ATOM 284 CA LEU A 41 10.039 129.789 220.136 1.00 48.80 C
ANISOU 284 CA LEU A 41 5964 7319 5257 2043 2009 1305 C
ATOM 285 C LEU A 41 10.461 129.874 221.608 1.00 48.62 C
ANISOU 285 C LEU A 41 6174 7125 5174 1991 2172 1092 C
ATOM 286 O LEU A 41 10.250 128.944 222.374 1.00 47.70 O
ANISOU 286 O LEU A 41 5993 7116 5015 1934 2175 999 O
ATOM 287 CB LEU A 41 10.326 128.398 219.585 1.00 46.55 C
ANISOU 287 CB LEU A 41 5498 7310 4878 1860 1779 1273 C
ATOM 288 CG LEU A 41 9.857 128.070 218.181 1.00 46.69 C
ANISOU 288 CG LEU A 41 5280 7540 4920 1874 1597 1462 C
ATOM 289 CD1 LEU A 41 10.235 126.644 217.870 1.00 44.54 C
ANISOU 289 CD1 LEU A 41 4889 7497 4538 1675 1403 1374 C
ATOM 290 CD2 LEU A 41 8.375 128.203 218.101 1.00 48.70 C
ANISOU 290 CD2 LEU A 41 5309 7871 5323 2087 1661 1658 C
ATOM 291 N PHE A 42 11.056 130.999 221.991 1.00 49.68 N
ANISOU 291 N PHE A 42 6591 6990 5295 1998 2301 1019 N
ATOM 292 CA PHE A 42 11.513 131.197 223.367 1.00 49.84 C
ANISOU 292 CA PHE A 42 6870 6833 5235 1929 2450 811 C
ATOM 293 C PHE A 42 10.409 130.944 224.380 1.00 51.00 C
ANISOU 293 C PHE A 42 6955 6986 5438 2084 2636 800 C
ATOM 294 O PHE A 42 10.615 130.203 225.339 1.00 50.02 O
ANISOU 294 O PHE A 42 6876 6915 5213 1969 2646 652 O
ATOM 295 CB PHE A 42 12.071 132.595 223.568 1.00 51.52 C
ANISOU 295 CB PHE A 42 7397 6731 5448 1944 2587 762 C
ATOM 296 CG PHE A 42 12.807 132.758 224.848 1.00 51.54 C
ANISOU 296 CG PHE A 42 7690 6569 5323 1799 2684 531 C
ATOM 297 CD1 PHE A 42 14.155 132.450 224.928 1.00 49.83 C
ANISOU 297 CD1 PHE A 42 7591 6382 4961 1526 2529 392 C
ATOM 298 CD2 PHE A 42 12.159 133.231 225.980 1.00 53.49 C
ANISOU 298 CD2 PHE A 42 8094 6639 5590 1933 2933 456 C
ATOM 299 CE1 PHE A 42 14.853 132.609 226.102 1.00 50.05 C
ANISOU 299 CE1 PHE A 42 7882 6274 4861 1375 2594 191 C
ATOM 300 CE2 PHE A 42 12.851 133.386 227.165 1.00 53.70 C
ANISOU 300 CE2 PHE A 42 8410 6520 5473 1778 3012 239 C
ATOM 301 CZ PHE A 42 14.211 133.062 227.210 1.00 51.94 C
ANISOU 301 CZ PHE A 42 8293 6340 5100 1489 2826 112 C
ATOM 302 N TRP A 43 9.243 131.559 224.150 1.00 53.26 N
ANISOU 302 N TRP A 43 7128 7223 5887 2349 2783 969 N
ATOM 303 CA TRP A 43 8.037 131.345 224.962 1.00 54.76 C
ANISOU 303 CA TRP A 43 7199 7446 6159 2531 2975 1001 C
ATOM 304 C TRP A 43 7.839 129.912 225.499 1.00 53.01 C
ANISOU 304 C TRP A 43 6809 7472 5861 2401 2889 932 C
ATOM 305 O TRP A 43 7.471 129.745 226.653 1.00 53.75 O
ANISOU 305 O TRP A 43 6976 7524 5923 2431 3064 834 O
ATOM 306 CB TRP A 43 6.770 131.901 224.265 1.00 57.13 C
ANISOU 306 CB TRP A 43 7269 7770 6668 2824 3060 1256 C
ATOM 307 CG TRP A 43 6.297 131.138 223.092 1.00 56.23 C
ANISOU 307 CG TRP A 43 6805 7950 6610 2812 2828 1449 C
ATOM 308 CD1 TRP A 43 6.731 131.268 221.797 1.00 55.52 C
ANISOU 308 CD1 TRP A 43 6653 7928 6515 2749 2618 1564 C
ATOM 309 CD2 TRP A 43 5.299 130.109 223.076 1.00 56.12 C
ANISOU 309 CD2 TRP A 43 6461 8211 6653 2844 2775 1549 C
ATOM 310 NE1 TRP A 43 6.066 130.378 220.976 1.00 55.00 N
ANISOU 310 NE1 TRP A 43 6250 8160 6486 2737 2433 1721 N
ATOM 311 CE2 TRP A 43 5.190 129.649 221.735 1.00 55.34 C
ANISOU 311 CE2 TRP A 43 6121 8333 6572 2787 2518 1715 C
ATOM 312 CE3 TRP A 43 4.482 129.527 224.059 1.00 56.78 C
ANISOU 312 CE3 TRP A 43 6431 8377 6764 2901 2921 1518 C
ATOM 313 CZ2 TRP A 43 4.300 128.642 221.359 1.00 55.23 C
ANISOU 313 CZ2 TRP A 43 5769 8611 6605 2776 2394 1843 C
ATOM 314 CZ3 TRP A 43 3.595 128.521 223.683 1.00 56.62 C
ANISOU 314 CZ3 TRP A 43 6059 8652 6803 2893 2802 1656 C
ATOM 315 CH2 TRP A 43 3.511 128.091 222.347 1.00 55.87 C
ANISOU 315 CH2 TRP A 43 5737 8765 6727 2825 2536 1813 C
ATOM 316 N LEU A 44 8.116 128.883 224.697 1.00 50.84 N
ANISOU 316 N LEU A 44 6335 7439 5544 2247 2629 976 N
ATOM 317 CA LEU A 44 7.956 127.480 225.162 1.00 49.28 C
ANISOU 317 CA LEU A 44 5990 7457 5277 2113 2537 916 C
ATOM 318 C LEU A 44 8.572 127.191 226.536 1.00 48.66 C
ANISOU 318 C LEU A 44 6150 7285 5055 1980 2627 698 C
ATOM 319 O LEU A 44 8.206 126.220 227.216 1.00 48.16 O
ANISOU 319 O LEU A 44 5999 7351 4950 1921 2632 660 O
ATOM 320 CB LEU A 44 8.442 126.472 224.112 1.00 47.03 C
ANISOU 320 CB LEU A 44 5537 7393 4941 1938 2244 950 C
ATOM 321 CG LEU A 44 7.570 126.473 222.847 1.00 47.85 C
ANISOU 321 CG LEU A 44 5356 7656 5168 2053 2142 1179 C
ATOM 322 CD1 LEU A 44 8.163 125.626 221.733 1.00 45.89 C
ANISOU 322 CD1 LEU A 44 4999 7594 4844 1873 1865 1193 C
ATOM 323 CD2 LEU A 44 6.174 125.994 223.171 1.00 49.23 C
ANISOU 323 CD2 LEU A 44 5274 7977 5453 2180 2226 1301 C
ATOM 324 N ARG A 45 9.502 128.043 226.935 1.00 48.89 N
ANISOU 324 N ARG A 45 6484 7089 5002 1920 2690 565 N
ATOM 325 CA ARG A 45 10.017 127.990 228.278 1.00 48.92 C
ANISOU 325 CA ARG A 45 6741 6981 4865 1809 2795 370 C
ATOM 326 C ARG A 45 9.052 128.631 229.291 1.00 51.55 C
ANISOU 326 C ARG A 45 7172 7171 5243 2001 3106 355 C
ATOM 327 O ARG A 45 8.721 129.804 229.191 1.00 53.64 O
ANISOU 327 O ARG A 45 7546 7237 5597 2178 3281 396 O
ATOM 328 CB ARG A 45 11.400 128.641 228.368 1.00 48.41 C
ANISOU 328 CB ARG A 45 6969 6741 4682 1642 2734 228 C
ATOM 329 CG ARG A 45 11.889 128.759 229.811 1.00 48.99 C
ANISOU 329 CG ARG A 45 7336 6680 4599 1527 2853 30 C
ATOM 330 CD ARG A 45 13.323 129.097 229.872 1.00 48.19 C
ANISOU 330 CD ARG A 45 7464 6478 4370 1308 2729 -101 C
ATOM 331 NE ARG A 45 13.721 129.608 231.165 1.00 49.55 N
ANISOU 331 NE ARG A 45 7962 6465 4399 1219 2869 -278 N
ATOM 332 CZ ARG A 45 14.746 130.429 231.340 1.00 50.11 C
ANISOU 332 CZ ARG A 45 8304 6355 4380 1073 2851 -389 C
ATOM 333 NH1 ARG A 45 15.473 130.839 230.318 1.00 49.41 N
ANISOU 333 NH1 ARG A 45 8190 6245 4337 1007 2712 -337 N
ATOM 334 NH2 ARG A 45 15.043 130.854 232.548 1.00 51.57 N
ANISOU 334 NH2 ARG A 45 8793 6381 4418 979 2975 -554 N
ATOM 335 N ASP A 46 8.596 127.837 230.249 1.00 51.58 N
ANISOU 335 N ASP A 46 7137 7275 5186 1971 3181 302 N
ATOM 336 CA ASP A 46 8.001 128.360 231.481 1.00 53.95 C
ANISOU 336 CA ASP A 46 7614 7428 5457 2088 3485 221 C
ATOM 337 C ASP A 46 8.676 127.713 232.672 1.00 53.12 C
ANISOU 337 C ASP A 46 7712 7333 5139 1870 3467 36 C
ATOM 338 O ASP A 46 8.625 126.491 232.867 1.00 51.64 O
ANISOU 338 O ASP A 46 7371 7352 4898 1750 3338 48 O
ATOM 339 CB ASP A 46 6.479 128.161 231.574 1.00 55.73 C
ANISOU 339 CB ASP A 46 7571 7769 5835 2318 3667 374 C
ATOM 340 CG ASP A 46 5.953 128.419 232.976 1.00 57.96 C
ANISOU 340 CG ASP A 46 8033 7943 6047 2396 3976 266 C
ATOM 341 OD1 ASP A 46 6.465 129.345 233.637 1.00 59.25 O
ANISOU 341 OD1 ASP A 46 8546 7852 6115 2393 4131 112 O
ATOM 342 OD2 ASP A 46 5.040 127.696 233.439 1.00 58.58 O
ANISOU 342 OD2 ASP A 46 7916 8188 6154 2448 4070 329 O
ATOM 343 N ASP A 47 9.303 128.552 233.472 1.00 54.30 N
ANISOU 343 N ASP A 47 8218 7251 5162 1814 3593 -130 N
ATOM 344 CA ASP A 47 10.019 128.044 234.617 1.00 53.79 C
ANISOU 344 CA ASP A 47 8374 7190 4876 1594 3562 -303 C
ATOM 345 C ASP A 47 9.090 127.392 235.624 1.00 54.87 C
ANISOU 345 C ASP A 47 8454 7428 4966 1647 3738 -305 C
ATOM 346 O ASP A 47 9.445 126.417 236.267 1.00 53.74 O
ANISOU 346 O ASP A 47 8327 7413 4681 1467 3630 -363 O
ATOM 347 CB ASP A 47 10.834 129.151 235.252 1.00 55.22 C
ANISOU 347 CB ASP A 47 8959 7098 4922 1510 3662 -479 C
ATOM 348 CG ASP A 47 12.123 129.401 234.506 1.00 53.59 C
ANISOU 348 CG ASP A 47 8823 6851 4686 1332 3414 -510 C
ATOM 349 OD1 ASP A 47 12.397 128.720 233.467 1.00 51.33 O
ANISOU 349 OD1 ASP A 47 8275 6747 4481 1288 3175 -398 O
ATOM 350 OD2 ASP A 47 12.866 130.281 234.989 1.00 56.91 O
ANISOU 350 OD2 ASP A 47 9572 7058 4994 1227 3467 -651 O
ATOM 351 N ASN A 48 7.879 127.911 235.716 1.00 57.17 N
ANISOU 351 N ASN A 48 8661 7671 5391 1902 4008 -223 N
ATOM 352 CA ASN A 48 6.910 127.333 236.610 1.00 58.47 C
ANISOU 352 CA ASN A 48 8742 7946 5529 1967 4201 -206 C
ATOM 353 C ASN A 48 6.175 126.099 236.093 1.00 57.15 C
ANISOU 353 C ASN A 48 8170 8071 5474 1973 4068 -31 C
ATOM 354 O ASN A 48 5.432 125.503 236.846 1.00 58.12 O
ANISOU 354 O ASN A 48 8214 8304 5565 1990 4206 -11 O
ATOM 355 CB ASN A 48 5.959 128.418 237.086 1.00 61.91 C
ANISOU 355 CB ASN A 48 9280 8199 6045 2235 4581 -210 C
ATOM 356 CG ASN A 48 6.650 129.411 237.992 1.00 63.58 C
ANISOU 356 CG ASN A 48 9956 8124 6077 2173 4744 -429 C
ATOM 357 OD1 ASN A 48 7.492 129.031 238.809 1.00 62.83 O
ANISOU 357 OD1 ASN A 48 10098 8026 5749 1928 4655 -586 O
ATOM 358 ND2 ASN A 48 6.304 130.690 237.857 1.00 66.04 N
ANISOU 358 ND2 ASN A 48 10410 8188 6494 2391 4978 -439 N
ATOM 359 N ARG A 49 6.422 125.682 234.847 1.00 55.05 N
ANISOU 359 N ARG A 49 7668 7929 5320 1935 3798 85 N
ATOM 360 CA ARG A 49 5.721 124.545 234.203 1.00 53.94 C
ANISOU 360 CA ARG A 49 7147 8057 5293 1928 3651 253 C
ATOM 361 C ARG A 49 4.191 124.614 234.309 1.00 56.33 C
ANISOU 361 C ARG A 49 7196 8450 5755 2155 3886 406 C
ATOM 362 O ARG A 49 3.535 123.594 234.535 1.00 56.23 O
ANISOU 362 O ARG A 49 6969 8639 5757 2104 3869 484 O
ATOM 363 CB ARG A 49 6.200 123.190 234.735 1.00 52.11 C
ANISOU 363 CB ARG A 49 6914 7974 4910 1683 3476 194 C
ATOM 364 CG ARG A 49 7.605 123.134 235.303 1.00 50.76 C
ANISOU 364 CG ARG A 49 7058 7699 4532 1466 3347 12 C
ATOM 365 CD ARG A 49 8.671 122.507 234.450 1.00 48.03 C
ANISOU 365 CD ARG A 49 6656 7428 4167 1294 3015 7 C
ATOM 366 NE ARG A 49 9.870 123.212 234.858 1.00 47.88 N
ANISOU 366 NE ARG A 49 6954 7232 4004 1184 2987 -151 N
ATOM 367 CZ ARG A 49 11.117 123.000 234.430 1.00 50.22 C
ANISOU 367 CZ ARG A 49 7315 7530 4236 1018 2745 -210 C
ATOM 368 NH1 ARG A 49 11.447 122.044 233.550 1.00 48.44 N
ANISOU 368 NH1 ARG A 49 6877 7463 4064 939 2498 -139 N
ATOM 369 NH2 ARG A 49 12.071 123.785 234.895 1.00 52.77 N
ANISOU 369 NH2 ARG A 49 7925 7689 4436 925 2755 -345 N
ATOM 370 N ALA A 50 3.623 125.807 234.133 1.00 58.62 N
ANISOU 370 N ALA A 50 7504 8594 6177 2406 4107 458 N
ATOM 371 CA ALA A 50 2.186 126.002 234.350 1.00 61.39 C
ANISOU 371 CA ALA A 50 7625 9014 6687 2651 4373 600 C
ATOM 372 C ALA A 50 1.449 126.796 233.268 1.00 62.86 C
ANISOU 372 C ALA A 50 7575 9191 7118 2912 4408 797 C
ATOM 373 O ALA A 50 0.230 126.914 233.319 1.00 65.24 O
ANISOU 373 O ALA A 50 7627 9582 7580 3125 4601 948 O
ATOM 374 CB ALA A 50 1.931 126.633 235.746 1.00 64.01 C
ANISOU 374 CB ALA A 50 8238 9168 6915 2746 4740 456 C
ATOM 375 N ASP A 51 2.170 127.340 232.300 1.00 61.66 N
ANISOU 375 N ASP A 51 7491 8940 6997 2898 4225 809 N
ATOM 376 CA ASP A 51 1.538 128.149 231.268 1.00 63.19 C
ANISOU 376 CA ASP A 51 7489 9111 7410 3142 4246 1006 C
ATOM 377 C ASP A 51 0.509 127.335 230.474 1.00 63.28 C
ANISOU 377 C ASP A 51 7031 9432 7579 3187 4112 1246 C
ATOM 378 O ASP A 51 0.811 126.229 230.019 1.00 60.88 O
ANISOU 378 O ASP A 51 6588 9332 7211 2963 3835 1260 O
ATOM 379 CB ASP A 51 2.585 128.776 230.339 1.00 61.72 C
ANISOU 379 CB ASP A 51 7468 8781 7202 3076 4046 980 C
ATOM 380 CG ASP A 51 2.040 129.956 229.536 1.00 63.99 C
ANISOU 380 CG ASP A 51 7680 8943 7692 3358 4143 1152 C
ATOM 381 OD1 ASP A 51 1.415 130.863 230.131 1.00 66.98 O
ANISOU 381 OD1 ASP A 51 8152 9138 8158 3605 4460 1157 O
ATOM 382 OD2 ASP A 51 2.254 129.986 228.301 1.00 62.95 O
ANISOU 382 OD2 ASP A 51 7406 8886 7624 3336 3907 1285 O
ATOM 383 N PRO A 52 -0.724 127.874 230.338 1.00 66.29 N
ANISOU 383 N PRO A 52 7171 9849 8169 3476 4313 1436 N
ATOM 384 CA PRO A 52 -1.809 127.256 229.566 1.00 67.03 C
ANISOU 384 CA PRO A 52 6795 10239 8434 3539 4198 1691 C
ATOM 385 C PRO A 52 -1.492 127.101 228.068 1.00 65.38 C
ANISOU 385 C PRO A 52 6424 10146 8272 3457 3849 1828 C
ATOM 386 O PRO A 52 -1.655 126.012 227.523 1.00 63.93 O
ANISOU 386 O PRO A 52 5999 10220 8073 3277 3603 1904 O
ATOM 387 CB PRO A 52 -2.973 128.220 229.785 1.00 70.99 C
ANISOU 387 CB PRO A 52 7152 10675 9148 3905 4523 1845 C
ATOM 388 CG PRO A 52 -2.684 128.829 231.126 1.00 72.21 C
ANISOU 388 CG PRO A 52 7682 10565 9191 3971 4858 1623 C
ATOM 389 CD PRO A 52 -1.210 129.046 231.092 1.00 69.56 C
ANISOU 389 CD PRO A 52 7748 10025 8659 3758 4697 1406 C
ATOM 390 N GLU A 53 -1.033 128.167 227.420 1.00 65.74 N
ANISOU 390 N GLU A 53 6619 9997 8362 3575 3832 1853 N
ATOM 391 CA GLU A 53 -0.610 128.082 226.022 1.00 64.21 C
ANISOU 391 CA GLU A 53 6322 9895 8178 3483 3512 1965 C
ATOM 392 C GLU A 53 0.457 127.004 225.801 1.00 60.58 C
ANISOU 392 C GLU A 53 5962 9535 7519 3136 3225 1809 C
ATOM 393 O GLU A 53 0.409 126.268 224.815 1.00 59.36 O
ANISOU 393 O GLU A 53 5591 9598 7364 3006 2952 1914 O
ATOM 394 CB GLU A 53 -0.141 129.445 225.517 1.00 65.18 C
ANISOU 394 CB GLU A 53 6659 9753 8353 3643 3566 1989 C
ATOM 395 CG GLU A 53 -1.119 130.553 225.884 1.00 71.73 C
ANISOU 395 CG GLU A 53 7444 10430 9380 4007 3890 2115 C
ATOM 396 CD GLU A 53 -1.219 131.671 224.842 1.00 78.17 C
ANISOU 396 CD GLU A 53 8239 11120 10341 4216 3856 2308 C
ATOM 397 OE1 GLU A 53 -1.589 131.408 223.666 1.00 78.87 O
ANISOU 397 OE1 GLU A 53 8034 11424 10509 4214 3613 2532 O
ATOM 398 OE2 GLU A 53 -0.952 132.836 225.216 1.00 82.35 O
ANISOU 398 OE2 GLU A 53 9060 11326 10904 4384 4078 2241 O
ATOM 399 N VAL A 54 1.401 126.892 226.730 1.00 59.07 N
ANISOU 399 N VAL A 54 6099 9189 7157 2987 3289 1563 N
ATOM 400 CA VAL A 54 2.454 125.893 226.599 1.00 55.87 C
ANISOU 400 CA VAL A 54 5793 8863 6574 2681 3035 1417 C
ATOM 401 C VAL A 54 1.893 124.477 226.815 1.00 55.13 C
ANISOU 401 C VAL A 54 5458 9030 6459 2537 2936 1449 C
ATOM 402 O VAL A 54 2.027 123.607 225.948 1.00 53.57 O
ANISOU 402 O VAL A 54 5098 9018 6240 2378 2669 1503 O
ATOM 403 CB VAL A 54 3.671 126.181 227.534 1.00 54.67 C
ANISOU 403 CB VAL A 54 6049 8480 6242 2554 3110 1159 C
ATOM 404 CG1 VAL A 54 4.784 125.177 227.297 1.00 51.57 C
ANISOU 404 CG1 VAL A 54 5728 8177 5690 2263 2838 1035 C
ATOM 405 CG2 VAL A 54 4.196 127.555 227.298 1.00 55.60 C
ANISOU 405 CG2 VAL A 54 6405 8337 6383 2672 3202 1132 C
ATOM 406 N LEU A 55 1.252 124.260 227.959 1.00 56.46 N
ANISOU 406 N LEU A 55 5614 9206 6631 2588 3159 1415 N
ATOM 407 CA LEU A 55 0.687 122.952 228.291 1.00 56.06 C
ANISOU 407 CA LEU A 55 5356 9385 6561 2445 3094 1448 C
ATOM 408 C LEU A 55 -0.251 122.459 227.197 1.00 56.75 C
ANISOU 408 C LEU A 55 5044 9727 6793 2462 2923 1680 C
ATOM 409 O LEU A 55 -0.346 121.252 226.934 1.00 55.56 O
ANISOU 409 O LEU A 55 4741 9769 6600 2259 2726 1700 O
ATOM 410 CB LEU A 55 -0.042 123.008 229.639 1.00 58.11 C
ANISOU 410 CB LEU A 55 5637 9615 6826 2545 3409 1416 C
ATOM 411 CG LEU A 55 0.841 123.243 230.868 1.00 57.52 C
ANISOU 411 CG LEU A 55 5961 9327 6566 2470 3560 1175 C
ATOM 412 CD1 LEU A 55 0.040 123.080 232.135 1.00 59.58 C
ANISOU 412 CD1 LEU A 55 6215 9611 6812 2535 3850 1157 C
ATOM 413 CD2 LEU A 55 2.046 122.305 230.860 1.00 54.39 C
ANISOU 413 CD2 LEU A 55 5729 8949 5987 2175 3296 1026 C
ATOM 414 N ALA A 56 -0.935 123.416 226.571 1.00 58.89 N
ANISOU 414 N ALA A 56 5156 9989 7230 2702 2997 1858 N
ATOM 415 CA ALA A 56 -1.812 123.160 225.442 1.00 59.95 C
ANISOU 415 CA ALA A 56 4915 10360 7503 2738 2824 2102 C
ATOM 416 C ALA A 56 -1.006 122.625 224.291 1.00 57.52 C
ANISOU 416 C ALA A 56 4631 10127 7096 2526 2482 2079 C
ATOM 417 O ALA A 56 -1.397 121.638 223.669 1.00 57.13 O
ANISOU 417 O ALA A 56 4349 10310 7048 2369 2267 2168 O
ATOM 418 CB ALA A 56 -2.522 124.426 225.022 1.00 62.76 C
ANISOU 418 CB ALA A 56 5148 10652 8046 3053 2970 2292 C
ATOM 419 N HIS A 57 0.122 123.278 224.013 1.00 56.06 N
ANISOU 419 N HIS A 57 4735 9743 6822 2513 2440 1958 N
ATOM 420 CA HIS A 57 0.929 122.878 222.883 1.00 53.99 C
ANISOU 420 CA HIS A 57 4505 9543 6464 2333 2143 1936 C
ATOM 421 C HIS A 57 1.454 121.505 223.144 1.00 51.71 C
ANISOU 421 C HIS A 57 4261 9351 6035 2059 1989 1788 C
ATOM 422 O HIS A 57 1.603 120.716 222.228 1.00 50.63 O
ANISOU 422 O HIS A 57 4019 9369 5851 1894 1739 1818 O
ATOM 423 CB HIS A 57 2.084 123.822 222.592 1.00 52.97 C
ANISOU 423 CB HIS A 57 4675 9186 6264 2356 2141 1832 C
ATOM 424 CG HIS A 57 2.978 123.318 221.501 1.00 50.83 C
ANISOU 424 CG HIS A 57 4445 8991 5878 2156 1856 1793 C
ATOM 425 ND1 HIS A 57 2.597 123.298 220.172 1.00 51.43 N
ANISOU 425 ND1 HIS A 57 4316 9229 5995 2157 1661 1973 N
ATOM 426 CD2 HIS A 57 4.217 122.765 221.549 1.00 48.30 C
ANISOU 426 CD2 HIS A 57 4336 8619 5398 1947 1737 1597 C
ATOM 427 CE1 HIS A 57 3.575 122.775 219.448 1.00 49.34 C
ANISOU 427 CE1 HIS A 57 4155 9000 5593 1958 1451 1875 C
ATOM 428 NE2 HIS A 57 4.565 122.437 220.260 1.00 47.43 N
ANISOU 428 NE2 HIS A 57 4153 8631 5238 1836 1496 1650 N
ATOM 429 N LEU A 58 1.725 121.208 224.398 1.00 51.16 N
ANISOU 429 N LEU A 58 4359 9185 5895 2010 2141 1632 N
ATOM 430 CA LEU A 58 2.214 119.893 224.714 1.00 49.21 C
ANISOU 430 CA LEU A 58 4161 9014 5523 1762 2002 1504 C
ATOM 431 C LEU A 58 1.123 118.844 224.549 1.00 50.13 C
ANISOU 431 C LEU A 58 3969 9373 5707 1680 1920 1638 C
ATOM 432 O LEU A 58 1.409 117.711 224.214 1.00 48.73 O
ANISOU 432 O LEU A 58 3765 9298 5453 1466 1718 1591 O
ATOM 433 CB LEU A 58 2.835 119.853 226.108 1.00 48.52 C
ANISOU 433 CB LEU A 58 4346 8764 5326 1720 2169 1313 C
ATOM 434 CG LEU A 58 4.177 120.576 226.317 1.00 47.16 C
ANISOU 434 CG LEU A 58 4510 8367 5041 1702 2185 1140 C
ATOM 435 CD1 LEU A 58 4.733 120.269 227.698 1.00 46.57 C
ANISOU 435 CD1 LEU A 58 4674 8183 4836 1610 2300 963 C
ATOM 436 CD2 LEU A 58 5.238 120.259 225.227 1.00 45.02 C
ANISOU 436 CD2 LEU A 58 4294 8117 4694 1554 1918 1090 C
ATOM 437 N HIS A 59 -0.133 119.220 224.764 1.00 52.70 N
ANISOU 437 N HIS A 59 4055 9788 6181 1848 2079 1810 N
ATOM 438 CA HIS A 59 -1.233 118.304 224.477 1.00 53.94 C
ANISOU 438 CA HIS A 59 3879 10198 6417 1761 1984 1968 C
ATOM 439 C HIS A 59 -1.263 117.937 223.000 1.00 53.56 C
ANISOU 439 C HIS A 59 3668 10308 6372 1652 1683 2072 C
ATOM 440 O HIS A 59 -1.250 116.763 222.671 1.00 52.69 O
ANISOU 440 O HIS A 59 3492 10329 6198 1423 1487 2049 O
ATOM 441 CB HIS A 59 -2.568 118.892 224.885 1.00 57.08 C
ANISOU 441 CB HIS A 59 4018 10678 6992 1985 2213 2156 C
ATOM 442 CG HIS A 59 -3.611 117.858 225.141 1.00 60.47 C
ANISOU 442 CG HIS A 59 4158 11338 7480 1866 2194 2269 C
ATOM 443 ND1 HIS A 59 -4.941 118.043 224.818 1.00 66.79 N
ANISOU 443 ND1 HIS A 59 4577 12339 8460 1989 2237 2516 N
ATOM 444 CD2 HIS A 59 -3.523 116.622 225.688 1.00 60.92 C
ANISOU 444 CD2 HIS A 59 4245 11457 7443 1628 2134 2181 C
ATOM 445 CE1 HIS A 59 -5.633 116.973 225.177 1.00 68.30 C
ANISOU 445 CE1 HIS A 59 4573 12713 8664 1819 2210 2570 C
ATOM 446 NE2 HIS A 59 -4.797 116.097 225.710 1.00 65.97 N
ANISOU 446 NE2 HIS A 59 4533 12329 8203 1599 2150 2368 N
ATOM 447 N LEU A 60 -1.282 118.950 222.123 1.00 54.52 N
ANISOU 447 N LEU A 60 3750 10408 6559 1812 1651 2183 N
ATOM 448 CA LEU A 60 -1.196 118.770 220.662 1.00 54.52 C
ANISOU 448 CA LEU A 60 3640 10542 6533 1717 1368 2279 C
ATOM 449 C LEU A 60 -0.178 117.703 220.325 1.00 52.24 C
ANISOU 449 C LEU A 60 3530 10250 6069 1444 1155 2094 C
ATOM 450 O LEU A 60 -0.434 116.785 219.556 1.00 51.94 O
ANISOU 450 O LEU A 60 3354 10389 5992 1260 933 2139 O
ATOM 451 CB LEU A 60 -0.815 120.085 219.980 1.00 54.55 C
ANISOU 451 CB LEU A 60 3736 10423 6568 1906 1388 2342 C
ATOM 452 CG LEU A 60 -1.933 121.121 219.887 1.00 58.90 C
ANISOU 452 CG LEU A 60 4054 11012 7314 2187 1533 2585 C
ATOM 453 CD1 LEU A 60 -1.404 122.561 219.875 1.00 59.59 C
ANISOU 453 CD1 LEU A 60 4353 10852 7436 2414 1686 2577 C
ATOM 454 CD2 LEU A 60 -2.821 120.850 218.678 1.00 61.63 C
ANISOU 454 CD2 LEU A 60 4062 11629 7725 2150 1301 2830 C
ATOM 455 N GLU A 61 0.975 117.832 220.955 1.00 51.21 N
ANISOU 455 N GLU A 61 3711 9912 5834 1421 1235 1884 N
ATOM 456 CA GLU A 61 2.069 116.914 220.786 1.00 50.17 C
ANISOU 456 CA GLU A 61 3771 9743 5548 1201 1073 1698 C
ATOM 457 C GLU A 61 1.726 115.551 221.403 1.00 50.12 C
ANISOU 457 C GLU A 61 3703 9826 5513 1017 1034 1648 C
ATOM 458 O GLU A 61 2.048 114.517 220.838 1.00 49.15 O
ANISOU 458 O GLU A 61 3591 9776 5309 817 833 1588 O
ATOM 459 CB GLU A 61 3.326 117.524 221.410 1.00 48.65 C
ANISOU 459 CB GLU A 61 3900 9313 5271 1244 1186 1513 C
ATOM 460 CG GLU A 61 4.631 117.106 220.773 1.00 49.49 C
ANISOU 460 CG GLU A 61 4193 9372 5240 1090 1009 1364 C
ATOM 461 CD GLU A 61 5.054 117.942 219.535 1.00 53.77 C
ANISOU 461 CD GLU A 61 4755 9907 5768 1146 914 1425 C
ATOM 462 OE1 GLU A 61 5.427 119.141 219.693 1.00 57.22 O
ANISOU 462 OE1 GLU A 61 5319 10192 6229 1292 1043 1425 O
ATOM 463 OE2 GLU A 61 5.068 117.377 218.409 1.00 52.43 O
ANISOU 463 OE2 GLU A 61 4498 9876 5549 1029 709 1463 O
ATOM 464 N LYS A 62 1.045 115.541 222.544 1.00 51.92 N
ANISOU 464 N LYS A 62 3873 10047 5808 1084 1232 1676 N
ATOM 465 CA LYS A 62 0.676 114.273 223.138 1.00 52.36 C
ANISOU 465 CA LYS A 62 3869 10185 5839 904 1201 1649 C
ATOM 466 C LYS A 62 -0.340 113.566 222.269 1.00 54.56 C
ANISOU 466 C LYS A 62 3850 10700 6182 787 1026 1812 C
ATOM 467 O LYS A 62 -0.260 112.352 222.129 1.00 54.71 O
ANISOU 467 O LYS A 62 3873 10779 6137 563 871 1757 O
ATOM 468 CB LYS A 62 0.117 114.424 224.537 1.00 53.10 C
ANISOU 468 CB LYS A 62 3959 10238 5980 993 1464 1657 C
ATOM 469 CG LYS A 62 -0.005 113.068 225.223 1.00 53.55 C
ANISOU 469 CG LYS A 62 4023 10343 5980 781 1426 1603 C
ATOM 470 CD LYS A 62 -1.058 113.057 226.302 1.00 56.35 C
ANISOU 470 CD LYS A 62 4236 10762 6412 843 1657 1697 C
ATOM 471 CE LYS A 62 -2.367 112.625 225.735 1.00 59.60 C
ANISOU 471 CE LYS A 62 4282 11413 6949 793 1585 1903 C
ATOM 472 NZ LYS A 62 -3.384 113.679 225.953 1.00 64.31 N
ANISOU 472 NZ LYS A 62 4660 12077 7698 1041 1807 2069 N
ATOM 473 N ASP A 63 -1.298 114.323 221.715 1.00 57.10 N
ANISOU 473 N ASP A 63 3916 11148 6630 936 1048 2015 N
ATOM 474 CA ASP A 63 -2.295 113.812 220.765 1.00 58.91 C
ANISOU 474 CA ASP A 63 3837 11625 6922 829 858 2198 C
ATOM 475 C ASP A 63 -1.551 113.203 219.593 1.00 57.03 C
ANISOU 475 C ASP A 63 3708 11410 6552 636 577 2113 C
ATOM 476 O ASP A 63 -1.687 112.014 219.330 1.00 56.79 O
ANISOU 476 O ASP A 63 3642 11473 6463 397 411 2080 O
ATOM 477 CB ASP A 63 -3.231 114.936 220.254 1.00 61.72 C
ANISOU 477 CB ASP A 63 3929 12092 7430 1059 915 2437 C
ATOM 478 CG ASP A 63 -4.495 115.127 221.127 1.00 66.28 C
ANISOU 478 CG ASP A 63 4238 12773 8173 1192 1133 2599 C
ATOM 479 OD1 ASP A 63 -5.062 114.112 221.606 1.00 68.14 O
ANISOU 479 OD1 ASP A 63 4348 13125 8417 1020 1122 2614 O
ATOM 480 OD2 ASP A 63 -4.943 116.296 221.308 1.00 68.39 O
ANISOU 480 OD2 ASP A 63 4414 13004 8569 1470 1323 2720 O
ATOM 481 N TYR A 64 -0.734 114.016 218.923 1.00 55.57 N
ANISOU 481 N TYR A 64 3676 11127 6313 734 539 2068 N
ATOM 482 CA TYR A 64 -0.047 113.587 217.721 1.00 54.24 C
ANISOU 482 CA TYR A 64 3604 10991 6015 577 296 1999 C
ATOM 483 C TYR A 64 0.675 112.290 217.981 1.00 52.88 C
ANISOU 483 C TYR A 64 3616 10754 5722 350 208 1798 C
ATOM 484 O TYR A 64 0.624 111.353 217.191 1.00 52.62 O
ANISOU 484 O TYR A 64 3556 10823 5614 143 1 1777 O
ATOM 485 CB TYR A 64 0.964 114.634 217.257 1.00 52.56 C
ANISOU 485 CB TYR A 64 3591 10633 5747 713 323 1938 C
ATOM 486 CG TYR A 64 1.686 114.221 216.005 1.00 50.44 C
ANISOU 486 CG TYR A 64 3424 10407 5336 558 95 1868 C
ATOM 487 CD1 TYR A 64 0.985 113.899 214.855 1.00 51.64 C
ANISOU 487 CD1 TYR A 64 3385 10769 5465 449 -115 2007 C
ATOM 488 CD2 TYR A 64 3.069 114.134 215.969 1.00 50.13 C
ANISOU 488 CD2 TYR A 64 3666 10207 5175 512 90 1663 C
ATOM 489 CE1 TYR A 64 1.629 113.506 213.681 1.00 51.73 C
ANISOU 489 CE1 TYR A 64 3508 10824 5324 298 -314 1934 C
ATOM 490 CE2 TYR A 64 3.755 113.739 214.786 1.00 49.98 C
ANISOU 490 CE2 TYR A 64 3743 10232 5017 374 -99 1592 C
ATOM 491 CZ TYR A 64 3.009 113.431 213.635 1.00 51.46 C
ANISOU 491 CZ TYR A 64 3757 10624 5170 268 -296 1725 C
ATOM 492 OH TYR A 64 3.637 113.040 212.456 1.00 50.08 O
ANISOU 492 OH TYR A 64 3689 10498 4840 127 -471 1650 O
ATOM 493 N TYR A 65 1.355 112.256 219.110 1.00 52.21 N
ANISOU 493 N TYR A 65 3731 10491 5618 391 369 1651 N
ATOM 494 CA TYR A 65 2.135 111.113 219.486 1.00 51.28 C
ANISOU 494 CA TYR A 65 3805 10282 5398 212 308 1466 C
ATOM 495 C TYR A 65 1.275 109.853 219.622 1.00 53.14 C
ANISOU 495 C TYR A 65 3895 10641 5653 11 218 1515 C
ATOM 496 O TYR A 65 1.570 108.811 219.038 1.00 52.59 O
ANISOU 496 O TYR A 65 3891 10589 5500 -189 39 1433 O
ATOM 497 CB TYR A 65 2.895 111.396 220.780 1.00 49.60 C
ANISOU 497 CB TYR A 65 3805 9873 5166 303 501 1335 C
ATOM 498 CG TYR A 65 3.341 110.131 221.411 1.00 48.46 C
ANISOU 498 CG TYR A 65 3795 9665 4955 129 459 1204 C
ATOM 499 CD1 TYR A 65 4.360 109.379 220.841 1.00 45.64 C
ANISOU 499 CD1 TYR A 65 3606 9243 4492 0 302 1059 C
ATOM 500 CD2 TYR A 65 2.697 109.645 222.561 1.00 49.49 C
ANISOU 500 CD2 TYR A 65 3875 9801 5129 95 580 1238 C
ATOM 501 CE1 TYR A 65 4.733 108.179 221.410 1.00 47.81 C
ANISOU 501 CE1 TYR A 65 4000 9446 4719 -147 262 954 C
ATOM 502 CE2 TYR A 65 3.068 108.462 223.150 1.00 47.92 C
ANISOU 502 CE2 TYR A 65 3802 9536 4870 -66 537 1138 C
ATOM 503 CZ TYR A 65 4.081 107.720 222.572 1.00 49.21 C
ANISOU 503 CZ TYR A 65 4134 9622 4941 -183 372 1000 C
ATOM 504 OH TYR A 65 4.465 106.526 223.163 1.00 51.66 O
ANISOU 504 OH TYR A 65 4578 9849 5204 -328 330 910 O
ATOM 505 N GLU A 66 0.215 109.950 220.404 1.00 56.00 N
ANISOU 505 N GLU A 66 4068 11083 6127 61 353 1646 N
ATOM 506 CA GLU A 66 -0.639 108.801 220.627 1.00 58.69 C
ANISOU 506 CA GLU A 66 4262 11543 6496 -139 286 1706 C
ATOM 507 C GLU A 66 -1.223 108.356 219.318 1.00 60.23 C
ANISOU 507 C GLU A 66 4282 11924 6680 -296 44 1803 C
ATOM 508 O GLU A 66 -1.110 107.192 218.979 1.00 60.18 O
ANISOU 508 O GLU A 66 4339 11928 6601 -531 -118 1727 O
ATOM 509 CB GLU A 66 -1.712 109.086 221.678 1.00 60.75 C
ANISOU 509 CB GLU A 66 4323 11877 6883 -44 496 1847 C
ATOM 510 CG GLU A 66 -1.423 108.380 223.005 1.00 62.41 C
ANISOU 510 CG GLU A 66 4696 11962 7053 -117 629 1739 C
ATOM 511 CD GLU A 66 -1.685 109.254 224.237 1.00 67.65 C
ANISOU 511 CD GLU A 66 5360 12567 7778 94 925 1771 C
ATOM 512 OE1 GLU A 66 -2.872 109.500 224.608 1.00 70.57 O
ANISOU 512 OE1 GLU A 66 5470 13078 8267 159 1059 1940 O
ATOM 513 OE2 GLU A 66 -0.677 109.670 224.861 1.00 68.50 O
ANISOU 513 OE2 GLU A 66 5735 12484 7808 187 1029 1622 O
ATOM 514 N LYS A 67 -1.778 109.305 218.567 1.00 62.50 N
ANISOU 514 N LYS A 67 4374 12342 7030 -166 16 1964 N
ATOM 515 CA LYS A 67 -2.363 109.073 217.226 1.00 64.95 C
ANISOU 515 CA LYS A 67 4505 12856 7319 -301 -229 2084 C
ATOM 516 C LYS A 67 -1.442 108.285 216.290 1.00 63.81 C
ANISOU 516 C LYS A 67 4589 12653 7003 -499 -440 1909 C
ATOM 517 O LYS A 67 -1.899 107.521 215.440 1.00 65.03 O
ANISOU 517 O LYS A 67 4659 12949 7102 -719 -653 1945 O
ATOM 518 CB LYS A 67 -2.783 110.422 216.599 1.00 66.35 C
ANISOU 518 CB LYS A 67 4506 13130 7572 -76 -209 2268 C
ATOM 519 CG LYS A 67 -3.230 110.414 215.119 1.00 69.24 C
ANISOU 519 CG LYS A 67 4718 13702 7890 -186 -471 2401 C
ATOM 520 CD LYS A 67 -3.367 111.857 214.533 1.00 71.69 C
ANISOU 520 CD LYS A 67 4925 14052 8262 70 -437 2567 C
ATOM 521 CE LYS A 67 -4.697 112.530 214.934 1.00 74.88 C
ANISOU 521 CE LYS A 67 4969 14610 8871 249 -322 2835 C
ATOM 522 NZ LYS A 67 -4.727 114.005 214.699 1.00 75.03 N
ANISOU 522 NZ LYS A 67 4939 14590 8979 554 -214 2976 N
ATOM 523 N ARG A 68 -0.143 108.456 216.489 1.00 62.23 N
ANISOU 523 N ARG A 68 4681 12245 6718 -424 -372 1717 N
ATOM 524 CA ARG A 68 0.878 107.921 215.590 1.00 61.55 C
ANISOU 524 CA ARG A 68 4822 12088 6476 -551 -529 1546 C
ATOM 525 C ARG A 68 1.583 106.673 216.156 1.00 60.24 C
ANISOU 525 C ARG A 68 4878 11765 6243 -707 -536 1346 C
ATOM 526 O ARG A 68 2.289 105.962 215.442 1.00 59.00 O
ANISOU 526 O ARG A 68 4895 11556 5967 -842 -667 1202 O
ATOM 527 CB ARG A 68 1.877 109.035 215.277 1.00 60.05 C
ANISOU 527 CB ARG A 68 4782 11792 6244 -356 -458 1490 C
ATOM 528 CG ARG A 68 2.650 108.832 214.023 1.00 60.64 C
ANISOU 528 CG ARG A 68 5001 11873 6168 -452 -623 1391 C
ATOM 529 CD ARG A 68 1.837 109.086 212.782 1.00 64.84 C
ANISOU 529 CD ARG A 68 5345 12622 6669 -516 -799 1558 C
ATOM 530 NE ARG A 68 2.723 108.937 211.631 1.00 67.69 N
ANISOU 530 NE ARG A 68 5888 12970 6860 -600 -928 1439 N
ATOM 531 CZ ARG A 68 2.527 109.497 210.436 1.00 71.50 C
ANISOU 531 CZ ARG A 68 6306 13594 7268 -604 -1056 1549 C
ATOM 532 NH1 ARG A 68 1.443 110.250 210.220 1.00 74.45 N
ANISOU 532 NH1 ARG A 68 6418 14135 7736 -520 -1088 1796 N
ATOM 533 NH2 ARG A 68 3.416 109.311 209.453 1.00 70.55 N
ANISOU 533 NH2 ARG A 68 6378 13451 6976 -686 -1147 1420 N
ATOM 534 N ALA A 69 1.345 106.424 217.445 1.00 60.70 N
ANISOU 534 N ALA A 69 4928 11753 6382 -681 -386 1348 N
ATOM 535 CA ALA A 69 1.847 105.269 218.188 1.00 60.16 C
ANISOU 535 CA ALA A 69 5043 11538 6276 -813 -374 1203 C
ATOM 536 C ALA A 69 0.874 104.059 218.287 1.00 62.50 C
ANISOU 536 C ALA A 69 5224 11923 6599 -1057 -471 1263 C
ATOM 537 O ALA A 69 1.123 103.112 219.054 1.00 62.39 O
ANISOU 537 O ALA A 69 5345 11786 6576 -1163 -442 1177 O
ATOM 538 CB ALA A 69 2.207 105.730 219.576 1.00 59.13 C
ANISOU 538 CB ALA A 69 4996 11275 6196 -652 -153 1174 C
ATOM 539 N VAL A 70 -0.233 104.095 217.544 1.00 64.91 N
ANISOU 539 N VAL A 70 5280 12442 6940 -1154 -590 1423 N
ATOM 540 CA VAL A 70 -1.266 103.058 217.653 1.00 67.18 C
ANISOU 540 CA VAL A 70 5421 12839 7265 -1399 -680 1508 C
ATOM 541 C VAL A 70 -0.705 101.707 217.206 1.00 67.12 C
ANISOU 541 C VAL A 70 5648 12711 7144 -1645 -840 1333 C
ATOM 542 O VAL A 70 -0.810 100.702 217.914 1.00 67.39 O
ANISOU 542 O VAL A 70 5759 12653 7193 -1793 -822 1292 O
ATOM 543 CB VAL A 70 -2.537 103.400 216.801 1.00 69.94 C
ANISOU 543 CB VAL A 70 5438 13469 7669 -1469 -810 1725 C
ATOM 544 CG1 VAL A 70 -3.637 102.323 216.964 1.00 72.47 C
ANISOU 544 CG1 VAL A 70 5587 13914 8034 -1749 -905 1823 C
ATOM 545 CG2 VAL A 70 -3.078 104.777 217.150 1.00 69.79 C
ANISOU 545 CG2 VAL A 70 5187 13556 7775 -1195 -648 1904 C
ATOM 546 N ASP A 71 -0.089 101.707 216.028 1.00 66.74 N
ANISOU 546 N ASP A 71 5726 12653 6978 -1681 -984 1231 N
ATOM 547 CA ASP A 71 0.314 100.474 215.360 1.00 66.81 C
ANISOU 547 CA ASP A 71 5942 12571 6871 -1919 -1147 1072 C
ATOM 548 C ASP A 71 1.687 99.934 215.811 1.00 63.93 C
ANISOU 548 C ASP A 71 5907 11933 6452 -1860 -1070 850 C
ATOM 549 O ASP A 71 2.272 99.077 215.161 1.00 63.88 O
ANISOU 549 O ASP A 71 6109 11818 6343 -1993 -1178 692 O
ATOM 550 CB ASP A 71 0.265 100.685 213.845 1.00 67.79 C
ANISOU 550 CB ASP A 71 6048 12830 6877 -2001 -1335 1069 C
ATOM 551 CG ASP A 71 0.989 101.939 213.430 1.00 67.14 C
ANISOU 551 CG ASP A 71 5992 12754 6764 -1748 -1267 1063 C
ATOM 552 OD1 ASP A 71 0.483 103.033 213.809 1.00 68.35 O
ANISOU 552 OD1 ASP A 71 5934 13013 7022 -1563 -1166 1233 O
ATOM 553 OD2 ASP A 71 2.061 101.824 212.766 1.00 64.13 O
ANISOU 553 OD2 ASP A 71 5845 12262 6259 -1733 -1301 891 O
ATOM 554 N ILE A 72 2.205 100.429 216.923 1.00 61.75 N
ANISOU 554 N ILE A 72 5677 11544 6241 -1659 -884 841 N
ATOM 555 CA ILE A 72 3.317 99.723 217.569 1.00 59.78 C
ANISOU 555 CA ILE A 72 5700 11051 5963 -1637 -824 669 C
ATOM 556 C ILE A 72 2.955 99.237 218.976 1.00 60.04 C
ANISOU 556 C ILE A 72 5723 11009 6080 -1665 -709 726 C
ATOM 557 O ILE A 72 3.694 98.472 219.569 1.00 59.11 O
ANISOU 557 O ILE A 72 5815 10699 5946 -1683 -681 616 O
ATOM 558 CB ILE A 72 4.651 100.501 217.521 1.00 57.11 C
ANISOU 558 CB ILE A 72 5516 10603 5580 -1411 -740 553 C
ATOM 559 CG1 ILE A 72 4.475 101.956 217.967 1.00 55.54 C
ANISOU 559 CG1 ILE A 72 5165 10492 5443 -1190 -601 670 C
ATOM 560 CG2 ILE A 72 5.214 100.457 216.120 1.00 56.88 C
ANISOU 560 CG2 ILE A 72 5583 10592 5438 -1450 -867 445 C
ATOM 561 CD1 ILE A 72 5.774 102.726 218.089 1.00 51.09 C
ANISOU 561 CD1 ILE A 72 4756 9813 4844 -991 -511 564 C
ATOM 562 N LYS A 73 1.787 99.644 219.472 1.00 61.74 N
ANISOU 562 N LYS A 73 5689 11384 6384 -1673 -645 909 N
ATOM 563 CA LYS A 73 1.268 99.163 220.762 1.00 63.26 C
ANISOU 563 CA LYS A 73 5848 11541 6648 -1727 -531 985 C
ATOM 564 C LYS A 73 1.412 97.663 220.918 1.00 63.22 C
ANISOU 564 C LYS A 73 6022 11386 6613 -1956 -622 902 C
ATOM 565 O LYS A 73 1.621 97.169 222.024 1.00 63.16 O
ANISOU 565 O LYS A 73 6124 11249 6626 -1962 -526 895 O
ATOM 566 CB LYS A 73 -0.212 99.540 220.991 1.00 65.81 C
ANISOU 566 CB LYS A 73 5842 12092 7069 -1772 -485 1202 C
ATOM 567 CG LYS A 73 -0.478 101.051 221.205 1.00 69.34 C
ANISOU 567 CG LYS A 73 6107 12661 7580 -1509 -333 1312 C
ATOM 568 CD LYS A 73 -0.451 101.541 222.690 1.00 72.73 C
ANISOU 568 CD LYS A 73 6551 13025 8059 -1346 -86 1347 C
ATOM 569 CE LYS A 73 -0.367 103.089 222.704 1.00 74.39 C
ANISOU 569 CE LYS A 73 6672 13287 8306 -1064 53 1395 C
ATOM 570 NZ LYS A 73 -0.464 103.735 224.046 1.00 74.52 N
ANISOU 570 NZ LYS A 73 6692 13260 8363 -897 305 1432 N
ATOM 571 N ASP A 74 1.304 96.941 219.814 1.00 63.59 N
ANISOU 571 N ASP A 74 6116 11442 6604 -2148 -806 840 N
ATOM 572 CA ASP A 74 1.251 95.502 219.900 1.00 64.20 C
ANISOU 572 CA ASP A 74 6352 11376 6663 -2390 -897 777 C
ATOM 573 C ASP A 74 2.647 94.898 219.860 1.00 61.43 C
ANISOU 573 C ASP A 74 6331 10761 6247 -2327 -906 573 C
ATOM 574 O ASP A 74 2.934 93.942 220.571 1.00 61.44 O
ANISOU 574 O ASP A 74 6505 10577 6265 -2402 -885 532 O
ATOM 575 CB ASP A 74 0.259 94.919 218.872 1.00 67.43 C
ANISOU 575 CB ASP A 74 6644 11926 7049 -2672 -1086 825 C
ATOM 576 CG ASP A 74 -1.229 94.886 219.408 1.00 72.96 C
ANISOU 576 CG ASP A 74 7041 12830 7849 -2823 -1065 1049 C
ATOM 577 OD1 ASP A 74 -1.552 95.510 220.464 1.00 75.57 O
ANISOU 577 OD1 ASP A 74 7226 13222 8265 -2675 -887 1171 O
ATOM 578 OD2 ASP A 74 -2.088 94.207 218.781 1.00 77.47 O
ANISOU 578 OD2 ASP A 74 7520 13503 8411 -3103 -1224 1102 O
ATOM 579 N LEU A 75 3.541 95.491 219.085 1.00 58.77 N
ANISOU 579 N LEU A 75 6076 10409 5845 -2173 -925 459 N
ATOM 580 CA LEU A 75 4.937 95.074 219.148 1.00 56.07 C
ANISOU 580 CA LEU A 75 6011 9834 5460 -2065 -902 282 C
ATOM 581 C LEU A 75 5.644 95.492 220.448 1.00 53.94 C
ANISOU 581 C LEU A 75 5796 9464 5236 -1861 -744 297 C
ATOM 582 O LEU A 75 6.331 94.678 221.052 1.00 53.59 O
ANISOU 582 O LEU A 75 5947 9218 5198 -1860 -727 227 O
ATOM 583 CB LEU A 75 5.709 95.567 217.939 1.00 54.93 C
ANISOU 583 CB LEU A 75 5931 9712 5227 -1971 -957 158 C
ATOM 584 CG LEU A 75 7.217 95.304 217.945 1.00 52.54 C
ANISOU 584 CG LEU A 75 5874 9201 4889 -1823 -915 -15 C
ATOM 585 CD1 LEU A 75 7.554 93.814 217.937 1.00 52.07 C
ANISOU 585 CD1 LEU A 75 6048 8915 4821 -1963 -974 -133 C
ATOM 586 CD2 LEU A 75 7.849 96.009 216.759 1.00 50.38 C
ANISOU 586 CD2 LEU A 75 5614 9000 4528 -1725 -944 -105 C
ATOM 587 N ALA A 76 5.484 96.749 220.862 1.00 52.31 N
ANISOU 587 N ALA A 76 5428 9390 5056 -1691 -635 389 N
ATOM 588 CA ALA A 76 5.980 97.216 222.156 1.00 50.93 C
ANISOU 588 CA ALA A 76 5295 9145 4910 -1528 -485 416 C
ATOM 589 C ALA A 76 5.560 96.265 223.279 1.00 52.43 C
ANISOU 589 C ALA A 76 5539 9244 5138 -1653 -448 481 C
ATOM 590 O ALA A 76 6.281 96.071 224.253 1.00 51.61 O
ANISOU 590 O ALA A 76 5581 9002 5029 -1573 -378 456 O
ATOM 591 CB ALA A 76 5.469 98.587 222.435 1.00 50.04 C
ANISOU 591 CB ALA A 76 4984 9199 4828 -1384 -370 528 C
ATOM 592 N GLU A 77 4.375 95.672 223.124 1.00 54.82 N
ANISOU 592 N GLU A 77 5721 9634 5475 -1862 -502 577 N
ATOM 593 CA GLU A 77 3.867 94.646 224.033 1.00 55.79 C
ANISOU 593 CA GLU A 77 5893 9675 5631 -2029 -484 649 C
ATOM 594 C GLU A 77 4.693 93.343 223.963 1.00 55.48 C
ANISOU 594 C GLU A 77 6133 9380 5565 -2119 -576 524 C
ATOM 595 O GLU A 77 5.160 92.873 224.977 1.00 55.26 O
ANISOU 595 O GLU A 77 6248 9203 5544 -2090 -517 533 O
ATOM 596 CB GLU A 77 2.373 94.408 223.754 1.00 58.13 C
ANISOU 596 CB GLU A 77 5960 10152 5974 -2245 -529 790 C
ATOM 597 CG GLU A 77 1.623 93.496 224.733 1.00 61.25 C
ANISOU 597 CG GLU A 77 6350 10510 6412 -2437 -487 903 C
ATOM 598 CD GLU A 77 1.722 93.914 226.212 1.00 62.38 C
ANISOU 598 CD GLU A 77 6499 10635 6565 -2302 -295 983 C
ATOM 599 OE1 GLU A 77 2.069 95.091 226.506 1.00 62.26 O
ANISOU 599 OE1 GLU A 77 6427 10688 6539 -2070 -178 981 O
ATOM 600 OE2 GLU A 77 1.436 93.050 227.084 1.00 62.93 O
ANISOU 600 OE2 GLU A 77 6645 10619 6647 -2443 -260 1051 O
ATOM 601 N THR A 78 4.900 92.771 222.784 1.00 55.45 N
ANISOU 601 N THR A 78 6219 9320 5530 -2217 -713 409 N
ATOM 602 CA THR A 78 5.682 91.547 222.703 1.00 55.83 C
ANISOU 602 CA THR A 78 6541 9107 5564 -2280 -781 286 C
ATOM 603 C THR A 78 7.043 91.774 223.363 1.00 53.62 C
ANISOU 603 C THR A 78 6416 8678 5278 -2039 -702 216 C
ATOM 604 O THR A 78 7.673 90.842 223.875 1.00 53.46 O
ANISOU 604 O THR A 78 6601 8439 5274 -2044 -710 177 O
ATOM 605 CB THR A 78 5.871 91.093 221.229 1.00 56.85 C
ANISOU 605 CB THR A 78 6764 9199 5637 -2377 -917 139 C
ATOM 606 OG1 THR A 78 4.919 91.763 220.397 1.00 58.65 O
ANISOU 606 OG1 THR A 78 6766 9677 5841 -2465 -975 202 O
ATOM 607 CG2 THR A 78 5.674 89.561 221.071 1.00 59.73 C
ANISOU 607 CG2 THR A 78 7332 9356 6008 -2617 -1012 84 C
ATOM 608 N ILE A 79 7.469 93.038 223.365 1.00 51.89 N
ANISOU 608 N ILE A 79 6092 8585 5040 -1834 -629 214 N
ATOM 609 CA ILE A 79 8.822 93.442 223.747 1.00 49.85 C
ANISOU 609 CA ILE A 79 5950 8226 4765 -1609 -574 136 C
ATOM 610 C ILE A 79 8.942 93.756 225.247 1.00 49.10 C
ANISOU 610 C ILE A 79 5858 8116 4683 -1524 -464 238 C
ATOM 611 O ILE A 79 9.986 93.528 225.846 1.00 48.90 O
ANISOU 611 O ILE A 79 5980 7950 4651 -1414 -450 198 O
ATOM 612 CB ILE A 79 9.294 94.633 222.886 1.00 48.23 C
ANISOU 612 CB ILE A 79 5654 8150 4521 -1453 -562 70 C
ATOM 613 CG1 ILE A 79 10.637 94.342 222.258 1.00 48.02 C
ANISOU 613 CG1 ILE A 79 5793 7985 4468 -1344 -601 -87 C
ATOM 614 CG2 ILE A 79 9.415 95.889 223.672 1.00 47.92 C
ANISOU 614 CG2 ILE A 79 5509 8217 4483 -1291 -444 143 C
ATOM 615 CD1 ILE A 79 10.530 94.046 220.800 1.00 50.47 C
ANISOU 615 CD1 ILE A 79 6125 8318 4733 -1431 -693 -191 C
ATOM 616 N TYR A 80 7.877 94.276 225.845 1.00 49.30 N
ANISOU 616 N TYR A 80 5717 8292 4721 -1576 -383 372 N
ATOM 617 CA TYR A 80 7.792 94.441 227.296 1.00 49.27 C
ANISOU 617 CA TYR A 80 5730 8279 4710 -1540 -268 474 C
ATOM 618 C TYR A 80 7.984 93.088 227.987 1.00 50.25 C
ANISOU 618 C TYR A 80 6039 8208 4844 -1656 -311 498 C
ATOM 619 O TYR A 80 8.677 92.980 229.016 1.00 49.84 O
ANISOU 619 O TYR A 80 6115 8058 4766 -1577 -269 520 O
ATOM 620 CB TYR A 80 6.438 95.056 227.657 1.00 50.12 C
ANISOU 620 CB TYR A 80 5618 8585 4839 -1602 -167 613 C
ATOM 621 CG TYR A 80 6.156 95.267 229.128 1.00 51.60 C
ANISOU 621 CG TYR A 80 5811 8789 5005 -1582 -22 722 C
ATOM 622 CD1 TYR A 80 6.675 96.369 229.822 1.00 52.06 C
ANISOU 622 CD1 TYR A 80 5882 8884 5016 -1397 97 712 C
ATOM 623 CD2 TYR A 80 5.326 94.386 229.830 1.00 54.21 C
ANISOU 623 CD2 TYR A 80 6141 9104 5354 -1765 3 836 C
ATOM 624 CE1 TYR A 80 6.384 96.562 231.204 1.00 51.83 C
ANISOU 624 CE1 TYR A 80 5879 8872 4941 -1391 241 805 C
ATOM 625 CE2 TYR A 80 5.043 94.574 231.196 1.00 54.77 C
ANISOU 625 CE2 TYR A 80 6225 9199 5384 -1755 151 939 C
ATOM 626 CZ TYR A 80 5.568 95.660 231.859 1.00 52.58 C
ANISOU 626 CZ TYR A 80 5971 8960 5047 -1566 269 918 C
ATOM 627 OH TYR A 80 5.269 95.820 233.171 1.00 52.97 O
ANISOU 627 OH TYR A 80 6054 9035 5038 -1570 417 1009 O
ATOM 628 N GLN A 81 7.380 92.058 227.403 1.00 51.31 N
ANISOU 628 N GLN A 81 6198 8285 5014 -1853 -403 498 N
ATOM 629 CA GLN A 81 7.401 90.723 227.991 1.00 52.62 C
ANISOU 629 CA GLN A 81 6542 8252 5199 -1991 -444 535 C
ATOM 630 C GLN A 81 8.799 90.152 227.945 1.00 52.04 C
ANISOU 630 C GLN A 81 6696 7953 5125 -1863 -504 426 C
ATOM 631 O GLN A 81 9.258 89.559 228.930 1.00 52.64 O
ANISOU 631 O GLN A 81 6919 7881 5202 -1846 -492 482 O
ATOM 632 CB GLN A 81 6.403 89.789 227.291 1.00 54.55 C
ANISOU 632 CB GLN A 81 6765 8481 5480 -2252 -534 552 C
ATOM 633 CG GLN A 81 4.957 90.231 227.416 1.00 54.97 C
ANISOU 633 CG GLN A 81 6566 8769 5551 -2396 -479 691 C
ATOM 634 CD GLN A 81 4.545 90.432 228.868 1.00 56.48 C
ANISOU 634 CD GLN A 81 6712 9012 5736 -2391 -338 844 C
ATOM 635 OE1 GLN A 81 5.145 89.860 229.781 1.00 56.30 O
ANISOU 635 OE1 GLN A 81 6877 8820 5694 -2368 -316 865 O
ATOM 636 NE2 GLN A 81 3.522 91.250 229.088 1.00 56.70 N
ANISOU 636 NE2 GLN A 81 6491 9276 5776 -2406 -235 955 N
ATOM 637 N GLU A 82 9.463 90.337 226.795 1.00 51.24 N
ANISOU 637 N GLU A 82 6615 7832 5020 -1772 -565 279 N
ATOM 638 CA GLU A 82 10.882 89.979 226.630 1.00 50.18 C
ANISOU 638 CA GLU A 82 6658 7516 4894 -1608 -603 166 C
ATOM 639 C GLU A 82 11.636 90.659 227.748 1.00 47.88 C
ANISOU 639 C GLU A 82 6366 7249 4578 -1433 -533 225 C
ATOM 640 O GLU A 82 12.308 89.981 228.503 1.00 48.16 O
ANISOU 640 O GLU A 82 6551 7120 4629 -1389 -551 258 O
ATOM 641 CB GLU A 82 11.457 90.385 225.259 1.00 49.56 C
ANISOU 641 CB GLU A 82 6558 7473 4798 -1515 -642 8 C
ATOM 642 CG GLU A 82 11.088 89.478 224.071 1.00 52.89 C
ANISOU 642 CG GLU A 82 7067 7806 5225 -1674 -731 -95 C
ATOM 643 CD GLU A 82 11.653 90.003 222.737 1.00 55.61 C
ANISOU 643 CD GLU A 82 7389 8216 5524 -1579 -754 -247 C
ATOM 644 OE1 GLU A 82 12.903 90.174 222.637 1.00 57.18 O
ANISOU 644 OE1 GLU A 82 7659 8339 5726 -1379 -728 -333 O
ATOM 645 OE2 GLU A 82 10.856 90.244 221.795 1.00 54.22 O
ANISOU 645 OE2 GLU A 82 7118 8176 5307 -1707 -799 -271 O
ATOM 646 N HIS A 83 11.477 91.977 227.881 1.00 45.48 N
ANISOU 646 N HIS A 83 5901 7146 4233 -1346 -457 247 N
ATOM 647 CA HIS A 83 12.057 92.694 229.012 1.00 44.53 C
ANISOU 647 CA HIS A 83 5788 7062 4070 -1215 -387 305 C
ATOM 648 C HIS A 83 11.828 92.007 230.374 1.00 45.83 C
ANISOU 648 C HIS A 83 6055 7140 4219 -1295 -363 435 C
ATOM 649 O HIS A 83 12.778 91.629 231.064 1.00 45.28 O
ANISOU 649 O HIS A 83 6121 6945 4137 -1213 -395 452 O
ATOM 650 CB HIS A 83 11.580 94.143 229.053 1.00 42.96 C
ANISOU 650 CB HIS A 83 5413 7079 3831 -1155 -288 327 C
ATOM 651 CG HIS A 83 12.287 95.036 228.092 1.00 40.56 C
ANISOU 651 CG HIS A 83 5051 6842 3520 -1015 -301 215 C
ATOM 652 ND1 HIS A 83 13.438 94.661 227.436 1.00 40.65 N
ANISOU 652 ND1 HIS A 83 5156 6742 3548 -926 -377 103 N
ATOM 653 CD2 HIS A 83 12.025 96.299 227.691 1.00 39.42 C
ANISOU 653 CD2 HIS A 83 4764 6859 3356 -945 -239 204 C
ATOM 654 CE1 HIS A 83 13.853 95.652 226.668 1.00 38.26 C
ANISOU 654 CE1 HIS A 83 4770 6540 3227 -822 -361 29 C
ATOM 655 NE2 HIS A 83 13.008 96.655 226.796 1.00 37.63 N
ANISOU 655 NE2 HIS A 83 4553 6619 3125 -833 -284 90 N
ATOM 656 N ILE A 84 10.564 91.834 230.735 1.00 47.52 N
ANISOU 656 N ILE A 84 6196 7427 4432 -1459 -309 539 N
ATOM 657 CA ILE A 84 10.207 91.149 231.961 1.00 49.58 C
ANISOU 657 CA ILE A 84 6551 7618 4670 -1564 -276 674 C
ATOM 658 C ILE A 84 10.871 89.789 232.073 1.00 50.90 C
ANISOU 658 C ILE A 84 6928 7534 4877 -1597 -382 674 C
ATOM 659 O ILE A 84 11.467 89.491 233.098 1.00 51.46 O
ANISOU 659 O ILE A 84 7126 7514 4913 -1550 -385 748 O
ATOM 660 CB ILE A 84 8.689 90.998 232.073 1.00 51.44 C
ANISOU 660 CB ILE A 84 6658 7967 4920 -1763 -211 779 C
ATOM 661 CG1 ILE A 84 8.063 92.359 232.389 1.00 52.13 C
ANISOU 661 CG1 ILE A 84 6555 8289 4965 -1697 -70 819 C
ATOM 662 CG2 ILE A 84 8.303 89.933 233.121 1.00 52.19 C
ANISOU 662 CG2 ILE A 84 6880 7945 5005 -1920 -201 915 C
ATOM 663 CD1 ILE A 84 8.054 92.707 233.888 1.00 54.37 C
ANISOU 663 CD1 ILE A 84 6892 8605 5159 -1669 54 923 C
ATOM 664 N SER A 85 10.786 88.971 231.027 1.00 51.93 N
ANISOU 664 N SER A 85 7107 7548 5077 -1674 -469 593 N
ATOM 665 CA SER A 85 11.383 87.649 231.081 1.00 53.82 C
ANISOU 665 CA SER A 85 7561 7519 5367 -1695 -556 587 C
ATOM 666 C SER A 85 12.906 87.695 231.153 1.00 53.47 C
ANISOU 666 C SER A 85 7619 7365 5333 -1464 -599 522 C
ATOM 667 O SER A 85 13.546 86.679 231.353 1.00 54.60 O
ANISOU 667 O SER A 85 7936 7283 5525 -1433 -662 537 O
ATOM 668 CB SER A 85 10.934 86.806 229.906 1.00 54.74 C
ANISOU 668 CB SER A 85 7725 7528 5545 -1837 -628 496 C
ATOM 669 OG SER A 85 11.542 87.280 228.742 1.00 54.27 O
ANISOU 669 OG SER A 85 7624 7505 5492 -1710 -657 333 O
ATOM 670 N HIS A 86 13.482 88.884 231.016 1.00 53.00 N
ANISOU 670 N HIS A 86 7442 7463 5232 -1302 -564 462 N
ATOM 671 CA HIS A 86 14.936 89.047 231.114 1.00 53.39 C
ANISOU 671 CA HIS A 86 7550 7446 5290 -1090 -604 413 C
ATOM 672 C HIS A 86 15.368 89.693 232.415 1.00 54.07 C
ANISOU 672 C HIS A 86 7632 7616 5297 -1017 -574 519 C
ATOM 673 O HIS A 86 16.557 89.893 232.629 1.00 54.17 O
ANISOU 673 O HIS A 86 7673 7600 5308 -858 -616 501 O
ATOM 674 CB HIS A 86 15.494 89.886 229.949 1.00 51.42 C
ANISOU 674 CB HIS A 86 7191 7298 5047 -961 -600 259 C
ATOM 675 CG HIS A 86 15.495 89.180 228.625 1.00 50.93 C
ANISOU 675 CG HIS A 86 7180 7125 5048 -989 -645 129 C
ATOM 676 ND1 HIS A 86 15.407 89.855 227.426 1.00 48.36 N
ANISOU 676 ND1 HIS A 86 6747 6921 4706 -968 -631 6 N
ATOM 677 CD2 HIS A 86 15.566 87.864 228.315 1.00 51.57 C
ANISOU 677 CD2 HIS A 86 7424 6975 5194 -1043 -699 101 C
ATOM 678 CE1 HIS A 86 15.425 88.983 226.436 1.00 50.95 C
ANISOU 678 CE1 HIS A 86 7173 7111 5074 -1015 -675 -99 C
ATOM 679 NE2 HIS A 86 15.519 87.767 226.949 1.00 52.66 N
ANISOU 679 NE2 HIS A 86 7559 7104 5345 -1060 -713 -51 N
ATOM 680 N ILE A 87 14.424 90.013 233.290 1.00 49.26 N
ANISOU 680 N ILE A 87 6926 7396 4396 -960 -241 937 N
ATOM 681 CA ILE A 87 14.724 90.968 234.347 1.00 49.89 C
ANISOU 681 CA ILE A 87 6931 7536 4488 -876 -166 952 C
ATOM 682 C ILE A 87 14.885 90.340 235.728 1.00 50.95 C
ANISOU 682 C ILE A 87 7127 7628 4602 -872 -116 981 C
ATOM 683 O ILE A 87 15.639 90.827 236.554 1.00 50.64 O
ANISOU 683 O ILE A 87 7089 7607 4545 -779 -68 970 O
ATOM 684 CB ILE A 87 13.760 92.246 234.273 1.00 50.09 C
ANISOU 684 CB ILE A 87 6784 7675 4573 -889 -140 987 C
ATOM 685 CG1 ILE A 87 14.461 93.507 234.787 1.00 50.29 C
ANISOU 685 CG1 ILE A 87 6751 7756 4602 -772 -83 967 C
ATOM 686 CG2 ILE A 87 12.352 92.010 234.874 1.00 49.86 C
ANISOU 686 CG2 ILE A 87 6675 7683 4588 -996 -117 1057 C
ATOM 687 CD1 ILE A 87 15.662 93.938 233.910 1.00 52.37 C
ANISOU 687 CD1 ILE A 87 7056 8007 4834 -685 -112 905 C
ATOM 688 N GLU A 88 14.245 89.196 235.911 1.00 52.64 N
ANISOU 688 N GLU A 88 7406 7779 4814 -975 -135 1016 N
ATOM 689 CA GLU A 88 14.113 88.515 237.203 1.00 54.15 C
ANISOU 689 CA GLU A 88 7653 7932 4989 -1001 -89 1063 C
ATOM 690 C GLU A 88 13.397 89.282 238.303 1.00 54.00 C
ANISOU 690 C GLU A 88 7516 8004 4997 -1009 -10 1116 C
ATOM 691 O GLU A 88 13.994 89.999 239.071 1.00 53.65 O
ANISOU 691 O GLU A 88 7449 7999 4935 -914 42 1105 O
ATOM 692 CB GLU A 88 15.358 87.692 237.652 1.00 54.51 C
ANISOU 692 CB GLU A 88 7857 7879 4976 -922 -96 1036 C
ATOM 693 CG GLU A 88 16.631 88.384 238.172 1.00 56.09 C
ANISOU 693 CG GLU A 88 8061 8105 5144 -775 -64 997 C
ATOM 694 CD GLU A 88 17.656 87.388 238.847 1.00 60.97 C
ANISOU 694 CD GLU A 88 8831 8627 5706 -711 -70 992 C
ATOM 695 OE1 GLU A 88 17.239 86.277 239.291 1.00 63.76 O
ANISOU 695 OE1 GLU A 88 9279 8900 6048 -784 -76 1036 O
ATOM 696 OE2 GLU A 88 18.877 87.721 238.946 1.00 60.36 O
ANISOU 696 OE2 GLU A 88 8778 8558 5600 -589 -69 947 O
ATOM 697 N GLU A 89 12.081 89.109 238.339 1.00 55.17 N
ANISOU 697 N GLU A 89 7587 8189 5188 -1128 -2 1172 N
ATOM 698 CA GLU A 89 11.164 89.920 239.129 1.00 54.98 C
ANISOU 698 CA GLU A 89 7422 8269 5200 -1145 73 1222 C
ATOM 699 C GLU A 89 11.313 89.798 240.642 1.00 54.84 C
ANISOU 699 C GLU A 89 7437 8253 5147 -1119 155 1257 C
ATOM 700 O GLU A 89 11.325 90.810 241.330 1.00 54.96 O
ANISOU 700 O GLU A 89 7371 8345 5165 -1047 221 1255 O
ATOM 701 CB GLU A 89 9.722 89.632 238.706 1.00 56.16 C
ANISOU 701 CB GLU A 89 7476 8458 5404 -1287 54 1275 C
ATOM 702 CG GLU A 89 9.187 90.608 237.683 1.00 56.41 C
ANISOU 702 CG GLU A 89 7370 8575 5490 -1280 21 1262 C
ATOM 703 CD GLU A 89 8.054 90.034 236.846 1.00 60.32 C
ANISOU 703 CD GLU A 89 7812 9080 6025 -1425 -43 1297 C
ATOM 704 OE1 GLU A 89 8.336 89.077 236.093 1.00 61.35 O
ANISOU 704 OE1 GLU A 89 8060 9121 6130 -1483 -121 1271 O
ATOM 705 OE2 GLU A 89 6.888 90.535 236.924 1.00 61.92 O
ANISOU 705 OE2 GLU A 89 7858 9383 6286 -1479 -19 1348 O
ATOM 706 N THR A 90 11.396 88.587 241.175 1.00 54.71 N
ANISOU 706 N THR A 90 7544 8151 5094 -1177 150 1289 N
ATOM 707 CA THR A 90 11.690 88.461 242.582 1.00 54.30 C
ANISOU 707 CA THR A 90 7542 8097 4993 -1140 221 1320 C
ATOM 708 C THR A 90 13.186 88.322 242.677 1.00 53.36 C
ANISOU 708 C THR A 90 7547 7911 4818 -1019 192 1266 C
ATOM 709 O THR A 90 13.754 87.419 242.095 1.00 53.56 O
ANISOU 709 O THR A 90 7690 7836 4824 -1023 127 1244 O
ATOM 710 CB THR A 90 11.002 87.242 243.203 1.00 55.77 C
ANISOU 710 CB THR A 90 7799 8225 5164 -1266 236 1395 C
ATOM 711 OG1 THR A 90 9.591 87.328 242.995 1.00 57.81 O
ANISOU 711 OG1 THR A 90 7929 8552 5482 -1389 256 1446 O
ATOM 712 CG2 THR A 90 11.239 87.161 244.717 1.00 56.47 C
ANISOU 712 CG2 THR A 90 7937 8323 5194 -1230 315 1436 C
ATOM 713 N ASP A 91 13.841 89.218 243.403 1.00 52.97 N
ANISOU 713 N ASP A 91 7469 7917 4740 -910 238 1241 N
ATOM 714 CA ASP A 91 15.300 89.153 243.506 1.00 52.89 C
ANISOU 714 CA ASP A 91 7558 7858 4678 -792 208 1190 C
ATOM 715 C ASP A 91 15.867 89.674 244.836 1.00 52.35 C
ANISOU 715 C ASP A 91 7500 7834 4557 -710 267 1193 C
ATOM 716 O ASP A 91 15.204 90.433 245.554 1.00 51.77 O
ANISOU 716 O ASP A 91 7337 7844 4491 -720 338 1215 O
ATOM 717 CB ASP A 91 15.960 89.884 242.313 1.00 52.51 C
ANISOU 717 CB ASP A 91 7467 7828 4658 -722 159 1117 C
ATOM 718 CG ASP A 91 17.396 89.436 242.070 1.00 53.97 C
ANISOU 718 CG ASP A 91 7765 7944 4799 -626 110 1067 C
ATOM 719 OD1 ASP A 91 17.674 88.229 242.298 1.00 57.33 O
ANISOU 719 OD1 ASP A 91 8318 8275 5190 -642 83 1088 O
ATOM 720 OD2 ASP A 91 18.236 90.280 241.653 1.00 53.93 O
ANISOU 720 OD2 ASP A 91 7720 7976 4794 -535 99 1010 O
ATOM 721 N MET A 92 17.090 89.227 245.142 1.00 51.98 N
ANISOU 721 N MET A 92 7564 7729 4455 -626 234 1169 N
ATOM 722 CA MET A 92 17.924 89.799 246.195 1.00 51.85 C
ANISOU 722 CA MET A 92 7561 7756 4383 -530 265 1153 C
ATOM 723 C MET A 92 19.190 90.304 245.539 1.00 50.73 C
ANISOU 723 C MET A 92 7419 7615 4241 -423 215 1078 C
ATOM 724 O MET A 92 19.621 89.723 244.546 1.00 51.23 O
ANISOU 724 O MET A 92 7529 7615 4319 -414 156 1052 O
ATOM 725 CB MET A 92 18.300 88.746 247.222 1.00 52.89 C
ANISOU 725 CB MET A 92 7827 7825 4446 -525 264 1202 C
ATOM 726 CG MET A 92 18.886 89.306 248.502 1.00 53.82 C
ANISOU 726 CG MET A 92 7954 7999 4496 -450 303 1200 C
ATOM 727 SD MET A 92 18.853 88.080 249.823 1.00 58.10 S
ANISOU 727 SD MET A 92 8640 8481 4955 -479 319 1286 S
ATOM 728 CE MET A 92 17.212 87.351 249.544 1.00 57.90 C
ANISOU 728 CE MET A 92 8596 8424 4978 -645 357 1361 C
ATOM 729 N SER A 93 19.769 91.381 246.082 1.00 49.69 N
ANISOU 729 N SER A 93 7234 7555 4089 -346 242 1041 N
ATOM 730 CA SER A 93 21.044 91.942 245.612 1.00 47.95 C
ANISOU 730 CA SER A 93 7005 7348 3864 -246 201 973 C
ATOM 731 C SER A 93 22.210 91.229 246.261 1.00 47.42 C
ANISOU 731 C SER A 93 7045 7241 3733 -172 165 973 C
ATOM 732 O SER A 93 22.033 90.168 246.852 1.00 48.44 O
ANISOU 732 O SER A 93 7269 7310 3824 -198 162 1025 O
ATOM 733 CB SER A 93 21.129 93.431 245.938 1.00 47.57 C
ANISOU 733 CB SER A 93 6856 7391 3826 -207 242 935 C
ATOM 734 OG SER A 93 21.192 93.653 247.338 1.00 48.91 O
ANISOU 734 OG SER A 93 7048 7597 3938 -187 286 953 O
ATOM 735 N ALA A 94 23.397 91.828 246.170 1.00 46.25 N
ANISOU 735 N ALA A 94 6877 7126 3570 -80 139 917 N
ATOM 736 CA ALA A 94 24.614 91.258 246.774 1.00 45.86 C
ANISOU 736 CA ALA A 94 6910 7053 3461 5 98 913 C
ATOM 737 C ALA A 94 24.882 91.816 248.178 1.00 45.49 C
ANISOU 737 C ALA A 94 6862 7069 3353 36 126 921 C
ATOM 738 O ALA A 94 25.351 92.958 248.309 1.00 44.54 O
ANISOU 738 O ALA A 94 6668 7021 3235 73 135 873 O
ATOM 739 CB ALA A 94 25.785 91.507 245.885 1.00 45.53 C
ANISOU 739 CB ALA A 94 6845 7019 3437 84 50 852 C
ATOM 740 N PRO A 95 24.581 91.011 249.227 1.00 45.68 N
ANISOU 740 N PRO A 95 6974 7062 3320 16 139 984 N
ATOM 741 CA PRO A 95 24.523 91.449 250.626 1.00 45.56 C
ANISOU 741 CA PRO A 95 6969 7106 3237 22 178 1003 C
ATOM 742 C PRO A 95 25.888 91.771 251.159 1.00 45.35 C
ANISOU 742 C PRO A 95 6955 7118 3157 120 131 966 C
ATOM 743 O PRO A 95 26.821 90.995 250.980 1.00 45.89 O
ANISOU 743 O PRO A 95 7085 7144 3209 184 69 968 O
ATOM 744 CB PRO A 95 23.966 90.227 251.354 1.00 46.35 C
ANISOU 744 CB PRO A 95 7179 7143 3290 -24 190 1087 C
ATOM 745 CG PRO A 95 23.388 89.370 250.279 1.00 46.88 C
ANISOU 745 CG PRO A 95 7270 7125 3419 -83 173 1108 C
ATOM 746 CD PRO A 95 24.272 89.583 249.114 1.00 46.13 C
ANISOU 746 CD PRO A 95 7139 7019 3369 -19 117 1041 C
ATOM 747 N TYR A 96 26.004 92.903 251.827 1.00 45.24 N
ANISOU 747 N TYR A 96 6886 7188 3117 132 160 930 N
ATOM 748 CA TYR A 96 27.302 93.350 252.317 1.00 45.80 C
ANISOU 748 CA TYR A 96 6954 7308 3140 213 111 888 C
ATOM 749 C TYR A 96 27.355 93.635 253.854 1.00 46.71 C
ANISOU 749 C TYR A 96 7113 7477 3157 220 131 904 C
ATOM 750 O TYR A 96 26.346 94.005 254.473 1.00 47.30 O
ANISOU 750 O TYR A 96 7184 7577 3212 163 204 923 O
ATOM 751 CB TYR A 96 27.742 94.561 251.493 1.00 44.95 C
ANISOU 751 CB TYR A 96 6737 7249 3092 230 106 810 C
ATOM 752 CG TYR A 96 26.720 95.667 251.484 1.00 44.93 C
ANISOU 752 CG TYR A 96 6661 7284 3125 170 180 789 C
ATOM 753 CD1 TYR A 96 25.671 95.683 250.570 1.00 45.36 C
ANISOU 753 CD1 TYR A 96 6670 7310 3254 112 217 803 C
ATOM 754 CD2 TYR A 96 26.797 96.699 252.410 1.00 45.68 C
ANISOU 754 CD2 TYR A 96 6735 7445 3178 176 209 755 C
ATOM 755 CE1 TYR A 96 24.726 96.713 250.593 1.00 46.01 C
ANISOU 755 CE1 TYR A 96 6680 7430 3371 69 284 788 C
ATOM 756 CE2 TYR A 96 25.871 97.729 252.434 1.00 45.37 C
ANISOU 756 CE2 TYR A 96 6633 7435 3171 134 280 734 C
ATOM 757 CZ TYR A 96 24.842 97.730 251.535 1.00 45.44 C
ANISOU 757 CZ TYR A 96 6591 7417 3258 86 318 753 C
ATOM 758 OH TYR A 96 23.949 98.764 251.612 1.00 46.58 O
ANISOU 758 OH TYR A 96 6671 7594 3435 57 388 734 O
ATOM 759 N VAL A 97 28.518 93.434 254.470 1.00 46.58 N
ANISOU 759 N VAL A 97 7139 7485 3076 292 67 897 N
ATOM 760 CA VAL A 97 28.656 93.748 255.867 1.00 47.07 C
ANISOU 760 CA VAL A 97 7244 7604 3038 301 76 905 C
ATOM 761 C VAL A 97 28.688 95.271 255.952 1.00 46.40 C
ANISOU 761 C VAL A 97 7070 7594 2966 288 107 827 C
ATOM 762 O VAL A 97 29.425 95.907 255.201 1.00 45.69 O
ANISOU 762 O VAL A 97 6906 7526 2930 317 70 766 O
ATOM 763 CB VAL A 97 29.954 93.087 256.512 1.00 48.41 C
ANISOU 763 CB VAL A 97 7482 7783 3131 386 -16 924 C
ATOM 764 CG1 VAL A 97 30.326 93.751 257.828 1.00 48.08 C
ANISOU 764 CG1 VAL A 97 7459 7822 2986 398 -22 906 C
ATOM 765 CG2 VAL A 97 29.798 91.554 256.740 1.00 49.18 C
ANISOU 765 CG2 VAL A 97 7696 7795 3194 398 -37 1015 C
ATOM 766 N TYR A 98 27.831 95.820 256.816 1.00 46.73 N
ANISOU 766 N TYR A 98 7123 7671 2961 243 180 830 N
ATOM 767 CA TYR A 98 27.878 97.193 257.354 1.00 46.75 C
ANISOU 767 CA TYR A 98 7081 7743 2939 238 211 760 C
ATOM 768 C TYR A 98 27.727 97.028 258.857 1.00 48.23 C
ANISOU 768 C TYR A 98 7357 7968 2999 236 234 789 C
ATOM 769 O TYR A 98 26.613 96.805 259.363 1.00 48.24 O
ANISOU 769 O TYR A 98 7391 7964 2972 189 315 835 O
ATOM 770 CB TYR A 98 26.667 98.011 256.894 1.00 46.33 C
ANISOU 770 CB TYR A 98 6957 7689 2957 184 304 739 C
ATOM 771 CG TYR A 98 26.761 99.543 256.978 1.00 45.63 C
ANISOU 771 CG TYR A 98 6806 7648 2883 186 332 654 C
ATOM 772 CD1 TYR A 98 27.681 100.188 257.812 1.00 44.10 C
ANISOU 772 CD1 TYR A 98 6637 7505 2613 216 292 599 C
ATOM 773 CD2 TYR A 98 25.904 100.347 256.205 1.00 44.99 C
ANISOU 773 CD2 TYR A 98 6643 7556 2894 157 394 628 C
ATOM 774 CE1 TYR A 98 27.765 101.599 257.854 1.00 43.78 C
ANISOU 774 CE1 TYR A 98 6549 7494 2590 211 316 517 C
ATOM 775 CE2 TYR A 98 25.970 101.756 256.249 1.00 44.61 C
ANISOU 775 CE2 TYR A 98 6547 7536 2865 161 420 552 C
ATOM 776 CZ TYR A 98 26.905 102.373 257.078 1.00 43.83 C
ANISOU 776 CZ TYR A 98 6484 7480 2691 186 382 494 C
ATOM 777 OH TYR A 98 26.969 103.747 257.110 1.00 41.70 O
ANISOU 777 OH TYR A 98 6178 7225 2442 184 406 417 O
ATOM 778 N ASP A 99 28.838 97.143 259.575 1.00 49.62 N
ANISOU 778 N ASP A 99 7570 8189 3095 283 161 765 N
ATOM 779 CA ASP A 99 28.838 97.021 261.036 1.00 51.47 C
ANISOU 779 CA ASP A 99 7897 8467 3193 286 169 789 C
ATOM 780 C ASP A 99 28.347 95.644 261.475 1.00 52.86 C
ANISOU 780 C ASP A 99 8170 8597 3317 276 181 895 C
ATOM 781 O ASP A 99 28.802 94.616 260.965 1.00 53.00 O
ANISOU 781 O ASP A 99 8214 8560 3364 307 120 944 O
ATOM 782 CB ASP A 99 27.980 98.120 261.674 1.00 51.62 C
ANISOU 782 CB ASP A 99 7904 8530 3178 244 266 743 C
ATOM 783 CG ASP A 99 28.687 99.465 261.727 1.00 52.07 C
ANISOU 783 CG ASP A 99 7910 8637 3237 258 238 638 C
ATOM 784 OD1 ASP A 99 29.511 99.649 262.644 1.00 54.52 O
ANISOU 784 OD1 ASP A 99 8272 9000 3445 282 180 613 O
ATOM 785 OD2 ASP A 99 28.395 100.354 260.891 1.00 51.99 O
ANISOU 785 OD2 ASP A 99 7814 8615 3325 241 273 583 O
ATOM 786 N ARG A 100 27.386 95.650 262.396 1.00 54.69 N
ANISOU 786 N ARG A 100 8456 8849 3475 231 267 930 N
ATOM 787 CA ARG A 100 26.820 94.446 263.031 1.00 56.21 C
ANISOU 787 CA ARG A 100 8752 9008 3599 206 294 1036 C
ATOM 788 C ARG A 100 25.709 93.862 262.144 1.00 55.17 C
ANISOU 788 C ARG A 100 8587 8806 3569 146 358 1088 C
ATOM 789 O ARG A 100 24.861 93.101 262.606 1.00 55.57 O
ANISOU 789 O ARG A 100 8701 8832 3582 96 416 1170 O
ATOM 790 CB ARG A 100 26.297 94.830 264.437 1.00 58.06 C
ANISOU 790 CB ARG A 100 9052 9308 3701 181 366 1045 C
ATOM 791 CG ARG A 100 25.913 93.690 265.386 1.00 62.45 C
ANISOU 791 CG ARG A 100 9733 9847 4148 159 387 1156 C
ATOM 792 CD ARG A 100 24.373 93.489 265.552 1.00 66.60 C
ANISOU 792 CD ARG A 100 10258 10365 4683 75 523 1212 C
ATOM 793 NE ARG A 100 23.998 92.233 266.242 1.00 71.84 N
ANISOU 793 NE ARG A 100 11040 10992 5264 42 539 1333 N
ATOM 794 CZ ARG A 100 24.687 91.071 266.240 1.00 74.59 C
ANISOU 794 CZ ARG A 100 11478 11276 5589 73 447 1405 C
ATOM 795 NH1 ARG A 100 25.832 90.923 265.566 1.00 74.09 N
ANISOU 795 NH1 ARG A 100 11396 11178 5577 146 330 1371 N
ATOM 796 NH2 ARG A 100 24.216 90.020 266.917 1.00 76.29 N
ANISOU 796 NH2 ARG A 100 11805 11455 5726 33 476 1518 N
ATOM 797 N PHE A 101 25.732 94.211 260.860 1.00 53.52 N
ANISOU 797 N PHE A 101 8281 8568 3488 146 344 1041 N
ATOM 798 CA PHE A 101 24.649 93.817 259.969 1.00 53.20 C
ANISOU 798 CA PHE A 101 8196 8473 3546 83 401 1077 C
ATOM 799 C PHE A 101 25.123 93.386 258.583 1.00 52.13 C
ANISOU 799 C PHE A 101 8019 8270 3517 104 332 1065 C
ATOM 800 O PHE A 101 26.206 93.766 258.152 1.00 52.32 O
ANISOU 800 O PHE A 101 8010 8307 3562 166 259 1007 O
ATOM 801 CB PHE A 101 23.650 94.967 259.807 1.00 52.96 C
ANISOU 801 CB PHE A 101 8068 8489 3565 41 498 1030 C
ATOM 802 CG PHE A 101 22.961 95.376 261.085 1.00 53.61 C
ANISOU 802 CG PHE A 101 8185 8635 3549 16 589 1041 C
ATOM 803 CD1 PHE A 101 21.917 94.618 261.608 1.00 53.68 C
ANISOU 803 CD1 PHE A 101 8239 8634 3521 -47 666 1128 C
ATOM 804 CD2 PHE A 101 23.351 96.527 261.758 1.00 52.76 C
ANISOU 804 CD2 PHE A 101 8067 8595 3383 52 602 963 C
ATOM 805 CE1 PHE A 101 21.279 95.012 262.770 1.00 53.08 C
ANISOU 805 CE1 PHE A 101 8192 8625 3351 -68 759 1138 C
ATOM 806 CE2 PHE A 101 22.715 96.914 262.923 1.00 52.28 C
ANISOU 806 CE2 PHE A 101 8045 8593 3225 33 692 967 C
ATOM 807 CZ PHE A 101 21.683 96.160 263.422 1.00 52.56 C
ANISOU 807 CZ PHE A 101 8120 8626 3223 -23 773 1054 C
ATOM 808 N LEU A 102 24.317 92.579 257.900 1.00 51.11 N
ANISOU 808 N LEU A 102 7895 8074 3452 48 355 1119 N
ATOM 809 CA LEU A 102 24.481 92.365 256.474 1.00 49.79 C
ANISOU 809 CA LEU A 102 7674 7851 3393 52 312 1096 C
ATOM 810 C LEU A 102 23.330 93.102 255.863 1.00 48.71 C
ANISOU 810 C LEU A 102 7435 7736 3336 -14 388 1076 C
ATOM 811 O LEU A 102 22.182 92.846 256.255 1.00 49.29 O
ANISOU 811 O LEU A 102 7514 7811 3402 -85 462 1130 O
ATOM 812 CB LEU A 102 24.371 90.888 256.102 1.00 50.46 C
ANISOU 812 CB LEU A 102 7846 7836 3490 31 277 1169 C
ATOM 813 CG LEU A 102 25.644 90.042 256.146 1.00 51.30 C
ANISOU 813 CG LEU A 102 8040 7894 3559 117 180 1181 C
ATOM 814 CD1 LEU A 102 25.353 88.566 256.402 1.00 52.04 C
ANISOU 814 CD1 LEU A 102 8261 7891 3622 90 167 1275 C
ATOM 815 CD2 LEU A 102 26.421 90.217 254.862 1.00 51.25 C
ANISOU 815 CD2 LEU A 102 7971 7868 3635 170 121 1117 C
ATOM 816 N TYR A 103 23.631 94.027 254.940 1.00 46.50 N
ANISOU 816 N TYR A 103 7059 7477 3131 11 371 1002 N
ATOM 817 CA TYR A 103 22.603 94.818 254.234 1.00 45.20 C
ANISOU 817 CA TYR A 103 6789 7334 3053 -39 433 980 C
ATOM 818 C TYR A 103 22.381 94.341 252.790 1.00 44.56 C
ANISOU 818 C TYR A 103 6670 7193 3067 -67 397 986 C
ATOM 819 O TYR A 103 23.325 93.936 252.099 1.00 44.29 O
ANISOU 819 O TYR A 103 6660 7119 3049 -22 322 964 O
ATOM 820 CB TYR A 103 22.952 96.320 254.212 1.00 44.48 C
ANISOU 820 CB TYR A 103 6617 7305 2977 0 447 897 C
ATOM 821 CG TYR A 103 22.548 97.110 255.432 1.00 42.57 C
ANISOU 821 CG TYR A 103 6379 7128 2668 0 520 882 C
ATOM 822 CD1 TYR A 103 23.186 96.911 256.651 1.00 43.70 C
ANISOU 822 CD1 TYR A 103 6610 7297 2699 31 504 888 C
ATOM 823 CD2 TYR A 103 21.566 98.069 255.364 1.00 41.15 C
ANISOU 823 CD2 TYR A 103 6119 6984 2533 -25 601 861 C
ATOM 824 CE1 TYR A 103 22.848 97.625 257.767 1.00 42.27 C
ANISOU 824 CE1 TYR A 103 6441 7174 2445 31 571 868 C
ATOM 825 CE2 TYR A 103 21.202 98.780 256.489 1.00 41.73 C
ANISOU 825 CE2 TYR A 103 6203 7113 2540 -18 673 841 C
ATOM 826 CZ TYR A 103 21.858 98.551 257.682 1.00 41.96 C
ANISOU 826 CZ TYR A 103 6326 7165 2451 8 658 842 C
ATOM 827 OH TYR A 103 21.524 99.231 258.815 1.00 43.71 O
ANISOU 827 OH TYR A 103 6571 7444 2595 15 730 818 O
ATOM 828 N TYR A 104 21.136 94.402 252.336 1.00 43.90 N
ANISOU 828 N TYR A 104 6528 7110 3044 -139 451 1013 N
ATOM 829 CA TYR A 104 20.820 93.993 250.985 1.00 43.21 C
ANISOU 829 CA TYR A 104 6405 6972 3040 -175 417 1017 C
ATOM 830 C TYR A 104 19.518 94.589 250.531 1.00 43.44 C
ANISOU 830 C TYR A 104 6330 7036 3140 -239 477 1026 C
ATOM 831 O TYR A 104 18.697 95.000 251.346 1.00 43.28 O
ANISOU 831 O TYR A 104 6277 7066 3101 -266 555 1048 O
ATOM 832 CB TYR A 104 20.766 92.467 250.866 1.00 43.79 C
ANISOU 832 CB TYR A 104 6578 6960 3098 -214 379 1078 C
ATOM 833 CG TYR A 104 19.796 91.815 251.815 1.00 43.10 C
ANISOU 833 CG TYR A 104 6537 6870 2969 -287 439 1157 C
ATOM 834 CD1 TYR A 104 20.195 91.453 253.104 1.00 43.26 C
ANISOU 834 CD1 TYR A 104 6648 6896 2892 -261 451 1190 C
ATOM 835 CD2 TYR A 104 18.487 91.566 251.434 1.00 41.67 C
ANISOU 835 CD2 TYR A 104 6305 6684 2842 -386 482 1202 C
ATOM 836 CE1 TYR A 104 19.311 90.853 254.005 1.00 43.09 C
ANISOU 836 CE1 TYR A 104 6673 6874 2824 -332 513 1268 C
ATOM 837 CE2 TYR A 104 17.596 90.964 252.309 1.00 43.14 C
ANISOU 837 CE2 TYR A 104 6527 6873 2991 -461 543 1278 C
ATOM 838 CZ TYR A 104 18.013 90.600 253.603 1.00 43.28 C
ANISOU 838 CZ TYR A 104 6642 6894 2907 -435 562 1313 C
ATOM 839 OH TYR A 104 17.137 90.003 254.491 1.00 42.09 O
ANISOU 839 OH TYR A 104 6532 6749 2713 -513 629 1394 O
ATOM 840 N THR A 105 19.352 94.636 249.213 1.00 44.04 N
ANISOU 840 N THR A 105 6351 7088 3293 -257 441 1009 N
ATOM 841 CA THR A 105 18.109 95.108 248.595 1.00 45.32 C
ANISOU 841 CA THR A 105 6408 7280 3530 -318 482 1024 C
ATOM 842 C THR A 105 17.272 93.915 248.119 1.00 45.86 C
ANISOU 842 C THR A 105 6500 7297 3626 -412 467 1086 C
ATOM 843 O THR A 105 17.848 92.852 247.833 1.00 45.93 O
ANISOU 843 O THR A 105 6606 7232 3614 -416 407 1098 O
ATOM 844 CB THR A 105 18.385 96.150 247.456 1.00 44.56 C
ANISOU 844 CB THR A 105 6226 7204 3501 -280 453 964 C
ATOM 845 OG1 THR A 105 17.480 97.252 247.618 1.00 46.29 O
ANISOU 845 OG1 THR A 105 6342 7487 3760 -286 521 960 O
ATOM 846 CG2 THR A 105 18.266 95.544 245.995 1.00 44.60 C
ANISOU 846 CG2 THR A 105 6224 7159 3563 -320 388 969 C
ATOM 847 N ARG A 106 15.942 94.083 248.071 1.00 46.35 N
ANISOU 847 N ARG A 106 6478 7400 3734 -486 520 1127 N
ATOM 848 CA ARG A 106 15.025 93.029 247.566 1.00 47.71 C
ANISOU 848 CA ARG A 106 6656 7532 3941 -594 505 1186 C
ATOM 849 C ARG A 106 13.919 93.519 246.611 1.00 48.64 C
ANISOU 849 C ARG A 106 6642 7693 4147 -651 511 1195 C
ATOM 850 O ARG A 106 13.361 94.589 246.809 1.00 49.07 O
ANISOU 850 O ARG A 106 6589 7825 4232 -628 568 1186 O
ATOM 851 CB ARG A 106 14.371 92.271 248.728 1.00 48.48 C
ANISOU 851 CB ARG A 106 6800 7630 3989 -660 565 1260 C
ATOM 852 CG ARG A 106 15.280 91.295 249.462 1.00 47.15 C
ANISOU 852 CG ARG A 106 6786 7392 3738 -636 537 1278 C
ATOM 853 CD ARG A 106 14.521 90.112 249.960 1.00 45.78 C
ANISOU 853 CD ARG A 106 6676 7176 3543 -741 560 1364 C
ATOM 854 NE ARG A 106 13.518 90.483 250.945 1.00 47.43 N
ANISOU 854 NE ARG A 106 6819 7467 3735 -787 664 1411 N
ATOM 855 CZ ARG A 106 12.203 90.518 250.711 1.00 48.51 C
ANISOU 855 CZ ARG A 106 6851 7650 3930 -884 712 1455 C
ATOM 856 NH1 ARG A 106 11.722 90.215 249.509 1.00 48.59 N
ANISOU 856 NH1 ARG A 106 6812 7631 4019 -950 657 1456 N
ATOM 857 NH2 ARG A 106 11.365 90.865 251.682 1.00 47.49 N
ANISOU 857 NH2 ARG A 106 6662 7602 3778 -913 815 1496 N
ATOM 858 N ASP A 107 13.594 92.734 245.586 1.00 49.88 N
ANISOU 858 N ASP A 107 6811 7799 4343 -724 449 1211 N
ATOM 859 CA ASP A 107 12.459 93.037 244.714 1.00 51.18 C
ANISOU 859 CA ASP A 107 6854 8007 4586 -793 444 1231 C
ATOM 860 C ASP A 107 11.417 91.943 244.840 1.00 52.37 C
ANISOU 860 C ASP A 107 7013 8139 4749 -925 451 1304 C
ATOM 861 O ASP A 107 11.773 90.783 244.993 1.00 53.33 O
ANISOU 861 O ASP A 107 7258 8174 4830 -966 418 1325 O
ATOM 862 CB ASP A 107 12.924 93.101 243.275 1.00 51.16 C
ANISOU 862 CB ASP A 107 6853 7969 4617 -777 357 1184 C
ATOM 863 CG ASP A 107 13.946 94.207 243.040 1.00 54.66 C
ANISOU 863 CG ASP A 107 7281 8432 5054 -658 349 1116 C
ATOM 864 OD1 ASP A 107 13.550 95.408 243.112 1.00 59.01 O
ANISOU 864 OD1 ASP A 107 7724 9057 5641 -620 393 1105 O
ATOM 865 OD2 ASP A 107 15.146 93.888 242.776 1.00 58.42 O
ANISOU 865 OD2 ASP A 107 7853 8852 5492 -602 299 1073 O
ATOM 866 N VAL A 108 10.133 92.291 244.777 1.00 52.86 N
ANISOU 866 N VAL A 108 6941 8276 4866 -993 494 1346 N
ATOM 867 CA VAL A 108 9.076 91.269 244.773 1.00 53.47 C
ANISOU 867 CA VAL A 108 7008 8343 4966 -1136 494 1418 C
ATOM 868 C VAL A 108 8.311 91.357 243.478 1.00 53.07 C
ANISOU 868 C VAL A 108 6857 8315 4990 -1204 432 1420 C
ATOM 869 O VAL A 108 8.079 92.454 243.006 1.00 52.23 O
ANISOU 869 O VAL A 108 6634 8281 4931 -1147 438 1395 O
ATOM 870 CB VAL A 108 8.092 91.440 245.947 1.00 54.44 C
ANISOU 870 CB VAL A 108 7051 8548 5084 -1179 605 1481 C
ATOM 871 CG1 VAL A 108 7.247 90.173 246.131 1.00 55.40 C
ANISOU 871 CG1 VAL A 108 7202 8639 5210 -1334 607 1560 C
ATOM 872 CG2 VAL A 108 8.843 91.730 247.205 1.00 54.18 C
ANISOU 872 CG2 VAL A 108 7094 8518 4973 -1087 672 1467 C
ATOM 873 N LYS A 109 7.896 90.204 242.947 1.00 53.96 N
ANISOU 873 N LYS A 109 7022 8366 5115 -1328 373 1453 N
ATOM 874 CA LYS A 109 7.251 90.069 241.602 1.00 54.65 C
ANISOU 874 CA LYS A 109 7042 8460 5263 -1409 290 1451 C
ATOM 875 C LYS A 109 6.107 90.994 241.187 1.00 54.75 C
ANISOU 875 C LYS A 109 6856 8596 5352 -1431 308 1476 C
ATOM 876 O LYS A 109 5.956 91.253 240.013 1.00 55.36 O
ANISOU 876 O LYS A 109 6884 8685 5467 -1441 232 1452 O
ATOM 877 CB LYS A 109 6.824 88.623 241.261 1.00 55.86 C
ANISOU 877 CB LYS A 109 7283 8529 5414 -1562 231 1489 C
ATOM 878 CG LYS A 109 6.601 88.419 239.740 1.00 55.90 C
ANISOU 878 CG LYS A 109 7273 8511 5456 -1622 121 1459 C
ATOM 879 CD LYS A 109 5.956 87.100 239.358 1.00 57.77 C
ANISOU 879 CD LYS A 109 7572 8676 5700 -1792 62 1497 C
ATOM 880 CE LYS A 109 5.402 87.177 237.943 1.00 58.42 C
ANISOU 880 CE LYS A 109 7586 8784 5827 -1861 -35 1477 C
ATOM 881 NZ LYS A 109 4.346 86.155 237.667 1.00 59.58 N
ANISOU 881 NZ LYS A 109 7726 8909 6003 -2053 -82 1529 N
ATOM 882 N GLY A 110 5.280 91.474 242.087 1.00 55.04 N
ANISOU 882 N GLY A 110 6775 8726 5410 -1438 404 1524 N
ATOM 883 CA GLY A 110 4.257 92.391 241.609 1.00 54.96 C
ANISOU 883 CA GLY A 110 6573 8832 5478 -1439 415 1544 C
ATOM 884 C GLY A 110 4.610 93.859 241.718 1.00 53.59 C
ANISOU 884 C GLY A 110 6326 8718 5317 -1284 461 1500 C
ATOM 885 O GLY A 110 3.880 94.692 241.191 1.00 54.30 O
ANISOU 885 O GLY A 110 6267 8892 5473 -1264 458 1510 O
ATOM 886 N LEU A 111 5.734 94.161 242.378 1.00 52.19 N
ANISOU 886 N LEU A 111 6257 8494 5078 -1176 496 1451 N
ATOM 887 CA LEU A 111 6.003 95.473 243.006 1.00 50.88 C
ANISOU 887 CA LEU A 111 6037 8384 4910 -1042 574 1418 C
ATOM 888 C LEU A 111 7.091 96.287 242.343 1.00 49.54 C
ANISOU 888 C LEU A 111 5913 8177 4732 -928 524 1344 C
ATOM 889 O LEU A 111 8.125 95.751 241.922 1.00 48.71 O
ANISOU 889 O LEU A 111 5936 7987 4584 -919 457 1306 O
ATOM 890 CB LEU A 111 6.399 95.299 244.465 1.00 50.81 C
ANISOU 890 CB LEU A 111 6110 8366 4831 -1011 665 1422 C
ATOM 891 CG LEU A 111 5.525 94.382 245.313 1.00 52.79 C
ANISOU 891 CG LEU A 111 6350 8640 5068 -1124 727 1497 C
ATOM 892 CD1 LEU A 111 5.637 94.723 246.825 1.00 51.66 C
ANISOU 892 CD1 LEU A 111 6232 8535 4863 -1065 846 1503 C
ATOM 893 CD2 LEU A 111 4.058 94.427 244.832 1.00 53.65 C
ANISOU 893 CD2 LEU A 111 6285 8839 5262 -1215 735 1557 C
ATOM 894 N SER A 112 6.869 97.604 242.319 1.00 49.30 N
ANISOU 894 N SER A 112 5779 8210 4743 -837 564 1326 N
ATOM 895 CA SER A 112 7.609 98.526 241.447 1.00 47.88 C
ANISOU 895 CA SER A 112 5604 8011 4578 -746 512 1270 C
ATOM 896 C SER A 112 8.840 99.139 242.082 1.00 46.49 C
ANISOU 896 C SER A 112 5520 7797 4347 -638 544 1207 C
ATOM 897 O SER A 112 9.637 99.782 241.388 1.00 45.75 O
ANISOU 897 O SER A 112 5452 7675 4256 -573 498 1160 O
ATOM 898 CB SER A 112 6.686 99.643 240.959 1.00 48.36 C
ANISOU 898 CB SER A 112 5506 8152 4719 -707 527 1289 C
ATOM 899 OG SER A 112 5.493 99.112 240.410 1.00 49.50 O
ANISOU 899 OG SER A 112 5546 8345 4915 -809 495 1351 O
ATOM 900 N TYR A 113 8.975 98.951 243.392 1.00 45.94 N
ANISOU 900 N TYR A 113 5498 7731 4225 -626 622 1210 N
ATOM 901 CA TYR A 113 10.026 99.578 244.160 1.00 44.63 C
ANISOU 901 CA TYR A 113 5408 7543 4005 -530 658 1153 C
ATOM 902 C TYR A 113 10.793 98.604 245.040 1.00 45.47 C
ANISOU 902 C TYR A 113 5651 7600 4026 -548 662 1151 C
ATOM 903 O TYR A 113 10.232 97.646 245.600 1.00 46.38 O
ANISOU 903 O TYR A 113 5786 7718 4120 -627 689 1204 O
ATOM 904 CB TYR A 113 9.419 100.675 245.001 1.00 44.58 C
ANISOU 904 CB TYR A 113 5316 7605 4016 -466 759 1150 C
ATOM 905 CG TYR A 113 8.838 101.741 244.164 1.00 42.33 C
ANISOU 905 CG TYR A 113 4912 7359 3814 -423 751 1147 C
ATOM 906 CD1 TYR A 113 9.651 102.737 243.647 1.00 41.87 C
ANISOU 906 CD1 TYR A 113 4874 7270 3766 -339 719 1091 C
ATOM 907 CD2 TYR A 113 7.486 101.754 243.861 1.00 41.61 C
ANISOU 907 CD2 TYR A 113 4686 7334 3791 -467 772 1206 C
ATOM 908 CE1 TYR A 113 9.140 103.750 242.856 1.00 40.69 C
ANISOU 908 CE1 TYR A 113 4624 7147 3690 -295 709 1094 C
ATOM 909 CE2 TYR A 113 6.953 102.743 243.058 1.00 41.22 C
ANISOU 909 CE2 TYR A 113 4525 7319 3818 -419 757 1209 C
ATOM 910 CZ TYR A 113 7.793 103.739 242.556 1.00 41.27 C
ANISOU 910 CZ TYR A 113 4565 7285 3829 -331 725 1154 C
ATOM 911 OH TYR A 113 7.310 104.735 241.761 1.00 39.00 O
ANISOU 911 OH TYR A 113 4181 7024 3615 -279 708 1162 O
ATOM 912 N LYS A 114 12.089 98.848 245.173 1.00 45.45 N
ANISOU 912 N LYS A 114 5740 7553 3975 -478 634 1093 N
ATOM 913 CA LYS A 114 12.891 97.984 246.030 1.00 46.77 C
ANISOU 913 CA LYS A 114 6035 7676 4059 -480 632 1091 C
ATOM 914 C LYS A 114 12.500 98.073 247.516 1.00 47.26 C
ANISOU 914 C LYS A 114 6105 7781 4069 -474 730 1113 C
ATOM 915 O LYS A 114 11.878 99.034 247.960 1.00 47.44 O
ANISOU 915 O LYS A 114 6045 7868 4113 -440 805 1107 O
ATOM 916 CB LYS A 114 14.428 98.122 245.800 1.00 46.41 C
ANISOU 916 CB LYS A 114 6081 7579 3972 -408 572 1028 C
ATOM 917 CG LYS A 114 14.933 99.276 244.896 1.00 47.87 C
ANISOU 917 CG LYS A 114 6215 7772 4201 -343 539 973 C
ATOM 918 CD LYS A 114 16.180 98.884 244.020 1.00 49.05 C
ANISOU 918 CD LYS A 114 6439 7865 4334 -320 452 934 C
ATOM 919 CE LYS A 114 15.789 98.097 242.718 1.00 47.87 C
ANISOU 919 CE LYS A 114 6283 7683 4224 -385 385 959 C
ATOM 920 NZ LYS A 114 16.958 97.534 241.947 1.00 45.32 N
ANISOU 920 NZ LYS A 114 6044 7303 3874 -362 310 922 N
ATOM 921 N LEU A 115 12.832 97.027 248.254 1.00 47.53 N
ANISOU 921 N LEU A 115 6245 7781 4034 -508 730 1142 N
ATOM 922 CA LEU A 115 12.799 97.047 249.690 1.00 48.54 C
ANISOU 922 CA LEU A 115 6415 7940 4087 -492 809 1155 C
ATOM 923 C LEU A 115 14.258 97.144 250.105 1.00 48.42 C
ANISOU 923 C LEU A 115 6510 7887 3999 -415 767 1100 C
ATOM 924 O LEU A 115 15.131 96.630 249.386 1.00 48.27 O
ANISOU 924 O LEU A 115 6552 7807 3983 -405 679 1081 O
ATOM 925 CB LEU A 115 12.211 95.737 250.205 1.00 49.68 C
ANISOU 925 CB LEU A 115 6612 8067 4198 -589 829 1234 C
ATOM 926 CG LEU A 115 10.698 95.516 250.285 1.00 50.70 C
ANISOU 926 CG LEU A 115 6638 8252 4374 -681 896 1303 C
ATOM 927 CD1 LEU A 115 9.976 95.918 249.035 1.00 51.84 C
ANISOU 927 CD1 LEU A 115 6656 8419 4623 -708 863 1302 C
ATOM 928 CD2 LEU A 115 10.442 94.061 250.551 1.00 52.04 C
ANISOU 928 CD2 LEU A 115 6891 8373 4511 -785 883 1376 C
ATOM 929 N HIS A 116 14.527 97.795 251.241 1.00 48.74 N
ANISOU 929 N HIS A 116 6575 7967 3976 -359 827 1073 N
ATOM 930 CA HIS A 116 15.882 97.919 251.783 1.00 48.43 C
ANISOU 930 CA HIS A 116 6634 7906 3862 -291 787 1023 C
ATOM 931 C HIS A 116 15.915 97.150 253.087 1.00 49.92 C
ANISOU 931 C HIS A 116 6918 8099 3950 -310 824 1067 C
ATOM 932 O HIS A 116 15.358 97.610 254.079 1.00 50.78 O
ANISOU 932 O HIS A 116 7012 8265 4016 -306 913 1073 O
ATOM 933 CB HIS A 116 16.224 99.376 252.079 1.00 47.89 C
ANISOU 933 CB HIS A 116 6526 7879 3792 -214 819 949 C
ATOM 934 CG HIS A 116 16.244 100.257 250.873 1.00 46.83 C
ANISOU 934 CG HIS A 116 6305 7738 3749 -188 787 908 C
ATOM 935 ND1 HIS A 116 17.411 100.720 250.316 1.00 45.36 N
ANISOU 935 ND1 HIS A 116 6142 7525 3570 -138 717 849 N
ATOM 936 CD2 HIS A 116 15.235 100.778 250.130 1.00 47.23 C
ANISOU 936 CD2 HIS A 116 6246 7812 3888 -206 815 922 C
ATOM 937 CE1 HIS A 116 17.121 101.476 249.267 1.00 46.23 C
ANISOU 937 CE1 HIS A 116 6167 7635 3764 -129 705 830 C
ATOM 938 NE2 HIS A 116 15.807 101.529 249.133 1.00 44.82 N
ANISOU 938 NE2 HIS A 116 5908 7486 3636 -166 760 874 N
ATOM 939 N CYS A 117 16.564 95.986 253.102 1.00 50.42 N
ANISOU 939 N CYS A 117 7084 8101 3972 -327 760 1099 N
ATOM 940 CA CYS A 117 16.488 95.115 254.262 1.00 51.44 C
ANISOU 940 CA CYS A 117 7310 8226 4009 -357 791 1158 C
ATOM 941 C CYS A 117 17.836 94.915 254.866 1.00 51.45 C
ANISOU 941 C CYS A 117 7421 8204 3923 -288 732 1132 C
ATOM 942 O CYS A 117 18.862 95.309 254.303 1.00 50.66 O
ANISOU 942 O CYS A 117 7320 8087 3841 -225 661 1071 O
ATOM 943 CB CYS A 117 15.920 93.752 253.910 1.00 51.78 C
ANISOU 943 CB CYS A 117 7393 8210 4071 -447 772 1239 C
ATOM 944 SG CYS A 117 14.596 93.763 252.717 1.00 55.71 S
ANISOU 944 SG CYS A 117 7760 8715 4691 -535 788 1265 S
ATOM 945 N ARG A 118 17.804 94.231 256.006 1.00 52.79 N
ANISOU 945 N ARG A 118 7684 8376 3997 -306 761 1186 N
ATOM 946 CA ARG A 118 18.890 94.149 256.942 1.00 52.83 C
ANISOU 946 CA ARG A 118 7790 8385 3897 -242 725 1171 C
ATOM 947 C ARG A 118 18.762 92.784 257.622 1.00 53.90 C
ANISOU 947 C ARG A 118 8043 8475 3962 -288 722 1265 C
ATOM 948 O ARG A 118 17.659 92.299 257.825 1.00 54.38 O
ANISOU 948 O ARG A 118 8095 8538 4030 -371 790 1333 O
ATOM 949 CB ARG A 118 18.695 95.280 257.940 1.00 52.79 C
ANISOU 949 CB ARG A 118 7759 8466 3832 -211 803 1128 C
ATOM 950 CG ARG A 118 19.769 95.449 258.947 1.00 54.00 C
ANISOU 950 CG ARG A 118 8003 8642 3873 -147 767 1099 C
ATOM 951 CD ARG A 118 19.174 96.040 260.192 1.00 57.19 C
ANISOU 951 CD ARG A 118 8419 9121 4189 -152 869 1097 C
ATOM 952 NE ARG A 118 19.167 97.501 260.212 1.00 57.44 N
ANISOU 952 NE ARG A 118 8378 9206 4241 -109 907 1004 N
ATOM 953 CZ ARG A 118 18.720 98.224 261.242 1.00 60.15 C
ANISOU 953 CZ ARG A 118 8730 9615 4511 -98 997 979 C
ATOM 954 NH1 ARG A 118 18.236 97.638 262.344 1.00 59.36 N
ANISOU 954 NH1 ARG A 118 8703 9546 4306 -130 1063 1042 N
ATOM 955 NH2 ARG A 118 18.758 99.544 261.174 1.00 60.97 N
ANISOU 955 NH2 ARG A 118 8775 9750 4640 -56 1026 890 N
ATOM 956 N VAL A 119 19.892 92.165 257.949 1.00 54.49 N
ANISOU 956 N VAL A 119 8224 8508 3971 -234 642 1272 N
ATOM 957 CA VAL A 119 19.943 90.896 258.684 1.00 55.93 C
ANISOU 957 CA VAL A 119 8538 8639 4075 -261 630 1362 C
ATOM 958 C VAL A 119 21.168 91.005 259.598 1.00 56.96 C
ANISOU 958 C VAL A 119 8752 8793 4096 -172 575 1341 C
ATOM 959 O VAL A 119 22.177 91.576 259.194 1.00 56.86 O
ANISOU 959 O VAL A 119 8708 8792 4103 -96 507 1267 O
ATOM 960 CB VAL A 119 19.988 89.668 257.707 1.00 55.84 C
ANISOU 960 CB VAL A 119 8573 8515 4129 -295 563 1407 C
ATOM 961 CG1 VAL A 119 20.960 88.591 258.154 1.00 56.75 C
ANISOU 961 CG1 VAL A 119 8833 8559 4172 -246 485 1453 C
ATOM 962 CG2 VAL A 119 18.605 89.086 257.506 1.00 55.29 C
ANISOU 962 CG2 VAL A 119 8482 8421 4103 -416 630 1478 C
ATOM 963 N PRO A 120 21.079 90.506 260.845 1.00 58.81 N
ANISOU 963 N PRO A 120 9089 9042 4214 -184 604 1407 N
ATOM 964 CA PRO A 120 22.179 90.704 261.791 1.00 59.57 C
ANISOU 964 CA PRO A 120 9259 9176 4197 -103 551 1386 C
ATOM 965 C PRO A 120 23.422 89.945 261.373 1.00 59.88 C
ANISOU 965 C PRO A 120 9363 9146 4242 -29 427 1391 C
ATOM 966 O PRO A 120 23.318 88.909 260.725 1.00 60.26 O
ANISOU 966 O PRO A 120 9452 9100 4342 -52 394 1443 O
ATOM 967 CB PRO A 120 21.631 90.118 263.097 1.00 60.80 C
ANISOU 967 CB PRO A 120 9520 9351 4232 -148 614 1477 C
ATOM 968 CG PRO A 120 20.160 90.161 262.946 1.00 61.06 C
ANISOU 968 CG PRO A 120 9489 9397 4314 -249 729 1513 C
ATOM 969 CD PRO A 120 19.937 89.838 261.493 1.00 60.27 C
ANISOU 969 CD PRO A 120 9319 9223 4358 -278 692 1502 C
ATOM 970 N ALA A 121 24.580 90.465 261.763 1.00 60.19 N
ANISOU 970 N ALA A 121 9410 9234 4227 57 359 1336 N
ATOM 971 CA ALA A 121 25.884 89.973 261.317 1.00 60.34 C
ANISOU 971 CA ALA A 121 9458 9209 4259 144 240 1323 C
ATOM 972 C ALA A 121 25.972 88.474 260.917 1.00 61.08 C
ANISOU 972 C ALA A 121 9648 9186 4375 147 191 1406 C
ATOM 973 O ALA A 121 26.352 88.149 259.766 1.00 60.51 O
ANISOU 973 O ALA A 121 9544 9051 4396 175 140 1381 O
ATOM 974 CB ALA A 121 26.946 90.315 262.368 1.00 61.29 C
ANISOU 974 CB ALA A 121 9625 9400 4264 219 179 1303 C
ATOM 975 N GLY A 122 25.622 87.579 261.843 1.00 61.58 N
ANISOU 975 N GLY A 122 9834 9216 4349 118 209 1504 N
ATOM 976 CA GLY A 122 25.960 86.178 261.672 1.00 62.52 C
ANISOU 976 CA GLY A 122 10068 9219 4467 142 147 1583 C
ATOM 977 C GLY A 122 24.807 85.303 261.247 1.00 63.44 C
ANISOU 977 C GLY A 122 10226 9241 4636 36 204 1655 C
ATOM 978 O GLY A 122 24.781 84.109 261.554 1.00 64.57 O
ANISOU 978 O GLY A 122 10500 9290 4743 25 180 1746 O
ATOM 979 N LYS A 123 23.846 85.903 260.549 1.00 62.92 N
ANISOU 979 N LYS A 123 10050 9199 4658 -45 276 1615 N
ATOM 980 CA LYS A 123 22.639 85.210 260.098 1.00 63.12 C
ANISOU 980 CA LYS A 123 10088 9152 4741 -163 334 1676 C
ATOM 981 C LYS A 123 22.596 85.160 258.571 1.00 62.80 C
ANISOU 981 C LYS A 123 9976 9053 4833 -172 300 1620 C
ATOM 982 O LYS A 123 23.542 85.590 257.889 1.00 62.03 O
ANISOU 982 O LYS A 123 9827 8965 4776 -82 234 1542 O
ATOM 983 CB LYS A 123 21.390 85.904 260.650 1.00 62.97 C
ANISOU 983 CB LYS A 123 9997 9223 4706 -260 455 1689 C
ATOM 984 CG LYS A 123 21.408 86.155 262.144 1.00 62.47 C
ANISOU 984 CG LYS A 123 9993 9237 4504 -249 501 1727 C
ATOM 985 CD LYS A 123 21.353 84.845 262.926 1.00 62.46 C
ANISOU 985 CD LYS A 123 10156 9159 4418 -279 491 1849 C
ATOM 986 CE LYS A 123 20.933 85.085 264.367 1.00 61.58 C
ANISOU 986 CE LYS A 123 10094 9133 4172 -309 571 1900 C
ATOM 987 NZ LYS A 123 20.160 83.946 264.903 1.00 60.52 N
ANISOU 987 NZ LYS A 123 10072 8932 3990 -406 619 2030 N
ATOM 988 N THR A 124 21.498 84.643 258.026 1.00 63.45 N
ANISOU 988 N THR A 124 10051 9078 4979 -284 343 1661 N
ATOM 989 CA THR A 124 21.460 84.329 256.603 1.00 63.42 C
ANISOU 989 CA THR A 124 10013 8998 5085 -300 299 1623 C
ATOM 990 C THR A 124 20.510 85.265 255.827 1.00 62.35 C
ANISOU 990 C THR A 124 9721 8932 5038 -372 358 1571 C
ATOM 991 O THR A 124 19.312 85.296 256.115 1.00 63.20 O
ANISOU 991 O THR A 124 9792 9069 5154 -480 437 1618 O
ATOM 992 CB THR A 124 21.138 82.816 256.375 1.00 64.77 C
ANISOU 992 CB THR A 124 10321 9022 5267 -364 272 1705 C
ATOM 993 OG1 THR A 124 21.968 82.005 257.226 1.00 66.86 O
ANISOU 993 OG1 THR A 124 10734 9227 5442 -291 224 1763 O
ATOM 994 CG2 THR A 124 21.368 82.415 254.920 1.00 64.49 C
ANISOU 994 CG2 THR A 124 10278 8897 5328 -355 209 1653 C
ATOM 995 N PRO A 125 21.042 86.028 254.838 1.00 60.72 N
ANISOU 995 N PRO A 125 9419 8753 4898 -311 319 1478 N
ATOM 996 CA PRO A 125 20.212 87.054 254.208 1.00 59.65 C
ANISOU 996 CA PRO A 125 9134 8693 4838 -363 372 1430 C
ATOM 997 C PRO A 125 19.055 86.469 253.394 1.00 59.81 C
ANISOU 997 C PRO A 125 9132 8659 4934 -484 391 1467 C
ATOM 998 O PRO A 125 19.257 85.570 252.598 1.00 59.92 O
ANISOU 998 O PRO A 125 9212 8571 4983 -498 331 1473 O
ATOM 999 CB PRO A 125 21.202 87.803 253.298 1.00 58.37 C
ANISOU 999 CB PRO A 125 8904 8552 4721 -267 313 1333 C
ATOM 1000 CG PRO A 125 22.567 87.327 253.671 1.00 58.00 C
ANISOU 1000 CG PRO A 125 8954 8469 4613 -160 240 1327 C
ATOM 1001 CD PRO A 125 22.379 85.961 254.215 1.00 59.90 C
ANISOU 1001 CD PRO A 125 9337 8614 4807 -195 229 1417 C
ATOM 1002 N GLY A 126 17.853 86.986 253.608 1.00 60.12 N
ANISOU 1002 N GLY A 126 9077 8770 4997 -571 475 1490 N
ATOM 1003 CA GLY A 126 16.667 86.540 252.895 1.00 60.42 C
ANISOU 1003 CA GLY A 126 9069 8778 5109 -696 494 1528 C
ATOM 1004 C GLY A 126 15.436 86.829 253.719 1.00 61.36 C
ANISOU 1004 C GLY A 126 9122 8978 5214 -786 600 1586 C
ATOM 1005 O GLY A 126 15.505 86.851 254.957 1.00 61.47 O
ANISOU 1005 O GLY A 126 9185 9029 5140 -769 653 1624 O
ATOM 1006 N GLU A 127 14.318 87.067 253.030 1.00 61.61 N
ANISOU 1006 N GLU A 127 9037 9044 5328 -877 632 1592 N
ATOM 1007 CA GLU A 127 12.999 87.236 253.663 1.00 62.92 C
ANISOU 1007 CA GLU A 127 9120 9289 5497 -975 736 1655 C
ATOM 1008 C GLU A 127 12.751 86.165 254.733 1.00 64.27 C
ANISOU 1008 C GLU A 127 9415 9416 5589 -1046 774 1754 C
ATOM 1009 O GLU A 127 12.738 84.977 254.448 1.00 65.25 O
ANISOU 1009 O GLU A 127 9643 9430 5719 -1116 725 1804 O
ATOM 1010 CB GLU A 127 11.918 87.190 252.593 1.00 62.96 C
ANISOU 1010 CB GLU A 127 9013 9303 5608 -1080 732 1664 C
ATOM 1011 CG GLU A 127 10.510 87.473 253.072 1.00 64.75 C
ANISOU 1011 CG GLU A 127 9118 9628 5857 -1178 838 1722 C
ATOM 1012 CD GLU A 127 9.507 87.343 251.935 1.00 66.29 C
ANISOU 1012 CD GLU A 127 9201 9828 6158 -1284 814 1733 C
ATOM 1013 OE1 GLU A 127 9.704 86.440 251.089 1.00 67.86 O
ANISOU 1013 OE1 GLU A 127 9475 9922 6387 -1338 726 1736 O
ATOM 1014 OE2 GLU A 127 8.540 88.139 251.873 1.00 65.64 O
ANISOU 1014 OE2 GLU A 127 8957 9856 6128 -1310 880 1736 O
ATOM 1015 N GLY A 128 12.577 86.589 255.971 1.00 64.88 N
ANISOU 1015 N GLY A 128 9490 9574 5587 -1027 862 1781 N
ATOM 1016 CA GLY A 128 12.583 85.649 257.082 1.00 66.41 C
ANISOU 1016 CA GLY A 128 9821 9727 5684 -1071 892 1872 C
ATOM 1017 C GLY A 128 12.418 86.319 258.428 1.00 67.09 C
ANISOU 1017 C GLY A 128 9894 9923 5674 -1037 994 1887 C
ATOM 1018 O GLY A 128 11.982 87.473 258.520 1.00 66.60 O
ANISOU 1018 O GLY A 128 9700 9973 5633 -1006 1063 1837 O
ATOM 1019 N GLU A 129 12.767 85.587 259.475 1.00 68.58 N
ANISOU 1019 N GLU A 129 10228 10076 5754 -1040 1004 1956 N
ATOM 1020 CA GLU A 129 12.516 86.037 260.847 1.00 69.96 C
ANISOU 1020 CA GLU A 129 10413 10351 5819 -1027 1108 1986 C
ATOM 1021 C GLU A 129 13.573 87.007 261.301 1.00 68.93 C
ANISOU 1021 C GLU A 129 10295 10274 5623 -881 1083 1898 C
ATOM 1022 O GLU A 129 13.316 87.837 262.174 1.00 69.52 O
ANISOU 1022 O GLU A 129 10329 10456 5631 -852 1172 1879 O
ATOM 1023 CB GLU A 129 12.457 84.864 261.832 1.00 71.76 C
ANISOU 1023 CB GLU A 129 10800 10522 5945 -1093 1129 2103 C
ATOM 1024 CG GLU A 129 13.754 84.081 261.992 1.00 72.91 C
ANISOU 1024 CG GLU A 129 11122 10555 6027 -1014 1015 2114 C
ATOM 1025 CD GLU A 129 13.888 83.470 263.378 1.00 77.80 C
ANISOU 1025 CD GLU A 129 11889 11172 6501 -1026 1054 2209 C
ATOM 1026 OE1 GLU A 129 13.586 84.172 264.379 1.00 79.23 O
ANISOU 1026 OE1 GLU A 129 12039 11472 6594 -1012 1149 2210 O
ATOM 1027 OE2 GLU A 129 14.299 82.288 263.468 1.00 79.10 O
ANISOU 1027 OE2 GLU A 129 12207 11214 6635 -1045 989 2283 O
ATOM 1028 N ASP A 130 14.760 86.882 260.709 1.00 67.52 N
ANISOU 1028 N ASP A 130 10173 10021 5460 -792 964 1844 N
ATOM 1029 CA ASP A 130 15.907 87.705 261.072 1.00 66.37 C
ANISOU 1029 CA ASP A 130 10045 9917 5256 -659 920 1762 C
ATOM 1030 C ASP A 130 15.871 89.065 260.363 1.00 64.80 C
ANISOU 1030 C ASP A 130 9693 9790 5139 -607 930 1653 C
ATOM 1031 O ASP A 130 16.486 90.037 260.824 1.00 64.29 O
ANISOU 1031 O ASP A 130 9612 9790 5025 -518 933 1582 O
ATOM 1032 CB ASP A 130 17.210 86.970 260.725 1.00 66.04 C
ANISOU 1032 CB ASP A 130 10119 9771 5201 -584 789 1754 C
ATOM 1033 CG ASP A 130 17.412 85.700 261.538 1.00 67.52 C
ANISOU 1033 CG ASP A 130 10476 9883 5296 -611 770 1860 C
ATOM 1034 OD1 ASP A 130 16.992 85.660 262.719 1.00 68.82 O
ANISOU 1034 OD1 ASP A 130 10688 10102 5357 -644 847 1920 O
ATOM 1035 OD2 ASP A 130 18.015 84.745 260.997 1.00 67.24 O
ANISOU 1035 OD2 ASP A 130 10531 9731 5287 -593 678 1883 O
ATOM 1036 N GLU A 131 15.144 89.115 259.247 1.00 63.69 N
ANISOU 1036 N GLU A 131 9446 9634 5120 -666 933 1643 N
ATOM 1037 CA GLU A 131 15.185 90.244 258.331 1.00 61.91 C
ANISOU 1037 CA GLU A 131 9087 9449 4986 -617 921 1549 C
ATOM 1038 C GLU A 131 14.298 91.374 258.807 1.00 61.96 C
ANISOU 1038 C GLU A 131 8977 9571 4995 -620 1036 1524 C
ATOM 1039 O GLU A 131 13.086 91.193 258.982 1.00 62.95 O
ANISOU 1039 O GLU A 131 9041 9735 5142 -708 1123 1583 O
ATOM 1040 CB GLU A 131 14.788 89.820 256.901 1.00 61.34 C
ANISOU 1040 CB GLU A 131 8954 9314 5037 -675 868 1550 C
ATOM 1041 CG GLU A 131 14.409 90.981 255.965 1.00 59.66 C
ANISOU 1041 CG GLU A 131 8584 9158 4925 -654 879 1476 C
ATOM 1042 CD GLU A 131 13.969 90.527 254.583 1.00 60.11 C
ANISOU 1042 CD GLU A 131 8588 9160 5092 -718 825 1483 C
ATOM 1043 OE1 GLU A 131 14.847 90.119 253.797 1.00 60.27 O
ANISOU 1043 OE1 GLU A 131 8665 9102 5133 -682 727 1451 O
ATOM 1044 OE2 GLU A 131 12.753 90.582 254.268 1.00 60.00 O
ANISOU 1044 OE2 GLU A 131 8471 9184 5140 -805 878 1518 O
ATOM 1045 N GLU A 132 14.922 92.531 259.012 1.00 60.76 N
ANISOU 1045 N GLU A 132 8794 9471 4821 -523 1035 1436 N
ATOM 1046 CA GLU A 132 14.210 93.765 259.235 1.00 60.53 C
ANISOU 1046 CA GLU A 132 8649 9536 4813 -503 1131 1390 C
ATOM 1047 C GLU A 132 14.163 94.546 257.935 1.00 58.58 C
ANISOU 1047 C GLU A 132 8282 9283 4691 -476 1091 1324 C
ATOM 1048 O GLU A 132 15.198 94.817 257.337 1.00 57.99 O
ANISOU 1048 O GLU A 132 8227 9169 4638 -413 1001 1263 O
ATOM 1049 CB GLU A 132 14.897 94.581 260.314 1.00 61.01 C
ANISOU 1049 CB GLU A 132 8764 9650 4766 -418 1155 1331 C
ATOM 1050 CG GLU A 132 13.901 95.344 261.175 1.00 65.10 C
ANISOU 1050 CG GLU A 132 9223 10265 5246 -425 1295 1329 C
ATOM 1051 CD GLU A 132 14.533 96.492 261.927 1.00 67.50 C
ANISOU 1051 CD GLU A 132 9554 10621 5474 -333 1315 1238 C
ATOM 1052 OE1 GLU A 132 15.495 96.236 262.697 1.00 67.36 O
ANISOU 1052 OE1 GLU A 132 9657 10592 5344 -298 1266 1231 O
ATOM 1053 OE2 GLU A 132 14.056 97.644 261.732 1.00 68.50 O
ANISOU 1053 OE2 GLU A 132 9579 10794 5653 -296 1375 1175 O
ATOM 1054 N ILE A 133 12.958 94.867 257.477 1.00 57.78 N
ANISOU 1054 N ILE A 133 8054 9225 4674 -527 1158 1342 N
ATOM 1055 CA ILE A 133 12.767 95.688 256.291 1.00 55.64 C
ANISOU 1055 CA ILE A 133 7662 8959 4519 -502 1130 1288 C
ATOM 1056 C ILE A 133 12.973 97.142 256.695 1.00 54.74 C
ANISOU 1056 C ILE A 133 7503 8905 4391 -408 1179 1204 C
ATOM 1057 O ILE A 133 12.071 97.762 257.272 1.00 55.33 O
ANISOU 1057 O ILE A 133 7509 9053 4461 -405 1287 1207 O
ATOM 1058 CB ILE A 133 11.334 95.570 255.742 1.00 56.27 C
ANISOU 1058 CB ILE A 133 7614 9076 4691 -585 1186 1342 C
ATOM 1059 CG1 ILE A 133 11.016 94.138 255.322 1.00 58.11 C
ANISOU 1059 CG1 ILE A 133 7889 9246 4942 -695 1139 1424 C
ATOM 1060 CG2 ILE A 133 11.121 96.508 254.569 1.00 55.32 C
ANISOU 1060 CG2 ILE A 133 7368 8968 4682 -549 1157 1288 C
ATOM 1061 CD1 ILE A 133 9.545 93.920 254.848 1.00 61.40 C
ANISOU 1061 CD1 ILE A 133 8176 9708 5446 -798 1191 1486 C
ATOM 1062 N VAL A 134 14.151 97.682 256.383 1.00 52.78 N
ANISOU 1062 N VAL A 134 7294 8624 4137 -333 1101 1129 N
ATOM 1063 CA VAL A 134 14.502 99.056 256.749 1.00 51.57 C
ANISOU 1063 CA VAL A 134 7118 8510 3967 -248 1133 1043 C
ATOM 1064 C VAL A 134 13.615 100.086 256.036 1.00 50.81 C
ANISOU 1064 C VAL A 134 6881 8447 3977 -232 1182 1016 C
ATOM 1065 O VAL A 134 13.015 100.916 256.690 1.00 51.83 O
ANISOU 1065 O VAL A 134 6968 8633 4090 -200 1279 993 O
ATOM 1066 CB VAL A 134 16.019 99.360 256.551 1.00 50.58 C
ANISOU 1066 CB VAL A 134 7063 8343 3814 -183 1031 973 C
ATOM 1067 CG1 VAL A 134 16.346 100.777 256.987 1.00 50.35 C
ANISOU 1067 CG1 VAL A 134 7017 8349 3764 -110 1065 885 C
ATOM 1068 CG2 VAL A 134 16.859 98.389 257.334 1.00 50.67 C
ANISOU 1068 CG2 VAL A 134 7205 8329 3717 -186 984 1003 C
ATOM 1069 N LEU A 135 13.522 100.047 254.716 1.00 49.36 N
ANISOU 1069 N LEU A 135 6628 8230 3898 -250 1118 1020 N
ATOM 1070 CA LEU A 135 12.611 100.949 254.027 1.00 48.98 C
ANISOU 1070 CA LEU A 135 6445 8215 3950 -236 1160 1008 C
ATOM 1071 C LEU A 135 11.808 100.182 252.988 1.00 49.56 C
ANISOU 1071 C LEU A 135 6442 8277 4110 -316 1127 1075 C
ATOM 1072 O LEU A 135 12.363 99.348 252.271 1.00 49.61 O
ANISOU 1072 O LEU A 135 6498 8224 4128 -353 1034 1090 O
ATOM 1073 CB LEU A 135 13.376 102.100 253.367 1.00 47.12 C
ANISOU 1073 CB LEU A 135 6192 7953 3758 -159 1109 926 C
ATOM 1074 CG LEU A 135 12.551 103.284 252.839 1.00 45.96 C
ANISOU 1074 CG LEU A 135 5922 7837 3702 -119 1159 903 C
ATOM 1075 CD1 LEU A 135 12.140 104.143 253.994 1.00 46.60 C
ANISOU 1075 CD1 LEU A 135 6001 7969 3736 -64 1271 869 C
ATOM 1076 CD2 LEU A 135 13.305 104.146 251.837 1.00 42.08 C
ANISOU 1076 CD2 LEU A 135 5417 7302 3270 -69 1084 844 C
ATOM 1077 N ASP A 136 10.510 100.453 252.897 1.00 50.36 N
ANISOU 1077 N ASP A 136 6423 8439 4272 -341 1201 1112 N
ATOM 1078 CA ASP A 136 9.716 99.908 251.783 1.00 50.75 C
ANISOU 1078 CA ASP A 136 6382 8486 4415 -417 1160 1167 C
ATOM 1079 C ASP A 136 9.265 100.992 250.783 1.00 49.84 C
ANISOU 1079 C ASP A 136 6140 8393 4404 -370 1148 1139 C
ATOM 1080 O ASP A 136 8.226 101.614 250.964 1.00 50.23 O
ANISOU 1080 O ASP A 136 6076 8510 4498 -353 1230 1155 O
ATOM 1081 CB ASP A 136 8.516 99.108 252.321 1.00 52.35 C
ANISOU 1081 CB ASP A 136 6535 8742 4614 -509 1236 1253 C
ATOM 1082 CG ASP A 136 7.787 98.297 251.232 1.00 53.75 C
ANISOU 1082 CG ASP A 136 6640 8908 4874 -612 1176 1315 C
ATOM 1083 OD1 ASP A 136 8.135 98.397 250.029 1.00 51.43 O
ANISOU 1083 OD1 ASP A 136 6330 8571 4640 -606 1080 1290 O
ATOM 1084 OD2 ASP A 136 6.842 97.554 251.608 1.00 57.08 O
ANISOU 1084 OD2 ASP A 136 7022 9368 5297 -704 1228 1389 O
ATOM 1085 N GLU A 137 10.031 101.188 249.716 1.00 48.70 N
ANISOU 1085 N GLU A 137 6015 8193 4296 -347 1049 1102 N
ATOM 1086 CA GLU A 137 9.732 102.240 248.731 1.00 48.64 C
ANISOU 1086 CA GLU A 137 5905 8196 4379 -298 1028 1078 C
ATOM 1087 C GLU A 137 8.300 102.286 248.161 1.00 49.41 C
ANISOU 1087 C GLU A 137 5852 8355 4566 -340 1054 1137 C
ATOM 1088 O GLU A 137 7.776 103.360 247.860 1.00 48.70 O
ANISOU 1088 O GLU A 137 5663 8301 4540 -277 1085 1124 O
ATOM 1089 CB GLU A 137 10.755 102.221 247.613 1.00 47.54 C
ANISOU 1089 CB GLU A 137 5817 7991 4257 -287 915 1042 C
ATOM 1090 CG GLU A 137 12.168 102.517 248.098 1.00 48.14 C
ANISOU 1090 CG GLU A 137 6009 8021 4261 -227 892 975 C
ATOM 1091 CD GLU A 137 13.103 102.790 246.960 1.00 48.90 C
ANISOU 1091 CD GLU A 137 6128 8067 4386 -203 797 936 C
ATOM 1092 OE1 GLU A 137 12.611 102.832 245.805 1.00 48.70 O
ANISOU 1092 OE1 GLU A 137 6031 8042 4432 -227 754 959 O
ATOM 1093 OE2 GLU A 137 14.320 102.955 247.220 1.00 49.72 O
ANISOU 1093 OE2 GLU A 137 6318 8137 4437 -162 766 884 O
ATOM 1094 N ASN A 138 7.676 101.118 248.049 1.00 50.60 N
ANISOU 1094 N ASN A 138 5986 8518 4722 -446 1041 1205 N
ATOM 1095 CA ASN A 138 6.248 100.990 247.711 1.00 52.17 C
ANISOU 1095 CA ASN A 138 6037 8790 4997 -506 1072 1272 C
ATOM 1096 C ASN A 138 5.264 101.707 248.654 1.00 53.87 C
ANISOU 1096 C ASN A 138 6149 9096 5224 -461 1205 1287 C
ATOM 1097 O ASN A 138 4.246 102.254 248.187 1.00 54.80 O
ANISOU 1097 O ASN A 138 6116 9279 5427 -448 1229 1315 O
ATOM 1098 CB ASN A 138 5.880 99.511 247.622 1.00 52.34 C
ANISOU 1098 CB ASN A 138 6085 8797 5005 -642 1038 1338 C
ATOM 1099 CG ASN A 138 6.841 98.747 246.778 1.00 51.00 C
ANISOU 1099 CG ASN A 138 6029 8534 4816 -679 917 1319 C
ATOM 1100 OD1 ASN A 138 6.835 98.852 245.552 1.00 51.97 O
ANISOU 1100 OD1 ASN A 138 6112 8638 4995 -689 832 1312 O
ATOM 1101 ND2 ASN A 138 7.709 98.002 247.421 1.00 50.94 N
ANISOU 1101 ND2 ASN A 138 6165 8466 4725 -690 908 1309 N
ATOM 1102 N LYS A 139 5.566 101.678 249.960 1.00 54.43 N
ANISOU 1102 N LYS A 139 6299 9174 5207 -435 1290 1270 N
ATOM 1103 CA LYS A 139 4.801 102.391 250.995 1.00 55.92 C
ANISOU 1103 CA LYS A 139 6417 9444 5385 -378 1429 1269 C
ATOM 1104 C LYS A 139 5.084 103.878 250.946 1.00 55.21 C
ANISOU 1104 C LYS A 139 6307 9349 5320 -243 1454 1194 C
ATOM 1105 O LYS A 139 4.222 104.696 251.203 1.00 56.24 O
ANISOU 1105 O LYS A 139 6328 9545 5495 -182 1543 1195 O
ATOM 1106 CB LYS A 139 5.100 101.852 252.411 1.00 56.98 C
ANISOU 1106 CB LYS A 139 6663 9585 5401 -397 1507 1273 C
ATOM 1107 CG LYS A 139 4.690 100.372 252.664 1.00 59.03 C
ANISOU 1107 CG LYS A 139 6947 9852 5629 -535 1505 1359 C
ATOM 1108 CD LYS A 139 4.154 100.126 254.076 1.00 63.91 C
ANISOU 1108 CD LYS A 139 7578 10537 6167 -554 1640 1394 C
ATOM 1109 CE LYS A 139 5.191 100.359 255.192 1.00 65.42 C
ANISOU 1109 CE LYS A 139 7926 10696 6233 -485 1671 1336 C
ATOM 1110 NZ LYS A 139 4.527 100.370 256.539 1.00 66.53 N
ANISOU 1110 NZ LYS A 139 8060 10920 6297 -487 1819 1364 N
ATOM 1111 N LEU A 140 6.315 104.220 250.625 1.00 54.52 N
ANISOU 1111 N LEU A 140 6328 9181 5206 -198 1376 1129 N
ATOM 1112 CA LEU A 140 6.677 105.593 250.260 1.00 54.43 C
ANISOU 1112 CA LEU A 140 6302 9143 5234 -87 1370 1062 C
ATOM 1113 C LEU A 140 5.929 106.127 249.016 1.00 54.68 C
ANISOU 1113 C LEU A 140 6196 9194 5387 -70 1328 1090 C
ATOM 1114 O LEU A 140 5.502 107.277 248.998 1.00 55.08 O
ANISOU 1114 O LEU A 140 6176 9263 5487 23 1379 1066 O
ATOM 1115 CB LEU A 140 8.201 105.695 250.026 1.00 52.85 C
ANISOU 1115 CB LEU A 140 6241 8854 4985 -65 1280 997 C
ATOM 1116 CG LEU A 140 9.127 106.313 251.069 1.00 51.80 C
ANISOU 1116 CG LEU A 140 6223 8694 4764 3 1319 920 C
ATOM 1117 CD1 LEU A 140 10.098 107.236 250.339 1.00 49.54 C
ANISOU 1117 CD1 LEU A 140 5976 8342 4507 62 1245 854 C
ATOM 1118 CD2 LEU A 140 8.371 107.093 252.124 1.00 51.80 C
ANISOU 1118 CD2 LEU A 140 6184 8750 4745 68 1453 900 C
ATOM 1119 N ALA A 141 5.801 105.290 247.986 1.00 54.76 N
ANISOU 1119 N ALA A 141 6176 9194 5437 -157 1233 1140 N
ATOM 1120 CA ALA A 141 5.268 105.708 246.695 1.00 55.25 C
ANISOU 1120 CA ALA A 141 6127 9267 5599 -150 1168 1166 C
ATOM 1121 C ALA A 141 3.731 105.652 246.588 1.00 57.12 C
ANISOU 1121 C ALA A 141 6190 9602 5912 -176 1219 1238 C
ATOM 1122 O ALA A 141 3.149 106.118 245.599 1.00 57.34 O
ANISOU 1122 O ALA A 141 6107 9653 6026 -158 1172 1265 O
ATOM 1123 CB ALA A 141 5.915 104.903 245.598 1.00 54.30 C
ANISOU 1123 CB ALA A 141 6065 9088 5478 -226 1037 1176 C
ATOM 1124 N GLU A 142 3.094 105.076 247.608 1.00 58.71 N
ANISOU 1124 N GLU A 142 6365 9864 6079 -222 1313 1273 N
ATOM 1125 CA GLU A 142 1.636 105.050 247.778 1.00 60.76 C
ANISOU 1125 CA GLU A 142 6453 10232 6401 -243 1389 1340 C
ATOM 1126 C GLU A 142 0.807 106.214 247.149 1.00 60.96 C
ANISOU 1126 C GLU A 142 6321 10309 6532 -146 1402 1349 C
ATOM 1127 O GLU A 142 0.735 107.332 247.696 1.00 61.05 O
ANISOU 1127 O GLU A 142 6318 10330 6550 -20 1488 1305 O
ATOM 1128 CB GLU A 142 1.335 104.916 249.273 1.00 62.14 C
ANISOU 1128 CB GLU A 142 6647 10459 6506 -235 1530 1341 C
ATOM 1129 CG GLU A 142 -0.146 105.011 249.636 1.00 67.34 C
ANISOU 1129 CG GLU A 142 7122 11241 7221 -240 1637 1404 C
ATOM 1130 CD GLU A 142 -1.017 103.992 248.892 1.00 71.04 C
ANISOU 1130 CD GLU A 142 7476 11764 7752 -380 1576 1495 C
ATOM 1131 OE1 GLU A 142 -0.448 103.132 248.172 1.00 71.00 O
ANISOU 1131 OE1 GLU A 142 7553 11691 7734 -476 1455 1506 O
ATOM 1132 OE2 GLU A 142 -2.266 104.048 249.047 1.00 73.43 O
ANISOU 1132 OE2 GLU A 142 7606 12178 8115 -393 1650 1554 O
ATOM 1133 N GLY A 143 0.185 105.928 246.001 1.00 60.73 N
ANISOU 1133 N GLY A 143 6182 10311 6582 -204 1313 1406 N
ATOM 1134 CA GLY A 143 -0.696 106.873 245.318 1.00 60.94 C
ANISOU 1134 CA GLY A 143 6047 10396 6713 -125 1310 1432 C
ATOM 1135 C GLY A 143 -0.009 108.165 244.918 1.00 60.13 C
ANISOU 1135 C GLY A 143 5998 10220 6628 12 1286 1368 C
ATOM 1136 O GLY A 143 -0.579 109.258 245.082 1.00 60.92 O
ANISOU 1136 O GLY A 143 6009 10354 6784 132 1355 1362 O
ATOM 1137 N LYS A 144 1.218 108.026 244.402 1.00 58.10 N
ANISOU 1137 N LYS A 144 5890 9862 6325 -8 1192 1323 N
ATOM 1138 CA LYS A 144 2.039 109.138 243.908 1.00 56.69 C
ANISOU 1138 CA LYS A 144 5782 9602 6157 95 1153 1265 C
ATOM 1139 C LYS A 144 2.524 108.904 242.479 1.00 55.59 C
ANISOU 1139 C LYS A 144 5668 9415 6037 46 1007 1279 C
ATOM 1140 O LYS A 144 2.973 107.810 242.137 1.00 55.13 O
ANISOU 1140 O LYS A 144 5678 9335 5936 -63 935 1289 O
ATOM 1141 CB LYS A 144 3.237 109.363 244.817 1.00 55.43 C
ANISOU 1141 CB LYS A 144 5790 9365 5906 133 1195 1183 C
ATOM 1142 CG LYS A 144 3.076 110.571 245.673 1.00 56.72 C
ANISOU 1142 CG LYS A 144 5947 9528 6075 263 1307 1135 C
ATOM 1143 CD LYS A 144 3.689 110.397 247.042 1.00 57.11 C
ANISOU 1143 CD LYS A 144 6117 9559 6023 267 1392 1077 C
ATOM 1144 CE LYS A 144 2.890 111.219 248.028 1.00 59.13 C
ANISOU 1144 CE LYS A 144 6309 9866 6290 368 1533 1060 C
ATOM 1145 NZ LYS A 144 3.748 111.772 249.083 1.00 59.87 N
ANISOU 1145 NZ LYS A 144 6545 9905 6298 428 1596 971 N
ATOM 1146 N SER A 145 2.439 109.928 241.639 1.00 55.09 N
ANISOU 1146 N SER A 145 5560 9334 6036 128 965 1281 N
ATOM 1147 CA SER A 145 2.914 109.794 240.270 1.00 53.63 C
ANISOU 1147 CA SER A 145 5406 9108 5864 88 833 1294 C
ATOM 1148 C SER A 145 4.408 109.499 240.254 1.00 51.71 C
ANISOU 1148 C SER A 145 5341 8770 5538 60 789 1230 C
ATOM 1149 O SER A 145 4.860 108.621 239.517 1.00 51.55 O
ANISOU 1149 O SER A 145 5372 8727 5487 -30 697 1239 O
ATOM 1150 CB SER A 145 2.596 111.037 239.445 1.00 53.90 C
ANISOU 1150 CB SER A 145 5371 9135 5973 190 803 1310 C
ATOM 1151 OG SER A 145 2.761 112.215 240.210 1.00 55.37 O
ANISOU 1151 OG SER A 145 5583 9286 6170 317 896 1262 O
ATOM 1152 N PHE A 146 5.178 110.188 241.091 1.00 50.10 N
ANISOU 1152 N PHE A 146 5230 8512 5295 134 855 1163 N
ATOM 1153 CA PHE A 146 6.626 110.012 241.041 1.00 47.48 C
ANISOU 1153 CA PHE A 146 5052 8097 4891 115 810 1103 C
ATOM 1154 C PHE A 146 7.281 109.778 242.428 1.00 46.46 C
ANISOU 1154 C PHE A 146 5024 7947 4682 119 888 1047 C
ATOM 1155 O PHE A 146 6.897 110.409 243.423 1.00 46.67 O
ANISOU 1155 O PHE A 146 5031 7994 4709 187 988 1026 O
ATOM 1156 CB PHE A 146 7.269 111.199 240.292 1.00 46.92 C
ANISOU 1156 CB PHE A 146 5017 7962 4848 191 770 1074 C
ATOM 1157 CG PHE A 146 8.767 111.122 240.234 1.00 45.90 C
ANISOU 1157 CG PHE A 146 5031 7758 4651 174 728 1013 C
ATOM 1158 CD1 PHE A 146 9.545 111.478 241.355 1.00 43.23 C
ANISOU 1158 CD1 PHE A 146 4785 7381 4258 212 793 945 C
ATOM 1159 CD2 PHE A 146 9.412 110.655 239.072 1.00 43.82 C
ANISOU 1159 CD2 PHE A 146 4809 7467 4373 118 625 1023 C
ATOM 1160 CE1 PHE A 146 10.933 111.366 241.326 1.00 41.92 C
ANISOU 1160 CE1 PHE A 146 4738 7158 4032 193 751 893 C
ATOM 1161 CE2 PHE A 146 10.797 110.543 239.038 1.00 41.16 C
ANISOU 1161 CE2 PHE A 146 4591 7071 3975 105 593 969 C
ATOM 1162 CZ PHE A 146 11.566 110.907 240.172 1.00 40.61 C
ANISOU 1162 CZ PHE A 146 4602 6970 3859 142 654 905 C
ATOM 1163 N CYS A 147 8.279 108.889 242.481 1.00 44.62 N
ANISOU 1163 N CYS A 147 4901 7675 4376 54 840 1023 N
ATOM 1164 CA CYS A 147 8.987 108.597 243.740 1.00 43.77 C
ANISOU 1164 CA CYS A 147 4897 7549 4186 55 896 975 C
ATOM 1165 C CYS A 147 10.414 108.048 243.599 1.00 41.98 C
ANISOU 1165 C CYS A 147 4801 7260 3889 20 828 933 C
ATOM 1166 O CYS A 147 10.590 106.874 243.250 1.00 41.52 O
ANISOU 1166 O CYS A 147 4773 7198 3804 -58 771 959 O
ATOM 1167 CB CYS A 147 8.162 107.632 244.610 1.00 44.89 C
ANISOU 1167 CB CYS A 147 5003 7751 4301 -4 959 1017 C
ATOM 1168 SG CYS A 147 8.939 107.209 246.226 1.00 45.14 S
ANISOU 1168 SG CYS A 147 5164 7769 4218 -5 1029 969 S
ATOM 1169 N VAL A 148 11.416 108.881 243.905 1.00 40.80 N
ANISOU 1169 N VAL A 148 4729 7063 3710 80 834 867 N
ATOM 1170 CA VAL A 148 12.825 108.432 243.985 1.00 39.68 C
ANISOU 1170 CA VAL A 148 4704 6874 3498 58 781 823 C
ATOM 1171 C VAL A 148 13.502 108.686 245.343 1.00 39.94 C
ANISOU 1171 C VAL A 148 4821 6897 3457 91 838 764 C
ATOM 1172 O VAL A 148 13.423 109.795 245.909 1.00 40.36 O
ANISOU 1172 O VAL A 148 4874 6944 3518 156 897 724 O
ATOM 1173 CB VAL A 148 13.713 108.973 242.802 1.00 38.70 C
ANISOU 1173 CB VAL A 148 4603 6702 3399 71 701 800 C
ATOM 1174 CG1 VAL A 148 15.235 108.803 243.080 1.00 37.07 C
ANISOU 1174 CG1 VAL A 148 4506 6456 3123 69 665 743 C
ATOM 1175 CG2 VAL A 148 13.369 108.249 241.499 1.00 38.69 C
ANISOU 1175 CG2 VAL A 148 4558 6709 3432 14 624 852 C
ATOM 1176 N VAL A 149 14.163 107.654 245.863 1.00 39.57 N
ANISOU 1176 N VAL A 149 4853 6846 3336 48 816 760 N
ATOM 1177 CA VAL A 149 14.948 107.803 247.082 1.00 40.21 C
ANISOU 1177 CA VAL A 149 5023 6920 3335 74 849 707 C
ATOM 1178 C VAL A 149 16.424 108.060 246.735 1.00 40.36 C
ANISOU 1178 C VAL A 149 5116 6894 3327 86 778 653 C
ATOM 1179 O VAL A 149 17.053 107.272 246.047 1.00 39.67 O
ANISOU 1179 O VAL A 149 5053 6789 3230 51 704 667 O
ATOM 1180 CB VAL A 149 14.820 106.573 248.008 1.00 39.98 C
ANISOU 1180 CB VAL A 149 5041 6916 3232 28 872 738 C
ATOM 1181 CG1 VAL A 149 15.632 106.751 249.279 1.00 39.30 C
ANISOU 1181 CG1 VAL A 149 5050 6829 3053 57 900 685 C
ATOM 1182 CG2 VAL A 149 13.387 106.346 248.363 1.00 41.67 C
ANISOU 1182 CG2 VAL A 149 5177 7182 3474 8 949 793 C
ATOM 1183 N GLY A 150 16.980 109.157 247.232 1.00 41.41 N
ANISOU 1183 N GLY A 150 5281 7008 3444 135 801 591 N
ATOM 1184 CA GLY A 150 18.374 109.448 246.997 1.00 41.97 C
ANISOU 1184 CA GLY A 150 5412 7046 3489 139 738 540 C
ATOM 1185 C GLY A 150 19.327 108.596 247.798 1.00 42.83 C
ANISOU 1185 C GLY A 150 5602 7163 3506 121 709 522 C
ATOM 1186 O GLY A 150 20.348 108.176 247.281 1.00 42.17 O
ANISOU 1186 O GLY A 150 5548 7066 3410 106 637 513 O
ATOM 1187 N CYS A 151 18.998 108.363 249.068 1.00 44.83 N
ANISOU 1187 N CYS A 151 5894 7444 3696 127 766 518 N
ATOM 1188 CA CYS A 151 19.945 107.807 250.040 1.00 46.68 C
ANISOU 1188 CA CYS A 151 6216 7689 3833 122 743 493 C
ATOM 1189 C CYS A 151 19.211 107.096 251.147 1.00 47.59 C
ANISOU 1189 C CYS A 151 6358 7840 3885 110 805 527 C
ATOM 1190 O CYS A 151 18.137 107.535 251.547 1.00 48.97 O
ANISOU 1190 O CYS A 151 6494 8036 4077 123 888 536 O
ATOM 1191 CB CYS A 151 20.784 108.918 250.685 1.00 47.22 C
ANISOU 1191 CB CYS A 151 6330 7748 3863 155 744 412 C
ATOM 1192 SG CYS A 151 22.499 108.433 251.168 1.00 51.24 S
ANISOU 1192 SG CYS A 151 6921 8263 4284 147 657 374 S
ATOM 1193 N VAL A 152 19.784 105.997 251.635 1.00 47.57 N
ANISOU 1193 N VAL A 152 6422 7844 3809 88 767 549 N
ATOM 1194 CA VAL A 152 19.276 105.324 252.822 1.00 48.08 C
ANISOU 1194 CA VAL A 152 6533 7941 3795 74 823 581 C
ATOM 1195 C VAL A 152 20.443 105.132 253.825 1.00 48.23 C
ANISOU 1195 C VAL A 152 6651 7968 3705 90 784 544 C
ATOM 1196 O VAL A 152 21.290 104.226 253.715 1.00 47.78 O
ANISOU 1196 O VAL A 152 6642 7898 3615 81 710 564 O
ATOM 1197 CB VAL A 152 18.523 104.023 252.480 1.00 48.02 C
ANISOU 1197 CB VAL A 152 6508 7932 3804 21 823 666 C
ATOM 1198 CG1 VAL A 152 18.039 103.353 253.749 1.00 50.36 C
ANISOU 1198 CG1 VAL A 152 6858 8261 4013 1 885 704 C
ATOM 1199 CG2 VAL A 152 17.334 104.323 251.634 1.00 47.75 C
ANISOU 1199 CG2 VAL A 152 6369 7904 3869 4 861 698 C
ATOM 1200 N ALA A 153 20.478 106.035 254.789 1.00 48.23 N
ANISOU 1200 N ALA A 153 6683 7990 3652 119 834 488 N
ATOM 1201 CA ALA A 153 21.638 106.203 255.626 1.00 48.07 C
ANISOU 1201 CA ALA A 153 6745 7981 3539 137 788 436 C
ATOM 1202 C ALA A 153 21.330 105.853 257.092 1.00 48.80 C
ANISOU 1202 C ALA A 153 6913 8115 3512 137 846 447 C
ATOM 1203 O ALA A 153 20.684 106.622 257.807 1.00 49.53 O
ANISOU 1203 O ALA A 153 7012 8230 3577 154 932 413 O
ATOM 1204 CB ALA A 153 22.156 107.638 255.485 1.00 47.77 C
ANISOU 1204 CB ALA A 153 6695 7927 3528 164 781 349 C
ATOM 1205 N PRO A 154 21.762 104.670 257.537 1.00 48.59 N
ANISOU 1205 N PRO A 154 6950 8099 3414 120 802 497 N
ATOM 1206 CA PRO A 154 21.639 104.332 258.959 1.00 49.48 C
ANISOU 1206 CA PRO A 154 7149 8252 3398 120 844 509 C
ATOM 1207 C PRO A 154 22.735 105.042 259.761 1.00 49.55 C
ANISOU 1207 C PRO A 154 7226 8281 3319 148 799 428 C
ATOM 1208 O PRO A 154 23.753 105.404 259.180 1.00 49.27 O
ANISOU 1208 O PRO A 154 7174 8228 3320 160 714 385 O
ATOM 1209 CB PRO A 154 21.869 102.816 258.976 1.00 49.78 C
ANISOU 1209 CB PRO A 154 7234 8279 3402 94 793 593 C
ATOM 1210 CG PRO A 154 21.870 102.363 257.521 1.00 48.32 C
ANISOU 1210 CG PRO A 154 6979 8046 3335 78 741 625 C
ATOM 1211 CD PRO A 154 22.289 103.552 256.736 1.00 47.98 C
ANISOU 1211 CD PRO A 154 6871 7990 3369 103 717 550 C
ATOM 1212 N ALA A 155 22.556 105.236 261.064 1.00 50.02 N
ANISOU 1212 N ALA A 155 7361 8383 3262 155 852 409 N
ATOM 1213 CA ALA A 155 23.578 105.959 261.850 1.00 50.53 C
ANISOU 1213 CA ALA A 155 7493 8470 3237 175 803 326 C
ATOM 1214 C ALA A 155 24.584 105.059 262.574 1.00 50.87 C
ANISOU 1214 C ALA A 155 7621 8541 3166 175 713 354 C
ATOM 1215 O ALA A 155 24.190 104.351 263.510 1.00 52.43 O
ANISOU 1215 O ALA A 155 7889 8770 3263 168 752 406 O
ATOM 1216 CB ALA A 155 22.939 106.950 262.838 1.00 51.08 C
ANISOU 1216 CB ALA A 155 7602 8566 3238 190 904 262 C
ATOM 1217 N PRO A 156 25.877 105.099 262.150 1.00 50.19 N
ANISOU 1217 N PRO A 156 7526 8447 3097 185 596 324 N
ATOM 1218 CA PRO A 156 27.015 104.418 262.734 1.00 50.49 C
ANISOU 1218 CA PRO A 156 7628 8515 3040 197 493 340 C
ATOM 1219 C PRO A 156 26.968 104.086 264.230 1.00 51.61 C
ANISOU 1219 C PRO A 156 7882 8709 3019 199 510 354 C
ATOM 1220 O PRO A 156 26.236 104.711 265.012 1.00 52.86 O
ANISOU 1220 O PRO A 156 8079 8889 3115 193 602 319 O
ATOM 1221 CB PRO A 156 28.165 105.344 262.374 1.00 50.81 C
ANISOU 1221 CB PRO A 156 7634 8560 3112 203 409 254 C
ATOM 1222 CG PRO A 156 27.842 105.725 260.959 1.00 48.88 C
ANISOU 1222 CG PRO A 156 7287 8264 3021 196 428 249 C
ATOM 1223 CD PRO A 156 26.305 105.763 260.897 1.00 49.40 C
ANISOU 1223 CD PRO A 156 7337 8310 3125 186 553 282 C
ATOM 1224 N PRO A 157 27.845 103.163 264.640 1.00 51.53 N
ANISOU 1224 N PRO A 157 7927 8720 2934 214 416 400 N
ATOM 1225 CA PRO A 157 27.565 101.993 265.419 1.00 51.48 C
ANISOU 1225 CA PRO A 157 8005 8727 2828 215 425 492 C
ATOM 1226 C PRO A 157 26.165 101.400 265.238 1.00 50.58 C
ANISOU 1226 C PRO A 157 7882 8583 2752 186 540 568 C
ATOM 1227 O PRO A 157 26.023 100.376 264.602 1.00 49.25 O
ANISOU 1227 O PRO A 157 7699 8372 2643 180 520 646 O
ATOM 1228 CB PRO A 157 27.824 102.487 266.854 1.00 52.90 C
ANISOU 1228 CB PRO A 157 8282 8972 2846 218 428 446 C
ATOM 1229 CG PRO A 157 28.979 103.451 266.695 1.00 52.56 C
ANISOU 1229 CG PRO A 157 8207 8948 2815 228 334 346 C
ATOM 1230 CD PRO A 157 29.062 103.793 265.183 1.00 52.65 C
ANISOU 1230 CD PRO A 157 8096 8905 3003 226 322 326 C
ATOM 1231 N GLU A 158 25.147 102.032 265.799 1.00 50.88 N
ANISOU 1231 N GLU A 158 7930 8645 2757 168 659 544 N
ATOM 1232 CA GLU A 158 23.949 101.287 266.159 1.00 51.35 C
ANISOU 1232 CA GLU A 158 8014 8706 2789 138 762 630 C
ATOM 1233 C GLU A 158 23.029 100.883 265.034 1.00 49.58 C
ANISOU 1233 C GLU A 158 7698 8433 2708 109 812 684 C
ATOM 1234 O GLU A 158 22.591 99.731 265.000 1.00 49.54 O
ANISOU 1234 O GLU A 158 7717 8406 2700 80 823 782 O
ATOM 1235 CB GLU A 158 23.188 102.015 267.252 1.00 52.92 C
ANISOU 1235 CB GLU A 158 8259 8961 2889 133 878 591 C
ATOM 1236 CG GLU A 158 24.086 102.376 268.451 1.00 57.40 C
ANISOU 1236 CG GLU A 158 8933 9580 3295 155 824 537 C
ATOM 1237 CD GLU A 158 24.790 101.161 269.078 1.00 60.80 C
ANISOU 1237 CD GLU A 158 9460 10024 3616 158 736 621 C
ATOM 1238 OE1 GLU A 158 25.817 100.690 268.517 1.00 59.35 O
ANISOU 1238 OE1 GLU A 158 9261 9814 3475 178 610 636 O
ATOM 1239 OE2 GLU A 158 24.304 100.688 270.140 1.00 62.54 O
ANISOU 1239 OE2 GLU A 158 9772 10284 3705 143 797 674 O
ATOM 1240 N HIS A 159 22.762 101.813 264.114 1.00 47.72 N
ANISOU 1240 N HIS A 159 7361 8177 2593 115 835 622 N
ATOM 1241 CA HIS A 159 21.754 101.637 263.048 1.00 46.11 C
ANISOU 1241 CA HIS A 159 7059 7937 2525 87 890 663 C
ATOM 1242 C HIS A 159 20.354 101.623 263.664 1.00 47.19 C
ANISOU 1242 C HIS A 159 7189 8109 2632 58 1031 703 C
ATOM 1243 O HIS A 159 19.453 100.925 263.187 1.00 47.29 O
ANISOU 1243 O HIS A 159 7153 8105 2707 16 1075 779 O
ATOM 1244 CB HIS A 159 21.994 100.366 262.190 1.00 45.23 C
ANISOU 1244 CB HIS A 159 6940 7772 2474 65 816 744 C
ATOM 1245 CG HIS A 159 23.331 100.328 261.516 1.00 41.86 C
ANISOU 1245 CG HIS A 159 6507 7315 2082 100 688 709 C
ATOM 1246 ND1 HIS A 159 23.473 100.335 260.152 1.00 40.58 N
ANISOU 1246 ND1 HIS A 159 6263 7107 2047 99 645 702 N
ATOM 1247 CD2 HIS A 159 24.584 100.323 262.021 1.00 41.54 C
ANISOU 1247 CD2 HIS A 159 6526 7292 1964 136 596 678 C
ATOM 1248 CE1 HIS A 159 24.757 100.346 259.843 1.00 40.94 C
ANISOU 1248 CE1 HIS A 159 6317 7145 2094 135 540 667 C
ATOM 1249 NE2 HIS A 159 25.453 100.340 260.963 1.00 40.60 N
ANISOU 1249 NE2 HIS A 159 6354 7142 1931 158 507 653 N
ATOM 1250 N ALA A 160 20.171 102.389 264.738 1.00 48.06 N
ANISOU 1250 N ALA A 160 7346 8272 2643 78 1101 650 N
ATOM 1251 CA ALA A 160 18.841 102.552 265.321 1.00 48.82 C
ANISOU 1251 CA ALA A 160 7424 8413 2714 62 1248 674 C
ATOM 1252 C ALA A 160 18.100 103.594 264.498 1.00 48.15 C
ANISOU 1252 C ALA A 160 7219 8317 2760 81 1311 623 C
ATOM 1253 O ALA A 160 17.076 103.289 263.874 1.00 48.24 O
ANISOU 1253 O ALA A 160 7139 8325 2864 52 1370 680 O
ATOM 1254 CB ALA A 160 18.920 102.961 266.766 1.00 50.00 C
ANISOU 1254 CB ALA A 160 7676 8622 2701 82 1305 634 C
ATOM 1255 N LEU A 161 18.636 104.812 264.463 1.00 47.49 N
ANISOU 1255 N LEU A 161 7134 8224 2685 128 1292 517 N
ATOM 1256 CA LEU A 161 18.129 105.817 263.526 1.00 46.50 C
ANISOU 1256 CA LEU A 161 6900 8071 2695 153 1326 469 C
ATOM 1257 C LEU A 161 18.555 105.433 262.104 1.00 44.48 C
ANISOU 1257 C LEU A 161 6572 7758 2568 135 1224 499 C
ATOM 1258 O LEU A 161 19.719 105.086 261.865 1.00 42.93 O
ANISOU 1258 O LEU A 161 6418 7537 2357 132 1108 490 O
ATOM 1259 CB LEU A 161 18.648 107.226 263.850 1.00 46.61 C
ANISOU 1259 CB LEU A 161 6947 8076 2686 203 1327 347 C
ATOM 1260 CG LEU A 161 18.586 107.864 265.240 1.00 48.98 C
ANISOU 1260 CG LEU A 161 7343 8421 2845 231 1402 280 C
ATOM 1261 CD1 LEU A 161 19.272 109.247 265.276 1.00 49.70 C
ANISOU 1261 CD1 LEU A 161 7465 8478 2939 269 1371 154 C
ATOM 1262 CD2 LEU A 161 17.154 107.999 265.710 1.00 52.37 C
ANISOU 1262 CD2 LEU A 161 7735 8895 3267 245 1562 304 C
ATOM 1263 N VAL A 162 17.603 105.470 261.177 1.00 43.71 N
ANISOU 1263 N VAL A 162 6366 7649 2594 124 1267 535 N
ATOM 1264 CA VAL A 162 17.937 105.477 259.755 1.00 42.42 C
ANISOU 1264 CA VAL A 162 6128 7432 2557 117 1183 540 C
ATOM 1265 C VAL A 162 17.223 106.632 259.040 1.00 42.61 C
ANISOU 1265 C VAL A 162 6052 7444 2693 150 1237 500 C
ATOM 1266 O VAL A 162 15.998 106.823 259.168 1.00 43.67 O
ANISOU 1266 O VAL A 162 6123 7610 2859 155 1341 526 O
ATOM 1267 CB VAL A 162 17.741 104.126 259.046 1.00 41.38 C
ANISOU 1267 CB VAL A 162 5971 7281 2470 63 1136 636 C
ATOM 1268 CG1 VAL A 162 16.669 103.316 259.692 1.00 43.39 C
ANISOU 1268 CG1 VAL A 162 6227 7575 2683 20 1225 716 C
ATOM 1269 CG2 VAL A 162 17.403 104.347 257.611 1.00 40.85 C
ANISOU 1269 CG2 VAL A 162 5798 7179 2545 56 1107 645 C
ATOM 1270 N ALA A 163 18.019 107.420 258.320 1.00 41.38 N
ANISOU 1270 N ALA A 163 5885 7244 2595 175 1165 438 N
ATOM 1271 CA ALA A 163 17.506 108.538 257.571 1.00 40.57 C
ANISOU 1271 CA ALA A 163 5700 7116 2598 210 1199 402 C
ATOM 1272 C ALA A 163 17.438 108.165 256.095 1.00 39.55 C
ANISOU 1272 C ALA A 163 5486 6954 2586 184 1133 452 C
ATOM 1273 O ALA A 163 18.131 107.229 255.645 1.00 39.10 O
ANISOU 1273 O ALA A 163 5451 6883 2524 148 1046 487 O
ATOM 1274 CB ALA A 163 18.390 109.723 257.783 1.00 40.02 C
ANISOU 1274 CB ALA A 163 5681 7015 2508 247 1170 303 C
ATOM 1275 N TYR A 164 16.596 108.886 255.348 1.00 39.04 N
ANISOU 1275 N TYR A 164 5328 6879 2625 208 1174 455 N
ATOM 1276 CA TYR A 164 16.474 108.721 253.880 1.00 38.18 C
ANISOU 1276 CA TYR A 164 5137 6741 2630 188 1112 495 C
ATOM 1277 C TYR A 164 16.028 110.045 253.211 1.00 38.19 C
ANISOU 1277 C TYR A 164 5069 6714 2726 239 1140 461 C
ATOM 1278 O TYR A 164 15.592 111.001 253.893 1.00 38.96 O
ANISOU 1278 O TYR A 164 5173 6817 2812 291 1222 414 O
ATOM 1279 CB TYR A 164 15.503 107.576 253.525 1.00 38.32 C
ANISOU 1279 CB TYR A 164 5093 6789 2679 137 1128 589 C
ATOM 1280 CG TYR A 164 14.076 107.913 253.837 1.00 39.26 C
ANISOU 1280 CG TYR A 164 5130 6954 2833 154 1240 617 C
ATOM 1281 CD1 TYR A 164 13.627 107.950 255.157 1.00 40.30 C
ANISOU 1281 CD1 TYR A 164 5298 7132 2882 169 1339 607 C
ATOM 1282 CD2 TYR A 164 13.174 108.240 252.820 1.00 39.21 C
ANISOU 1282 CD2 TYR A 164 5007 6951 2941 160 1248 652 C
ATOM 1283 CE1 TYR A 164 12.316 108.280 255.472 1.00 41.29 C
ANISOU 1283 CE1 TYR A 164 5341 7308 3038 192 1451 632 C
ATOM 1284 CE2 TYR A 164 11.836 108.582 253.131 1.00 40.22 C
ANISOU 1284 CE2 TYR A 164 5045 7131 3105 184 1354 679 C
ATOM 1285 CZ TYR A 164 11.424 108.598 254.459 1.00 41.25 C
ANISOU 1285 CZ TYR A 164 5210 7310 3155 201 1459 667 C
ATOM 1286 OH TYR A 164 10.123 108.933 254.790 1.00 42.73 O
ANISOU 1286 OH TYR A 164 5303 7557 3377 231 1572 693 O
ATOM 1287 N SER A 165 16.147 110.115 251.893 1.00 37.42 N
ANISOU 1287 N SER A 165 4914 6585 2718 227 1074 483 N
ATOM 1288 CA SER A 165 15.817 111.341 251.200 1.00 37.43 C
ANISOU 1288 CA SER A 165 4861 6553 2807 275 1088 458 C
ATOM 1289 C SER A 165 14.941 110.993 250.027 1.00 37.21 C
ANISOU 1289 C SER A 165 4727 6536 2875 256 1070 532 C
ATOM 1290 O SER A 165 15.137 109.955 249.377 1.00 36.63 O
ANISOU 1290 O SER A 165 4644 6468 2807 199 1004 580 O
ATOM 1291 CB SER A 165 17.078 112.102 250.743 1.00 36.79 C
ANISOU 1291 CB SER A 165 4831 6414 2733 283 1015 397 C
ATOM 1292 OG SER A 165 17.907 111.341 249.867 1.00 35.86 O
ANISOU 1292 OG SER A 165 4718 6286 2622 235 917 423 O
ATOM 1293 N VAL A 166 13.976 111.852 249.745 1.00 37.75 N
ANISOU 1293 N VAL A 166 4718 6607 3019 306 1125 540 N
ATOM 1294 CA VAL A 166 12.999 111.493 248.734 1.00 37.76 C
ANISOU 1294 CA VAL A 166 4608 6633 3106 287 1111 615 C
ATOM 1295 C VAL A 166 12.618 112.685 247.819 1.00 37.85 C
ANISOU 1295 C VAL A 166 4554 6611 3215 345 1106 613 C
ATOM 1296 O VAL A 166 12.466 113.820 248.280 1.00 38.43 O
ANISOU 1296 O VAL A 166 4640 6660 3302 418 1166 565 O
ATOM 1297 CB VAL A 166 11.793 110.777 249.407 1.00 38.65 C
ANISOU 1297 CB VAL A 166 4659 6820 3208 268 1192 669 C
ATOM 1298 CG1 VAL A 166 11.142 111.676 250.461 1.00 39.75 C
ANISOU 1298 CG1 VAL A 166 4789 6981 3333 343 1311 631 C
ATOM 1299 CG2 VAL A 166 10.791 110.281 248.399 1.00 38.76 C
ANISOU 1299 CG2 VAL A 166 4553 6868 3305 232 1167 750 C
ATOM 1300 N ASP A 167 12.539 112.424 246.522 1.00 37.31 N
ANISOU 1300 N ASP A 167 4431 6535 3209 314 1029 662 N
ATOM 1301 CA ASP A 167 12.067 113.416 245.576 1.00 37.73 C
ANISOU 1301 CA ASP A 167 4418 6564 3355 365 1017 678 C
ATOM 1302 C ASP A 167 10.745 112.919 245.040 1.00 38.55 C
ANISOU 1302 C ASP A 167 4395 6730 3521 350 1024 759 C
ATOM 1303 O ASP A 167 10.670 111.792 244.563 1.00 38.01 O
ANISOU 1303 O ASP A 167 4307 6692 3444 272 970 806 O
ATOM 1304 CB ASP A 167 13.056 113.597 244.398 1.00 36.91 C
ANISOU 1304 CB ASP A 167 4349 6406 3268 340 915 673 C
ATOM 1305 CG ASP A 167 12.590 114.664 243.372 1.00 37.25 C
ANISOU 1305 CG ASP A 167 4333 6419 3403 392 898 698 C
ATOM 1306 OD1 ASP A 167 11.732 115.530 243.682 1.00 41.94 O
ANISOU 1306 OD1 ASP A 167 4877 7012 4046 467 966 699 O
ATOM 1307 OD2 ASP A 167 13.106 114.665 242.246 1.00 36.42 O
ANISOU 1307 OD2 ASP A 167 4233 6287 3318 364 817 717 O
ATOM 1308 N TYR A 168 9.724 113.773 245.076 1.00 40.35 N
ANISOU 1308 N TYR A 168 4540 6976 3817 424 1087 775 N
ATOM 1309 CA TYR A 168 8.379 113.382 244.644 1.00 42.11 C
ANISOU 1309 CA TYR A 168 4624 7272 4105 415 1099 854 C
ATOM 1310 C TYR A 168 7.964 113.906 243.285 1.00 43.06 C
ANISOU 1310 C TYR A 168 4665 7382 4315 438 1031 902 C
ATOM 1311 O TYR A 168 6.902 113.532 242.805 1.00 43.83 O
ANISOU 1311 O TYR A 168 4642 7545 4467 421 1022 971 O
ATOM 1312 CB TYR A 168 7.330 113.771 245.684 1.00 42.89 C
ANISOU 1312 CB TYR A 168 4656 7424 4216 481 1223 853 C
ATOM 1313 CG TYR A 168 7.371 112.887 246.881 1.00 43.94 C
ANISOU 1313 CG TYR A 168 4834 7600 4263 431 1286 841 C
ATOM 1314 CD1 TYR A 168 7.078 111.535 246.752 1.00 46.13 C
ANISOU 1314 CD1 TYR A 168 5078 7930 4520 329 1254 900 C
ATOM 1315 CD2 TYR A 168 7.738 113.378 248.155 1.00 43.77 C
ANISOU 1315 CD2 TYR A 168 4898 7561 4171 482 1373 769 C
ATOM 1316 CE1 TYR A 168 7.111 110.666 247.878 1.00 48.16 C
ANISOU 1316 CE1 TYR A 168 5383 8223 4692 279 1312 898 C
ATOM 1317 CE2 TYR A 168 7.766 112.522 249.294 1.00 44.75 C
ANISOU 1317 CE2 TYR A 168 5069 7730 4205 435 1431 764 C
ATOM 1318 CZ TYR A 168 7.446 111.158 249.141 1.00 46.63 C
ANISOU 1318 CZ TYR A 168 5271 8020 4427 333 1401 834 C
ATOM 1319 OH TYR A 168 7.448 110.244 250.190 1.00 45.71 O
ANISOU 1319 OH TYR A 168 5203 7944 4222 278 1452 843 O
ATOM 1320 N CYS A 169 8.764 114.777 242.669 1.00 43.71 N
ANISOU 1320 N CYS A 169 4809 7387 4411 474 983 870 N
ATOM 1321 CA CYS A 169 8.415 115.255 241.326 1.00 44.94 C
ANISOU 1321 CA CYS A 169 4899 7532 4643 493 912 922 C
ATOM 1322 C CYS A 169 9.531 115.081 240.309 1.00 43.69 C
ANISOU 1322 C CYS A 169 4819 7323 4461 437 809 916 C
ATOM 1323 O CYS A 169 9.305 115.181 239.089 1.00 43.60 O
ANISOU 1323 O CYS A 169 4760 7313 4493 428 735 967 O
ATOM 1324 CB CYS A 169 7.888 116.700 241.343 1.00 46.36 C
ANISOU 1324 CB CYS A 169 5045 7676 4894 613 963 917 C
ATOM 1325 SG CYS A 169 9.086 117.909 241.847 1.00 48.00 S
ANISOU 1325 SG CYS A 169 5398 7768 5071 670 991 823 S
ATOM 1326 N GLY A 170 10.736 114.838 240.811 1.00 42.88 N
ANISOU 1326 N GLY A 170 4830 7179 4284 403 804 854 N
ATOM 1327 CA GLY A 170 11.873 114.558 239.928 1.00 41.97 C
ANISOU 1327 CA GLY A 170 4785 7025 4137 347 715 845 C
ATOM 1328 C GLY A 170 12.733 115.743 239.533 1.00 41.54 C
ANISOU 1328 C GLY A 170 4795 6892 4095 388 698 809 C
ATOM 1329 O GLY A 170 13.581 115.608 238.677 1.00 41.57 O
ANISOU 1329 O GLY A 170 4841 6873 4082 346 628 810 O
ATOM 1330 N ASP A 171 12.513 116.903 240.139 1.00 41.90 N
ANISOU 1330 N ASP A 171 4852 6897 4172 467 763 777 N
ATOM 1331 CA ASP A 171 13.325 118.068 239.858 1.00 41.59 C
ANISOU 1331 CA ASP A 171 4884 6773 4146 499 751 740 C
ATOM 1332 C ASP A 171 14.611 117.948 240.656 1.00 40.74 C
ANISOU 1332 C ASP A 171 4882 6636 3962 461 757 662 C
ATOM 1333 O ASP A 171 15.508 118.815 240.590 1.00 40.18 O
ANISOU 1333 O ASP A 171 4884 6495 3887 466 747 619 O
ATOM 1334 CB ASP A 171 12.578 119.335 240.215 1.00 43.12 C
ANISOU 1334 CB ASP A 171 5057 6923 4402 600 818 734 C
ATOM 1335 CG ASP A 171 12.344 119.475 241.688 1.00 46.25 C
ANISOU 1335 CG ASP A 171 5480 7326 4767 641 914 673 C
ATOM 1336 OD1 ASP A 171 12.369 118.466 242.437 1.00 48.95 O
ANISOU 1336 OD1 ASP A 171 5822 7727 5048 596 935 659 O
ATOM 1337 OD2 ASP A 171 12.124 120.624 242.109 1.00 50.85 O
ANISOU 1337 OD2 ASP A 171 6089 7848 5383 723 970 638 O
ATOM 1338 N GLU A 172 14.675 116.845 241.401 1.00 39.59 N
ANISOU 1338 N GLU A 172 4742 6544 3755 418 771 649 N
ATOM 1339 CA GLU A 172 15.872 116.428 242.118 1.00 38.77 C
ANISOU 1339 CA GLU A 172 4727 6433 3571 375 762 587 C
ATOM 1340 C GLU A 172 16.266 117.275 243.327 1.00 38.66 C
ANISOU 1340 C GLU A 172 4786 6378 3524 414 824 509 C
ATOM 1341 O GLU A 172 17.440 117.367 243.663 1.00 38.28 O
ANISOU 1341 O GLU A 172 4816 6304 3425 383 799 454 O
ATOM 1342 CB GLU A 172 17.037 116.221 241.157 1.00 37.93 C
ANISOU 1342 CB GLU A 172 4658 6306 3447 320 679 587 C
ATOM 1343 CG GLU A 172 16.960 114.853 240.514 1.00 38.59 C
ANISOU 1343 CG GLU A 172 4709 6443 3510 263 625 635 C
ATOM 1344 CD GLU A 172 17.977 114.643 239.407 1.00 38.14 C
ANISOU 1344 CD GLU A 172 4679 6373 3441 218 549 641 C
ATOM 1345 OE1 GLU A 172 19.204 114.576 239.720 1.00 36.46 O
ANISOU 1345 OE1 GLU A 172 4530 6146 3178 195 531 592 O
ATOM 1346 OE2 GLU A 172 17.511 114.516 238.243 1.00 36.52 O
ANISOU 1346 OE2 GLU A 172 4425 6177 3272 207 507 697 O
ATOM 1347 N VAL A 173 15.266 117.873 243.967 1.00 38.86 N
ANISOU 1347 N VAL A 173 4783 6402 3580 483 903 503 N
ATOM 1348 CA VAL A 173 15.395 118.488 245.274 1.00 38.80 C
ANISOU 1348 CA VAL A 173 4842 6369 3529 523 976 427 C
ATOM 1349 C VAL A 173 14.786 117.498 246.277 1.00 39.21 C
ANISOU 1349 C VAL A 173 4872 6500 3526 514 1032 435 C
ATOM 1350 O VAL A 173 13.671 116.987 246.061 1.00 38.91 O
ANISOU 1350 O VAL A 173 4741 6518 3526 524 1058 498 O
ATOM 1351 CB VAL A 173 14.631 119.831 245.326 1.00 40.31 C
ANISOU 1351 CB VAL A 173 5022 6505 3790 616 1039 414 C
ATOM 1352 CG1 VAL A 173 14.726 120.493 246.739 1.00 40.64 C
ANISOU 1352 CG1 VAL A 173 5145 6516 3779 663 1122 324 C
ATOM 1353 CG2 VAL A 173 15.090 120.765 244.212 1.00 38.13 C
ANISOU 1353 CG2 VAL A 173 4762 6149 3577 623 982 426 C
ATOM 1354 N TYR A 174 15.510 117.256 247.376 1.00 39.40 N
ANISOU 1354 N TYR A 174 4982 6530 3460 492 1049 373 N
ATOM 1355 CA TYR A 174 15.150 116.202 248.351 1.00 39.59 C
ANISOU 1355 CA TYR A 174 5004 6626 3412 470 1092 383 C
ATOM 1356 C TYR A 174 14.759 116.726 249.738 1.00 41.05 C
ANISOU 1356 C TYR A 174 5235 6817 3544 524 1195 325 C
ATOM 1357 O TYR A 174 15.278 117.748 250.204 1.00 41.70 O
ANISOU 1357 O TYR A 174 5394 6841 3609 557 1212 248 O
ATOM 1358 CB TYR A 174 16.287 115.177 248.471 1.00 38.07 C
ANISOU 1358 CB TYR A 174 4872 6452 3143 394 1020 377 C
ATOM 1359 CG TYR A 174 16.575 114.419 247.172 1.00 37.57 C
ANISOU 1359 CG TYR A 174 4764 6393 3117 341 930 437 C
ATOM 1360 CD1 TYR A 174 17.249 115.031 246.099 1.00 35.46 C
ANISOU 1360 CD1 TYR A 174 4499 6076 2898 335 866 431 C
ATOM 1361 CD2 TYR A 174 16.161 113.075 247.006 1.00 36.61 C
ANISOU 1361 CD2 TYR A 174 4604 6326 2981 294 912 499 C
ATOM 1362 CE1 TYR A 174 17.489 114.332 244.911 1.00 34.72 C
ANISOU 1362 CE1 TYR A 174 4370 5992 2830 290 790 483 C
ATOM 1363 CE2 TYR A 174 16.409 112.376 245.829 1.00 35.02 C
ANISOU 1363 CE2 TYR A 174 4373 6124 2808 247 832 545 C
ATOM 1364 CZ TYR A 174 17.077 113.015 244.807 1.00 34.51 C
ANISOU 1364 CZ TYR A 174 4312 6017 2784 249 774 535 C
ATOM 1365 OH TYR A 174 17.319 112.334 243.657 1.00 35.20 O
ANISOU 1365 OH TYR A 174 4376 6108 2890 206 701 576 O
ATOM 1366 N SER A 175 13.812 116.047 250.385 1.00 41.88 N
ANISOU 1366 N SER A 175 5294 6993 3625 529 1265 360 N
ATOM 1367 CA SER A 175 13.656 116.179 251.838 1.00 42.48 C
ANISOU 1367 CA SER A 175 5431 7093 3614 559 1356 305 C
ATOM 1368 C SER A 175 14.337 115.007 252.518 1.00 41.61 C
ANISOU 1368 C SER A 175 5385 7027 3399 487 1324 309 C
ATOM 1369 O SER A 175 14.452 113.941 251.947 1.00 40.67 O
ANISOU 1369 O SER A 175 5231 6935 3285 426 1263 372 O
ATOM 1370 CB SER A 175 12.188 116.330 252.298 1.00 44.01 C
ANISOU 1370 CB SER A 175 5542 7340 3838 621 1474 333 C
ATOM 1371 OG SER A 175 11.225 116.108 251.274 1.00 44.89 O
ANISOU 1371 OG SER A 175 5523 7482 4053 625 1464 417 O
ATOM 1372 N ILE A 176 14.841 115.215 253.719 1.00 42.55 N
ANISOU 1372 N ILE A 176 5603 7147 3417 496 1359 240 N
ATOM 1373 CA ILE A 176 15.420 114.112 254.458 1.00 42.49 C
ANISOU 1373 CA ILE A 176 5658 7184 3302 438 1333 250 C
ATOM 1374 C ILE A 176 14.539 113.845 255.657 1.00 44.99 C
ANISOU 1374 C ILE A 176 5983 7564 3549 459 1447 255 C
ATOM 1375 O ILE A 176 14.087 114.770 256.338 1.00 46.66 O
ANISOU 1375 O ILE A 176 6216 7769 3744 524 1536 198 O
ATOM 1376 CB ILE A 176 16.835 114.392 254.905 1.00 41.83 C
ANISOU 1376 CB ILE A 176 5687 7065 3142 417 1265 175 C
ATOM 1377 CG1 ILE A 176 17.747 114.648 253.693 1.00 38.81 C
ANISOU 1377 CG1 ILE A 176 5290 6627 2829 391 1158 174 C
ATOM 1378 CG2 ILE A 176 17.355 113.224 255.702 1.00 40.77 C
ANISOU 1378 CG2 ILE A 176 5613 6981 2897 368 1238 194 C
ATOM 1379 CD1 ILE A 176 18.822 115.666 253.973 1.00 38.90 C
ANISOU 1379 CD1 ILE A 176 5385 6583 2811 396 1121 82 C
ATOM 1380 N ARG A 177 14.283 112.569 255.894 1.00 45.76 N
ANISOU 1380 N ARG A 177 6065 7719 3603 405 1446 324 N
ATOM 1381 CA ARG A 177 13.300 112.144 256.848 1.00 47.58 C
ANISOU 1381 CA ARG A 177 6280 8020 3779 411 1557 355 C
ATOM 1382 C ARG A 177 13.877 110.902 257.509 1.00 47.40 C
ANISOU 1382 C ARG A 177 6333 8029 3646 344 1520 388 C
ATOM 1383 O ARG A 177 14.956 110.443 257.139 1.00 46.02 O
ANISOU 1383 O ARG A 177 6209 7823 3455 304 1411 386 O
ATOM 1384 CB ARG A 177 11.971 111.888 256.105 1.00 48.04 C
ANISOU 1384 CB ARG A 177 6193 8115 3944 412 1603 437 C
ATOM 1385 CG ARG A 177 11.182 113.188 255.856 1.00 52.18 C
ANISOU 1385 CG ARG A 177 6648 8624 4554 503 1677 403 C
ATOM 1386 CD ARG A 177 9.913 113.069 254.998 1.00 57.07 C
ANISOU 1386 CD ARG A 177 7110 9282 5292 512 1707 483 C
ATOM 1387 NE ARG A 177 9.586 114.384 254.408 1.00 63.06 N
ANISOU 1387 NE ARG A 177 7820 9993 6146 602 1724 447 N
ATOM 1388 CZ ARG A 177 9.165 114.588 253.143 1.00 65.09 C
ANISOU 1388 CZ ARG A 177 7974 10235 6523 610 1672 497 C
ATOM 1389 NH1 ARG A 177 8.990 113.558 252.301 1.00 63.65 N
ANISOU 1389 NH1 ARG A 177 7722 10083 6379 531 1599 579 N
ATOM 1390 NH2 ARG A 177 8.921 115.834 252.705 1.00 64.38 N
ANISOU 1390 NH2 ARG A 177 7857 10094 6512 699 1689 464 N
ATOM 1391 N PHE A 178 13.179 110.362 258.497 1.00 48.99 N
ANISOU 1391 N PHE A 178 6545 8296 3773 333 1612 420 N
ATOM 1392 CA PHE A 178 13.650 109.154 259.150 1.00 49.70 C
ANISOU 1392 CA PHE A 178 6713 8414 3757 271 1581 462 C
ATOM 1393 C PHE A 178 12.631 108.072 259.074 1.00 50.78 C
ANISOU 1393 C PHE A 178 6778 8603 3915 216 1628 566 C
ATOM 1394 O PHE A 178 11.439 108.343 259.164 1.00 52.39 O
ANISOU 1394 O PHE A 178 6892 8853 4162 236 1732 591 O
ATOM 1395 CB PHE A 178 13.993 109.462 260.597 1.00 50.60 C
ANISOU 1395 CB PHE A 178 6943 8555 3727 297 1637 401 C
ATOM 1396 CG PHE A 178 15.240 110.250 260.724 1.00 50.34 C
ANISOU 1396 CG PHE A 178 7001 8471 3656 323 1561 305 C
ATOM 1397 CD1 PHE A 178 15.216 111.633 260.593 1.00 50.26 C
ANISOU 1397 CD1 PHE A 178 6985 8420 3691 386 1590 219 C
ATOM 1398 CD2 PHE A 178 16.458 109.610 260.882 1.00 50.62 C
ANISOU 1398 CD2 PHE A 178 7121 8493 3621 283 1451 304 C
ATOM 1399 CE1 PHE A 178 16.376 112.373 260.665 1.00 49.30 C
ANISOU 1399 CE1 PHE A 178 6944 8247 3540 397 1515 132 C
ATOM 1400 CE2 PHE A 178 17.635 110.344 260.960 1.00 50.91 C
ANISOU 1400 CE2 PHE A 178 7227 8489 3628 299 1374 217 C
ATOM 1401 CZ PHE A 178 17.592 111.734 260.844 1.00 50.07 C
ANISOU 1401 CZ PHE A 178 7116 8343 3565 350 1405 131 C
ATOM 1402 N VAL A 179 13.097 106.843 258.915 1.00 51.03 N
ANISOU 1402 N VAL A 179 6848 8625 3916 146 1551 627 N
ATOM 1403 CA VAL A 179 12.217 105.679 258.907 1.00 52.69 C
ANISOU 1403 CA VAL A 179 7010 8876 4134 76 1586 730 C
ATOM 1404 C VAL A 179 11.228 105.672 260.091 1.00 55.63 C
ANISOU 1404 C VAL A 179 7377 9326 4434 80 1732 752 C
ATOM 1405 O VAL A 179 11.549 106.159 261.204 1.00 56.25 O
ANISOU 1405 O VAL A 179 7545 9426 4402 122 1786 694 O
ATOM 1406 CB VAL A 179 13.028 104.386 258.913 1.00 51.77 C
ANISOU 1406 CB VAL A 179 6981 8729 3960 11 1491 779 C
ATOM 1407 CG1 VAL A 179 12.105 103.178 258.803 1.00 52.30 C
ANISOU 1407 CG1 VAL A 179 7003 8822 4046 -72 1521 887 C
ATOM 1408 CG2 VAL A 179 14.002 104.402 257.771 1.00 50.46 C
ANISOU 1408 CG2 VAL A 179 6817 8494 3861 14 1359 754 C
ATOM 1409 N ARG A 180 10.025 105.141 259.834 1.00 57.46 N
ANISOU 1409 N ARG A 180 7501 9605 4725 33 1796 834 N
ATOM 1410 CA ARG A 180 8.976 105.005 260.852 1.00 60.36 C
ANISOU 1410 CA ARG A 180 7842 10059 5034 25 1942 871 C
ATOM 1411 C ARG A 180 8.909 106.196 261.814 1.00 61.34 C
ANISOU 1411 C ARG A 180 8002 10214 5090 119 2046 782 C
ATOM 1412 O ARG A 180 8.490 106.034 262.963 1.00 63.07 O
ANISOU 1412 O ARG A 180 8263 10498 5204 117 2155 793 O
ATOM 1413 CB ARG A 180 9.179 103.731 261.680 1.00 61.11 C
ANISOU 1413 CB ARG A 180 8037 10170 5012 -56 1943 941 C
ATOM 1414 CG ARG A 180 8.976 102.400 260.981 1.00 63.35 C
ANISOU 1414 CG ARG A 180 8293 10431 5347 -161 1875 1043 C
ATOM 1415 CD ARG A 180 9.591 101.351 261.889 1.00 68.76 C
ANISOU 1415 CD ARG A 180 9124 11104 5897 -212 1854 1086 C
ATOM 1416 NE ARG A 180 9.471 99.967 261.428 1.00 73.88 N
ANISOU 1416 NE ARG A 180 9783 11717 6570 -316 1793 1185 N
ATOM 1417 CZ ARG A 180 10.383 99.320 260.688 1.00 75.92 C
ANISOU 1417 CZ ARG A 180 10101 11891 6853 -338 1656 1192 C
ATOM 1418 NH1 ARG A 180 11.499 99.928 260.260 1.00 74.65 N
ANISOU 1418 NH1 ARG A 180 9982 11679 6703 -268 1561 1109 N
ATOM 1419 NH2 ARG A 180 10.173 98.047 260.365 1.00 76.97 N
ANISOU 1419 NH2 ARG A 180 10253 11989 7003 -433 1615 1281 N
ATOM 1420 N ASP A 181 9.349 107.370 261.360 1.00 60.69 N
ANISOU 1420 N ASP A 181 7915 10084 5062 199 2012 692 N
ATOM 1421 CA ASP A 181 9.310 108.593 262.161 1.00 61.81 C
ANISOU 1421 CA ASP A 181 8097 10237 5150 293 2102 596 C
ATOM 1422 C ASP A 181 9.839 108.431 263.560 1.00 62.02 C
ANISOU 1422 C ASP A 181 8272 10291 5003 292 2142 560 C
ATOM 1423 O ASP A 181 9.335 109.061 264.484 1.00 63.15 O
ANISOU 1423 O ASP A 181 8435 10480 5078 348 2266 513 O
ATOM 1424 CB ASP A 181 7.882 109.125 262.243 1.00 63.66 C
ANISOU 1424 CB ASP A 181 8201 10540 5449 343 2247 612 C
ATOM 1425 CG ASP A 181 7.462 109.828 260.970 1.00 66.15 C
ANISOU 1425 CG ASP A 181 8386 10820 5928 387 2212 609 C
ATOM 1426 OD1 ASP A 181 7.236 109.135 259.946 1.00 68.59 O
ANISOU 1426 OD1 ASP A 181 8608 11123 6331 323 2137 686 O
ATOM 1427 OD2 ASP A 181 7.383 111.079 260.986 1.00 68.69 O
ANISOU 1427 OD2 ASP A 181 8703 11116 6283 486 2255 529 O
ATOM 1428 N VAL A 182 10.842 107.572 263.720 1.00 60.96 N
ANISOU 1428 N VAL A 182 8241 10128 4793 233 2037 582 N
ATOM 1429 CA VAL A 182 11.458 107.322 265.027 1.00 60.62 C
ANISOU 1429 CA VAL A 182 8347 10110 4575 227 2053 557 C
ATOM 1430 C VAL A 182 11.820 108.656 265.685 1.00 60.60 C
ANISOU 1430 C VAL A 182 8416 10097 4511 312 2094 429 C
ATOM 1431 O VAL A 182 11.713 108.804 266.891 1.00 61.88 O
ANISOU 1431 O VAL A 182 8664 10308 4537 331 2179 398 O
ATOM 1432 CB VAL A 182 12.689 106.393 264.886 1.00 59.68 C
ANISOU 1432 CB VAL A 182 8323 9945 4408 170 1903 586 C
ATOM 1433 CG1 VAL A 182 13.562 106.420 266.138 1.00 60.11 C
ANISOU 1433 CG1 VAL A 182 8536 10016 4288 182 1889 536 C
ATOM 1434 CG2 VAL A 182 12.233 104.963 264.567 1.00 59.41 C
ANISOU 1434 CG2 VAL A 182 8251 9923 4397 83 1888 713 C
ATOM 1435 N VAL A 183 12.242 109.616 264.866 1.00 59.17 N
ANISOU 1435 N VAL A 183 8204 9848 4428 358 2032 358 N
ATOM 1436 CA VAL A 183 12.367 111.013 265.257 1.00 58.84 C
ANISOU 1436 CA VAL A 183 8207 9782 4368 441 2079 239 C
ATOM 1437 C VAL A 183 11.683 111.893 264.210 1.00 58.41 C
ANISOU 1437 C VAL A 183 8024 9689 4478 498 2107 224 C
ATOM 1438 O VAL A 183 11.303 111.430 263.123 1.00 57.36 O
ANISOU 1438 O VAL A 183 7777 9549 4470 467 2064 300 O
ATOM 1439 CB VAL A 183 13.838 111.454 265.432 1.00 58.49 C
ANISOU 1439 CB VAL A 183 8288 9676 4259 440 1958 150 C
ATOM 1440 CG1 VAL A 183 14.560 110.562 266.448 1.00 59.00 C
ANISOU 1440 CG1 VAL A 183 8477 9782 4159 389 1917 171 C
ATOM 1441 CG2 VAL A 183 14.575 111.467 264.112 1.00 55.75 C
ANISOU 1441 CG2 VAL A 183 7889 9257 4036 417 1819 159 C
ATOM 1442 N ALA A 184 11.534 113.169 264.539 1.00 58.97 N
ANISOU 1442 N ALA A 184 8124 9735 4549 582 2174 125 N
ATOM 1443 CA ALA A 184 10.622 114.049 263.804 1.00 58.92 C
ANISOU 1443 CA ALA A 184 7998 9706 4682 656 2239 116 C
ATOM 1444 C ALA A 184 11.335 115.028 262.880 1.00 57.75 C
ANISOU 1444 C ALA A 184 7858 9453 4631 688 2141 51 C
ATOM 1445 O ALA A 184 10.695 115.889 262.259 1.00 58.00 O
ANISOU 1445 O ALA A 184 7807 9451 4777 758 2183 36 O
ATOM 1446 CB ALA A 184 9.710 114.806 264.799 1.00 60.51 C
ANISOU 1446 CB ALA A 184 8211 9954 4828 744 2410 59 C
ATOM 1447 N ASP A 185 12.655 114.904 262.799 1.00 56.17 N
ANISOU 1447 N ASP A 185 7754 9204 4385 637 2013 17 N
ATOM 1448 CA ASP A 185 13.453 115.860 262.054 1.00 55.25 C
ANISOU 1448 CA ASP A 185 7661 8990 4341 656 1923 -50 C
ATOM 1449 C ASP A 185 13.168 115.756 260.550 1.00 54.00 C
ANISOU 1449 C ASP A 185 7372 8801 4346 646 1862 22 C
ATOM 1450 O ASP A 185 12.977 114.660 260.018 1.00 53.15 O
ANISOU 1450 O ASP A 185 7192 8733 4270 587 1821 117 O
ATOM 1451 CB ASP A 185 14.959 115.655 262.311 1.00 54.64 C
ANISOU 1451 CB ASP A 185 7702 8882 4176 595 1796 -95 C
ATOM 1452 CG ASP A 185 15.317 115.590 263.784 1.00 55.71 C
ANISOU 1452 CG ASP A 185 7971 9060 4138 591 1835 -155 C
ATOM 1453 OD1 ASP A 185 14.610 114.880 264.526 1.00 57.38 O
ANISOU 1453 OD1 ASP A 185 8178 9350 4273 587 1923 -106 O
ATOM 1454 OD2 ASP A 185 16.328 116.213 264.191 1.00 54.98 O
ANISOU 1454 OD2 ASP A 185 7988 8924 3980 584 1774 -247 O
ATOM 1455 N LYS A 186 13.155 116.911 259.886 1.00 53.63 N
ANISOU 1455 N LYS A 186 7305 8676 4395 703 1854 -27 N
ATOM 1456 CA LYS A 186 12.936 117.016 258.453 1.00 52.57 C
ANISOU 1456 CA LYS A 186 7060 8505 4409 703 1793 31 C
ATOM 1457 C LYS A 186 13.963 117.987 257.904 1.00 51.60 C
ANISOU 1457 C LYS A 186 7002 8280 4324 707 1705 -39 C
ATOM 1458 O LYS A 186 14.284 118.970 258.555 1.00 52.34 O
ANISOU 1458 O LYS A 186 7191 8323 4372 749 1738 -136 O
ATOM 1459 CB LYS A 186 11.537 117.560 258.172 1.00 53.71 C
ANISOU 1459 CB LYS A 186 7091 8666 4649 787 1901 59 C
ATOM 1460 CG LYS A 186 10.427 116.518 258.306 1.00 56.24 C
ANISOU 1460 CG LYS A 186 7302 9093 4975 766 1971 156 C
ATOM 1461 CD LYS A 186 9.124 117.090 258.927 1.00 59.93 C
ANISOU 1461 CD LYS A 186 7707 9608 5455 862 2130 146 C
ATOM 1462 CE LYS A 186 8.322 115.954 259.612 1.00 63.66 C
ANISOU 1462 CE LYS A 186 8123 10198 5865 817 2213 220 C
ATOM 1463 NZ LYS A 186 7.136 116.402 260.460 1.00 68.25 N
ANISOU 1463 NZ LYS A 186 8656 10847 6428 905 2385 205 N
ATOM 1464 N VAL A 187 14.504 117.705 256.719 1.00 50.05 N
ANISOU 1464 N VAL A 187 6759 8053 4205 659 1594 8 N
ATOM 1465 CA VAL A 187 15.449 118.632 256.081 1.00 49.13 C
ANISOU 1465 CA VAL A 187 6691 7842 4134 655 1513 -47 C
ATOM 1466 C VAL A 187 15.054 118.877 254.631 1.00 48.12 C
ANISOU 1466 C VAL A 187 6458 7679 4147 669 1474 17 C
ATOM 1467 O VAL A 187 14.996 117.957 253.830 1.00 46.78 O
ANISOU 1467 O VAL A 187 6213 7547 4016 620 1417 98 O
ATOM 1468 CB VAL A 187 16.929 118.181 256.197 1.00 47.81 C
ANISOU 1468 CB VAL A 187 6605 7668 3892 573 1400 -75 C
ATOM 1469 CG1 VAL A 187 17.799 119.119 255.445 1.00 48.50 C
ANISOU 1469 CG1 VAL A 187 6723 7667 4039 562 1324 -119 C
ATOM 1470 CG2 VAL A 187 17.393 118.236 257.626 1.00 49.24 C
ANISOU 1470 CG2 VAL A 187 6904 7871 3934 568 1430 -152 C
ATOM 1471 N GLU A 188 14.777 120.129 254.309 1.00 48.72 N
ANISOU 1471 N GLU A 188 6538 7679 4296 737 1504 -22 N
ATOM 1472 CA GLU A 188 14.206 120.460 253.006 1.00 49.31 C
ANISOU 1472 CA GLU A 188 6511 7723 4501 766 1481 43 C
ATOM 1473 C GLU A 188 15.250 121.025 252.047 1.00 47.68 C
ANISOU 1473 C GLU A 188 6342 7432 4342 728 1377 29 C
ATOM 1474 O GLU A 188 16.203 121.680 252.496 1.00 48.64 O
ANISOU 1474 O GLU A 188 6572 7493 4416 710 1353 -54 O
ATOM 1475 CB GLU A 188 13.060 121.475 253.159 1.00 51.01 C
ANISOU 1475 CB GLU A 188 6691 7909 4781 881 1587 28 C
ATOM 1476 CG GLU A 188 11.952 121.039 254.097 1.00 54.73 C
ANISOU 1476 CG GLU A 188 7114 8469 5212 928 1707 41 C
ATOM 1477 CD GLU A 188 11.163 119.814 253.608 1.00 58.74 C
ANISOU 1477 CD GLU A 188 7487 9079 5753 887 1701 153 C
ATOM 1478 OE1 GLU A 188 10.789 119.754 252.407 1.00 59.98 O
ANISOU 1478 OE1 GLU A 188 7545 9233 6013 885 1648 226 O
ATOM 1479 OE2 GLU A 188 10.884 118.922 254.450 1.00 61.79 O
ANISOU 1479 OE2 GLU A 188 7870 9549 6058 855 1752 168 O
ATOM 1480 N GLY A 189 15.070 120.770 250.748 1.00 45.30 N
ANISOU 1480 N GLY A 189 5952 7132 4129 710 1316 109 N
ATOM 1481 CA GLY A 189 15.901 121.393 249.694 1.00 42.69 C
ANISOU 1481 CA GLY A 189 5643 6722 3854 682 1230 109 C
ATOM 1482 C GLY A 189 17.361 120.984 249.576 1.00 40.40 C
ANISOU 1482 C GLY A 189 5416 6427 3507 589 1135 83 C
ATOM 1483 O GLY A 189 18.240 121.836 249.450 1.00 40.43 O
ANISOU 1483 O GLY A 189 5491 6356 3515 570 1098 30 O
ATOM 1484 N THR A 190 17.608 119.674 249.564 1.00 38.66 N
ANISOU 1484 N THR A 190 5166 6286 3239 530 1094 126 N
ATOM 1485 CA THR A 190 18.952 119.094 249.616 1.00 37.87 C
ANISOU 1485 CA THR A 190 5117 6200 3073 452 1012 104 C
ATOM 1486 C THR A 190 19.235 118.343 248.322 1.00 36.84 C
ANISOU 1486 C THR A 190 4919 6090 2987 404 932 178 C
ATOM 1487 O THR A 190 18.301 118.062 247.568 1.00 36.73 O
ANISOU 1487 O THR A 190 4823 6095 3038 423 942 248 O
ATOM 1488 CB THR A 190 19.065 118.094 250.790 1.00 37.98 C
ANISOU 1488 CB THR A 190 5166 6285 2979 430 1031 89 C
ATOM 1489 OG1 THR A 190 18.753 116.781 250.333 1.00 37.33 O
ANISOU 1489 OG1 THR A 190 5017 6267 2899 397 1005 170 O
ATOM 1490 CG2 THR A 190 18.125 118.455 251.924 1.00 39.09 C
ANISOU 1490 CG2 THR A 190 5329 6440 3085 491 1140 55 C
ATOM 1491 N ASN A 191 20.503 117.997 248.074 1.00 36.16 N
ANISOU 1491 N ASN A 191 4868 6007 2865 343 853 162 N
ATOM 1492 CA ASN A 191 20.886 117.241 246.864 1.00 35.24 C
ANISOU 1492 CA ASN A 191 4698 5911 2779 300 779 224 C
ATOM 1493 C ASN A 191 20.624 115.747 247.023 1.00 34.84 C
ANISOU 1493 C ASN A 191 4618 5933 2685 277 768 272 C
ATOM 1494 O ASN A 191 20.674 114.991 246.063 1.00 34.43 O
ANISOU 1494 O ASN A 191 4523 5902 2658 248 719 327 O
ATOM 1495 CB ASN A 191 22.363 117.460 246.494 1.00 34.79 C
ANISOU 1495 CB ASN A 191 4680 5834 2703 249 705 189 C
ATOM 1496 CG ASN A 191 23.323 116.815 247.494 1.00 35.77 C
ANISOU 1496 CG ASN A 191 4858 6000 2731 217 677 144 C
ATOM 1497 OD1 ASN A 191 22.913 116.398 248.579 1.00 41.63 O
ANISOU 1497 OD1 ASN A 191 5628 6775 3413 234 718 129 O
ATOM 1498 ND2 ASN A 191 24.606 116.753 247.148 1.00 34.34 N
ANISOU 1498 ND2 ASN A 191 4691 5824 2533 171 608 125 N
ATOM 1499 N GLY A 192 20.374 115.315 248.243 1.00 35.28 N
ANISOU 1499 N GLY A 192 4709 6024 2672 286 813 251 N
ATOM 1500 CA GLY A 192 20.057 113.937 248.479 1.00 35.07 C
ANISOU 1500 CA GLY A 192 4665 6056 2604 262 810 300 C
ATOM 1501 C GLY A 192 21.057 113.246 249.361 1.00 34.98 C
ANISOU 1501 C GLY A 192 4725 6073 2494 234 776 269 C
ATOM 1502 O GLY A 192 20.674 112.365 250.128 1.00 35.24 O
ANISOU 1502 O GLY A 192 4773 6149 2469 229 803 292 O
ATOM 1503 N SER A 193 22.333 113.617 249.254 1.00 34.70 N
ANISOU 1503 N SER A 193 4729 6018 2438 215 715 222 N
ATOM 1504 CA SER A 193 23.368 112.987 250.091 1.00 34.71 C
ANISOU 1504 CA SER A 193 4791 6053 2345 193 671 193 C
ATOM 1505 C SER A 193 23.148 113.231 251.595 1.00 35.58 C
ANISOU 1505 C SER A 193 4967 6179 2371 212 727 146 C
ATOM 1506 O SER A 193 22.967 114.362 252.009 1.00 36.15 O
ANISOU 1506 O SER A 193 5066 6220 2449 234 770 90 O
ATOM 1507 CB SER A 193 24.750 113.478 249.691 1.00 34.41 C
ANISOU 1507 CB SER A 193 4768 5997 2309 167 598 149 C
ATOM 1508 OG SER A 193 24.839 113.628 248.283 1.00 35.03 O
ANISOU 1508 OG SER A 193 4789 6052 2469 155 566 183 O
ATOM 1509 N VAL A 194 23.130 112.165 252.388 1.00 35.75 N
ANISOU 1509 N VAL A 194 5021 6248 2313 204 728 170 N
ATOM 1510 CA VAL A 194 23.224 112.277 253.845 1.00 36.58 C
ANISOU 1510 CA VAL A 194 5204 6380 2314 214 762 124 C
ATOM 1511 C VAL A 194 24.515 111.652 254.356 1.00 36.51 C
ANISOU 1511 C VAL A 194 5250 6403 2220 190 679 108 C
ATOM 1512 O VAL A 194 24.759 110.479 254.117 1.00 36.11 O
ANISOU 1512 O VAL A 194 5190 6376 2154 178 636 164 O
ATOM 1513 CB VAL A 194 22.075 111.510 254.542 1.00 37.08 C
ANISOU 1513 CB VAL A 194 5270 6482 2337 226 840 175 C
ATOM 1514 CG1 VAL A 194 22.029 111.808 256.043 1.00 38.10 C
ANISOU 1514 CG1 VAL A 194 5483 6638 2355 242 894 122 C
ATOM 1515 CG2 VAL A 194 20.742 111.817 253.887 1.00 37.12 C
ANISOU 1515 CG2 VAL A 194 5195 6472 2436 247 913 214 C
ATOM 1516 N VAL A 195 25.338 112.403 255.064 1.00 36.99 N
ANISOU 1516 N VAL A 195 5369 6464 2224 185 654 31 N
ATOM 1517 CA VAL A 195 26.541 111.795 255.669 1.00 37.11 C
ANISOU 1517 CA VAL A 195 5430 6521 2150 166 571 18 C
ATOM 1518 C VAL A 195 26.545 111.944 257.208 1.00 38.16 C
ANISOU 1518 C VAL A 195 5654 6686 2157 173 599 -29 C
ATOM 1519 O VAL A 195 26.320 113.040 257.737 1.00 38.81 O
ANISOU 1519 O VAL A 195 5777 6746 2223 180 645 -99 O
ATOM 1520 CB VAL A 195 27.855 112.355 255.039 1.00 36.77 C
ANISOU 1520 CB VAL A 195 5364 6466 2141 139 483 -24 C
ATOM 1521 CG1 VAL A 195 29.116 111.871 255.811 1.00 37.13 C
ANISOU 1521 CG1 VAL A 195 5452 6566 2090 125 396 -47 C
ATOM 1522 CG2 VAL A 195 27.944 112.003 253.553 1.00 35.80 C
ANISOU 1522 CG2 VAL A 195 5158 6323 2121 133 453 29 C
ATOM 1523 N TRP A 196 26.808 110.852 257.920 1.00 38.40 N
ANISOU 1523 N TRP A 196 5727 6767 2097 173 569 10 N
ATOM 1524 CA TRP A 196 26.652 110.862 259.367 1.00 39.45 C
ANISOU 1524 CA TRP A 196 5950 6937 2102 180 604 -20 C
ATOM 1525 C TRP A 196 27.854 111.346 260.164 1.00 40.08 C
ANISOU 1525 C TRP A 196 6093 7043 2091 163 527 -95 C
ATOM 1526 O TRP A 196 28.989 111.159 259.766 1.00 39.72 O
ANISOU 1526 O TRP A 196 6023 7012 2058 146 427 -98 O
ATOM 1527 CB TRP A 196 26.227 109.485 259.854 1.00 39.61 C
ANISOU 1527 CB TRP A 196 5997 6997 2058 187 619 64 C
ATOM 1528 CG TRP A 196 24.745 109.242 259.703 1.00 39.65 C
ANISOU 1528 CG TRP A 196 5969 6991 2104 197 729 117 C
ATOM 1529 CD1 TRP A 196 24.113 108.547 258.703 1.00 38.93 C
ANISOU 1529 CD1 TRP A 196 5805 6880 2106 191 742 194 C
ATOM 1530 CD2 TRP A 196 23.702 109.727 260.573 1.00 40.55 C
ANISOU 1530 CD2 TRP A 196 6118 7119 2170 214 843 96 C
ATOM 1531 NE1 TRP A 196 22.761 108.543 258.917 1.00 39.34 N
ANISOU 1531 NE1 TRP A 196 5838 6939 2173 198 851 225 N
ATOM 1532 CE2 TRP A 196 22.478 109.264 260.049 1.00 40.34 C
ANISOU 1532 CE2 TRP A 196 6025 7087 2215 216 920 167 C
ATOM 1533 CE3 TRP A 196 23.690 110.479 261.769 1.00 41.63 C
ANISOU 1533 CE3 TRP A 196 6337 7276 2202 228 889 22 C
ATOM 1534 CZ2 TRP A 196 21.247 109.535 260.676 1.00 41.17 C
ANISOU 1534 CZ2 TRP A 196 6132 7213 2298 235 1044 171 C
ATOM 1535 CZ3 TRP A 196 22.454 110.746 262.388 1.00 42.44 C
ANISOU 1535 CZ3 TRP A 196 6453 7395 2279 252 1019 21 C
ATOM 1536 CH2 TRP A 196 21.262 110.270 261.840 1.00 42.21 C
ANISOU 1536 CH2 TRP A 196 6344 7366 2328 257 1096 98 C
ATOM 1537 N GLY A 197 27.581 111.998 261.295 1.00 42.11 N
ANISOU 1537 N GLY A 197 6433 7312 2256 168 577 -159 N
ATOM 1538 CA GLY A 197 28.590 112.280 262.302 1.00 43.42 C
ANISOU 1538 CA GLY A 197 6676 7516 2304 148 506 -224 C
ATOM 1539 C GLY A 197 28.659 111.036 263.152 1.00 45.07 C
ANISOU 1539 C GLY A 197 6938 7790 2398 158 485 -161 C
ATOM 1540 O GLY A 197 28.020 110.021 262.824 1.00 45.24 O
ANISOU 1540 O GLY A 197 6929 7813 2446 174 519 -70 O
ATOM 1541 N PRO A 198 29.461 111.077 264.230 1.00 46.86 N
ANISOU 1541 N PRO A 198 7245 8067 2494 146 421 -204 N
ATOM 1542 CA PRO A 198 29.495 110.002 265.221 1.00 47.86 C
ANISOU 1542 CA PRO A 198 7442 8254 2488 158 404 -147 C
ATOM 1543 C PRO A 198 28.199 109.844 266.008 1.00 48.82 C
ANISOU 1543 C PRO A 198 7625 8384 2539 177 534 -125 C
ATOM 1544 O PRO A 198 27.370 110.761 266.045 1.00 49.09 O
ANISOU 1544 O PRO A 198 7664 8386 2603 185 635 -179 O
ATOM 1545 CB PRO A 198 30.629 110.432 266.168 1.00 49.00 C
ANISOU 1545 CB PRO A 198 7658 8448 2512 136 307 -221 C
ATOM 1546 CG PRO A 198 30.938 111.852 265.820 1.00 48.86 C
ANISOU 1546 CG PRO A 198 7621 8387 2556 106 302 -327 C
ATOM 1547 CD PRO A 198 30.628 111.963 264.376 1.00 47.40 C
ANISOU 1547 CD PRO A 198 7327 8141 2543 111 328 -294 C
ATOM 1548 N ASN A 199 28.056 108.664 266.616 1.00 49.60 N
ANISOU 1548 N ASN A 199 7771 8527 2549 186 532 -42 N
ATOM 1549 CA ASN A 199 27.022 108.351 267.602 1.00 50.69 C
ANISOU 1549 CA ASN A 199 7983 8694 2583 195 642 -12 C
ATOM 1550 C ASN A 199 25.669 108.975 267.300 1.00 50.09 C
ANISOU 1550 C ASN A 199 7866 8583 2582 208 788 -27 C
ATOM 1551 O ASN A 199 24.983 109.453 268.210 1.00 52.21 O
ANISOU 1551 O ASN A 199 8200 8874 2762 219 887 -67 O
ATOM 1552 CB ASN A 199 27.451 108.784 269.008 1.00 52.56 C
ANISOU 1552 CB ASN A 199 8342 8986 2644 191 625 -81 C
ATOM 1553 CG ASN A 199 28.958 108.780 269.200 1.00 55.16 C
ANISOU 1553 CG ASN A 199 8692 9346 2921 176 466 -114 C
ATOM 1554 OD1 ASN A 199 29.650 107.778 268.913 1.00 54.97 O
ANISOU 1554 OD1 ASN A 199 8642 9339 2905 182 370 -38 O
ATOM 1555 ND2 ASN A 199 29.483 109.908 269.717 1.00 57.92 N
ANISOU 1555 ND2 ASN A 199 9090 9703 3213 158 436 -230 N
ATOM 1556 N ALA A 200 25.287 108.998 266.034 1.00 47.68 N
ANISOU 1556 N ALA A 200 7453 8226 2436 209 803 3 N
ATOM 1557 CA ALA A 200 23.978 109.491 265.660 1.00 46.52 C
ANISOU 1557 CA ALA A 200 7252 8052 2373 226 934 3 C
ATOM 1558 C ALA A 200 23.657 110.852 266.234 1.00 46.79 C
ANISOU 1558 C ALA A 200 7330 8075 2373 248 1009 -106 C
ATOM 1559 O ALA A 200 22.501 111.185 266.393 1.00 47.36 O
ANISOU 1559 O ALA A 200 7386 8146 2462 273 1135 -107 O
ATOM 1560 CB ALA A 200 22.919 108.498 266.072 1.00 46.34 C
ANISOU 1560 CB ALA A 200 7234 8063 2308 224 1025 98 C
ATOM 1561 N GLU A 201 24.660 111.649 266.548 1.00 47.00 N
ANISOU 1561 N GLU A 201 7411 8092 2354 238 933 -200 N
ATOM 1562 CA GLU A 201 24.366 112.914 267.173 1.00 48.65 C
ANISOU 1562 CA GLU A 201 7683 8282 2520 257 1003 -309 C
ATOM 1563 C GLU A 201 23.966 113.986 266.155 1.00 48.21 C
ANISOU 1563 C GLU A 201 7552 8146 2618 276 1043 -354 C
ATOM 1564 O GLU A 201 23.276 114.950 266.518 1.00 49.42 O
ANISOU 1564 O GLU A 201 7738 8272 2766 311 1142 -425 O
ATOM 1565 CB GLU A 201 25.521 113.359 268.061 1.00 49.71 C
ANISOU 1565 CB GLU A 201 7922 8439 2526 230 910 -397 C
ATOM 1566 CG GLU A 201 25.221 113.198 269.539 1.00 53.47 C
ANISOU 1566 CG GLU A 201 8521 8979 2817 240 969 -419 C
ATOM 1567 CD GLU A 201 26.324 112.449 270.316 1.00 57.80 C
ANISOU 1567 CD GLU A 201 9142 9593 3224 208 845 -400 C
ATOM 1568 OE1 GLU A 201 27.514 112.552 269.918 1.00 57.75 O
ANISOU 1568 OE1 GLU A 201 9113 9581 3248 178 708 -423 O
ATOM 1569 OE2 GLU A 201 25.987 111.755 271.329 1.00 59.26 O
ANISOU 1569 OE2 GLU A 201 9406 9842 3267 215 886 -357 O
ATOM 1570 N CYS A 202 24.379 113.793 264.895 1.00 46.36 N
ANISOU 1570 N CYS A 202 7222 7877 2517 259 969 -311 N
ATOM 1571 CA CYS A 202 24.197 114.767 263.829 1.00 45.48 C
ANISOU 1571 CA CYS A 202 7042 7689 2551 270 982 -345 C
ATOM 1572 C CYS A 202 24.560 114.172 262.473 1.00 43.79 C
ANISOU 1572 C CYS A 202 6720 7457 2461 249 905 -269 C
ATOM 1573 O CYS A 202 25.119 113.065 262.419 1.00 43.33 O
ANISOU 1573 O CYS A 202 6651 7440 2371 226 832 -204 O
ATOM 1574 CB CYS A 202 25.159 115.906 264.033 1.00 46.20 C
ANISOU 1574 CB CYS A 202 7194 7739 2621 246 918 -456 C
ATOM 1575 SG CYS A 202 26.836 115.435 263.521 1.00 47.71 S
ANISOU 1575 SG CYS A 202 7356 7951 2820 184 741 -442 S
ATOM 1576 N PHE A 203 24.288 114.925 261.398 1.00 42.39 N
ANISOU 1576 N PHE A 203 6473 7214 2419 259 920 -278 N
ATOM 1577 CA PHE A 203 24.686 114.524 260.049 1.00 41.13 C
ANISOU 1577 CA PHE A 203 6219 7035 2375 238 848 -218 C
ATOM 1578 C PHE A 203 24.863 115.700 259.077 1.00 40.78 C
ANISOU 1578 C PHE A 203 6134 6913 2446 236 835 -262 C
ATOM 1579 O PHE A 203 24.565 116.865 259.406 1.00 41.51 O
ANISOU 1579 O PHE A 203 6272 6957 2543 256 889 -338 O
ATOM 1580 CB PHE A 203 23.719 113.505 259.445 1.00 40.53 C
ANISOU 1580 CB PHE A 203 6065 6978 2358 252 893 -113 C
ATOM 1581 CG PHE A 203 22.372 114.082 259.014 1.00 40.67 C
ANISOU 1581 CG PHE A 203 6026 6963 2464 292 1001 -100 C
ATOM 1582 CD1 PHE A 203 22.267 114.941 257.930 1.00 40.67 C
ANISOU 1582 CD1 PHE A 203 5966 6899 2587 303 995 -113 C
ATOM 1583 CD2 PHE A 203 21.202 113.713 259.672 1.00 41.68 C
ANISOU 1583 CD2 PHE A 203 6153 7129 2553 320 1107 -66 C
ATOM 1584 CE1 PHE A 203 21.028 115.463 257.535 1.00 41.28 C
ANISOU 1584 CE1 PHE A 203 5986 6951 2747 349 1089 -96 C
ATOM 1585 CE2 PHE A 203 19.965 114.210 259.277 1.00 42.66 C
ANISOU 1585 CE2 PHE A 203 6211 7235 2763 362 1205 -50 C
ATOM 1586 CZ PHE A 203 19.880 115.095 258.200 1.00 41.95 C
ANISOU 1586 CZ PHE A 203 6061 7080 2797 381 1192 -65 C
ATOM 1587 N PHE A 204 25.313 115.385 257.868 1.00 39.73 N
ANISOU 1587 N PHE A 204 5923 6766 2406 213 768 -213 N
ATOM 1588 CA PHE A 204 25.737 116.417 256.968 1.00 39.42 C
ANISOU 1588 CA PHE A 204 5856 6662 2461 198 738 -250 C
ATOM 1589 C PHE A 204 25.015 116.326 255.615 1.00 38.58 C
ANISOU 1589 C PHE A 204 5653 6523 2484 216 761 -178 C
ATOM 1590 O PHE A 204 24.837 115.223 255.027 1.00 37.84 O
ANISOU 1590 O PHE A 204 5500 6465 2415 212 740 -97 O
ATOM 1591 CB PHE A 204 27.270 116.381 256.795 1.00 39.16 C
ANISOU 1591 CB PHE A 204 5828 6644 2407 143 620 -276 C
ATOM 1592 CG PHE A 204 28.042 116.438 258.096 1.00 40.05 C
ANISOU 1592 CG PHE A 204 6030 6797 2390 121 580 -343 C
ATOM 1593 CD1 PHE A 204 28.378 117.667 258.680 1.00 41.04 C
ANISOU 1593 CD1 PHE A 204 6228 6880 2484 101 581 -444 C
ATOM 1594 CD2 PHE A 204 28.440 115.267 258.752 1.00 40.09 C
ANISOU 1594 CD2 PHE A 204 6054 6880 2300 118 535 -306 C
ATOM 1595 CE1 PHE A 204 29.090 117.733 259.897 1.00 41.89 C
ANISOU 1595 CE1 PHE A 204 6423 7030 2464 74 537 -510 C
ATOM 1596 CE2 PHE A 204 29.137 115.330 259.970 1.00 41.02 C
ANISOU 1596 CE2 PHE A 204 6256 7040 2290 99 492 -364 C
ATOM 1597 CZ PHE A 204 29.465 116.566 260.530 1.00 41.91 C
ANISOU 1597 CZ PHE A 204 6437 7118 2370 74 491 -468 C
ATOM 1598 N TYR A 205 24.626 117.491 255.106 1.00 38.77 N
ANISOU 1598 N TYR A 205 5667 6476 2589 235 799 -209 N
ATOM 1599 CA TYR A 205 23.882 117.522 253.874 1.00 38.15 C
ANISOU 1599 CA TYR A 205 5502 6367 2626 256 821 -144 C
ATOM 1600 C TYR A 205 24.246 118.757 253.054 1.00 38.14 C
ANISOU 1600 C TYR A 205 5496 6284 2709 246 800 -177 C
ATOM 1601 O TYR A 205 25.025 119.606 253.456 1.00 38.64 O
ANISOU 1601 O TYR A 205 5626 6311 2747 220 773 -253 O
ATOM 1602 CB TYR A 205 22.370 117.441 254.176 1.00 38.62 C
ANISOU 1602 CB TYR A 205 5536 6436 2701 315 928 -112 C
ATOM 1603 CG TYR A 205 21.861 118.675 254.867 1.00 39.71 C
ANISOU 1603 CG TYR A 205 5732 6522 2833 363 1008 -188 C
ATOM 1604 CD1 TYR A 205 21.955 118.823 256.248 1.00 40.65 C
ANISOU 1604 CD1 TYR A 205 5943 6662 2840 372 1046 -257 C
ATOM 1605 CD2 TYR A 205 21.335 119.728 254.130 1.00 39.89 C
ANISOU 1605 CD2 TYR A 205 5727 6470 2958 402 1041 -193 C
ATOM 1606 CE1 TYR A 205 21.518 119.972 256.884 1.00 41.75 C
ANISOU 1606 CE1 TYR A 205 6148 6748 2968 419 1121 -336 C
ATOM 1607 CE2 TYR A 205 20.905 120.897 254.768 1.00 41.94 C
ANISOU 1607 CE2 TYR A 205 6051 6669 3213 454 1114 -269 C
ATOM 1608 CZ TYR A 205 20.992 120.999 256.144 1.00 41.93 C
ANISOU 1608 CZ TYR A 205 6144 6690 3099 462 1156 -343 C
ATOM 1609 OH TYR A 205 20.552 122.162 256.732 1.00 43.12 O
ANISOU 1609 OH TYR A 205 6364 6774 3245 519 1233 -423 O
ATOM 1610 N ILE A 206 23.643 118.857 251.893 1.00 37.64 N
ANISOU 1610 N ILE A 206 5360 6193 2748 265 811 -117 N
ATOM 1611 CA ILE A 206 24.068 119.785 250.899 1.00 37.46 C
ANISOU 1611 CA ILE A 206 5324 6102 2807 247 777 -123 C
ATOM 1612 C ILE A 206 22.862 120.423 250.273 1.00 37.69 C
ANISOU 1612 C ILE A 206 5313 6080 2929 307 841 -89 C
ATOM 1613 O ILE A 206 22.123 119.748 249.541 1.00 37.17 O
ANISOU 1613 O ILE A 206 5167 6046 2911 325 849 -9 O
ATOM 1614 CB ILE A 206 24.811 119.014 249.811 1.00 36.43 C
ANISOU 1614 CB ILE A 206 5132 6006 2705 199 696 -65 C
ATOM 1615 CG1 ILE A 206 26.244 118.739 250.281 1.00 36.37 C
ANISOU 1615 CG1 ILE A 206 5161 6033 2624 141 621 -109 C
ATOM 1616 CG2 ILE A 206 24.750 119.743 248.423 1.00 36.13 C
ANISOU 1616 CG2 ILE A 206 5049 5906 2771 195 680 -29 C
ATOM 1617 CD1 ILE A 206 27.089 117.940 249.330 1.00 35.50 C
ANISOU 1617 CD1 ILE A 206 4992 5965 2531 102 546 -60 C
ATOM 1618 N THR A 207 22.663 121.715 250.535 1.00 38.55 N
ANISOU 1618 N THR A 207 5477 6106 3065 338 883 -147 N
ATOM 1619 CA THR A 207 21.618 122.459 249.816 1.00 38.86 C
ANISOU 1619 CA THR A 207 5477 6085 3204 402 934 -111 C
ATOM 1620 C THR A 207 21.979 122.912 248.403 1.00 38.36 C
ANISOU 1620 C THR A 207 5375 5969 3228 375 878 -64 C
ATOM 1621 O THR A 207 23.123 123.252 248.078 1.00 38.14 O
ANISOU 1621 O THR A 207 5382 5913 3197 310 814 -89 O
ATOM 1622 CB THR A 207 21.045 123.691 250.576 1.00 40.14 C
ANISOU 1622 CB THR A 207 5713 6167 3373 468 1015 -183 C
ATOM 1623 OG1 THR A 207 22.015 124.750 250.642 1.00 40.59 O
ANISOU 1623 OG1 THR A 207 5858 6135 3428 427 978 -256 O
ATOM 1624 CG2 THR A 207 20.518 123.291 251.943 1.00 40.80 C
ANISOU 1624 CG2 THR A 207 5830 6305 3366 505 1087 -226 C
ATOM 1625 N LYS A 208 20.936 122.908 247.581 1.00 38.27 N
ANISOU 1625 N LYS A 208 5290 5955 3296 427 905 9 N
ATOM 1626 CA LYS A 208 20.910 123.573 246.280 1.00 38.13 C
ANISOU 1626 CA LYS A 208 5243 5875 3369 429 873 59 C
ATOM 1627 C LYS A 208 20.965 125.085 246.443 1.00 40.07 C
ANISOU 1627 C LYS A 208 5569 6001 3655 459 902 3 C
ATOM 1628 O LYS A 208 21.286 125.599 247.523 1.00 40.78 O
ANISOU 1628 O LYS A 208 5745 6055 3693 460 932 -85 O
ATOM 1629 CB LYS A 208 19.659 123.153 245.511 1.00 37.97 C
ANISOU 1629 CB LYS A 208 5124 5891 3414 484 895 149 C
ATOM 1630 CG LYS A 208 19.957 122.232 244.375 1.00 37.56 C
ANISOU 1630 CG LYS A 208 5003 5894 3374 429 823 224 C
ATOM 1631 CD LYS A 208 20.069 120.780 244.734 1.00 38.02 C
ANISOU 1631 CD LYS A 208 5029 6051 3366 392 805 240 C
ATOM 1632 CE LYS A 208 20.307 120.004 243.428 1.00 40.14 C
ANISOU 1632 CE LYS A 208 5237 6357 3657 346 735 313 C
ATOM 1633 NZ LYS A 208 20.457 118.544 243.687 1.00 42.92 N
ANISOU 1633 NZ LYS A 208 5566 6793 3949 309 712 330 N
ATOM 1634 N ASP A 209 20.644 125.776 245.358 1.00 42.00 N
ANISOU 1634 N ASP A 209 5789 6181 3987 483 891 57 N
ATOM 1635 CA ASP A 209 20.882 127.206 245.213 1.00 45.07 C
ANISOU 1635 CA ASP A 209 6260 6441 4424 496 899 20 C
ATOM 1636 C ASP A 209 20.088 127.717 244.003 1.00 44.56 C
ANISOU 1636 C ASP A 209 6143 6328 4459 553 898 107 C
ATOM 1637 O ASP A 209 19.305 126.974 243.392 1.00 43.63 O
ANISOU 1637 O ASP A 209 5925 6283 4367 584 894 187 O
ATOM 1638 CB ASP A 209 22.406 127.466 245.020 1.00 46.30 C
ANISOU 1638 CB ASP A 209 6474 6568 4550 384 829 -17 C
ATOM 1639 CG ASP A 209 22.853 128.998 245.239 1.00 53.77 C
ANISOU 1639 CG ASP A 209 7536 7368 5525 374 839 -84 C
ATOM 1640 OD1 ASP A 209 22.029 129.970 245.082 1.00 59.44 O
ANISOU 1640 OD1 ASP A 209 8286 7986 6311 456 887 -77 O
ATOM 1641 OD2 ASP A 209 24.081 129.223 245.536 1.00 58.10 O
ANISOU 1641 OD2 ASP A 209 8144 7901 6031 278 793 -142 O
ATOM 1642 N ALA A 210 20.258 129.019 243.747 1.00 44.89 N
ANISOU 1642 N ALA A 210 6261 6243 4554 568 903 88 N
ATOM 1643 CA ALA A 210 19.981 129.680 242.500 1.00 44.52 C
ANISOU 1643 CA ALA A 210 6197 6128 4592 590 878 168 C
ATOM 1644 C ALA A 210 20.369 128.723 241.406 1.00 43.11 C
ANISOU 1644 C ALA A 210 5934 6040 4404 521 808 249 C
ATOM 1645 O ALA A 210 21.504 128.205 241.413 1.00 43.04 O
ANISOU 1645 O ALA A 210 5937 6076 4340 422 761 225 O
ATOM 1646 CB ALA A 210 20.836 130.954 242.403 1.00 45.28 C
ANISOU 1646 CB ALA A 210 6409 6085 4709 545 862 124 C
ATOM 1647 N SER A 211 19.431 128.458 240.490 1.00 41.54 N
ANISOU 1647 N SER A 211 5650 5875 4259 575 800 343 N
ATOM 1648 CA SER A 211 19.696 127.599 239.339 1.00 39.34 C
ANISOU 1648 CA SER A 211 5298 5675 3973 516 733 422 C
ATOM 1649 C SER A 211 20.131 126.199 239.732 1.00 38.01 C
ANISOU 1649 C SER A 211 5086 5627 3728 456 713 403 C
ATOM 1650 O SER A 211 20.765 125.492 238.927 1.00 37.17 O
ANISOU 1650 O SER A 211 4948 5578 3597 387 655 441 O
ATOM 1651 CB SER A 211 20.773 128.205 238.451 1.00 39.65 C
ANISOU 1651 CB SER A 211 5390 5653 4021 437 681 441 C
ATOM 1652 OG SER A 211 20.515 129.578 238.232 1.00 43.62 O
ANISOU 1652 OG SER A 211 5959 6025 4590 484 700 449 O
ATOM 1653 N LYS A 212 19.814 125.817 240.972 1.00 38.15 N
ANISOU 1653 N LYS A 212 5110 5681 3705 485 763 343 N
ATOM 1654 CA LYS A 212 19.889 124.434 241.430 1.00 37.35 C
ANISOU 1654 CA LYS A 212 4962 5693 3538 451 754 338 C
ATOM 1655 C LYS A 212 21.300 123.940 241.545 1.00 36.65 C
ANISOU 1655 C LYS A 212 4910 5634 3383 356 703 299 C
ATOM 1656 O LYS A 212 21.521 122.728 241.519 1.00 35.88 O
ANISOU 1656 O LYS A 212 4770 5625 3238 320 675 315 O
ATOM 1657 CB LYS A 212 19.039 123.508 240.537 1.00 36.86 C
ANISOU 1657 CB LYS A 212 4796 5708 3501 465 730 430 C
ATOM 1658 CG LYS A 212 17.683 123.161 241.133 1.00 37.33 C
ANISOU 1658 CG LYS A 212 4793 5813 3577 539 790 446 C
ATOM 1659 CD LYS A 212 16.531 123.026 240.130 1.00 37.50 C
ANISOU 1659 CD LYS A 212 4718 5865 3667 583 777 541 C
ATOM 1660 CE LYS A 212 15.261 123.562 240.806 1.00 38.58 C
ANISOU 1660 CE LYS A 212 4819 5991 3850 688 858 539 C
ATOM 1661 NZ LYS A 212 14.007 123.253 240.097 1.00 38.89 N
ANISOU 1661 NZ LYS A 212 4742 6086 3948 733 851 627 N
ATOM 1662 N ARG A 213 22.247 124.870 241.699 1.00 37.03 N
ANISOU 1662 N ARG A 213 5034 5606 3427 316 692 246 N
ATOM 1663 CA ARG A 213 23.651 124.495 241.993 1.00 36.57 C
ANISOU 1663 CA ARG A 213 5008 5582 3304 227 646 198 C
ATOM 1664 C ARG A 213 23.926 123.920 243.421 1.00 36.59 C
ANISOU 1664 C ARG A 213 5041 5635 3226 221 665 123 C
ATOM 1665 O ARG A 213 23.372 124.364 244.416 1.00 37.30 O
ANISOU 1665 O ARG A 213 5176 5693 3305 270 720 72 O
ATOM 1666 CB ARG A 213 24.573 125.673 241.748 1.00 37.09 C
ANISOU 1666 CB ARG A 213 5142 5558 3394 174 626 166 C
ATOM 1667 CG ARG A 213 26.047 125.309 241.657 1.00 36.64 C
ANISOU 1667 CG ARG A 213 5088 5546 3287 75 569 140 C
ATOM 1668 CD ARG A 213 26.837 126.513 241.282 1.00 37.27 C
ANISOU 1668 CD ARG A 213 5225 5535 3400 16 552 122 C
ATOM 1669 NE ARG A 213 27.604 127.066 242.400 1.00 37.92 N
ANISOU 1669 NE ARG A 213 5383 5583 3443 -30 551 26 N
ATOM 1670 CZ ARG A 213 27.238 128.118 243.103 1.00 38.92 C
ANISOU 1670 CZ ARG A 213 5594 5608 3587 -1 590 -32 C
ATOM 1671 NH1 ARG A 213 26.086 128.711 242.877 1.00 39.40 N
ANISOU 1671 NH1 ARG A 213 5669 5593 3707 85 639 -2 N
ATOM 1672 NH2 ARG A 213 28.017 128.562 244.036 1.00 39.53 N
ANISOU 1672 NH2 ARG A 213 5740 5659 3621 -56 578 -120 N
ATOM 1673 N ASP A 214 24.792 122.937 243.544 1.00 35.91 N
ANISOU 1673 N ASP A 214 4936 5628 3079 165 619 116 N
ATOM 1674 CA ASP A 214 25.114 122.480 244.877 1.00 36.06 C
ANISOU 1674 CA ASP A 214 4993 5690 3017 158 629 50 C
ATOM 1675 C ASP A 214 26.190 123.356 245.473 1.00 36.65 C
ANISOU 1675 C ASP A 214 5144 5717 3065 104 608 -31 C
ATOM 1676 O ASP A 214 27.379 123.202 245.190 1.00 36.36 O
ANISOU 1676 O ASP A 214 5101 5708 3008 32 549 -40 O
ATOM 1677 CB ASP A 214 25.496 121.009 244.855 1.00 35.21 C
ANISOU 1677 CB ASP A 214 4838 5686 2856 133 589 79 C
ATOM 1678 CG ASP A 214 24.321 120.129 244.520 1.00 34.83 C
ANISOU 1678 CG ASP A 214 4728 5681 2826 181 616 147 C
ATOM 1679 OD1 ASP A 214 23.183 120.683 244.395 1.00 35.27 O
ANISOU 1679 OD1 ASP A 214 4769 5697 2936 237 667 169 O
ATOM 1680 OD2 ASP A 214 24.530 118.895 244.380 1.00 34.19 O
ANISOU 1680 OD2 ASP A 214 4611 5671 2708 162 584 178 O
ATOM 1681 N ASN A 215 25.775 124.294 246.303 1.00 37.59 N
ANISOU 1681 N ASN A 215 5334 5764 3183 138 657 -93 N
ATOM 1682 CA ASN A 215 26.718 125.296 246.733 1.00 38.31 C
ANISOU 1682 CA ASN A 215 5506 5790 3260 80 635 -169 C
ATOM 1683 C ASN A 215 26.983 125.333 248.223 1.00 38.96 C
ANISOU 1683 C ASN A 215 5663 5887 3255 74 648 -262 C
ATOM 1684 O ASN A 215 27.843 126.096 248.641 1.00 39.63 O
ANISOU 1684 O ASN A 215 5814 5924 3318 14 619 -332 O
ATOM 1685 CB ASN A 215 26.260 126.662 246.275 1.00 39.09 C
ANISOU 1685 CB ASN A 215 5653 5762 3439 106 669 -171 C
ATOM 1686 CG ASN A 215 25.101 127.142 247.056 1.00 39.90 C
ANISOU 1686 CG ASN A 215 5801 5813 3547 200 750 -206 C
ATOM 1687 OD1 ASN A 215 24.129 126.408 247.264 1.00 39.63 O
ANISOU 1687 OD1 ASN A 215 5714 5839 3504 269 792 -172 O
ATOM 1688 ND2 ASN A 215 25.183 128.371 247.527 1.00 41.01 N
ANISOU 1688 ND2 ASN A 215 6040 5842 3701 203 774 -277 N
ATOM 1689 N LYS A 216 26.270 124.535 249.023 1.00 38.88 N
ANISOU 1689 N LYS A 216 5643 5940 3190 129 689 -264 N
ATOM 1690 CA LYS A 216 26.473 124.574 250.465 1.00 39.60 C
ANISOU 1690 CA LYS A 216 5813 6048 3187 127 705 -351 C
ATOM 1691 C LYS A 216 26.402 123.281 251.225 1.00 39.21 C
ANISOU 1691 C LYS A 216 5740 6109 3049 139 703 -339 C
ATOM 1692 O LYS A 216 25.526 122.454 250.994 1.00 38.70 O
ANISOU 1692 O LYS A 216 5614 6092 2997 188 738 -272 O
ATOM 1693 CB LYS A 216 25.504 125.529 251.109 1.00 40.68 C
ANISOU 1693 CB LYS A 216 6021 6101 3335 200 791 -403 C
ATOM 1694 CG LYS A 216 26.157 126.799 251.476 1.00 41.69 C
ANISOU 1694 CG LYS A 216 6252 6129 3460 157 777 -493 C
ATOM 1695 CD LYS A 216 25.217 127.757 252.141 1.00 42.89 C
ANISOU 1695 CD LYS A 216 6487 6190 3620 238 867 -553 C
ATOM 1696 CE LYS A 216 24.356 128.451 251.140 1.00 43.00 C
ANISOU 1696 CE LYS A 216 6470 6117 3751 303 909 -497 C
ATOM 1697 NZ LYS A 216 23.783 129.619 251.807 1.00 44.41 N
ANISOU 1697 NZ LYS A 216 6754 6183 3938 368 982 -576 N
ATOM 1698 N VAL A 217 27.315 123.161 252.188 1.00 39.60 N
ANISOU 1698 N VAL A 217 5846 6194 3005 90 660 -405 N
ATOM 1699 CA VAL A 217 27.403 122.038 253.121 1.00 39.48 C
ANISOU 1699 CA VAL A 217 5834 6278 2888 95 651 -405 C
ATOM 1700 C VAL A 217 27.039 122.532 254.516 1.00 40.63 C
ANISOU 1700 C VAL A 217 6082 6407 2949 123 706 -490 C
ATOM 1701 O VAL A 217 27.567 123.556 254.979 1.00 41.51 O
ANISOU 1701 O VAL A 217 6274 6457 3039 89 692 -577 O
ATOM 1702 CB VAL A 217 28.831 121.453 253.144 1.00 39.13 C
ANISOU 1702 CB VAL A 217 5772 6301 2793 20 548 -410 C
ATOM 1703 CG1 VAL A 217 28.898 120.206 253.958 1.00 38.96 C
ANISOU 1703 CG1 VAL A 217 5751 6378 2676 34 533 -391 C
ATOM 1704 CG2 VAL A 217 29.270 121.120 251.745 1.00 38.16 C
ANISOU 1704 CG2 VAL A 217 5558 6188 2753 -7 501 -338 C
ATOM 1705 N TRP A 218 26.143 121.778 255.162 1.00 40.69 N
ANISOU 1705 N TRP A 218 6086 6469 2905 180 768 -465 N
ATOM 1706 CA TRP A 218 25.603 122.074 256.485 1.00 41.80 C
ANISOU 1706 CA TRP A 218 6316 6610 2955 219 839 -534 C
ATOM 1707 C TRP A 218 25.636 120.859 257.394 1.00 41.75 C
ANISOU 1707 C TRP A 218 6319 6709 2836 218 834 -512 C
ATOM 1708 O TRP A 218 25.572 119.735 256.912 1.00 40.85 O
ANISOU 1708 O TRP A 218 6129 6656 2736 215 809 -426 O
ATOM 1709 CB TRP A 218 24.117 122.383 256.401 1.00 42.14 C
ANISOU 1709 CB TRP A 218 6340 6619 3054 308 955 -511 C
ATOM 1710 CG TRP A 218 23.657 123.433 255.486 1.00 42.25 C
ANISOU 1710 CG TRP A 218 6332 6532 3187 341 985 -507 C
ATOM 1711 CD1 TRP A 218 23.548 123.356 254.124 1.00 41.35 C
ANISOU 1711 CD1 TRP A 218 6128 6399 3185 337 955 -427 C
ATOM 1712 CD2 TRP A 218 23.140 124.713 255.866 1.00 43.43 C
ANISOU 1712 CD2 TRP A 218 6559 6585 3357 394 1056 -582 C
ATOM 1713 NE1 TRP A 218 23.034 124.534 253.626 1.00 41.90 N
ANISOU 1713 NE1 TRP A 218 6212 6364 3343 381 998 -443 N
ATOM 1714 CE2 TRP A 218 22.760 125.379 254.672 1.00 43.18 C
ANISOU 1714 CE2 TRP A 218 6476 6473 3456 421 1062 -537 C
ATOM 1715 CE3 TRP A 218 22.955 125.361 257.096 1.00 44.76 C
ANISOU 1715 CE3 TRP A 218 6840 6723 3442 425 1117 -683 C
ATOM 1716 CZ2 TRP A 218 22.201 126.655 254.679 1.00 44.22 C
ANISOU 1716 CZ2 TRP A 218 6666 6491 3643 482 1125 -587 C
ATOM 1717 CZ3 TRP A 218 22.426 126.628 257.098 1.00 45.78 C
ANISOU 1717 CZ3 TRP A 218 7030 6739 3626 484 1182 -740 C
ATOM 1718 CH2 TRP A 218 22.043 127.259 255.904 1.00 45.51 C
ANISOU 1718 CH2 TRP A 218 6943 6623 3728 515 1186 -690 C
ATOM 1719 N ARG A 219 25.637 121.127 258.703 1.00 42.85 N
ANISOU 1719 N ARG A 219 6558 6860 2861 226 865 -589 N
ATOM 1720 CA ARG A 219 25.514 120.141 259.774 1.00 43.15 C
ANISOU 1720 CA ARG A 219 6630 6991 2774 234 879 -577 C
ATOM 1721 C ARG A 219 24.061 120.145 260.252 1.00 43.75 C
ANISOU 1721 C ARG A 219 6712 7071 2840 313 1014 -565 C
ATOM 1722 O ARG A 219 23.460 121.209 260.459 1.00 44.60 O
ANISOU 1722 O ARG A 219 6864 7111 2971 358 1091 -627 O
ATOM 1723 CB ARG A 219 26.402 120.549 260.977 1.00 44.21 C
ANISOU 1723 CB ARG A 219 6882 7139 2778 193 832 -678 C
ATOM 1724 CG ARG A 219 26.805 119.414 261.914 1.00 44.36 C
ANISOU 1724 CG ARG A 219 6931 7263 2662 176 792 -654 C
ATOM 1725 CD ARG A 219 27.484 119.886 263.198 1.00 45.64 C
ANISOU 1725 CD ARG A 219 7217 7442 2683 144 758 -757 C
ATOM 1726 NE ARG A 219 28.829 120.472 263.093 1.00 45.81 N
ANISOU 1726 NE ARG A 219 7260 7445 2702 68 639 -820 N
ATOM 1727 CZ ARG A 219 29.976 119.849 263.411 1.00 45.78 C
ANISOU 1727 CZ ARG A 219 7254 7516 2625 14 523 -812 C
ATOM 1728 NH1 ARG A 219 29.998 118.582 263.832 1.00 45.53 N
ANISOU 1728 NH1 ARG A 219 7207 7577 2517 31 502 -741 N
ATOM 1729 NH2 ARG A 219 31.125 120.508 263.304 1.00 46.09 N
ANISOU 1729 NH2 ARG A 219 7304 7539 2671 -59 424 -874 N
ATOM 1730 N HIS A 220 23.484 118.973 260.464 1.00 43.45 N
ANISOU 1730 N HIS A 220 6631 7111 2766 330 1046 -486 N
ATOM 1731 CA HIS A 220 22.214 118.951 261.157 1.00 44.28 C
ANISOU 1731 CA HIS A 220 6750 7238 2835 394 1176 -482 C
ATOM 1732 C HIS A 220 22.302 118.105 262.412 1.00 44.90 C
ANISOU 1732 C HIS A 220 6897 7403 2759 382 1188 -480 C
ATOM 1733 O HIS A 220 22.706 116.932 262.332 1.00 44.23 O
ANISOU 1733 O HIS A 220 6783 7379 2643 345 1125 -407 O
ATOM 1734 CB HIS A 220 21.079 118.440 260.277 1.00 43.64 C
ANISOU 1734 CB HIS A 220 6550 7169 2863 431 1236 -382 C
ATOM 1735 CG HIS A 220 19.784 118.330 261.016 1.00 44.59 C
ANISOU 1735 CG HIS A 220 6668 7329 2944 492 1372 -370 C
ATOM 1736 ND1 HIS A 220 19.007 119.427 261.317 1.00 45.63 N
ANISOU 1736 ND1 HIS A 220 6825 7414 3098 563 1475 -433 N
ATOM 1737 CD2 HIS A 220 19.165 117.264 261.569 1.00 44.78 C
ANISOU 1737 CD2 HIS A 220 6673 7438 2904 492 1424 -305 C
ATOM 1738 CE1 HIS A 220 17.947 119.037 261.996 1.00 46.41 C
ANISOU 1738 CE1 HIS A 220 6908 7575 3150 607 1590 -407 C
ATOM 1739 NE2 HIS A 220 18.015 117.727 262.158 1.00 45.91 N
ANISOU 1739 NE2 HIS A 220 6818 7592 3034 559 1561 -326 N
ATOM 1740 N ILE A 221 21.911 118.706 263.539 1.00 46.24 N
ANISOU 1740 N ILE A 221 7163 7575 2832 416 1271 -559 N
ATOM 1741 CA ILE A 221 21.905 118.045 264.831 1.00 47.09 C
ANISOU 1741 CA ILE A 221 7351 7764 2778 410 1297 -565 C
ATOM 1742 C ILE A 221 20.510 117.530 265.188 1.00 47.59 C
ANISOU 1742 C ILE A 221 7376 7879 2827 463 1436 -504 C
ATOM 1743 O ILE A 221 19.525 118.273 265.179 1.00 48.24 O
ANISOU 1743 O ILE A 221 7441 7930 2959 528 1550 -533 O
ATOM 1744 CB ILE A 221 22.420 119.012 265.941 1.00 48.45 C
ANISOU 1744 CB ILE A 221 7667 7913 2828 408 1299 -698 C
ATOM 1745 CG1 ILE A 221 23.858 119.468 265.636 1.00 48.08 C
ANISOU 1745 CG1 ILE A 221 7651 7826 2790 340 1153 -754 C
ATOM 1746 CG2 ILE A 221 22.216 118.423 267.386 1.00 49.61 C
ANISOU 1746 CG2 ILE A 221 7910 8149 2790 413 1351 -707 C
ATOM 1747 CD1 ILE A 221 24.317 120.617 266.476 1.00 49.39 C
ANISOU 1747 CD1 ILE A 221 7950 7946 2871 329 1150 -891 C
ATOM 1748 N ILE A 222 20.437 116.253 265.515 1.00 47.38 N
ANISOU 1748 N ILE A 222 7335 7932 2734 436 1427 -418 N
ATOM 1749 CA ILE A 222 19.201 115.631 265.961 1.00 47.97 C
ANISOU 1749 CA ILE A 222 7378 8069 2779 467 1553 -352 C
ATOM 1750 C ILE A 222 18.604 116.351 267.175 1.00 49.64 C
ANISOU 1750 C ILE A 222 7682 8299 2878 519 1678 -436 C
ATOM 1751 O ILE A 222 19.292 116.715 268.138 1.00 50.48 O
ANISOU 1751 O ILE A 222 7917 8413 2852 507 1651 -521 O
ATOM 1752 CB ILE A 222 19.426 114.136 266.301 1.00 47.68 C
ANISOU 1752 CB ILE A 222 7347 8109 2662 416 1509 -253 C
ATOM 1753 CG1 ILE A 222 20.407 113.482 265.313 1.00 46.23 C
ANISOU 1753 CG1 ILE A 222 7112 7903 2551 366 1361 -199 C
ATOM 1754 CG2 ILE A 222 18.110 113.385 266.325 1.00 47.96 C
ANISOU 1754 CG2 ILE A 222 7308 8197 2719 430 1625 -158 C
ATOM 1755 CD1 ILE A 222 19.994 113.554 263.827 1.00 45.06 C
ANISOU 1755 CD1 ILE A 222 6832 7704 2585 371 1350 -149 C
ATOM 1756 N GLY A 223 17.308 116.575 267.123 1.00 50.21 N
ANISOU 1756 N GLY A 223 7690 8383 3004 579 1817 -415 N
ATOM 1757 CA GLY A 223 16.677 117.331 268.183 1.00 51.86 C
ANISOU 1757 CA GLY A 223 7979 8606 3119 641 1949 -500 C
ATOM 1758 C GLY A 223 16.471 118.773 267.785 1.00 52.23 C
ANISOU 1758 C GLY A 223 8030 8557 3259 708 1987 -596 C
ATOM 1759 O GLY A 223 15.998 119.565 268.606 1.00 53.69 O
ANISOU 1759 O GLY A 223 8291 8734 3374 772 2097 -684 O
ATOM 1760 N GLN A 224 16.782 119.118 266.527 1.00 51.03 N
ANISOU 1760 N GLN A 224 7798 8329 3260 699 1905 -578 N
ATOM 1761 CA GLN A 224 16.723 120.518 266.101 1.00 51.38 C
ANISOU 1761 CA GLN A 224 7860 8266 3394 756 1924 -667 C
ATOM 1762 C GLN A 224 15.999 120.908 264.824 1.00 50.74 C
ANISOU 1762 C GLN A 224 7645 8132 3501 804 1946 -613 C
ATOM 1763 O GLN A 224 15.926 120.133 263.868 1.00 49.48 O
ANISOU 1763 O GLN A 224 7371 7997 3433 767 1889 -508 O
ATOM 1764 CB GLN A 224 18.101 121.111 266.080 1.00 51.10 C
ANISOU 1764 CB GLN A 224 7924 8159 3330 698 1793 -752 C
ATOM 1765 CG GLN A 224 18.573 121.474 267.448 1.00 52.45 C
ANISOU 1765 CG GLN A 224 8257 8345 3326 690 1809 -861 C
ATOM 1766 CD GLN A 224 19.851 122.215 267.372 1.00 52.35 C
ANISOU 1766 CD GLN A 224 8333 8255 3301 633 1684 -952 C
ATOM 1767 OE1 GLN A 224 19.900 123.394 267.702 1.00 56.18 O
ANISOU 1767 OE1 GLN A 224 8914 8658 3774 664 1716 -1067 O
ATOM 1768 NE2 GLN A 224 20.897 121.557 266.887 1.00 51.14 N
ANISOU 1768 NE2 GLN A 224 8147 8124 3160 548 1541 -902 N
ATOM 1769 N PRO A 225 15.452 122.137 264.818 1.00 51.71 N
ANISOU 1769 N PRO A 225 7792 8179 3678 892 2028 -688 N
ATOM 1770 CA PRO A 225 14.843 122.699 263.647 1.00 51.31 C
ANISOU 1770 CA PRO A 225 7632 8064 3799 947 2042 -649 C
ATOM 1771 C PRO A 225 15.907 122.960 262.622 1.00 50.03 C
ANISOU 1771 C PRO A 225 7469 7821 3720 882 1894 -646 C
ATOM 1772 O PRO A 225 16.951 123.490 262.945 1.00 50.16 O
ANISOU 1772 O PRO A 225 7600 7780 3678 837 1822 -732 O
ATOM 1773 CB PRO A 225 14.290 124.033 264.150 1.00 52.91 C
ANISOU 1773 CB PRO A 225 7909 8191 4004 1054 2153 -756 C
ATOM 1774 CG PRO A 225 14.057 123.822 265.533 1.00 54.19 C
ANISOU 1774 CG PRO A 225 8160 8423 4006 1071 2247 -811 C
ATOM 1775 CD PRO A 225 15.234 123.010 265.979 1.00 53.46 C
ANISOU 1775 CD PRO A 225 8142 8377 3792 955 2130 -810 C
ATOM 1776 N GLN A 226 15.636 122.587 261.386 1.00 48.89 N
ANISOU 1776 N GLN A 226 7193 7676 3707 872 1850 -546 N
ATOM 1777 CA GLN A 226 16.570 122.884 260.319 1.00 47.76 C
ANISOU 1777 CA GLN A 226 7041 7457 3648 816 1722 -538 C
ATOM 1778 C GLN A 226 17.077 124.333 260.427 1.00 48.54 C
ANISOU 1778 C GLN A 226 7253 7431 3761 841 1713 -652 C
ATOM 1779 O GLN A 226 18.264 124.622 260.131 1.00 48.00 O
ANISOU 1779 O GLN A 226 7241 7308 3689 765 1602 -688 O
ATOM 1780 CB GLN A 226 15.954 122.555 258.942 1.00 46.78 C
ANISOU 1780 CB GLN A 226 6765 7337 3672 828 1701 -425 C
ATOM 1781 CG GLN A 226 16.276 123.507 257.812 1.00 46.37 C
ANISOU 1781 CG GLN A 226 6700 7176 3743 837 1641 -431 C
ATOM 1782 CD GLN A 226 16.440 122.785 256.512 1.00 44.93 C
ANISOU 1782 CD GLN A 226 6405 7015 3650 784 1551 -325 C
ATOM 1783 OE1 GLN A 226 15.555 122.036 256.076 1.00 44.61 O
ANISOU 1783 OE1 GLN A 226 6250 7043 3657 801 1580 -233 O
ATOM 1784 NE2 GLN A 226 17.602 122.980 255.878 1.00 44.10 N
ANISOU 1784 NE2 GLN A 226 6334 6858 3564 714 1438 -337 N
ATOM 1785 N SER A 227 16.188 125.222 260.888 1.00 49.93 N
ANISOU 1785 N SER A 227 7462 7563 3948 944 1833 -709 N
ATOM 1786 CA SER A 227 16.513 126.625 261.000 1.00 50.88 C
ANISOU 1786 CA SER A 227 7696 7550 4087 978 1839 -818 C
ATOM 1787 C SER A 227 17.706 126.828 261.878 1.00 51.24 C
ANISOU 1787 C SER A 227 7891 7576 4003 899 1774 -922 C
ATOM 1788 O SER A 227 18.307 127.867 261.802 1.00 51.73 O
ANISOU 1788 O SER A 227 8048 7524 4084 885 1735 -1004 O
ATOM 1789 CB SER A 227 15.335 127.433 261.500 1.00 52.49 C
ANISOU 1789 CB SER A 227 7919 7719 4307 1113 1990 -868 C
ATOM 1790 OG SER A 227 15.084 127.238 262.898 1.00 53.67 O
ANISOU 1790 OG SER A 227 8152 7934 4308 1138 2082 -936 O
ATOM 1791 N GLU A 228 18.082 125.825 262.671 1.00 51.03 N
ANISOU 1791 N GLU A 228 7884 7658 3847 840 1752 -913 N
ATOM 1792 CA GLU A 228 19.207 125.968 263.633 1.00 51.55 C
ANISOU 1792 CA GLU A 228 8093 7721 3771 765 1685 -1012 C
ATOM 1793 C GLU A 228 20.506 125.382 263.116 1.00 50.22 C
ANISOU 1793 C GLU A 228 7902 7577 3603 646 1527 -975 C
ATOM 1794 O GLU A 228 21.547 125.536 263.778 1.00 50.61 O
ANISOU 1794 O GLU A 228 8055 7624 3549 575 1451 -1051 O
ATOM 1795 CB GLU A 228 18.910 125.355 265.033 1.00 52.50 C
ANISOU 1795 CB GLU A 228 8280 7946 3721 778 1759 -1043 C
ATOM 1796 CG GLU A 228 18.099 126.206 266.029 1.00 54.38 C
ANISOU 1796 CG GLU A 228 8619 8152 3891 876 1903 -1145 C
ATOM 1797 CD GLU A 228 18.822 127.490 266.475 1.00 55.51 C
ANISOU 1797 CD GLU A 228 8926 8173 3992 862 1871 -1294 C
ATOM 1798 OE1 GLU A 228 20.075 127.532 266.373 1.00 58.82 O
ANISOU 1798 OE1 GLU A 228 9396 8569 4384 756 1734 -1324 O
ATOM 1799 OE2 GLU A 228 18.150 128.462 266.916 1.00 56.99 O
ANISOU 1799 OE2 GLU A 228 9191 8288 4176 956 1983 -1381 O
ATOM 1800 N ASP A 229 20.439 124.719 261.958 1.00 48.78 N
ANISOU 1800 N ASP A 229 7585 7420 3530 627 1479 -860 N
ATOM 1801 CA ASP A 229 21.615 124.078 261.305 1.00 47.46 C
ANISOU 1801 CA ASP A 229 7375 7280 3378 526 1335 -811 C
ATOM 1802 C ASP A 229 22.701 125.093 261.018 1.00 47.63 C
ANISOU 1802 C ASP A 229 7467 7204 3426 465 1247 -888 C
ATOM 1803 O ASP A 229 22.412 126.249 260.850 1.00 48.38 O
ANISOU 1803 O ASP A 229 7610 7191 3580 504 1290 -946 O
ATOM 1804 CB ASP A 229 21.235 123.388 259.975 1.00 46.05 C
ANISOU 1804 CB ASP A 229 7046 7125 3327 528 1312 -684 C
ATOM 1805 CG ASP A 229 20.224 122.254 260.143 1.00 45.80 C
ANISOU 1805 CG ASP A 229 6932 7193 3278 567 1383 -594 C
ATOM 1806 OD1 ASP A 229 20.162 121.621 261.222 1.00 46.32 O
ANISOU 1806 OD1 ASP A 229 7046 7336 3218 561 1415 -606 O
ATOM 1807 OD2 ASP A 229 19.466 122.003 259.186 1.00 45.17 O
ANISOU 1807 OD2 ASP A 229 6739 7115 3309 598 1407 -508 O
ATOM 1808 N VAL A 230 23.943 124.645 260.956 1.00 47.01 N
ANISOU 1808 N VAL A 230 7391 7163 3306 370 1125 -886 N
ATOM 1809 CA VAL A 230 25.091 125.500 260.739 1.00 47.22 C
ANISOU 1809 CA VAL A 230 7476 7117 3349 292 1032 -955 C
ATOM 1810 C VAL A 230 25.614 125.148 259.355 1.00 45.81 C
ANISOU 1810 C VAL A 230 7182 6939 3286 245 950 -865 C
ATOM 1811 O VAL A 230 25.890 123.968 259.054 1.00 44.76 O
ANISOU 1811 O VAL A 230 6966 6901 3142 220 900 -783 O
ATOM 1812 CB VAL A 230 26.171 125.248 261.823 1.00 47.80 C
ANISOU 1812 CB VAL A 230 7637 7251 3275 216 952 -1025 C
ATOM 1813 CG1 VAL A 230 27.333 126.191 261.685 1.00 48.25 C
ANISOU 1813 CG1 VAL A 230 7754 7235 3345 126 857 -1104 C
ATOM 1814 CG2 VAL A 230 25.593 125.391 263.160 1.00 49.12 C
ANISOU 1814 CG2 VAL A 230 7912 7437 3315 265 1036 -1100 C
ATOM 1815 N CYS A 231 25.713 126.171 258.502 1.00 45.87 N
ANISOU 1815 N CYS A 231 7189 6836 3402 236 941 -878 N
ATOM 1816 CA CYS A 231 26.331 126.038 257.183 1.00 44.74 C
ANISOU 1816 CA CYS A 231 6954 6683 3361 182 863 -805 C
ATOM 1817 C CYS A 231 27.838 126.092 257.334 1.00 44.77 C
ANISOU 1817 C CYS A 231 6986 6708 3318 69 745 -849 C
ATOM 1818 O CYS A 231 28.373 127.049 257.897 1.00 45.86 O
ANISOU 1818 O CYS A 231 7226 6779 3419 24 725 -948 O
ATOM 1819 CB CYS A 231 25.916 127.176 256.275 1.00 44.98 C
ANISOU 1819 CB CYS A 231 6987 6586 3517 210 896 -802 C
ATOM 1820 SG CYS A 231 27.000 127.261 254.820 1.00 43.96 S
ANISOU 1820 SG CYS A 231 6780 6436 3487 115 788 -740 S
ATOM 1821 N LEU A 232 28.524 125.074 256.827 1.00 43.69 N
ANISOU 1821 N LEU A 232 6757 6663 3181 24 669 -778 N
ATOM 1822 CA LEU A 232 29.949 124.925 257.099 1.00 43.79 C
ANISOU 1822 CA LEU A 232 6778 6725 3135 -74 557 -813 C
ATOM 1823 C LEU A 232 30.790 125.526 256.022 1.00 43.49 C
ANISOU 1823 C LEU A 232 6697 6637 3192 -148 493 -799 C
ATOM 1824 O LEU A 232 31.914 125.971 256.277 1.00 44.07 O
ANISOU 1824 O LEU A 232 6802 6709 3234 -239 414 -857 O
ATOM 1825 CB LEU A 232 30.331 123.454 257.257 1.00 42.97 C
ANISOU 1825 CB LEU A 232 6605 6754 2969 -77 506 -747 C
ATOM 1826 CG LEU A 232 29.882 122.790 258.561 1.00 43.50 C
ANISOU 1826 CG LEU A 232 6731 6889 2906 -34 542 -769 C
ATOM 1827 CD1 LEU A 232 29.891 121.266 258.425 1.00 42.52 C
ANISOU 1827 CD1 LEU A 232 6528 6874 2756 -13 516 -673 C
ATOM 1828 CD2 LEU A 232 30.713 123.226 259.777 1.00 44.72 C
ANISOU 1828 CD2 LEU A 232 6991 7061 2940 -90 487 -873 C
ATOM 1829 N TYR A 233 30.225 125.542 254.817 1.00 42.68 N
ANISOU 1829 N TYR A 233 6521 6496 3201 -113 527 -720 N
ATOM 1830 CA TYR A 233 30.971 125.830 253.595 1.00 42.16 C
ANISOU 1830 CA TYR A 233 6389 6405 3225 -178 471 -677 C
ATOM 1831 C TYR A 233 30.057 126.303 252.496 1.00 41.79 C
ANISOU 1831 C TYR A 233 6310 6274 3293 -124 532 -616 C
ATOM 1832 O TYR A 233 29.128 125.582 252.152 1.00 41.07 O
ANISOU 1832 O TYR A 233 6160 6219 3225 -49 579 -546 O
ATOM 1833 CB TYR A 233 31.600 124.531 253.117 1.00 41.06 C
ANISOU 1833 CB TYR A 233 6143 6386 3072 -197 408 -602 C
ATOM 1834 CG TYR A 233 32.590 124.735 252.014 1.00 40.67 C
ANISOU 1834 CG TYR A 233 6026 6337 3091 -274 344 -567 C
ATOM 1835 CD1 TYR A 233 33.815 125.365 252.268 1.00 41.42 C
ANISOU 1835 CD1 TYR A 233 6145 6427 3165 -375 273 -629 C
ATOM 1836 CD2 TYR A 233 32.321 124.301 250.722 1.00 39.66 C
ANISOU 1836 CD2 TYR A 233 5808 6218 3044 -251 354 -474 C
ATOM 1837 CE1 TYR A 233 34.736 125.559 251.269 1.00 41.18 C
ANISOU 1837 CE1 TYR A 233 6045 6404 3196 -449 221 -594 C
ATOM 1838 CE2 TYR A 233 33.241 124.485 249.700 1.00 39.39 C
ANISOU 1838 CE2 TYR A 233 5712 6189 3064 -321 303 -441 C
ATOM 1839 CZ TYR A 233 34.447 125.117 249.979 1.00 40.15 C
ANISOU 1839 CZ TYR A 233 5829 6285 3142 -419 240 -500 C
ATOM 1840 OH TYR A 233 35.372 125.304 248.977 1.00 40.63 O
ANISOU 1840 OH TYR A 233 5822 6359 3256 -493 196 -465 O
ATOM 1841 N THR A 234 30.284 127.496 251.947 1.00 42.35 N
ANISOU 1841 N THR A 234 6420 6234 3435 -164 529 -638 N
ATOM 1842 CA THR A 234 29.630 127.884 250.666 1.00 41.91 C
ANISOU 1842 CA THR A 234 6320 6110 3495 -125 565 -560 C
ATOM 1843 C THR A 234 30.738 128.020 249.659 1.00 41.54 C
ANISOU 1843 C THR A 234 6221 6069 3495 -222 492 -523 C
ATOM 1844 O THR A 234 31.853 128.231 250.030 1.00 41.98 O
ANISOU 1844 O THR A 234 6298 6142 3511 -314 431 -575 O
ATOM 1845 CB THR A 234 28.860 129.222 250.730 1.00 42.98 C
ANISOU 1845 CB THR A 234 6548 6096 3686 -78 631 -602 C
ATOM 1846 OG1 THR A 234 28.126 129.311 251.952 1.00 43.74 O
ANISOU 1846 OG1 THR A 234 6720 6183 3717 -7 695 -672 O
ATOM 1847 CG2 THR A 234 27.880 129.320 249.640 1.00 42.52 C
ANISOU 1847 CG2 THR A 234 6433 5996 3726 -3 677 -512 C
ATOM 1848 N ASP A 235 30.456 127.804 248.394 1.00 40.75 N
ANISOU 1848 N ASP A 235 6043 5969 3471 -204 497 -430 N
ATOM 1849 CA ASP A 235 31.342 128.223 247.324 1.00 40.65 C
ANISOU 1849 CA ASP A 235 5995 5934 3514 -290 449 -392 C
ATOM 1850 C ASP A 235 30.450 129.122 246.519 1.00 40.93 C
ANISOU 1850 C ASP A 235 6059 5851 3642 -240 500 -349 C
ATOM 1851 O ASP A 235 29.334 128.770 246.202 1.00 40.49 O
ANISOU 1851 O ASP A 235 5970 5799 3616 -146 548 -296 O
ATOM 1852 CB ASP A 235 31.778 127.045 246.468 1.00 39.46 C
ANISOU 1852 CB ASP A 235 5728 5902 3363 -303 409 -311 C
ATOM 1853 CG ASP A 235 33.004 127.349 245.617 1.00 40.72 C
ANISOU 1853 CG ASP A 235 5847 6071 3552 -408 353 -290 C
ATOM 1854 OD1 ASP A 235 33.359 128.546 245.377 1.00 44.09 O
ANISOU 1854 OD1 ASP A 235 6330 6398 4023 -472 350 -313 O
ATOM 1855 OD2 ASP A 235 33.631 126.355 245.176 1.00 42.54 O
ANISOU 1855 OD2 ASP A 235 5989 6413 3762 -427 314 -248 O
ATOM 1856 N ASP A 236 30.903 130.323 246.242 1.00 41.82 N
ANISOU 1856 N ASP A 236 6237 5852 3799 -303 490 -374 N
ATOM 1857 CA ASP A 236 30.029 131.256 245.578 1.00 42.29 C
ANISOU 1857 CA ASP A 236 6339 5784 3944 -246 539 -336 C
ATOM 1858 C ASP A 236 30.271 131.271 244.072 1.00 41.75 C
ANISOU 1858 C ASP A 236 6204 5717 3942 -281 515 -233 C
ATOM 1859 O ASP A 236 29.474 131.832 243.297 1.00 41.94 O
ANISOU 1859 O ASP A 236 6240 5657 4038 -224 548 -173 O
ATOM 1860 CB ASP A 236 30.151 132.637 246.239 1.00 43.80 C
ANISOU 1860 CB ASP A 236 6667 5827 4147 -275 555 -425 C
ATOM 1861 CG ASP A 236 29.071 132.863 247.300 1.00 48.32 C
ANISOU 1861 CG ASP A 236 7313 6352 4695 -164 625 -490 C
ATOM 1862 OD1 ASP A 236 27.914 132.379 247.096 1.00 51.96 O
ANISOU 1862 OD1 ASP A 236 7722 6843 5179 -48 678 -436 O
ATOM 1863 OD2 ASP A 236 29.376 133.506 248.338 1.00 53.88 O
ANISOU 1863 OD2 ASP A 236 8124 6994 5353 -194 628 -597 O
ATOM 1864 N ASP A 237 31.365 130.617 243.680 1.00 41.13 N
ANISOU 1864 N ASP A 237 6053 5741 3835 -369 458 -212 N
ATOM 1865 CA ASP A 237 31.770 130.537 242.294 1.00 40.66 C
ANISOU 1865 CA ASP A 237 5928 5702 3820 -414 435 -121 C
ATOM 1866 C ASP A 237 30.888 129.587 241.463 1.00 39.58 C
ANISOU 1866 C ASP A 237 5706 5635 3699 -326 453 -30 C
ATOM 1867 O ASP A 237 30.969 128.351 241.587 1.00 38.67 O
ANISOU 1867 O ASP A 237 5517 5642 3535 -307 437 -19 O
ATOM 1868 CB ASP A 237 33.246 130.177 242.218 1.00 40.54 C
ANISOU 1868 CB ASP A 237 5860 5777 3766 -532 375 -137 C
ATOM 1869 CG ASP A 237 33.795 130.244 240.820 1.00 40.30 C
ANISOU 1869 CG ASP A 237 5772 5764 3777 -592 359 -52 C
ATOM 1870 OD1 ASP A 237 33.006 130.328 239.864 1.00 40.01 O
ANISOU 1870 OD1 ASP A 237 5725 5690 3787 -535 386 27 O
ATOM 1871 OD2 ASP A 237 35.030 130.187 240.699 1.00 40.47 O
ANISOU 1871 OD2 ASP A 237 5754 5845 3780 -696 317 -63 O
ATOM 1872 N PRO A 238 30.039 130.195 240.604 1.00 39.80 N
ANISOU 1872 N PRO A 238 5749 5577 3794 -274 482 36 N
ATOM 1873 CA PRO A 238 29.066 129.564 239.676 1.00 39.05 C
ANISOU 1873 CA PRO A 238 5586 5523 3727 -194 497 129 C
ATOM 1874 C PRO A 238 29.664 128.430 238.826 1.00 38.01 C
ANISOU 1874 C PRO A 238 5358 5520 3565 -234 457 186 C
ATOM 1875 O PRO A 238 28.946 127.525 238.388 1.00 37.26 O
ANISOU 1875 O PRO A 238 5200 5491 3464 -173 461 239 O
ATOM 1876 CB PRO A 238 28.619 130.731 238.780 1.00 39.80 C
ANISOU 1876 CB PRO A 238 5730 5492 3900 -179 512 188 C
ATOM 1877 CG PRO A 238 29.539 131.868 239.100 1.00 40.83 C
ANISOU 1877 CG PRO A 238 5949 5522 4042 -271 502 132 C
ATOM 1878 CD PRO A 238 30.008 131.663 240.482 1.00 40.99 C
ANISOU 1878 CD PRO A 238 5999 5572 4003 -297 499 24 C
ATOM 1879 N LEU A 239 30.980 128.461 238.642 1.00 38.07 N
ANISOU 1879 N LEU A 239 5353 5562 3549 -337 421 170 N
ATOM 1880 CA LEU A 239 31.648 127.325 238.056 1.00 37.20 C
ANISOU 1880 CA LEU A 239 5155 5581 3399 -368 389 204 C
ATOM 1881 C LEU A 239 31.749 126.103 238.969 1.00 36.54 C
ANISOU 1881 C LEU A 239 5031 5603 3250 -338 376 158 C
ATOM 1882 O LEU A 239 32.223 125.089 238.513 1.00 35.86 O
ANISOU 1882 O LEU A 239 4876 5617 3131 -348 352 185 O
ATOM 1883 CB LEU A 239 33.030 127.704 237.535 1.00 37.56 C
ANISOU 1883 CB LEU A 239 5185 5645 3442 -482 360 206 C
ATOM 1884 CG LEU A 239 33.155 128.759 236.432 1.00 38.19 C
ANISOU 1884 CG LEU A 239 5296 5639 3577 -533 368 268 C
ATOM 1885 CD1 LEU A 239 34.622 129.068 236.263 1.00 38.68 C
ANISOU 1885 CD1 LEU A 239 5337 5733 3625 -658 342 251 C
ATOM 1886 CD2 LEU A 239 32.477 128.364 235.105 1.00 37.65 C
ANISOU 1886 CD2 LEU A 239 5188 5593 3526 -483 376 368 C
ATOM 1887 N PHE A 240 31.315 126.151 240.231 1.00 36.80 N
ANISOU 1887 N PHE A 240 5109 5614 3259 -298 394 92 N
ATOM 1888 CA PHE A 240 31.634 125.038 241.121 1.00 36.32 C
ANISOU 1888 CA PHE A 240 5018 5655 3128 -287 374 51 C
ATOM 1889 C PHE A 240 30.457 124.383 241.816 1.00 36.00 C
ANISOU 1889 C PHE A 240 4982 5631 3067 -194 409 47 C
ATOM 1890 O PHE A 240 29.442 125.007 242.089 1.00 36.43 O
ANISOU 1890 O PHE A 240 5079 5608 3153 -138 454 42 O
ATOM 1891 CB PHE A 240 32.622 125.478 242.194 1.00 37.01 C
ANISOU 1891 CB PHE A 240 5147 5741 3175 -354 348 -37 C
ATOM 1892 CG PHE A 240 34.009 125.753 241.702 1.00 37.28 C
ANISOU 1892 CG PHE A 240 5150 5806 3211 -458 303 -39 C
ATOM 1893 CD1 PHE A 240 34.292 126.891 240.932 1.00 37.91 C
ANISOU 1893 CD1 PHE A 240 5256 5800 3348 -520 309 -17 C
ATOM 1894 CD2 PHE A 240 35.052 124.924 242.075 1.00 37.07 C
ANISOU 1894 CD2 PHE A 240 5067 5891 3128 -495 257 -63 C
ATOM 1895 CE1 PHE A 240 35.579 127.168 240.522 1.00 38.29 C
ANISOU 1895 CE1 PHE A 240 5269 5881 3397 -626 273 -17 C
ATOM 1896 CE2 PHE A 240 36.351 125.194 241.681 1.00 37.47 C
ANISOU 1896 CE2 PHE A 240 5075 5980 3181 -591 218 -67 C
ATOM 1897 CZ PHE A 240 36.610 126.314 240.898 1.00 38.07 C
ANISOU 1897 CZ PHE A 240 5173 5977 3315 -661 229 -44 C
ATOM 1898 N SER A 241 30.626 123.118 242.164 1.00 35.36 N
ANISOU 1898 N SER A 241 4856 5649 2930 -178 389 48 N
ATOM 1899 CA SER A 241 29.707 122.501 243.064 1.00 35.23 C
ANISOU 1899 CA SER A 241 4852 5654 2880 -109 421 34 C
ATOM 1900 C SER A 241 30.430 122.027 244.292 1.00 35.40 C
ANISOU 1900 C SER A 241 4896 5732 2822 -131 396 -32 C
ATOM 1901 O SER A 241 31.600 121.677 244.211 1.00 35.28 O
ANISOU 1901 O SER A 241 4853 5775 2777 -185 344 -44 O
ATOM 1902 CB SER A 241 29.102 121.327 242.369 1.00 34.39 C
ANISOU 1902 CB SER A 241 4681 5610 2776 -68 420 104 C
ATOM 1903 OG SER A 241 28.226 121.826 241.400 1.00 34.39 O
ANISOU 1903 OG SER A 241 4667 5556 2844 -38 445 162 O
ATOM 1904 N VAL A 242 29.745 121.993 245.430 1.00 35.75 N
ANISOU 1904 N VAL A 242 4987 5768 2829 -85 432 -73 N
ATOM 1905 CA VAL A 242 30.344 121.454 246.660 1.00 35.96 C
ANISOU 1905 CA VAL A 242 5042 5856 2767 -100 407 -130 C
ATOM 1906 C VAL A 242 30.001 119.951 246.845 1.00 35.27 C
ANISOU 1906 C VAL A 242 4913 5856 2634 -57 403 -87 C
ATOM 1907 O VAL A 242 28.904 119.493 246.491 1.00 34.89 O
ANISOU 1907 O VAL A 242 4840 5805 2613 -5 444 -34 O
ATOM 1908 CB VAL A 242 30.011 122.334 247.951 1.00 36.97 C
ANISOU 1908 CB VAL A 242 5263 5925 2858 -87 444 -214 C
ATOM 1909 CG1 VAL A 242 30.182 123.847 247.693 1.00 37.74 C
ANISOU 1909 CG1 VAL A 242 5414 5914 3013 -123 454 -253 C
ATOM 1910 CG2 VAL A 242 28.616 122.096 248.443 1.00 37.03 C
ANISOU 1910 CG2 VAL A 242 5287 5923 2861 -4 517 -201 C
ATOM 1911 N GLY A 243 30.958 119.188 247.376 1.00 35.20 N
ANISOU 1911 N GLY A 243 4896 5922 2557 -82 350 -106 N
ATOM 1912 CA GLY A 243 30.755 117.780 247.731 1.00 34.74 C
ANISOU 1912 CA GLY A 243 4818 5936 2444 -45 341 -72 C
ATOM 1913 C GLY A 243 31.020 117.555 249.218 1.00 35.44 C
ANISOU 1913 C GLY A 243 4965 6061 2439 -43 331 -127 C
ATOM 1914 O GLY A 243 31.531 118.464 249.915 1.00 36.65 O
ANISOU 1914 O GLY A 243 5169 6192 2565 -78 319 -197 O
ATOM 1915 N VAL A 244 30.681 116.358 249.723 1.00 35.09 N
ANISOU 1915 N VAL A 244 4922 6071 2339 -6 333 -95 N
ATOM 1916 CA VAL A 244 30.956 116.013 251.123 1.00 35.69 C
ANISOU 1916 CA VAL A 244 5056 6190 2313 -1 319 -136 C
ATOM 1917 C VAL A 244 30.994 114.513 251.400 1.00 35.35 C
ANISOU 1917 C VAL A 244 5003 6214 2215 28 294 -85 C
ATOM 1918 O VAL A 244 30.115 113.746 251.007 1.00 34.87 O
ANISOU 1918 O VAL A 244 4922 6151 2177 60 331 -24 O
ATOM 1919 CB VAL A 244 30.012 116.763 252.088 1.00 36.41 C
ANISOU 1919 CB VAL A 244 5220 6238 2376 22 391 -183 C
ATOM 1920 CG1 VAL A 244 28.607 116.200 252.041 1.00 36.15 C
ANISOU 1920 CG1 VAL A 244 5176 6199 2360 76 467 -127 C
ATOM 1921 CG2 VAL A 244 30.546 116.747 253.501 1.00 37.23 C
ANISOU 1921 CG2 VAL A 244 5396 6380 2369 9 366 -244 C
ATOM 1922 N GLY A 245 32.035 114.098 252.106 1.00 36.00 N
ANISOU 1922 N GLY A 245 5102 6354 2222 14 228 -109 N
ATOM 1923 CA GLY A 245 32.234 112.679 252.456 1.00 36.16 C
ANISOU 1923 CA GLY A 245 5123 6433 2182 45 195 -62 C
ATOM 1924 C GLY A 245 32.923 112.388 253.782 1.00 36.33 C
ANISOU 1924 C GLY A 245 5200 6511 2093 43 146 -95 C
ATOM 1925 O GLY A 245 33.497 113.274 254.408 1.00 37.01 O
ANISOU 1925 O GLY A 245 5316 6603 2144 9 120 -164 O
ATOM 1926 N ARG A 246 32.879 111.122 254.169 1.00 36.29 N
ANISOU 1926 N ARG A 246 5211 6546 2033 79 128 -44 N
ATOM 1927 CA ARG A 246 33.404 110.652 255.436 1.00 37.97 C
ANISOU 1927 CA ARG A 246 5482 6814 2131 88 81 -58 C
ATOM 1928 C ARG A 246 34.685 109.851 255.254 1.00 37.69 C
ANISOU 1928 C ARG A 246 5404 6838 2077 101 -16 -36 C
ATOM 1929 O ARG A 246 34.773 109.040 254.326 1.00 36.81 O
ANISOU 1929 O ARG A 246 5243 6723 2019 127 -27 19 O
ATOM 1930 CB ARG A 246 32.361 109.766 256.106 1.00 38.63 C
ANISOU 1930 CB ARG A 246 5625 6896 2158 123 137 -7 C
ATOM 1931 CG ARG A 246 32.423 109.869 257.597 1.00 43.10 C
ANISOU 1931 CG ARG A 246 6278 7499 2600 122 132 -43 C
ATOM 1932 CD ARG A 246 31.535 108.838 258.288 1.00 48.73 C
ANISOU 1932 CD ARG A 246 7049 8220 3245 153 180 20 C
ATOM 1933 NE ARG A 246 31.435 109.160 259.715 1.00 51.29 N
ANISOU 1933 NE ARG A 246 7465 8576 3448 149 195 -22 N
ATOM 1934 CZ ARG A 246 31.205 108.273 260.676 1.00 54.49 C
ANISOU 1934 CZ ARG A 246 7940 9016 3748 168 200 21 C
ATOM 1935 NH1 ARG A 246 31.073 106.976 260.397 1.00 55.38 N
ANISOU 1935 NH1 ARG A 246 8046 9131 3866 193 186 109 N
ATOM 1936 NH2 ARG A 246 31.114 108.690 261.927 1.00 56.07 N
ANISOU 1936 NH2 ARG A 246 8225 9246 3833 162 217 -25 N
ATOM 1937 N SER A 247 35.666 110.051 256.147 1.00 38.15 N
ANISOU 1937 N SER A 247 5484 6954 2057 86 -89 -79 N
ATOM 1938 CA SER A 247 36.938 109.313 256.049 1.00 38.09 C
ANISOU 1938 CA SER A 247 5427 7016 2031 106 -186 -58 C
ATOM 1939 C SER A 247 36.749 107.860 256.442 1.00 38.31 C
ANISOU 1939 C SER A 247 5494 7062 2002 168 -200 15 C
ATOM 1940 O SER A 247 35.791 107.514 257.158 1.00 39.27 O
ANISOU 1940 O SER A 247 5693 7160 2067 182 -148 38 O
ATOM 1941 CB SER A 247 38.016 109.948 256.912 1.00 39.09 C
ANISOU 1941 CB SER A 247 5558 7204 2089 68 -267 -121 C
ATOM 1942 OG SER A 247 37.647 110.001 258.279 1.00 39.90 O
ANISOU 1942 OG SER A 247 5761 7321 2079 68 -263 -145 O
ATOM 1943 N GLY A 248 37.658 107.005 256.002 1.00 38.24 N
ANISOU 1943 N GLY A 248 5432 7093 2005 208 -269 52 N
ATOM 1944 CA GLY A 248 37.529 105.586 256.285 1.00 39.53 C
ANISOU 1944 CA GLY A 248 5637 7260 2122 271 -286 125 C
ATOM 1945 C GLY A 248 37.280 105.316 257.750 1.00 41.13 C
ANISOU 1945 C GLY A 248 5938 7487 2201 280 -297 131 C
ATOM 1946 O GLY A 248 36.300 104.675 258.123 1.00 41.68 O
ANISOU 1946 O GLY A 248 6080 7519 2236 296 -242 179 O
ATOM 1947 N ASP A 249 38.163 105.835 258.590 1.00 42.63 N
ANISOU 1947 N ASP A 249 6133 7743 2320 262 -369 83 N
ATOM 1948 CA ASP A 249 38.022 105.693 260.019 1.00 44.31 C
ANISOU 1948 CA ASP A 249 6445 7990 2403 264 -387 81 C
ATOM 1949 C ASP A 249 36.880 106.544 260.607 1.00 44.41 C
ANISOU 1949 C ASP A 249 6532 7962 2382 219 -292 38 C
ATOM 1950 O ASP A 249 36.542 106.428 261.797 1.00 45.48 O
ANISOU 1950 O ASP A 249 6761 8118 2401 221 -283 38 O
ATOM 1951 CB ASP A 249 39.363 105.992 260.707 1.00 45.79 C
ANISOU 1951 CB ASP A 249 6610 8267 2521 256 -504 40 C
ATOM 1952 CG ASP A 249 39.749 107.470 260.657 1.00 48.07 C
ANISOU 1952 CG ASP A 249 6861 8568 2836 178 -512 -57 C
ATOM 1953 OD1 ASP A 249 39.118 108.268 259.891 1.00 49.17 O
ANISOU 1953 OD1 ASP A 249 6976 8643 3065 139 -433 -88 O
ATOM 1954 OD2 ASP A 249 40.714 107.818 261.391 1.00 50.35 O
ANISOU 1954 OD2 ASP A 249 7145 8932 3055 154 -605 -98 O
ATOM 1955 N GLY A 250 36.299 107.408 259.787 1.00 43.30 N
ANISOU 1955 N GLY A 250 6350 7764 2337 184 -220 3 N
ATOM 1956 CA GLY A 250 35.103 108.131 260.201 1.00 44.06 C
ANISOU 1956 CA GLY A 250 6507 7814 2419 158 -118 -30 C
ATOM 1957 C GLY A 250 35.326 109.273 261.182 1.00 44.81 C
ANISOU 1957 C GLY A 250 6658 7931 2437 115 -127 -121 C
ATOM 1958 O GLY A 250 34.377 109.888 261.648 1.00 44.62 O
ANISOU 1958 O GLY A 250 6694 7871 2387 103 -41 -155 O
ATOM 1959 N LYS A 251 36.589 109.561 261.458 1.00 45.83 N
ANISOU 1959 N LYS A 251 6765 8118 2532 92 -233 -163 N
ATOM 1960 CA LYS A 251 37.000 110.634 262.343 1.00 47.45 C
ANISOU 1960 CA LYS A 251 7020 8347 2662 41 -264 -256 C
ATOM 1961 C LYS A 251 37.224 111.982 261.621 1.00 47.13 C
ANISOU 1961 C LYS A 251 6929 8259 2717 -20 -253 -332 C
ATOM 1962 O LYS A 251 37.416 113.030 262.258 1.00 48.26 O
ANISOU 1962 O LYS A 251 7124 8398 2813 -72 -264 -419 O
ATOM 1963 CB LYS A 251 38.268 110.180 263.069 1.00 48.76 C
ANISOU 1963 CB LYS A 251 7185 8609 2734 42 -396 -255 C
ATOM 1964 CG LYS A 251 37.998 109.348 264.366 1.00 52.66 C
ANISOU 1964 CG LYS A 251 7785 9146 3075 81 -408 -217 C
ATOM 1965 CD LYS A 251 37.841 107.834 264.120 1.00 55.31 C
ANISOU 1965 CD LYS A 251 8111 9489 3416 153 -412 -103 C
ATOM 1966 CE LYS A 251 39.201 107.101 264.122 1.00 56.99 C
ANISOU 1966 CE LYS A 251 8266 9779 3608 185 -548 -67 C
ATOM 1967 NZ LYS A 251 40.063 107.340 265.340 1.00 58.39 N
ANISOU 1967 NZ LYS A 251 8490 10044 3649 166 -653 -108 N
ATOM 1968 N THR A 252 37.176 111.945 260.290 1.00 45.71 N
ANISOU 1968 N THR A 252 6658 8042 2669 -15 -229 -297 N
ATOM 1969 CA THR A 252 37.516 113.084 259.449 1.00 45.03 C
ANISOU 1969 CA THR A 252 6513 7914 2681 -72 -227 -350 C
ATOM 1970 C THR A 252 36.410 113.260 258.424 1.00 43.40 C
ANISOU 1970 C THR A 252 6283 7622 2583 -53 -123 -318 C
ATOM 1971 O THR A 252 35.952 112.282 257.827 1.00 43.20 O
ANISOU 1971 O THR A 252 6225 7593 2596 -4 -95 -241 O
ATOM 1972 CB THR A 252 38.872 112.851 258.678 1.00 45.14 C
ANISOU 1972 CB THR A 252 6413 7986 2751 -90 -325 -333 C
ATOM 1973 OG1 THR A 252 39.863 112.269 259.553 1.00 46.24 O
ANISOU 1973 OG1 THR A 252 6556 8221 2792 -82 -430 -332 O
ATOM 1974 CG2 THR A 252 39.401 114.155 258.032 1.00 44.37 C
ANISOU 1974 CG2 THR A 252 6268 7858 2734 -169 -335 -396 C
ATOM 1975 N LEU A 253 35.993 114.510 258.216 1.00 42.54 N
ANISOU 1975 N LEU A 253 6195 7445 2524 -92 -70 -378 N
ATOM 1976 CA LEU A 253 35.007 114.852 257.187 1.00 40.24 C
ANISOU 1976 CA LEU A 253 5875 7073 2342 -76 20 -351 C
ATOM 1977 C LEU A 253 35.670 115.634 256.072 1.00 39.51 C
ANISOU 1977 C LEU A 253 5707 6951 2353 -126 -7 -367 C
ATOM 1978 O LEU A 253 36.566 116.439 256.302 1.00 39.90 O
ANISOU 1978 O LEU A 253 5759 7010 2392 -188 -64 -430 O
ATOM 1979 CB LEU A 253 33.875 115.685 257.781 1.00 40.50 C
ANISOU 1979 CB LEU A 253 5991 7039 2356 -68 114 -399 C
ATOM 1980 CG LEU A 253 32.553 115.827 257.033 1.00 39.33 C
ANISOU 1980 CG LEU A 253 5825 6821 2296 -29 219 -359 C
ATOM 1981 CD1 LEU A 253 31.737 114.571 257.178 1.00 38.91 C
ANISOU 1981 CD1 LEU A 253 5770 6799 2215 25 260 -280 C
ATOM 1982 CD2 LEU A 253 31.775 117.026 257.560 1.00 40.04 C
ANISOU 1982 CD2 LEU A 253 5991 6843 2381 -28 296 -430 C
ATOM 1983 N ILE A 254 35.195 115.393 254.855 1.00 38.49 N
ANISOU 1983 N ILE A 254 5516 6786 2322 -104 34 -308 N
ATOM 1984 CA ILE A 254 35.864 115.872 253.639 1.00 37.86 C
ANISOU 1984 CA ILE A 254 5355 6692 2337 -145 8 -301 C
ATOM 1985 C ILE A 254 34.931 116.769 252.824 1.00 37.48 C
ANISOU 1985 C ILE A 254 5311 6549 2382 -148 87 -299 C
ATOM 1986 O ILE A 254 33.920 116.324 252.302 1.00 36.82 O
ANISOU 1986 O ILE A 254 5216 6437 2338 -100 147 -244 O
ATOM 1987 CB ILE A 254 36.504 114.685 252.828 1.00 37.19 C
ANISOU 1987 CB ILE A 254 5182 6671 2276 -117 -39 -231 C
ATOM 1988 CG1 ILE A 254 37.532 113.968 253.737 1.00 37.81 C
ANISOU 1988 CG1 ILE A 254 5261 6842 2263 -111 -126 -240 C
ATOM 1989 CG2 ILE A 254 37.154 115.183 251.550 1.00 36.84 C
ANISOU 1989 CG2 ILE A 254 5056 6618 2325 -158 -54 -222 C
ATOM 1990 CD1 ILE A 254 37.912 112.542 253.321 1.00 37.58 C
ANISOU 1990 CD1 ILE A 254 5178 6870 2230 -53 -162 -170 C
ATOM 1991 N ILE A 255 35.273 118.045 252.753 1.00 38.03 N
ANISOU 1991 N ILE A 255 5398 6568 2483 -207 83 -358 N
ATOM 1992 CA ILE A 255 34.470 118.991 252.020 1.00 37.85 C
ANISOU 1992 CA ILE A 255 5387 6448 2547 -208 151 -356 C
ATOM 1993 C ILE A 255 35.243 119.373 250.779 1.00 37.54 C
ANISOU 1993 C ILE A 255 5273 6402 2589 -260 119 -332 C
ATOM 1994 O ILE A 255 36.434 119.660 250.880 1.00 38.03 O
ANISOU 1994 O ILE A 255 5310 6503 2637 -325 52 -366 O
ATOM 1995 CB ILE A 255 34.234 120.201 252.877 1.00 38.85 C
ANISOU 1995 CB ILE A 255 5607 6507 2647 -235 177 -441 C
ATOM 1996 CG1 ILE A 255 33.181 119.843 253.916 1.00 39.10 C
ANISOU 1996 CG1 ILE A 255 5710 6538 2608 -169 238 -453 C
ATOM 1997 CG2 ILE A 255 33.825 121.384 252.029 1.00 38.90 C
ANISOU 1997 CG2 ILE A 255 5622 6408 2752 -254 222 -447 C
ATOM 1998 CD1 ILE A 255 32.776 120.974 254.710 1.00 40.10 C
ANISOU 1998 CD1 ILE A 255 5934 6592 2708 -177 280 -536 C
ATOM 1999 N CYS A 256 34.617 119.381 249.603 1.00 36.82 N
ANISOU 1999 N CYS A 256 5141 6269 2581 -236 163 -273 N
ATOM 2000 CA CYS A 256 35.362 119.808 248.445 1.00 36.65 C
ANISOU 2000 CA CYS A 256 5057 6241 2628 -289 137 -251 C
ATOM 2001 C CYS A 256 34.583 120.708 247.506 1.00 36.50 C
ANISOU 2001 C CYS A 256 5048 6125 2697 -289 194 -226 C
ATOM 2002 O CYS A 256 33.407 120.902 247.666 1.00 36.44 O
ANISOU 2002 O CYS A 256 5083 6060 2704 -236 254 -219 O
ATOM 2003 CB CYS A 256 35.830 118.574 247.728 1.00 35.91 C
ANISOU 2003 CB CYS A 256 4879 6231 2535 -265 106 -188 C
ATOM 2004 SG CYS A 256 34.500 117.748 246.921 1.00 34.93 S
ANISOU 2004 SG CYS A 256 4739 6083 2448 -187 165 -110 S
ATOM 2005 N SER A 257 35.269 121.247 246.513 1.00 36.52 N
ANISOU 2005 N SER A 257 5007 6114 2756 -347 175 -207 N
ATOM 2006 CA SER A 257 34.690 122.054 245.442 1.00 36.41 C
ANISOU 2006 CA SER A 257 4995 6014 2824 -351 218 -169 C
ATOM 2007 C SER A 257 35.219 121.478 244.157 1.00 35.78 C
ANISOU 2007 C SER A 257 4828 5989 2777 -364 198 -102 C
ATOM 2008 O SER A 257 36.384 121.089 244.091 1.00 35.86 O
ANISOU 2008 O SER A 257 4784 6078 2763 -407 149 -109 O
ATOM 2009 CB SER A 257 35.154 123.514 245.544 1.00 37.37 C
ANISOU 2009 CB SER A 257 5169 6052 2978 -429 213 -220 C
ATOM 2010 OG SER A 257 34.224 124.309 246.259 1.00 37.92 O
ANISOU 2010 OG SER A 257 5332 6027 3051 -396 260 -265 O
ATOM 2011 N MET A 258 34.383 121.409 243.134 1.00 35.23 N
ANISOU 2011 N MET A 258 4744 5885 2759 -326 236 -38 N
ATOM 2012 CA MET A 258 34.747 120.734 241.915 1.00 34.63 C
ANISOU 2012 CA MET A 258 4594 5863 2701 -327 223 25 C
ATOM 2013 C MET A 258 34.170 121.555 240.816 1.00 34.64 C
ANISOU 2013 C MET A 258 4604 5788 2771 -335 256 72 C
ATOM 2014 O MET A 258 32.953 121.667 240.630 1.00 34.44 O
ANISOU 2014 O MET A 258 4605 5708 2774 -280 294 102 O
ATOM 2015 CB MET A 258 34.121 119.326 241.814 1.00 33.83 C
ANISOU 2015 CB MET A 258 4465 5817 2571 -253 228 65 C
ATOM 2016 CG MET A 258 34.479 118.297 242.917 1.00 39.21 C
ANISOU 2016 CG MET A 258 5147 6571 3180 -225 198 33 C
ATOM 2017 SD MET A 258 33.087 117.453 243.828 1.00 50.41 S
ANISOU 2017 SD MET A 258 6611 7982 4562 -144 233 41 S
ATOM 2018 CE MET A 258 31.600 118.503 243.674 1.00 45.65 C
ANISOU 2018 CE MET A 258 6051 7275 4019 -118 301 52 C
ATOM 2019 N SER A 259 35.053 122.180 240.082 1.00 34.99 N
ANISOU 2019 N SER A 259 4625 5829 2842 -407 242 83 N
ATOM 2020 CA SER A 259 34.661 122.643 238.790 1.00 34.90 C
ANISOU 2020 CA SER A 259 4606 5771 2882 -412 266 149 C
ATOM 2021 C SER A 259 35.309 121.639 237.893 1.00 34.37 C
ANISOU 2021 C SER A 259 4464 5803 2793 -414 247 190 C
ATOM 2022 O SER A 259 35.899 120.637 238.343 1.00 34.10 O
ANISOU 2022 O SER A 259 4390 5857 2711 -399 220 168 O
ATOM 2023 CB SER A 259 35.114 124.068 238.499 1.00 35.75 C
ANISOU 2023 CB SER A 259 4751 5798 3036 -491 271 142 C
ATOM 2024 OG SER A 259 36.408 124.078 237.984 1.00 36.01 O
ANISOU 2024 OG SER A 259 4728 5893 3060 -571 246 148 O
ATOM 2025 N SER A 260 35.149 121.902 236.609 1.00 34.29 N
ANISOU 2025 N SER A 260 4439 5775 2816 -426 263 253 N
ATOM 2026 CA SER A 260 35.402 120.904 235.610 1.00 33.76 C
ANISOU 2026 CA SER A 260 4314 5787 2726 -408 257 299 C
ATOM 2027 C SER A 260 36.900 120.730 235.528 1.00 34.09 C
ANISOU 2027 C SER A 260 4297 5912 2743 -467 235 277 C
ATOM 2028 O SER A 260 37.378 119.612 235.352 1.00 33.72 O
ANISOU 2028 O SER A 260 4200 5955 2658 -437 221 279 O
ATOM 2029 CB SER A 260 34.794 121.327 234.295 1.00 33.73 C
ANISOU 2029 CB SER A 260 4320 5740 2756 -407 279 370 C
ATOM 2030 OG SER A 260 35.149 120.414 233.305 1.00 33.35 O
ANISOU 2030 OG SER A 260 4223 5770 2678 -397 274 407 O
ATOM 2031 N GLU A 261 37.638 121.816 235.751 1.00 34.87 N
ANISOU 2031 N GLU A 261 4403 5982 2864 -550 231 253 N
ATOM 2032 CA GLU A 261 39.085 121.735 235.685 1.00 35.34 C
ANISOU 2032 CA GLU A 261 4393 6128 2905 -616 210 234 C
ATOM 2033 C GLU A 261 39.889 122.177 236.894 1.00 36.01 C
ANISOU 2033 C GLU A 261 4477 6226 2980 -672 176 164 C
ATOM 2034 O GLU A 261 41.051 122.504 236.738 1.00 36.67 O
ANISOU 2034 O GLU A 261 4504 6363 3065 -752 160 155 O
ATOM 2035 CB GLU A 261 39.611 122.385 234.405 1.00 35.79 C
ANISOU 2035 CB GLU A 261 4423 6185 2988 -685 234 288 C
ATOM 2036 CG GLU A 261 39.108 123.770 234.048 1.00 38.15 C
ANISOU 2036 CG GLU A 261 4793 6363 3340 -738 257 315 C
ATOM 2037 CD GLU A 261 39.276 124.039 232.549 1.00 41.94 C
ANISOU 2037 CD GLU A 261 5254 6849 3832 -772 286 392 C
ATOM 2038 OE1 GLU A 261 39.171 123.061 231.770 1.00 43.75 O
ANISOU 2038 OE1 GLU A 261 5443 7151 4029 -719 294 427 O
ATOM 2039 OE2 GLU A 261 39.521 125.201 232.144 1.00 44.32 O
ANISOU 2039 OE2 GLU A 261 5587 7084 4170 -854 300 418 O
ATOM 2040 N THR A 262 39.286 122.102 238.087 1.00 35.90 N
ANISOU 2040 N THR A 262 4518 6174 2948 -631 163 115 N
ATOM 2041 CA THR A 262 39.815 122.687 239.334 1.00 36.64 C
ANISOU 2041 CA THR A 262 4638 6256 3026 -685 129 42 C
ATOM 2042 C THR A 262 39.135 122.138 240.568 1.00 36.34 C
ANISOU 2042 C THR A 262 4649 6212 2945 -613 119 -2 C
ATOM 2043 O THR A 262 37.922 121.999 240.595 1.00 35.83 O
ANISOU 2043 O THR A 262 4636 6089 2890 -543 152 15 O
ATOM 2044 CB THR A 262 39.594 124.195 239.380 1.00 37.41 C
ANISOU 2044 CB THR A 262 4811 6232 3172 -757 146 26 C
ATOM 2045 OG1 THR A 262 39.684 124.757 238.044 1.00 37.55 O
ANISOU 2045 OG1 THR A 262 4812 6217 3236 -800 176 91 O
ATOM 2046 CG2 THR A 262 40.591 124.847 240.313 1.00 38.42 C
ANISOU 2046 CG2 THR A 262 4943 6370 3285 -850 103 -45 C
ATOM 2047 N SER A 263 39.931 121.874 241.607 1.00 36.77 N
ANISOU 2047 N SER A 263 4686 6331 2953 -635 71 -58 N
ATOM 2048 CA SER A 263 39.462 121.266 242.864 1.00 36.61 C
ANISOU 2048 CA SER A 263 4710 6324 2876 -572 55 -100 C
ATOM 2049 C SER A 263 39.930 122.012 244.079 1.00 37.56 C
ANISOU 2049 C SER A 263 4877 6427 2966 -633 19 -179 C
ATOM 2050 O SER A 263 40.890 122.759 244.012 1.00 38.35 O
ANISOU 2050 O SER A 263 4953 6536 3082 -729 -11 -203 O
ATOM 2051 CB SER A 263 39.962 119.831 242.992 1.00 36.17 C
ANISOU 2051 CB SER A 263 4586 6385 2771 -515 21 -84 C
ATOM 2052 OG SER A 263 39.369 119.008 242.006 1.00 35.65 O
ANISOU 2052 OG SER A 263 4496 6326 2722 -448 54 -20 O
ATOM 2053 N GLU A 264 39.244 121.793 245.195 1.00 37.55 N
ANISOU 2053 N GLU A 264 4946 6404 2917 -581 22 -218 N
ATOM 2054 CA GLU A 264 39.680 122.255 246.494 1.00 38.45 C
ANISOU 2054 CA GLU A 264 5112 6521 2979 -626 -20 -298 C
ATOM 2055 C GLU A 264 39.016 121.375 247.555 1.00 38.17 C
ANISOU 2055 C GLU A 264 5120 6512 2869 -540 -17 -314 C
ATOM 2056 O GLU A 264 37.861 120.981 247.405 1.00 37.49 O
ANISOU 2056 O GLU A 264 5065 6387 2793 -462 38 -279 O
ATOM 2057 CB GLU A 264 39.323 123.724 246.701 1.00 39.23 C
ANISOU 2057 CB GLU A 264 5301 6494 3112 -685 7 -346 C
ATOM 2058 CG GLU A 264 40.079 124.363 247.858 1.00 40.41 C
ANISOU 2058 CG GLU A 264 5496 6647 3210 -764 -49 -435 C
ATOM 2059 CD GLU A 264 39.818 125.848 248.008 1.00 41.56 C
ANISOU 2059 CD GLU A 264 5742 6658 3393 -830 -25 -487 C
ATOM 2060 OE1 GLU A 264 38.825 126.203 248.693 1.00 42.46 O
ANISOU 2060 OE1 GLU A 264 5957 6687 3487 -777 19 -527 O
ATOM 2061 OE2 GLU A 264 40.628 126.654 247.478 1.00 41.98 O
ANISOU 2061 OE2 GLU A 264 5771 6687 3492 -935 -49 -491 O
ATOM 2062 N SER A 265 39.756 121.083 248.625 1.00 38.77 N
ANISOU 2062 N SER A 265 5199 6661 2872 -560 -79 -362 N
ATOM 2063 CA SER A 265 39.272 120.251 249.706 1.00 38.67 C
ANISOU 2063 CA SER A 265 5233 6683 2778 -489 -84 -376 C
ATOM 2064 C SER A 265 39.501 120.940 251.013 1.00 39.76 C
ANISOU 2064 C SER A 265 5451 6806 2848 -536 -116 -462 C
ATOM 2065 O SER A 265 40.351 121.796 251.117 1.00 40.61 O
ANISOU 2065 O SER A 265 5555 6909 2964 -629 -161 -510 O
ATOM 2066 CB SER A 265 40.017 118.917 249.732 1.00 38.37 C
ANISOU 2066 CB SER A 265 5115 6767 2698 -450 -139 -338 C
ATOM 2067 OG SER A 265 39.435 117.977 248.831 1.00 37.33 O
ANISOU 2067 OG SER A 265 4944 6641 2600 -376 -99 -262 O
ATOM 2068 N HIS A 266 38.725 120.548 252.014 1.00 39.80 N
ANISOU 2068 N HIS A 266 5533 6806 2783 -474 -93 -482 N
ATOM 2069 CA HIS A 266 38.967 120.895 253.391 1.00 40.84 C
ANISOU 2069 CA HIS A 266 5745 6951 2823 -503 -130 -562 C
ATOM 2070 C HIS A 266 38.663 119.686 254.219 1.00 40.63 C
ANISOU 2070 C HIS A 266 5736 6996 2706 -426 -139 -538 C
ATOM 2071 O HIS A 266 37.959 118.778 253.776 1.00 39.70 O
ANISOU 2071 O HIS A 266 5593 6886 2607 -349 -94 -469 O
ATOM 2072 CB HIS A 266 38.046 122.013 253.820 1.00 41.37 C
ANISOU 2072 CB HIS A 266 5925 6898 2895 -508 -63 -621 C
ATOM 2073 CG HIS A 266 38.043 123.170 252.874 1.00 42.25 C
ANISOU 2073 CG HIS A 266 6034 6911 3108 -565 -35 -627 C
ATOM 2074 ND1 HIS A 266 38.685 124.361 253.154 1.00 43.92 N
ANISOU 2074 ND1 HIS A 266 6293 7069 3324 -664 -70 -702 N
ATOM 2075 CD2 HIS A 266 37.489 123.312 251.644 1.00 41.48 C
ANISOU 2075 CD2 HIS A 266 5896 6756 3107 -539 20 -563 C
ATOM 2076 CE1 HIS A 266 38.500 125.197 252.146 1.00 45.08 C
ANISOU 2076 CE1 HIS A 266 6435 7124 3569 -695 -31 -681 C
ATOM 2077 NE2 HIS A 266 37.794 124.579 251.211 1.00 44.21 N
ANISOU 2077 NE2 HIS A 266 6269 7014 3514 -619 22 -595 N
ATOM 2078 N LEU A 267 39.175 119.731 255.445 1.00 41.61 N
ANISOU 2078 N LEU A 267 5912 7168 2729 -452 -197 -598 N
ATOM 2079 CA LEU A 267 38.983 118.722 256.441 1.00 41.72 C
ANISOU 2079 CA LEU A 267 5963 7250 2639 -391 -215 -585 C
ATOM 2080 C LEU A 267 38.336 119.294 257.694 1.00 42.61 C
ANISOU 2080 C LEU A 267 6207 7320 2662 -391 -181 -660 C
ATOM 2081 O LEU A 267 38.655 120.412 258.117 1.00 43.71 O
ANISOU 2081 O LEU A 267 6403 7417 2786 -462 -200 -744 O
ATOM 2082 CB LEU A 267 40.334 118.168 256.828 1.00 42.28 C
ANISOU 2082 CB LEU A 267 5972 7437 2653 -421 -330 -586 C
ATOM 2083 CG LEU A 267 41.162 117.503 255.732 1.00 41.64 C
ANISOU 2083 CG LEU A 267 5757 7420 2644 -414 -372 -519 C
ATOM 2084 CD1 LEU A 267 42.422 116.912 256.391 1.00 42.44 C
ANISOU 2084 CD1 LEU A 267 5807 7647 2672 -427 -488 -524 C
ATOM 2085 CD2 LEU A 267 40.345 116.446 254.918 1.00 40.36 C
ANISOU 2085 CD2 LEU A 267 5564 7244 2529 -321 -306 -429 C
ATOM 2086 N LEU A 268 37.448 118.502 258.304 1.00 42.39 N
ANISOU 2086 N LEU A 268 6230 7306 2569 -313 -131 -629 N
ATOM 2087 CA LEU A 268 36.887 118.778 259.624 1.00 43.32 C
ANISOU 2087 CA LEU A 268 6470 7412 2576 -300 -100 -691 C
ATOM 2088 C LEU A 268 37.040 117.584 260.578 1.00 43.75 C
ANISOU 2088 C LEU A 268 6549 7565 2510 -256 -142 -656 C
ATOM 2089 O LEU A 268 36.720 116.437 260.236 1.00 42.76 O
ANISOU 2089 O LEU A 268 6378 7473 2396 -194 -126 -568 O
ATOM 2090 CB LEU A 268 35.417 119.103 259.469 1.00 42.96 C
ANISOU 2090 CB LEU A 268 6475 7277 2570 -243 29 -684 C
ATOM 2091 CG LEU A 268 34.685 119.697 260.667 1.00 44.00 C
ANISOU 2091 CG LEU A 268 6738 7374 2609 -228 90 -760 C
ATOM 2092 CD1 LEU A 268 35.004 121.183 260.847 1.00 45.89 C
ANISOU 2092 CD1 LEU A 268 7043 7532 2860 -296 82 -867 C
ATOM 2093 CD2 LEU A 268 33.203 119.486 260.507 1.00 43.50 C
ANISOU 2093 CD2 LEU A 268 6689 7263 2577 -147 217 -718 C
ATOM 2094 N ASP A 269 37.507 117.869 261.791 1.00 45.77 N
ANISOU 2094 N ASP A 269 6885 7861 2643 -290 -197 -726 N
ATOM 2095 CA ASP A 269 37.689 116.832 262.814 1.00 46.82 C
ANISOU 2095 CA ASP A 269 7057 8086 2645 -253 -243 -696 C
ATOM 2096 C ASP A 269 36.394 116.478 263.515 1.00 46.79 C
ANISOU 2096 C ASP A 269 7147 8059 2571 -188 -138 -680 C
ATOM 2097 O ASP A 269 35.820 117.310 264.227 1.00 48.38 O
ANISOU 2097 O ASP A 269 7450 8216 2718 -198 -79 -757 O
ATOM 2098 CB ASP A 269 38.709 117.259 263.874 1.00 48.38 C
ANISOU 2098 CB ASP A 269 7307 8347 2727 -317 -351 -776 C
ATOM 2099 CG ASP A 269 39.081 116.115 264.824 1.00 50.80 C
ANISOU 2099 CG ASP A 269 7639 8761 2903 -277 -421 -731 C
ATOM 2100 OD1 ASP A 269 38.542 114.984 264.639 1.00 50.30 O
ANISOU 2100 OD1 ASP A 269 7556 8713 2842 -201 -381 -637 O
ATOM 2101 OD2 ASP A 269 39.921 116.348 265.747 1.00 52.93 O
ANISOU 2101 OD2 ASP A 269 7950 9096 3064 -325 -521 -787 O
ATOM 2102 N LEU A 270 35.964 115.230 263.356 1.00 45.64 N
ANISOU 2102 N LEU A 270 6971 7948 2423 -123 -114 -582 N
ATOM 2103 CA LEU A 270 34.742 114.767 263.993 1.00 45.12 C
ANISOU 2103 CA LEU A 270 6981 7871 2292 -67 -12 -553 C
ATOM 2104 C LEU A 270 34.989 114.264 265.446 1.00 46.88 C
ANISOU 2104 C LEU A 270 7303 8172 2338 -60 -56 -564 C
ATOM 2105 O LEU A 270 34.063 113.912 266.196 1.00 47.23 O
ANISOU 2105 O LEU A 270 7426 8221 2299 -22 26 -545 O
ATOM 2106 CB LEU A 270 34.047 113.737 263.088 1.00 43.51 C
ANISOU 2106 CB LEU A 270 6705 7653 2175 -13 42 -443 C
ATOM 2107 CG LEU A 270 33.579 114.116 261.654 1.00 42.36 C
ANISOU 2107 CG LEU A 270 6469 7432 2193 -10 97 -420 C
ATOM 2108 CD1 LEU A 270 33.087 112.898 260.910 1.00 41.34 C
ANISOU 2108 CD1 LEU A 270 6279 7308 2121 36 122 -312 C
ATOM 2109 CD2 LEU A 270 32.497 115.191 261.600 1.00 42.49 C
ANISOU 2109 CD2 LEU A 270 6525 7367 2254 -6 209 -471 C
ATOM 2110 N ARG A 271 36.243 114.279 265.864 1.00 48.05 N
ANISOU 2110 N ARG A 271 7446 8387 2424 -100 -184 -594 N
ATOM 2111 CA ARG A 271 36.577 113.829 267.208 1.00 50.36 C
ANISOU 2111 CA ARG A 271 7831 8759 2544 -96 -242 -602 C
ATOM 2112 C ARG A 271 36.311 114.922 268.263 1.00 52.37 C
ANISOU 2112 C ARG A 271 8212 8996 2691 -134 -210 -718 C
ATOM 2113 O ARG A 271 36.354 114.661 269.476 1.00 53.32 O
ANISOU 2113 O ARG A 271 8433 9175 2651 -130 -234 -734 O
ATOM 2114 CB ARG A 271 38.026 113.336 267.240 1.00 50.56 C
ANISOU 2114 CB ARG A 271 7793 8874 2544 -116 -400 -582 C
ATOM 2115 CG ARG A 271 38.317 112.289 266.138 1.00 50.79 C
ANISOU 2115 CG ARG A 271 7700 8914 2685 -70 -426 -475 C
ATOM 2116 CD ARG A 271 39.790 112.111 265.819 1.00 51.49 C
ANISOU 2116 CD ARG A 271 7689 9077 2798 -92 -568 -470 C
ATOM 2117 NE ARG A 271 40.465 113.395 265.788 1.00 53.92 N
ANISOU 2117 NE ARG A 271 7979 9379 3127 -180 -616 -572 N
ATOM 2118 CZ ARG A 271 41.781 113.548 265.750 1.00 56.74 C
ANISOU 2118 CZ ARG A 271 8261 9811 3486 -225 -744 -594 C
ATOM 2119 NH1 ARG A 271 42.587 112.496 265.715 1.00 57.95 N
ANISOU 2119 NH1 ARG A 271 8343 10051 3623 -178 -836 -521 N
ATOM 2120 NH2 ARG A 271 42.297 114.763 265.740 1.00 58.63 N
ANISOU 2120 NH2 ARG A 271 8495 10037 3747 -317 -779 -689 N
ATOM 2121 N LYS A 272 36.008 116.134 267.786 1.00 53.20 N
ANISOU 2121 N LYS A 272 8319 9014 2882 -169 -153 -797 N
ATOM 2122 CA LYS A 272 35.820 117.314 268.649 1.00 55.00 C
ANISOU 2122 CA LYS A 272 8667 9204 3025 -208 -124 -921 C
ATOM 2123 C LYS A 272 34.350 117.744 268.816 1.00 55.38 C
ANISOU 2123 C LYS A 272 8788 9176 3079 -157 43 -943 C
ATOM 2124 O LYS A 272 34.055 118.749 269.480 1.00 55.79 O
ANISOU 2124 O LYS A 272 8946 9182 3068 -175 88 -1050 O
ATOM 2125 CB LYS A 272 36.714 118.475 268.185 1.00 55.09 C
ANISOU 2125 CB LYS A 272 8649 9172 3109 -294 -198 -1009 C
ATOM 2126 CG LYS A 272 38.173 118.073 268.160 1.00 55.67 C
ANISOU 2126 CG LYS A 272 8648 9340 3164 -346 -362 -992 C
ATOM 2127 CD LYS A 272 39.149 119.231 268.046 1.00 58.49 C
ANISOU 2127 CD LYS A 272 8997 9676 3551 -451 -450 -1091 C
ATOM 2128 CE LYS A 272 40.557 118.731 268.426 1.00 61.00 C
ANISOU 2128 CE LYS A 272 9258 10118 3801 -498 -618 -1078 C
ATOM 2129 NZ LYS A 272 41.687 119.487 267.798 1.00 61.33 N
ANISOU 2129 NZ LYS A 272 9210 10162 3931 -598 -715 -1122 N
ATOM 2130 N GLY A 273 33.440 116.973 268.217 1.00 54.67 N
ANISOU 2130 N GLY A 273 8638 9073 3063 -92 132 -844 N
ATOM 2131 CA GLY A 273 32.019 117.114 268.521 1.00 55.68 C
ANISOU 2131 CA GLY A 273 8823 9159 3176 -34 288 -845 C
ATOM 2132 C GLY A 273 31.295 118.232 267.793 1.00 55.86 C
ANISOU 2132 C GLY A 273 8828 9071 3326 -24 384 -897 C
ATOM 2133 O GLY A 273 31.920 119.037 267.070 1.00 56.14 O
ANISOU 2133 O GLY A 273 8824 9051 3458 -70 330 -942 O
ATOM 2134 N VAL A 274 29.980 118.288 268.005 1.00 55.80 N
ANISOU 2134 N VAL A 274 8851 9035 3316 39 528 -887 N
ATOM 2135 CA VAL A 274 29.085 119.061 267.146 1.00 55.41 C
ANISOU 2135 CA VAL A 274 8757 8889 3407 74 630 -898 C
ATOM 2136 C VAL A 274 29.312 120.561 267.107 1.00 56.68 C
ANISOU 2136 C VAL A 274 8978 8954 3602 46 633 -1019 C
ATOM 2137 O VAL A 274 29.022 121.195 266.091 1.00 55.85 O
ANISOU 2137 O VAL A 274 8813 8764 3641 55 664 -1016 O
ATOM 2138 CB VAL A 274 27.602 118.796 267.435 1.00 55.61 C
ANISOU 2138 CB VAL A 274 8793 8916 3421 151 786 -860 C
ATOM 2139 CG1 VAL A 274 27.211 117.410 266.945 1.00 54.41 C
ANISOU 2139 CG1 VAL A 274 8545 8821 3307 173 794 -722 C
ATOM 2140 CG2 VAL A 274 27.285 118.984 268.903 1.00 56.03 C
ANISOU 2140 CG2 VAL A 274 8983 9006 3298 168 846 -931 C
ATOM 2141 N LYS A 275 29.820 121.142 268.189 1.00 58.64 N
ANISOU 2141 N LYS A 275 9351 9212 3718 10 597 -1125 N
ATOM 2142 CA LYS A 275 30.085 122.585 268.154 1.00 59.86 C
ANISOU 2142 CA LYS A 275 9575 9264 3906 -26 592 -1246 C
ATOM 2143 C LYS A 275 31.452 123.013 267.550 1.00 59.71 C
ANISOU 2143 C LYS A 275 9514 9226 3949 -125 447 -1273 C
ATOM 2144 O LYS A 275 31.768 124.199 267.545 1.00 61.54 O
ANISOU 2144 O LYS A 275 9810 9370 4204 -171 431 -1373 O
ATOM 2145 CB LYS A 275 29.810 123.241 269.513 1.00 61.44 C
ANISOU 2145 CB LYS A 275 9941 9455 3950 -16 645 -1366 C
ATOM 2146 CG LYS A 275 28.304 123.372 269.811 1.00 62.34 C
ANISOU 2146 CG LYS A 275 10090 9540 4057 87 824 -1366 C
ATOM 2147 CD LYS A 275 27.947 124.672 270.545 1.00 64.08 C
ANISOU 2147 CD LYS A 275 10459 9672 4217 106 899 -1512 C
ATOM 2148 CE LYS A 275 28.508 124.706 271.976 1.00 65.24 C
ANISOU 2148 CE LYS A 275 10755 9882 4153 64 851 -1606 C
ATOM 2149 NZ LYS A 275 28.942 126.081 272.320 1.00 64.38 N
ANISOU 2149 NZ LYS A 275 10775 9669 4019 18 825 -1759 N
ATOM 2150 N HIS A 276 32.243 122.072 267.030 1.00 57.78 N
ANISOU 2150 N HIS A 276 9161 9059 3733 -156 345 -1185 N
ATOM 2151 CA HIS A 276 33.524 122.414 266.453 1.00 56.55 C
ANISOU 2151 CA HIS A 276 8949 8901 3636 -246 215 -1202 C
ATOM 2152 C HIS A 276 33.311 122.533 264.970 1.00 54.93 C
ANISOU 2152 C HIS A 276 8626 8632 3614 -235 243 -1134 C
ATOM 2153 O HIS A 276 32.974 121.566 264.300 1.00 53.28 O
ANISOU 2153 O HIS A 276 8318 8462 3464 -188 263 -1026 O
ATOM 2154 CB HIS A 276 34.543 121.324 266.754 1.00 56.69 C
ANISOU 2154 CB HIS A 276 8915 9048 3577 -277 90 -1146 C
ATOM 2155 CG HIS A 276 35.753 121.365 265.870 1.00 57.25 C
ANISOU 2155 CG HIS A 276 8876 9137 3740 -349 -29 -1124 C
ATOM 2156 ND1 HIS A 276 36.842 122.176 266.126 1.00 57.14 N
ANISOU 2156 ND1 HIS A 276 8889 9121 3701 -449 -133 -1211 N
ATOM 2157 CD2 HIS A 276 36.041 120.698 264.722 1.00 57.42 C
ANISOU 2157 CD2 HIS A 276 8759 9180 3877 -339 -56 -1025 C
ATOM 2158 CE1 HIS A 276 37.747 122.005 265.179 1.00 58.38 C
ANISOU 2158 CE1 HIS A 276 8919 9305 3956 -496 -215 -1163 C
ATOM 2159 NE2 HIS A 276 37.284 121.118 264.309 1.00 58.85 N
ANISOU 2159 NE2 HIS A 276 8881 9379 4102 -427 -168 -1052 N
ATOM 2160 N ASN A 277 33.501 123.723 264.429 1.00 55.04 N
ANISOU 2160 N ASN A 277 8654 8542 3715 -281 242 -1196 N
ATOM 2161 CA ASN A 277 33.187 123.914 263.009 1.00 53.23 C
ANISOU 2161 CA ASN A 277 8324 8246 3656 -265 279 -1129 C
ATOM 2162 C ASN A 277 34.313 124.409 262.119 1.00 52.64 C
ANISOU 2162 C ASN A 277 8180 8147 3672 -359 182 -1132 C
ATOM 2163 O ASN A 277 34.072 124.632 260.915 1.00 51.45 O
ANISOU 2163 O ASN A 277 7954 7938 3658 -349 212 -1077 O
ATOM 2164 CB ASN A 277 31.973 124.841 262.834 1.00 53.48 C
ANISOU 2164 CB ASN A 277 8414 8154 3750 -202 409 -1165 C
ATOM 2165 CG ASN A 277 30.673 124.211 263.298 1.00 52.83 C
ANISOU 2165 CG ASN A 277 8346 8101 3624 -96 526 -1125 C
ATOM 2166 OD1 ASN A 277 30.521 122.984 263.340 1.00 50.65 O
ANISOU 2166 OD1 ASN A 277 8008 7922 3316 -66 522 -1038 O
ATOM 2167 ND2 ASN A 277 29.716 125.060 263.636 1.00 53.15 N
ANISOU 2167 ND2 ASN A 277 8470 8055 3668 -39 635 -1186 N
ATOM 2168 N THR A 278 35.511 124.602 262.678 1.00 52.79 N
ANISOU 2168 N THR A 278 8223 8214 3619 -450 68 -1192 N
ATOM 2169 CA THR A 278 36.602 125.153 261.866 1.00 53.02 C
ANISOU 2169 CA THR A 278 8185 8225 3735 -551 -19 -1197 C
ATOM 2170 C THR A 278 37.254 124.116 260.956 1.00 51.40 C
ANISOU 2170 C THR A 278 7824 8116 3591 -552 -81 -1088 C
ATOM 2171 O THR A 278 37.636 123.010 261.384 1.00 51.06 O
ANISOU 2171 O THR A 278 7738 8189 3472 -529 -135 -1044 O
ATOM 2172 CB THR A 278 37.674 125.943 262.664 1.00 54.60 C
ANISOU 2172 CB THR A 278 8459 8429 3857 -666 -121 -1308 C
ATOM 2173 OG1 THR A 278 38.318 125.060 263.584 1.00 56.03 O
ANISOU 2173 OG1 THR A 278 8634 8747 3908 -675 -208 -1306 O
ATOM 2174 CG2 THR A 278 37.053 127.160 263.428 1.00 56.22 C
ANISOU 2174 CG2 THR A 278 8833 8511 4016 -671 -56 -1430 C
ATOM 2175 N LEU A 279 37.337 124.514 259.686 1.00 50.41 N
ANISOU 2175 N LEU A 279 7621 7931 3602 -575 -66 -1046 N
ATOM 2176 CA LEU A 279 37.913 123.745 258.589 1.00 48.81 C
ANISOU 2176 CA LEU A 279 7272 7796 3479 -579 -108 -949 C
ATOM 2177 C LEU A 279 39.435 123.875 258.513 1.00 49.68 C
ANISOU 2177 C LEU A 279 7315 7977 3584 -687 -231 -969 C
ATOM 2178 O LEU A 279 40.038 124.764 259.143 1.00 50.81 O
ANISOU 2178 O LEU A 279 7524 8097 3685 -777 -285 -1060 O
ATOM 2179 CB LEU A 279 37.318 124.219 257.250 1.00 47.57 C
ANISOU 2179 CB LEU A 279 7070 7541 3462 -562 -35 -898 C
ATOM 2180 CG LEU A 279 35.874 123.914 256.827 1.00 45.76 C
ANISOU 2180 CG LEU A 279 6847 7260 3281 -453 79 -840 C
ATOM 2181 CD1 LEU A 279 35.296 122.689 257.555 1.00 44.82 C
ANISOU 2181 CD1 LEU A 279 6733 7224 3073 -369 103 -802 C
ATOM 2182 CD2 LEU A 279 34.988 125.098 257.041 1.00 46.47 C
ANISOU 2182 CD2 LEU A 279 7043 7218 3396 -435 162 -903 C
ATOM 2183 N GLU A 280 40.035 122.998 257.703 1.00 48.81 N
ANISOU 2183 N GLU A 280 7072 7953 3521 -678 -273 -884 N
ATOM 2184 CA GLU A 280 41.475 122.967 257.475 1.00 49.20 C
ANISOU 2184 CA GLU A 280 7025 8089 3579 -766 -382 -885 C
ATOM 2185 C GLU A 280 41.724 122.866 255.979 1.00 47.88 C
ANISOU 2185 C GLU A 280 6737 7917 3538 -773 -363 -807 C
ATOM 2186 O GLU A 280 41.682 121.783 255.413 1.00 47.11 O
ANISOU 2186 O GLU A 280 6555 7884 3461 -702 -355 -725 O
ATOM 2187 CB GLU A 280 42.093 121.774 258.202 1.00 49.53 C
ANISOU 2187 CB GLU A 280 7022 8273 3523 -730 -463 -859 C
ATOM 2188 CG GLU A 280 41.495 121.560 259.606 1.00 52.84 C
ANISOU 2188 CG GLU A 280 7568 8700 3809 -685 -454 -907 C
ATOM 2189 CD GLU A 280 42.100 120.394 260.384 1.00 55.49 C
ANISOU 2189 CD GLU A 280 7873 9171 4038 -647 -540 -876 C
ATOM 2190 OE1 GLU A 280 42.929 119.644 259.811 1.00 55.24 O
ANISOU 2190 OE1 GLU A 280 7716 9229 4042 -639 -602 -812 O
ATOM 2191 OE2 GLU A 280 41.727 120.229 261.578 1.00 56.90 O
ANISOU 2191 OE2 GLU A 280 8157 9367 4095 -620 -542 -914 O
ATOM 2192 N MET A 281 41.953 124.009 255.337 1.00 47.53 N
ANISOU 2192 N MET A 281 6695 7789 3574 -859 -352 -834 N
ATOM 2193 CA MET A 281 42.367 124.075 253.940 1.00 45.55 C
ANISOU 2193 CA MET A 281 6334 7538 3433 -890 -342 -768 C
ATOM 2194 C MET A 281 43.353 122.943 253.612 1.00 44.08 C
ANISOU 2194 C MET A 281 6008 7503 3239 -875 -410 -707 C
ATOM 2195 O MET A 281 44.188 122.615 254.458 1.00 45.23 O
ANISOU 2195 O MET A 281 6131 7746 3307 -904 -498 -740 O
ATOM 2196 CB MET A 281 43.011 125.443 253.713 1.00 46.83 C
ANISOU 2196 CB MET A 281 6517 7631 3646 -1025 -368 -823 C
ATOM 2197 CG MET A 281 43.498 125.690 252.328 1.00 48.25 C
ANISOU 2197 CG MET A 281 6594 7806 3932 -1076 -356 -761 C
ATOM 2198 SD MET A 281 42.206 125.299 251.143 1.00 52.79 S
ANISOU 2198 SD MET A 281 7162 8308 4586 -959 -242 -668 S
ATOM 2199 CE MET A 281 41.447 126.925 250.931 1.00 53.51 C
ANISOU 2199 CE MET A 281 7382 8205 4742 -1007 -176 -712 C
ATOM 2200 N VAL A 282 43.248 122.316 252.430 1.00 42.98 N
ANISOU 2200 N VAL A 282 5776 7384 3170 -825 -371 -621 N
ATOM 2201 CA VAL A 282 44.242 121.300 252.044 1.00 42.76 C
ANISOU 2201 CA VAL A 282 5614 7494 3141 -807 -430 -569 C
ATOM 2202 C VAL A 282 45.231 121.895 251.092 1.00 43.15 C
ANISOU 2202 C VAL A 282 5563 7566 3266 -905 -452 -556 C
ATOM 2203 O VAL A 282 46.350 122.152 251.467 1.00 44.18 O
ANISOU 2203 O VAL A 282 5637 7774 3377 -988 -532 -590 O
ATOM 2204 CB VAL A 282 43.690 120.032 251.394 1.00 41.48 C
ANISOU 2204 CB VAL A 282 5406 7361 2992 -687 -385 -485 C
ATOM 2205 CG1 VAL A 282 44.858 119.135 250.984 1.00 41.52 C
ANISOU 2205 CG1 VAL A 282 5275 7501 3000 -674 -448 -441 C
ATOM 2206 CG2 VAL A 282 42.782 119.276 252.334 1.00 41.15 C
ANISOU 2206 CG2 VAL A 282 5451 7312 2872 -593 -366 -485 C
ATOM 2207 N ARG A 283 44.840 122.072 249.842 1.00 42.38 N
ANISOU 2207 N ARG A 283 5437 7413 3254 -895 -382 -501 N
ATOM 2208 CA ARG A 283 45.646 122.849 248.946 1.00 42.87 C
ANISOU 2208 CA ARG A 283 5426 7476 3388 -1001 -388 -490 C
ATOM 2209 C ARG A 283 44.728 123.831 248.296 1.00 42.60 C
ANISOU 2209 C ARG A 283 5475 7291 3419 -1022 -308 -484 C
ATOM 2210 O ARG A 283 43.726 123.444 247.727 1.00 41.55 O
ANISOU 2210 O ARG A 283 5369 7107 3312 -932 -240 -435 O
ATOM 2211 CB ARG A 283 46.339 121.990 247.915 1.00 42.38 C
ANISOU 2211 CB ARG A 283 5221 7521 3361 -970 -390 -418 C
ATOM 2212 CG ARG A 283 47.237 122.806 247.046 1.00 43.06 C
ANISOU 2212 CG ARG A 283 5226 7620 3513 -1088 -393 -406 C
ATOM 2213 CD ARG A 283 48.197 121.944 246.306 1.00 42.96 C
ANISOU 2213 CD ARG A 283 5060 7748 3516 -1065 -410 -352 C
ATOM 2214 NE ARG A 283 49.199 122.758 245.618 1.00 43.88 N
ANISOU 2214 NE ARG A 283 5088 7897 3688 -1194 -419 -345 N
ATOM 2215 CZ ARG A 283 49.010 123.394 244.459 1.00 43.69 C
ANISOU 2215 CZ ARG A 283 5062 7806 3732 -1242 -352 -302 C
ATOM 2216 NH1 ARG A 283 47.846 123.343 243.801 1.00 43.23 N
ANISOU 2216 NH1 ARG A 283 5083 7645 3699 -1169 -275 -263 N
ATOM 2217 NH2 ARG A 283 49.997 124.107 243.953 1.00 44.69 N
ANISOU 2217 NH2 ARG A 283 5106 7973 3901 -1369 -364 -296 N
ATOM 2218 N PRO A 284 45.041 125.120 248.423 1.00 43.64 N
ANISOU 2218 N PRO A 284 5655 7347 3578 -1140 -320 -534 N
ATOM 2219 CA PRO A 284 44.231 126.165 247.810 1.00 43.58 C
ANISOU 2219 CA PRO A 284 5735 7186 3638 -1163 -249 -528 C
ATOM 2220 C PRO A 284 44.014 125.918 246.312 1.00 42.67 C
ANISOU 2220 C PRO A 284 5550 7066 3596 -1131 -190 -434 C
ATOM 2221 O PRO A 284 44.935 125.489 245.611 1.00 42.65 O
ANISOU 2221 O PRO A 284 5426 7167 3611 -1163 -212 -390 O
ATOM 2222 CB PRO A 284 45.071 127.419 248.025 1.00 45.04 C
ANISOU 2222 CB PRO A 284 5943 7326 3843 -1320 -292 -585 C
ATOM 2223 CG PRO A 284 45.823 127.142 249.295 1.00 45.89 C
ANISOU 2223 CG PRO A 284 6042 7528 3866 -1355 -383 -657 C
ATOM 2224 CD PRO A 284 46.034 125.661 249.368 1.00 45.04 C
ANISOU 2224 CD PRO A 284 5834 7567 3712 -1251 -407 -611 C
ATOM 2225 N ARG A 285 42.803 126.176 245.833 1.00 42.01 N
ANISOU 2225 N ARG A 285 5541 6870 3550 -1065 -116 -403 N
ATOM 2226 CA ARG A 285 42.488 125.994 244.432 1.00 41.22 C
ANISOU 2226 CA ARG A 285 5392 6758 3511 -1034 -63 -315 C
ATOM 2227 C ARG A 285 43.489 126.749 243.570 1.00 41.96 C
ANISOU 2227 C ARG A 285 5427 6859 3658 -1158 -73 -291 C
ATOM 2228 O ARG A 285 43.914 127.875 243.920 1.00 43.10 O
ANISOU 2228 O ARG A 285 5623 6935 3820 -1270 -95 -340 O
ATOM 2229 CB ARG A 285 41.068 126.466 244.122 1.00 40.75 C
ANISOU 2229 CB ARG A 285 5432 6562 3490 -965 8 -294 C
ATOM 2230 CG ARG A 285 40.793 127.911 244.526 1.00 41.79 C
ANISOU 2230 CG ARG A 285 5680 6548 3651 -1031 22 -348 C
ATOM 2231 CD ARG A 285 39.383 128.356 244.152 1.00 41.41 C
ANISOU 2231 CD ARG A 285 5717 6369 3647 -948 94 -319 C
ATOM 2232 NE ARG A 285 38.357 127.700 244.966 1.00 40.84 N
ANISOU 2232 NE ARG A 285 5686 6301 3529 -831 119 -341 N
ATOM 2233 CZ ARG A 285 37.050 127.872 244.789 1.00 40.48 C
ANISOU 2233 CZ ARG A 285 5697 6169 3514 -740 181 -316 C
ATOM 2234 NH1 ARG A 285 36.613 128.682 243.812 1.00 40.61 N
ANISOU 2234 NH1 ARG A 285 5740 6085 3606 -746 218 -267 N
ATOM 2235 NH2 ARG A 285 36.185 127.236 245.568 1.00 40.06 N
ANISOU 2235 NH2 ARG A 285 5671 6134 3416 -643 205 -336 N
ATOM 2236 N GLU A 286 43.874 126.100 242.466 1.00 41.40 N
ANISOU 2236 N GLU A 286 5251 6871 3607 -1142 -57 -218 N
ATOM 2237 CA GLU A 286 44.750 126.655 241.444 1.00 41.99 C
ANISOU 2237 CA GLU A 286 5256 6967 3730 -1246 -50 -176 C
ATOM 2238 C GLU A 286 44.194 126.180 240.115 1.00 41.03 C
ANISOU 2238 C GLU A 286 5106 6847 3637 -1176 10 -88 C
ATOM 2239 O GLU A 286 44.101 124.976 239.836 1.00 40.15 O
ANISOU 2239 O GLU A 286 4932 6826 3497 -1081 15 -57 O
ATOM 2240 CB GLU A 286 46.205 126.205 241.658 1.00 42.64 C
ANISOU 2240 CB GLU A 286 5208 7205 3786 -1312 -110 -192 C
ATOM 2241 CG GLU A 286 47.195 126.551 240.498 1.00 43.48 C
ANISOU 2241 CG GLU A 286 5212 7371 3938 -1411 -93 -137 C
ATOM 2242 CD GLU A 286 48.673 126.305 240.872 1.00 46.42 C
ANISOU 2242 CD GLU A 286 5451 7895 4291 -1491 -158 -163 C
ATOM 2243 OE1 GLU A 286 49.009 125.210 241.386 1.00 46.89 O
ANISOU 2243 OE1 GLU A 286 5440 8073 4302 -1411 -197 -177 O
ATOM 2244 OE2 GLU A 286 49.505 127.207 240.644 1.00 48.48 O
ANISOU 2244 OE2 GLU A 286 5677 8158 4587 -1635 -170 -165 O
ATOM 2245 N LYS A 287 43.781 127.155 239.319 1.00 41.29 N
ANISOU 2245 N LYS A 287 5196 6768 3724 -1221 54 -49 N
ATOM 2246 CA LYS A 287 43.072 126.909 238.061 1.00 40.51 C
ANISOU 2246 CA LYS A 287 5096 6644 3651 -1158 110 35 C
ATOM 2247 C LYS A 287 43.850 125.890 237.251 1.00 40.13 C
ANISOU 2247 C LYS A 287 4921 6745 3582 -1142 112 81 C
ATOM 2248 O LYS A 287 45.072 125.959 237.179 1.00 40.87 O
ANISOU 2248 O LYS A 287 4927 6929 3673 -1227 89 73 O
ATOM 2249 CB LYS A 287 42.929 128.236 237.292 1.00 41.24 C
ANISOU 2249 CB LYS A 287 5253 6614 3804 -1244 143 74 C
ATOM 2250 CG LYS A 287 41.607 128.438 236.564 1.00 40.64 C
ANISOU 2250 CG LYS A 287 5252 6431 3756 -1161 193 133 C
ATOM 2251 CD LYS A 287 41.754 128.297 235.032 1.00 42.95 C
ANISOU 2251 CD LYS A 287 5494 6761 4064 -1172 229 228 C
ATOM 2252 CE LYS A 287 40.376 128.052 234.391 1.00 45.40 C
ANISOU 2252 CE LYS A 287 5856 7009 4386 -1059 263 285 C
ATOM 2253 NZ LYS A 287 40.281 128.612 232.990 1.00 49.22 N
ANISOU 2253 NZ LYS A 287 6352 7452 4898 -1095 298 376 N
ATOM 2254 N GLY A 288 43.148 124.932 236.668 1.00 39.07 N
ANISOU 2254 N GLY A 288 4776 6639 3431 -1031 139 124 N
ATOM 2255 CA GLY A 288 43.799 123.852 235.979 1.00 38.71 C
ANISOU 2255 CA GLY A 288 4624 6728 3358 -995 143 158 C
ATOM 2256 C GLY A 288 44.088 122.657 236.871 1.00 38.32 C
ANISOU 2256 C GLY A 288 4525 6776 3258 -919 101 114 C
ATOM 2257 O GLY A 288 44.271 121.549 236.379 1.00 37.80 O
ANISOU 2257 O GLY A 288 4397 6800 3165 -847 108 140 O
ATOM 2258 N VAL A 289 44.132 122.845 238.184 1.00 38.63 N
ANISOU 2258 N VAL A 289 4599 6799 3279 -931 57 48 N
ATOM 2259 CA VAL A 289 44.531 121.738 239.017 1.00 38.42 C
ANISOU 2259 CA VAL A 289 4525 6873 3201 -866 12 15 C
ATOM 2260 C VAL A 289 43.296 121.073 239.541 1.00 37.50 C
ANISOU 2260 C VAL A 289 4487 6703 3058 -756 22 9 C
ATOM 2261 O VAL A 289 42.436 121.726 240.093 1.00 37.49 O
ANISOU 2261 O VAL A 289 4580 6598 3065 -757 33 -15 O
ATOM 2262 CB VAL A 289 45.506 122.129 240.204 1.00 39.44 C
ANISOU 2262 CB VAL A 289 4627 7051 3308 -942 -54 -53 C
ATOM 2263 CG1 VAL A 289 46.062 120.893 240.847 1.00 39.32 C
ANISOU 2263 CG1 VAL A 289 4543 7158 3239 -869 -103 -71 C
ATOM 2264 CG2 VAL A 289 46.681 122.955 239.750 1.00 40.54 C
ANISOU 2264 CG2 VAL A 289 4689 7233 3481 -1073 -64 -50 C
ATOM 2265 N ARG A 290 43.213 119.764 239.354 1.00 36.82 N
ANISOU 2265 N ARG A 290 4362 6687 2939 -660 20 33 N
ATOM 2266 CA ARG A 290 42.178 118.910 239.972 1.00 36.04 C
ANISOU 2266 CA ARG A 290 4325 6560 2807 -559 22 28 C
ATOM 2267 C ARG A 290 42.867 117.931 240.913 1.00 36.20 C
ANISOU 2267 C ARG A 290 4305 6678 2773 -515 -33 -3 C
ATOM 2268 O ARG A 290 44.016 117.505 240.674 1.00 36.62 O
ANISOU 2268 O ARG A 290 4263 6835 2816 -524 -61 1 O
ATOM 2269 CB ARG A 290 41.376 118.120 238.909 1.00 35.14 C
ANISOU 2269 CB ARG A 290 4216 6434 2702 -483 64 88 C
ATOM 2270 CG ARG A 290 40.473 119.000 238.032 1.00 35.55 C
ANISOU 2270 CG ARG A 290 4319 6385 2803 -508 113 126 C
ATOM 2271 CD ARG A 290 39.987 118.331 236.770 1.00 39.53 C
ANISOU 2271 CD ARG A 290 4809 6898 3312 -457 145 186 C
ATOM 2272 NE ARG A 290 39.411 117.011 236.992 1.00 43.71 N
ANISOU 2272 NE ARG A 290 5350 7453 3806 -364 138 193 N
ATOM 2273 CZ ARG A 290 39.950 115.866 236.558 1.00 46.14 C
ANISOU 2273 CZ ARG A 290 5607 7841 4083 -316 129 205 C
ATOM 2274 NH1 ARG A 290 41.091 115.852 235.865 1.00 44.56 N
ANISOU 2274 NH1 ARG A 290 5331 7717 3882 -346 130 212 N
ATOM 2275 NH2 ARG A 290 39.340 114.714 236.823 1.00 48.48 N
ANISOU 2275 NH2 ARG A 290 5930 8141 4350 -237 122 211 N
ATOM 2276 N TYR A 291 42.171 117.571 241.984 1.00 35.97 N
ANISOU 2276 N TYR A 291 4345 6618 2705 -465 -47 -29 N
ATOM 2277 CA TYR A 291 42.699 116.591 242.913 1.00 36.14 C
ANISOU 2277 CA TYR A 291 4343 6723 2667 -414 -100 -50 C
ATOM 2278 C TYR A 291 41.626 116.143 243.858 1.00 35.73 C
ANISOU 2278 C TYR A 291 4383 6620 2574 -351 -94 -61 C
ATOM 2279 O TYR A 291 40.741 116.930 244.199 1.00 35.70 O
ANISOU 2279 O TYR A 291 4456 6526 2582 -372 -63 -79 O
ATOM 2280 CB TYR A 291 43.898 117.151 243.674 1.00 37.20 C
ANISOU 2280 CB TYR A 291 4431 6922 2783 -490 -162 -99 C
ATOM 2281 CG TYR A 291 43.561 118.148 244.718 1.00 37.72 C
ANISOU 2281 CG TYR A 291 4580 6920 2833 -548 -176 -156 C
ATOM 2282 CD1 TYR A 291 43.310 117.730 246.015 1.00 37.88 C
ANISOU 2282 CD1 TYR A 291 4657 6950 2786 -508 -211 -192 C
ATOM 2283 CD2 TYR A 291 43.516 119.524 244.425 1.00 38.18 C
ANISOU 2283 CD2 TYR A 291 4667 6900 2939 -645 -153 -176 C
ATOM 2284 CE1 TYR A 291 43.029 118.648 247.023 1.00 38.48 C
ANISOU 2284 CE1 TYR A 291 4818 6967 2837 -561 -222 -253 C
ATOM 2285 CE2 TYR A 291 43.205 120.465 245.414 1.00 38.78 C
ANISOU 2285 CE2 TYR A 291 4833 6904 2998 -696 -165 -238 C
ATOM 2286 CZ TYR A 291 42.963 120.001 246.720 1.00 38.93 C
ANISOU 2286 CZ TYR A 291 4906 6940 2943 -651 -198 -279 C
ATOM 2287 OH TYR A 291 42.683 120.849 247.750 1.00 39.61 O
ANISOU 2287 OH TYR A 291 5086 6964 3000 -694 -209 -347 O
ATOM 2288 N THR A 292 41.733 114.873 244.256 1.00 35.52 N
ANISOU 2288 N THR A 292 4345 6652 2500 -272 -121 -46 N
ATOM 2289 CA THR A 292 40.817 114.204 245.186 1.00 35.30 C
ANISOU 2289 CA THR A 292 4396 6593 2422 -208 -117 -47 C
ATOM 2290 C THR A 292 41.599 113.714 246.412 1.00 36.61 C
ANISOU 2290 C THR A 292 4558 6835 2517 -193 -187 -77 C
ATOM 2291 O THR A 292 42.733 113.259 246.284 1.00 36.93 O
ANISOU 2291 O THR A 292 4518 6964 2548 -184 -236 -74 O
ATOM 2292 CB THR A 292 40.141 112.999 244.493 1.00 34.40 C
ANISOU 2292 CB THR A 292 4288 6470 2313 -127 -87 10 C
ATOM 2293 OG1 THR A 292 39.170 113.455 243.540 1.00 33.82 O
ANISOU 2293 OG1 THR A 292 4236 6320 2294 -138 -27 38 O
ATOM 2294 CG2 THR A 292 39.451 112.123 245.498 1.00 35.32 C
ANISOU 2294 CG2 THR A 292 4472 6575 2371 -65 -93 15 C
ATOM 2295 N VAL A 293 40.969 113.787 247.583 1.00 37.70 N
ANISOU 2295 N VAL A 293 4780 6941 2603 -183 -190 -104 N
ATOM 2296 CA VAL A 293 41.593 113.443 248.869 1.00 39.38 C
ANISOU 2296 CA VAL A 293 5008 7220 2736 -174 -258 -135 C
ATOM 2297 C VAL A 293 40.955 112.229 249.561 1.00 39.99 C
ANISOU 2297 C VAL A 293 5144 7298 2750 -88 -257 -103 C
ATOM 2298 O VAL A 293 39.709 112.123 249.647 1.00 39.88 O
ANISOU 2298 O VAL A 293 5202 7213 2736 -63 -197 -87 O
ATOM 2299 CB VAL A 293 41.530 114.662 249.841 1.00 40.17 C
ANISOU 2299 CB VAL A 293 5169 7286 2808 -249 -268 -204 C
ATOM 2300 CG1 VAL A 293 41.990 114.301 251.303 1.00 39.84 C
ANISOU 2300 CG1 VAL A 293 5165 7307 2664 -237 -339 -238 C
ATOM 2301 CG2 VAL A 293 42.326 115.828 249.254 1.00 40.92 C
ANISOU 2301 CG2 VAL A 293 5206 7381 2960 -345 -282 -236 C
ATOM 2302 N GLU A 294 41.814 111.339 250.068 1.00 41.05 N
ANISOU 2302 N GLU A 294 5249 7517 2833 -44 -326 -92 N
ATOM 2303 CA GLU A 294 41.398 110.185 250.887 1.00 41.92 C
ANISOU 2303 CA GLU A 294 5422 7635 2870 32 -340 -60 C
ATOM 2304 C GLU A 294 42.336 110.070 252.074 1.00 42.89 C
ANISOU 2304 C GLU A 294 5544 7840 2912 31 -428 -88 C
ATOM 2305 O GLU A 294 43.558 110.132 251.889 1.00 44.01 O
ANISOU 2305 O GLU A 294 5594 8062 3064 18 -492 -99 O
ATOM 2306 CB GLU A 294 41.423 108.866 250.092 1.00 41.13 C
ANISOU 2306 CB GLU A 294 5291 7543 2792 114 -334 3 C
ATOM 2307 CG GLU A 294 40.393 108.760 248.957 1.00 43.28 C
ANISOU 2307 CG GLU A 294 5576 7737 3132 121 -255 36 C
ATOM 2308 CD GLU A 294 39.037 108.208 249.418 1.00 48.33 C
ANISOU 2308 CD GLU A 294 6312 8310 3744 152 -206 66 C
ATOM 2309 OE1 GLU A 294 39.046 107.118 250.083 1.00 50.02 O
ANISOU 2309 OE1 GLU A 294 6567 8541 3898 209 -235 97 O
ATOM 2310 OE2 GLU A 294 37.980 108.862 249.105 1.00 46.45 O
ANISOU 2310 OE2 GLU A 294 6102 8003 3544 118 -140 63 O
ATOM 2311 N MET A 295 41.766 109.889 253.270 1.00 42.97 N
ANISOU 2311 N MET A 295 5650 7837 2838 45 -432 -96 N
ATOM 2312 CA MET A 295 42.529 109.735 254.517 1.00 43.73 C
ANISOU 2312 CA MET A 295 5765 8011 2839 47 -519 -118 C
ATOM 2313 C MET A 295 42.928 108.296 254.757 1.00 43.71 C
ANISOU 2313 C MET A 295 5756 8060 2792 141 -569 -57 C
ATOM 2314 O MET A 295 42.247 107.352 254.313 1.00 42.79 O
ANISOU 2314 O MET A 295 5669 7895 2693 204 -523 0 O
ATOM 2315 CB MET A 295 41.712 110.176 255.733 1.00 44.16 C
ANISOU 2315 CB MET A 295 5938 8029 2810 23 -496 -154 C
ATOM 2316 CG MET A 295 41.117 111.568 255.656 1.00 45.92 C
ANISOU 2316 CG MET A 295 6196 8182 3069 -55 -436 -217 C
ATOM 2317 SD MET A 295 42.314 112.870 255.995 1.00 53.34 S
ANISOU 2317 SD MET A 295 7095 9171 4002 -159 -513 -302 S
ATOM 2318 CE MET A 295 42.898 112.488 257.661 1.00 52.84 C
ANISOU 2318 CE MET A 295 7092 9196 3790 -150 -611 -328 C
ATOM 2319 N HIS A 296 44.050 108.154 255.455 1.00 44.67 N
ANISOU 2319 N HIS A 296 5840 8277 2857 147 -669 -70 N
ATOM 2320 CA HIS A 296 44.462 106.918 256.087 1.00 45.49 C
ANISOU 2320 CA HIS A 296 5961 8434 2891 236 -734 -18 C
ATOM 2321 C HIS A 296 44.734 107.315 257.530 1.00 46.72 C
ANISOU 2321 C HIS A 296 6176 8642 2935 201 -802 -57 C
ATOM 2322 O HIS A 296 45.592 108.173 257.785 1.00 47.94 O
ANISOU 2322 O HIS A 296 6273 8860 3081 134 -865 -113 O
ATOM 2323 CB HIS A 296 45.717 106.364 255.421 1.00 46.11 C
ANISOU 2323 CB HIS A 296 5913 8594 3013 287 -798 7 C
ATOM 2324 CG HIS A 296 46.074 104.974 255.861 1.00 47.76 C
ANISOU 2324 CG HIS A 296 6140 8840 3168 399 -856 70 C
ATOM 2325 ND1 HIS A 296 47.334 104.632 256.307 1.00 48.91 N
ANISOU 2325 ND1 HIS A 296 6209 9096 3277 441 -963 78 N
ATOM 2326 CD2 HIS A 296 45.333 103.841 255.927 1.00 48.14 C
ANISOU 2326 CD2 HIS A 296 6275 8824 3193 478 -822 133 C
ATOM 2327 CE1 HIS A 296 47.351 103.350 256.629 1.00 50.22 C
ANISOU 2327 CE1 HIS A 296 6422 9261 3401 549 -994 143 C
ATOM 2328 NE2 HIS A 296 46.147 102.848 256.414 1.00 49.08 N
ANISOU 2328 NE2 HIS A 296 6380 9007 3261 569 -908 177 N
ATOM 2329 N GLY A 297 43.981 106.729 258.468 1.00 46.71 N
ANISOU 2329 N GLY A 297 6293 8612 2843 238 -789 -28 N
ATOM 2330 CA GLY A 297 43.980 107.183 259.853 1.00 47.16 C
ANISOU 2330 CA GLY A 297 6434 8704 2781 199 -832 -70 C
ATOM 2331 C GLY A 297 43.728 108.679 259.912 1.00 47.22 C
ANISOU 2331 C GLY A 297 6455 8680 2807 93 -796 -159 C
ATOM 2332 O GLY A 297 42.990 109.221 259.105 1.00 46.26 O
ANISOU 2332 O GLY A 297 6329 8477 2769 64 -704 -173 O
ATOM 2333 N THR A 298 44.359 109.371 260.846 1.00 48.54 N
ANISOU 2333 N THR A 298 6639 8908 2896 35 -872 -220 N
ATOM 2334 CA THR A 298 43.974 110.757 261.063 1.00 48.72 C
ANISOU 2334 CA THR A 298 6709 8881 2920 -62 -831 -309 C
ATOM 2335 C THR A 298 44.958 111.736 260.455 1.00 49.49 C
ANISOU 2335 C THR A 298 6699 9011 3094 -147 -880 -364 C
ATOM 2336 O THR A 298 44.694 112.935 260.399 1.00 49.35 O
ANISOU 2336 O THR A 298 6711 8936 3102 -231 -842 -435 O
ATOM 2337 CB THR A 298 43.717 111.070 262.559 1.00 49.41 C
ANISOU 2337 CB THR A 298 6924 8986 2862 -87 -857 -358 C
ATOM 2338 OG1 THR A 298 44.806 110.596 263.340 1.00 50.62 O
ANISOU 2338 OG1 THR A 298 7053 9254 2925 -74 -989 -348 O
ATOM 2339 CG2 THR A 298 42.474 110.372 263.045 1.00 49.10 C
ANISOU 2339 CG2 THR A 298 7000 8894 2763 -24 -771 -311 C
ATOM 2340 N ASP A 299 46.061 111.211 259.937 1.00 50.63 N
ANISOU 2340 N ASP A 299 6717 9239 3279 -122 -956 -327 N
ATOM 2341 CA ASP A 299 47.252 112.031 259.641 1.00 52.74 C
ANISOU 2341 CA ASP A 299 6872 9575 3591 -208 -1031 -376 C
ATOM 2342 C ASP A 299 47.751 111.992 258.198 1.00 51.69 C
ANISOU 2342 C ASP A 299 6600 9450 3590 -206 -1005 -344 C
ATOM 2343 O ASP A 299 48.210 113.005 257.663 1.00 52.06 O
ANISOU 2343 O ASP A 299 6582 9495 3703 -302 -1005 -389 O
ATOM 2344 CB ASP A 299 48.394 111.590 260.552 1.00 54.87 C
ANISOU 2344 CB ASP A 299 7099 9978 3771 -196 -1171 -373 C
ATOM 2345 CG ASP A 299 48.181 110.164 261.105 1.00 58.83 C
ANISOU 2345 CG ASP A 299 7649 10508 4195 -70 -1194 -295 C
ATOM 2346 OD1 ASP A 299 47.616 109.289 260.338 1.00 58.91 O
ANISOU 2346 OD1 ASP A 299 7655 10465 4263 17 -1120 -225 O
ATOM 2347 OD2 ASP A 299 48.559 109.948 262.310 1.00 61.02 O
ANISOU 2347 OD2 ASP A 299 7977 10858 4350 -63 -1286 -303 O
ATOM 2348 N THR A 300 47.686 110.815 257.586 1.00 50.32 N
ANISOU 2348 N THR A 300 6385 9285 3449 -99 -983 -266 N
ATOM 2349 CA THR A 300 48.256 110.629 256.270 1.00 49.15 C
ANISOU 2349 CA THR A 300 6105 9161 3409 -83 -965 -233 C
ATOM 2350 C THR A 300 47.202 110.884 255.174 1.00 46.79 C
ANISOU 2350 C THR A 300 5836 8743 3198 -87 -839 -220 C
ATOM 2351 O THR A 300 46.132 110.296 255.182 1.00 45.67 O
ANISOU 2351 O THR A 300 5784 8526 3043 -27 -774 -186 O
ATOM 2352 CB THR A 300 49.054 109.264 256.158 1.00 49.81 C
ANISOU 2352 CB THR A 300 6107 9336 3483 35 -1027 -165 C
ATOM 2353 OG1 THR A 300 48.764 108.594 254.915 1.00 50.31 O
ANISOU 2353 OG1 THR A 300 6130 9356 3631 105 -952 -113 O
ATOM 2354 CG2 THR A 300 48.770 108.339 257.329 1.00 49.54 C
ANISOU 2354 CG2 THR A 300 6172 9314 3336 114 -1074 -132 C
ATOM 2355 N LEU A 301 47.507 111.784 254.253 1.00 45.51 N
ANISOU 2355 N LEU A 301 5600 8569 3123 -165 -809 -246 N
ATOM 2356 CA LEU A 301 46.566 112.125 253.200 1.00 43.65 C
ANISOU 2356 CA LEU A 301 5390 8227 2968 -175 -701 -232 C
ATOM 2357 C LEU A 301 46.999 111.543 251.887 1.00 42.63 C
ANISOU 2357 C LEU A 301 5154 8126 2918 -128 -675 -182 C
ATOM 2358 O LEU A 301 48.124 111.755 251.465 1.00 43.60 O
ANISOU 2358 O LEU A 301 5157 8334 3075 -161 -718 -187 O
ATOM 2359 CB LEU A 301 46.504 113.622 253.016 1.00 43.83 C
ANISOU 2359 CB LEU A 301 5423 8198 3033 -297 -675 -293 C
ATOM 2360 CG LEU A 301 45.561 114.406 253.889 1.00 43.91 C
ANISOU 2360 CG LEU A 301 5568 8120 2996 -340 -644 -346 C
ATOM 2361 CD1 LEU A 301 46.213 114.671 255.255 1.00 43.12 C
ANISOU 2361 CD1 LEU A 301 5499 8088 2797 -383 -740 -402 C
ATOM 2362 CD2 LEU A 301 45.185 115.690 253.105 1.00 42.53 C
ANISOU 2362 CD2 LEU A 301 5402 7852 2904 -427 -577 -377 C
ATOM 2363 N ILE A 302 46.113 110.829 251.221 1.00 40.74 N
ANISOU 2363 N ILE A 302 4954 7819 2705 -57 -603 -134 N
ATOM 2364 CA ILE A 302 46.516 110.156 250.021 1.00 39.86 C
ANISOU 2364 CA ILE A 302 4755 7735 2655 -2 -580 -89 C
ATOM 2365 C ILE A 302 45.778 110.846 248.924 1.00 38.75 C
ANISOU 2365 C ILE A 302 4625 7508 2589 -49 -491 -87 C
ATOM 2366 O ILE A 302 44.568 110.687 248.818 1.00 38.36 O
ANISOU 2366 O ILE A 302 4665 7367 2542 -26 -430 -70 O
ATOM 2367 CB ILE A 302 46.165 108.685 250.088 1.00 39.48 C
ANISOU 2367 CB ILE A 302 4747 7680 2575 120 -579 -34 C
ATOM 2368 CG1 ILE A 302 46.996 108.044 251.185 1.00 40.19 C
ANISOU 2368 CG1 ILE A 302 4822 7860 2589 170 -676 -30 C
ATOM 2369 CG2 ILE A 302 46.461 108.025 248.765 1.00 38.73 C
ANISOU 2369 CG2 ILE A 302 4578 7596 2542 178 -544 5 C
ATOM 2370 CD1 ILE A 302 46.460 106.781 251.684 1.00 40.03 C
ANISOU 2370 CD1 ILE A 302 4886 7810 2514 272 -681 17 C
ATOM 2371 N VAL A 303 46.521 111.618 248.131 1.00 38.92 N
ANISOU 2371 N VAL A 303 4553 7565 2669 -119 -487 -101 N
ATOM 2372 CA VAL A 303 45.980 112.541 247.109 1.00 38.34 C
ANISOU 2372 CA VAL A 303 4486 7414 2666 -185 -412 -102 C
ATOM 2373 C VAL A 303 46.140 112.034 245.664 1.00 37.81 C
ANISOU 2373 C VAL A 303 4350 7361 2656 -145 -364 -56 C
ATOM 2374 O VAL A 303 47.259 111.797 245.184 1.00 38.36 O
ANISOU 2374 O VAL A 303 4307 7525 2741 -138 -389 -48 O
ATOM 2375 CB VAL A 303 46.691 113.930 247.214 1.00 39.16 C
ANISOU 2375 CB VAL A 303 4546 7537 2796 -313 -437 -151 C
ATOM 2376 CG1 VAL A 303 46.134 114.920 246.194 1.00 38.67 C
ANISOU 2376 CG1 VAL A 303 4502 7388 2805 -381 -362 -146 C
ATOM 2377 CG2 VAL A 303 46.680 114.482 248.685 1.00 39.91 C
ANISOU 2377 CG2 VAL A 303 4710 7627 2826 -361 -494 -209 C
ATOM 2378 N LEU A 304 45.028 111.869 244.959 1.00 36.85 N
ANISOU 2378 N LEU A 304 4292 7149 2560 -118 -294 -27 N
ATOM 2379 CA LEU A 304 45.077 111.614 243.496 1.00 36.39 C
ANISOU 2379 CA LEU A 304 4183 7092 2553 -99 -242 10 C
ATOM 2380 C LEU A 304 44.958 112.943 242.750 1.00 36.37 C
ANISOU 2380 C LEU A 304 4168 7044 2605 -200 -199 2 C
ATOM 2381 O LEU A 304 44.020 113.705 242.985 1.00 36.17 O
ANISOU 2381 O LEU A 304 4223 6927 2592 -242 -171 -10 O
ATOM 2382 CB LEU A 304 43.973 110.644 243.089 1.00 35.48 C
ANISOU 2382 CB LEU A 304 4141 6909 2432 -17 -200 48 C
ATOM 2383 CG LEU A 304 43.413 110.621 241.669 1.00 35.48 C
ANISOU 2383 CG LEU A 304 4142 6862 2477 -14 -135 82 C
ATOM 2384 CD1 LEU A 304 44.427 110.019 240.701 1.00 35.11 C
ANISOU 2384 CD1 LEU A 304 4002 6897 2441 25 -133 98 C
ATOM 2385 CD2 LEU A 304 42.113 109.819 241.677 1.00 34.04 C
ANISOU 2385 CD2 LEU A 304 4052 6600 2280 45 -108 109 C
ATOM 2386 N THR A 305 45.898 113.239 241.869 1.00 36.79 N
ANISOU 2386 N THR A 305 4123 7162 2694 -239 -191 11 N
ATOM 2387 CA THR A 305 45.897 114.557 241.267 1.00 36.97 C
ANISOU 2387 CA THR A 305 4138 7143 2765 -346 -157 7 C
ATOM 2388 C THR A 305 46.483 114.650 239.849 1.00 37.58 C
ANISOU 2388 C THR A 305 4131 7265 2882 -367 -113 42 C
ATOM 2389 O THR A 305 47.271 113.791 239.439 1.00 37.86 O
ANISOU 2389 O THR A 305 4084 7394 2906 -309 -119 57 O
ATOM 2390 CB THR A 305 46.629 115.512 242.159 1.00 37.92 C
ANISOU 2390 CB THR A 305 4234 7292 2882 -441 -208 -41 C
ATOM 2391 OG1 THR A 305 46.774 116.747 241.472 1.00 38.24 O
ANISOU 2391 OG1 THR A 305 4261 7294 2974 -550 -175 -39 O
ATOM 2392 CG2 THR A 305 47.987 114.982 242.436 1.00 38.78 C
ANISOU 2392 CG2 THR A 305 4226 7538 2970 -428 -266 -49 C
ATOM 2393 N ASN A 306 46.099 115.708 239.125 1.00 38.20 N
ANISOU 2393 N ASN A 306 4236 7276 3004 -447 -67 55 N
ATOM 2394 CA ASN A 306 46.633 116.002 237.778 1.00 39.24 C
ANISOU 2394 CA ASN A 306 4297 7445 3168 -487 -20 91 C
ATOM 2395 C ASN A 306 47.728 117.080 237.756 1.00 41.16 C
ANISOU 2395 C ASN A 306 4460 7738 3439 -611 -33 77 C
ATOM 2396 O ASN A 306 48.142 117.541 236.683 1.00 41.87 O
ANISOU 2396 O ASN A 306 4500 7851 3559 -667 11 110 O
ATOM 2397 CB ASN A 306 45.502 116.352 236.786 1.00 38.07 C
ANISOU 2397 CB ASN A 306 4227 7194 3045 -489 41 132 C
ATOM 2398 CG ASN A 306 44.944 117.787 236.960 1.00 37.61 C
ANISOU 2398 CG ASN A 306 4239 7029 3024 -585 53 124 C
ATOM 2399 OD1 ASN A 306 44.868 118.315 238.046 1.00 36.95 O
ANISOU 2399 OD1 ASN A 306 4193 6908 2936 -621 18 81 O
ATOM 2400 ND2 ASN A 306 44.519 118.384 235.872 1.00 39.00 N
ANISOU 2400 ND2 ASN A 306 4438 7149 3231 -620 103 167 N
ATOM 2401 N LYS A 307 48.189 117.484 238.941 1.00 42.49 N
ANISOU 2401 N LYS A 307 4621 7926 3597 -660 -95 30 N
ATOM 2402 CA LYS A 307 49.178 118.571 239.066 1.00 44.25 C
ANISOU 2402 CA LYS A 307 4777 8188 3847 -795 -118 10 C
ATOM 2403 C LYS A 307 50.472 118.259 238.338 1.00 45.52 C
ANISOU 2403 C LYS A 307 4786 8492 4020 -811 -111 33 C
ATOM 2404 O LYS A 307 50.789 117.090 238.102 1.00 45.72 O
ANISOU 2404 O LYS A 307 4750 8601 4020 -703 -110 49 O
ATOM 2405 CB LYS A 307 49.490 118.869 240.532 1.00 44.73 C
ANISOU 2405 CB LYS A 307 4854 8260 3881 -835 -197 -51 C
ATOM 2406 CG LYS A 307 50.304 120.126 240.733 1.00 45.74 C
ANISOU 2406 CG LYS A 307 4942 8397 4038 -991 -225 -79 C
ATOM 2407 CD LYS A 307 50.622 120.280 242.177 1.00 48.24 C
ANISOU 2407 CD LYS A 307 5277 8736 4316 -1021 -310 -143 C
ATOM 2408 CE LYS A 307 52.062 120.691 242.344 1.00 51.91 C
ANISOU 2408 CE LYS A 307 5608 9321 4793 -1130 -366 -161 C
ATOM 2409 NZ LYS A 307 52.456 120.572 243.758 1.00 54.00 N
ANISOU 2409 NZ LYS A 307 5876 9636 5005 -1138 -463 -219 N
ATOM 2410 N ASP A 308 51.215 119.312 238.004 1.00 46.93 N
ANISOU 2410 N ASP A 308 4904 8692 4235 -945 -104 36 N
ATOM 2411 CA ASP A 308 52.479 119.190 237.263 1.00 48.64 C
ANISOU 2411 CA ASP A 308 4964 9049 4467 -981 -87 62 C
ATOM 2412 C ASP A 308 52.345 118.454 235.906 1.00 47.91 C
ANISOU 2412 C ASP A 308 4844 8989 4372 -896 -8 116 C
ATOM 2413 O ASP A 308 53.176 117.607 235.577 1.00 47.78 O
ANISOU 2413 O ASP A 308 4711 9103 4342 -830 -1 126 O
ATOM 2414 CB ASP A 308 53.554 118.510 238.125 1.00 49.59 C
ANISOU 2414 CB ASP A 308 4965 9314 4562 -946 -162 31 C
ATOM 2415 CG ASP A 308 53.596 119.040 239.548 1.00 52.21 C
ANISOU 2415 CG ASP A 308 5340 9618 4879 -1010 -250 -27 C
ATOM 2416 OD1 ASP A 308 53.957 120.234 239.752 1.00 56.08 O
ANISOU 2416 OD1 ASP A 308 5827 10083 5397 -1160 -269 -48 O
ATOM 2417 OD2 ASP A 308 53.283 118.248 240.471 1.00 51.96 O
ANISOU 2417 OD2 ASP A 308 5351 9590 4802 -911 -301 -53 O
ATOM 2418 N LYS A 309 51.303 118.781 235.138 1.00 46.87 N
ANISOU 2418 N LYS A 309 4819 8740 4250 -895 51 148 N
ATOM 2419 CA LYS A 309 51.057 118.179 233.807 1.00 46.58 C
ANISOU 2419 CA LYS A 309 4777 8720 4203 -825 124 198 C
ATOM 2420 C LYS A 309 50.789 116.656 233.803 1.00 45.13 C
ANISOU 2420 C LYS A 309 4596 8574 3977 -661 121 194 C
ATOM 2421 O LYS A 309 50.829 116.017 232.745 1.00 44.31 O
ANISOU 2421 O LYS A 309 4470 8509 3856 -599 176 224 O
ATOM 2422 CB LYS A 309 52.160 118.508 232.787 1.00 47.80 C
ANISOU 2422 CB LYS A 309 4806 8982 4372 -897 176 233 C
ATOM 2423 CG LYS A 309 52.744 119.917 232.836 1.00 51.93 C
ANISOU 2423 CG LYS A 309 5296 9496 4938 -1072 173 238 C
ATOM 2424 CD LYS A 309 51.770 121.014 232.395 1.00 55.22 C
ANISOU 2424 CD LYS A 309 5846 9755 5381 -1150 206 267 C
ATOM 2425 CE LYS A 309 52.348 122.411 232.743 1.00 58.61 C
ANISOU 2425 CE LYS A 309 6261 10156 5854 -1326 185 259 C
ATOM 2426 NZ LYS A 309 52.633 122.585 234.229 1.00 59.89 N
ANISOU 2426 NZ LYS A 309 6418 10318 6018 -1358 96 189 N
ATOM 2427 N CYS A 310 50.498 116.086 234.975 1.00 43.86 N
ANISOU 2427 N CYS A 310 4473 8396 3795 -595 59 156 N
ATOM 2428 CA CYS A 310 50.119 114.675 235.047 1.00 42.51 C
ANISOU 2428 CA CYS A 310 4330 8236 3586 -446 53 155 C
ATOM 2429 C CYS A 310 48.634 114.413 234.678 1.00 41.48 C
ANISOU 2429 C CYS A 310 4338 7976 3446 -395 84 174 C
ATOM 2430 O CYS A 310 47.810 114.081 235.556 1.00 40.22 O
ANISOU 2430 O CYS A 310 4264 7746 3270 -349 49 155 O
ATOM 2431 CB CYS A 310 50.451 114.118 236.429 1.00 42.84 C
ANISOU 2431 CB CYS A 310 4355 8318 3604 -396 -27 116 C
ATOM 2432 SG CYS A 310 52.188 114.229 236.869 1.00 41.94 S
ANISOU 2432 SG CYS A 310 4064 8374 3497 -438 -76 96 S
ATOM 2433 N VAL A 311 48.318 114.541 233.380 1.00 40.86 N
ANISOU 2433 N VAL A 311 4276 7876 3374 -403 149 213 N
ATOM 2434 CA VAL A 311 46.919 114.503 232.890 1.00 39.88 C
ANISOU 2434 CA VAL A 311 4272 7633 3246 -377 176 238 C
ATOM 2435 C VAL A 311 46.095 113.272 233.266 1.00 38.78 C
ANISOU 2435 C VAL A 311 4203 7455 3075 -260 156 229 C
ATOM 2436 O VAL A 311 44.928 113.393 233.618 1.00 38.18 O
ANISOU 2436 O VAL A 311 4223 7279 3004 -254 149 232 O
ATOM 2437 CB VAL A 311 46.809 114.713 231.353 1.00 39.68 C
ANISOU 2437 CB VAL A 311 4247 7609 3221 -398 244 284 C
ATOM 2438 CG1 VAL A 311 47.403 116.048 230.971 1.00 42.48 C
ANISOU 2438 CG1 VAL A 311 4556 7974 3609 -528 268 304 C
ATOM 2439 CG2 VAL A 311 47.510 113.604 230.592 1.00 39.42 C
ANISOU 2439 CG2 VAL A 311 4148 7677 3152 -315 273 288 C
ATOM 2440 N ASN A 312 46.686 112.092 233.148 1.00 39.02 N
ANISOU 2440 N ASN A 312 4187 7563 3075 -167 152 221 N
ATOM 2441 CA ASN A 312 45.995 110.861 233.495 1.00 38.70 C
ANISOU 2441 CA ASN A 312 4216 7483 3005 -60 132 214 C
ATOM 2442 C ASN A 312 45.982 110.606 235.001 1.00 38.72 C
ANISOU 2442 C ASN A 312 4236 7479 2998 -35 68 185 C
ATOM 2443 O ASN A 312 45.330 109.668 235.454 1.00 37.96 O
ANISOU 2443 O ASN A 312 4208 7338 2876 42 48 183 O
ATOM 2444 CB ASN A 312 46.642 109.669 232.783 1.00 39.60 C
ANISOU 2444 CB ASN A 312 4287 7672 3089 38 152 215 C
ATOM 2445 CG ASN A 312 46.323 109.613 231.308 1.00 40.96 C
ANISOU 2445 CG ASN A 312 4482 7831 3251 37 214 243 C
ATOM 2446 OD1 ASN A 312 45.689 110.508 230.754 1.00 43.13 O
ANISOU 2446 OD1 ASN A 312 4795 8049 3542 -40 241 268 O
ATOM 2447 ND2 ASN A 312 46.749 108.541 230.660 1.00 42.85 N
ANISOU 2447 ND2 ASN A 312 4703 8119 3458 129 237 237 N
ATOM 2448 N GLY A 313 46.730 111.418 235.760 1.00 39.27 N
ANISOU 2448 N GLY A 313 4245 7593 3082 -104 35 162 N
ATOM 2449 CA GLY A 313 46.742 111.343 237.213 1.00 39.37 C
ANISOU 2449 CA GLY A 313 4278 7602 3077 -95 -28 132 C
ATOM 2450 C GLY A 313 47.958 110.666 237.845 1.00 40.59 C
ANISOU 2450 C GLY A 313 4340 7872 3209 -41 -80 114 C
ATOM 2451 O GLY A 313 48.648 109.850 237.214 1.00 41.71 O
ANISOU 2451 O GLY A 313 4416 8088 3344 32 -66 125 O
ATOM 2452 N LYS A 314 48.229 111.027 239.097 1.00 40.30 N
ANISOU 2452 N LYS A 314 4300 7852 3160 -75 -142 85 N
ATOM 2453 CA LYS A 314 49.304 110.437 239.884 1.00 40.99 C
ANISOU 2453 CA LYS A 314 4306 8047 3222 -25 -207 70 C
ATOM 2454 C LYS A 314 48.871 110.492 241.364 1.00 41.17 C
ANISOU 2454 C LYS A 314 4405 8030 3207 -30 -270 45 C
ATOM 2455 O LYS A 314 48.213 111.442 241.791 1.00 41.31 O
ANISOU 2455 O LYS A 314 4492 7973 3231 -113 -267 25 O
ATOM 2456 CB LYS A 314 50.626 111.192 239.665 1.00 41.74 C
ANISOU 2456 CB LYS A 314 4259 8255 3344 -105 -220 59 C
ATOM 2457 CG LYS A 314 50.611 112.625 240.158 1.00 41.15 C
ANISOU 2457 CG LYS A 314 4195 8149 3290 -250 -239 32 C
ATOM 2458 CD LYS A 314 51.926 113.357 239.974 1.00 41.74 C
ANISOU 2458 CD LYS A 314 4128 8338 3395 -344 -256 23 C
ATOM 2459 CE LYS A 314 51.846 114.723 240.704 1.00 42.34 C
ANISOU 2459 CE LYS A 314 4241 8364 3483 -488 -290 -12 C
ATOM 2460 NZ LYS A 314 53.130 115.445 240.895 1.00 42.71 N
ANISOU 2460 NZ LYS A 314 4157 8520 3551 -596 -333 -30 N
ATOM 2461 N VAL A 315 49.211 109.472 242.137 1.00 41.13 N
ANISOU 2461 N VAL A 315 4396 8072 3159 64 -325 46 N
ATOM 2462 CA VAL A 315 48.772 109.439 243.515 1.00 41.02 C
ANISOU 2462 CA VAL A 315 4462 8024 3098 66 -381 27 C
ATOM 2463 C VAL A 315 49.968 109.695 244.431 1.00 42.85 C
ANISOU 2463 C VAL A 315 4604 8369 3307 37 -467 1 C
ATOM 2464 O VAL A 315 51.029 109.046 244.351 1.00 44.18 O
ANISOU 2464 O VAL A 315 4666 8646 3472 101 -504 12 O
ATOM 2465 CB VAL A 315 47.918 108.175 243.856 1.00 39.97 C
ANISOU 2465 CB VAL A 315 4434 7828 2925 179 -380 53 C
ATOM 2466 CG1 VAL A 315 48.667 106.926 243.600 1.00 41.01 C
ANISOU 2466 CG1 VAL A 315 4508 8028 3044 298 -401 77 C
ATOM 2467 CG2 VAL A 315 47.472 108.209 245.258 1.00 38.48 C
ANISOU 2467 CG2 VAL A 315 4328 7611 2682 172 -429 37 C
ATOM 2468 N VAL A 316 49.778 110.691 245.281 1.00 42.80 N
ANISOU 2468 N VAL A 316 4640 8336 3286 -60 -498 -37 N
ATOM 2469 CA VAL A 316 50.835 111.282 246.041 1.00 43.18 C
ANISOU 2469 CA VAL A 316 4607 8481 3320 -130 -576 -70 C
ATOM 2470 C VAL A 316 50.536 110.977 247.497 1.00 43.08 C
ANISOU 2470 C VAL A 316 4681 8458 3231 -101 -645 -89 C
ATOM 2471 O VAL A 316 49.423 110.571 247.839 1.00 41.22 O
ANISOU 2471 O VAL A 316 4570 8128 2964 -53 -616 -79 O
ATOM 2472 CB VAL A 316 50.841 112.787 245.745 1.00 43.21 C
ANISOU 2472 CB VAL A 316 4602 8448 3367 -281 -550 -103 C
ATOM 2473 CG1 VAL A 316 50.412 113.611 246.963 1.00 44.33 C
ANISOU 2473 CG1 VAL A 316 4841 8534 3468 -359 -593 -153 C
ATOM 2474 CG2 VAL A 316 52.173 113.188 245.302 1.00 44.83 C
ANISOU 2474 CG2 VAL A 316 4651 8773 3609 -343 -576 -105 C
ATOM 2475 N LEU A 317 51.535 111.177 248.349 1.00 44.75 N
ANISOU 2475 N LEU A 317 4822 8772 3410 -135 -737 -115 N
ATOM 2476 CA LEU A 317 51.405 110.939 249.792 1.00 45.80 C
ANISOU 2476 CA LEU A 317 5032 8914 3458 -115 -814 -134 C
ATOM 2477 C LEU A 317 51.948 112.127 250.605 1.00 47.15 C
ANISOU 2477 C LEU A 317 5186 9123 3607 -249 -882 -195 C
ATOM 2478 O LEU A 317 53.086 112.577 250.406 1.00 48.11 O
ANISOU 2478 O LEU A 317 5173 9348 3758 -315 -929 -208 O
ATOM 2479 CB LEU A 317 52.136 109.648 250.143 1.00 46.52 C
ANISOU 2479 CB LEU A 317 5061 9104 3510 13 -881 -96 C
ATOM 2480 CG LEU A 317 51.613 108.596 251.114 1.00 47.02 C
ANISOU 2480 CG LEU A 317 5233 9141 3493 119 -918 -70 C
ATOM 2481 CD1 LEU A 317 52.338 107.284 250.825 1.00 46.60 C
ANISOU 2481 CD1 LEU A 317 5100 9165 3442 260 -949 -18 C
ATOM 2482 CD2 LEU A 317 51.821 109.039 252.592 1.00 49.82 C
ANISOU 2482 CD2 LEU A 317 5633 9535 3762 64 -1012 -109 C
ATOM 2483 N THR A 318 51.124 112.646 251.507 1.00 47.71 N
ANISOU 2483 N THR A 318 5392 9111 3625 -294 -884 -234 N
ATOM 2484 CA THR A 318 51.525 113.779 252.325 1.00 49.83 C
ANISOU 2484 CA THR A 318 5672 9397 3864 -422 -946 -300 C
ATOM 2485 C THR A 318 50.910 113.732 253.699 1.00 50.12 C
ANISOU 2485 C THR A 318 5847 9397 3800 -410 -985 -333 C
ATOM 2486 O THR A 318 50.149 112.826 253.995 1.00 49.09 O
ANISOU 2486 O THR A 318 5800 9227 3626 -306 -959 -297 O
ATOM 2487 CB THR A 318 51.195 115.136 251.646 1.00 49.88 C
ANISOU 2487 CB THR A 318 5699 9314 3941 -549 -879 -336 C
ATOM 2488 OG1 THR A 318 51.757 116.212 252.434 1.00 53.44 O
ANISOU 2488 OG1 THR A 318 6153 9787 4364 -681 -951 -404 O
ATOM 2489 CG2 THR A 318 49.680 115.328 251.474 1.00 47.41 C
ANISOU 2489 CG2 THR A 318 5534 8845 3635 -524 -780 -335 C
ATOM 2490 N LYS A 319 51.240 114.722 254.527 1.00 52.18 N
ANISOU 2490 N LYS A 319 6136 9670 4021 -523 -1045 -401 N
ATOM 2491 CA LYS A 319 50.764 114.764 255.924 1.00 53.67 C
ANISOU 2491 CA LYS A 319 6458 9836 4097 -522 -1089 -442 C
ATOM 2492 C LYS A 319 49.743 115.863 256.218 1.00 53.78 C
ANISOU 2492 C LYS A 319 6616 9715 4103 -599 -1023 -504 C
ATOM 2493 O LYS A 319 49.727 116.899 255.563 1.00 54.34 O
ANISOU 2493 O LYS A 319 6673 9725 4247 -694 -981 -535 O
ATOM 2494 CB LYS A 319 51.934 114.810 256.895 1.00 54.66 C
ANISOU 2494 CB LYS A 319 6522 10095 4152 -566 -1228 -473 C
ATOM 2495 CG LYS A 319 52.654 113.485 256.972 1.00 56.55 C
ANISOU 2495 CG LYS A 319 6665 10456 4367 -446 -1295 -405 C
ATOM 2496 CD LYS A 319 54.180 113.664 256.997 1.00 61.70 C
ANISOU 2496 CD LYS A 319 7145 11264 5035 -502 -1408 -414 C
ATOM 2497 CE LYS A 319 54.928 112.301 256.918 1.00 64.46 C
ANISOU 2497 CE LYS A 319 7382 11735 5376 -361 -1466 -339 C
ATOM 2498 NZ LYS A 319 56.435 112.393 257.112 1.00 64.90 N
ANISOU 2498 NZ LYS A 319 7260 11962 5435 -402 -1589 -344 N
ATOM 2499 N ARG A 320 48.879 115.604 257.195 1.00 54.26 N
ANISOU 2499 N ARG A 320 6815 9727 4073 -552 -1011 -519 N
ATOM 2500 CA ARG A 320 47.793 116.507 257.576 1.00 54.38 C
ANISOU 2500 CA ARG A 320 6977 9616 4070 -598 -939 -576 C
ATOM 2501 C ARG A 320 48.355 117.845 258.010 1.00 55.40 C
ANISOU 2501 C ARG A 320 7123 9737 4189 -740 -991 -666 C
ATOM 2502 O ARG A 320 47.731 118.900 257.847 1.00 55.46 O
ANISOU 2502 O ARG A 320 7211 9629 4232 -805 -926 -716 O
ATOM 2503 CB ARG A 320 46.980 115.900 258.727 1.00 54.31 C
ANISOU 2503 CB ARG A 320 7100 9591 3945 -523 -932 -576 C
ATOM 2504 CG ARG A 320 45.583 116.485 258.814 1.00 55.92 C
ANISOU 2504 CG ARG A 320 7439 9658 4152 -521 -818 -605 C
ATOM 2505 CD ARG A 320 45.020 116.487 260.228 1.00 59.85 C
ANISOU 2505 CD ARG A 320 8078 10146 4515 -506 -825 -650 C
ATOM 2506 NE ARG A 320 43.992 115.466 260.454 1.00 61.41 N
ANISOU 2506 NE ARG A 320 8341 10319 4672 -396 -758 -588 N
ATOM 2507 CZ ARG A 320 42.726 115.724 260.787 1.00 62.11 C
ANISOU 2507 CZ ARG A 320 8545 10316 4736 -372 -658 -605 C
ATOM 2508 NH1 ARG A 320 42.304 116.980 260.914 1.00 61.42 N
ANISOU 2508 NH1 ARG A 320 8529 10145 4663 -439 -611 -685 N
ATOM 2509 NH2 ARG A 320 41.880 114.718 261.007 1.00 62.41 N
ANISOU 2509 NH2 ARG A 320 8631 10347 4737 -281 -604 -542 N
ATOM 2510 N SER A 321 49.549 117.766 258.563 1.00 56.42 N
ANISOU 2510 N SER A 321 7175 9990 4271 -786 -1113 -685 N
ATOM 2511 CA SER A 321 50.210 118.882 259.167 1.00 57.99 C
ANISOU 2511 CA SER A 321 7390 10203 4439 -926 -1189 -772 C
ATOM 2512 C SER A 321 50.968 119.719 258.156 1.00 58.52 C
ANISOU 2512 C SER A 321 7341 10272 4620 -1039 -1191 -780 C
ATOM 2513 O SER A 321 51.240 120.877 258.427 1.00 60.12 O
ANISOU 2513 O SER A 321 7583 10436 4825 -1171 -1220 -856 O
ATOM 2514 CB SER A 321 51.191 118.358 260.193 1.00 59.22 C
ANISOU 2514 CB SER A 321 7501 10507 4492 -926 -1330 -780 C
ATOM 2515 OG SER A 321 51.972 117.334 259.614 1.00 58.33 O
ANISOU 2515 OG SER A 321 7230 10512 4421 -850 -1371 -699 O
ATOM 2516 N ALA A 322 51.342 119.134 257.018 1.00 57.32 N
ANISOU 2516 N ALA A 322 7051 10169 4559 -990 -1162 -704 N
ATOM 2517 CA ALA A 322 52.020 119.868 255.948 1.00 57.03 C
ANISOU 2517 CA ALA A 322 6900 10137 4632 -1092 -1148 -699 C
ATOM 2518 C ALA A 322 51.409 119.434 254.598 1.00 55.24 C
ANISOU 2518 C ALA A 322 6638 9852 4500 -1011 -1030 -624 C
ATOM 2519 O ALA A 322 52.054 118.775 253.751 1.00 54.40 O
ANISOU 2519 O ALA A 322 6388 9834 4447 -967 -1030 -561 O
ATOM 2520 CB ALA A 322 53.526 119.653 256.013 1.00 58.19 C
ANISOU 2520 CB ALA A 322 6874 10455 4780 -1143 -1263 -690 C
ATOM 2521 N PRO A 323 50.129 119.789 254.419 1.00 54.02 N
ANISOU 2521 N PRO A 323 6616 9549 4361 -984 -930 -631 N
ATOM 2522 CA PRO A 323 49.310 119.237 253.362 1.00 52.61 C
ANISOU 2522 CA PRO A 323 6434 9309 4245 -888 -825 -562 C
ATOM 2523 C PRO A 323 49.569 119.803 251.949 1.00 52.66 C
ANISOU 2523 C PRO A 323 6356 9287 4366 -949 -768 -530 C
ATOM 2524 O PRO A 323 48.904 119.379 250.997 1.00 51.50 O
ANISOU 2524 O PRO A 323 6207 9091 4270 -875 -684 -473 O
ATOM 2525 CB PRO A 323 47.891 119.534 253.855 1.00 51.83 C
ANISOU 2525 CB PRO A 323 6507 9074 4114 -852 -753 -590 C
ATOM 2526 CG PRO A 323 48.014 120.733 254.674 1.00 52.01 C
ANISOU 2526 CG PRO A 323 6614 9048 4102 -967 -789 -681 C
ATOM 2527 CD PRO A 323 49.355 120.685 255.300 1.00 53.97 C
ANISOU 2527 CD PRO A 323 6775 9430 4302 -1035 -914 -709 C
ATOM 2528 N THR A 324 50.519 120.727 251.795 1.00 54.08 N
ANISOU 2528 N THR A 324 6467 9499 4580 -1084 -813 -563 N
ATOM 2529 CA THR A 324 50.893 121.148 250.440 1.00 54.24 C
ANISOU 2529 CA THR A 324 6393 9514 4701 -1141 -761 -521 C
ATOM 2530 C THR A 324 52.162 120.470 249.922 1.00 55.11 C
ANISOU 2530 C THR A 324 6317 9789 4835 -1133 -807 -476 C
ATOM 2531 O THR A 324 52.517 120.622 248.746 1.00 55.47 O
ANISOU 2531 O THR A 324 6270 9851 4955 -1162 -757 -431 O
ATOM 2532 CB THR A 324 50.959 122.689 250.249 1.00 55.21 C
ANISOU 2532 CB THR A 324 6565 9537 4873 -1299 -746 -569 C
ATOM 2533 OG1 THR A 324 51.839 123.290 251.209 1.00 55.44 O
ANISOU 2533 OG1 THR A 324 6583 9621 4860 -1417 -849 -638 O
ATOM 2534 CG2 THR A 324 49.574 123.288 250.361 1.00 53.75 C
ANISOU 2534 CG2 THR A 324 6553 9177 4692 -1276 -668 -593 C
ATOM 2535 N ASP A 325 52.826 119.716 250.793 1.00 55.95 N
ANISOU 2535 N ASP A 325 6367 10018 4873 -1087 -900 -484 N
ATOM 2536 CA ASP A 325 54.016 118.965 250.415 1.00 56.92 C
ANISOU 2536 CA ASP A 325 6308 10306 5013 -1055 -948 -441 C
ATOM 2537 C ASP A 325 53.629 117.688 249.696 1.00 55.08 C
ANISOU 2537 C ASP A 325 6047 10089 4792 -892 -887 -370 C
ATOM 2538 O ASP A 325 53.208 116.706 250.312 1.00 54.04 O
ANISOU 2538 O ASP A 325 5970 9964 4599 -771 -907 -356 O
ATOM 2539 CB ASP A 325 54.884 118.643 251.640 1.00 59.10 C
ANISOU 2539 CB ASP A 325 6534 10709 5211 -1062 -1079 -474 C
ATOM 2540 CG ASP A 325 56.255 118.073 251.257 1.00 62.75 C
ANISOU 2540 CG ASP A 325 6787 11353 5702 -1048 -1137 -435 C
ATOM 2541 OD1 ASP A 325 56.878 118.595 250.298 1.00 67.25 O
ANISOU 2541 OD1 ASP A 325 7243 11959 6351 -1132 -1103 -417 O
ATOM 2542 OD2 ASP A 325 56.715 117.105 251.915 1.00 64.74 O
ANISOU 2542 OD2 ASP A 325 6988 11714 5896 -950 -1215 -418 O
ATOM 2543 N TRP A 326 53.777 117.718 248.377 1.00 54.45 N
ANISOU 2543 N TRP A 326 5888 10011 4789 -895 -812 -324 N
ATOM 2544 CA TRP A 326 53.378 116.600 247.541 1.00 52.98 C
ANISOU 2544 CA TRP A 326 5684 9826 4619 -752 -746 -262 C
ATOM 2545 C TRP A 326 54.545 116.011 246.793 1.00 53.22 C
ANISOU 2545 C TRP A 326 5534 10003 4685 -718 -754 -221 C
ATOM 2546 O TRP A 326 54.379 115.496 245.690 1.00 52.77 O
ANISOU 2546 O TRP A 326 5444 9941 4666 -649 -678 -175 O
ATOM 2547 CB TRP A 326 52.322 117.043 246.548 1.00 52.08 C
ANISOU 2547 CB TRP A 326 5657 9574 4556 -762 -635 -241 C
ATOM 2548 CG TRP A 326 51.012 117.409 247.184 1.00 51.83 C
ANISOU 2548 CG TRP A 326 5802 9399 4494 -757 -610 -270 C
ATOM 2549 CD1 TRP A 326 50.683 117.323 248.503 1.00 51.08 C
ANISOU 2549 CD1 TRP A 326 5797 9286 4326 -741 -666 -313 C
ATOM 2550 CD2 TRP A 326 49.844 117.876 246.508 1.00 51.43 C
ANISOU 2550 CD2 TRP A 326 5852 9208 4482 -759 -518 -256 C
ATOM 2551 NE1 TRP A 326 49.400 117.742 248.696 1.00 50.87 N
ANISOU 2551 NE1 TRP A 326 5917 9118 4292 -735 -608 -329 N
ATOM 2552 CE2 TRP A 326 48.852 118.078 247.486 1.00 51.00 C
ANISOU 2552 CE2 TRP A 326 5940 9058 4380 -743 -520 -294 C
ATOM 2553 CE3 TRP A 326 49.541 118.156 245.170 1.00 51.69 C
ANISOU 2553 CE3 TRP A 326 5869 9191 4582 -772 -436 -213 C
ATOM 2554 CZ2 TRP A 326 47.568 118.553 247.171 1.00 49.45 C
ANISOU 2554 CZ2 TRP A 326 5860 8721 4209 -735 -441 -290 C
ATOM 2555 CZ3 TRP A 326 48.254 118.620 244.859 1.00 50.63 C
ANISOU 2555 CZ3 TRP A 326 5855 8912 4468 -766 -366 -207 C
ATOM 2556 CH2 TRP A 326 47.294 118.816 245.862 1.00 48.32 C
ANISOU 2556 CH2 TRP A 326 5693 8531 4136 -746 -369 -245 C
ATOM 2557 N GLY A 327 55.729 116.095 247.393 1.00 53.96 N
ANISOU 2557 N GLY A 327 5507 10231 4763 -766 -848 -241 N
ATOM 2558 CA GLY A 327 56.937 115.603 246.762 1.00 53.56 C
ANISOU 2558 CA GLY A 327 5266 10337 4748 -737 -861 -205 C
ATOM 2559 C GLY A 327 57.028 114.095 246.820 1.00 52.55 C
ANISOU 2559 C GLY A 327 5107 10274 4587 -550 -874 -166 C
ATOM 2560 O GLY A 327 57.759 113.497 246.041 1.00 52.92 O
ANISOU 2560 O GLY A 327 5018 10422 4668 -483 -849 -128 O
ATOM 2561 N THR A 328 56.304 113.475 247.747 1.00 51.46 N
ANISOU 2561 N THR A 328 5095 10076 4383 -463 -910 -173 N
ATOM 2562 CA THR A 328 56.336 112.022 247.858 1.00 50.72 C
ANISOU 2562 CA THR A 328 4992 10025 4255 -285 -925 -132 C
ATOM 2563 C THR A 328 55.325 111.465 246.921 1.00 48.97 C
ANISOU 2563 C THR A 328 4859 9691 4056 -200 -817 -98 C
ATOM 2564 O THR A 328 54.158 111.794 247.007 1.00 48.19 O
ANISOU 2564 O THR A 328 4907 9456 3947 -225 -770 -110 O
ATOM 2565 CB THR A 328 55.940 111.525 249.215 1.00 50.79 C
ANISOU 2565 CB THR A 328 5108 10013 4178 -228 -1004 -144 C
ATOM 2566 OG1 THR A 328 56.381 112.456 250.212 1.00 51.79 O
ANISOU 2566 OG1 THR A 328 5228 10181 4270 -355 -1093 -196 O
ATOM 2567 CG2 THR A 328 56.541 110.130 249.423 1.00 51.12 C
ANISOU 2567 CG2 THR A 328 5080 10151 4190 -64 -1055 -100 C
ATOM 2568 N VAL A 329 55.760 110.614 246.015 1.00 48.85 N
ANISOU 2568 N VAL A 329 4756 9734 4072 -97 -776 -58 N
ATOM 2569 CA VAL A 329 54.862 110.141 245.001 1.00 47.28 C
ANISOU 2569 CA VAL A 329 4635 9434 3896 -30 -675 -30 C
ATOM 2570 C VAL A 329 54.757 108.659 245.160 1.00 47.04 C
ANISOU 2570 C VAL A 329 4634 9409 3831 143 -689 2 C
ATOM 2571 O VAL A 329 55.757 107.976 245.137 1.00 48.38 O
ANISOU 2571 O VAL A 329 4686 9695 4001 227 -727 19 O
ATOM 2572 CB VAL A 329 55.358 110.532 243.600 1.00 47.80 C
ANISOU 2572 CB VAL A 329 4592 9542 4028 -72 -595 -14 C
ATOM 2573 CG1 VAL A 329 54.509 109.843 242.513 1.00 46.17 C
ANISOU 2573 CG1 VAL A 329 4463 9246 3834 17 -498 17 C
ATOM 2574 CG2 VAL A 329 55.334 112.067 243.433 1.00 47.19 C
ANISOU 2574 CG2 VAL A 329 4511 9433 3987 -255 -577 -41 C
ATOM 2575 N LEU A 330 53.546 108.160 245.348 1.00 45.93 N
ANISOU 2575 N LEU A 330 4651 9141 3660 196 -659 13 N
ATOM 2576 CA LEU A 330 53.361 106.744 245.569 1.00 46.15 C
ANISOU 2576 CA LEU A 330 4729 9154 3652 352 -674 46 C
ATOM 2577 C LEU A 330 53.271 106.008 244.248 1.00 46.23 C
ANISOU 2577 C LEU A 330 4722 9143 3699 439 -592 73 C
ATOM 2578 O LEU A 330 54.110 105.165 243.955 1.00 47.35 O
ANISOU 2578 O LEU A 330 4775 9368 3846 547 -606 91 O
ATOM 2579 CB LEU A 330 52.111 106.494 246.395 1.00 45.45 C
ANISOU 2579 CB LEU A 330 4814 8943 3512 364 -679 48 C
ATOM 2580 CG LEU A 330 51.923 105.021 246.736 1.00 45.29 C
ANISOU 2580 CG LEU A 330 4857 8901 3449 516 -702 86 C
ATOM 2581 CD1 LEU A 330 52.900 104.605 247.826 1.00 46.94 C
ANISOU 2581 CD1 LEU A 330 5006 9219 3610 571 -812 92 C
ATOM 2582 CD2 LEU A 330 50.503 104.757 247.159 1.00 43.62 C
ANISOU 2582 CD2 LEU A 330 4818 8553 3203 519 -671 97 C
ATOM 2583 N ILE A 331 52.242 106.324 243.460 1.00 45.61 N
ANISOU 2583 N ILE A 331 4731 8954 3644 395 -509 75 N
ATOM 2584 CA ILE A 331 52.117 105.836 242.073 1.00 45.24 C
ANISOU 2584 CA ILE A 331 4673 8886 3631 450 -426 94 C
ATOM 2585 C ILE A 331 52.336 106.945 241.050 1.00 45.25 C
ANISOU 2585 C ILE A 331 4602 8909 3682 337 -363 84 C
ATOM 2586 O ILE A 331 51.534 107.891 241.015 1.00 44.27 O
ANISOU 2586 O ILE A 331 4548 8702 3571 230 -336 74 O
ATOM 2587 CB ILE A 331 50.747 105.252 241.832 1.00 43.71 C
ANISOU 2587 CB ILE A 331 4636 8551 3423 490 -380 110 C
ATOM 2588 CG1 ILE A 331 50.660 103.912 242.534 1.00 44.63 C
ANISOU 2588 CG1 ILE A 331 4816 8648 3494 621 -426 130 C
ATOM 2589 CG2 ILE A 331 50.522 105.048 240.369 1.00 43.26 C
ANISOU 2589 CG2 ILE A 331 4576 8466 3397 510 -295 121 C
ATOM 2590 CD1 ILE A 331 49.295 103.602 242.998 1.00 44.74 C
ANISOU 2590 CD1 ILE A 331 4988 8531 3479 620 -416 142 C
ATOM 2591 N PRO A 332 53.405 106.828 240.208 1.00 46.26 N
ANISOU 2591 N PRO A 332 4592 9148 3838 363 -336 90 N
ATOM 2592 CA PRO A 332 53.751 107.923 239.281 1.00 46.44 C
ANISOU 2592 CA PRO A 332 4535 9206 3904 246 -278 87 C
ATOM 2593 C PRO A 332 52.852 107.950 238.049 1.00 45.72 C
ANISOU 2593 C PRO A 332 4525 9020 3825 239 -185 103 C
ATOM 2594 O PRO A 332 52.103 106.997 237.803 1.00 44.85 O
ANISOU 2594 O PRO A 332 4515 8833 3693 336 -164 115 O
ATOM 2595 CB PRO A 332 55.224 107.646 238.915 1.00 47.36 C
ANISOU 2595 CB PRO A 332 4469 9487 4038 290 -282 91 C
ATOM 2596 CG PRO A 332 55.641 106.433 239.703 1.00 47.36 C
ANISOU 2596 CG PRO A 332 4456 9534 4005 438 -350 95 C
ATOM 2597 CD PRO A 332 54.357 105.709 240.070 1.00 46.92 C
ANISOU 2597 CD PRO A 332 4584 9330 3913 504 -353 102 C
ATOM 2598 N HIS A 333 52.900 109.057 237.315 1.00 46.49 N
ANISOU 2598 N HIS A 333 4588 9119 3956 119 -135 107 N
ATOM 2599 CA HIS A 333 52.014 109.274 236.181 1.00 46.44 C
ANISOU 2599 CA HIS A 333 4663 9023 3960 94 -55 125 C
ATOM 2600 C HIS A 333 52.470 108.385 235.046 1.00 47.54 C
ANISOU 2600 C HIS A 333 4753 9221 4091 193 5 140 C
ATOM 2601 O HIS A 333 53.668 108.268 234.814 1.00 49.22 O
ANISOU 2601 O HIS A 333 4826 9562 4312 215 11 139 O
ATOM 2602 CB HIS A 333 52.069 110.747 235.759 1.00 46.42 C
ANISOU 2602 CB HIS A 333 4633 9012 3994 -63 -24 130 C
ATOM 2603 CG HIS A 333 51.174 111.106 234.592 1.00 46.06 C
ANISOU 2603 CG HIS A 333 4667 8877 3956 -97 53 156 C
ATOM 2604 ND1 HIS A 333 51.668 111.419 233.341 1.00 43.56 N
ANISOU 2604 ND1 HIS A 333 4284 8614 3651 -133 123 180 N
ATOM 2605 CD2 HIS A 333 49.827 111.244 234.503 1.00 44.13 C
ANISOU 2605 CD2 HIS A 333 4560 8498 3708 -106 67 165 C
ATOM 2606 CE1 HIS A 333 50.670 111.733 232.538 1.00 41.95 C
ANISOU 2606 CE1 HIS A 333 4179 8313 3448 -161 171 203 C
ATOM 2607 NE2 HIS A 333 49.542 111.631 233.214 1.00 41.70 N
ANISOU 2607 NE2 HIS A 333 4267 8168 3411 -143 137 195 N
ATOM 2608 N ASP A 334 51.522 107.732 234.377 1.00 47.58 N
ANISOU 2608 N ASP A 334 4869 9133 4076 255 47 151 N
ATOM 2609 CA ASP A 334 51.790 106.960 233.166 1.00 48.56 C
ANISOU 2609 CA ASP A 334 4974 9293 4185 339 113 159 C
ATOM 2610 C ASP A 334 50.954 107.524 232.008 1.00 48.03 C
ANISOU 2610 C ASP A 334 4979 9151 4118 269 181 179 C
ATOM 2611 O ASP A 334 49.754 107.817 232.181 1.00 46.35 O
ANISOU 2611 O ASP A 334 4884 8821 3907 227 171 187 O
ATOM 2612 CB ASP A 334 51.491 105.460 233.373 1.00 48.39 C
ANISOU 2612 CB ASP A 334 5027 9230 4130 492 93 152 C
ATOM 2613 CG ASP A 334 52.056 104.566 232.232 1.00 51.02 C
ANISOU 2613 CG ASP A 334 5323 9619 4443 599 156 148 C
ATOM 2614 OD1 ASP A 334 51.959 104.908 231.021 1.00 51.81 O
ANISOU 2614 OD1 ASP A 334 5423 9725 4539 560 230 157 O
ATOM 2615 OD2 ASP A 334 52.611 103.495 232.547 1.00 52.97 O
ANISOU 2615 OD2 ASP A 334 5546 9904 4676 730 133 137 O
ATOM 2616 N ASP A 335 51.609 107.694 230.849 1.00 49.16 N
ANISOU 2616 N ASP A 335 5047 9373 4260 258 251 190 N
ATOM 2617 CA ASP A 335 50.948 108.122 229.593 1.00 49.09 C
ANISOU 2617 CA ASP A 335 5101 9311 4239 205 319 213 C
ATOM 2618 C ASP A 335 49.773 107.215 229.247 1.00 48.00 C
ANISOU 2618 C ASP A 335 5107 9062 4068 281 322 212 C
ATOM 2619 O ASP A 335 48.692 107.699 228.939 1.00 47.13 O
ANISOU 2619 O ASP A 335 5092 8855 3959 219 329 231 O
ATOM 2620 CB ASP A 335 51.928 108.141 228.405 1.00 50.39 C
ANISOU 2620 CB ASP A 335 5164 9591 4390 212 398 223 C
ATOM 2621 CG ASP A 335 52.879 109.344 228.425 1.00 53.26 C
ANISOU 2621 CG ASP A 335 5396 10051 4790 89 413 238 C
ATOM 2622 OD1 ASP A 335 52.457 110.412 228.961 1.00 53.90 O
ANISOU 2622 OD1 ASP A 335 5506 10070 4903 -30 379 248 O
ATOM 2623 OD2 ASP A 335 54.034 109.214 227.887 1.00 54.24 O
ANISOU 2623 OD2 ASP A 335 5389 10309 4910 110 461 239 O
ATOM 2624 N LYS A 336 49.973 105.901 229.301 1.00 48.26 N
ANISOU 2624 N LYS A 336 5157 9106 4073 414 315 191 N
ATOM 2625 CA LYS A 336 48.924 104.997 228.847 1.00 47.71 C
ANISOU 2625 CA LYS A 336 5225 8934 3971 478 321 188 C
ATOM 2626 C LYS A 336 48.006 104.493 229.943 1.00 46.11 C
ANISOU 2626 C LYS A 336 5119 8628 3771 505 254 184 C
ATOM 2627 O LYS A 336 47.144 103.656 229.698 1.00 45.74 O
ANISOU 2627 O LYS A 336 5185 8496 3700 555 251 182 O
ATOM 2628 CB LYS A 336 49.422 103.867 227.899 1.00 49.18 C
ANISOU 2628 CB LYS A 336 5411 9161 4114 597 370 169 C
ATOM 2629 CG LYS A 336 50.716 103.136 228.268 1.00 52.41 C
ANISOU 2629 CG LYS A 336 5714 9677 4523 709 366 146 C
ATOM 2630 CD LYS A 336 51.878 103.485 227.305 1.00 54.56 C
ANISOU 2630 CD LYS A 336 5856 10086 4790 707 443 145 C
ATOM 2631 CE LYS A 336 53.164 102.766 227.750 1.00 55.97 C
ANISOU 2631 CE LYS A 336 5913 10378 4974 827 435 125 C
ATOM 2632 NZ LYS A 336 54.364 103.617 227.567 1.00 57.66 N
ANISOU 2632 NZ LYS A 336 5950 10744 5215 767 470 135 N
ATOM 2633 N VAL A 337 48.146 105.028 231.144 1.00 45.50 N
ANISOU 2633 N VAL A 337 5008 8559 3722 462 200 184 N
ATOM 2634 CA VAL A 337 47.196 104.679 232.192 1.00 44.13 C
ANISOU 2634 CA VAL A 337 4932 8289 3547 474 145 184 C
ATOM 2635 C VAL A 337 46.513 105.894 232.808 1.00 43.75 C
ANISOU 2635 C VAL A 337 4906 8190 3528 357 125 195 C
ATOM 2636 O VAL A 337 47.180 106.800 233.303 1.00 45.00 O
ANISOU 2636 O VAL A 337 4984 8406 3709 291 109 189 O
ATOM 2637 CB VAL A 337 47.849 103.829 233.307 1.00 44.38 C
ANISOU 2637 CB VAL A 337 4937 8357 3568 567 88 170 C
ATOM 2638 CG1 VAL A 337 46.855 103.581 234.399 1.00 42.69 C
ANISOU 2638 CG1 VAL A 337 4825 8048 3347 564 37 176 C
ATOM 2639 CG2 VAL A 337 48.325 102.495 232.769 1.00 44.38 C
ANISOU 2639 CG2 VAL A 337 4944 8377 3540 702 105 159 C
ATOM 2640 N THR A 338 45.183 105.896 232.783 1.00 43.00 N
ANISOU 2640 N THR A 338 4920 7987 3431 332 125 209 N
ATOM 2641 CA THR A 338 44.357 106.867 233.516 1.00 42.38 C
ANISOU 2641 CA THR A 338 4881 7844 3377 246 105 216 C
ATOM 2642 C THR A 338 43.941 106.270 234.863 1.00 41.96 C
ANISOU 2642 C THR A 338 4883 7751 3310 289 53 207 C
ATOM 2643 O THR A 338 43.569 105.091 234.907 1.00 42.08 O
ANISOU 2643 O THR A 338 4959 7730 3299 368 43 210 O
ATOM 2644 CB THR A 338 43.074 107.251 232.712 1.00 41.84 C
ANISOU 2644 CB THR A 338 4893 7687 3318 198 138 242 C
ATOM 2645 OG1 THR A 338 43.420 108.089 231.593 1.00 42.43 O
ANISOU 2645 OG1 THR A 338 4921 7795 3405 138 183 257 O
ATOM 2646 CG2 THR A 338 42.118 108.027 233.581 1.00 41.48 C
ANISOU 2646 CG2 THR A 338 4897 7567 3296 138 118 247 C
ATOM 2647 N ILE A 339 44.027 107.081 235.934 1.00 41.58 N
ANISOU 2647 N ILE A 339 4818 7707 3274 233 21 194 N
ATOM 2648 CA ILE A 339 43.529 106.770 237.289 1.00 41.17 C
ANISOU 2648 CA ILE A 339 4825 7615 3202 253 -24 187 C
ATOM 2649 C ILE A 339 42.299 107.654 237.590 1.00 41.66 C
ANISOU 2649 C ILE A 339 4956 7590 3283 179 -9 193 C
ATOM 2650 O ILE A 339 42.426 108.879 237.719 1.00 41.40 O
ANISOU 2650 O ILE A 339 4895 7559 3276 98 -3 182 O
ATOM 2651 CB ILE A 339 44.624 107.045 238.378 1.00 41.89 C
ANISOU 2651 CB ILE A 339 4846 7788 3283 248 -77 162 C
ATOM 2652 CG1 ILE A 339 45.940 106.359 238.034 1.00 41.30 C
ANISOU 2652 CG1 ILE A 339 4678 7816 3199 318 -89 157 C
ATOM 2653 CG2 ILE A 339 44.186 106.585 239.779 1.00 40.63 C
ANISOU 2653 CG2 ILE A 339 4755 7596 3088 279 -125 157 C
ATOM 2654 CD1 ILE A 339 47.125 107.044 238.613 1.00 40.14 C
ANISOU 2654 CD1 ILE A 339 4424 7768 3059 275 -128 136 C
ATOM 2655 N ASP A 340 41.115 107.044 237.699 1.00 42.53 N
ANISOU 2655 N ASP A 340 5154 7621 3383 207 -2 212 N
ATOM 2656 CA ASP A 340 39.870 107.816 237.807 1.00 43.91 C
ANISOU 2656 CA ASP A 340 5385 7718 3581 150 22 223 C
ATOM 2657 C ASP A 340 39.552 108.117 239.245 1.00 44.95 C
ANISOU 2657 C ASP A 340 5551 7829 3696 136 -3 205 C
ATOM 2658 O ASP A 340 39.040 109.204 239.532 1.00 45.35 O
ANISOU 2658 O ASP A 340 5618 7843 3771 76 13 196 O
ATOM 2659 CB ASP A 340 38.683 107.111 237.151 1.00 43.65 C
ANISOU 2659 CB ASP A 340 5419 7618 3550 174 45 254 C
ATOM 2660 CG ASP A 340 38.781 107.098 235.632 1.00 47.32 C
ANISOU 2660 CG ASP A 340 5861 8091 4027 168 75 270 C
ATOM 2661 OD1 ASP A 340 39.186 108.130 235.046 1.00 50.29 O
ANISOU 2661 OD1 ASP A 340 6189 8490 4428 114 95 270 O
ATOM 2662 OD2 ASP A 340 38.453 106.056 235.002 1.00 51.49 O
ANISOU 2662 OD2 ASP A 340 6427 8600 4537 214 78 283 O
ATOM 2663 N ASP A 341 39.824 107.163 240.144 1.00 45.74 N
ANISOU 2663 N ASP A 341 5673 7951 3754 194 -40 201 N
ATOM 2664 CA ASP A 341 39.889 107.501 241.544 1.00 47.15 C
ANISOU 2664 CA ASP A 341 5872 8138 3905 180 -70 178 C
ATOM 2665 C ASP A 341 40.397 106.409 242.467 1.00 47.21 C
ANISOU 2665 C ASP A 341 5897 8183 3860 250 -119 180 C
ATOM 2666 O ASP A 341 40.432 105.242 242.069 1.00 47.17 O
ANISOU 2666 O ASP A 341 5909 8173 3842 318 -123 203 O
ATOM 2667 CB ASP A 341 38.586 108.183 242.023 1.00 48.00 C
ANISOU 2667 CB ASP A 341 6045 8169 4022 137 -38 179 C
ATOM 2668 CG ASP A 341 37.702 107.278 242.854 1.00 51.41 C
ANISOU 2668 CG ASP A 341 6554 8564 4416 178 -40 199 C
ATOM 2669 OD1 ASP A 341 37.784 106.039 242.648 1.00 53.47 O
ANISOU 2669 OD1 ASP A 341 6832 8827 4656 238 -54 224 O
ATOM 2670 OD2 ASP A 341 36.932 107.826 243.711 1.00 53.68 O
ANISOU 2670 OD2 ASP A 341 6887 8816 4693 151 -23 189 O
ATOM 2671 N VAL A 342 40.824 106.799 243.674 1.00 47.08 N
ANISOU 2671 N VAL A 342 5879 8200 3809 234 -159 154 N
ATOM 2672 CA VAL A 342 41.282 105.854 244.681 1.00 47.57 C
ANISOU 2672 CA VAL A 342 5963 8298 3812 298 -212 160 C
ATOM 2673 C VAL A 342 40.255 105.659 245.744 1.00 46.81 C
ANISOU 2673 C VAL A 342 5964 8148 3675 297 -206 169 C
ATOM 2674 O VAL A 342 39.524 106.605 246.068 1.00 47.24 O
ANISOU 2674 O VAL A 342 6048 8165 3738 236 -174 151 O
ATOM 2675 CB VAL A 342 42.507 106.342 245.487 1.00 48.78 C
ANISOU 2675 CB VAL A 342 6054 8541 3939 282 -274 126 C
ATOM 2676 CG1 VAL A 342 43.772 106.053 244.730 1.00 50.47 C
ANISOU 2676 CG1 VAL A 342 6164 8836 4176 316 -296 126 C
ATOM 2677 CG2 VAL A 342 42.375 107.835 245.901 1.00 49.91 C
ANISOU 2677 CG2 VAL A 342 6193 8675 4094 181 -265 84 C
ATOM 2678 N ALA A 343 40.233 104.450 246.313 1.00 45.64 N
ANISOU 2678 N ALA A 343 5865 7997 3478 367 -234 199 N
ATOM 2679 CA ALA A 343 39.593 104.224 247.612 1.00 44.58 C
ANISOU 2679 CA ALA A 343 5815 7839 3283 369 -243 208 C
ATOM 2680 C ALA A 343 40.606 103.728 248.665 1.00 44.07 C
ANISOU 2680 C ALA A 343 5748 7845 3152 417 -320 206 C
ATOM 2681 O ALA A 343 41.470 102.909 248.363 1.00 43.52 O
ANISOU 2681 O ALA A 343 5642 7814 3081 485 -360 223 O
ATOM 2682 CB ALA A 343 38.392 103.276 247.478 1.00 44.41 C
ANISOU 2682 CB ALA A 343 5877 7739 3258 394 -203 255 C
ATOM 2683 N VAL A 344 40.508 104.248 249.886 1.00 42.99 N
ANISOU 2683 N VAL A 344 5651 7726 2958 384 -340 185 N
ATOM 2684 CA VAL A 344 41.504 103.915 250.907 1.00 43.06 C
ANISOU 2684 CA VAL A 344 5652 7810 2898 421 -423 181 C
ATOM 2685 C VAL A 344 40.973 103.192 252.142 1.00 42.54 C
ANISOU 2685 C VAL A 344 5692 7726 2745 454 -439 213 C
ATOM 2686 O VAL A 344 40.004 103.616 252.758 1.00 42.36 O
ANISOU 2686 O VAL A 344 5740 7662 2692 409 -395 206 O
ATOM 2687 CB VAL A 344 42.287 105.144 251.352 1.00 43.61 C
ANISOU 2687 CB VAL A 344 5663 7948 2959 354 -461 122 C
ATOM 2688 CG1 VAL A 344 43.136 104.821 252.614 1.00 44.19 C
ANISOU 2688 CG1 VAL A 344 5745 8100 2945 385 -553 119 C
ATOM 2689 CG2 VAL A 344 43.154 105.623 250.216 1.00 43.33 C
ANISOU 2689 CG2 VAL A 344 5511 7954 2999 335 -464 102 C
ATOM 2690 N PHE A 345 41.633 102.109 252.507 1.00 42.26 N
ANISOU 2690 N PHE A 345 5667 7724 2668 534 -500 251 N
ATOM 2691 CA PHE A 345 41.195 101.336 253.628 1.00 42.71 C
ANISOU 2691 CA PHE A 345 5829 7762 2639 568 -518 292 C
ATOM 2692 C PHE A 345 42.319 101.218 254.635 1.00 44.35 C
ANISOU 2692 C PHE A 345 6019 8061 2770 604 -617 288 C
ATOM 2693 O PHE A 345 43.422 101.704 254.391 1.00 45.23 O
ANISOU 2693 O PHE A 345 6028 8251 2906 601 -670 254 O
ATOM 2694 CB PHE A 345 40.662 100.002 253.145 1.00 41.88 C
ANISOU 2694 CB PHE A 345 5782 7583 2548 633 -493 357 C
ATOM 2695 CG PHE A 345 39.419 100.137 252.300 1.00 41.48 C
ANISOU 2695 CG PHE A 345 5756 7446 2560 585 -401 362 C
ATOM 2696 CD1 PHE A 345 39.514 100.368 250.914 1.00 40.85 C
ANISOU 2696 CD1 PHE A 345 5604 7350 2568 577 -370 344 C
ATOM 2697 CD2 PHE A 345 38.149 100.079 252.882 1.00 40.32 C
ANISOU 2697 CD2 PHE A 345 5699 7241 2380 546 -345 386 C
ATOM 2698 CE1 PHE A 345 38.380 100.514 250.141 1.00 37.18 C
ANISOU 2698 CE1 PHE A 345 5158 6812 2156 533 -295 351 C
ATOM 2699 CE2 PHE A 345 37.001 100.218 252.094 1.00 38.65 C
ANISOU 2699 CE2 PHE A 345 5496 6960 2230 502 -266 393 C
ATOM 2700 CZ PHE A 345 37.124 100.438 250.732 1.00 37.56 C
ANISOU 2700 CZ PHE A 345 5287 6806 2177 496 -247 376 C
ATOM 2701 N ALA A 346 42.033 100.622 255.786 1.00 45.45 N
ANISOU 2701 N ALA A 346 6257 8197 2817 631 -644 325 N
ATOM 2702 CA ALA A 346 43.051 100.399 256.816 1.00 47.06 C
ANISOU 2702 CA ALA A 346 6456 8488 2936 672 -747 332 C
ATOM 2703 C ALA A 346 44.308 99.687 256.286 1.00 48.09 C
ANISOU 2703 C ALA A 346 6497 8676 3101 764 -821 354 C
ATOM 2704 O ALA A 346 45.420 100.014 256.689 1.00 49.50 O
ANISOU 2704 O ALA A 346 6599 8956 3254 773 -906 331 O
ATOM 2705 CB ALA A 346 42.459 99.626 257.972 1.00 47.11 C
ANISOU 2705 CB ALA A 346 6595 8467 2837 700 -756 387 C
ATOM 2706 N LYS A 347 44.129 98.731 255.382 1.00 47.81 N
ANISOU 2706 N LYS A 347 6467 8577 3121 831 -788 396 N
ATOM 2707 CA LYS A 347 45.211 97.838 255.029 1.00 49.13 C
ANISOU 2707 CA LYS A 347 6576 8786 3307 942 -853 427 C
ATOM 2708 C LYS A 347 45.650 97.947 253.572 1.00 48.40 C
ANISOU 2708 C LYS A 347 6374 8697 3319 959 -817 401 C
ATOM 2709 O LYS A 347 46.513 97.171 253.133 1.00 49.19 O
ANISOU 2709 O LYS A 347 6421 8827 3443 1060 -855 423 O
ATOM 2710 CB LYS A 347 44.804 96.387 255.310 1.00 50.08 C
ANISOU 2710 CB LYS A 347 6812 8826 3388 1033 -858 505 C
ATOM 2711 CG LYS A 347 45.055 95.865 256.727 1.00 54.39 C
ANISOU 2711 CG LYS A 347 7438 9406 3823 1078 -938 552 C
ATOM 2712 CD LYS A 347 44.358 94.484 256.897 1.00 58.75 C
ANISOU 2712 CD LYS A 347 8129 9847 4345 1144 -919 634 C
ATOM 2713 CE LYS A 347 44.030 94.161 258.382 1.00 62.21 C
ANISOU 2713 CE LYS A 347 8690 10289 4659 1142 -959 685 C
ATOM 2714 NZ LYS A 347 42.886 93.175 258.505 1.00 62.97 N
ANISOU 2714 NZ LYS A 347 8934 10259 4734 1145 -899 755 N
ATOM 2715 N PHE A 348 45.070 98.872 252.807 1.00 46.48 N
ANISOU 2715 N PHE A 348 6100 8424 3137 867 -741 357 N
ATOM 2716 CA PHE A 348 45.398 98.939 251.397 1.00 44.86 C
ANISOU 2716 CA PHE A 348 5806 8218 3022 879 -700 339 C
ATOM 2717 C PHE A 348 44.576 100.008 250.726 1.00 43.73 C
ANISOU 2717 C PHE A 348 5652 8031 2931 770 -620 299 C
ATOM 2718 O PHE A 348 43.745 100.621 251.398 1.00 43.77 O
ANISOU 2718 O PHE A 348 5721 8004 2904 696 -595 287 O
ATOM 2719 CB PHE A 348 45.080 97.595 250.777 1.00 44.76 C
ANISOU 2719 CB PHE A 348 5858 8123 3028 973 -676 387 C
ATOM 2720 CG PHE A 348 43.617 97.328 250.648 1.00 43.81 C
ANISOU 2720 CG PHE A 348 5855 7883 2908 927 -604 410 C
ATOM 2721 CD1 PHE A 348 42.898 96.820 251.713 1.00 44.35 C
ANISOU 2721 CD1 PHE A 348 6042 7902 2907 927 -613 452 C
ATOM 2722 CD2 PHE A 348 42.949 97.578 249.441 1.00 42.05 C
ANISOU 2722 CD2 PHE A 348 5621 7602 2755 883 -527 393 C
ATOM 2723 CE1 PHE A 348 41.526 96.578 251.578 1.00 44.35 C
ANISOU 2723 CE1 PHE A 348 6139 7800 2913 878 -543 475 C
ATOM 2724 CE2 PHE A 348 41.584 97.349 249.310 1.00 40.37 C
ANISOU 2724 CE2 PHE A 348 5505 7288 2547 836 -466 415 C
ATOM 2725 CZ PHE A 348 40.872 96.848 250.364 1.00 41.11 C
ANISOU 2725 CZ PHE A 348 5707 7337 2578 832 -472 456 C
ATOM 2726 N ALA A 349 44.784 100.227 249.415 1.00 42.65 N
ANISOU 2726 N ALA A 349 5440 7893 2871 764 -576 281 N
ATOM 2727 CA ALA A 349 43.888 101.082 248.598 1.00 41.40 C
ANISOU 2727 CA ALA A 349 5284 7677 2767 674 -495 257 C
ATOM 2728 C ALA A 349 43.544 100.431 247.295 1.00 40.97 C
ANISOU 2728 C ALA A 349 5236 7564 2766 711 -442 275 C
ATOM 2729 O ALA A 349 44.417 99.796 246.737 1.00 42.53 O
ANISOU 2729 O ALA A 349 5380 7801 2980 789 -462 281 O
ATOM 2730 CB ALA A 349 44.522 102.399 248.301 1.00 40.97 C
ANISOU 2730 CB ALA A 349 5125 7692 2749 595 -496 207 C
ATOM 2731 N VAL A 350 42.303 100.603 246.808 1.00 39.99 N
ANISOU 2731 N VAL A 350 5174 7353 2668 658 -375 281 N
ATOM 2732 CA VAL A 350 41.910 100.299 245.413 1.00 39.34 C
ANISOU 2732 CA VAL A 350 5089 7220 2640 665 -321 287 C
ATOM 2733 C VAL A 350 42.028 101.506 244.490 1.00 39.21 C
ANISOU 2733 C VAL A 350 4989 7231 2678 590 -282 253 C
ATOM 2734 O VAL A 350 41.455 102.552 244.759 1.00 39.43 O
ANISOU 2734 O VAL A 350 5021 7245 2716 507 -259 236 O
ATOM 2735 CB VAL A 350 40.417 100.000 245.240 1.00 38.48 C
ANISOU 2735 CB VAL A 350 5077 7006 2536 629 -270 314 C
ATOM 2736 CG1 VAL A 350 40.214 98.932 244.202 1.00 38.38 C
ANISOU 2736 CG1 VAL A 350 5099 6937 2545 682 -251 335 C
ATOM 2737 CG2 VAL A 350 39.747 99.664 246.518 1.00 39.14 C
ANISOU 2737 CG2 VAL A 350 5250 7057 2565 624 -284 340 C
ATOM 2738 N LEU A 351 42.702 101.346 243.368 1.00 39.64 N
ANISOU 2738 N LEU A 351 4977 7317 2768 622 -268 245 N
ATOM 2739 CA LEU A 351 42.669 102.359 242.324 1.00 39.79 C
ANISOU 2739 CA LEU A 351 4935 7348 2837 551 -222 225 C
ATOM 2740 C LEU A 351 41.792 101.861 241.217 1.00 39.65 C
ANISOU 2740 C LEU A 351 4970 7253 2841 557 -172 243 C
ATOM 2741 O LEU A 351 41.965 100.741 240.743 1.00 40.29 O
ANISOU 2741 O LEU A 351 5078 7316 2913 635 -174 255 O
ATOM 2742 CB LEU A 351 44.049 102.604 241.723 1.00 40.09 C
ANISOU 2742 CB LEU A 351 4853 7484 2894 572 -232 204 C
ATOM 2743 CG LEU A 351 45.033 103.437 242.531 1.00 39.49 C
ANISOU 2743 CG LEU A 351 4692 7501 2811 535 -280 179 C
ATOM 2744 CD1 LEU A 351 45.448 102.696 243.756 1.00 37.66 C
ANISOU 2744 CD1 LEU A 351 4483 7299 2528 603 -348 189 C
ATOM 2745 CD2 LEU A 351 46.230 103.702 241.660 1.00 40.01 C
ANISOU 2745 CD2 LEU A 351 4632 7660 2908 542 -272 165 C
ATOM 2746 N SER A 352 40.863 102.704 240.806 1.00 38.93 N
ANISOU 2746 N SER A 352 4895 7117 2779 476 -130 243 N
ATOM 2747 CA SER A 352 40.016 102.413 239.690 1.00 38.89 C
ANISOU 2747 CA SER A 352 4930 7051 2797 467 -87 259 C
ATOM 2748 C SER A 352 40.541 103.231 238.500 1.00 38.90 C
ANISOU 2748 C SER A 352 4852 7095 2833 430 -56 244 C
ATOM 2749 O SER A 352 40.844 104.425 238.634 1.00 39.61 O
ANISOU 2749 O SER A 352 4885 7220 2944 366 -51 229 O
ATOM 2750 CB SER A 352 38.591 102.870 240.041 1.00 38.84 C
ANISOU 2750 CB SER A 352 4985 6973 2801 403 -63 275 C
ATOM 2751 OG SER A 352 37.720 101.813 240.438 1.00 40.92 O
ANISOU 2751 OG SER A 352 5336 7170 3041 431 -68 303 O
ATOM 2752 N GLY A 353 40.637 102.631 237.324 1.00 38.34 N
ANISOU 2752 N GLY A 353 4785 7019 2766 465 -33 249 N
ATOM 2753 CA GLY A 353 40.984 103.433 236.181 1.00 37.39 C
ANISOU 2753 CA GLY A 353 4601 6934 2670 422 3 242 C
ATOM 2754 C GLY A 353 40.889 102.720 234.865 1.00 37.61 C
ANISOU 2754 C GLY A 353 4654 6946 2691 458 32 246 C
ATOM 2755 O GLY A 353 39.981 101.915 234.646 1.00 36.16 O
ANISOU 2755 O GLY A 353 4554 6689 2494 476 32 260 O
ATOM 2756 N ARG A 354 41.870 103.032 234.001 1.00 38.78 N
ANISOU 2756 N ARG A 354 4725 7168 2843 464 58 233 N
ATOM 2757 CA ARG A 354 41.878 102.662 232.585 1.00 39.04 C
ANISOU 2757 CA ARG A 354 4770 7200 2863 483 97 233 C
ATOM 2758 C ARG A 354 43.236 102.354 231.988 1.00 40.58 C
ANISOU 2758 C ARG A 354 4888 7487 3045 546 118 212 C
ATOM 2759 O ARG A 354 44.219 103.007 232.316 1.00 41.33 O
ANISOU 2759 O ARG A 354 4883 7666 3154 530 117 204 O
ATOM 2760 CB ARG A 354 41.269 103.784 231.778 1.00 38.20 C
ANISOU 2760 CB ARG A 354 4657 7079 2778 390 130 251 C
ATOM 2761 CG ARG A 354 39.807 103.789 231.942 1.00 36.73 C
ANISOU 2761 CG ARG A 354 4554 6800 2600 350 119 273 C
ATOM 2762 CD ARG A 354 39.038 104.270 230.765 1.00 35.28 C
ANISOU 2762 CD ARG A 354 4395 6587 2422 297 147 294 C
ATOM 2763 NE ARG A 354 37.717 103.796 231.074 1.00 36.09 N
ANISOU 2763 NE ARG A 354 4578 6608 2528 288 126 311 N
ATOM 2764 CZ ARG A 354 37.089 102.853 230.392 1.00 37.41 C
ANISOU 2764 CZ ARG A 354 4813 6730 2670 309 122 316 C
ATOM 2765 NH1 ARG A 354 37.637 102.342 229.294 1.00 37.11 N
ANISOU 2765 NH1 ARG A 354 4782 6720 2599 344 140 300 N
ATOM 2766 NH2 ARG A 354 35.886 102.456 230.791 1.00 36.69 N
ANISOU 2766 NH2 ARG A 354 4785 6570 2587 290 101 334 N
ATOM 2767 N ARG A 355 43.260 101.358 231.099 1.00 41.88 N
ANISOU 2767 N ARG A 355 5098 7635 3179 614 140 202 N
ATOM 2768 CA ARG A 355 44.368 101.098 230.149 1.00 43.41 C
ANISOU 2768 CA ARG A 355 5229 7912 3355 672 182 182 C
ATOM 2769 C ARG A 355 43.784 100.383 228.907 1.00 43.58 C
ANISOU 2769 C ARG A 355 5340 7879 3339 697 214 174 C
ATOM 2770 O ARG A 355 42.835 99.611 229.042 1.00 43.62 O
ANISOU 2770 O ARG A 355 5453 7789 3332 711 188 176 O
ATOM 2771 CB ARG A 355 45.456 100.252 230.812 1.00 44.23 C
ANISOU 2771 CB ARG A 355 5286 8069 3450 784 159 162 C
ATOM 2772 CG ARG A 355 46.758 100.118 230.000 1.00 45.69 C
ANISOU 2772 CG ARG A 355 5373 8363 3623 849 206 141 C
ATOM 2773 CD ARG A 355 47.791 99.189 230.658 1.00 47.70 C
ANISOU 2773 CD ARG A 355 5582 8668 3873 978 179 125 C
ATOM 2774 NE ARG A 355 47.209 98.048 231.389 1.00 47.13 N
ANISOU 2774 NE ARG A 355 5625 8496 3787 1052 130 127 N
ATOM 2775 CZ ARG A 355 46.621 97.007 230.797 1.00 46.63 C
ANISOU 2775 CZ ARG A 355 5682 8341 3695 1109 143 115 C
ATOM 2776 NH1 ARG A 355 46.508 96.961 229.462 1.00 45.47 N
ANISOU 2776 NH1 ARG A 355 5558 8193 3524 1104 201 97 N
ATOM 2777 NH2 ARG A 355 46.133 96.023 231.538 1.00 45.23 N
ANISOU 2777 NH2 ARG A 355 5607 8072 3508 1166 97 123 N
ATOM 2778 N ASP A 356 44.302 100.670 227.712 1.00 44.03 N
ANISOU 2778 N ASP A 356 5356 7997 3376 692 269 166 N
ATOM 2779 CA ASP A 356 43.760 100.088 226.445 1.00 45.03 C
ANISOU 2779 CA ASP A 356 5572 8080 3458 706 300 155 C
ATOM 2780 C ASP A 356 42.248 100.253 226.125 1.00 43.39 C
ANISOU 2780 C ASP A 356 5465 7774 3247 625 279 178 C
ATOM 2781 O ASP A 356 41.627 99.388 225.478 1.00 43.58 O
ANISOU 2781 O ASP A 356 5590 7734 3233 650 276 164 O
ATOM 2782 CB ASP A 356 44.181 98.625 226.301 1.00 46.73 C
ANISOU 2782 CB ASP A 356 5843 8275 3637 835 302 117 C
ATOM 2783 CG ASP A 356 45.506 98.484 225.574 1.00 52.10 C
ANISOU 2783 CG ASP A 356 6441 9063 4294 910 362 89 C
ATOM 2784 OD1 ASP A 356 45.438 98.425 224.303 1.00 57.60 O
ANISOU 2784 OD1 ASP A 356 7171 9769 4944 906 412 76 O
ATOM 2785 OD2 ASP A 356 46.590 98.469 226.258 1.00 54.19 O
ANISOU 2785 OD2 ASP A 356 6603 9406 4581 970 358 83 O
ATOM 2786 N GLY A 357 41.678 101.364 226.585 1.00 41.85 N
ANISOU 2786 N GLY A 357 5242 7568 3092 530 263 212 N
ATOM 2787 CA GLY A 357 40.278 101.667 226.431 1.00 39.21 C
ANISOU 2787 CA GLY A 357 4978 7153 2766 456 240 240 C
ATOM 2788 C GLY A 357 39.334 100.747 227.153 1.00 37.62 C
ANISOU 2788 C GLY A 357 4866 6860 2569 476 194 240 C
ATOM 2789 O GLY A 357 38.198 100.633 226.757 1.00 37.29 O
ANISOU 2789 O GLY A 357 4892 6754 2521 432 178 257 O
ATOM 2790 N LEU A 358 39.789 100.081 228.205 1.00 37.33 N
ANISOU 2790 N LEU A 358 4827 6817 2539 540 170 226 N
ATOM 2791 CA LEU A 358 38.883 99.293 229.050 1.00 36.17 C
ANISOU 2791 CA LEU A 358 4763 6581 2398 548 127 235 C
ATOM 2792 C LEU A 358 39.119 99.644 230.478 1.00 35.43 C
ANISOU 2792 C LEU A 358 4626 6502 2334 549 102 245 C
ATOM 2793 O LEU A 358 40.239 99.990 230.830 1.00 35.44 O
ANISOU 2793 O LEU A 358 4545 6579 2341 580 109 232 O
ATOM 2794 CB LEU A 358 39.146 97.810 228.884 1.00 36.84 C
ANISOU 2794 CB LEU A 358 4926 6625 2447 641 118 208 C
ATOM 2795 CG LEU A 358 39.079 97.175 227.500 1.00 38.36 C
ANISOU 2795 CG LEU A 358 5182 6799 2596 663 141 183 C
ATOM 2796 CD1 LEU A 358 39.653 95.776 227.630 1.00 38.49 C
ANISOU 2796 CD1 LEU A 358 5262 6779 2583 776 134 149 C
ATOM 2797 CD2 LEU A 358 37.641 97.160 226.912 1.00 38.44 C
ANISOU 2797 CD2 LEU A 358 5271 6735 2599 579 123 202 C
ATOM 2798 N THR A 359 38.077 99.525 231.307 1.00 35.35 N
ANISOU 2798 N THR A 359 4668 6424 2338 513 74 268 N
ATOM 2799 CA THR A 359 38.213 99.631 232.801 1.00 34.89 C
ANISOU 2799 CA THR A 359 4594 6370 2294 522 46 276 C
ATOM 2800 C THR A 359 39.219 98.647 233.389 1.00 35.56 C
ANISOU 2800 C THR A 359 4683 6473 2355 623 25 259 C
ATOM 2801 O THR A 359 39.162 97.443 233.113 1.00 34.98 O
ANISOU 2801 O THR A 359 4684 6349 2257 684 16 252 O
ATOM 2802 CB THR A 359 36.909 99.323 233.587 1.00 34.05 C
ANISOU 2802 CB THR A 359 4560 6182 2194 484 25 304 C
ATOM 2803 OG1 THR A 359 36.590 97.932 233.458 1.00 35.15 O
ANISOU 2803 OG1 THR A 359 4793 6254 2308 530 8 305 O
ATOM 2804 CG2 THR A 359 35.756 100.143 233.124 1.00 33.11 C
ANISOU 2804 CG2 THR A 359 4442 6037 2102 396 41 326 C
ATOM 2805 N ARG A 360 40.109 99.186 234.224 1.00 36.67 N
ANISOU 2805 N ARG A 360 4745 6683 2504 637 11 253 N
ATOM 2806 CA ARG A 360 41.059 98.413 235.019 1.00 38.12 C
ANISOU 2806 CA ARG A 360 4919 6896 2669 731 -20 245 C
ATOM 2807 C ARG A 360 41.015 98.782 236.496 1.00 38.51 C
ANISOU 2807 C ARG A 360 4958 6956 2719 711 -58 258 C
ATOM 2808 O ARG A 360 40.501 99.825 236.874 1.00 38.05 O
ANISOU 2808 O ARG A 360 4878 6901 2678 627 -52 264 O
ATOM 2809 CB ARG A 360 42.461 98.609 234.482 1.00 38.71 C
ANISOU 2809 CB ARG A 360 4893 7072 2744 783 -4 219 C
ATOM 2810 CG ARG A 360 42.908 97.478 233.587 1.00 40.58 C
ANISOU 2810 CG ARG A 360 5164 7296 2957 880 14 201 C
ATOM 2811 CD ARG A 360 42.753 97.737 232.099 1.00 39.68 C
ANISOU 2811 CD ARG A 360 5049 7189 2839 849 66 186 C
ATOM 2812 NE ARG A 360 42.751 96.429 231.446 1.00 42.17 N
ANISOU 2812 NE ARG A 360 5451 7448 3123 938 74 168 N
ATOM 2813 CZ ARG A 360 42.895 96.216 230.141 1.00 43.16 C
ANISOU 2813 CZ ARG A 360 5591 7582 3227 956 118 144 C
ATOM 2814 NH1 ARG A 360 43.064 97.210 229.303 1.00 41.78 N
ANISOU 2814 NH1 ARG A 360 5347 7473 3056 892 159 142 N
ATOM 2815 NH2 ARG A 360 42.878 94.984 229.665 1.00 47.37 N
ANISOU 2815 NH2 ARG A 360 6217 8053 3728 1039 121 121 N
ATOM 2816 N VAL A 361 41.558 97.904 237.332 1.00 40.15 N
ANISOU 2816 N VAL A 361 5188 7166 2901 794 -97 263 N
ATOM 2817 CA VAL A 361 41.551 98.088 238.785 1.00 40.39 C
ANISOU 2817 CA VAL A 361 5223 7207 2917 785 -139 278 C
ATOM 2818 C VAL A 361 42.801 97.495 239.422 1.00 41.48 C
ANISOU 2818 C VAL A 361 5321 7408 3033 886 -184 274 C
ATOM 2819 O VAL A 361 43.096 96.318 239.217 1.00 41.73 O
ANISOU 2819 O VAL A 361 5400 7406 3048 982 -194 280 O
ATOM 2820 CB VAL A 361 40.242 97.524 239.445 1.00 40.00 C
ANISOU 2820 CB VAL A 361 5291 7056 2851 757 -145 310 C
ATOM 2821 CG1 VAL A 361 39.706 96.351 238.685 1.00 40.64 C
ANISOU 2821 CG1 VAL A 361 5464 7051 2927 795 -134 320 C
ATOM 2822 CG2 VAL A 361 40.460 97.143 240.927 1.00 41.87 C
ANISOU 2822 CG2 VAL A 361 5558 7298 3050 793 -194 330 C
ATOM 2823 N TRP A 362 43.529 98.335 240.168 1.00 42.48 N
ANISOU 2823 N TRP A 362 5360 7622 3160 862 -212 264 N
ATOM 2824 CA TRP A 362 44.695 97.913 240.964 1.00 44.26 C
ANISOU 2824 CA TRP A 362 5534 7921 3362 948 -268 265 C
ATOM 2825 C TRP A 362 44.524 98.088 242.478 1.00 44.80 C
ANISOU 2825 C TRP A 362 5634 7994 3394 926 -321 281 C
ATOM 2826 O TRP A 362 43.705 98.860 242.973 1.00 44.32 O
ANISOU 2826 O TRP A 362 5604 7905 3331 833 -311 281 O
ATOM 2827 CB TRP A 362 45.955 98.673 240.565 1.00 44.78 C
ANISOU 2827 CB TRP A 362 5452 8111 3451 945 -268 237 C
ATOM 2828 CG TRP A 362 46.147 98.738 239.122 1.00 46.06 C
ANISOU 2828 CG TRP A 362 5574 8286 3643 949 -208 220 C
ATOM 2829 CD1 TRP A 362 46.893 97.892 238.365 1.00 48.74 C
ANISOU 2829 CD1 TRP A 362 5886 8651 3981 1055 -193 212 C
ATOM 2830 CD2 TRP A 362 45.598 99.707 238.225 1.00 44.82 C
ANISOU 2830 CD2 TRP A 362 5401 8115 3513 847 -153 210 C
ATOM 2831 NE1 TRP A 362 46.833 98.261 237.041 1.00 48.59 N
ANISOU 2831 NE1 TRP A 362 5840 8641 3983 1021 -128 195 N
ATOM 2832 CE2 TRP A 362 46.040 99.373 236.930 1.00 45.94 C
ANISOU 2832 CE2 TRP A 362 5511 8280 3665 892 -106 197 C
ATOM 2833 CE3 TRP A 362 44.774 100.822 238.389 1.00 44.40 C
ANISOU 2833 CE3 TRP A 362 5362 8031 3477 727 -138 211 C
ATOM 2834 CZ2 TRP A 362 45.681 100.109 235.806 1.00 44.47 C
ANISOU 2834 CZ2 TRP A 362 5308 8089 3498 816 -49 190 C
ATOM 2835 CZ3 TRP A 362 44.417 101.560 237.272 1.00 42.42 C
ANISOU 2835 CZ3 TRP A 362 5093 7772 3254 657 -83 206 C
ATOM 2836 CH2 TRP A 362 44.860 101.191 235.999 1.00 44.22 C
ANISOU 2836 CH2 TRP A 362 5292 8025 3485 699 -42 198 C
ATOM 2837 N THR A 363 45.372 97.386 243.203 1.00 45.97 N
ANISOU 2837 N THR A 363 5769 8185 3511 1019 -379 294 N
ATOM 2838 CA THR A 363 45.320 97.346 244.623 1.00 46.11 C
ANISOU 2838 CA THR A 363 5826 8211 3482 1018 -437 314 C
ATOM 2839 C THR A 363 46.733 97.674 245.118 1.00 47.53 C
ANISOU 2839 C THR A 363 5884 8522 3654 1057 -498 300 C
ATOM 2840 O THR A 363 47.715 97.307 244.456 1.00 48.05 O
ANISOU 2840 O THR A 363 5865 8648 3742 1137 -502 292 O
ATOM 2841 CB THR A 363 44.840 95.957 245.041 1.00 46.28 C
ANISOU 2841 CB THR A 363 5977 8141 3468 1101 -456 358 C
ATOM 2842 OG1 THR A 363 44.397 96.005 246.389 1.00 48.41 O
ANISOU 2842 OG1 THR A 363 6312 8396 3684 1071 -493 383 O
ATOM 2843 CG2 THR A 363 45.921 94.887 244.886 1.00 46.44 C
ANISOU 2843 CG2 THR A 363 5972 8190 3482 1245 -494 370 C
ATOM 2844 N VAL A 364 46.841 98.400 246.234 1.00 47.90 N
ANISOU 2844 N VAL A 364 5914 8618 3667 998 -545 293 N
ATOM 2845 CA VAL A 364 48.147 98.770 246.798 1.00 49.63 C
ANISOU 2845 CA VAL A 364 6016 8968 3874 1019 -615 279 C
ATOM 2846 C VAL A 364 48.186 98.569 248.312 1.00 50.80 C
ANISOU 2846 C VAL A 364 6218 9133 3949 1033 -693 301 C
ATOM 2847 O VAL A 364 47.336 99.072 249.045 1.00 50.86 O
ANISOU 2847 O VAL A 364 6305 9096 3922 952 -687 297 O
ATOM 2848 CB VAL A 364 48.629 100.218 246.346 1.00 49.61 C
ANISOU 2848 CB VAL A 364 5888 9047 3914 907 -596 232 C
ATOM 2849 CG1 VAL A 364 47.958 101.337 247.128 1.00 48.77 C
ANISOU 2849 CG1 VAL A 364 5824 8920 3787 781 -598 209 C
ATOM 2850 CG2 VAL A 364 50.144 100.362 246.449 1.00 50.88 C
ANISOU 2850 CG2 VAL A 364 5897 9352 4083 946 -656 221 C
ATOM 2851 N ARG A 365 49.181 97.821 248.764 1.00 52.62 N
ANISOU 2851 N ARG A 365 6407 9432 4155 1142 -766 324 N
ATOM 2852 CA ARG A 365 49.294 97.364 250.160 1.00 53.87 C
ANISOU 2852 CA ARG A 365 6628 9606 4235 1183 -849 357 C
ATOM 2853 C ARG A 365 50.252 98.217 251.032 1.00 54.74 C
ANISOU 2853 C ARG A 365 6633 9851 4313 1138 -933 332 C
ATOM 2854 O ARG A 365 51.022 99.007 250.526 1.00 54.57 O
ANISOU 2854 O ARG A 365 6476 9921 4337 1093 -935 294 O
ATOM 2855 CB ARG A 365 49.801 95.922 250.149 1.00 54.75 C
ANISOU 2855 CB ARG A 365 6766 9702 4333 1345 -887 407 C
ATOM 2856 CG ARG A 365 48.757 94.859 250.293 1.00 56.11 C
ANISOU 2856 CG ARG A 365 7109 9732 4478 1389 -858 454 C
ATOM 2857 CD ARG A 365 49.289 93.507 249.806 1.00 59.75 C
ANISOU 2857 CD ARG A 365 7587 10160 4955 1548 -872 489 C
ATOM 2858 NE ARG A 365 48.872 93.335 248.421 1.00 63.46 N
ANISOU 2858 NE ARG A 365 8063 10558 5489 1545 -783 465 N
ATOM 2859 CZ ARG A 365 49.683 93.262 247.362 1.00 66.48 C
ANISOU 2859 CZ ARG A 365 8339 10993 5926 1608 -758 438 C
ATOM 2860 NH1 ARG A 365 51.019 93.278 247.496 1.00 66.93 N
ANISOU 2860 NH1 ARG A 365 8260 11179 5990 1690 -814 433 N
ATOM 2861 NH2 ARG A 365 49.141 93.142 246.151 1.00 66.47 N
ANISOU 2861 NH2 ARG A 365 8367 10919 5970 1590 -675 416 N
ATOM 2862 N LEU A 366 50.226 98.032 252.346 1.00 56.20 N
ANISOU 2862 N LEU A 366 6885 10052 4416 1147 -1007 355 N
ATOM 2863 CA LEU A 366 51.272 98.616 253.170 1.00 58.32 C
ANISOU 2863 CA LEU A 366 7054 10458 4648 1126 -1105 336 C
ATOM 2864 C LEU A 366 52.504 97.730 253.149 1.00 60.49 C
ANISOU 2864 C LEU A 366 7233 10822 4927 1269 -1180 371 C
ATOM 2865 O LEU A 366 52.403 96.530 252.876 1.00 60.89 O
ANISOU 2865 O LEU A 366 7344 10810 4983 1394 -1169 419 O
ATOM 2866 CB LEU A 366 50.827 98.800 254.610 1.00 58.37 C
ANISOU 2866 CB LEU A 366 7167 10458 4554 1080 -1160 344 C
ATOM 2867 CG LEU A 366 49.588 99.614 254.944 1.00 57.55 C
ANISOU 2867 CG LEU A 366 7171 10270 4423 954 -1095 313 C
ATOM 2868 CD1 LEU A 366 49.605 99.905 256.441 1.00 59.15 C
ANISOU 2868 CD1 LEU A 366 7439 10518 4517 917 -1173 311 C
ATOM 2869 CD2 LEU A 366 49.503 100.899 254.131 1.00 56.78 C
ANISOU 2869 CD2 LEU A 366 6995 10180 4400 835 -1033 248 C
ATOM 2870 N GLY A 367 53.663 98.332 253.431 1.00 62.36 N
ANISOU 2870 N GLY A 367 7321 11207 5166 1248 -1258 347 N
ATOM 2871 CA GLY A 367 54.904 97.599 253.572 1.00 64.33 C
ANISOU 2871 CA GLY A 367 7461 11566 5416 1382 -1343 380 C
ATOM 2872 C GLY A 367 55.015 97.129 255.006 1.00 66.40 C
ANISOU 2872 C GLY A 367 7800 11853 5575 1429 -1453 423 C
ATOM 2873 O GLY A 367 54.215 97.548 255.862 1.00 65.55 O
ANISOU 2873 O GLY A 367 7814 11696 5398 1339 -1459 415 O
ATOM 2874 N PRO A 368 55.986 96.224 255.270 1.00 68.57 N
ANISOU 2874 N PRO A 368 8010 12205 5838 1579 -1539 471 N
ATOM 2875 CA PRO A 368 56.519 95.968 256.598 1.00 70.46 C
ANISOU 2875 CA PRO A 368 8260 12526 5984 1622 -1672 508 C
ATOM 2876 C PRO A 368 56.668 97.238 257.442 1.00 71.38 C
ANISOU 2876 C PRO A 368 8340 12735 6048 1464 -1734 456 C
ATOM 2877 O PRO A 368 56.505 97.173 258.655 1.00 72.57 O
ANISOU 2877 O PRO A 368 8583 12896 6094 1452 -1813 478 O
ATOM 2878 CB PRO A 368 57.899 95.369 256.297 1.00 71.69 C
ANISOU 2878 CB PRO A 368 8247 12809 6183 1769 -1742 536 C
ATOM 2879 CG PRO A 368 57.809 94.852 254.862 1.00 70.60 C
ANISOU 2879 CG PRO A 368 8079 12601 6145 1847 -1629 532 C
ATOM 2880 CD PRO A 368 56.454 95.193 254.326 1.00 68.74 C
ANISOU 2880 CD PRO A 368 7982 12212 5926 1737 -1506 502 C
ATOM 2881 N ASP A 369 56.968 98.378 256.817 1.00 71.68 N
ANISOU 2881 N ASP A 369 8253 12832 6150 1341 -1698 388 N
ATOM 2882 CA ASP A 369 57.113 99.652 257.550 1.00 72.71 C
ANISOU 2882 CA ASP A 369 8353 13037 6236 1179 -1753 330 C
ATOM 2883 C ASP A 369 55.801 100.223 258.137 1.00 71.64 C
ANISOU 2883 C ASP A 369 8402 12781 6036 1061 -1700 301 C
ATOM 2884 O ASP A 369 55.847 101.092 259.026 1.00 72.47 O
ANISOU 2884 O ASP A 369 8525 12935 6074 949 -1759 258 O
ATOM 2885 CB ASP A 369 57.911 100.720 256.740 1.00 73.17 C
ANISOU 2885 CB ASP A 369 8221 13198 6384 1076 -1738 270 C
ATOM 2886 CG ASP A 369 57.268 101.097 255.367 1.00 74.36 C
ANISOU 2886 CG ASP A 369 8373 13249 6632 1024 -1588 240 C
ATOM 2887 OD1 ASP A 369 56.083 100.761 255.073 1.00 75.77 O
ANISOU 2887 OD1 ASP A 369 8703 13276 6810 1035 -1494 252 O
ATOM 2888 OD2 ASP A 369 57.976 101.759 254.562 1.00 76.20 O
ANISOU 2888 OD2 ASP A 369 8446 13563 6943 966 -1566 207 O
ATOM 2889 N ASN A 370 54.655 99.701 257.659 1.00 70.07 N
ANISOU 2889 N ASN A 370 8339 12430 5855 1092 -1590 324 N
ATOM 2890 CA ASN A 370 53.292 100.207 257.961 1.00 68.07 C
ANISOU 2890 CA ASN A 370 8247 12054 5564 989 -1510 298 C
ATOM 2891 C ASN A 370 52.937 101.444 257.128 1.00 66.57 C
ANISOU 2891 C ASN A 370 8009 11833 5452 852 -1422 227 C
ATOM 2892 O ASN A 370 51.966 102.150 257.420 1.00 65.75 O
ANISOU 2892 O ASN A 370 8009 11651 5322 751 -1366 191 O
ATOM 2893 CB ASN A 370 53.080 100.473 259.466 1.00 68.76 C
ANISOU 2893 CB ASN A 370 8439 12166 5522 940 -1588 294 C
ATOM 2894 CG ASN A 370 53.084 99.196 260.306 1.00 69.94 C
ANISOU 2894 CG ASN A 370 8684 12306 5583 1071 -1655 377 C
ATOM 2895 OD1 ASN A 370 52.642 98.124 259.859 1.00 70.16 O
ANISOU 2895 OD1 ASN A 370 8779 12244 5637 1175 -1604 436 O
ATOM 2896 ND2 ASN A 370 53.575 99.310 261.540 1.00 70.93 N
ANISOU 2896 ND2 ASN A 370 8827 12523 5600 1062 -1772 381 N
ATOM 2897 N LEU A 371 53.737 101.697 256.095 1.00 65.94 N
ANISOU 2897 N LEU A 371 7771 11817 5466 853 -1407 209 N
ATOM 2898 CA LEU A 371 53.524 102.813 255.188 1.00 64.88 C
ANISOU 2898 CA LEU A 371 7581 11659 5411 731 -1325 152 C
ATOM 2899 C LEU A 371 53.326 102.268 253.776 1.00 63.50 C
ANISOU 2899 C LEU A 371 7373 11424 5328 798 -1227 175 C
ATOM 2900 O LEU A 371 53.920 101.242 253.411 1.00 64.05 O
ANISOU 2900 O LEU A 371 7388 11530 5418 931 -1246 219 O
ATOM 2901 CB LEU A 371 54.716 103.776 255.233 1.00 66.33 C
ANISOU 2901 CB LEU A 371 7600 11983 5618 644 -1396 106 C
ATOM 2902 CG LEU A 371 54.730 104.987 256.187 1.00 68.11 C
ANISOU 2902 CG LEU A 371 7852 12241 5787 496 -1453 44 C
ATOM 2903 CD1 LEU A 371 54.744 104.617 257.688 1.00 68.96 C
ANISOU 2903 CD1 LEU A 371 8051 12382 5768 525 -1558 58 C
ATOM 2904 CD2 LEU A 371 55.916 105.910 255.839 1.00 69.82 C
ANISOU 2904 CD2 LEU A 371 7885 12584 6058 401 -1501 2 C
ATOM 2905 N PHE A 372 52.503 102.961 252.988 1.00 61.46 N
ANISOU 2905 N PHE A 372 7150 11077 5123 710 -1124 145 N
ATOM 2906 CA PHE A 372 52.076 102.468 251.676 1.00 59.58 C
ANISOU 2906 CA PHE A 372 6914 10764 4959 761 -1025 165 C
ATOM 2907 C PHE A 372 53.256 102.197 250.745 1.00 60.19 C
ANISOU 2907 C PHE A 372 6826 10942 5101 825 -1030 171 C
ATOM 2908 O PHE A 372 54.102 103.053 250.541 1.00 60.55 O
ANISOU 2908 O PHE A 372 6737 11088 5180 751 -1053 138 O
ATOM 2909 CB PHE A 372 51.059 103.412 251.011 1.00 57.94 C
ANISOU 2909 CB PHE A 372 6760 10459 4795 645 -924 130 C
ATOM 2910 CG PHE A 372 49.601 103.071 251.294 1.00 55.41 C
ANISOU 2910 CG PHE A 372 6611 10001 4442 647 -867 149 C
ATOM 2911 CD1 PHE A 372 48.967 102.029 250.631 1.00 53.30 C
ANISOU 2911 CD1 PHE A 372 6409 9648 4195 733 -811 191 C
ATOM 2912 CD2 PHE A 372 48.850 103.825 252.194 1.00 53.47 C
ANISOU 2912 CD2 PHE A 372 6457 9712 4146 557 -866 121 C
ATOM 2913 CE1 PHE A 372 47.624 101.735 250.879 1.00 50.58 C
ANISOU 2913 CE1 PHE A 372 6209 9184 3824 723 -759 210 C
ATOM 2914 CE2 PHE A 372 47.516 103.529 252.446 1.00 50.11 C
ANISOU 2914 CE2 PHE A 372 6175 9173 3694 558 -808 140 C
ATOM 2915 CZ PHE A 372 46.906 102.488 251.788 1.00 49.08 C
ANISOU 2915 CZ PHE A 372 6096 8964 3586 636 -755 187 C
ATOM 2916 N SER A 373 53.274 100.999 250.170 1.00 60.24 N
ANISOU 2916 N SER A 373 6849 10916 5125 962 -1004 213 N
ATOM 2917 CA SER A 373 54.420 100.479 249.449 1.00 61.32 C
ANISOU 2917 CA SER A 373 6841 11151 5309 1062 -1014 225 C
ATOM 2918 C SER A 373 54.232 100.423 247.930 1.00 60.93 C
ANISOU 2918 C SER A 373 6761 11058 5332 1072 -905 217 C
ATOM 2919 O SER A 373 53.633 99.480 247.402 1.00 60.07 O
ANISOU 2919 O SER A 373 6745 10850 5228 1160 -853 241 O
ATOM 2920 CB SER A 373 54.732 99.087 249.978 1.00 62.06 C
ANISOU 2920 CB SER A 373 6975 11246 5361 1230 -1075 278 C
ATOM 2921 OG SER A 373 55.847 98.522 249.316 1.00 63.77 O
ANISOU 2921 OG SER A 373 7052 11557 5622 1346 -1084 290 O
ATOM 2922 N SER A 374 54.784 101.419 247.239 1.00 61.18 N
ANISOU 2922 N SER A 374 6663 11167 5417 978 -873 183 N
ATOM 2923 CA SER A 374 54.788 101.476 245.785 1.00 61.32 C
ANISOU 2923 CA SER A 374 6631 11170 5498 981 -774 175 C
ATOM 2924 C SER A 374 54.925 100.106 245.122 1.00 61.60 C
ANISOU 2924 C SER A 374 6685 11178 5541 1150 -742 204 C
ATOM 2925 O SER A 374 54.228 99.783 244.144 1.00 60.35 O
ANISOU 2925 O SER A 374 6601 10925 5405 1167 -656 204 O
ATOM 2926 CB SER A 374 55.938 102.375 245.312 1.00 62.44 C
ANISOU 2926 CB SER A 374 6581 11456 5687 909 -775 151 C
ATOM 2927 OG SER A 374 55.987 103.579 246.063 1.00 64.15 O
ANISOU 2927 OG SER A 374 6776 11705 5891 759 -824 122 O
ATOM 2928 N ALA A 375 55.825 99.308 245.685 1.00 63.23 N
ANISOU 2928 N ALA A 375 6830 11467 5729 1276 -817 228 N
ATOM 2929 CA ALA A 375 56.259 98.042 245.096 1.00 64.36 C
ANISOU 2929 CA ALA A 375 6961 11608 5884 1452 -797 251 C
ATOM 2930 C ALA A 375 55.239 96.913 245.213 1.00 63.67 C
ANISOU 2930 C ALA A 375 7068 11360 5764 1540 -780 280 C
ATOM 2931 O ALA A 375 55.484 95.794 244.768 1.00 64.37 O
ANISOU 2931 O ALA A 375 7178 11420 5858 1690 -764 298 O
ATOM 2932 CB ALA A 375 57.586 97.619 245.718 1.00 66.01 C
ANISOU 2932 CB ALA A 375 7031 11963 6086 1562 -889 271 C
ATOM 2933 N THR A 376 54.100 97.212 245.820 1.00 62.78 N
ANISOU 2933 N THR A 376 7097 11142 5616 1447 -783 283 N
ATOM 2934 CA THR A 376 53.071 96.203 246.074 1.00 61.99 C
ANISOU 2934 CA THR A 376 7182 10892 5480 1507 -773 315 C
ATOM 2935 C THR A 376 51.888 96.322 245.104 1.00 60.44 C
ANISOU 2935 C THR A 376 7086 10568 5309 1438 -673 300 C
ATOM 2936 O THR A 376 50.925 95.565 245.200 1.00 60.07 O
ANISOU 2936 O THR A 376 7192 10393 5240 1464 -655 324 O
ATOM 2937 CB THR A 376 52.574 96.290 247.526 1.00 61.91 C
ANISOU 2937 CB THR A 376 7266 10853 5403 1464 -846 339 C
ATOM 2938 OG1 THR A 376 52.113 97.627 247.781 1.00 60.68 O
ANISOU 2938 OG1 THR A 376 7099 10711 5248 1297 -832 304 O
ATOM 2939 CG2 THR A 376 53.701 95.933 248.490 1.00 62.13 C
ANISOU 2939 CG2 THR A 376 7214 10995 5396 1555 -956 364 C
ATOM 2940 N LEU A 377 51.967 97.279 244.185 1.00 59.58 N
ANISOU 2940 N LEU A 377 6892 10501 5246 1345 -611 264 N
ATOM 2941 CA LEU A 377 50.961 97.452 243.154 1.00 58.65 C
ANISOU 2941 CA LEU A 377 6851 10282 5153 1283 -521 251 C
ATOM 2942 C LEU A 377 50.666 96.138 242.414 1.00 59.11 C
ANISOU 2942 C LEU A 377 7000 10247 5212 1403 -483 265 C
ATOM 2943 O LEU A 377 51.570 95.542 241.813 1.00 60.23 O
ANISOU 2943 O LEU A 377 7071 10444 5370 1516 -473 259 O
ATOM 2944 CB LEU A 377 51.422 98.513 242.146 1.00 58.29 C
ANISOU 2944 CB LEU A 377 6678 10315 5156 1199 -465 217 C
ATOM 2945 CG LEU A 377 50.419 98.875 241.040 1.00 57.26 C
ANISOU 2945 CG LEU A 377 6614 10094 5049 1121 -377 205 C
ATOM 2946 CD1 LEU A 377 49.673 100.174 241.362 1.00 54.43 C
ANISOU 2946 CD1 LEU A 377 6275 9709 4697 963 -368 193 C
ATOM 2947 CD2 LEU A 377 51.081 98.933 239.631 1.00 59.32 C
ANISOU 2947 CD2 LEU A 377 6779 10415 5345 1148 -308 186 C
ATOM 2948 N LYS A 378 49.401 95.710 242.458 1.00 58.51 N
ANISOU 2948 N LYS A 378 7080 10033 5118 1376 -460 281 N
ATOM 2949 CA LYS A 378 48.915 94.535 241.725 1.00 58.71 C
ANISOU 2949 CA LYS A 378 7217 9948 5143 1461 -422 290 C
ATOM 2950 C LYS A 378 47.761 94.944 240.790 1.00 57.53 C
ANISOU 2950 C LYS A 378 7133 9712 5012 1356 -349 274 C
ATOM 2951 O LYS A 378 46.829 95.614 241.218 1.00 56.89 O
ANISOU 2951 O LYS A 378 7099 9590 4927 1243 -345 281 O
ATOM 2952 CB LYS A 378 48.485 93.431 242.718 1.00 59.12 C
ANISOU 2952 CB LYS A 378 7403 9908 5152 1533 -476 333 C
ATOM 2953 CG LYS A 378 48.245 92.040 242.114 1.00 60.29 C
ANISOU 2953 CG LYS A 378 7666 9944 5298 1645 -454 345 C
ATOM 2954 CD LYS A 378 47.606 91.061 243.118 1.00 62.91 C
ANISOU 2954 CD LYS A 378 8151 10165 5587 1684 -501 395 C
ATOM 2955 CE LYS A 378 46.924 89.852 242.407 1.00 64.32 C
ANISOU 2955 CE LYS A 378 8478 10193 5767 1738 -466 402 C
ATOM 2956 NZ LYS A 378 46.677 88.655 243.297 1.00 64.70 N
ANISOU 2956 NZ LYS A 378 8666 10139 5777 1817 -517 456 N
ATOM 2957 N GLU A 379 47.850 94.585 239.508 1.00 57.93 N
ANISOU 2957 N GLU A 379 7184 9745 5083 1395 -291 252 N
ATOM 2958 CA GLU A 379 46.747 94.787 238.567 1.00 57.04 C
ANISOU 2958 CA GLU A 379 7146 9545 4981 1311 -231 242 C
ATOM 2959 C GLU A 379 45.881 93.550 238.609 1.00 57.53 C
ANISOU 2959 C GLU A 379 7369 9468 5021 1359 -236 262 C
ATOM 2960 O GLU A 379 46.393 92.434 238.541 1.00 58.11 O
ANISOU 2960 O GLU A 379 7484 9514 5083 1486 -251 264 O
ATOM 2961 CB GLU A 379 47.209 95.059 237.132 1.00 56.74 C
ANISOU 2961 CB GLU A 379 7038 9557 4965 1317 -166 208 C
ATOM 2962 CG GLU A 379 46.005 95.516 236.279 1.00 57.57 C
ANISOU 2962 CG GLU A 379 7211 9586 5077 1206 -115 203 C
ATOM 2963 CD GLU A 379 46.244 95.679 234.768 1.00 58.15 C
ANISOU 2963 CD GLU A 379 7250 9688 5159 1206 -48 174 C
ATOM 2964 OE1 GLU A 379 47.045 96.555 234.370 1.00 59.10 O
ANISOU 2964 OE1 GLU A 379 7242 9917 5295 1177 -22 160 O
ATOM 2965 OE2 GLU A 379 45.569 94.962 233.982 1.00 56.36 O
ANISOU 2965 OE2 GLU A 379 7128 9370 4916 1222 -22 166 O
ATOM 2966 N LEU A 380 44.571 93.756 238.729 1.00 57.58 N
ANISOU 2966 N LEU A 380 7467 9385 5025 1257 -225 277 N
ATOM 2967 CA LEU A 380 43.620 92.669 238.951 1.00 58.30 C
ANISOU 2967 CA LEU A 380 7712 9342 5096 1273 -235 304 C
ATOM 2968 C LEU A 380 43.252 91.975 237.656 1.00 59.48 C
ANISOU 2968 C LEU A 380 7933 9416 5250 1296 -193 282 C
ATOM 2969 O LEU A 380 42.955 92.635 236.645 1.00 59.65 O
ANISOU 2969 O LEU A 380 7919 9456 5289 1227 -147 257 O
ATOM 2970 CB LEU A 380 42.365 93.183 239.658 1.00 57.15 C
ANISOU 2970 CB LEU A 380 7623 9146 4947 1153 -238 332 C
ATOM 2971 CG LEU A 380 42.351 93.060 241.185 1.00 56.95 C
ANISOU 2971 CG LEU A 380 7626 9123 4890 1161 -290 368 C
ATOM 2972 CD1 LEU A 380 43.240 94.088 241.842 1.00 56.60 C
ANISOU 2972 CD1 LEU A 380 7458 9204 4845 1148 -316 355 C
ATOM 2973 CD2 LEU A 380 40.937 93.179 241.709 1.00 55.84 C
ANISOU 2973 CD2 LEU A 380 7574 8903 4741 1060 -278 398 C
ATOM 2974 N HIS A 381 43.261 90.645 237.697 1.00 61.08 N
ANISOU 2974 N HIS A 381 8245 9528 5434 1391 -211 292 N
ATOM 2975 CA HIS A 381 43.115 89.828 236.499 1.00 62.37 C
ANISOU 2975 CA HIS A 381 8486 9617 5594 1435 -177 262 C
ATOM 2976 C HIS A 381 41.661 89.513 236.197 1.00 61.99 C
ANISOU 2976 C HIS A 381 8564 9447 5543 1335 -167 275 C
ATOM 2977 O HIS A 381 40.898 89.087 237.061 1.00 61.78 O
ANISOU 2977 O HIS A 381 8625 9342 5508 1300 -197 316 O
ATOM 2978 CB HIS A 381 43.904 88.534 236.663 1.00 63.96 C
ANISOU 2978 CB HIS A 381 8748 9773 5779 1595 -202 262 C
ATOM 2979 CG HIS A 381 43.971 87.698 235.421 1.00 66.62 C
ANISOU 2979 CG HIS A 381 9161 10043 6109 1662 -164 219 C
ATOM 2980 ND1 HIS A 381 43.056 86.702 235.144 1.00 67.59 N
ANISOU 2980 ND1 HIS A 381 9451 10014 6218 1648 -168 222 N
ATOM 2981 CD2 HIS A 381 44.858 87.692 234.393 1.00 68.94 C
ANISOU 2981 CD2 HIS A 381 9390 10401 6403 1742 -121 170 C
ATOM 2982 CE1 HIS A 381 43.367 86.128 233.992 1.00 68.89 C
ANISOU 2982 CE1 HIS A 381 9658 10146 6372 1717 -132 172 C
ATOM 2983 NE2 HIS A 381 44.458 86.708 233.518 1.00 69.58 N
ANISOU 2983 NE2 HIS A 381 9607 10366 6466 1779 -99 140 N
ATOM 2984 N PHE A 382 41.280 89.720 234.950 1.00 62.18 N
ANISOU 2984 N PHE A 382 8594 9459 5571 1288 -126 241 N
ATOM 2985 CA PHE A 382 39.968 89.300 234.510 1.00 62.51 C
ANISOU 2985 CA PHE A 382 8753 9388 5609 1201 -122 248 C
ATOM 2986 C PHE A 382 40.083 88.393 233.288 1.00 63.83 C
ANISOU 2986 C PHE A 382 9006 9489 5757 1260 -101 204 C
ATOM 2987 O PHE A 382 41.083 88.457 232.546 1.00 64.59 O
ANISOU 2987 O PHE A 382 9042 9652 5845 1343 -70 163 O
ATOM 2988 CB PHE A 382 39.120 90.519 234.212 1.00 61.60 C
ANISOU 2988 CB PHE A 382 8575 9315 5513 1062 -100 256 C
ATOM 2989 CG PHE A 382 38.878 91.394 235.412 1.00 61.55 C
ANISOU 2989 CG PHE A 382 8504 9359 5523 1001 -117 293 C
ATOM 2990 CD1 PHE A 382 37.953 91.023 236.388 1.00 61.08 C
ANISOU 2990 CD1 PHE A 382 8521 9227 5460 952 -142 337 C
ATOM 2991 CD2 PHE A 382 39.569 92.596 235.561 1.00 61.06 C
ANISOU 2991 CD2 PHE A 382 8308 9416 5477 987 -105 283 C
ATOM 2992 CE1 PHE A 382 37.722 91.836 237.488 1.00 60.48 C
ANISOU 2992 CE1 PHE A 382 8392 9198 5390 899 -151 365 C
ATOM 2993 CE2 PHE A 382 39.343 93.416 236.652 1.00 59.45 C
ANISOU 2993 CE2 PHE A 382 8054 9250 5282 929 -120 309 C
ATOM 2994 CZ PHE A 382 38.421 93.035 237.621 1.00 59.83 C
ANISOU 2994 CZ PHE A 382 8183 9228 5321 890 -141 348 C
ATOM 2995 N ASP A 383 39.060 87.558 233.073 1.00 64.31 N
ANISOU 2995 N ASP A 383 9206 9421 5807 1212 -114 211 N
ATOM 2996 CA ASP A 383 39.101 86.501 232.028 1.00 65.10 C
ANISOU 2996 CA ASP A 383 9423 9432 5882 1269 -103 166 C
ATOM 2997 C ASP A 383 38.868 86.937 230.562 1.00 63.77 C
ANISOU 2997 C ASP A 383 9239 9293 5699 1217 -65 118 C
ATOM 2998 O ASP A 383 39.660 86.572 229.683 1.00 64.40 O
ANISOU 2998 O ASP A 383 9327 9387 5753 1310 -34 66 O
ATOM 2999 CB ASP A 383 38.225 85.274 232.404 1.00 66.30 C
ANISOU 2999 CB ASP A 383 9746 9421 6025 1247 -140 189 C
ATOM 3000 CG ASP A 383 36.835 85.658 232.948 1.00 67.26 C
ANISOU 3000 CG ASP A 383 9883 9508 6163 1090 -159 241 C
ATOM 3001 OD1 ASP A 383 36.662 86.792 233.476 1.00 69.53 O
ANISOU 3001 OD1 ASP A 383 10054 9892 6472 1025 -153 269 O
ATOM 3002 OD2 ASP A 383 35.921 84.803 232.875 1.00 67.25 O
ANISOU 3002 OD2 ASP A 383 10013 9384 6156 1033 -180 253 O
ATOM 3003 N GLU A 384 37.804 87.694 230.290 1.00 61.48 N
ANISOU 3003 N GLU A 384 8927 9013 5420 1075 -65 137 N
ATOM 3004 CA GLU A 384 37.496 88.064 228.889 1.00 59.99 C
ANISOU 3004 CA GLU A 384 8737 8846 5210 1021 -37 99 C
ATOM 3005 C GLU A 384 38.414 89.174 228.386 1.00 58.38 C
ANISOU 3005 C GLU A 384 8389 8786 5007 1046 8 81 C
ATOM 3006 O GLU A 384 38.875 89.990 229.178 1.00 58.26 O
ANISOU 3006 O GLU A 384 8260 8854 5021 1047 10 108 O
ATOM 3007 CB GLU A 384 36.027 88.422 228.714 1.00 58.87 C
ANISOU 3007 CB GLU A 384 8624 8665 5079 868 -59 129 C
ATOM 3008 CG GLU A 384 35.136 87.229 229.009 1.00 61.32 C
ANISOU 3008 CG GLU A 384 9082 8832 5384 835 -99 141 C
ATOM 3009 CD GLU A 384 33.648 87.582 229.100 1.00 63.72 C
ANISOU 3009 CD GLU A 384 9394 9107 5709 681 -124 183 C
ATOM 3010 OE1 GLU A 384 33.107 88.096 228.099 1.00 66.01 O
ANISOU 3010 OE1 GLU A 384 9664 9427 5990 607 -119 169 O
ATOM 3011 OE2 GLU A 384 33.015 87.327 230.159 1.00 63.10 O
ANISOU 3011 OE2 GLU A 384 9340 8979 5654 637 -147 233 O
ATOM 3012 N PRO A 385 38.716 89.189 227.072 1.00 57.34 N
ANISOU 3012 N PRO A 385 8266 8682 4839 1064 45 33 N
ATOM 3013 CA PRO A 385 39.616 90.233 226.559 1.00 55.67 C
ANISOU 3013 CA PRO A 385 7918 8608 4626 1082 93 21 C
ATOM 3014 C PRO A 385 38.969 91.619 226.539 1.00 53.11 C
ANISOU 3014 C PRO A 385 7503 8348 4329 952 94 61 C
ATOM 3015 O PRO A 385 39.683 92.615 226.643 1.00 52.39 O
ANISOU 3015 O PRO A 385 7285 8365 4256 952 122 70 O
ATOM 3016 CB PRO A 385 39.928 89.764 225.128 1.00 56.32 C
ANISOU 3016 CB PRO A 385 8060 8688 4652 1127 134 -38 C
ATOM 3017 CG PRO A 385 38.760 88.901 224.741 1.00 56.98 C
ANISOU 3017 CG PRO A 385 8301 8638 4710 1069 96 -49 C
ATOM 3018 CD PRO A 385 38.279 88.252 226.013 1.00 58.00 C
ANISOU 3018 CD PRO A 385 8488 8673 4876 1067 44 -12 C
ATOM 3019 N VAL A 386 37.639 91.644 226.398 1.00 51.05 N
ANISOU 3019 N VAL A 386 7307 8018 4072 844 64 83 N
ATOM 3020 CA VAL A 386 36.807 92.841 226.353 1.00 49.02 C
ANISOU 3020 CA VAL A 386 6984 7800 3842 723 59 123 C
ATOM 3021 C VAL A 386 35.708 92.686 227.407 1.00 47.83 C
ANISOU 3021 C VAL A 386 6869 7578 3728 656 15 168 C
ATOM 3022 O VAL A 386 34.792 91.885 227.249 1.00 48.35 O
ANISOU 3022 O VAL A 386 7038 7551 3782 616 -16 170 O
ATOM 3023 CB VAL A 386 36.207 93.067 224.928 1.00 49.22 C
ANISOU 3023 CB VAL A 386 7045 7826 3829 658 68 109 C
ATOM 3024 CG1 VAL A 386 35.490 91.813 224.409 1.00 52.12 C
ANISOU 3024 CG1 VAL A 386 7560 8083 4159 651 37 82 C
ATOM 3025 CG2 VAL A 386 35.243 94.254 224.878 1.00 47.88 C
ANISOU 3025 CG2 VAL A 386 6814 7686 3690 539 57 157 C
ATOM 3026 N PHE A 387 35.809 93.466 228.477 1.00 46.26 N
ANISOU 3026 N PHE A 387 6585 7424 3569 640 13 202 N
ATOM 3027 CA PHE A 387 34.988 93.324 229.670 1.00 44.74 C
ANISOU 3027 CA PHE A 387 6416 7179 3406 596 -19 242 C
ATOM 3028 C PHE A 387 34.766 94.695 230.321 1.00 43.93 C
ANISOU 3028 C PHE A 387 6206 7142 3343 534 -9 276 C
ATOM 3029 O PHE A 387 35.278 95.679 229.836 1.00 44.26 O
ANISOU 3029 O PHE A 387 6164 7261 3391 526 17 268 O
ATOM 3030 CB PHE A 387 35.732 92.425 230.656 1.00 45.07 C
ANISOU 3030 CB PHE A 387 6493 7190 3440 692 -34 239 C
ATOM 3031 CG PHE A 387 36.992 93.043 231.222 1.00 43.15 C
ANISOU 3031 CG PHE A 387 6145 7044 3207 760 -19 232 C
ATOM 3032 CD1 PHE A 387 38.212 92.877 230.584 1.00 41.93 C
ANISOU 3032 CD1 PHE A 387 5955 6944 3032 852 6 193 C
ATOM 3033 CD2 PHE A 387 36.961 93.772 232.412 1.00 40.80 C
ANISOU 3033 CD2 PHE A 387 5782 6784 2935 732 -29 263 C
ATOM 3034 CE1 PHE A 387 39.386 93.450 231.115 1.00 41.53 C
ANISOU 3034 CE1 PHE A 387 5794 6991 2993 908 16 189 C
ATOM 3035 CE2 PHE A 387 38.123 94.345 232.939 1.00 39.14 C
ANISOU 3035 CE2 PHE A 387 5474 6665 2731 784 -24 254 C
ATOM 3036 CZ PHE A 387 39.334 94.186 232.292 1.00 39.94 C
ANISOU 3036 CZ PHE A 387 5530 6826 2818 869 -4 219 C
ATOM 3037 N THR A 388 34.036 94.758 231.434 1.00 43.32 N
ANISOU 3037 N THR A 388 6136 7034 3290 493 -27 312 N
ATOM 3038 CA THR A 388 33.936 95.984 232.238 1.00 42.22 C
ANISOU 3038 CA THR A 388 5907 6952 3184 452 -17 335 C
ATOM 3039 C THR A 388 33.983 95.601 233.716 1.00 43.10 C
ANISOU 3039 C THR A 388 6038 7041 3295 478 -34 355 C
ATOM 3040 O THR A 388 33.283 94.667 234.138 1.00 43.29 O
ANISOU 3040 O THR A 388 6146 6991 3311 467 -53 376 O
ATOM 3041 CB THR A 388 32.599 96.711 231.995 1.00 41.50 C
ANISOU 3041 CB THR A 388 5800 6847 3122 351 -14 367 C
ATOM 3042 OG1 THR A 388 32.348 96.826 230.591 1.00 41.12 O
ANISOU 3042 OG1 THR A 388 5759 6801 3062 322 -9 356 O
ATOM 3043 CG2 THR A 388 32.594 98.086 232.648 1.00 38.92 C
ANISOU 3043 CG2 THR A 388 5383 6576 2828 318 4 381 C
ATOM 3044 N ALA A 389 34.778 96.323 234.508 1.00 43.43 N
ANISOU 3044 N ALA A 389 6007 7150 3345 504 -30 351 N
ATOM 3045 CA ALA A 389 34.798 96.110 235.958 1.00 44.36 C
ANISOU 3045 CA ALA A 389 6141 7260 3455 521 -48 371 C
ATOM 3046 C ALA A 389 34.840 97.401 236.758 1.00 44.75 C
ANISOU 3046 C ALA A 389 6111 7369 3523 481 -38 375 C
ATOM 3047 O ALA A 389 35.545 98.319 236.396 1.00 45.55 O
ANISOU 3047 O ALA A 389 6134 7537 3638 479 -25 353 O
ATOM 3048 CB ALA A 389 35.944 95.248 236.336 1.00 44.32 C
ANISOU 3048 CB ALA A 389 6157 7262 3421 623 -71 357 C
ATOM 3049 N HIS A 390 34.067 97.486 237.832 1.00 45.40 N
ANISOU 3049 N HIS A 390 6219 7427 3604 445 -40 403 N
ATOM 3050 CA HIS A 390 34.310 98.506 238.849 1.00 45.94 C
ANISOU 3050 CA HIS A 390 6232 7548 3674 428 -36 398 C
ATOM 3051 C HIS A 390 34.229 97.867 240.229 1.00 45.62 C
ANISOU 3051 C HIS A 390 6247 7487 3597 453 -56 420 C
ATOM 3052 O HIS A 390 33.529 96.877 240.433 1.00 45.71 O
ANISOU 3052 O HIS A 390 6339 7434 3595 451 -61 451 O
ATOM 3053 CB HIS A 390 33.302 99.679 238.830 1.00 46.22 C
ANISOU 3053 CB HIS A 390 6231 7584 3745 347 -4 407 C
ATOM 3054 CG HIS A 390 32.904 100.162 237.470 1.00 48.86 C
ANISOU 3054 CG HIS A 390 6536 7915 4113 308 15 405 C
ATOM 3055 ND1 HIS A 390 31.849 99.614 236.763 1.00 51.05 N
ANISOU 3055 ND1 HIS A 390 6856 8140 4401 275 19 428 N
ATOM 3056 CD2 HIS A 390 33.357 101.204 236.727 1.00 51.51 C
ANISOU 3056 CD2 HIS A 390 6805 8293 4472 290 30 387 C
ATOM 3057 CE1 HIS A 390 31.693 100.278 235.627 1.00 52.95 C
ANISOU 3057 CE1 HIS A 390 7058 8394 4666 244 31 424 C
ATOM 3058 NE2 HIS A 390 32.602 101.243 235.577 1.00 53.18 N
ANISOU 3058 NE2 HIS A 390 7024 8479 4704 254 41 401 N
ATOM 3059 N VAL A 391 34.953 98.470 241.165 1.00 45.15 N
ANISOU 3059 N VAL A 391 6148 7487 3521 469 -70 406 N
ATOM 3060 CA VAL A 391 34.809 98.230 242.587 1.00 44.78 C
ANISOU 3060 CA VAL A 391 6144 7436 3433 477 -85 426 C
ATOM 3061 C VAL A 391 33.513 98.857 243.038 1.00 44.30 C
ANISOU 3061 C VAL A 391 6096 7352 3384 401 -46 443 C
ATOM 3062 O VAL A 391 33.203 99.997 242.659 1.00 43.38 O
ANISOU 3062 O VAL A 391 5923 7257 3305 353 -18 424 O
ATOM 3063 CB VAL A 391 36.016 98.844 243.375 1.00 45.26 C
ANISOU 3063 CB VAL A 391 6149 7578 3469 509 -117 398 C
ATOM 3064 CG1 VAL A 391 36.747 99.878 242.542 1.00 45.15 C
ANISOU 3064 CG1 VAL A 391 6038 7623 3493 492 -108 358 C
ATOM 3065 CG2 VAL A 391 35.604 99.454 244.727 1.00 45.33 C
ANISOU 3065 CG2 VAL A 391 6175 7603 3445 472 -113 401 C
ATOM 3066 N VAL A 392 32.743 98.123 243.838 1.00 44.63 N
ANISOU 3066 N VAL A 392 6211 7350 3396 392 -42 481 N
ATOM 3067 CA VAL A 392 31.517 98.702 244.372 1.00 44.64 C
ANISOU 3067 CA VAL A 392 6217 7340 3406 327 3 499 C
ATOM 3068 C VAL A 392 31.773 99.349 245.733 1.00 46.17 C
ANISOU 3068 C VAL A 392 6410 7579 3556 329 4 486 C
ATOM 3069 O VAL A 392 31.861 98.669 246.776 1.00 47.38 O
ANISOU 3069 O VAL A 392 6624 7727 3650 353 -12 511 O
ATOM 3070 CB VAL A 392 30.362 97.710 244.391 1.00 43.94 C
ANISOU 3070 CB VAL A 392 6196 7185 3315 295 20 549 C
ATOM 3071 CG1 VAL A 392 29.130 98.419 244.789 1.00 43.35 C
ANISOU 3071 CG1 VAL A 392 6101 7112 3258 232 72 564 C
ATOM 3072 CG2 VAL A 392 30.146 97.167 243.022 1.00 43.74 C
ANISOU 3072 CG2 VAL A 392 6174 7118 3329 287 12 551 C
ATOM 3073 N CYS A 393 31.921 100.669 245.746 1.00 47.11 N
ANISOU 3073 N CYS A 393 6466 7739 3696 304 22 447 N
ATOM 3074 CA CYS A 393 32.271 101.308 247.026 1.00 48.78 C
ANISOU 3074 CA CYS A 393 6683 7992 3858 305 17 424 C
ATOM 3075 C CYS A 393 31.078 101.474 247.929 1.00 48.30 C
ANISOU 3075 C CYS A 393 6664 7913 3774 269 67 445 C
ATOM 3076 O CYS A 393 31.230 101.487 249.162 1.00 48.87 O
ANISOU 3076 O CYS A 393 6778 8011 3781 278 62 442 O
ATOM 3077 CB CYS A 393 33.046 102.610 246.851 1.00 48.70 C
ANISOU 3077 CB CYS A 393 6603 8029 3870 291 9 369 C
ATOM 3078 SG CYS A 393 34.810 102.230 246.727 1.00 55.06 S
ANISOU 3078 SG CYS A 393 7373 8894 4654 349 -65 347 S
ATOM 3079 N SER A 394 29.895 101.570 247.312 1.00 46.96 N
ANISOU 3079 N SER A 394 6481 7706 3654 230 116 468 N
ATOM 3080 CA SER A 394 28.653 101.624 248.069 1.00 46.66 C
ANISOU 3080 CA SER A 394 6472 7655 3602 197 172 495 C
ATOM 3081 C SER A 394 28.342 100.300 248.821 1.00 46.63 C
ANISOU 3081 C SER A 394 6548 7629 3541 203 167 549 C
ATOM 3082 O SER A 394 27.239 100.130 249.356 1.00 46.65 O
ANISOU 3082 O SER A 394 6573 7619 3531 169 219 583 O
ATOM 3083 CB SER A 394 27.516 101.975 247.129 1.00 46.22 C
ANISOU 3083 CB SER A 394 6370 7572 3620 156 216 512 C
ATOM 3084 OG SER A 394 27.165 100.837 246.369 1.00 46.84 O
ANISOU 3084 OG SER A 394 6468 7610 3716 147 199 554 O
ATOM 3085 N GLN A 395 29.306 99.369 248.828 1.00 45.89 N
ANISOU 3085 N GLN A 395 6494 7529 3413 247 108 558 N
ATOM 3086 CA GLN A 395 29.160 98.084 249.489 1.00 45.70 C
ANISOU 3086 CA GLN A 395 6557 7474 3334 260 94 613 C
ATOM 3087 C GLN A 395 30.395 97.757 250.332 1.00 46.52 C
ANISOU 3087 C GLN A 395 6699 7609 3366 321 35 605 C
ATOM 3088 O GLN A 395 30.489 96.710 250.969 1.00 46.74 O
ANISOU 3088 O GLN A 395 6806 7613 3339 345 12 651 O
ATOM 3089 CB GLN A 395 28.891 97.007 248.464 1.00 44.98 C
ANISOU 3089 CB GLN A 395 6490 7319 3283 256 78 647 C
ATOM 3090 CG GLN A 395 27.473 97.017 247.944 1.00 44.10 C
ANISOU 3090 CG GLN A 395 6359 7174 3221 186 131 675 C
ATOM 3091 CD GLN A 395 27.222 95.993 246.816 1.00 44.01 C
ANISOU 3091 CD GLN A 395 6374 7098 3250 172 107 700 C
ATOM 3092 OE1 GLN A 395 27.891 94.959 246.721 1.00 43.81 O
ANISOU 3092 OE1 GLN A 395 6413 7033 3199 214 62 713 O
ATOM 3093 NE2 GLN A 395 26.235 96.280 245.969 1.00 43.47 N
ANISOU 3093 NE2 GLN A 395 6258 7017 3241 115 136 706 N
ATOM 3094 N MET A 396 31.340 98.678 250.337 1.00 46.61 N
ANISOU 3094 N MET A 396 6654 7677 3379 343 7 549 N
ATOM 3095 CA MET A 396 32.526 98.526 251.120 1.00 47.57 C
ANISOU 3095 CA MET A 396 6793 7844 3437 396 -54 536 C
ATOM 3096 C MET A 396 32.339 99.403 252.298 1.00 48.22 C
ANISOU 3096 C MET A 396 6887 7972 3462 370 -33 512 C
ATOM 3097 O MET A 396 32.812 100.540 252.295 1.00 47.94 O
ANISOU 3097 O MET A 396 6795 7981 3440 356 -38 454 O
ATOM 3098 CB MET A 396 33.721 99.050 250.352 1.00 47.97 C
ANISOU 3098 CB MET A 396 6763 7937 3527 427 -99 487 C
ATOM 3099 CG MET A 396 33.740 98.610 248.896 1.00 48.90 C
ANISOU 3099 CG MET A 396 6848 8014 3717 438 -98 491 C
ATOM 3100 SD MET A 396 34.916 97.302 248.626 1.00 49.19 S
ANISOU 3100 SD MET A 396 6910 8045 3734 532 -167 511 S
ATOM 3101 CE MET A 396 34.910 96.396 250.185 1.00 51.62 C
ANISOU 3101 CE MET A 396 7322 8345 3946 566 -199 563 C
ATOM 3102 N LYS A 397 31.666 98.877 253.316 1.00 49.00 N
ANISOU 3102 N LYS A 397 7066 8059 3494 359 -7 556 N
ATOM 3103 CA LYS A 397 31.373 99.663 254.494 1.00 49.70 C
ANISOU 3103 CA LYS A 397 7178 8189 3516 334 24 532 C
ATOM 3104 C LYS A 397 32.365 99.461 255.649 1.00 50.84 C
ANISOU 3104 C LYS A 397 7372 8387 3559 374 -43 529 C
ATOM 3105 O LYS A 397 32.235 100.039 256.744 1.00 51.50 O
ANISOU 3105 O LYS A 397 7491 8509 3566 357 -27 507 O
ATOM 3106 CB LYS A 397 29.950 99.376 254.935 1.00 49.86 C
ANISOU 3106 CB LYS A 397 7246 8177 3520 291 105 579 C
ATOM 3107 CG LYS A 397 28.935 99.824 253.925 1.00 50.94 C
ANISOU 3107 CG LYS A 397 7321 8280 3754 248 169 574 C
ATOM 3108 CD LYS A 397 29.075 101.297 253.556 1.00 51.05 C
ANISOU 3108 CD LYS A 397 7260 8321 3816 235 187 501 C
ATOM 3109 CE LYS A 397 28.145 101.604 252.413 1.00 50.83 C
ANISOU 3109 CE LYS A 397 7170 8256 3887 203 236 508 C
ATOM 3110 NZ LYS A 397 27.832 103.037 252.444 1.00 53.29 N
ANISOU 3110 NZ LYS A 397 7435 8585 4229 185 281 452 N
ATOM 3111 N THR A 398 33.369 98.633 255.431 1.00 51.29 N
ANISOU 3111 N THR A 398 7434 8447 3609 432 -120 550 N
ATOM 3112 CA THR A 398 34.206 98.297 256.563 1.00 52.30 C
ANISOU 3112 CA THR A 398 7613 8624 3636 474 -188 562 C
ATOM 3113 C THR A 398 35.669 98.655 256.327 1.00 52.51 C
ANISOU 3113 C THR A 398 7566 8712 3672 517 -275 516 C
ATOM 3114 O THR A 398 36.320 98.181 255.400 1.00 51.72 O
ANISOU 3114 O THR A 398 7418 8601 3631 562 -311 522 O
ATOM 3115 CB THR A 398 33.915 96.847 257.138 1.00 52.98 C
ANISOU 3115 CB THR A 398 7807 8665 3659 507 -200 652 C
ATOM 3116 OG1 THR A 398 35.109 96.064 257.119 1.00 54.62 O
ANISOU 3116 OG1 THR A 398 8020 8886 3848 588 -293 673 O
ATOM 3117 CG2 THR A 398 32.809 96.095 256.354 1.00 51.78 C
ANISOU 3117 CG2 THR A 398 7680 8424 3572 478 -137 702 C
ATOM 3118 N TYR A 399 36.147 99.561 257.170 1.00 53.94 N
ANISOU 3118 N TYR A 399 7737 8963 3794 498 -302 466 N
ATOM 3119 CA TYR A 399 37.490 100.120 257.069 1.00 54.92 C
ANISOU 3119 CA TYR A 399 7782 9159 3924 518 -382 415 C
ATOM 3120 C TYR A 399 38.595 99.071 257.257 1.00 56.39 C
ANISOU 3120 C TYR A 399 7971 9380 4076 604 -478 458 C
ATOM 3121 O TYR A 399 39.618 99.110 256.570 1.00 56.30 O
ANISOU 3121 O TYR A 399 7870 9406 4115 639 -530 437 O
ATOM 3122 CB TYR A 399 37.649 101.259 258.073 1.00 54.98 C
ANISOU 3122 CB TYR A 399 7798 9227 3863 468 -393 353 C
ATOM 3123 CG TYR A 399 38.962 101.972 257.935 1.00 55.06 C
ANISOU 3123 CG TYR A 399 7719 9313 3888 466 -473 295 C
ATOM 3124 CD1 TYR A 399 39.287 102.664 256.753 1.00 52.79 C
ANISOU 3124 CD1 TYR A 399 7329 9023 3707 440 -458 253 C
ATOM 3125 CD2 TYR A 399 39.893 101.950 258.979 1.00 56.00 C
ANISOU 3125 CD2 TYR A 399 7852 9513 3912 486 -565 286 C
ATOM 3126 CE1 TYR A 399 40.513 103.328 256.619 1.00 53.41 C
ANISOU 3126 CE1 TYR A 399 7316 9176 3801 428 -529 203 C
ATOM 3127 CE2 TYR A 399 41.119 102.601 258.863 1.00 56.72 C
ANISOU 3127 CE2 TYR A 399 7849 9682 4018 475 -643 234 C
ATOM 3128 CZ TYR A 399 41.422 103.288 257.680 1.00 56.66 C
ANISOU 3128 CZ TYR A 399 7736 9669 4122 443 -622 193 C
ATOM 3129 OH TYR A 399 42.629 103.929 257.581 1.00 57.94 O
ANISOU 3129 OH TYR A 399 7801 9912 4299 422 -696 146 O
ATOM 3130 N ASP A 400 38.359 98.138 258.178 1.00 58.10 N
ANISOU 3130 N ASP A 400 8289 9581 4204 639 -496 521 N
ATOM 3131 CA ASP A 400 39.267 97.038 258.471 1.00 60.03 C
ANISOU 3131 CA ASP A 400 8558 9844 4408 730 -584 575 C
ATOM 3132 C ASP A 400 39.197 95.869 257.479 1.00 59.62 C
ANISOU 3132 C ASP A 400 8515 9713 4425 791 -575 627 C
ATOM 3133 O ASP A 400 39.952 94.915 257.614 1.00 60.37 O
ANISOU 3133 O ASP A 400 8631 9811 4497 880 -645 672 O
ATOM 3134 CB ASP A 400 38.968 96.507 259.881 1.00 62.22 C
ANISOU 3134 CB ASP A 400 8957 10128 4556 740 -604 629 C
ATOM 3135 CG ASP A 400 40.202 95.849 260.570 1.00 66.60 C
ANISOU 3135 CG ASP A 400 9522 10746 5038 829 -725 665 C
ATOM 3136 OD1 ASP A 400 41.326 95.887 259.984 1.00 68.57 O
ANISOU 3136 OD1 ASP A 400 9670 11045 5339 882 -792 640 O
ATOM 3137 OD2 ASP A 400 40.039 95.310 261.715 1.00 70.81 O
ANISOU 3137 OD2 ASP A 400 10162 11285 5458 846 -751 720 O
ATOM 3138 N ALA A 401 38.312 95.937 256.485 1.00 58.95 N
ANISOU 3138 N ALA A 401 8418 9557 4424 748 -494 620 N
ATOM 3139 CA ALA A 401 38.052 94.794 255.580 1.00 58.78 C
ANISOU 3139 CA ALA A 401 8429 9446 4459 792 -478 668 C
ATOM 3140 C ALA A 401 39.272 94.203 254.855 1.00 59.14 C
ANISOU 3140 C ALA A 401 8417 9507 4546 890 -545 666 C
ATOM 3141 O ALA A 401 40.332 94.845 254.734 1.00 59.15 O
ANISOU 3141 O ALA A 401 8317 9596 4560 913 -594 619 O
ATOM 3142 CB ALA A 401 36.942 95.115 254.579 1.00 57.59 C
ANISOU 3142 CB ALA A 401 8260 9231 4391 720 -388 652 C
ATOM 3143 N SER A 402 39.106 92.961 254.399 1.00 59.34 N
ANISOU 3143 N SER A 402 8510 9446 4591 946 -545 718 N
ATOM 3144 CA SER A 402 40.119 92.285 253.589 1.00 59.83 C
ANISOU 3144 CA SER A 402 8529 9504 4698 1049 -592 717 C
ATOM 3145 C SER A 402 39.491 91.764 252.292 1.00 58.82 C
ANISOU 3145 C SER A 402 8421 9279 4650 1039 -534 716 C
ATOM 3146 O SER A 402 40.190 91.287 251.404 1.00 58.76 O
ANISOU 3146 O SER A 402 8377 9261 4688 1115 -552 702 O
ATOM 3147 CB SER A 402 40.805 91.154 254.374 1.00 61.12 C
ANISOU 3147 CB SER A 402 8768 9658 4796 1157 -669 780 C
ATOM 3148 OG SER A 402 39.850 90.323 255.021 1.00 62.91 O
ANISOU 3148 OG SER A 402 9139 9792 4971 1136 -647 851 O
ATOM 3149 N LEU A 403 38.167 91.857 252.203 1.00 58.02 N
ANISOU 3149 N LEU A 403 8374 9111 4559 945 -464 729 N
ATOM 3150 CA LEU A 403 37.447 91.429 251.014 1.00 56.99 C
ANISOU 3150 CA LEU A 403 8264 8892 4497 918 -413 728 C
ATOM 3151 C LEU A 403 36.972 92.678 250.300 1.00 55.72 C
ANISOU 3151 C LEU A 403 8008 8770 4394 830 -357 670 C
ATOM 3152 O LEU A 403 36.378 93.589 250.926 1.00 55.91 O
ANISOU 3152 O LEU A 403 8015 8831 4398 755 -325 658 O
ATOM 3153 CB LEU A 403 36.286 90.484 251.360 1.00 56.95 C
ANISOU 3153 CB LEU A 403 8391 8779 4469 876 -381 794 C
ATOM 3154 CG LEU A 403 36.753 89.079 251.779 1.00 59.60 C
ANISOU 3154 CG LEU A 403 8837 9047 4763 970 -435 856 C
ATOM 3155 CD1 LEU A 403 35.765 88.358 252.716 1.00 61.09 C
ANISOU 3155 CD1 LEU A 403 9158 9161 4893 920 -415 935 C
ATOM 3156 CD2 LEU A 403 37.147 88.185 250.590 1.00 60.48 C
ANISOU 3156 CD2 LEU A 403 8968 9081 4931 1042 -447 846 C
ATOM 3157 N LEU A 404 37.267 92.723 248.999 1.00 54.04 N
ANISOU 3157 N LEU A 404 7736 8547 4248 847 -346 633 N
ATOM 3158 CA LEU A 404 36.930 93.844 248.147 1.00 51.87 C
ANISOU 3158 CA LEU A 404 7372 8305 4032 776 -299 583 C
ATOM 3159 C LEU A 404 35.886 93.441 247.101 1.00 51.04 C
ANISOU 3159 C LEU A 404 7305 8113 3977 727 -250 592 C
ATOM 3160 O LEU A 404 36.043 92.447 246.378 1.00 50.79 O
ANISOU 3160 O LEU A 404 7319 8018 3961 776 -262 602 O
ATOM 3161 CB LEU A 404 38.205 94.401 247.524 1.00 51.72 C
ANISOU 3161 CB LEU A 404 7242 8367 4042 826 -327 532 C
ATOM 3162 CG LEU A 404 38.243 94.998 246.113 1.00 51.65 C
ANISOU 3162 CG LEU A 404 7154 8370 4103 798 -289 488 C
ATOM 3163 CD1 LEU A 404 39.170 96.207 246.076 1.00 51.03 C
ANISOU 3163 CD1 LEU A 404 6955 8397 4038 786 -302 440 C
ATOM 3164 CD2 LEU A 404 38.681 93.974 245.062 1.00 51.10 C
ANISOU 3164 CD2 LEU A 404 7105 8255 4056 874 -296 488 C
ATOM 3165 N ARG A 405 34.821 94.235 247.037 1.00 49.78 N
ANISOU 3165 N ARG A 405 7124 7950 3840 632 -198 587 N
ATOM 3166 CA ARG A 405 33.642 93.937 246.254 1.00 48.51 C
ANISOU 3166 CA ARG A 405 6996 7717 3719 569 -155 604 C
ATOM 3167 C ARG A 405 33.741 94.513 244.827 1.00 47.78 C
ANISOU 3167 C ARG A 405 6827 7637 3689 553 -137 559 C
ATOM 3168 O ARG A 405 33.972 95.717 244.642 1.00 47.56 O
ANISOU 3168 O ARG A 405 6711 7674 3684 528 -122 522 O
ATOM 3169 CB ARG A 405 32.426 94.473 247.013 1.00 47.96 C
ANISOU 3169 CB ARG A 405 6938 7646 3638 484 -108 627 C
ATOM 3170 CG ARG A 405 31.084 94.262 246.340 1.00 48.20 C
ANISOU 3170 CG ARG A 405 6987 7616 3712 407 -63 650 C
ATOM 3171 CD ARG A 405 30.663 92.781 246.216 1.00 49.55 C
ANISOU 3171 CD ARG A 405 7263 7692 3871 409 -77 700 C
ATOM 3172 NE ARG A 405 30.589 92.062 247.496 1.00 49.95 N
ANISOU 3172 NE ARG A 405 7402 7720 3858 422 -87 752 N
ATOM 3173 CZ ARG A 405 29.675 92.272 248.437 1.00 49.03 C
ANISOU 3173 CZ ARG A 405 7304 7612 3712 360 -46 789 C
ATOM 3174 NH1 ARG A 405 28.757 93.205 248.269 1.00 47.58 N
ANISOU 3174 NH1 ARG A 405 7053 7461 3565 288 7 775 N
ATOM 3175 NH2 ARG A 405 29.684 91.553 249.554 1.00 49.64 N
ANISOU 3175 NH2 ARG A 405 7469 7668 3723 375 -57 840 N
ATOM 3176 N LEU A 406 33.577 93.641 243.821 1.00 47.56 N
ANISOU 3176 N LEU A 406 6842 7544 3684 567 -140 564 N
ATOM 3177 CA LEU A 406 33.612 94.021 242.388 1.00 46.25 C
ANISOU 3177 CA LEU A 406 6622 7383 3566 552 -124 527 C
ATOM 3178 C LEU A 406 32.365 93.580 241.664 1.00 46.02 C
ANISOU 3178 C LEU A 406 6641 7280 3563 482 -101 548 C
ATOM 3179 O LEU A 406 31.846 92.489 241.924 1.00 46.81 O
ANISOU 3179 O LEU A 406 6836 7303 3646 476 -111 584 O
ATOM 3180 CB LEU A 406 34.760 93.331 241.661 1.00 46.35 C
ANISOU 3180 CB LEU A 406 6640 7394 3576 645 -153 501 C
ATOM 3181 CG LEU A 406 36.114 93.257 242.346 1.00 46.73 C
ANISOU 3181 CG LEU A 406 6658 7502 3593 739 -191 491 C
ATOM 3182 CD1 LEU A 406 36.932 92.062 241.854 1.00 45.23 C
ANISOU 3182 CD1 LEU A 406 6519 7273 3394 845 -218 486 C
ATOM 3183 CD2 LEU A 406 36.838 94.609 242.197 1.00 45.59 C
ANISOU 3183 CD2 LEU A 406 6388 7465 3469 727 -183 450 C
ATOM 3184 N ARG A 407 31.929 94.429 240.732 1.00 45.21 N
ANISOU 3184 N ARG A 407 6473 7202 3501 429 -75 526 N
ATOM 3185 CA ARG A 407 30.911 94.139 239.701 1.00 44.57 C
ANISOU 3185 CA ARG A 407 6417 7069 3451 366 -63 534 C
ATOM 3186 C ARG A 407 31.651 93.908 238.358 1.00 43.99 C
ANISOU 3186 C ARG A 407 6336 6995 3383 410 -76 494 C
ATOM 3187 O ARG A 407 32.424 94.758 237.923 1.00 43.56 O
ANISOU 3187 O ARG A 407 6204 7009 3340 435 -68 461 O
ATOM 3188 CB ARG A 407 29.987 95.364 239.580 1.00 44.23 C
ANISOU 3188 CB ARG A 407 6296 7064 3444 287 -29 539 C
ATOM 3189 CG ARG A 407 28.625 95.169 238.971 1.00 43.98 C
ANISOU 3189 CG ARG A 407 6280 6990 3442 205 -17 566 C
ATOM 3190 CD ARG A 407 27.810 96.437 239.111 1.00 45.07 C
ANISOU 3190 CD ARG A 407 6335 7174 3615 149 18 575 C
ATOM 3191 NE ARG A 407 27.780 97.172 237.863 1.00 51.53 N
ANISOU 3191 NE ARG A 407 7095 8016 4466 131 20 554 N
ATOM 3192 CZ ARG A 407 28.417 98.325 237.625 1.00 54.81 C
ANISOU 3192 CZ ARG A 407 7440 8487 4896 151 31 526 C
ATOM 3193 NH1 ARG A 407 29.127 98.917 238.590 1.00 54.96 N
ANISOU 3193 NH1 ARG A 407 7434 8546 4902 184 41 510 N
ATOM 3194 NH2 ARG A 407 28.324 98.899 236.412 1.00 54.37 N
ANISOU 3194 NH2 ARG A 407 7344 8447 4867 131 32 516 N
ATOM 3195 N TYR A 408 31.427 92.757 237.727 1.00 43.61 N
ANISOU 3195 N TYR A 408 6375 6870 3326 417 -93 496 N
ATOM 3196 CA TYR A 408 32.135 92.365 236.518 1.00 43.55 C
ANISOU 3196 CA TYR A 408 6382 6854 3313 469 -101 455 C
ATOM 3197 C TYR A 408 31.112 91.968 235.519 1.00 43.96 C
ANISOU 3197 C TYR A 408 6481 6846 3374 397 -103 457 C
ATOM 3198 O TYR A 408 30.148 91.282 235.877 1.00 44.66 O
ANISOU 3198 O TYR A 408 6640 6866 3464 340 -113 492 O
ATOM 3199 CB TYR A 408 32.975 91.130 236.770 1.00 44.10 C
ANISOU 3199 CB TYR A 408 6536 6871 3350 566 -126 448 C
ATOM 3200 CG TYR A 408 33.496 90.460 235.523 1.00 43.87 C
ANISOU 3200 CG TYR A 408 6551 6809 3310 620 -130 405 C
ATOM 3201 CD1 TYR A 408 34.653 90.910 234.922 1.00 45.60 C
ANISOU 3201 CD1 TYR A 408 6698 7102 3524 693 -117 362 C
ATOM 3202 CD2 TYR A 408 32.851 89.353 234.957 1.00 44.37 C
ANISOU 3202 CD2 TYR A 408 6730 6765 3362 596 -145 405 C
ATOM 3203 CE1 TYR A 408 35.155 90.304 233.760 1.00 45.68 C
ANISOU 3203 CE1 TYR A 408 6750 7089 3518 749 -111 319 C
ATOM 3204 CE2 TYR A 408 33.358 88.722 233.816 1.00 43.23 C
ANISOU 3204 CE2 TYR A 408 6639 6587 3199 651 -147 357 C
ATOM 3205 CZ TYR A 408 34.508 89.217 233.230 1.00 43.89 C
ANISOU 3205 CZ TYR A 408 6647 6753 3276 731 -126 314 C
ATOM 3206 OH TYR A 408 35.067 88.653 232.126 1.00 43.67 O
ANISOU 3206 OH TYR A 408 6663 6704 3224 794 -117 264 O
ATOM 3207 N SER A 409 31.354 92.341 234.261 1.00 43.89 N
ANISOU 3207 N SER A 409 6441 6867 3370 398 -96 421 N
ATOM 3208 CA SER A 409 30.372 92.204 233.172 1.00 43.46 C
ANISOU 3208 CA SER A 409 6414 6776 3321 320 -102 420 C
ATOM 3209 C SER A 409 31.028 92.184 231.793 1.00 43.89 C
ANISOU 3209 C SER A 409 6473 6850 3355 358 -99 371 C
ATOM 3210 O SER A 409 32.149 92.660 231.588 1.00 43.54 O
ANISOU 3210 O SER A 409 6371 6870 3302 427 -79 343 O
ATOM 3211 CB SER A 409 29.418 93.387 233.225 1.00 42.61 C
ANISOU 3211 CB SER A 409 6219 6719 3251 232 -87 450 C
ATOM 3212 OG SER A 409 28.201 93.065 232.632 1.00 42.59 O
ANISOU 3212 OG SER A 409 6251 6673 3260 146 -104 469 O
ATOM 3213 N SER A 410 30.315 91.625 230.838 1.00 44.68 N
ANISOU 3213 N SER A 410 6639 6896 3443 306 -117 362 N
ATOM 3214 CA SER A 410 30.640 91.863 229.450 1.00 45.62 C
ANISOU 3214 CA SER A 410 6750 7045 3538 314 -110 323 C
ATOM 3215 C SER A 410 29.357 91.767 228.634 1.00 46.12 C
ANISOU 3215 C SER A 410 6847 7074 3602 209 -137 336 C
ATOM 3216 O SER A 410 28.393 91.127 229.043 1.00 46.20 O
ANISOU 3216 O SER A 410 6912 7018 3625 145 -164 363 O
ATOM 3217 CB SER A 410 31.639 90.828 228.958 1.00 46.50 C
ANISOU 3217 CB SER A 410 6946 7116 3606 412 -109 271 C
ATOM 3218 OG SER A 410 30.959 89.652 228.551 1.00 47.45 O
ANISOU 3218 OG SER A 410 7193 7130 3704 378 -141 261 O
ATOM 3219 N MET A 411 29.361 92.386 227.463 1.00 46.73 N
ANISOU 3219 N MET A 411 6890 7201 3663 188 -132 318 N
ATOM 3220 CA MET A 411 28.238 92.306 226.536 1.00 47.13 C
ANISOU 3220 CA MET A 411 6972 7231 3706 94 -166 326 C
ATOM 3221 C MET A 411 27.760 90.867 226.244 1.00 47.69 C
ANISOU 3221 C MET A 411 7177 7196 3746 66 -206 305 C
ATOM 3222 O MET A 411 26.732 90.668 225.617 1.00 48.02 O
ANISOU 3222 O MET A 411 7249 7212 3783 -25 -244 315 O
ATOM 3223 CB MET A 411 28.618 93.010 225.241 1.00 47.27 C
ANISOU 3223 CB MET A 411 6955 7314 3690 100 -154 302 C
ATOM 3224 CG MET A 411 28.720 94.512 225.363 1.00 47.19 C
ANISOU 3224 CG MET A 411 6820 7396 3716 90 -125 335 C
ATOM 3225 SD MET A 411 28.907 95.262 223.732 1.00 49.59 S
ANISOU 3225 SD MET A 411 7103 7765 3975 74 -119 321 S
ATOM 3226 CE MET A 411 30.584 94.719 223.357 1.00 52.44 C
ANISOU 3226 CE MET A 411 7501 8143 4280 191 -74 255 C
ATOM 3227 N THR A 412 28.519 89.880 226.705 1.00 48.10 N
ANISOU 3227 N THR A 412 7311 7184 3779 145 -200 277 N
ATOM 3228 CA THR A 412 28.190 88.458 226.549 1.00 48.49 C
ANISOU 3228 CA THR A 412 7506 7116 3803 129 -235 255 C
ATOM 3229 C THR A 412 27.763 87.839 227.897 1.00 48.12 C
ANISOU 3229 C THR A 412 7493 7000 3790 110 -245 300 C
ATOM 3230 O THR A 412 26.782 87.137 227.998 1.00 48.06 O
ANISOU 3230 O THR A 412 7554 6916 3789 21 -280 321 O
ATOM 3231 CB THR A 412 29.414 87.736 225.979 1.00 48.96 C
ANISOU 3231 CB THR A 412 7648 7144 3811 247 -217 187 C
ATOM 3232 OG1 THR A 412 29.324 87.727 224.557 1.00 48.85 O
ANISOU 3232 OG1 THR A 412 7672 7140 3748 224 -225 141 O
ATOM 3233 CG2 THR A 412 29.534 86.310 226.511 1.00 51.07 C
ANISOU 3233 CG2 THR A 412 8053 7282 4068 287 -236 174 C
ATOM 3234 N THR A 413 28.510 88.162 228.930 1.00 47.49 N
ANISOU 3234 N THR A 413 7359 6955 3728 187 -215 318 N
ATOM 3235 CA THR A 413 28.361 87.595 230.242 1.00 48.14 C
ANISOU 3235 CA THR A 413 7480 6983 3830 192 -220 359 C
ATOM 3236 C THR A 413 27.450 88.448 231.127 1.00 47.52 C
ANISOU 3236 C THR A 413 7303 6958 3795 109 -210 422 C
ATOM 3237 O THR A 413 27.817 89.566 231.474 1.00 47.35 O
ANISOU 3237 O THR A 413 7170 7031 3792 136 -181 430 O
ATOM 3238 CB THR A 413 29.769 87.544 230.868 1.00 48.23 C
ANISOU 3238 CB THR A 413 7479 7018 3828 331 -196 342 C
ATOM 3239 OG1 THR A 413 30.510 86.494 230.239 1.00 50.34 O
ANISOU 3239 OG1 THR A 413 7856 7212 4057 415 -204 289 O
ATOM 3240 CG2 THR A 413 29.756 87.369 232.383 1.00 47.54 C
ANISOU 3240 CG2 THR A 413 7392 6914 3758 345 -195 393 C
ATOM 3241 N PRO A 414 26.278 87.918 231.532 1.00 47.69 N
ANISOU 3241 N PRO A 414 7366 6919 3833 8 -230 465 N
ATOM 3242 CA PRO A 414 25.442 88.651 232.499 1.00 46.96 C
ANISOU 3242 CA PRO A 414 7183 6879 3781 -58 -211 525 C
ATOM 3243 C PRO A 414 26.237 88.991 233.746 1.00 46.03 C
ANISOU 3243 C PRO A 414 7031 6797 3663 25 -180 541 C
ATOM 3244 O PRO A 414 27.101 88.220 234.118 1.00 46.72 O
ANISOU 3244 O PRO A 414 7195 6834 3722 107 -187 527 O
ATOM 3245 CB PRO A 414 24.350 87.639 232.855 1.00 47.82 C
ANISOU 3245 CB PRO A 414 7373 6897 3897 -157 -235 566 C
ATOM 3246 CG PRO A 414 24.274 86.733 231.665 1.00 48.57 C
ANISOU 3246 CG PRO A 414 7574 6914 3966 -182 -277 523 C
ATOM 3247 CD PRO A 414 25.700 86.602 231.198 1.00 48.79 C
ANISOU 3247 CD PRO A 414 7641 6940 3957 -49 -269 462 C
ATOM 3248 N THR A 415 25.938 90.116 234.385 1.00 45.08 N
ANISOU 3248 N THR A 415 6799 6759 3569 4 -150 569 N
ATOM 3249 CA THR A 415 26.707 90.607 235.559 1.00 45.14 C
ANISOU 3249 CA THR A 415 6766 6815 3571 76 -124 578 C
ATOM 3250 C THR A 415 27.014 89.599 236.700 1.00 45.92 C
ANISOU 3250 C THR A 415 6957 6850 3643 115 -131 605 C
ATOM 3251 O THR A 415 26.184 88.736 237.026 1.00 46.59 O
ANISOU 3251 O THR A 415 7116 6859 3725 50 -141 644 O
ATOM 3252 CB THR A 415 26.040 91.867 236.198 1.00 44.16 C
ANISOU 3252 CB THR A 415 6528 6770 3479 29 -90 608 C
ATOM 3253 OG1 THR A 415 25.529 92.730 235.165 1.00 45.54 O
ANISOU 3253 OG1 THR A 415 6627 6992 3685 -18 -88 597 O
ATOM 3254 CG2 THR A 415 27.044 92.616 236.986 1.00 42.19 C
ANISOU 3254 CG2 THR A 415 6227 6583 3219 106 -69 593 C
ATOM 3255 N VAL A 416 28.214 89.705 237.286 1.00 46.12 N
ANISOU 3255 N VAL A 416 6975 6904 3644 218 -129 589 N
ATOM 3256 CA VAL A 416 28.554 89.014 238.545 1.00 46.77 C
ANISOU 3256 CA VAL A 416 7124 6948 3697 262 -135 623 C
ATOM 3257 C VAL A 416 29.043 90.070 239.529 1.00 46.90 C
ANISOU 3257 C VAL A 416 7051 7061 3709 297 -114 627 C
ATOM 3258 O VAL A 416 29.726 91.009 239.132 1.00 46.73 O
ANISOU 3258 O VAL A 416 6941 7116 3698 335 -106 588 O
ATOM 3259 CB VAL A 416 29.679 87.921 238.391 1.00 47.49 C
ANISOU 3259 CB VAL A 416 7313 6975 3758 373 -166 599 C
ATOM 3260 CG1 VAL A 416 29.944 87.216 239.727 1.00 46.88 C
ANISOU 3260 CG1 VAL A 416 7308 6856 3648 416 -179 646 C
ATOM 3261 CG2 VAL A 416 29.356 86.882 237.299 1.00 47.40 C
ANISOU 3261 CG2 VAL A 416 7403 6861 3745 351 -188 578 C
ATOM 3262 N TRP A 417 28.663 89.933 240.800 1.00 47.96 N
ANISOU 3262 N TRP A 417 7210 7190 3824 277 -104 675 N
ATOM 3263 CA TRP A 417 29.357 90.603 241.921 1.00 48.10 C
ANISOU 3263 CA TRP A 417 7180 7280 3814 330 -97 677 C
ATOM 3264 C TRP A 417 30.105 89.541 242.659 1.00 50.32 C
ANISOU 3264 C TRP A 417 7558 7512 4051 408 -130 700 C
ATOM 3265 O TRP A 417 29.553 88.455 242.896 1.00 51.32 O
ANISOU 3265 O TRP A 417 7789 7546 4163 380 -139 743 O
ATOM 3266 CB TRP A 417 28.402 91.203 242.958 1.00 47.00 C
ANISOU 3266 CB TRP A 417 7010 7176 3672 257 -59 717 C
ATOM 3267 CG TRP A 417 27.569 92.291 242.464 1.00 43.45 C
ANISOU 3267 CG TRP A 417 6465 6776 3267 186 -23 705 C
ATOM 3268 CD1 TRP A 417 27.681 93.617 242.766 1.00 38.28 C
ANISOU 3268 CD1 TRP A 417 5717 6204 2624 187 3 682 C
ATOM 3269 CD2 TRP A 417 26.474 92.161 241.552 1.00 40.23 C
ANISOU 3269 CD2 TRP A 417 6049 6336 2900 103 -15 716 C
ATOM 3270 NE1 TRP A 417 26.712 94.319 242.108 1.00 38.32 N
ANISOU 3270 NE1 TRP A 417 5657 6226 2677 118 31 681 N
ATOM 3271 CE2 TRP A 417 25.961 93.459 241.346 1.00 38.41 C
ANISOU 3271 CE2 TRP A 417 5712 6174 2707 66 18 703 C
ATOM 3272 CE3 TRP A 417 25.873 91.070 240.905 1.00 36.41 C
ANISOU 3272 CE3 TRP A 417 5640 5769 2425 56 -35 736 C
ATOM 3273 CZ2 TRP A 417 24.876 93.704 240.516 1.00 36.69 C
ANISOU 3273 CZ2 TRP A 417 5452 5954 2534 -10 29 714 C
ATOM 3274 CZ3 TRP A 417 24.806 91.301 240.099 1.00 37.73 C
ANISOU 3274 CZ3 TRP A 417 5766 5935 2633 -30 -27 743 C
ATOM 3275 CH2 TRP A 417 24.309 92.615 239.899 1.00 38.56 C
ANISOU 3275 CH2 TRP A 417 5755 6119 2775 -60 3 734 C
ATOM 3276 N TYR A 418 31.334 89.844 243.068 1.00 51.67 N
ANISOU 3276 N TYR A 418 7693 7741 4198 503 -151 676 N
ATOM 3277 CA TYR A 418 31.978 88.939 244.002 1.00 53.81 C
ANISOU 3277 CA TYR A 418 8049 7977 4422 579 -185 710 C
ATOM 3278 C TYR A 418 33.056 89.518 244.855 1.00 54.22 C
ANISOU 3278 C TYR A 418 8043 8118 4441 654 -206 698 C
ATOM 3279 O TYR A 418 33.639 90.517 244.483 1.00 53.86 O
ANISOU 3279 O TYR A 418 7891 8157 4414 669 -201 651 O
ATOM 3280 CB TYR A 418 32.484 87.677 243.313 1.00 55.00 C
ANISOU 3280 CB TYR A 418 8294 8034 4571 651 -217 703 C
ATOM 3281 CG TYR A 418 33.204 87.809 241.982 1.00 55.76 C
ANISOU 3281 CG TYR A 418 8342 8147 4696 706 -221 639 C
ATOM 3282 CD1 TYR A 418 33.712 89.027 241.534 1.00 54.96 C
ANISOU 3282 CD1 TYR A 418 8110 8155 4617 711 -205 592 C
ATOM 3283 CD2 TYR A 418 33.414 86.659 241.196 1.00 56.51 C
ANISOU 3283 CD2 TYR A 418 8536 8144 4793 756 -240 626 C
ATOM 3284 CE1 TYR A 418 34.379 89.092 240.326 1.00 56.66 C
ANISOU 3284 CE1 TYR A 418 8288 8388 4852 760 -203 539 C
ATOM 3285 CE2 TYR A 418 34.059 86.713 240.008 1.00 57.73 C
ANISOU 3285 CE2 TYR A 418 8657 8314 4964 810 -237 567 C
ATOM 3286 CZ TYR A 418 34.544 87.924 239.578 1.00 58.27 C
ANISOU 3286 CZ TYR A 418 8590 8499 5051 811 -217 526 C
ATOM 3287 OH TYR A 418 35.216 87.945 238.399 1.00 61.05 O
ANISOU 3287 OH TYR A 418 8912 8872 5414 866 -209 472 O
ATOM 3288 N ASP A 419 33.287 88.887 246.007 1.00 55.57 N
ANISOU 3288 N ASP A 419 8288 8268 4559 694 -233 746 N
ATOM 3289 CA ASP A 419 34.356 89.281 246.923 1.00 56.81 C
ANISOU 3289 CA ASP A 419 8403 8508 4674 770 -267 741 C
ATOM 3290 C ASP A 419 35.692 88.751 246.413 1.00 57.96 C
ANISOU 3290 C ASP A 419 8539 8659 4824 897 -314 715 C
ATOM 3291 O ASP A 419 35.726 87.752 245.691 1.00 59.29 O
ANISOU 3291 O ASP A 419 8780 8738 5008 938 -322 717 O
ATOM 3292 CB ASP A 419 34.075 88.768 248.340 1.00 57.39 C
ANISOU 3292 CB ASP A 419 8565 8559 4680 767 -281 808 C
ATOM 3293 CG ASP A 419 32.962 89.553 249.049 1.00 57.09 C
ANISOU 3293 CG ASP A 419 8509 8555 4628 656 -229 826 C
ATOM 3294 OD1 ASP A 419 32.818 90.780 248.792 1.00 56.38 O
ANISOU 3294 OD1 ASP A 419 8315 8540 4567 611 -199 779 O
ATOM 3295 OD2 ASP A 419 32.241 88.945 249.878 1.00 56.52 O
ANISOU 3295 OD2 ASP A 419 8528 8433 4513 617 -216 888 O
ATOM 3296 N GLU A 420 36.780 89.445 246.734 1.00 58.39 N
ANISOU 3296 N GLU A 420 8500 8819 4866 956 -342 685 N
ATOM 3297 CA GLU A 420 38.126 88.971 246.398 1.00 59.78 C
ANISOU 3297 CA GLU A 420 8650 9020 5045 1086 -387 665 C
ATOM 3298 C GLU A 420 39.111 89.404 247.465 1.00 60.47 C
ANISOU 3298 C GLU A 420 8679 9209 5089 1143 -437 670 C
ATOM 3299 O GLU A 420 39.169 90.596 247.781 1.00 60.28 O
ANISOU 3299 O GLU A 420 8562 9278 5063 1084 -428 641 O
ATOM 3300 CB GLU A 420 38.591 89.481 245.022 1.00 59.40 C
ANISOU 3300 CB GLU A 420 8506 9012 5052 1097 -362 600 C
ATOM 3301 CG GLU A 420 40.120 89.322 244.798 1.00 61.20 C
ANISOU 3301 CG GLU A 420 8662 9310 5281 1228 -401 572 C
ATOM 3302 CD GLU A 420 40.613 89.779 243.421 1.00 62.24 C
ANISOU 3302 CD GLU A 420 8701 9487 5461 1241 -368 512 C
ATOM 3303 OE1 GLU A 420 39.793 89.839 242.464 1.00 61.16 O
ANISOU 3303 OE1 GLU A 420 8590 9295 5353 1172 -323 494 O
ATOM 3304 OE2 GLU A 420 41.837 90.059 243.312 1.00 62.56 O
ANISOU 3304 OE2 GLU A 420 8640 9622 5507 1320 -389 485 O
ATOM 3305 N ASP A 421 39.873 88.453 248.016 1.00 61.43 N
ANISOU 3305 N ASP A 421 8856 9311 5174 1256 -493 706 N
ATOM 3306 CA ASP A 421 40.865 88.779 249.031 1.00 62.21 C
ANISOU 3306 CA ASP A 421 8898 9512 5227 1316 -554 715 C
ATOM 3307 C ASP A 421 42.007 89.546 248.402 1.00 62.31 C
ANISOU 3307 C ASP A 421 8757 9641 5277 1361 -567 654 C
ATOM 3308 O ASP A 421 42.701 89.018 247.536 1.00 63.12 O
ANISOU 3308 O ASP A 421 8834 9734 5414 1452 -570 634 O
ATOM 3309 CB ASP A 421 41.402 87.522 249.719 1.00 63.81 C
ANISOU 3309 CB ASP A 421 9200 9663 5384 1436 -616 776 C
ATOM 3310 CG ASP A 421 42.225 87.838 250.975 1.00 64.91 C
ANISOU 3310 CG ASP A 421 9297 9906 5459 1482 -687 798 C
ATOM 3311 OD1 ASP A 421 41.636 88.385 251.941 1.00 65.79 O
ANISOU 3311 OD1 ASP A 421 9433 10045 5519 1396 -683 818 O
ATOM 3312 OD2 ASP A 421 43.446 87.537 251.002 1.00 64.30 O
ANISOU 3312 OD2 ASP A 421 9164 9887 5381 1606 -747 796 O
ATOM 3313 N VAL A 422 42.177 90.796 248.839 1.00 62.24 N
ANISOU 3313 N VAL A 422 8650 9739 5261 1291 -569 623 N
ATOM 3314 CA VAL A 422 43.277 91.685 248.428 1.00 62.75 C
ANISOU 3314 CA VAL A 422 8558 9928 5355 1310 -585 569 C
ATOM 3315 C VAL A 422 44.651 90.976 248.433 1.00 64.83 C
ANISOU 3315 C VAL A 422 8774 10243 5614 1459 -648 577 C
ATOM 3316 O VAL A 422 45.487 91.201 247.553 1.00 64.99 O
ANISOU 3316 O VAL A 422 8686 10326 5680 1505 -640 537 O
ATOM 3317 CB VAL A 422 43.334 92.949 249.345 1.00 62.29 C
ANISOU 3317 CB VAL A 422 8434 9967 5265 1224 -603 549 C
ATOM 3318 CG1 VAL A 422 44.619 93.755 249.137 1.00 61.67 C
ANISOU 3318 CG1 VAL A 422 8200 10023 5210 1246 -638 502 C
ATOM 3319 CG2 VAL A 422 42.126 93.824 249.122 1.00 60.62 C
ANISOU 3319 CG2 VAL A 422 8238 9720 5075 1090 -533 527 C
ATOM 3320 N LEU A 423 44.876 90.118 249.424 1.00 66.59 N
ANISOU 3320 N LEU A 423 9078 10442 5781 1537 -709 633 N
ATOM 3321 CA LEU A 423 46.128 89.397 249.504 1.00 68.60 C
ANISOU 3321 CA LEU A 423 9292 10741 6031 1690 -773 649 C
ATOM 3322 C LEU A 423 46.106 88.124 248.643 1.00 69.32 C
ANISOU 3322 C LEU A 423 9468 10717 6153 1795 -751 663 C
ATOM 3323 O LEU A 423 46.921 87.973 247.720 1.00 69.57 O
ANISOU 3323 O LEU A 423 9417 10785 6230 1880 -740 627 O
ATOM 3324 CB LEU A 423 46.453 89.064 250.959 1.00 69.80 C
ANISOU 3324 CB LEU A 423 9492 10924 6105 1736 -858 706 C
ATOM 3325 CG LEU A 423 47.926 89.284 251.312 1.00 71.90 C
ANISOU 3325 CG LEU A 423 9621 11335 6363 1831 -939 697 C
ATOM 3326 CD1 LEU A 423 48.081 90.674 251.937 1.00 70.71 C
ANISOU 3326 CD1 LEU A 423 9370 11310 6189 1715 -960 660 C
ATOM 3327 CD2 LEU A 423 48.502 88.152 252.229 1.00 74.05 C
ANISOU 3327 CD2 LEU A 423 9967 11591 6578 1973 -1027 771 C
ATOM 3328 N SER A 424 45.151 87.235 248.942 1.00 69.47 N
ANISOU 3328 N SER A 424 9653 10596 6145 1783 -740 713 N
ATOM 3329 CA SER A 424 45.145 85.862 248.430 1.00 69.90 C
ANISOU 3329 CA SER A 424 9823 10522 6213 1890 -737 738 C
ATOM 3330 C SER A 424 44.928 85.770 246.926 1.00 69.40 C
ANISOU 3330 C SER A 424 9748 10406 6213 1882 -668 681 C
ATOM 3331 O SER A 424 45.500 84.888 246.277 1.00 70.12 O
ANISOU 3331 O SER A 424 9868 10449 6326 2008 -670 672 O
ATOM 3332 CB SER A 424 44.123 84.998 249.191 1.00 70.17 C
ANISOU 3332 CB SER A 424 10042 10418 6200 1856 -743 810 C
ATOM 3333 OG SER A 424 42.842 84.995 248.589 1.00 68.99 O
ANISOU 3333 OG SER A 424 9970 10168 6076 1735 -673 799 O
ATOM 3334 N GLY A 425 44.110 86.686 246.396 1.00 67.95 N
ANISOU 3334 N GLY A 425 9528 10236 6055 1740 -608 644 N
ATOM 3335 CA GLY A 425 43.695 86.676 244.992 1.00 67.08 C
ANISOU 3335 CA GLY A 425 9419 10073 5994 1706 -542 594 C
ATOM 3336 C GLY A 425 42.394 85.940 244.685 1.00 66.66 C
ANISOU 3336 C GLY A 425 9524 9862 5941 1637 -508 616 C
ATOM 3337 O GLY A 425 41.786 86.180 243.635 1.00 65.93 O
ANISOU 3337 O GLY A 425 9430 9737 5882 1565 -455 578 O
ATOM 3338 N GLU A 426 41.959 85.061 245.597 1.00 67.19 N
ANISOU 3338 N GLU A 426 9725 9835 5969 1651 -540 682 N
ATOM 3339 CA GLU A 426 40.787 84.168 245.370 1.00 67.39 C
ANISOU 3339 CA GLU A 426 9912 9699 5994 1590 -516 712 C
ATOM 3340 C GLU A 426 39.416 84.883 245.296 1.00 65.25 C
ANISOU 3340 C GLU A 426 9643 9416 5733 1413 -466 712 C
ATOM 3341 O GLU A 426 39.113 85.763 246.108 1.00 64.98 O
ANISOU 3341 O GLU A 426 9552 9460 5679 1336 -463 727 O
ATOM 3342 CB GLU A 426 40.763 82.982 246.380 1.00 69.21 C
ANISOU 3342 CB GLU A 426 10291 9827 6178 1658 -564 790 C
ATOM 3343 CG GLU A 426 40.127 83.271 247.772 1.00 70.40 C
ANISOU 3343 CG GLU A 426 10478 9996 6275 1572 -580 856 C
ATOM 3344 CD GLU A 426 40.735 82.443 248.932 1.00 74.00 C
ANISOU 3344 CD GLU A 426 11016 10426 6673 1682 -649 929 C
ATOM 3345 OE1 GLU A 426 41.987 82.303 249.011 1.00 74.00 O
ANISOU 3345 OE1 GLU A 426 10956 10490 6670 1824 -699 920 O
ATOM 3346 OE2 GLU A 426 39.949 81.955 249.788 1.00 74.86 O
ANISOU 3346 OE2 GLU A 426 11247 10458 6737 1623 -653 1000 O
ATOM 3347 N ARG A 427 38.592 84.459 244.343 1.00 63.54 N
ANISOU 3347 N ARG A 427 9497 9100 5546 1353 -428 695 N
ATOM 3348 CA ARG A 427 37.350 85.146 244.001 1.00 61.18 C
ANISOU 3348 CA ARG A 427 9179 8798 5268 1196 -381 686 C
ATOM 3349 C ARG A 427 36.105 84.283 244.254 1.00 60.86 C
ANISOU 3349 C ARG A 427 9284 8623 5218 1110 -371 740 C
ATOM 3350 O ARG A 427 35.797 83.371 243.469 1.00 61.45 O
ANISOU 3350 O ARG A 427 9457 8583 5308 1113 -369 731 O
ATOM 3351 CB ARG A 427 37.399 85.515 242.514 1.00 60.47 C
ANISOU 3351 CB ARG A 427 9028 8725 5223 1182 -346 617 C
ATOM 3352 CG ARG A 427 36.988 86.917 242.190 1.00 58.38 C
ANISOU 3352 CG ARG A 427 8637 8561 4983 1079 -309 586 C
ATOM 3353 CD ARG A 427 37.399 87.272 240.798 1.00 57.08 C
ANISOU 3353 CD ARG A 427 8405 8431 4851 1098 -283 522 C
ATOM 3354 NE ARG A 427 38.776 87.719 240.771 1.00 59.73 N
ANISOU 3354 NE ARG A 427 8633 8875 5188 1199 -295 490 N
ATOM 3355 CZ ARG A 427 39.357 88.320 239.742 1.00 61.19 C
ANISOU 3355 CZ ARG A 427 8722 9131 5396 1216 -269 436 C
ATOM 3356 NH1 ARG A 427 38.675 88.565 238.619 1.00 60.84 N
ANISOU 3356 NH1 ARG A 427 8683 9062 5373 1142 -231 407 N
ATOM 3357 NH2 ARG A 427 40.634 88.673 239.847 1.00 62.27 N
ANISOU 3357 NH2 ARG A 427 8756 9372 5533 1306 -282 415 N
ATOM 3358 N LYS A 428 35.376 84.568 245.322 1.00 59.28 N
ANISOU 3358 N LYS A 428 9097 8436 4989 1027 -364 793 N
ATOM 3359 CA LYS A 428 34.082 83.928 245.516 1.00 59.04 C
ANISOU 3359 CA LYS A 428 9180 8298 4956 919 -344 845 C
ATOM 3360 C LYS A 428 32.977 84.775 244.858 1.00 56.98 C
ANISOU 3360 C LYS A 428 8846 8069 4735 781 -294 818 C
ATOM 3361 O LYS A 428 32.967 85.999 245.042 1.00 55.67 O
ANISOU 3361 O LYS A 428 8558 8016 4576 746 -271 795 O
ATOM 3362 CB LYS A 428 33.791 83.745 247.016 1.00 60.25 C
ANISOU 3362 CB LYS A 428 9390 8451 5052 898 -354 922 C
ATOM 3363 CG LYS A 428 34.832 82.883 247.788 1.00 63.81 C
ANISOU 3363 CG LYS A 428 9920 8869 5455 1035 -413 962 C
ATOM 3364 CD LYS A 428 34.622 82.847 249.327 1.00 65.57 C
ANISOU 3364 CD LYS A 428 10192 9114 5609 1015 -425 1040 C
ATOM 3365 CE LYS A 428 35.606 81.833 249.993 1.00 68.52 C
ANISOU 3365 CE LYS A 428 10662 9436 5936 1157 -492 1089 C
ATOM 3366 NZ LYS A 428 35.250 81.412 251.414 1.00 68.98 N
ANISOU 3366 NZ LYS A 428 10822 9471 5918 1133 -506 1183 N
ATOM 3367 N VAL A 429 32.075 84.138 244.086 1.00 55.75 N
ANISOU 3367 N VAL A 429 8765 7812 4606 704 -280 821 N
ATOM 3368 CA VAL A 429 30.801 84.775 243.659 1.00 53.57 C
ANISOU 3368 CA VAL A 429 8435 7555 4364 560 -238 819 C
ATOM 3369 C VAL A 429 29.919 85.074 244.870 1.00 53.59 C
ANISOU 3369 C VAL A 429 8436 7584 4343 473 -210 882 C
ATOM 3370 O VAL A 429 29.735 84.216 245.740 1.00 54.34 O
ANISOU 3370 O VAL A 429 8637 7609 4400 471 -221 946 O
ATOM 3371 CB VAL A 429 29.960 83.920 242.676 1.00 53.39 C
ANISOU 3371 CB VAL A 429 8501 7415 4369 486 -239 816 C
ATOM 3372 CG1 VAL A 429 28.606 84.544 242.446 1.00 51.33 C
ANISOU 3372 CG1 VAL A 429 8179 7185 4140 338 -202 828 C
ATOM 3373 CG2 VAL A 429 30.642 83.798 241.370 1.00 52.87 C
ANISOU 3373 CG2 VAL A 429 8429 7337 4324 553 -254 744 C
ATOM 3374 N VAL A 430 29.398 86.299 244.926 1.00 52.32 N
ANISOU 3374 N VAL A 430 8155 7523 4201 406 -171 867 N
ATOM 3375 CA VAL A 430 28.396 86.682 245.913 1.00 51.68 C
ANISOU 3375 CA VAL A 430 8060 7473 4104 314 -131 918 C
ATOM 3376 C VAL A 430 27.021 86.564 245.252 1.00 51.03 C
ANISOU 3376 C VAL A 430 7975 7350 4067 186 -100 933 C
ATOM 3377 O VAL A 430 26.135 85.885 245.761 1.00 51.46 O
ANISOU 3377 O VAL A 430 8100 7345 4109 108 -84 995 O
ATOM 3378 CB VAL A 430 28.628 88.112 246.451 1.00 50.92 C
ANISOU 3378 CB VAL A 430 7840 7507 4001 323 -104 890 C
ATOM 3379 CG1 VAL A 430 27.545 88.479 247.463 1.00 51.82 C
ANISOU 3379 CG1 VAL A 430 7945 7652 4094 234 -53 939 C
ATOM 3380 CG2 VAL A 430 29.982 88.222 247.101 1.00 51.13 C
ANISOU 3380 CG2 VAL A 430 7864 7580 3982 438 -143 875 C
ATOM 3381 N LYS A 431 26.860 87.222 244.110 1.00 49.68 N
ANISOU 3381 N LYS A 431 7718 7213 3945 163 -94 881 N
ATOM 3382 CA LYS A 431 25.649 87.103 243.325 1.00 49.41 C
ANISOU 3382 CA LYS A 431 7673 7145 3954 49 -79 890 C
ATOM 3383 C LYS A 431 26.008 87.095 241.869 1.00 49.14 C
ANISOU 3383 C LYS A 431 7625 7093 3952 72 -108 829 C
ATOM 3384 O LYS A 431 26.752 87.965 241.420 1.00 49.10 O
ANISOU 3384 O LYS A 431 7537 7162 3957 134 -107 777 O
ATOM 3385 CB LYS A 431 24.705 88.285 243.557 1.00 48.45 C
ANISOU 3385 CB LYS A 431 7431 7117 3861 -28 -29 898 C
ATOM 3386 CG LYS A 431 23.458 88.175 242.699 1.00 48.74 C
ANISOU 3386 CG LYS A 431 7443 7131 3947 -142 -21 911 C
ATOM 3387 CD LYS A 431 22.511 89.363 242.802 1.00 49.22 C
ANISOU 3387 CD LYS A 431 7373 7284 4044 -205 28 918 C
ATOM 3388 CE LYS A 431 21.217 89.096 242.007 1.00 49.08 C
ANISOU 3388 CE LYS A 431 7332 7244 4074 -323 27 941 C
ATOM 3389 NZ LYS A 431 20.490 87.912 242.572 1.00 52.20 N
ANISOU 3389 NZ LYS A 431 7819 7561 4452 -405 30 1006 N
ATOM 3390 N ALA A 432 25.469 86.125 241.127 1.00 49.56 N
ANISOU 3390 N ALA A 432 7763 7050 4019 15 -131 835 N
ATOM 3391 CA ALA A 432 25.481 86.165 239.645 1.00 48.37 C
ANISOU 3391 CA ALA A 432 7597 6886 3895 5 -152 778 C
ATOM 3392 C ALA A 432 24.068 86.413 239.138 1.00 47.61 C
ANISOU 3392 C ALA A 432 7452 6800 3839 -132 -142 799 C
ATOM 3393 O ALA A 432 23.101 85.822 239.632 1.00 48.14 O
ANISOU 3393 O ALA A 432 7563 6819 3910 -227 -135 855 O
ATOM 3394 CB ALA A 432 26.066 84.881 239.046 1.00 48.72 C
ANISOU 3394 CB ALA A 432 7780 6812 3920 57 -194 754 C
ATOM 3395 N ARG A 433 23.946 87.308 238.170 1.00 46.13 N
ANISOU 3395 N ARG A 433 7168 6680 3679 -145 -140 759 N
ATOM 3396 CA ARG A 433 22.640 87.646 237.656 1.00 45.55 C
ANISOU 3396 CA ARG A 433 7032 6631 3645 -265 -136 780 C
ATOM 3397 C ARG A 433 22.137 86.495 236.784 1.00 46.39 C
ANISOU 3397 C ARG A 433 7241 6634 3750 -337 -181 775 C
ATOM 3398 O ARG A 433 22.900 85.942 236.002 1.00 46.29 O
ANISOU 3398 O ARG A 433 7307 6565 3715 -279 -213 724 O
ATOM 3399 CB ARG A 433 22.698 88.962 236.890 1.00 44.08 C
ANISOU 3399 CB ARG A 433 6720 6544 3486 -250 -125 744 C
ATOM 3400 CG ARG A 433 21.347 89.524 236.556 1.00 43.96 C
ANISOU 3400 CG ARG A 433 6614 6575 3514 -358 -117 775 C
ATOM 3401 CD ARG A 433 21.401 90.234 235.237 1.00 44.17 C
ANISOU 3401 CD ARG A 433 6579 6646 3557 -355 -138 734 C
ATOM 3402 NE ARG A 433 20.116 90.738 234.740 1.00 44.74 N
ANISOU 3402 NE ARG A 433 6564 6763 3671 -454 -143 763 N
ATOM 3403 CZ ARG A 433 20.016 91.892 234.075 1.00 45.59 C
ANISOU 3403 CZ ARG A 433 6570 6948 3804 -442 -139 750 C
ATOM 3404 NH1 ARG A 433 21.099 92.627 233.871 1.00 44.35 N
ANISOU 3404 NH1 ARG A 433 6390 6827 3633 -349 -126 709 N
ATOM 3405 NH2 ARG A 433 18.854 92.337 233.622 1.00 47.30 N
ANISOU 3405 NH2 ARG A 433 6705 7207 4061 -522 -149 781 N
ATOM 3406 N LYS A 434 20.864 86.120 236.972 1.00 47.65 N
ANISOU 3406 N LYS A 434 7402 6770 3933 -465 -181 826 N
ATOM 3407 CA LYS A 434 20.120 85.168 236.106 1.00 48.61 C
ANISOU 3407 CA LYS A 434 7601 6806 4061 -569 -228 825 C
ATOM 3408 C LYS A 434 19.270 85.905 235.034 1.00 47.99 C
ANISOU 3408 C LYS A 434 7415 6799 4018 -648 -247 811 C
ATOM 3409 O LYS A 434 18.557 86.868 235.346 1.00 47.48 O
ANISOU 3409 O LYS A 434 7218 6833 3990 -686 -215 845 O
ATOM 3410 CB LYS A 434 19.196 84.286 236.956 1.00 49.97 C
ANISOU 3410 CB LYS A 434 7834 6912 4240 -677 -221 896 C
ATOM 3411 CG LYS A 434 19.880 83.496 238.093 1.00 53.12 C
ANISOU 3411 CG LYS A 434 8348 7235 4601 -613 -206 926 C
ATOM 3412 CD LYS A 434 18.865 83.119 239.202 1.00 58.64 C
ANISOU 3412 CD LYS A 434 9051 7923 5308 -721 -173 1014 C
ATOM 3413 CE LYS A 434 19.542 82.595 240.498 1.00 60.83 C
ANISOU 3413 CE LYS A 434 9421 8152 5540 -649 -150 1055 C
ATOM 3414 NZ LYS A 434 18.749 82.903 241.739 1.00 61.18 N
ANISOU 3414 NZ LYS A 434 9405 8257 5583 -715 -90 1132 N
ATOM 3415 N VAL A 435 19.362 85.463 233.776 1.00 47.84 N
ANISOU 3415 N VAL A 435 7458 6734 3987 -666 -298 761 N
ATOM 3416 CA VAL A 435 18.518 85.989 232.685 1.00 47.51 C
ANISOU 3416 CA VAL A 435 7334 6749 3969 -749 -330 752 C
ATOM 3417 C VAL A 435 17.660 84.881 232.068 1.00 48.79 C
ANISOU 3417 C VAL A 435 7587 6822 4130 -880 -389 756 C
ATOM 3418 O VAL A 435 18.187 83.901 231.538 1.00 49.66 O
ANISOU 3418 O VAL A 435 7842 6826 4201 -863 -425 710 O
ATOM 3419 CB VAL A 435 19.338 86.644 231.551 1.00 46.67 C
ANISOU 3419 CB VAL A 435 7205 6688 3840 -665 -345 685 C
ATOM 3420 CG1 VAL A 435 18.443 87.487 230.658 1.00 45.06 C
ANISOU 3420 CG1 VAL A 435 6888 6571 3664 -739 -369 694 C
ATOM 3421 CG2 VAL A 435 20.459 87.488 232.111 1.00 46.47 C
ANISOU 3421 CG2 VAL A 435 7126 6723 3807 -530 -295 669 C
ATOM 3422 N GLY A 436 16.341 85.044 232.130 1.00 49.11 N
ANISOU 3422 N GLY A 436 7542 6907 4212 -1010 -398 810 N
ATOM 3423 CA GLY A 436 15.423 84.034 231.627 1.00 50.22 C
ANISOU 3423 CA GLY A 436 7753 6971 4356 -1156 -457 821 C
ATOM 3424 C GLY A 436 15.144 84.242 230.146 1.00 50.74 C
ANISOU 3424 C GLY A 436 7803 7064 4411 -1199 -523 774 C
ATOM 3425 O GLY A 436 16.039 84.652 229.379 1.00 49.92 O
ANISOU 3425 O GLY A 436 7718 6978 4273 -1097 -529 712 O
ATOM 3426 N GLY A 437 13.901 83.951 229.744 1.00 51.28 N
ANISOU 3426 N GLY A 437 7837 7142 4507 -1353 -572 805 N
ATOM 3427 CA GLY A 437 13.474 84.093 228.363 1.00 51.22 C
ANISOU 3427 CA GLY A 437 7813 7164 4485 -1415 -646 769 C
ATOM 3428 C GLY A 437 14.300 83.234 227.424 1.00 51.77 C
ANISOU 3428 C GLY A 437 8061 7121 4486 -1380 -693 683 C
ATOM 3429 O GLY A 437 14.352 83.507 226.210 1.00 51.33 O
ANISOU 3429 O GLY A 437 8007 7097 4397 -1382 -742 634 O
ATOM 3430 N GLY A 438 14.963 82.222 228.001 1.00 51.93 N
ANISOU 3430 N GLY A 438 8233 7014 4483 -1341 -674 666 N
ATOM 3431 CA GLY A 438 15.785 81.275 227.252 1.00 52.34 C
ANISOU 3431 CA GLY A 438 8474 6942 4473 -1294 -709 583 C
ATOM 3432 C GLY A 438 17.118 81.785 226.742 1.00 51.32 C
ANISOU 3432 C GLY A 438 8362 6840 4298 -1123 -680 515 C
ATOM 3433 O GLY A 438 17.736 81.164 225.888 1.00 52.00 O
ANISOU 3433 O GLY A 438 8582 6848 4327 -1082 -708 439 O
ATOM 3434 N PHE A 439 17.565 82.914 227.275 1.00 50.19 N
ANISOU 3434 N PHE A 439 8085 6808 4178 -1024 -619 541 N
ATOM 3435 CA PHE A 439 18.859 83.525 226.935 1.00 49.29 C
ANISOU 3435 CA PHE A 439 7962 6737 4030 -863 -582 487 C
ATOM 3436 C PHE A 439 20.064 82.559 227.106 1.00 49.89 C
ANISOU 3436 C PHE A 439 8199 6695 4062 -748 -565 434 C
ATOM 3437 O PHE A 439 20.050 81.732 228.027 1.00 50.83 O
ANISOU 3437 O PHE A 439 8398 6721 4193 -756 -556 464 O
ATOM 3438 CB PHE A 439 19.028 84.779 227.825 1.00 47.76 C
ANISOU 3438 CB PHE A 439 7604 6663 3879 -797 -518 538 C
ATOM 3439 CG PHE A 439 20.417 85.322 227.869 1.00 45.24 C
ANISOU 3439 CG PHE A 439 7275 6380 3535 -637 -471 497 C
ATOM 3440 CD1 PHE A 439 20.881 86.176 226.870 1.00 45.19 C
ANISOU 3440 CD1 PHE A 439 7211 6455 3505 -585 -470 458 C
ATOM 3441 CD2 PHE A 439 21.274 84.971 228.895 1.00 43.76 C
ANISOU 3441 CD2 PHE A 439 7133 6149 3345 -540 -430 502 C
ATOM 3442 CE1 PHE A 439 22.195 86.683 226.906 1.00 42.95 C
ANISOU 3442 CE1 PHE A 439 6908 6210 3199 -444 -423 422 C
ATOM 3443 CE2 PHE A 439 22.585 85.465 228.933 1.00 42.02 C
ANISOU 3443 CE2 PHE A 439 6892 5970 3103 -395 -390 465 C
ATOM 3444 CZ PHE A 439 23.037 86.329 227.936 1.00 41.42 C
ANISOU 3444 CZ PHE A 439 6751 5978 3009 -351 -385 425 C
ATOM 3445 N GLU A 440 21.081 82.650 226.232 1.00 49.34 N
ANISOU 3445 N GLU A 440 8175 6631 3941 -640 -559 360 N
ATOM 3446 CA GLU A 440 22.422 82.097 226.540 1.00 49.51 C
ANISOU 3446 CA GLU A 440 8295 6585 3932 -488 -523 316 C
ATOM 3447 C GLU A 440 23.632 82.777 225.901 1.00 48.59 C
ANISOU 3447 C GLU A 440 8137 6546 3779 -347 -486 259 C
ATOM 3448 O GLU A 440 23.645 83.000 224.722 1.00 49.07 O
ANISOU 3448 O GLU A 440 8204 6638 3801 -359 -504 211 O
ATOM 3449 CB GLU A 440 22.525 80.575 226.361 1.00 51.05 C
ANISOU 3449 CB GLU A 440 8694 6608 4094 -498 -557 275 C
ATOM 3450 CG GLU A 440 21.369 79.863 225.681 1.00 54.40 C
ANISOU 3450 CG GLU A 440 9203 6957 4510 -663 -626 267 C
ATOM 3451 CD GLU A 440 21.502 78.316 225.710 1.00 58.24 C
ANISOU 3451 CD GLU A 440 9908 7252 4970 -672 -656 232 C
ATOM 3452 OE1 GLU A 440 22.117 77.750 226.664 1.00 57.69 O
ANISOU 3452 OE1 GLU A 440 9906 7103 4911 -586 -625 253 O
ATOM 3453 OE2 GLU A 440 20.979 77.677 224.759 1.00 59.69 O
ANISOU 3453 OE2 GLU A 440 10197 7362 5119 -767 -714 184 O
ATOM 3454 N SER A 441 24.664 83.067 226.700 1.00 48.18 N
ANISOU 3454 N SER A 441 8045 6524 3738 -217 -434 267 N
ATOM 3455 CA SER A 441 25.908 83.704 226.231 1.00 47.24 C
ANISOU 3455 CA SER A 441 7875 6485 3591 -81 -392 219 C
ATOM 3456 C SER A 441 26.430 83.161 224.909 1.00 48.20 C
ANISOU 3456 C SER A 441 8104 6565 3646 -36 -403 133 C
ATOM 3457 O SER A 441 26.888 83.928 224.057 1.00 47.73 O
ANISOU 3457 O SER A 441 7979 6598 3558 3 -382 100 O
ATOM 3458 CB SER A 441 27.017 83.562 227.273 1.00 46.83 C
ANISOU 3458 CB SER A 441 7820 6425 3549 55 -351 227 C
ATOM 3459 OG SER A 441 26.687 84.261 228.455 1.00 46.09 O
ANISOU 3459 OG SER A 441 7615 6393 3503 28 -333 299 O
ATOM 3460 N LYS A 442 26.378 81.838 224.746 1.00 54.05 N
ANISOU 3460 N LYS A 442 9466 6775 4295 -17 -175 329 N
ATOM 3461 CA LYS A 442 26.995 81.193 223.586 1.00 54.35 C
ANISOU 3461 CA LYS A 442 9539 6739 4372 66 -156 279 C
ATOM 3462 C LYS A 442 26.291 81.573 222.290 1.00 53.32 C
ANISOU 3462 C LYS A 442 9336 6679 4244 -25 -94 219 C
ATOM 3463 O LYS A 442 26.812 81.331 221.193 1.00 53.79 O
ANISOU 3463 O LYS A 442 9391 6711 4335 40 -68 167 O
ATOM 3464 CB LYS A 442 27.105 79.663 223.764 1.00 56.17 C
ANISOU 3464 CB LYS A 442 9990 6783 4571 87 -169 297 C
ATOM 3465 CG LYS A 442 25.814 78.926 224.193 1.00 57.37 C
ANISOU 3465 CG LYS A 442 10295 6864 4638 -86 -151 325 C
ATOM 3466 CD LYS A 442 26.021 77.407 224.168 1.00 60.11 C
ANISOU 3466 CD LYS A 442 10865 7012 4960 -56 -158 334 C
ATOM 3467 CE LYS A 442 24.733 76.624 223.919 1.00 60.21 C
ANISOU 3467 CE LYS A 442 11018 6954 4904 -242 -116 326 C
ATOM 3468 NZ LYS A 442 24.932 75.648 222.789 1.00 61.69 N
ANISOU 3468 NZ LYS A 442 11324 7016 5100 -218 -86 266 N
ATOM 3469 N ASN A 443 25.114 82.175 222.420 1.00 51.96 N
ANISOU 3469 N ASN A 443 9108 6598 4038 -173 -72 228 N
ATOM 3470 CA ASN A 443 24.394 82.693 221.265 1.00 51.20 C
ANISOU 3470 CA ASN A 443 8922 6589 3944 -262 -27 181 C
ATOM 3471 C ASN A 443 24.933 84.044 220.782 1.00 50.07 C
ANISOU 3471 C ASN A 443 8581 6584 3860 -191 -20 159 C
ATOM 3472 O ASN A 443 24.567 84.528 219.715 1.00 49.95 O
ANISOU 3472 O ASN A 443 8487 6639 3852 -236 11 121 O
ATOM 3473 CB ASN A 443 22.915 82.826 221.582 1.00 50.79 C
ANISOU 3473 CB ASN A 443 8870 6584 3842 -441 -7 202 C
ATOM 3474 CG ASN A 443 22.293 81.528 222.044 1.00 51.86 C
ANISOU 3474 CG ASN A 443 9199 6588 3916 -534 -7 225 C
ATOM 3475 OD1 ASN A 443 22.805 80.433 221.777 1.00 52.47 O
ANISOU 3475 OD1 ASN A 443 9425 6527 3984 -482 -15 212 O
ATOM 3476 ND2 ASN A 443 21.158 81.644 222.733 1.00 50.72 N
ANISOU 3476 ND2 ASN A 443 9056 6482 3733 -675 8 259 N
ATOM 3477 N TYR A 444 25.813 84.647 221.561 1.00 49.55 N
ANISOU 3477 N TYR A 444 8440 6554 3833 -86 -54 184 N
ATOM 3478 CA TYR A 444 26.294 85.959 221.238 1.00 48.72 C
ANISOU 3478 CA TYR A 444 8154 6575 3782 -32 -48 169 C
ATOM 3479 C TYR A 444 27.819 86.031 221.199 1.00 49.70 C
ANISOU 3479 C TYR A 444 8231 6682 3969 136 -73 159 C
ATOM 3480 O TYR A 444 28.500 85.240 221.849 1.00 50.94 O
ANISOU 3480 O TYR A 444 8481 6744 4129 219 -113 182 O
ATOM 3481 CB TYR A 444 25.725 86.925 222.252 1.00 47.55 C
ANISOU 3481 CB TYR A 444 7924 6518 3624 -94 -60 206 C
ATOM 3482 CG TYR A 444 24.243 86.735 222.449 1.00 47.64 C
ANISOU 3482 CG TYR A 444 7984 6539 3580 -253 -32 221 C
ATOM 3483 CD1 TYR A 444 23.342 87.051 221.439 1.00 47.16 C
ANISOU 3483 CD1 TYR A 444 7863 6540 3516 -348 6 193 C
ATOM 3484 CD2 TYR A 444 23.734 86.239 223.644 1.00 49.48 C
ANISOU 3484 CD2 TYR A 444 8318 6722 3761 -314 -45 265 C
ATOM 3485 CE1 TYR A 444 21.980 86.882 221.602 1.00 46.40 C
ANISOU 3485 CE1 TYR A 444 7793 6461 3378 -495 28 208 C
ATOM 3486 CE2 TYR A 444 22.351 86.069 223.822 1.00 49.20 C
ANISOU 3486 CE2 TYR A 444 8314 6701 3680 -467 -11 279 C
ATOM 3487 CZ TYR A 444 21.492 86.397 222.792 1.00 48.26 C
ANISOU 3487 CZ TYR A 444 8118 6648 3569 -555 25 249 C
ATOM 3488 OH TYR A 444 20.142 86.241 222.962 1.00 49.57 O
ANISOU 3488 OH TYR A 444 8297 6837 3700 -705 55 264 O
ATOM 3489 N VAL A 445 28.344 86.974 220.415 1.00 49.53 N
ANISOU 3489 N VAL A 445 8065 6754 4000 184 -50 127 N
ATOM 3490 CA VAL A 445 29.768 87.278 220.388 1.00 49.84 C
ANISOU 3490 CA VAL A 445 8020 6806 4110 332 -68 118 C
ATOM 3491 C VAL A 445 29.963 88.775 220.291 1.00 49.33 C
ANISOU 3491 C VAL A 445 7776 6879 4088 331 -60 114 C
ATOM 3492 O VAL A 445 29.145 89.482 219.680 1.00 47.84 O
ANISOU 3492 O VAL A 445 7526 6765 3884 240 -23 100 O
ATOM 3493 CB VAL A 445 30.513 86.580 219.221 1.00 50.66 C
ANISOU 3493 CB VAL A 445 8157 6847 4243 420 -28 69 C
ATOM 3494 CG1 VAL A 445 30.554 85.074 219.463 1.00 52.01 C
ANISOU 3494 CG1 VAL A 445 8514 6864 4384 450 -42 75 C
ATOM 3495 CG2 VAL A 445 29.891 86.934 217.835 1.00 49.44 C
ANISOU 3495 CG2 VAL A 445 7970 6747 4069 340 38 22 C
ATOM 3496 N CYS A 446 31.049 89.244 220.900 1.00 50.30 N
ANISOU 3496 N CYS A 446 7815 7030 4265 431 -101 128 N
ATOM 3497 CA CYS A 446 31.416 90.652 220.840 1.00 51.03 C
ANISOU 3497 CA CYS A 446 7741 7242 4406 439 -97 122 C
ATOM 3498 C CYS A 446 32.873 90.882 220.462 1.00 50.69 C
ANISOU 3498 C CYS A 446 7597 7218 4444 569 -101 102 C
ATOM 3499 O CYS A 446 33.787 90.440 221.152 1.00 51.88 O
ANISOU 3499 O CYS A 446 7759 7328 4627 665 -155 121 O
ATOM 3500 CB CYS A 446 31.038 91.410 222.131 1.00 50.93 C
ANISOU 3500 CB CYS A 446 7698 7279 4372 387 -142 161 C
ATOM 3501 SG CYS A 446 31.986 91.005 223.666 1.00 58.47 S
ANISOU 3501 SG CYS A 446 8698 8186 5332 476 -240 205 S
ATOM 3502 N ARG A 447 33.074 91.599 219.363 1.00 49.93 N
ANISOU 3502 N ARG A 447 7400 7191 4382 568 -43 68 N
ATOM 3503 CA ARG A 447 34.408 92.002 218.938 1.00 49.78 C
ANISOU 3503 CA ARG A 447 7261 7210 4445 674 -31 47 C
ATOM 3504 C ARG A 447 34.525 93.524 218.805 1.00 48.32 C
ANISOU 3504 C ARG A 447 6922 7142 4294 637 -17 45 C
ATOM 3505 O ARG A 447 33.534 94.224 218.922 1.00 47.41 O
ANISOU 3505 O ARG A 447 6800 7072 4141 536 -10 57 O
ATOM 3506 CB ARG A 447 34.779 91.306 217.634 1.00 50.93 C
ANISOU 3506 CB ARG A 447 7439 7311 4601 726 40 1 C
ATOM 3507 CG ARG A 447 33.636 91.135 216.701 1.00 50.55 C
ANISOU 3507 CG ARG A 447 7468 7255 4483 621 94 -21 C
ATOM 3508 CD ARG A 447 34.065 91.520 215.347 1.00 53.41 C
ANISOU 3508 CD ARG A 447 7765 7661 4866 640 171 -64 C
ATOM 3509 NE ARG A 447 33.106 91.011 214.386 1.00 57.08 N
ANISOU 3509 NE ARG A 447 8337 8094 5258 557 215 -90 N
ATOM 3510 CZ ARG A 447 33.134 91.264 213.088 1.00 57.80 C
ANISOU 3510 CZ ARG A 447 8411 8218 5333 539 284 -127 C
ATOM 3511 NH1 ARG A 447 34.075 92.046 212.571 1.00 58.48 N
ANISOU 3511 NH1 ARG A 447 8373 8370 5475 598 326 -142 N
ATOM 3512 NH2 ARG A 447 32.212 90.735 212.307 1.00 58.94 N
ANISOU 3512 NH2 ARG A 447 8664 8329 5401 455 309 -149 N
ATOM 3513 N ARG A 448 35.747 94.016 218.579 1.00 48.08 N
ANISOU 3513 N ARG A 448 6769 7156 4342 720 -11 31 N
ATOM 3514 CA ARG A 448 36.035 95.453 218.456 1.00 46.62 C
ANISOU 3514 CA ARG A 448 6439 7074 4199 690 2 29 C
ATOM 3515 C ARG A 448 36.682 95.881 217.111 1.00 45.90 C
ANISOU 3515 C ARG A 448 6257 7029 4155 719 85 -7 C
ATOM 3516 O ARG A 448 37.840 95.597 216.858 1.00 46.72 O
ANISOU 3516 O ARG A 448 6301 7129 4323 817 98 -24 O
ATOM 3517 CB ARG A 448 36.911 95.899 219.627 1.00 46.68 C
ANISOU 3517 CB ARG A 448 6367 7110 4258 738 -77 52 C
ATOM 3518 CG ARG A 448 36.183 96.005 220.957 1.00 47.18 C
ANISOU 3518 CG ARG A 448 6498 7163 4267 678 -148 88 C
ATOM 3519 CD ARG A 448 37.115 96.613 222.024 1.00 48.85 C
ANISOU 3519 CD ARG A 448 6623 7415 4524 716 -228 106 C
ATOM 3520 NE ARG A 448 36.410 97.484 222.970 1.00 47.91 N
ANISOU 3520 NE ARG A 448 6512 7332 4360 626 -261 123 N
ATOM 3521 CZ ARG A 448 36.730 98.754 223.244 1.00 48.83 C
ANISOU 3521 CZ ARG A 448 6522 7522 4510 593 -272 117 C
ATOM 3522 NH1 ARG A 448 37.762 99.349 222.641 1.00 49.47 N
ANISOU 3522 NH1 ARG A 448 6470 7654 4671 636 -255 98 N
ATOM 3523 NH2 ARG A 448 36.011 99.445 224.133 1.00 48.23 N
ANISOU 3523 NH2 ARG A 448 6476 7465 4386 514 -294 129 N
ATOM 3524 N GLU A 449 35.925 96.560 216.257 1.00 44.15 N
ANISOU 3524 N GLU A 449 6025 6851 3899 635 141 -15 N
ATOM 3525 CA GLU A 449 36.490 97.248 215.086 1.00 43.24 C
ANISOU 3525 CA GLU A 449 5817 6792 3818 644 217 -41 C
ATOM 3526 C GLU A 449 37.119 98.620 215.463 1.00 41.29 C
ANISOU 3526 C GLU A 449 5423 6628 3636 635 203 -28 C
ATOM 3527 O GLU A 449 37.047 99.056 216.603 1.00 40.81 O
ANISOU 3527 O GLU A 449 5340 6580 3586 617 134 -3 O
ATOM 3528 CB GLU A 449 35.415 97.491 214.017 1.00 43.23 C
ANISOU 3528 CB GLU A 449 5868 6807 3750 554 272 -48 C
ATOM 3529 CG GLU A 449 34.386 96.399 213.825 1.00 46.14 C
ANISOU 3529 CG GLU A 449 6385 7106 4040 513 268 -53 C
ATOM 3530 CD GLU A 449 34.826 95.297 212.873 1.00 51.69 C
ANISOU 3530 CD GLU A 449 7165 7748 4726 570 323 -94 C
ATOM 3531 OE1 GLU A 449 35.300 95.586 211.733 1.00 54.16 O
ANISOU 3531 OE1 GLU A 449 7440 8093 5047 584 397 -123 O
ATOM 3532 OE2 GLU A 449 34.666 94.122 213.274 1.00 54.00 O
ANISOU 3532 OE2 GLU A 449 7567 7954 4995 597 297 -99 O
ATOM 3533 N LEU A 450 37.718 99.291 214.483 1.00 39.71 N
ANISOU 3533 N LEU A 450 5135 6480 3472 640 272 -46 N
ATOM 3534 CA LEU A 450 38.301 100.613 214.666 1.00 38.76 C
ANISOU 3534 CA LEU A 450 4882 6433 3411 618 272 -36 C
ATOM 3535 C LEU A 450 37.926 101.453 213.469 1.00 38.36 C
ANISOU 3535 C LEU A 450 4810 6426 3338 554 350 -39 C
ATOM 3536 O LEU A 450 38.207 101.079 212.337 1.00 38.82 O
ANISOU 3536 O LEU A 450 4883 6481 3385 576 425 -64 O
ATOM 3537 CB LEU A 450 39.828 100.534 214.760 1.00 39.71 C
ANISOU 3537 CB LEU A 450 4889 6575 3624 710 275 -52 C
ATOM 3538 CG LEU A 450 40.539 100.015 216.022 1.00 40.31 C
ANISOU 3538 CG LEU A 450 4940 6629 3747 783 181 -40 C
ATOM 3539 CD1 LEU A 450 42.038 99.971 215.832 1.00 41.40 C
ANISOU 3539 CD1 LEU A 450 4946 6798 3985 873 199 -58 C
ATOM 3540 CD2 LEU A 450 40.228 100.871 217.273 1.00 40.97 C
ANISOU 3540 CD2 LEU A 450 5001 6740 3827 722 94 -12 C
ATOM 3541 N ALA A 451 37.282 102.587 213.691 1.00 37.61 N
ANISOU 3541 N ALA A 451 4688 6368 3232 475 336 -15 N
ATOM 3542 CA ALA A 451 37.012 103.482 212.569 1.00 37.35 C
ANISOU 3542 CA ALA A 451 4630 6377 3184 419 405 -9 C
ATOM 3543 C ALA A 451 38.096 104.535 212.397 1.00 37.66 C
ANISOU 3543 C ALA A 451 4542 6470 3298 423 438 -11 C
ATOM 3544 O ALA A 451 38.871 104.841 213.323 1.00 37.89 O
ANISOU 3544 O ALA A 451 4491 6513 3392 448 392 -11 O
ATOM 3545 CB ALA A 451 35.611 104.114 212.641 1.00 36.49 C
ANISOU 3545 CB ALA A 451 4571 6273 3021 333 384 21 C
ATOM 3546 N THR A 452 38.135 105.087 211.191 1.00 37.76 N
ANISOU 3546 N THR A 452 4539 6511 3296 390 516 -10 N
ATOM 3547 CA THR A 452 39.072 106.145 210.875 1.00 38.10 C
ANISOU 3547 CA THR A 452 4470 6605 3403 377 562 -8 C
ATOM 3548 C THR A 452 38.443 107.524 210.668 1.00 37.53 C
ANISOU 3548 C THR A 452 4384 6556 3318 291 570 26 C
ATOM 3549 O THR A 452 37.868 107.815 209.632 1.00 37.41 O
ANISOU 3549 O THR A 452 4416 6548 3250 250 620 41 O
ATOM 3550 CB THR A 452 39.950 105.710 209.730 1.00 38.98 C
ANISOU 3550 CB THR A 452 4557 6730 3524 418 656 -36 C
ATOM 3551 OG1 THR A 452 40.686 104.559 210.183 1.00 39.64 O
ANISOU 3551 OG1 THR A 452 4628 6787 3645 511 638 -66 O
ATOM 3552 CG2 THR A 452 40.877 106.826 209.315 1.00 39.43 C
ANISOU 3552 CG2 THR A 452 4497 6841 3643 391 715 -31 C
ATOM 3553 N ALA A 453 38.569 108.348 211.708 1.00 37.26 N
ANISOU 3553 N ALA A 453 4294 6532 3333 268 516 38 N
ATOM 3554 CA ALA A 453 38.229 109.780 211.704 1.00 36.91 C
ANISOU 3554 CA ALA A 453 4220 6502 3300 197 522 66 C
ATOM 3555 C ALA A 453 38.906 110.527 210.571 1.00 37.42 C
ANISOU 3555 C ALA A 453 4232 6601 3387 170 609 73 C
ATOM 3556 O ALA A 453 39.994 110.149 210.147 1.00 38.18 O
ANISOU 3556 O ALA A 453 4267 6719 3520 206 657 49 O
ATOM 3557 CB ALA A 453 38.654 110.387 212.999 1.00 36.88 C
ANISOU 3557 CB ALA A 453 4156 6502 3356 188 459 62 C
ATOM 3558 N PRO A 454 38.283 111.617 210.087 1.00 37.13 N
ANISOU 3558 N PRO A 454 4213 6564 3329 106 633 108 N
ATOM 3559 CA PRO A 454 38.933 112.379 209.025 1.00 37.71 C
ANISOU 3559 CA PRO A 454 4245 6664 3417 71 717 120 C
ATOM 3560 C PRO A 454 40.371 112.789 209.358 1.00 38.44 C
ANISOU 3560 C PRO A 454 4216 6787 3602 74 739 98 C
ATOM 3561 O PRO A 454 41.186 112.938 208.443 1.00 39.18 O
ANISOU 3561 O PRO A 454 4264 6910 3711 66 824 94 O
ATOM 3562 CB PRO A 454 38.048 113.616 208.890 1.00 37.27 C
ANISOU 3562 CB PRO A 454 4224 6594 3345 6 711 166 C
ATOM 3563 CG PRO A 454 36.763 113.178 209.361 1.00 36.53 C
ANISOU 3563 CG PRO A 454 4207 6473 3201 16 648 176 C
ATOM 3564 CD PRO A 454 37.012 112.238 210.478 1.00 36.39 C
ANISOU 3564 CD PRO A 454 4177 6447 3204 65 589 140 C
ATOM 3565 N ASP A 455 40.696 112.988 210.631 1.00 38.35 N
ANISOU 3565 N ASP A 455 4151 6772 3647 79 666 85 N
ATOM 3566 CA ASP A 455 42.057 113.410 210.962 1.00 39.16 C
ANISOU 3566 CA ASP A 455 4129 6909 3840 73 675 66 C
ATOM 3567 C ASP A 455 43.025 112.257 211.208 1.00 39.81 C
ANISOU 3567 C ASP A 455 4147 7016 3965 154 665 29 C
ATOM 3568 O ASP A 455 44.084 112.441 211.788 1.00 40.49 O
ANISOU 3568 O ASP A 455 4121 7132 4131 160 640 13 O
ATOM 3569 CB ASP A 455 42.075 114.405 212.125 1.00 38.98 C
ANISOU 3569 CB ASP A 455 4074 6876 3862 22 605 69 C
ATOM 3570 CG ASP A 455 41.899 113.742 213.479 1.00 38.68 C
ANISOU 3570 CG ASP A 455 4051 6822 3824 64 500 49 C
ATOM 3571 OD1 ASP A 455 41.330 112.638 213.538 1.00 39.87 O
ANISOU 3571 OD1 ASP A 455 4269 6954 3924 121 478 45 O
ATOM 3572 OD2 ASP A 455 42.308 114.337 214.501 1.00 39.67 O
ANISOU 3572 OD2 ASP A 455 4128 6950 3993 34 439 39 O
ATOM 3573 N GLY A 456 42.665 111.064 210.772 1.00 39.71 N
ANISOU 3573 N GLY A 456 4202 6986 3900 216 680 18 N
ATOM 3574 CA GLY A 456 43.571 109.953 210.898 1.00 40.46 C
ANISOU 3574 CA GLY A 456 4243 7093 4037 304 680 -15 C
ATOM 3575 C GLY A 456 43.297 109.100 212.106 1.00 40.15 C
ANISOU 3575 C GLY A 456 4240 7023 3994 359 572 -22 C
ATOM 3576 O GLY A 456 43.578 107.910 212.057 1.00 40.56 O
ANISOU 3576 O GLY A 456 4307 7059 4046 441 572 -42 O
ATOM 3577 N THR A 457 42.724 109.679 213.169 1.00 39.51 N
ANISOU 3577 N THR A 457 4183 6926 3904 315 487 -7 N
ATOM 3578 CA THR A 457 42.520 108.983 214.457 1.00 39.33 C
ANISOU 3578 CA THR A 457 4195 6876 3874 356 380 -10 C
ATOM 3579 C THR A 457 41.679 107.715 214.363 1.00 38.95 C
ANISOU 3579 C THR A 457 4267 6779 3752 406 369 -12 C
ATOM 3580 O THR A 457 40.647 107.664 213.662 1.00 38.34 O
ANISOU 3580 O THR A 457 4281 6681 3605 375 411 -1 O
ATOM 3581 CB THR A 457 41.798 109.895 215.478 1.00 38.65 C
ANISOU 3581 CB THR A 457 4143 6775 3767 287 311 5 C
ATOM 3582 OG1 THR A 457 42.010 111.265 215.134 1.00 38.69 O
ANISOU 3582 OG1 THR A 457 4092 6804 3805 211 353 13 O
ATOM 3583 CG2 THR A 457 42.287 109.645 216.893 1.00 38.99 C
ANISOU 3583 CG2 THR A 457 4158 6817 3838 311 204 -3 C
ATOM 3584 N LYS A 458 42.094 106.702 215.116 1.00 39.38 N
ANISOU 3584 N LYS A 458 4324 6814 3823 480 306 -22 N
ATOM 3585 CA LYS A 458 41.326 105.447 215.185 1.00 39.12 C
ANISOU 3585 CA LYS A 458 4414 6726 3724 524 286 -22 C
ATOM 3586 C LYS A 458 40.285 105.480 216.313 1.00 38.38 C
ANISOU 3586 C LYS A 458 4409 6599 3574 484 204 -3 C
ATOM 3587 O LYS A 458 40.656 105.615 217.484 1.00 38.58 O
ANISOU 3587 O LYS A 458 4406 6628 3624 490 121 2 O
ATOM 3588 CB LYS A 458 42.268 104.246 215.327 1.00 40.09 C
ANISOU 3588 CB LYS A 458 4512 6832 3891 632 269 -40 C
ATOM 3589 CG LYS A 458 43.336 104.137 214.225 1.00 41.01 C
ANISOU 3589 CG LYS A 458 4534 6980 4067 681 364 -65 C
ATOM 3590 CD LYS A 458 42.720 103.883 212.864 1.00 40.77 C
ANISOU 3590 CD LYS A 458 4585 6933 3971 662 468 -76 C
ATOM 3591 CE LYS A 458 43.755 103.360 211.874 1.00 44.30 C
ANISOU 3591 CE LYS A 458 4972 7395 4466 735 564 -109 C
ATOM 3592 NZ LYS A 458 43.275 103.359 210.445 1.00 47.05 N
ANISOU 3592 NZ LYS A 458 5392 7740 4745 699 675 -122 N
ATOM 3593 N VAL A 459 38.992 105.389 215.947 1.00 37.61 N
ANISOU 3593 N VAL A 459 4416 6475 3401 438 228 9 N
ATOM 3594 CA VAL A 459 37.867 105.404 216.904 1.00 36.95 C
ANISOU 3594 CA VAL A 459 4417 6362 3260 395 170 27 C
ATOM 3595 C VAL A 459 37.361 103.975 217.135 1.00 37.03 C
ANISOU 3595 C VAL A 459 4536 6317 3217 434 143 27 C
ATOM 3596 O VAL A 459 37.005 103.293 216.180 1.00 37.05 O
ANISOU 3596 O VAL A 459 4594 6299 3186 445 193 19 O
ATOM 3597 CB VAL A 459 36.694 106.237 216.370 1.00 36.17 C
ANISOU 3597 CB VAL A 459 4353 6272 3120 317 212 43 C
ATOM 3598 CG1 VAL A 459 35.547 106.282 217.404 1.00 35.62 C
ANISOU 3598 CG1 VAL A 459 4357 6176 3000 275 162 59 C
ATOM 3599 CG2 VAL A 459 37.149 107.665 215.952 1.00 36.16 C
ANISOU 3599 CG2 VAL A 459 4259 6314 3168 275 251 47 C
ATOM 3600 N PRO A 460 37.349 103.504 218.401 1.00 37.18 N
ANISOU 3600 N PRO A 460 4595 6307 3223 453 63 35 N
ATOM 3601 CA PRO A 460 36.990 102.107 218.636 1.00 37.42 C
ANISOU 3601 CA PRO A 460 4733 6277 3208 493 37 38 C
ATOM 3602 C PRO A 460 35.506 101.900 218.522 1.00 36.75 C
ANISOU 3602 C PRO A 460 4752 6165 3045 425 56 50 C
ATOM 3603 O PRO A 460 34.751 102.766 218.929 1.00 36.16 O
ANISOU 3603 O PRO A 460 4674 6113 2952 358 52 63 O
ATOM 3604 CB PRO A 460 37.431 101.872 220.093 1.00 37.83 C
ANISOU 3604 CB PRO A 460 4794 6313 3266 521 -59 51 C
ATOM 3605 CG PRO A 460 38.360 103.007 220.427 1.00 38.03 C
ANISOU 3605 CG PRO A 460 4694 6397 3357 515 -82 46 C
ATOM 3606 CD PRO A 460 37.837 104.151 219.632 1.00 37.34 C
ANISOU 3606 CD PRO A 460 4567 6348 3272 443 -10 41 C
ATOM 3607 N ILE A 461 35.091 100.762 217.986 1.00 36.93 N
ANISOU 3607 N ILE A 461 4865 6140 3027 442 76 45 N
ATOM 3608 CA ILE A 461 33.694 100.367 218.050 1.00 36.48 C
ANISOU 3608 CA ILE A 461 4911 6054 2897 375 79 58 C
ATOM 3609 C ILE A 461 33.498 99.024 218.772 1.00 36.94 C
ANISOU 3609 C ILE A 461 5083 6039 2915 401 34 65 C
ATOM 3610 O ILE A 461 34.192 98.047 218.495 1.00 37.63 O
ANISOU 3610 O ILE A 461 5203 6080 3014 473 33 52 O
ATOM 3611 CB ILE A 461 33.074 100.267 216.655 1.00 36.29 C
ANISOU 3611 CB ILE A 461 4910 6037 2843 339 145 47 C
ATOM 3612 CG1 ILE A 461 33.233 101.572 215.879 1.00 35.93 C
ANISOU 3612 CG1 ILE A 461 4766 6057 2830 312 190 47 C
ATOM 3613 CG2 ILE A 461 31.616 99.952 216.764 1.00 35.91 C
ANISOU 3613 CG2 ILE A 461 4948 5970 2728 262 140 63 C
ATOM 3614 CD1 ILE A 461 32.931 101.414 214.412 1.00 35.99 C
ANISOU 3614 CD1 ILE A 461 4797 6072 2806 292 252 36 C
ATOM 3615 N SER A 462 32.554 98.981 219.702 1.00 36.65 N
ANISOU 3615 N SER A 462 5110 5987 2830 343 3 87 N
ATOM 3616 CA SER A 462 32.248 97.745 220.415 1.00 37.12 C
ANISOU 3616 CA SER A 462 5290 5973 2841 351 -36 100 C
ATOM 3617 C SER A 462 30.919 97.204 219.885 1.00 36.89 C
ANISOU 3617 C SER A 462 5347 5918 2750 273 1 102 C
ATOM 3618 O SER A 462 29.954 97.969 219.704 1.00 36.28 O
ANISOU 3618 O SER A 462 5240 5887 2657 196 28 109 O
ATOM 3619 CB SER A 462 32.203 97.967 221.943 1.00 37.18 C
ANISOU 3619 CB SER A 462 5320 5977 2830 338 -99 124 C
ATOM 3620 OG SER A 462 33.519 97.998 222.488 1.00 37.75 O
ANISOU 3620 OG SER A 462 5342 6051 2949 420 -155 125 O
ATOM 3621 N LEU A 463 30.861 95.909 219.594 1.00 37.46 N
ANISOU 3621 N LEU A 463 5524 5916 2792 293 1 96 N
ATOM 3622 CA LEU A 463 29.633 95.368 219.047 1.00 37.36 C
ANISOU 3622 CA LEU A 463 5592 5881 2722 209 31 95 C
ATOM 3623 C LEU A 463 29.283 93.999 219.497 1.00 38.01 C
ANISOU 3623 C LEU A 463 5817 5870 2754 199 9 103 C
ATOM 3624 O LEU A 463 30.149 93.171 219.766 1.00 38.71 O
ANISOU 3624 O LEU A 463 5959 5892 2855 282 -17 101 O
ATOM 3625 CB LEU A 463 29.608 95.370 217.516 1.00 37.33 C
ANISOU 3625 CB LEU A 463 5570 5895 2720 203 84 65 C
ATOM 3626 CG LEU A 463 30.852 95.300 216.685 1.00 37.73 C
ANISOU 3626 CG LEU A 463 5577 5943 2815 295 112 35 C
ATOM 3627 CD1 LEU A 463 30.656 94.305 215.601 1.00 38.25 C
ANISOU 3627 CD1 LEU A 463 5737 5956 2842 289 150 5 C
ATOM 3628 CD2 LEU A 463 31.002 96.664 216.117 1.00 37.13 C
ANISOU 3628 CD2 LEU A 463 5376 5957 2775 279 142 34 C
ATOM 3629 N VAL A 464 27.984 93.758 219.518 1.00 37.86 N
ANISOU 3629 N VAL A 464 5856 5845 2682 96 22 115 N
ATOM 3630 CA VAL A 464 27.496 92.460 219.842 1.00 39.72 C
ANISOU 3630 CA VAL A 464 6236 5991 2865 63 10 123 C
ATOM 3631 C VAL A 464 26.383 92.085 218.870 1.00 40.59 C
ANISOU 3631 C VAL A 464 6389 6099 2934 -35 45 109 C
ATOM 3632 O VAL A 464 25.631 92.950 218.431 1.00 39.65 O
ANISOU 3632 O VAL A 464 6188 6061 2818 -101 66 111 O
ATOM 3633 CB VAL A 464 27.083 92.415 221.309 1.00 39.38 C
ANISOU 3633 CB VAL A 464 6237 5932 2792 28 -24 161 C
ATOM 3634 CG1 VAL A 464 26.249 93.628 221.630 1.00 40.16 C
ANISOU 3634 CG1 VAL A 464 6241 6124 2893 -46 -5 173 C
ATOM 3635 CG2 VAL A 464 26.352 91.149 221.627 1.00 39.57 C
ANISOU 3635 CG2 VAL A 464 6412 5867 2754 -33 -28 175 C
ATOM 3636 N TYR A 465 26.348 90.793 218.525 1.00 42.98 N
ANISOU 3636 N TYR A 465 6822 6308 3202 -39 46 94 N
ATOM 3637 CA TYR A 465 25.358 90.164 217.639 1.00 45.07 C
ANISOU 3637 CA TYR A 465 7158 6549 3416 -138 69 76 C
ATOM 3638 C TYR A 465 25.156 88.651 217.937 1.00 47.29 C
ANISOU 3638 C TYR A 465 7615 6703 3650 -161 58 76 C
ATOM 3639 O TYR A 465 26.075 87.928 218.370 1.00 48.01 O
ANISOU 3639 O TYR A 465 7782 6707 3753 -66 40 77 O
ATOM 3640 CB TYR A 465 25.726 90.375 216.147 1.00 45.14 C
ANISOU 3640 CB TYR A 465 7131 6587 3435 -113 103 34 C
ATOM 3641 CG TYR A 465 27.160 89.998 215.808 1.00 46.29 C
ANISOU 3641 CG TYR A 465 7291 6681 3616 21 115 5 C
ATOM 3642 CD1 TYR A 465 28.221 90.917 215.969 1.00 46.43 C
ANISOU 3642 CD1 TYR A 465 7186 6757 3699 119 116 7 C
ATOM 3643 CD2 TYR A 465 27.465 88.726 215.366 1.00 45.98 C
ANISOU 3643 CD2 TYR A 465 7386 6532 3550 51 128 -26 C
ATOM 3644 CE1 TYR A 465 29.538 90.550 215.680 1.00 46.32 C
ANISOU 3644 CE1 TYR A 465 7170 6701 3727 243 131 -18 C
ATOM 3645 CE2 TYR A 465 28.754 88.370 215.083 1.00 47.34 C
ANISOU 3645 CE2 TYR A 465 7566 6657 3764 182 146 -53 C
ATOM 3646 CZ TYR A 465 29.778 89.271 215.233 1.00 47.57 C
ANISOU 3646 CZ TYR A 465 7460 6753 3862 278 148 -48 C
ATOM 3647 OH TYR A 465 31.046 88.856 214.926 1.00 51.03 O
ANISOU 3647 OH TYR A 465 7896 7146 4347 408 170 -76 O
ATOM 3648 N ASP A 466 23.937 88.181 217.690 1.00 49.03 N
ANISOU 3648 N ASP A 466 7898 6911 3819 -290 66 77 N
ATOM 3649 CA ASP A 466 23.646 86.764 217.731 1.00 51.19 C
ANISOU 3649 CA ASP A 466 8344 7063 4045 -334 63 71 C
ATOM 3650 C ASP A 466 24.569 86.080 216.738 1.00 52.28 C
ANISOU 3650 C ASP A 466 8553 7125 4187 -247 80 22 C
ATOM 3651 O ASP A 466 24.558 86.420 215.546 1.00 52.13 O
ANISOU 3651 O ASP A 466 8488 7154 4166 -258 105 -15 O
ATOM 3652 CB ASP A 466 22.184 86.496 217.346 1.00 51.94 C
ANISOU 3652 CB ASP A 466 8470 7176 4090 -500 71 71 C
ATOM 3653 CG ASP A 466 21.764 85.032 217.587 1.00 54.06 C
ANISOU 3653 CG ASP A 466 8925 7310 4304 -568 67 70 C
ATOM 3654 OD1 ASP A 466 22.147 84.167 216.764 1.00 55.83 O
ANISOU 3654 OD1 ASP A 466 9258 7447 4508 -545 76 28 O
ATOM 3655 OD2 ASP A 466 21.057 84.752 218.595 1.00 53.31 O
ANISOU 3655 OD2 ASP A 466 8874 7196 4185 -647 59 110 O
ATOM 3656 N THR A 467 25.350 85.127 217.246 1.00 53.27 N
ANISOU 3656 N THR A 467 8792 7132 4317 -159 67 24 N
ATOM 3657 CA THR A 467 26.324 84.331 216.478 1.00 54.65 C
ANISOU 3657 CA THR A 467 9049 7213 4504 -55 89 -21 C
ATOM 3658 C THR A 467 25.856 83.694 215.139 1.00 55.63 C
ANISOU 3658 C THR A 467 9265 7295 4579 -126 127 -78 C
ATOM 3659 O THR A 467 26.663 83.190 214.355 1.00 56.29 O
ANISOU 3659 O THR A 467 9402 7314 4670 -39 160 -126 O
ATOM 3660 CB THR A 467 26.949 83.234 217.383 1.00 55.63 C
ANISOU 3660 CB THR A 467 9307 7197 4632 30 62 2 C
ATOM 3661 OG1 THR A 467 28.027 82.613 216.691 1.00 57.19 O
ANISOU 3661 OG1 THR A 467 9556 7314 4861 158 88 -42 O
ATOM 3662 CG2 THR A 467 25.934 82.168 217.793 1.00 56.39 C
ANISOU 3662 CG2 THR A 467 9573 7191 4662 -92 51 20 C
ATOM 3663 N SER A 468 24.560 83.727 214.874 1.00 55.95 N
ANISOU 3663 N SER A 468 9319 7373 4567 -285 123 -75 N
ATOM 3664 CA SER A 468 24.022 83.030 213.732 1.00 56.83 C
ANISOU 3664 CA SER A 468 9537 7437 4620 -372 145 -125 C
ATOM 3665 C SER A 468 23.493 83.967 212.671 1.00 56.73 C
ANISOU 3665 C SER A 468 9410 7553 4591 -443 155 -144 C
ATOM 3666 O SER A 468 22.780 83.540 211.776 1.00 57.84 O
ANISOU 3666 O SER A 468 9622 7680 4673 -551 158 -178 O
ATOM 3667 CB SER A 468 22.889 82.137 214.184 1.00 57.43 C
ANISOU 3667 CB SER A 468 9738 7441 4640 -517 124 -107 C
ATOM 3668 OG SER A 468 21.759 82.945 214.418 1.00 56.51 O
ANISOU 3668 OG SER A 468 9509 7446 4517 -642 105 -72 O
ATOM 3669 N ILE A 469 23.801 85.247 212.742 1.00 56.32 N
ANISOU 3669 N ILE A 469 9187 7623 4588 -391 155 -122 N
ATOM 3670 CA ILE A 469 23.423 86.080 211.608 1.00 56.25 C
ANISOU 3670 CA ILE A 469 9089 7722 4561 -444 165 -140 C
ATOM 3671 C ILE A 469 24.445 85.890 210.507 1.00 57.21 C
ANISOU 3671 C ILE A 469 9248 7811 4677 -351 211 -198 C
ATOM 3672 O ILE A 469 25.602 85.532 210.765 1.00 57.32 O
ANISOU 3672 O ILE A 469 9291 7758 4732 -218 237 -213 O
ATOM 3673 CB ILE A 469 23.233 87.561 211.954 1.00 54.81 C
ANISOU 3673 CB ILE A 469 8718 7679 4427 -439 152 -96 C
ATOM 3674 CG1 ILE A 469 24.463 88.118 212.676 1.00 54.23 C
ANISOU 3674 CG1 ILE A 469 8563 7615 4425 -292 162 -81 C
ATOM 3675 CG2 ILE A 469 21.979 87.720 212.777 1.00 54.58 C
ANISOU 3675 CG2 ILE A 469 8657 7690 4391 -556 118 -50 C
ATOM 3676 CD1 ILE A 469 24.780 89.546 212.341 1.00 53.16 C
ANISOU 3676 CD1 ILE A 469 8264 7601 4333 -254 172 -69 C
ATOM 3677 N ASP A 470 24.000 86.110 209.281 1.00 58.08 N
ANISOU 3677 N ASP A 470 9361 7970 4735 -424 222 -228 N
ATOM 3678 CA ASP A 470 24.871 85.995 208.134 1.00 59.54 C
ANISOU 3678 CA ASP A 470 9586 8136 4901 -353 277 -285 C
ATOM 3679 C ASP A 470 25.692 87.253 208.030 1.00 58.95 C
ANISOU 3679 C ASP A 470 9349 8164 4887 -256 301 -268 C
ATOM 3680 O ASP A 470 25.138 88.332 207.801 1.00 58.98 O
ANISOU 3680 O ASP A 470 9235 8283 4891 -314 280 -235 O
ATOM 3681 CB ASP A 470 24.046 85.856 206.867 1.00 60.32 C
ANISOU 3681 CB ASP A 470 9749 8260 4908 -479 272 -319 C
ATOM 3682 CG ASP A 470 24.892 85.543 205.660 1.00 62.74 C
ANISOU 3682 CG ASP A 470 10135 8527 5175 -418 338 -388 C
ATOM 3683 OD1 ASP A 470 26.151 85.537 205.778 1.00 63.72 O
ANISOU 3683 OD1 ASP A 470 10239 8617 5354 -270 393 -407 O
ATOM 3684 OD2 ASP A 470 24.282 85.293 204.592 1.00 64.99 O
ANISOU 3684 OD2 ASP A 470 10503 8819 5372 -521 334 -423 O
ATOM 3685 N LEU A 471 27.004 87.119 208.184 1.00 59.04 N
ANISOU 3685 N LEU A 471 9349 8131 4952 -111 345 -288 N
ATOM 3686 CA LEU A 471 27.890 88.267 208.099 1.00 58.35 C
ANISOU 3686 CA LEU A 471 9108 8135 4928 -20 373 -275 C
ATOM 3687 C LEU A 471 28.355 88.581 206.672 1.00 59.08 C
ANISOU 3687 C LEU A 471 9199 8265 4985 -6 438 -321 C
ATOM 3688 O LEU A 471 28.944 89.636 206.437 1.00 58.83 O
ANISOU 3688 O LEU A 471 9039 8320 4994 42 465 -307 O
ATOM 3689 CB LEU A 471 29.096 88.091 209.013 1.00 58.47 C
ANISOU 3689 CB LEU A 471 9083 8103 5028 127 382 -268 C
ATOM 3690 CG LEU A 471 28.963 88.208 210.533 1.00 57.69 C
ANISOU 3690 CG LEU A 471 8940 8000 4979 141 320 -212 C
ATOM 3691 CD1 LEU A 471 30.357 88.289 211.123 1.00 56.30 C
ANISOU 3691 CD1 LEU A 471 8695 7807 4888 295 330 -209 C
ATOM 3692 CD2 LEU A 471 28.111 89.411 210.984 1.00 56.94 C
ANISOU 3692 CD2 LEU A 471 8723 8021 4892 54 279 -160 C
ATOM 3693 N LYS A 472 28.088 87.687 205.719 1.00 60.11 N
ANISOU 3693 N LYS A 472 9477 8328 5033 -55 466 -376 N
ATOM 3694 CA LYS A 472 28.476 87.935 204.319 1.00 60.50 C
ANISOU 3694 CA LYS A 472 9547 8410 5029 -53 532 -423 C
ATOM 3695 C LYS A 472 27.528 88.896 203.564 1.00 59.39 C
ANISOU 3695 C LYS A 472 9351 8386 4828 -176 499 -394 C
ATOM 3696 O LYS A 472 27.680 89.112 202.347 1.00 59.76 O
ANISOU 3696 O LYS A 472 9431 8464 4810 -197 544 -427 O
ATOM 3697 CB LYS A 472 28.675 86.617 203.550 1.00 62.34 C
ANISOU 3697 CB LYS A 472 9971 8523 5193 -48 584 -501 C
ATOM 3698 CG LYS A 472 30.067 85.969 203.766 1.00 65.02 C
ANISOU 3698 CG LYS A 472 10336 8769 5599 120 658 -542 C
ATOM 3699 CD LYS A 472 30.249 84.696 202.892 1.00 69.65 C
ANISOU 3699 CD LYS A 472 11122 9229 6113 127 723 -628 C
ATOM 3700 CE LYS A 472 31.014 83.574 203.624 1.00 71.43 C
ANISOU 3700 CE LYS A 472 11427 9310 6402 256 745 -650 C
ATOM 3701 NZ LYS A 472 30.244 83.085 204.822 1.00 71.68 N
ANISOU 3701 NZ LYS A 472 11499 9287 6449 202 652 -599 N
ATOM 3702 N LYS A 473 26.550 89.456 204.278 1.00 57.44 N
ANISOU 3702 N LYS A 473 9025 8200 4600 -254 422 -332 N
ATOM 3703 CA LYS A 473 25.735 90.553 203.736 1.00 55.99 C
ANISOU 3703 CA LYS A 473 8752 8134 4386 -345 384 -290 C
ATOM 3704 C LYS A 473 25.373 91.603 204.820 1.00 53.58 C
ANISOU 3704 C LYS A 473 8288 7907 4163 -341 336 -218 C
ATOM 3705 O LYS A 473 25.454 91.310 206.017 1.00 52.98 O
ANISOU 3705 O LYS A 473 8195 7790 4144 -305 316 -200 O
ATOM 3706 CB LYS A 473 24.520 90.051 202.921 1.00 56.54 C
ANISOU 3706 CB LYS A 473 8928 8205 4350 -492 338 -304 C
ATOM 3707 CG LYS A 473 23.770 88.837 203.458 1.00 58.95 C
ANISOU 3707 CG LYS A 473 9349 8419 4628 -566 296 -319 C
ATOM 3708 CD LYS A 473 22.695 89.202 204.504 1.00 61.84 C
ANISOU 3708 CD LYS A 473 9624 8835 5038 -640 223 -253 C
ATOM 3709 CE LYS A 473 21.766 87.997 204.816 1.00 64.71 C
ANISOU 3709 CE LYS A 473 10113 9118 5356 -750 182 -268 C
ATOM 3710 NZ LYS A 473 21.305 87.886 206.257 1.00 64.33 N
ANISOU 3710 NZ LYS A 473 10017 9054 5371 -762 150 -221 N
ATOM 3711 N PRO A 474 25.023 92.842 204.401 1.00 51.61 N
ANISOU 3711 N PRO A 474 7928 7764 3916 -374 320 -176 N
ATOM 3712 CA PRO A 474 24.706 93.887 205.372 1.00 49.41 C
ANISOU 3712 CA PRO A 474 7505 7553 3715 -366 283 -114 C
ATOM 3713 C PRO A 474 23.530 93.539 206.290 1.00 48.36 C
ANISOU 3713 C PRO A 474 7375 7413 3589 -446 220 -83 C
ATOM 3714 O PRO A 474 22.665 92.764 205.919 1.00 49.26 O
ANISOU 3714 O PRO A 474 7578 7501 3638 -542 189 -96 O
ATOM 3715 CB PRO A 474 24.369 95.091 204.484 1.00 49.49 C
ANISOU 3715 CB PRO A 474 7435 7664 3706 -404 276 -79 C
ATOM 3716 CG PRO A 474 24.179 94.529 203.073 1.00 50.35 C
ANISOU 3716 CG PRO A 474 7663 7762 3708 -465 287 -118 C
ATOM 3717 CD PRO A 474 25.108 93.383 203.031 1.00 51.53 C
ANISOU 3717 CD PRO A 474 7926 7811 3844 -401 345 -185 C
ATOM 3718 N ASN A 475 23.513 94.098 207.492 1.00 46.41 N
ANISOU 3718 N ASN A 475 7032 7186 3416 -412 205 -44 N
ATOM 3719 CA ASN A 475 22.503 93.755 208.488 1.00 44.92 C
ANISOU 3719 CA ASN A 475 6845 6986 3236 -480 161 -17 C
ATOM 3720 C ASN A 475 21.922 94.995 209.116 1.00 43.72 C
ANISOU 3720 C ASN A 475 6551 6921 3141 -492 140 38 C
ATOM 3721 O ASN A 475 22.569 96.039 209.140 1.00 44.29 O
ANISOU 3721 O ASN A 475 6530 7037 3260 -424 160 53 O
ATOM 3722 CB ASN A 475 23.114 92.901 209.582 1.00 44.40 C
ANISOU 3722 CB ASN A 475 6843 6829 3197 -420 172 -32 C
ATOM 3723 CG ASN A 475 23.488 91.535 209.100 1.00 44.55 C
ANISOU 3723 CG ASN A 475 7017 6745 3164 -415 190 -84 C
ATOM 3724 OD1 ASN A 475 22.665 90.635 209.060 1.00 41.88 O
ANISOU 3724 OD1 ASN A 475 6778 6361 2776 -506 166 -93 O
ATOM 3725 ND2 ASN A 475 24.749 91.370 208.730 1.00 45.83 N
ANISOU 3725 ND2 ASN A 475 7203 6869 3341 -308 236 -120 N
ATOM 3726 N PRO A 476 20.698 94.907 209.631 1.00 42.73 N
ANISOU 3726 N PRO A 476 6406 6817 3012 -581 103 67 N
ATOM 3727 CA PRO A 476 20.248 96.100 210.307 1.00 41.69 C
ANISOU 3727 CA PRO A 476 6140 6759 2942 -575 95 114 C
ATOM 3728 C PRO A 476 21.012 96.326 211.640 1.00 40.74 C
ANISOU 3728 C PRO A 476 5993 6608 2879 -491 117 118 C
ATOM 3729 O PRO A 476 21.243 95.389 212.389 1.00 41.06 O
ANISOU 3729 O PRO A 476 6115 6577 2909 -483 118 103 O
ATOM 3730 CB PRO A 476 18.770 95.826 210.513 1.00 41.91 C
ANISOU 3730 CB PRO A 476 6156 6815 2954 -690 59 139 C
ATOM 3731 CG PRO A 476 18.674 94.327 210.583 1.00 42.51 C
ANISOU 3731 CG PRO A 476 6373 6804 2974 -742 53 105 C
ATOM 3732 CD PRO A 476 19.710 93.818 209.677 1.00 43.07 C
ANISOU 3732 CD PRO A 476 6538 6822 3006 -688 74 60 C
ATOM 3733 N THR A 477 21.417 97.564 211.901 1.00 39.82 N
ANISOU 3733 N THR A 477 5768 6542 2818 -433 131 139 N
ATOM 3734 CA THR A 477 22.295 97.890 213.041 1.00 39.01 C
ANISOU 3734 CA THR A 477 5639 6418 2766 -352 146 138 C
ATOM 3735 C THR A 477 21.748 99.059 213.869 1.00 37.76 C
ANISOU 3735 C THR A 477 5374 6316 2658 -359 146 173 C
ATOM 3736 O THR A 477 21.035 99.934 213.347 1.00 37.67 O
ANISOU 3736 O THR A 477 5285 6368 2662 -391 143 199 O
ATOM 3737 CB THR A 477 23.756 98.211 212.526 1.00 38.73 C
ANISOU 3737 CB THR A 477 5588 6374 2754 -257 172 114 C
ATOM 3738 OG1 THR A 477 24.421 96.986 212.209 1.00 41.45 O
ANISOU 3738 OG1 THR A 477 6039 6645 3064 -227 181 76 O
ATOM 3739 CG2 THR A 477 24.592 98.936 213.527 1.00 36.35 C
ANISOU 3739 CG2 THR A 477 5221 6078 2513 -184 178 121 C
ATOM 3740 N MET A 478 22.076 99.060 215.150 1.00 36.25 N
ANISOU 3740 N MET A 478 5186 6097 2489 -326 149 174 N
ATOM 3741 CA MET A 478 21.883 100.234 215.961 1.00 35.42 C
ANISOU 3741 CA MET A 478 4990 6034 2432 -312 159 196 C
ATOM 3742 C MET A 478 23.223 100.698 216.518 1.00 35.12 C
ANISOU 3742 C MET A 478 4933 5979 2430 -226 163 181 C
ATOM 3743 O MET A 478 23.957 99.934 217.174 1.00 35.74 O
ANISOU 3743 O MET A 478 5077 6005 2497 -188 150 166 O
ATOM 3744 CB MET A 478 20.937 99.942 217.095 1.00 35.94 C
ANISOU 3744 CB MET A 478 5074 6093 2488 -367 160 210 C
ATOM 3745 CG MET A 478 21.051 100.929 218.237 1.00 36.39 C
ANISOU 3745 CG MET A 478 5075 6168 2584 -336 176 219 C
ATOM 3746 SD MET A 478 20.148 102.404 217.843 1.00 38.69 S
ANISOU 3746 SD MET A 478 5238 6536 2925 -353 198 245 S
ATOM 3747 CE MET A 478 18.453 101.845 218.062 1.00 36.18 C
ANISOU 3747 CE MET A 478 4918 6242 2588 -453 206 267 C
ATOM 3748 N LEU A 479 23.554 101.952 216.239 1.00 34.18 N
ANISOU 3748 N LEU A 479 4726 5906 2357 -195 177 189 N
ATOM 3749 CA LEU A 479 24.807 102.515 216.687 1.00 34.00 C
ANISOU 3749 CA LEU A 479 4670 5876 2373 -125 179 176 C
ATOM 3750 C LEU A 479 24.507 103.532 217.797 1.00 33.73 C
ANISOU 3750 C LEU A 479 4583 5861 2371 -130 184 188 C
ATOM 3751 O LEU A 479 23.789 104.518 217.565 1.00 33.53 O
ANISOU 3751 O LEU A 479 4494 5876 2371 -154 202 207 O
ATOM 3752 CB LEU A 479 25.535 103.157 215.515 1.00 33.93 C
ANISOU 3752 CB LEU A 479 4609 5894 2388 -93 198 172 C
ATOM 3753 CG LEU A 479 26.839 103.882 215.847 1.00 33.82 C
ANISOU 3753 CG LEU A 479 4541 5884 2425 -31 204 159 C
ATOM 3754 CD1 LEU A 479 27.958 102.885 216.196 1.00 34.18 C
ANISOU 3754 CD1 LEU A 479 4633 5886 2468 26 188 132 C
ATOM 3755 CD2 LEU A 479 27.225 104.702 214.672 1.00 33.78 C
ANISOU 3755 CD2 LEU A 479 4479 5914 2441 -22 234 165 C
ATOM 3756 N TYR A 480 25.037 103.282 218.995 1.00 33.81 N
ANISOU 3756 N TYR A 480 4627 5841 2378 -106 166 177 N
ATOM 3757 CA TYR A 480 24.707 104.085 220.146 1.00 33.69 C
ANISOU 3757 CA TYR A 480 4588 5836 2376 -118 173 181 C
ATOM 3758 C TYR A 480 25.913 104.920 220.476 1.00 33.59 C
ANISOU 3758 C TYR A 480 4530 5828 2405 -67 162 166 C
ATOM 3759 O TYR A 480 27.039 104.427 220.381 1.00 33.77 O
ANISOU 3759 O TYR A 480 4567 5832 2434 -20 136 152 O
ATOM 3760 CB TYR A 480 24.336 103.167 221.296 1.00 34.00 C
ANISOU 3760 CB TYR A 480 4712 5837 2367 -144 158 182 C
ATOM 3761 CG TYR A 480 24.043 103.862 222.605 1.00 34.01 C
ANISOU 3761 CG TYR A 480 4712 5845 2367 -159 169 181 C
ATOM 3762 CD1 TYR A 480 25.072 104.202 223.455 1.00 34.10 C
ANISOU 3762 CD1 TYR A 480 4731 5842 2383 -119 140 166 C
ATOM 3763 CD2 TYR A 480 22.749 104.175 222.990 1.00 34.06 C
ANISOU 3763 CD2 TYR A 480 4706 5871 2365 -213 209 192 C
ATOM 3764 CE1 TYR A 480 24.845 104.818 224.638 1.00 34.21 C
ANISOU 3764 CE1 TYR A 480 4758 5857 2384 -137 149 159 C
ATOM 3765 CE2 TYR A 480 22.503 104.809 224.182 1.00 34.18 C
ANISOU 3765 CE2 TYR A 480 4728 5887 2373 -225 230 185 C
ATOM 3766 CZ TYR A 480 23.562 105.128 225.012 1.00 34.25 C
ANISOU 3766 CZ TYR A 480 4761 5877 2377 -189 200 167 C
ATOM 3767 OH TYR A 480 23.403 105.764 226.235 1.00 34.47 O
ANISOU 3767 OH TYR A 480 4810 5901 2385 -204 218 154 O
ATOM 3768 N GLY A 481 25.674 106.185 220.842 1.00 33.40 N
ANISOU 3768 N GLY A 481 4450 5828 2414 -76 183 168 N
ATOM 3769 CA GLY A 481 26.740 107.111 221.267 1.00 33.39 C
ANISOU 3769 CA GLY A 481 4406 5830 2452 -44 172 152 C
ATOM 3770 C GLY A 481 26.481 107.926 222.529 1.00 33.46 C
ANISOU 3770 C GLY A 481 4419 5833 2461 -62 178 142 C
ATOM 3771 O GLY A 481 25.342 108.155 222.896 1.00 33.44 O
ANISOU 3771 O GLY A 481 4426 5836 2445 -96 211 150 O
ATOM 3772 N TYR A 482 27.552 108.355 223.201 1.00 33.63 N
ANISOU 3772 N TYR A 482 4433 5849 2498 -41 147 121 N
ATOM 3773 CA TYR A 482 27.439 109.363 224.279 1.00 33.77 C
ANISOU 3773 CA TYR A 482 4453 5861 2517 -61 155 104 C
ATOM 3774 C TYR A 482 27.991 110.697 223.789 1.00 33.68 C
ANISOU 3774 C TYR A 482 4368 5862 2569 -54 173 96 C
ATOM 3775 O TYR A 482 27.209 111.375 223.199 1.00 33.49 O
ANISOU 3775 O TYR A 482 4309 5845 2569 -65 220 110 O
ATOM 3776 CB TYR A 482 27.915 108.909 225.641 1.00 34.18 C
ANISOU 3776 CB TYR A 482 4575 5892 2521 -63 107 88 C
ATOM 3777 CG TYR A 482 27.428 109.784 226.753 1.00 34.39 C
ANISOU 3777 CG TYR A 482 4630 5910 2527 -97 131 69 C
ATOM 3778 CD1 TYR A 482 26.097 109.848 227.086 1.00 34.38 C
ANISOU 3778 CD1 TYR A 482 4658 5906 2500 -129 189 74 C
ATOM 3779 CD2 TYR A 482 28.313 110.539 227.503 1.00 34.72 C
ANISOU 3779 CD2 TYR A 482 4671 5946 2575 -99 97 41 C
ATOM 3780 CE1 TYR A 482 25.651 110.649 228.133 1.00 34.69 C
ANISOU 3780 CE1 TYR A 482 4729 5933 2519 -156 223 50 C
ATOM 3781 CE2 TYR A 482 27.874 111.328 228.558 1.00 35.02 C
ANISOU 3781 CE2 TYR A 482 4752 5970 2585 -133 123 16 C
ATOM 3782 CZ TYR A 482 26.547 111.386 228.852 1.00 35.00 C
ANISOU 3782 CZ TYR A 482 4781 5961 2556 -158 191 20 C
ATOM 3783 OH TYR A 482 26.140 112.198 229.874 1.00 35.40 O
ANISOU 3783 OH TYR A 482 4875 5994 2580 -187 228 -11 O
ATOM 3784 N GLY A 483 29.234 111.168 223.899 1.00 33.89 N
ANISOU 3784 N GLY A 483 4359 5890 2626 -40 140 78 N
ATOM 3785 CA GLY A 483 30.379 110.818 224.682 1.00 34.30 C
ANISOU 3785 CA GLY A 483 4425 5938 2668 -26 75 59 C
ATOM 3786 C GLY A 483 30.829 112.254 224.992 1.00 34.48 C
ANISOU 3786 C GLY A 483 4408 5961 2732 -50 83 37 C
ATOM 3787 O GLY A 483 31.432 112.949 224.155 1.00 34.45 O
ANISOU 3787 O GLY A 483 4333 5970 2786 -47 100 38 O
ATOM 3788 N SER A 484 30.421 112.725 226.179 1.00 34.72 N
ANISOU 3788 N SER A 484 4493 5972 2727 -81 82 16 N
ATOM 3789 CA SER A 484 30.816 114.008 226.718 1.00 35.05 C
ANISOU 3789 CA SER A 484 4523 6001 2792 -112 84 -14 C
ATOM 3790 C SER A 484 31.414 113.755 228.056 1.00 35.62 C
ANISOU 3790 C SER A 484 4654 6067 2813 -128 15 -40 C
ATOM 3791 O SER A 484 31.581 112.601 228.427 1.00 35.74 O
ANISOU 3791 O SER A 484 4708 6087 2783 -108 -34 -28 O
ATOM 3792 CB SER A 484 29.604 114.870 226.849 1.00 34.92 C
ANISOU 3792 CB SER A 484 4530 5961 2777 -133 159 -18 C
ATOM 3793 OG SER A 484 29.082 115.049 225.553 1.00 34.48 O
ANISOU 3793 OG SER A 484 4418 5915 2767 -114 208 14 O
ATOM 3794 N TYR A 485 31.797 114.822 228.754 1.00 36.07 N
ANISOU 3794 N TYR A 485 4720 6109 2875 -167 5 -75 N
ATOM 3795 CA TYR A 485 32.153 114.756 230.182 1.00 36.73 C
ANISOU 3795 CA TYR A 485 4882 6183 2893 -196 -58 -104 C
ATOM 3796 C TYR A 485 33.364 113.917 230.618 1.00 37.24 C
ANISOU 3796 C TYR A 485 4938 6271 2938 -180 -168 -99 C
ATOM 3797 O TYR A 485 33.836 114.074 231.765 1.00 37.94 O
ANISOU 3797 O TYR A 485 5083 6356 2977 -212 -234 -124 O
ATOM 3798 CB TYR A 485 30.953 114.295 230.992 1.00 36.73 C
ANISOU 3798 CB TYR A 485 4982 6162 2810 -207 -19 -104 C
ATOM 3799 CG TYR A 485 29.750 115.131 230.788 1.00 36.46 C
ANISOU 3799 CG TYR A 485 4955 6106 2794 -220 85 -112 C
ATOM 3800 CD1 TYR A 485 29.748 116.455 231.179 1.00 36.83 C
ANISOU 3800 CD1 TYR A 485 5012 6123 2858 -252 118 -151 C
ATOM 3801 CD2 TYR A 485 28.595 114.607 230.217 1.00 35.97 C
ANISOU 3801 CD2 TYR A 485 4886 6047 2732 -199 149 -81 C
ATOM 3802 CE1 TYR A 485 28.639 117.261 231.013 1.00 36.72 C
ANISOU 3802 CE1 TYR A 485 5003 6082 2867 -252 217 -158 C
ATOM 3803 CE2 TYR A 485 27.438 115.429 230.047 1.00 35.86 C
ANISOU 3803 CE2 TYR A 485 4866 6016 2744 -204 244 -86 C
ATOM 3804 CZ TYR A 485 27.492 116.762 230.460 1.00 36.26 C
ANISOU 3804 CZ TYR A 485 4926 6034 2816 -225 278 -124 C
ATOM 3805 OH TYR A 485 26.437 117.612 230.364 1.00 36.32 O
ANISOU 3805 OH TYR A 485 4929 6016 2854 -219 369 -130 O
ATOM 3806 N GLY A 486 33.854 113.047 229.734 1.00 36.99 N
ANISOU 3806 N GLY A 486 4844 6263 2946 -129 -190 -68 N
ATOM 3807 CA GLY A 486 34.912 112.106 230.060 1.00 37.51 C
ANISOU 3807 CA GLY A 486 4899 6350 3005 -95 -289 -56 C
ATOM 3808 C GLY A 486 34.295 110.778 230.422 1.00 37.44 C
ANISOU 3808 C GLY A 486 4977 6323 2925 -65 -302 -28 C
ATOM 3809 O GLY A 486 34.993 109.795 230.731 1.00 37.91 O
ANISOU 3809 O GLY A 486 5049 6386 2969 -25 -383 -10 O
ATOM 3810 N ILE A 487 32.971 110.755 230.377 1.00 36.93 N
ANISOU 3810 N ILE A 487 4972 6237 2823 -84 -222 -23 N
ATOM 3811 CA ILE A 487 32.225 109.534 230.615 1.00 36.84 C
ANISOU 3811 CA ILE A 487 5045 6206 2748 -69 -217 4 C
ATOM 3812 C ILE A 487 32.354 108.523 229.446 1.00 36.48 C
ANISOU 3812 C ILE A 487 4956 6164 2742 -14 -210 34 C
ATOM 3813 O ILE A 487 32.392 108.892 228.295 1.00 36.02 O
ANISOU 3813 O ILE A 487 4816 6123 2749 0 -163 34 O
ATOM 3814 CB ILE A 487 30.758 109.832 231.033 1.00 36.60 C
ANISOU 3814 CB ILE A 487 5085 6155 2665 -115 -133 -2 C
ATOM 3815 CG1 ILE A 487 30.768 110.509 232.415 1.00 37.22 C
ANISOU 3815 CG1 ILE A 487 5240 6223 2680 -163 -152 -34 C
ATOM 3816 CG2 ILE A 487 29.907 108.552 231.022 1.00 36.47 C
ANISOU 3816 CG2 ILE A 487 5139 6122 2596 -108 -113 30 C
ATOM 3817 CD1 ILE A 487 29.509 111.282 232.795 1.00 37.12 C
ANISOU 3817 CD1 ILE A 487 5269 6194 2641 -206 -53 -56 C
ATOM 3818 N CYS A 488 32.456 107.245 229.797 1.00 36.80 N
ANISOU 3818 N CYS A 488 5063 6183 2736 16 -259 57 N
ATOM 3819 CA CYS A 488 32.732 106.184 228.856 1.00 36.69 C
ANISOU 3819 CA CYS A 488 5027 6161 2752 72 -263 80 C
ATOM 3820 C CYS A 488 31.471 105.367 228.802 1.00 36.41 C
ANISOU 3820 C CYS A 488 5079 6095 2659 50 -213 99 C
ATOM 3821 O CYS A 488 30.906 105.061 229.874 1.00 36.72 O
ANISOU 3821 O CYS A 488 5218 6112 2622 15 -224 106 O
ATOM 3822 CB CYS A 488 33.850 105.279 229.387 1.00 37.48 C
ANISOU 3822 CB CYS A 488 5147 6249 2844 128 -364 94 C
ATOM 3823 SG CYS A 488 35.360 106.105 230.000 1.00 38.22 S
ANISOU 3823 SG CYS A 488 5158 6381 2982 139 -459 75 S
ATOM 3824 N ILE A 489 31.019 105.031 227.581 1.00 35.91 N
ANISOU 3824 N ILE A 489 4983 6034 2629 61 -157 107 N
ATOM 3825 CA ILE A 489 30.014 103.960 227.430 1.00 35.83 C
ANISOU 3825 CA ILE A 489 5054 5991 2569 44 -128 128 C
ATOM 3826 C ILE A 489 30.703 102.619 227.414 1.00 36.34 C
ANISOU 3826 C ILE A 489 5172 6016 2620 99 -185 145 C
ATOM 3827 O ILE A 489 31.411 102.298 226.489 1.00 36.35 O
ANISOU 3827 O ILE A 489 5121 6020 2672 153 -190 141 O
ATOM 3828 CB ILE A 489 29.089 104.092 226.202 1.00 35.23 C
ANISOU 3828 CB ILE A 489 4936 5930 2518 20 -51 130 C
ATOM 3829 CG1 ILE A 489 28.415 105.471 226.157 1.00 34.82 C
ANISOU 3829 CG1 ILE A 489 4824 5913 2491 -22 5 118 C
ATOM 3830 CG2 ILE A 489 28.035 102.928 226.205 1.00 35.31 C
ANISOU 3830 CG2 ILE A 489 5038 5907 2471 -13 -30 150 C
ATOM 3831 CD1 ILE A 489 27.680 105.887 227.504 1.00 35.04 C
ANISOU 3831 CD1 ILE A 489 4913 5934 2466 -71 19 112 C
ATOM 3832 N GLU A 490 30.498 101.862 228.490 1.00 38.86 N
ANISOU 3832 N GLU A 490 5602 6296 2868 87 -225 164 N
ATOM 3833 CA GLU A 490 31.168 100.563 228.755 1.00 40.00 C
ANISOU 3833 CA GLU A 490 5819 6389 2990 145 -293 187 C
ATOM 3834 C GLU A 490 30.671 99.409 227.910 1.00 41.01 C
ANISOU 3834 C GLU A 490 5999 6471 3111 154 -259 199 C
ATOM 3835 O GLU A 490 29.498 99.355 227.564 1.00 40.93 O
ANISOU 3835 O GLU A 490 6015 6461 3076 90 -194 200 O
ATOM 3836 CB GLU A 490 30.987 100.242 230.212 1.00 39.47 C
ANISOU 3836 CB GLU A 490 5866 6292 2838 116 -342 208 C
ATOM 3837 CG GLU A 490 31.480 101.380 231.030 1.00 38.54 C
ANISOU 3837 CG GLU A 490 5707 6217 2719 100 -378 190 C
ATOM 3838 CD GLU A 490 32.993 101.486 231.012 1.00 39.19 C
ANISOU 3838 CD GLU A 490 5714 6316 2860 174 -467 187 C
ATOM 3839 OE1 GLU A 490 33.589 100.987 230.029 1.00 40.46 O
ANISOU 3839 OE1 GLU A 490 5814 6472 3086 240 -467 188 O
ATOM 3840 OE2 GLU A 490 33.597 102.056 231.977 1.00 39.31 O
ANISOU 3840 OE2 GLU A 490 5729 6352 2854 166 -535 182 O
ATOM 3841 N PRO A 491 31.565 98.482 227.546 1.00 43.10 N
ANISOU 3841 N PRO A 491 6278 6698 3402 233 -302 207 N
ATOM 3842 CA PRO A 491 31.017 97.264 226.909 1.00 43.79 C
ANISOU 3842 CA PRO A 491 6449 6725 3466 232 -272 216 C
ATOM 3843 C PRO A 491 30.666 96.294 228.052 1.00 44.76 C
ANISOU 3843 C PRO A 491 6720 6780 3507 213 -315 252 C
ATOM 3844 O PRO A 491 31.449 95.405 228.388 1.00 45.92 O
ANISOU 3844 O PRO A 491 6927 6871 3651 283 -380 272 O
ATOM 3845 CB PRO A 491 32.188 96.763 226.051 1.00 44.02 C
ANISOU 3845 CB PRO A 491 6428 6736 3561 334 -292 205 C
ATOM 3846 CG PRO A 491 33.493 97.271 226.836 1.00 44.84 C
ANISOU 3846 CG PRO A 491 6463 6870 3704 399 -375 209 C
ATOM 3847 CD PRO A 491 33.016 98.359 227.835 1.00 44.10 C
ANISOU 3847 CD PRO A 491 6362 6824 3572 323 -384 210 C
ATOM 3848 N GLU A 492 29.534 96.540 228.707 1.00 44.80 N
ANISOU 3848 N GLU A 492 6781 6793 3449 120 -280 261 N
ATOM 3849 CA GLU A 492 29.080 95.708 229.831 1.00 45.51 C
ANISOU 3849 CA GLU A 492 7018 6822 3450 82 -306 296 C
ATOM 3850 C GLU A 492 27.790 95.001 229.406 1.00 45.09 C
ANISOU 3850 C GLU A 492 7037 6736 3360 2 -236 303 C
ATOM 3851 O GLU A 492 27.236 95.281 228.327 1.00 44.42 O
ANISOU 3851 O GLU A 492 6880 6684 3314 -26 -176 280 O
ATOM 3852 CB GLU A 492 28.892 96.542 231.118 1.00 45.46 C
ANISOU 3852 CB GLU A 492 7029 6854 3392 34 -321 301 C
ATOM 3853 CG GLU A 492 27.733 97.539 231.059 1.00 45.35 C
ANISOU 3853 CG GLU A 492 6962 6897 3371 -54 -231 278 C
ATOM 3854 CD GLU A 492 27.892 98.738 231.975 1.00 47.55 C
ANISOU 3854 CD GLU A 492 7207 7226 3634 -75 -240 261 C
ATOM 3855 OE1 GLU A 492 28.600 98.663 233.000 1.00 51.73 O
ANISOU 3855 OE1 GLU A 492 7798 7740 4119 -53 -315 275 O
ATOM 3856 OE2 GLU A 492 27.279 99.778 231.686 1.00 47.91 O
ANISOU 3856 OE2 GLU A 492 7171 7323 3710 -114 -172 235 O
ATOM 3857 N PHE A 493 27.319 94.077 230.228 1.00 45.06 N
ANISOU 3857 N PHE A 493 7176 6667 3278 -39 -248 337 N
ATOM 3858 CA PHE A 493 26.086 93.422 229.888 1.00 44.99 C
ANISOU 3858 CA PHE A 493 7232 6629 3234 -128 -183 343 C
ATOM 3859 C PHE A 493 24.934 94.372 230.075 1.00 44.36 C
ANISOU 3859 C PHE A 493 7090 6622 3143 -224 -107 330 C
ATOM 3860 O PHE A 493 24.865 95.086 231.062 1.00 44.31 O
ANISOU 3860 O PHE A 493 7082 6649 3104 -244 -106 333 O
ATOM 3861 CB PHE A 493 25.824 92.173 230.724 1.00 45.42 C
ANISOU 3861 CB PHE A 493 7462 6590 3206 -160 -206 386 C
ATOM 3862 CG PHE A 493 24.543 91.510 230.372 1.00 46.00 C
ANISOU 3862 CG PHE A 493 7597 6635 3246 -266 -137 392 C
ATOM 3863 CD1 PHE A 493 24.439 90.741 229.215 1.00 48.96 C
ANISOU 3863 CD1 PHE A 493 7983 6966 3652 -261 -124 378 C
ATOM 3864 CD2 PHE A 493 23.419 91.716 231.130 1.00 45.89 C
ANISOU 3864 CD2 PHE A 493 7618 6645 3174 -375 -80 405 C
ATOM 3865 CE1 PHE A 493 23.246 90.142 228.871 1.00 48.68 C
ANISOU 3865 CE1 PHE A 493 8000 6909 3587 -370 -67 381 C
ATOM 3866 CE2 PHE A 493 22.224 91.129 230.793 1.00 46.96 C
ANISOU 3866 CE2 PHE A 493 7792 6763 3286 -481 -17 410 C
ATOM 3867 CZ PHE A 493 22.134 90.338 229.674 1.00 48.72 C
ANISOU 3867 CZ PHE A 493 8031 6942 3539 -482 -15 399 C
ATOM 3868 N ASN A 494 24.005 94.349 229.140 1.00 44.35 N
ANISOU 3868 N ASN A 494 7042 6643 3165 -282 -45 317 N
ATOM 3869 CA ASN A 494 22.790 95.093 229.324 1.00 44.53 C
ANISOU 3869 CA ASN A 494 7010 6728 3181 -372 29 310 C
ATOM 3870 C ASN A 494 21.592 94.465 228.578 1.00 44.65 C
ANISOU 3870 C ASN A 494 7035 6738 3193 -460 83 314 C
ATOM 3871 O ASN A 494 21.484 94.564 227.354 1.00 43.35 O
ANISOU 3871 O ASN A 494 6794 6597 3078 -453 92 295 O
ATOM 3872 CB ASN A 494 23.035 96.564 228.946 1.00 43.81 C
ANISOU 3872 CB ASN A 494 6769 6722 3157 -336 45 281 C
ATOM 3873 CG ASN A 494 21.779 97.367 228.958 1.00 45.29 C
ANISOU 3873 CG ASN A 494 6882 6971 3353 -412 124 274 C
ATOM 3874 OD1 ASN A 494 21.014 97.329 229.927 1.00 50.40 O
ANISOU 3874 OD1 ASN A 494 7583 7618 3948 -478 164 285 O
ATOM 3875 ND2 ASN A 494 21.513 98.064 227.867 1.00 46.81 N
ANISOU 3875 ND2 ASN A 494 6954 7217 3612 -405 149 257 N
ATOM 3876 N SER A 495 20.709 93.816 229.339 1.00 46.04 N
ANISOU 3876 N SER A 495 7308 6883 3304 -550 116 338 N
ATOM 3877 CA SER A 495 19.507 93.105 228.815 1.00 46.99 C
ANISOU 3877 CA SER A 495 7449 6994 3413 -654 164 346 C
ATOM 3878 C SER A 495 18.672 93.951 227.865 1.00 46.30 C
ANISOU 3878 C SER A 495 7208 6995 3388 -691 211 325 C
ATOM 3879 O SER A 495 18.007 93.451 226.958 1.00 46.30 O
ANISOU 3879 O SER A 495 7195 6996 3401 -749 223 322 O
ATOM 3880 CB SER A 495 18.616 92.611 229.984 1.00 48.25 C
ANISOU 3880 CB SER A 495 7709 7128 3496 -755 210 375 C
ATOM 3881 OG SER A 495 17.897 93.673 230.639 1.00 49.20 O
ANISOU 3881 OG SER A 495 7748 7327 3619 -796 276 369 O
ATOM 3882 N ARG A 496 18.733 95.251 228.091 1.00 46.03 N
ANISOU 3882 N ARG A 496 7065 7033 3391 -656 232 311 N
ATOM 3883 CA ARG A 496 17.953 96.205 227.362 1.00 46.24 C
ANISOU 3883 CA ARG A 496 6946 7145 3480 -680 275 298 C
ATOM 3884 C ARG A 496 18.125 96.102 225.845 1.00 45.60 C
ANISOU 3884 C ARG A 496 6804 7075 3445 -656 246 285 C
ATOM 3885 O ARG A 496 17.225 96.449 225.104 1.00 46.44 O
ANISOU 3885 O ARG A 496 6820 7239 3588 -705 273 285 O
ATOM 3886 CB ARG A 496 18.327 97.595 227.843 1.00 46.06 C
ANISOU 3886 CB ARG A 496 6838 7173 3489 -621 290 282 C
ATOM 3887 CG ARG A 496 17.132 98.353 228.409 1.00 50.24 C
ANISOU 3887 CG ARG A 496 7300 7761 4028 -683 371 283 C
ATOM 3888 CD ARG A 496 16.866 98.119 229.927 1.00 52.96 C
ANISOU 3888 CD ARG A 496 7746 8079 4297 -728 410 292 C
ATOM 3889 NE ARG A 496 17.584 99.065 230.792 1.00 56.38 N
ANISOU 3889 NE ARG A 496 8183 8520 4720 -670 405 274 N
ATOM 3890 CZ ARG A 496 18.379 100.080 230.399 1.00 58.17 C
ANISOU 3890 CZ ARG A 496 8329 8772 5001 -590 375 252 C
ATOM 3891 NH1 ARG A 496 18.625 100.371 229.111 1.00 58.35 N
ANISOU 3891 NH1 ARG A 496 8256 8819 5095 -548 348 246 N
ATOM 3892 NH2 ARG A 496 18.959 100.830 231.328 1.00 59.39 N
ANISOU 3892 NH2 ARG A 496 8506 8927 5133 -556 371 234 N
ATOM 3893 N PHE A 497 19.273 95.625 225.381 1.00 44.74 N
ANISOU 3893 N PHE A 497 6746 6916 3337 -582 191 275 N
ATOM 3894 CA PHE A 497 19.536 95.540 223.957 1.00 43.15 C
ANISOU 3894 CA PHE A 497 6501 6724 3171 -556 170 259 C
ATOM 3895 C PHE A 497 19.165 94.182 223.321 1.00 42.82 C
ANISOU 3895 C PHE A 497 6556 6621 3092 -614 159 259 C
ATOM 3896 O PHE A 497 19.209 94.015 222.077 1.00 41.76 O
ANISOU 3896 O PHE A 497 6399 6494 2975 -612 147 243 O
ATOM 3897 CB PHE A 497 20.977 96.000 223.640 1.00 43.31 C
ANISOU 3897 CB PHE A 497 6490 6738 3226 -439 132 241 C
ATOM 3898 CG PHE A 497 22.088 95.076 224.139 1.00 45.40 C
ANISOU 3898 CG PHE A 497 6869 6919 3462 -374 86 242 C
ATOM 3899 CD1 PHE A 497 22.090 93.705 223.863 1.00 48.24 C
ANISOU 3899 CD1 PHE A 497 7347 7196 3784 -391 70 245 C
ATOM 3900 CD2 PHE A 497 23.187 95.613 224.828 1.00 47.88 C
ANISOU 3900 CD2 PHE A 497 7165 7235 3793 -290 53 240 C
ATOM 3901 CE1 PHE A 497 23.156 92.861 224.315 1.00 50.99 C
ANISOU 3901 CE1 PHE A 497 7798 7460 4114 -315 24 250 C
ATOM 3902 CE2 PHE A 497 24.250 94.792 225.290 1.00 49.53 C
ANISOU 3902 CE2 PHE A 497 7465 7371 3984 -219 0 247 C
ATOM 3903 CZ PHE A 497 24.237 93.411 225.023 1.00 51.10 C
ANISOU 3903 CZ PHE A 497 7784 7484 4150 -225 -14 254 C
ATOM 3904 N LEU A 498 18.769 93.225 224.169 1.00 42.19 N
ANISOU 3904 N LEU A 498 6593 6480 2958 -674 165 278 N
ATOM 3905 CA LEU A 498 18.399 91.900 223.676 1.00 42.08 C
ANISOU 3905 CA LEU A 498 6689 6395 2906 -739 156 278 C
ATOM 3906 C LEU A 498 17.248 91.942 222.656 1.00 41.97 C
ANISOU 3906 C LEU A 498 6603 6436 2905 -837 175 271 C
ATOM 3907 O LEU A 498 17.333 91.281 221.618 1.00 42.63 O
ANISOU 3907 O LEU A 498 6730 6486 2980 -851 153 253 O
ATOM 3908 CB LEU A 498 18.104 90.919 224.801 1.00 42.27 C
ANISOU 3908 CB LEU A 498 6853 6340 2866 -798 163 305 C
ATOM 3909 CG LEU A 498 19.305 90.304 225.523 1.00 42.76 C
ANISOU 3909 CG LEU A 498 7039 6310 2898 -706 119 316 C
ATOM 3910 CD1 LEU A 498 18.960 90.025 226.994 1.00 43.42 C
ANISOU 3910 CD1 LEU A 498 7215 6362 2922 -756 135 352 C
ATOM 3911 CD2 LEU A 498 19.837 89.043 224.854 1.00 41.98 C
ANISOU 3911 CD2 LEU A 498 7063 6105 2782 -681 86 306 C
ATOM 3912 N PRO A 499 16.197 92.741 222.913 1.00 41.17 N
ANISOU 3912 N PRO A 499 6392 6422 2828 -901 215 285 N
ATOM 3913 CA PRO A 499 15.208 92.779 221.867 1.00 41.38 C
ANISOU 3913 CA PRO A 499 6343 6505 2874 -983 217 282 C
ATOM 3914 C PRO A 499 15.768 93.091 220.457 1.00 40.99 C
ANISOU 3914 C PRO A 499 6247 6478 2851 -925 180 258 C
ATOM 3915 O PRO A 499 15.173 92.627 219.474 1.00 41.89 O
ANISOU 3915 O PRO A 499 6364 6601 2953 -997 162 250 O
ATOM 3916 CB PRO A 499 14.238 93.865 222.341 1.00 41.34 C
ANISOU 3916 CB PRO A 499 6198 6599 2912 -1018 263 300 C
ATOM 3917 CG PRO A 499 14.357 93.856 223.784 1.00 40.74 C
ANISOU 3917 CG PRO A 499 6178 6493 2808 -1011 299 312 C
ATOM 3918 CD PRO A 499 15.801 93.593 224.048 1.00 41.15 C
ANISOU 3918 CD PRO A 499 6328 6470 2836 -906 259 301 C
ATOM 3919 N TYR A 500 16.881 93.828 220.341 1.00 39.49 N
ANISOU 3919 N TYR A 500 6019 6295 2689 -806 168 246 N
ATOM 3920 CA TYR A 500 17.428 94.138 219.009 1.00 38.63 C
ANISOU 3920 CA TYR A 500 5870 6208 2599 -756 144 225 C
ATOM 3921 C TYR A 500 18.257 93.004 218.485 1.00 38.89 C
ANISOU 3921 C TYR A 500 6033 6149 2594 -726 120 199 C
ATOM 3922 O TYR A 500 18.157 92.633 217.334 1.00 39.13 O
ANISOU 3922 O TYR A 500 6084 6176 2607 -752 107 179 O
ATOM 3923 CB TYR A 500 18.354 95.346 219.040 1.00 37.96 C
ANISOU 3923 CB TYR A 500 5696 6164 2563 -646 146 221 C
ATOM 3924 CG TYR A 500 17.708 96.674 219.347 1.00 37.07 C
ANISOU 3924 CG TYR A 500 5448 6140 2499 -652 171 241 C
ATOM 3925 CD1 TYR A 500 16.612 97.129 218.607 1.00 36.86 C
ANISOU 3925 CD1 TYR A 500 5329 6184 2492 -716 174 256 C
ATOM 3926 CD2 TYR A 500 18.229 97.504 220.353 1.00 36.35 C
ANISOU 3926 CD2 TYR A 500 5321 6057 2433 -589 188 244 C
ATOM 3927 CE1 TYR A 500 16.049 98.356 218.873 1.00 36.58 C
ANISOU 3927 CE1 TYR A 500 5170 6221 2509 -707 199 275 C
ATOM 3928 CE2 TYR A 500 17.655 98.725 220.630 1.00 36.06 C
ANISOU 3928 CE2 TYR A 500 5171 6090 2442 -589 218 257 C
ATOM 3929 CZ TYR A 500 16.574 99.142 219.887 1.00 36.18 C
ANISOU 3929 CZ TYR A 500 5095 6169 2483 -643 226 273 C
ATOM 3930 OH TYR A 500 16.005 100.354 220.154 1.00 36.01 O
ANISOU 3930 OH TYR A 500 4960 6208 2513 -632 257 288 O
ATOM 3931 N VAL A 501 19.125 92.477 219.332 1.00 38.96 N
ANISOU 3931 N VAL A 501 6132 6082 2590 -662 115 198 N
ATOM 3932 CA VAL A 501 20.063 91.477 218.888 1.00 39.01 C
ANISOU 3932 CA VAL A 501 6253 5995 2573 -606 97 172 C
ATOM 3933 C VAL A 501 19.342 90.151 218.666 1.00 40.48 C
ANISOU 3933 C VAL A 501 6569 6106 2705 -706 94 167 C
ATOM 3934 O VAL A 501 19.707 89.367 217.782 1.00 40.59 O
ANISOU 3934 O VAL A 501 6668 6059 2696 -696 85 136 O
ATOM 3935 CB VAL A 501 21.198 91.355 219.873 1.00 38.85 C
ANISOU 3935 CB VAL A 501 6279 5920 2562 -502 83 179 C
ATOM 3936 CG1 VAL A 501 22.024 90.178 219.549 1.00 39.50 C
ANISOU 3936 CG1 VAL A 501 6490 5895 2624 -446 66 159 C
ATOM 3937 CG2 VAL A 501 22.041 92.603 219.826 1.00 38.08 C
ANISOU 3937 CG2 VAL A 501 6057 5892 2520 -407 82 174 C
ATOM 3938 N ASP A 502 18.281 89.933 219.437 1.00 41.39 N
ANISOU 3938 N ASP A 502 6699 6228 2799 -810 106 195 N
ATOM 3939 CA ASP A 502 17.435 88.759 219.258 1.00 42.86 C
ANISOU 3939 CA ASP A 502 6996 6352 2936 -930 106 193 C
ATOM 3940 C ASP A 502 16.731 88.710 217.903 1.00 43.00 C
ANISOU 3940 C ASP A 502 6979 6415 2946 -1012 95 170 C
ATOM 3941 O ASP A 502 16.239 87.656 217.518 1.00 44.48 O
ANISOU 3941 O ASP A 502 7273 6538 3089 -1104 87 157 O
ATOM 3942 CB ASP A 502 16.408 88.670 220.386 1.00 43.41 C
ANISOU 3942 CB ASP A 502 7066 6436 2990 -1031 131 230 C
ATOM 3943 CG ASP A 502 17.005 88.141 221.692 1.00 45.12 C
ANISOU 3943 CG ASP A 502 7398 6567 3179 -985 134 253 C
ATOM 3944 OD1 ASP A 502 18.148 87.615 221.639 1.00 45.12 O
ANISOU 3944 OD1 ASP A 502 7491 6481 3172 -884 107 240 O
ATOM 3945 OD2 ASP A 502 16.316 88.230 222.756 1.00 46.55 O
ANISOU 3945 OD2 ASP A 502 7579 6765 3344 -1052 163 284 O
ATOM 3946 N ARG A 503 16.687 89.834 217.186 1.00 42.39 N
ANISOU 3946 N ARG A 503 6760 6440 2907 -982 91 167 N
ATOM 3947 CA ARG A 503 16.026 89.923 215.848 1.00 42.74 C
ANISOU 3947 CA ARG A 503 6761 6539 2939 -1055 71 151 C
ATOM 3948 C ARG A 503 17.002 90.106 214.651 1.00 42.43 C
ANISOU 3948 C ARG A 503 6733 6495 2895 -968 60 115 C
ATOM 3949 O ARG A 503 16.650 90.602 213.561 1.00 41.40 O
ANISOU 3949 O ARG A 503 6537 6434 2760 -999 42 108 O
ATOM 3950 CB ARG A 503 14.942 91.010 215.840 1.00 42.36 C
ANISOU 3950 CB ARG A 503 6545 6618 2931 -1113 71 183 C
ATOM 3951 CG ARG A 503 13.820 90.762 216.830 1.00 43.34 C
ANISOU 3951 CG ARG A 503 6652 6756 3058 -1219 92 213 C
ATOM 3952 CD ARG A 503 12.852 91.927 216.869 1.00 43.37 C
ANISOU 3952 CD ARG A 503 6476 6887 3117 -1250 101 244 C
ATOM 3953 NE ARG A 503 11.545 91.487 217.308 1.00 44.46 N
ANISOU 3953 NE ARG A 503 6592 7049 3252 -1387 115 265 N
ATOM 3954 CZ ARG A 503 11.211 91.293 218.573 1.00 45.96 C
ANISOU 3954 CZ ARG A 503 6801 7219 3443 -1418 162 284 C
ATOM 3955 NH1 ARG A 503 12.105 91.521 219.532 1.00 46.51 N
ANISOU 3955 NH1 ARG A 503 6916 7243 3511 -1319 189 285 N
ATOM 3956 NH2 ARG A 503 9.984 90.871 218.871 1.00 46.34 N
ANISOU 3956 NH2 ARG A 503 6821 7295 3489 -1553 180 302 N
ATOM 3957 N GLY A 504 18.236 89.692 214.890 1.00 42.95 N
ANISOU 3957 N GLY A 504 6882 6477 2959 -860 71 94 N
ATOM 3958 CA GLY A 504 19.248 89.658 213.871 1.00 43.88 C
ANISOU 3958 CA GLY A 504 7029 6572 3071 -775 76 55 C
ATOM 3959 C GLY A 504 19.996 90.961 213.694 1.00 43.83 C
ANISOU 3959 C GLY A 504 6890 6645 3117 -671 87 62 C
ATOM 3960 O GLY A 504 20.728 91.093 212.710 1.00 44.26 O
ANISOU 3960 O GLY A 504 6949 6701 3166 -614 98 33 O
ATOM 3961 N MET A 505 19.822 91.915 214.624 1.00 43.19 N
ANISOU 3961 N MET A 505 6700 6627 3084 -652 90 99 N
ATOM 3962 CA MET A 505 20.505 93.208 214.544 1.00 42.17 C
ANISOU 3962 CA MET A 505 6447 6568 3007 -562 101 107 C
ATOM 3963 C MET A 505 21.870 93.179 215.173 1.00 41.95 C
ANISOU 3963 C MET A 505 6439 6491 3009 -441 110 97 C
ATOM 3964 O MET A 505 22.166 92.331 216.012 1.00 42.80 O
ANISOU 3964 O MET A 505 6639 6520 3105 -421 103 97 O
ATOM 3965 CB MET A 505 19.729 94.272 215.264 1.00 41.81 C
ANISOU 3965 CB MET A 505 6281 6604 3001 -593 103 146 C
ATOM 3966 CG MET A 505 18.455 94.664 214.583 1.00 42.91 C
ANISOU 3966 CG MET A 505 6351 6818 3134 -691 91 164 C
ATOM 3967 SD MET A 505 17.915 96.163 215.423 1.00 43.54 S
ANISOU 3967 SD MET A 505 6274 6988 3280 -677 108 204 S
ATOM 3968 CE MET A 505 18.966 97.350 214.580 1.00 46.00 C
ANISOU 3968 CE MET A 505 6506 7341 3629 -575 113 198 C
ATOM 3969 N ILE A 506 22.702 94.128 214.767 1.00 41.00 N
ANISOU 3969 N ILE A 506 6230 6419 2930 -361 122 91 N
ATOM 3970 CA ILE A 506 23.998 94.344 215.392 1.00 39.94 C
ANISOU 3970 CA ILE A 506 6077 6261 2838 -248 125 86 C
ATOM 3971 C ILE A 506 23.937 95.579 216.302 1.00 38.38 C
ANISOU 3971 C ILE A 506 5767 6129 2686 -234 122 115 C
ATOM 3972 O ILE A 506 23.676 96.695 215.847 1.00 38.50 O
ANISOU 3972 O ILE A 506 5681 6220 2728 -245 133 125 O
ATOM 3973 CB ILE A 506 25.076 94.540 214.329 1.00 39.98 C
ANISOU 3973 CB ILE A 506 6059 6272 2860 -170 149 55 C
ATOM 3974 CG1 ILE A 506 25.317 93.228 213.587 1.00 41.14 C
ANISOU 3974 CG1 ILE A 506 6334 6335 2961 -165 161 18 C
ATOM 3975 CG2 ILE A 506 26.363 95.083 214.958 1.00 40.39 C
ANISOU 3975 CG2 ILE A 506 6045 6329 2973 -61 150 55 C
ATOM 3976 CD1 ILE A 506 26.148 93.382 212.305 1.00 41.63 C
ANISOU 3976 CD1 ILE A 506 6383 6410 3025 -111 200 -18 C
ATOM 3977 N TYR A 507 24.162 95.381 217.584 1.00 36.78 N
ANISOU 3977 N TYR A 507 5593 5893 2489 -211 105 129 N
ATOM 3978 CA TYR A 507 24.203 96.508 218.491 1.00 36.07 C
ANISOU 3978 CA TYR A 507 5414 5856 2436 -196 103 148 C
ATOM 3979 C TYR A 507 25.671 96.945 218.676 1.00 35.96 C
ANISOU 3979 C TYR A 507 5356 5840 2466 -89 92 136 C
ATOM 3980 O TYR A 507 26.571 96.097 218.778 1.00 36.43 O
ANISOU 3980 O TYR A 507 5479 5839 2525 -25 74 123 O
ATOM 3981 CB TYR A 507 23.551 96.138 219.820 1.00 36.27 C
ANISOU 3981 CB TYR A 507 5496 5855 2431 -243 93 171 C
ATOM 3982 CG TYR A 507 23.428 97.298 220.758 1.00 37.39 C
ANISOU 3982 CG TYR A 507 5558 6049 2599 -241 100 185 C
ATOM 3983 CD1 TYR A 507 22.296 98.104 220.732 1.00 38.94 C
ANISOU 3983 CD1 TYR A 507 5682 6307 2806 -306 130 199 C
ATOM 3984 CD2 TYR A 507 24.434 97.595 221.682 1.00 37.30 C
ANISOU 3984 CD2 TYR A 507 5546 6024 2604 -172 75 185 C
ATOM 3985 CE1 TYR A 507 22.163 99.170 221.607 1.00 39.54 C
ANISOU 3985 CE1 TYR A 507 5694 6422 2905 -301 145 207 C
ATOM 3986 CE2 TYR A 507 24.315 98.666 222.541 1.00 36.53 C
ANISOU 3986 CE2 TYR A 507 5387 5969 2522 -177 82 192 C
ATOM 3987 CZ TYR A 507 23.179 99.437 222.505 1.00 39.63 C
ANISOU 3987 CZ TYR A 507 5719 6415 2923 -240 122 201 C
ATOM 3988 OH TYR A 507 23.031 100.510 223.355 1.00 44.74 O
ANISOU 3988 OH TYR A 507 6315 7097 3587 -242 139 202 O
ATOM 3989 N ALA A 508 25.903 98.259 218.719 1.00 35.43 N
ANISOU 3989 N ALA A 508 5179 5839 2445 -72 102 140 N
ATOM 3990 CA ALA A 508 27.235 98.816 218.493 1.00 35.36 C
ANISOU 3990 CA ALA A 508 5104 5845 2485 12 100 125 C
ATOM 3991 C ALA A 508 27.392 100.094 219.278 1.00 34.94 C
ANISOU 3991 C ALA A 508 4966 5840 2470 17 95 136 C
ATOM 3992 O ALA A 508 26.528 100.968 219.214 1.00 34.55 O
ANISOU 3992 O ALA A 508 4866 5835 2426 -34 116 148 O
ATOM 3993 CB ALA A 508 27.435 99.098 216.983 1.00 35.29 C
ANISOU 3993 CB ALA A 508 5052 5866 2489 19 135 110 C
ATOM 3994 N ILE A 509 28.482 100.205 220.025 1.00 35.12 N
ANISOU 3994 N ILE A 509 4973 5851 2520 79 63 130 N
ATOM 3995 CA ILE A 509 28.778 101.454 220.724 1.00 34.83 C
ANISOU 3995 CA ILE A 509 4859 5856 2518 81 56 132 C
ATOM 3996 C ILE A 509 29.939 102.220 220.048 1.00 34.79 C
ANISOU 3996 C ILE A 509 4758 5885 2575 133 65 117 C
ATOM 3997 O ILE A 509 31.061 101.706 219.960 1.00 35.23 O
ANISOU 3997 O ILE A 509 4807 5923 2655 199 44 105 O
ATOM 3998 CB ILE A 509 29.086 101.256 222.256 1.00 35.14 C
ANISOU 3998 CB ILE A 509 4945 5869 2537 93 5 139 C
ATOM 3999 CG1 ILE A 509 27.958 100.516 222.978 1.00 35.28 C
ANISOU 3999 CG1 ILE A 509 5063 5852 2489 35 6 156 C
ATOM 4000 CG2 ILE A 509 29.341 102.597 222.908 1.00 34.90 C
ANISOU 4000 CG2 ILE A 509 4844 5881 2538 85 1 135 C
ATOM 4001 CD1 ILE A 509 28.436 99.671 224.154 1.00 35.88 C
ANISOU 4001 CD1 ILE A 509 5230 5875 2527 61 -50 168 C
ATOM 4002 N ALA A 510 29.672 103.437 219.563 1.00 34.37 N
ANISOU 4002 N ALA A 510 4627 5879 2551 104 99 120 N
ATOM 4003 CA ALA A 510 30.737 104.279 219.019 1.00 34.39 C
ANISOU 4003 CA ALA A 510 4540 5914 2612 139 113 109 C
ATOM 4004 C ALA A 510 31.461 104.944 220.193 1.00 34.52 C
ANISOU 4004 C ALA A 510 4519 5938 2659 153 73 103 C
ATOM 4005 O ALA A 510 30.823 105.585 221.005 1.00 34.30 O
ANISOU 4005 O ALA A 510 4499 5915 2618 113 68 109 O
ATOM 4006 CB ALA A 510 30.149 105.304 218.106 1.00 34.00 C
ANISOU 4006 CB ALA A 510 4438 5903 2577 100 159 120 C
ATOM 4007 N HIS A 511 32.781 104.768 220.290 1.00 34.98 N
ANISOU 4007 N HIS A 511 4536 5998 2757 210 44 90 N
ATOM 4008 CA HIS A 511 33.566 105.332 221.418 1.00 35.27 C
ANISOU 4008 CA HIS A 511 4536 6045 2819 219 -9 83 C
ATOM 4009 C HIS A 511 34.179 106.715 221.108 1.00 35.20 C
ANISOU 4009 C HIS A 511 4425 6079 2872 202 13 73 C
ATOM 4010 O HIS A 511 35.396 106.917 221.179 1.00 35.69 O
ANISOU 4010 O HIS A 511 4415 6160 2985 234 -13 62 O
ATOM 4011 CB HIS A 511 34.622 104.335 221.925 1.00 35.98 C
ANISOU 4011 CB HIS A 511 4638 6113 2920 288 -71 80 C
ATOM 4012 CG HIS A 511 34.037 103.071 222.488 1.00 36.16 C
ANISOU 4012 CG HIS A 511 4777 6082 2879 299 -101 94 C
ATOM 4013 ND1 HIS A 511 33.421 103.019 223.721 1.00 36.16 N
ANISOU 4013 ND1 HIS A 511 4851 6062 2824 261 -140 106 N
ATOM 4014 CD2 HIS A 511 33.975 101.810 221.985 1.00 36.43 C
ANISOU 4014 CD2 HIS A 511 4875 6073 2893 337 -94 97 C
ATOM 4015 CE1 HIS A 511 32.994 101.785 223.940 1.00 36.40 C
ANISOU 4015 CE1 HIS A 511 4985 6042 2805 273 -156 120 C
ATOM 4016 NE2 HIS A 511 33.327 101.030 222.910 1.00 36.58 N
ANISOU 4016 NE2 HIS A 511 5003 6045 2849 320 -131 114 N
ATOM 4017 N VAL A 512 33.323 107.678 220.796 1.00 34.70 N
ANISOU 4017 N VAL A 512 4352 6028 2805 149 58 80 N
ATOM 4018 CA VAL A 512 33.811 108.949 220.312 1.00 34.68 C
ANISOU 4018 CA VAL A 512 4266 6054 2857 129 90 76 C
ATOM 4019 C VAL A 512 34.576 109.778 221.328 1.00 35.02 C
ANISOU 4019 C VAL A 512 4269 6106 2932 115 46 59 C
ATOM 4020 O VAL A 512 34.425 109.631 222.526 1.00 35.16 O
ANISOU 4020 O VAL A 512 4334 6107 2917 106 -4 53 O
ATOM 4021 CB VAL A 512 32.700 109.773 219.655 1.00 34.18 C
ANISOU 4021 CB VAL A 512 4206 5994 2785 85 147 93 C
ATOM 4022 CG1 VAL A 512 32.155 109.017 218.489 1.00 34.00 C
ANISOU 4022 CG1 VAL A 512 4211 5974 2735 94 182 108 C
ATOM 4023 CG2 VAL A 512 31.596 110.106 220.654 1.00 33.92 C
ANISOU 4023 CG2 VAL A 512 4227 5944 2719 49 139 97 C
ATOM 4024 N ARG A 513 35.416 110.654 220.814 1.00 35.25 N
ANISOU 4024 N ARG A 513 4212 6159 3020 105 66 52 N
ATOM 4025 CA ARG A 513 36.141 111.591 221.630 1.00 35.64 C
ANISOU 4025 CA ARG A 513 4218 6218 3105 76 29 34 C
ATOM 4026 C ARG A 513 35.115 112.509 222.271 1.00 35.29 C
ANISOU 4026 C ARG A 513 4227 6150 3032 23 44 33 C
ATOM 4027 O ARG A 513 34.092 112.799 221.663 1.00 34.81 O
ANISOU 4027 O ARG A 513 4190 6078 2957 9 101 50 O
ATOM 4028 CB ARG A 513 37.147 112.366 220.773 1.00 35.99 C
ANISOU 4028 CB ARG A 513 4160 6293 3221 65 64 30 C
ATOM 4029 CG ARG A 513 38.433 111.596 220.476 1.00 36.63 C
ANISOU 4029 CG ARG A 513 4168 6404 3346 119 41 22 C
ATOM 4030 CD ARG A 513 39.353 112.425 219.635 1.00 37.04 C
ANISOU 4030 CD ARG A 513 4117 6490 3468 97 89 18 C
ATOM 4031 NE ARG A 513 38.974 112.297 218.235 1.00 36.74 N
ANISOU 4031 NE ARG A 513 4084 6453 3421 106 175 35 N
ATOM 4032 CZ ARG A 513 39.669 112.759 217.191 1.00 37.10 C
ANISOU 4032 CZ ARG A 513 4057 6527 3513 96 240 37 C
ATOM 4033 NH1 ARG A 513 40.796 113.437 217.379 1.00 37.79 N
ANISOU 4033 NH1 ARG A 513 4046 6644 3669 70 231 24 N
ATOM 4034 NH2 ARG A 513 39.216 112.545 215.958 1.00 36.85 N
ANISOU 4034 NH2 ARG A 513 4053 6496 3454 103 313 54 N
ATOM 4035 N GLY A 514 35.421 112.974 223.482 1.00 35.66 N
ANISOU 4035 N GLY A 514 4288 6188 3071 -4 -8 11 N
ATOM 4036 CA GLY A 514 34.445 113.530 224.398 1.00 35.49 C
ANISOU 4036 CA GLY A 514 4341 6138 3006 -43 -1 1 C
ATOM 4037 C GLY A 514 34.254 112.510 225.505 1.00 35.67 C
ANISOU 4037 C GLY A 514 4442 6149 2962 -28 -60 -2 C
ATOM 4038 O GLY A 514 34.089 112.872 226.677 1.00 35.96 O
ANISOU 4038 O GLY A 514 4534 6170 2959 -60 -90 -22 O
ATOM 4039 N GLY A 515 34.278 111.230 225.104 1.00 35.58 N
ANISOU 4039 N GLY A 515 4443 6142 2933 20 -74 18 N
ATOM 4040 CA GLY A 515 34.363 110.121 226.003 1.00 35.90 C
ANISOU 4040 CA GLY A 515 4553 6169 2919 44 -139 22 C
ATOM 4041 C GLY A 515 35.757 110.091 226.610 1.00 36.67 C
ANISOU 4041 C GLY A 515 4606 6286 3043 62 -226 10 C
ATOM 4042 O GLY A 515 36.609 110.932 226.289 1.00 36.93 O
ANISOU 4042 O GLY A 515 4548 6344 3139 49 -229 -5 O
ATOM 4043 N GLY A 516 36.005 109.114 227.487 1.00 37.15 N
ANISOU 4043 N GLY A 516 4727 6333 3056 90 -301 19 N
ATOM 4044 CA GLY A 516 37.285 108.949 228.151 1.00 38.03 C
ANISOU 4044 CA GLY A 516 4799 6464 3188 114 -402 15 C
ATOM 4045 C GLY A 516 37.739 107.527 227.974 1.00 38.39 C
ANISOU 4045 C GLY A 516 4855 6499 3235 194 -446 40 C
ATOM 4046 O GLY A 516 38.611 107.039 228.708 1.00 39.24 O
ANISOU 4046 O GLY A 516 4957 6611 3340 228 -544 49 O
ATOM 4047 N GLU A 517 37.148 106.844 226.997 1.00 37.86 N
ANISOU 4047 N GLU A 517 4804 6412 3168 224 -376 53 N
ATOM 4048 CA GLU A 517 37.460 105.432 226.793 1.00 38.23 C
ANISOU 4048 CA GLU A 517 4881 6433 3212 300 -406 75 C
ATOM 4049 C GLU A 517 38.971 105.214 226.650 1.00 39.10 C
ANISOU 4049 C GLU A 517 4885 6572 3400 369 -467 73 C
ATOM 4050 O GLU A 517 39.541 104.420 227.388 1.00 39.89 O
ANISOU 4050 O GLU A 517 5012 6656 3487 420 -556 91 O
ATOM 4051 CB GLU A 517 36.644 104.853 225.650 1.00 37.59 C
ANISOU 4051 CB GLU A 517 4830 6329 3124 312 -318 80 C
ATOM 4052 CG GLU A 517 35.154 104.654 225.984 1.00 37.02 C
ANISOU 4052 CG GLU A 517 4872 6223 2969 256 -280 91 C
ATOM 4053 CD GLU A 517 34.168 105.756 225.504 1.00 36.23 C
ANISOU 4053 CD GLU A 517 4751 6144 2871 188 -198 80 C
ATOM 4054 OE1 GLU A 517 34.562 106.910 225.137 1.00 37.04 O
ANISOU 4054 OE1 GLU A 517 4767 6281 3027 168 -175 65 O
ATOM 4055 OE2 GLU A 517 32.950 105.434 225.508 1.00 35.83 O
ANISOU 4055 OE2 GLU A 517 4775 6071 2768 154 -157 91 O
ATOM 4056 N MET A 518 39.625 106.003 225.803 1.00 39.08 N
ANISOU 4056 N MET A 518 4758 6614 3477 365 -424 55 N
ATOM 4057 CA MET A 518 41.060 105.870 225.529 1.00 39.98 C
ANISOU 4057 CA MET A 518 4745 6765 3679 426 -464 51 C
ATOM 4058 C MET A 518 42.002 106.674 226.427 1.00 40.74 C
ANISOU 4058 C MET A 518 4764 6905 3810 396 -555 41 C
ATOM 4059 O MET A 518 43.134 106.991 226.008 1.00 41.40 O
ANISOU 4059 O MET A 518 4709 7036 3983 418 -563 31 O
ATOM 4060 CB MET A 518 41.384 106.273 224.071 1.00 39.74 C
ANISOU 4060 CB MET A 518 4613 6765 3722 434 -362 35 C
ATOM 4061 CG MET A 518 40.697 105.489 222.966 1.00 39.21 C
ANISOU 4061 CG MET A 518 4601 6665 3632 467 -273 39 C
ATOM 4062 SD MET A 518 40.716 103.715 223.235 1.00 39.73 S
ANISOU 4062 SD MET A 518 4760 6672 3666 564 -319 58 S
ATOM 4063 CE MET A 518 42.479 103.347 223.297 1.00 41.12 C
ANISOU 4063 CE MET A 518 4796 6882 3946 664 -381 55 C
ATOM 4064 N GLY A 519 41.559 107.039 227.629 1.00 40.75 N
ANISOU 4064 N GLY A 519 4850 6894 3740 339 -618 41 N
ATOM 4065 CA GLY A 519 42.381 107.894 228.497 1.00 41.52 C
ANISOU 4065 CA GLY A 519 4887 7031 3857 292 -706 27 C
ATOM 4066 C GLY A 519 41.844 109.304 228.663 1.00 41.00 C
ANISOU 4066 C GLY A 519 4835 6970 3772 187 -660 -2 C
ATOM 4067 O GLY A 519 41.061 109.779 227.899 1.00 40.12 O
ANISOU 4067 O GLY A 519 4738 6845 3662 158 -555 -10 O
ATOM 4068 N ARG A 520 42.296 110.000 229.678 1.00 41.66 N
ANISOU 4068 N ARG A 520 4917 7072 3840 130 -744 -19 N
ATOM 4069 CA ARG A 520 41.766 111.324 229.936 1.00 41.30 C
ANISOU 4069 CA ARG A 520 4904 7018 3771 32 -700 -51 C
ATOM 4070 C ARG A 520 41.860 112.217 228.710 1.00 40.83 C
ANISOU 4070 C ARG A 520 4746 6974 3794 6 -597 -64 C
ATOM 4071 O ARG A 520 40.995 113.090 228.533 1.00 40.17 O
ANISOU 4071 O ARG A 520 4711 6862 3689 -51 -518 -79 O
ATOM 4072 CB ARG A 520 42.489 111.979 231.110 1.00 42.32 C
ANISOU 4072 CB ARG A 520 5029 7169 3882 -30 -813 -73 C
ATOM 4073 CG ARG A 520 42.005 113.379 231.448 1.00 42.12 C
ANISOU 4073 CG ARG A 520 5048 7125 3832 -133 -769 -114 C
ATOM 4074 CD ARG A 520 40.764 113.328 232.318 1.00 41.71 C
ANISOU 4074 CD ARG A 520 5164 7022 3662 -162 -748 -120 C
ATOM 4075 NE ARG A 520 40.362 114.660 232.764 1.00 41.74 N
ANISOU 4075 NE ARG A 520 5216 7001 3641 -253 -710 -164 N
ATOM 4076 CZ ARG A 520 39.131 115.023 233.130 1.00 41.21 C
ANISOU 4076 CZ ARG A 520 5268 6886 3503 -284 -634 -180 C
ATOM 4077 NH1 ARG A 520 38.128 114.148 233.117 1.00 40.58 N
ANISOU 4077 NH1 ARG A 520 5268 6783 3367 -240 -588 -154 N
ATOM 4078 NH2 ARG A 520 38.914 116.287 233.513 1.00 41.42 N
ANISOU 4078 NH2 ARG A 520 5331 6887 3519 -362 -601 -224 N
ATOM 4079 N THR A 521 42.885 112.036 227.877 1.00 41.26 N
ANISOU 4079 N THR A 521 4664 7070 3941 47 -593 -58 N
ATOM 4080 CA THR A 521 43.055 112.976 226.772 1.00 40.98 C
ANISOU 4080 CA THR A 521 4541 7051 3978 9 -496 -69 C
ATOM 4081 C THR A 521 42.021 112.782 225.672 1.00 39.90 C
ANISOU 4081 C THR A 521 4450 6884 3825 32 -376 -54 C
ATOM 4082 O THR A 521 41.752 113.674 224.893 1.00 39.50 O
ANISOU 4082 O THR A 521 4376 6829 3802 -11 -291 -59 O
ATOM 4083 CB THR A 521 44.458 112.950 226.184 1.00 41.87 C
ANISOU 4083 CB THR A 521 4490 7223 4197 34 -513 -70 C
ATOM 4084 OG1 THR A 521 44.751 111.629 225.724 1.00 42.02 O
ANISOU 4084 OG1 THR A 521 4480 7250 4234 139 -516 -47 O
ATOM 4085 CG2 THR A 521 45.478 113.403 227.241 1.00 43.06 C
ANISOU 4085 CG2 THR A 521 4578 7410 4371 -13 -636 -87 C
ATOM 4086 N TRP A 522 41.413 111.611 225.641 1.00 39.50 N
ANISOU 4086 N TRP A 522 4474 6810 3724 97 -375 -34 N
ATOM 4087 CA TRP A 522 40.371 111.330 224.682 1.00 38.57 C
ANISOU 4087 CA TRP A 522 4409 6664 3580 113 -276 -19 C
ATOM 4088 C TRP A 522 39.249 112.326 224.916 1.00 37.91 C
ANISOU 4088 C TRP A 522 4400 6551 3454 42 -228 -27 C
ATOM 4089 O TRP A 522 38.384 112.546 224.054 1.00 37.21 O
ANISOU 4089 O TRP A 522 4334 6447 3357 35 -143 -16 O
ATOM 4090 CB TRP A 522 39.878 109.906 224.898 1.00 38.41 C
ANISOU 4090 CB TRP A 522 4474 6616 3503 179 -300 0 C
ATOM 4091 CG TRP A 522 39.093 109.293 223.763 1.00 37.72 C
ANISOU 4091 CG TRP A 522 4422 6510 3401 209 -213 14 C
ATOM 4092 CD1 TRP A 522 37.767 108.951 223.767 1.00 37.01 C
ANISOU 4092 CD1 TRP A 522 4438 6384 3242 194 -177 26 C
ATOM 4093 CD2 TRP A 522 39.592 108.901 222.495 1.00 37.81 C
ANISOU 4093 CD2 TRP A 522 4366 6538 3462 255 -155 17 C
ATOM 4094 NE1 TRP A 522 37.411 108.371 222.587 1.00 36.66 N
ANISOU 4094 NE1 TRP A 522 4398 6333 3199 224 -111 36 N
ATOM 4095 CE2 TRP A 522 38.510 108.339 221.775 1.00 37.13 C
ANISOU 4095 CE2 TRP A 522 4358 6422 3326 262 -92 29 C
ATOM 4096 CE3 TRP A 522 40.836 108.986 221.885 1.00 38.48 C
ANISOU 4096 CE3 TRP A 522 4330 6664 3628 287 -145 8 C
ATOM 4097 CZ2 TRP A 522 38.650 107.859 220.481 1.00 37.10 C
ANISOU 4097 CZ2 TRP A 522 4330 6425 3343 299 -24 31 C
ATOM 4098 CZ3 TRP A 522 40.969 108.514 220.632 1.00 38.46 C
ANISOU 4098 CZ3 TRP A 522 4300 6665 3647 327 -68 9 C
ATOM 4099 CH2 TRP A 522 39.893 107.947 219.932 1.00 37.77 C
ANISOU 4099 CH2 TRP A 522 4306 6545 3501 333 -9 19 C
ATOM 4100 N TYR A 523 39.270 112.929 226.100 1.00 38.26 N
ANISOU 4100 N TYR A 523 4483 6586 3468 -8 -287 -47 N
ATOM 4101 CA TYR A 523 38.251 113.860 226.451 1.00 37.82 C
ANISOU 4101 CA TYR A 523 4501 6496 3373 -67 -241 -59 C
ATOM 4102 C TYR A 523 38.801 115.290 226.410 1.00 38.19 C
ANISOU 4102 C TYR A 523 4490 6548 3474 -135 -228 -84 C
ATOM 4103 O TYR A 523 38.290 116.096 225.664 1.00 37.77 O
ANISOU 4103 O TYR A 523 4430 6476 3445 -160 -146 -80 O
ATOM 4104 CB TYR A 523 37.589 113.431 227.762 1.00 37.89 C
ANISOU 4104 CB TYR A 523 4628 6477 3291 -76 -290 -65 C
ATOM 4105 CG TYR A 523 36.912 114.526 228.547 1.00 37.90 C
ANISOU 4105 CG TYR A 523 4699 6447 3253 -144 -268 -94 C
ATOM 4106 CD1 TYR A 523 35.839 115.240 228.019 1.00 37.27 C
ANISOU 4106 CD1 TYR A 523 4643 6338 3178 -163 -169 -93 C
ATOM 4107 CD2 TYR A 523 37.368 114.853 229.836 1.00 38.66 C
ANISOU 4107 CD2 TYR A 523 4841 6541 3309 -187 -348 -122 C
ATOM 4108 CE1 TYR A 523 35.251 116.266 228.767 1.00 37.41 C
ANISOU 4108 CE1 TYR A 523 4726 6321 3168 -217 -142 -123 C
ATOM 4109 CE2 TYR A 523 36.790 115.847 230.577 1.00 38.80 C
ANISOU 4109 CE2 TYR A 523 4932 6524 3286 -249 -321 -156 C
ATOM 4110 CZ TYR A 523 35.740 116.562 230.050 1.00 38.18 C
ANISOU 4110 CZ TYR A 523 4875 6412 3221 -261 -214 -158 C
ATOM 4111 OH TYR A 523 35.183 117.568 230.813 1.00 38.44 O
ANISOU 4111 OH TYR A 523 4983 6404 3220 -315 -181 -195 O
ATOM 4112 N GLU A 524 39.865 115.599 227.139 1.00 39.07 N
ANISOU 4112 N GLU A 524 4558 6682 3606 -166 -311 -106 N
ATOM 4113 CA GLU A 524 40.285 116.996 227.285 1.00 39.53 C
ANISOU 4113 CA GLU A 524 4583 6733 3703 -247 -304 -135 C
ATOM 4114 C GLU A 524 40.877 117.623 226.040 1.00 39.58 C
ANISOU 4114 C GLU A 524 4480 6759 3799 -263 -238 -126 C
ATOM 4115 O GLU A 524 40.764 118.846 225.840 1.00 39.65 O
ANISOU 4115 O GLU A 524 4491 6740 3834 -327 -190 -140 O
ATOM 4116 CB GLU A 524 41.327 117.146 228.357 1.00 40.60 C
ANISOU 4116 CB GLU A 524 4693 6895 3839 -287 -419 -162 C
ATOM 4117 CG GLU A 524 40.956 116.548 229.656 1.00 40.81 C
ANISOU 4117 CG GLU A 524 4828 6907 3771 -280 -498 -169 C
ATOM 4118 CD GLU A 524 41.843 117.055 230.767 1.00 41.95 C
ANISOU 4118 CD GLU A 524 4968 7069 3903 -346 -609 -202 C
ATOM 4119 OE1 GLU A 524 42.874 117.688 230.486 1.00 42.63 O
ANISOU 4119 OE1 GLU A 524 4945 7187 4066 -388 -636 -215 O
ATOM 4120 OE2 GLU A 524 41.504 116.835 231.934 1.00 42.26 O
ANISOU 4120 OE2 GLU A 524 5116 7089 3851 -363 -671 -215 O
ATOM 4121 N VAL A 525 41.572 116.831 225.234 1.00 39.69 N
ANISOU 4121 N VAL A 525 4402 6817 3860 -206 -235 -105 N
ATOM 4122 CA VAL A 525 42.131 117.371 224.017 1.00 39.81 C
ANISOU 4122 CA VAL A 525 4319 6854 3953 -222 -162 -95 C
ATOM 4123 C VAL A 525 41.192 117.007 222.900 1.00 38.89 C
ANISOU 4123 C VAL A 525 4241 6719 3817 -177 -66 -65 C
ATOM 4124 O VAL A 525 40.859 117.852 222.090 1.00 38.64 O
ANISOU 4124 O VAL A 525 4208 6669 3805 -212 14 -53 O
ATOM 4125 CB VAL A 525 43.597 116.939 223.772 1.00 40.74 C
ANISOU 4125 CB VAL A 525 4296 7037 4147 -201 -204 -96 C
ATOM 4126 CG1 VAL A 525 44.481 117.360 224.959 1.00 41.77 C
ANISOU 4126 CG1 VAL A 525 4387 7188 4293 -256 -316 -125 C
ATOM 4127 CG2 VAL A 525 43.729 115.446 223.583 1.00 40.66 C
ANISOU 4127 CG2 VAL A 525 4274 7050 4127 -98 -227 -78 C
ATOM 4128 N GLY A 526 40.685 115.776 222.919 1.00 38.45 N
ANISOU 4128 N GLY A 526 4233 6662 3713 -106 -79 -50 N
ATOM 4129 CA GLY A 526 39.914 115.226 221.811 1.00 37.73 C
ANISOU 4129 CA GLY A 526 4171 6563 3601 -62 -1 -23 C
ATOM 4130 C GLY A 526 38.502 115.713 221.552 1.00 36.93 C
ANISOU 4130 C GLY A 526 4159 6419 3455 -83 59 -8 C
ATOM 4131 O GLY A 526 38.029 115.675 220.424 1.00 36.53 O
ANISOU 4131 O GLY A 526 4109 6367 3403 -70 128 16 O
ATOM 4132 N GLY A 527 37.816 116.163 222.597 1.00 36.80 N
ANISOU 4132 N GLY A 527 4216 6369 3398 -115 32 -22 N
ATOM 4133 CA GLY A 527 36.377 116.380 222.514 1.00 36.13 C
ANISOU 4133 CA GLY A 527 4213 6246 3269 -118 81 -7 C
ATOM 4134 C GLY A 527 35.826 117.277 223.573 1.00 36.23 C
ANISOU 4134 C GLY A 527 4287 6220 3258 -164 73 -31 C
ATOM 4135 O GLY A 527 35.078 116.853 224.431 1.00 36.06 O
ANISOU 4135 O GLY A 527 4341 6181 3179 -156 54 -38 O
ATOM 4136 N LYS A 528 36.163 118.549 223.499 1.00 36.58 N
ANISOU 4136 N LYS A 528 4307 6244 3346 -215 97 -43 N
ATOM 4137 CA LYS A 528 35.655 119.497 224.486 1.00 36.79 C
ANISOU 4137 CA LYS A 528 4402 6224 3354 -259 98 -72 C
ATOM 4138 C LYS A 528 36.090 120.855 224.002 1.00 37.19 C
ANISOU 4138 C LYS A 528 4417 6248 3465 -311 138 -77 C
ATOM 4139 O LYS A 528 36.956 120.944 223.120 1.00 37.39 O
ANISOU 4139 O LYS A 528 4361 6302 3543 -319 148 -61 O
ATOM 4140 CB LYS A 528 36.235 119.119 225.853 1.00 37.33 C
ANISOU 4140 CB LYS A 528 4499 6302 3381 -277 9 -109 C
ATOM 4141 CG LYS A 528 36.513 120.207 226.846 1.00 38.01 C
ANISOU 4141 CG LYS A 528 4624 6353 3463 -345 -15 -154 C
ATOM 4142 CD LYS A 528 36.765 119.568 228.175 1.00 38.43 C
ANISOU 4142 CD LYS A 528 4733 6420 3450 -352 -103 -181 C
ATOM 4143 CE LYS A 528 36.482 120.540 229.266 1.00 38.97 C
ANISOU 4143 CE LYS A 528 4888 6439 3479 -413 -105 -228 C
ATOM 4144 NZ LYS A 528 36.226 119.747 230.483 1.00 39.18 N
ANISOU 4144 NZ LYS A 528 5002 6471 3413 -406 -165 -243 N
ATOM 4145 N TYR A 529 35.479 121.906 224.527 1.00 37.37 N
ANISOU 4145 N TYR A 529 4503 6212 3483 -345 169 -97 N
ATOM 4146 CA TYR A 529 35.843 123.278 224.178 1.00 37.86 C
ANISOU 4146 CA TYR A 529 4552 6232 3602 -400 207 -103 C
ATOM 4147 C TYR A 529 36.016 123.370 222.689 1.00 37.64 C
ANISOU 4147 C TYR A 529 4458 6221 3622 -386 259 -54 C
ATOM 4148 O TYR A 529 35.228 122.819 221.949 1.00 37.02 O
ANISOU 4148 O TYR A 529 4384 6155 3526 -332 294 -15 O
ATOM 4149 CB TYR A 529 37.145 123.674 224.848 1.00 38.72 C
ANISOU 4149 CB TYR A 529 4627 6352 3733 -468 142 -145 C
ATOM 4150 CG TYR A 529 37.097 124.007 226.314 1.00 39.24 C
ANISOU 4150 CG TYR A 529 4773 6386 3752 -510 93 -200 C
ATOM 4151 CD1 TYR A 529 36.024 124.735 226.867 1.00 39.24 C
ANISOU 4151 CD1 TYR A 529 4874 6314 3722 -515 144 -221 C
ATOM 4152 CD2 TYR A 529 38.156 123.663 227.136 1.00 39.89 C
ANISOU 4152 CD2 TYR A 529 4828 6509 3821 -547 -3 -232 C
ATOM 4153 CE1 TYR A 529 35.998 125.092 228.231 1.00 39.86 C
ANISOU 4153 CE1 TYR A 529 5038 6359 3747 -560 107 -279 C
ATOM 4154 CE2 TYR A 529 38.141 123.993 228.502 1.00 40.50 C
ANISOU 4154 CE2 TYR A 529 4990 6557 3842 -594 -55 -285 C
ATOM 4155 CZ TYR A 529 37.065 124.713 229.046 1.00 40.48 C
ANISOU 4155 CZ TYR A 529 5100 6480 3800 -604 4 -311 C
ATOM 4156 OH TYR A 529 37.084 125.032 230.397 1.00 41.19 O
ANISOU 4156 OH TYR A 529 5284 6541 3826 -655 -41 -368 O
ATOM 4157 N LEU A 530 37.058 124.035 222.213 1.00 38.22 N
ANISOU 4157 N LEU A 530 4472 6298 3751 -438 265 -54 N
ATOM 4158 CA LEU A 530 37.187 124.179 220.757 1.00 38.09 C
ANISOU 4158 CA LEU A 530 4407 6296 3772 -429 326 -5 C
ATOM 4159 C LEU A 530 37.621 122.910 220.045 1.00 37.77 C
ANISOU 4159 C LEU A 530 4300 6330 3722 -380 316 16 C
ATOM 4160 O LEU A 530 38.150 122.999 218.979 1.00 37.95 O
ANISOU 4160 O LEU A 530 4268 6375 3776 -389 357 43 O
ATOM 4161 CB LEU A 530 38.110 125.327 220.368 1.00 38.90 C
ANISOU 4161 CB LEU A 530 4469 6374 3935 -507 352 -7 C
ATOM 4162 CG LEU A 530 37.696 126.683 220.898 1.00 39.34 C
ANISOU 4162 CG LEU A 530 4600 6340 4005 -557 375 -25 C
ATOM 4163 CD1 LEU A 530 38.720 127.714 220.497 1.00 40.22 C
ANISOU 4163 CD1 LEU A 530 4672 6432 4179 -644 398 -27 C
ATOM 4164 CD2 LEU A 530 36.366 127.066 220.421 1.00 38.88 C
ANISOU 4164 CD2 LEU A 530 4611 6228 3934 -510 434 13 C
ATOM 4165 N THR A 531 37.421 121.734 220.606 1.00 37.39 N
ANISOU 4165 N THR A 531 4263 6315 3630 -330 266 4 N
ATOM 4166 CA THR A 531 37.540 120.556 219.786 1.00 37.05 C
ANISOU 4166 CA THR A 531 4181 6322 3573 -274 273 28 C
ATOM 4167 C THR A 531 36.335 119.667 220.006 1.00 36.32 C
ANISOU 4167 C THR A 531 4158 6224 3418 -219 266 39 C
ATOM 4168 O THR A 531 36.452 118.449 219.838 1.00 36.11 O
ANISOU 4168 O THR A 531 4120 6233 3366 -172 244 43 O
ATOM 4169 CB THR A 531 38.806 119.714 220.075 1.00 37.51 C
ANISOU 4169 CB THR A 531 4162 6438 3653 -261 217 5 C
ATOM 4170 OG1 THR A 531 38.680 119.061 221.358 1.00 37.48 O
ANISOU 4170 OG1 THR A 531 4198 6434 3608 -241 138 -22 O
ATOM 4171 CG2 THR A 531 40.076 120.552 220.018 1.00 38.39 C
ANISOU 4171 CG2 THR A 531 4189 6565 3833 -324 215 -11 C
ATOM 4172 N LYS A 532 35.191 120.246 220.389 1.00 36.04 N
ANISOU 4172 N LYS A 532 4192 6142 3360 -225 286 44 N
ATOM 4173 CA LYS A 532 33.948 119.477 220.560 1.00 35.44 C
ANISOU 4173 CA LYS A 532 4174 6063 3230 -181 288 57 C
ATOM 4174 C LYS A 532 33.379 118.882 219.255 1.00 35.01 C
ANISOU 4174 C LYS A 532 4110 6031 3161 -146 326 102 C
ATOM 4175 O LYS A 532 32.662 117.861 219.297 1.00 34.60 O
ANISOU 4175 O LYS A 532 4090 5993 3064 -112 313 110 O
ATOM 4176 CB LYS A 532 32.883 120.295 221.272 1.00 35.41 C
ANISOU 4176 CB LYS A 532 4233 6007 3215 -194 310 49 C
ATOM 4177 CG LYS A 532 31.596 119.545 221.606 1.00 34.94 C
ANISOU 4177 CG LYS A 532 4224 5948 3105 -158 315 59 C
ATOM 4178 CD LYS A 532 31.861 118.228 222.357 1.00 34.84 C
ANISOU 4178 CD LYS A 532 4230 5965 3041 -141 258 39 C
ATOM 4179 CE LYS A 532 30.572 117.493 222.739 1.00 34.47 C
ANISOU 4179 CE LYS A 532 4239 5917 2943 -119 268 48 C
ATOM 4180 NZ LYS A 532 30.822 116.355 223.712 1.00 34.53 N
ANISOU 4180 NZ LYS A 532 4286 5938 2895 -112 212 27 N
ATOM 4181 N ARG A 533 33.713 119.469 218.106 1.00 35.18 N
ANISOU 4181 N ARG A 533 4096 6055 3215 -160 370 130 N
ATOM 4182 CA ARG A 533 33.176 118.874 216.889 1.00 34.87 C
ANISOU 4182 CA ARG A 533 4060 6039 3149 -131 399 171 C
ATOM 4183 C ARG A 533 33.662 117.448 216.611 1.00 34.75 C
ANISOU 4183 C ARG A 533 4031 6068 3105 -97 377 160 C
ATOM 4184 O ARG A 533 33.022 116.736 215.832 1.00 34.47 O
ANISOU 4184 O ARG A 533 4019 6047 3030 -74 391 184 O
ATOM 4185 CB ARG A 533 33.303 119.758 215.655 1.00 35.13 C
ANISOU 4185 CB ARG A 533 4076 6065 3207 -153 453 211 C
ATOM 4186 CG ARG A 533 32.898 121.177 215.894 1.00 35.37 C
ANISOU 4186 CG ARG A 533 4127 6040 3272 -182 475 223 C
ATOM 4187 CD ARG A 533 33.194 122.048 214.747 1.00 35.77 C
ANISOU 4187 CD ARG A 533 4166 6077 3347 -208 524 265 C
ATOM 4188 NE ARG A 533 31.954 122.237 214.016 1.00 35.58 N
ANISOU 4188 NE ARG A 533 4181 6039 3300 -183 541 318 N
ATOM 4189 CZ ARG A 533 31.688 121.730 212.806 1.00 35.51 C
ANISOU 4189 CZ ARG A 533 4177 6063 3252 -170 555 359 C
ATOM 4190 NH1 ARG A 533 32.582 120.975 212.195 1.00 35.59 N
ANISOU 4190 NH1 ARG A 533 4160 6120 3243 -175 566 348 N
ATOM 4191 NH2 ARG A 533 30.501 121.964 212.247 1.00 35.45 N
ANISOU 4191 NH2 ARG A 533 4200 6043 3225 -149 556 410 N
ATOM 4192 N ASN A 534 34.742 117.006 217.260 1.00 35.05 N
ANISOU 4192 N ASN A 534 4033 6124 3160 -92 340 125 N
ATOM 4193 CA ASN A 534 35.175 115.635 217.028 1.00 35.04 C
ANISOU 4193 CA ASN A 534 4023 6155 3137 -48 321 115 C
ATOM 4194 C ASN A 534 34.124 114.674 217.518 1.00 34.57 C
ANISOU 4194 C ASN A 534 4033 6084 3019 -22 292 117 C
ATOM 4195 O ASN A 534 33.969 113.591 216.962 1.00 34.45 O
ANISOU 4195 O ASN A 534 4039 6081 2971 10 295 123 O
ATOM 4196 CB ASN A 534 36.499 115.288 217.693 1.00 35.57 C
ANISOU 4196 CB ASN A 534 4033 6243 3239 -37 277 82 C
ATOM 4197 CG ASN A 534 37.675 115.978 217.076 1.00 36.18 C
ANISOU 4197 CG ASN A 534 4024 6344 3377 -63 311 80 C
ATOM 4198 OD1 ASN A 534 37.689 116.264 215.882 1.00 36.23 O
ANISOU 4198 OD1 ASN A 534 4017 6359 3389 -72 376 103 O
ATOM 4199 ND2 ASN A 534 38.695 116.252 217.894 1.00 36.74 N
ANISOU 4199 ND2 ASN A 534 4038 6429 3494 -80 265 52 N
ATOM 4200 N THR A 535 33.393 115.048 218.559 1.00 34.39 N
ANISOU 4200 N THR A 535 4051 6034 2982 -38 269 110 N
ATOM 4201 CA THR A 535 32.430 114.093 219.105 1.00 34.06 C
ANISOU 4201 CA THR A 535 4073 5983 2884 -20 246 111 C
ATOM 4202 C THR A 535 31.594 113.672 217.929 1.00 33.76 C
ANISOU 4202 C THR A 535 4051 5955 2820 -12 282 143 C
ATOM 4203 O THR A 535 31.386 112.473 217.706 1.00 33.65 O
ANISOU 4203 O THR A 535 4070 5949 2768 10 269 143 O
ATOM 4204 CB THR A 535 31.503 114.675 220.162 1.00 33.94 C
ANISOU 4204 CB THR A 535 4102 5940 2853 -43 242 104 C
ATOM 4205 OG1 THR A 535 32.210 114.830 221.385 1.00 34.28 O
ANISOU 4205 OG1 THR A 535 4152 5974 2899 -55 197 70 O
ATOM 4206 CG2 THR A 535 30.425 113.744 220.411 1.00 33.65 C
ANISOU 4206 CG2 THR A 535 4120 5900 2764 -33 238 113 C
ATOM 4207 N PHE A 536 31.174 114.660 217.146 1.00 33.72 N
ANISOU 4207 N PHE A 536 4028 5948 2836 -31 323 170 N
ATOM 4208 CA PHE A 536 30.202 114.400 216.099 1.00 33.52 C
ANISOU 4208 CA PHE A 536 4023 5933 2780 -30 347 206 C
ATOM 4209 C PHE A 536 30.838 113.774 214.901 1.00 33.67 C
ANISOU 4209 C PHE A 536 4032 5977 2785 -18 364 212 C
ATOM 4210 O PHE A 536 30.258 112.942 214.271 1.00 33.57 O
ANISOU 4210 O PHE A 536 4053 5975 2727 -13 364 224 O
ATOM 4211 CB PHE A 536 29.392 115.660 215.753 1.00 33.53 C
ANISOU 4211 CB PHE A 536 4015 5919 2806 -49 376 240 C
ATOM 4212 CG PHE A 536 28.958 116.431 216.975 1.00 33.54 C
ANISOU 4212 CG PHE A 536 4025 5888 2831 -57 373 224 C
ATOM 4213 CD1 PHE A 536 28.349 115.790 218.029 1.00 33.38 C
ANISOU 4213 CD1 PHE A 536 4039 5863 2782 -53 351 203 C
ATOM 4214 CD2 PHE A 536 29.203 117.792 217.085 1.00 33.81 C
ANISOU 4214 CD2 PHE A 536 4041 5891 2913 -72 397 227 C
ATOM 4215 CE1 PHE A 536 27.963 116.514 219.160 1.00 33.50 C
ANISOU 4215 CE1 PHE A 536 4070 5847 2811 -62 358 184 C
ATOM 4216 CE2 PHE A 536 28.834 118.501 218.232 1.00 33.92 C
ANISOU 4216 CE2 PHE A 536 4074 5869 2945 -80 400 204 C
ATOM 4217 CZ PHE A 536 28.225 117.863 219.269 1.00 33.77 C
ANISOU 4217 CZ PHE A 536 4089 5850 2893 -74 382 181 C
ATOM 4218 N MET A 537 32.054 114.152 214.596 1.00 34.01 N
ANISOU 4218 N MET A 537 4030 6029 2864 -18 383 200 N
ATOM 4219 CA MET A 537 32.683 113.618 213.403 1.00 34.28 C
ANISOU 4219 CA MET A 537 4054 6087 2883 -6 416 203 C
ATOM 4220 C MET A 537 33.249 112.225 213.575 1.00 34.40 C
ANISOU 4220 C MET A 537 4081 6109 2879 34 397 171 C
ATOM 4221 O MET A 537 33.222 111.437 212.616 1.00 34.53 O
ANISOU 4221 O MET A 537 4127 6136 2857 48 421 172 O
ATOM 4222 CB MET A 537 33.669 114.609 212.837 1.00 34.71 C
ANISOU 4222 CB MET A 537 4053 6152 2984 -26 459 209 C
ATOM 4223 CG MET A 537 32.881 115.826 212.547 1.00 34.63 C
ANISOU 4223 CG MET A 537 4054 6122 2980 -60 477 249 C
ATOM 4224 SD MET A 537 33.687 116.942 211.456 1.00 41.47 S
ANISOU 4224 SD MET A 537 4886 6993 3878 -95 540 276 S
ATOM 4225 CE MET A 537 33.188 116.231 209.851 1.00 40.90 C
ANISOU 4225 CE MET A 537 4864 6949 3729 -89 573 309 C
ATOM 4226 N ASP A 538 33.727 111.922 214.782 1.00 34.44 N
ANISOU 4226 N ASP A 538 4074 6104 2906 53 352 143 N
ATOM 4227 CA ASP A 538 34.131 110.593 215.100 1.00 34.60 C
ANISOU 4227 CA ASP A 538 4116 6120 2908 98 323 119 C
ATOM 4228 C ASP A 538 32.929 109.647 214.930 1.00 34.26 C
ANISOU 4228 C ASP A 538 4158 6060 2799 97 313 130 C
ATOM 4229 O ASP A 538 33.051 108.588 214.348 1.00 34.45 O
ANISOU 4229 O ASP A 538 4217 6080 2793 123 322 120 O
ATOM 4230 CB ASP A 538 34.671 110.541 216.527 1.00 34.74 C
ANISOU 4230 CB ASP A 538 4118 6129 2952 111 263 98 C
ATOM 4231 CG ASP A 538 36.084 111.200 216.686 1.00 35.29 C
ANISOU 4231 CG ASP A 538 4095 6222 3092 114 261 81 C
ATOM 4232 OD1 ASP A 538 36.694 111.750 215.694 1.00 36.14 O
ANISOU 4232 OD1 ASP A 538 4145 6353 3233 104 316 86 O
ATOM 4233 OD2 ASP A 538 36.574 111.166 217.851 1.00 35.52 O
ANISOU 4233 OD2 ASP A 538 4110 6248 3140 122 200 64 O
ATOM 4234 N PHE A 539 31.765 110.053 215.412 1.00 33.86 N
ANISOU 4234 N PHE A 539 4137 5999 2728 63 298 148 N
ATOM 4235 CA PHE A 539 30.542 109.258 215.326 1.00 33.62 C
ANISOU 4235 CA PHE A 539 4173 5958 2641 49 287 161 C
ATOM 4236 C PHE A 539 30.194 108.929 213.880 1.00 33.70 C
ANISOU 4236 C PHE A 539 4206 5983 2617 39 319 176 C
ATOM 4237 O PHE A 539 29.977 107.770 213.500 1.00 33.83 O
ANISOU 4237 O PHE A 539 4278 5989 2588 46 314 166 O
ATOM 4238 CB PHE A 539 29.371 109.998 216.018 1.00 33.30 C
ANISOU 4238 CB PHE A 539 4138 5913 2601 14 280 180 C
ATOM 4239 CG PHE A 539 28.193 109.118 216.309 1.00 33.16 C
ANISOU 4239 CG PHE A 539 4179 5886 2535 -4 263 187 C
ATOM 4240 CD1 PHE A 539 28.213 108.237 217.387 1.00 33.21 C
ANISOU 4240 CD1 PHE A 539 4234 5869 2518 4 231 169 C
ATOM 4241 CD2 PHE A 539 27.078 109.140 215.491 1.00 33.09 C
ANISOU 4241 CD2 PHE A 539 4179 5893 2502 -34 275 216 C
ATOM 4242 CE1 PHE A 539 27.141 107.393 217.641 1.00 33.18 C
ANISOU 4242 CE1 PHE A 539 4286 5854 2468 -23 221 177 C
ATOM 4243 CE2 PHE A 539 25.996 108.289 215.723 1.00 33.08 C
ANISOU 4243 CE2 PHE A 539 4223 5887 2458 -62 259 222 C
ATOM 4244 CZ PHE A 539 26.024 107.418 216.807 1.00 33.12 C
ANISOU 4244 CZ PHE A 539 4276 5865 2441 -59 237 202 C
ATOM 4245 N ILE A 540 30.168 109.977 213.079 1.00 33.73 N
ANISOU 4245 N ILE A 540 4172 6006 2637 19 352 200 N
ATOM 4246 CA ILE A 540 29.902 109.918 211.663 1.00 33.92 C
ANISOU 4246 CA ILE A 540 4215 6048 2623 3 381 220 C
ATOM 4247 C ILE A 540 30.905 108.988 210.980 1.00 34.33 C
ANISOU 4247 C ILE A 540 4286 6102 2657 34 409 189 C
ATOM 4248 O ILE A 540 30.536 108.197 210.122 1.00 34.53 O
ANISOU 4248 O ILE A 540 4368 6127 2623 25 418 187 O
ATOM 4249 CB ILE A 540 29.902 111.388 211.099 1.00 33.97 C
ANISOU 4249 CB ILE A 540 4178 6070 2661 -19 411 256 C
ATOM 4250 CG1 ILE A 540 28.497 111.986 211.294 1.00 33.72 C
ANISOU 4250 CG1 ILE A 540 4151 6037 2626 -45 387 294 C
ATOM 4251 CG2 ILE A 540 30.337 111.444 209.648 1.00 34.39 C
ANISOU 4251 CG2 ILE A 540 4241 6143 2683 -28 455 269 C
ATOM 4252 CD1 ILE A 540 28.418 113.480 211.367 1.00 33.75 C
ANISOU 4252 CD1 ILE A 540 4112 6033 2679 -55 403 324 C
ATOM 4253 N ALA A 541 32.172 109.079 211.392 1.00 34.57 N
ANISOU 4253 N ALA A 541 4265 6131 2737 69 422 163 N
ATOM 4254 CA ALA A 541 33.220 108.175 210.925 1.00 35.08 C
ANISOU 4254 CA ALA A 541 4333 6195 2801 113 451 130 C
ATOM 4255 C ALA A 541 32.934 106.686 211.240 1.00 35.15 C
ANISOU 4255 C ALA A 541 4416 6169 2769 142 421 106 C
ATOM 4256 O ALA A 541 33.083 105.826 210.366 1.00 35.54 O
ANISOU 4256 O ALA A 541 4516 6210 2779 158 453 87 O
ATOM 4257 CB ALA A 541 34.544 108.603 211.459 1.00 35.39 C
ANISOU 4257 CB ALA A 541 4288 6245 2915 144 459 111 C
ATOM 4258 N CYS A 542 32.484 106.393 212.464 1.00 34.83 N
ANISOU 4258 N CYS A 542 4394 6107 2734 144 364 106 N
ATOM 4259 CA CYS A 542 32.159 105.027 212.870 1.00 34.94 C
ANISOU 4259 CA CYS A 542 4487 6080 2708 164 333 90 C
ATOM 4260 C CYS A 542 31.076 104.478 212.016 1.00 34.90 C
ANISOU 4260 C CYS A 542 4559 6068 2633 121 342 98 C
ATOM 4261 O CYS A 542 31.030 103.288 211.717 1.00 35.24 O
ANISOU 4261 O CYS A 542 4677 6078 2636 135 343 77 O
ATOM 4262 CB CYS A 542 31.646 105.002 214.281 1.00 34.61 C
ANISOU 4262 CB CYS A 542 4460 6020 2671 153 277 98 C
ATOM 4263 SG CYS A 542 32.891 105.480 215.438 1.00 34.80 S
ANISOU 4263 SG CYS A 542 4410 6048 2764 198 245 86 S
ATOM 4264 N ALA A 543 30.183 105.356 211.608 1.00 34.57 N
ANISOU 4264 N ALA A 543 4501 6057 2579 67 346 130 N
ATOM 4265 CA ALA A 543 29.044 104.892 210.890 1.00 34.60 C
ANISOU 4265 CA ALA A 543 4567 6062 2517 18 339 143 C
ATOM 4266 C ALA A 543 29.409 104.671 209.443 1.00 35.07 C
ANISOU 4266 C ALA A 543 4657 6132 2535 16 383 133 C
ATOM 4267 O ALA A 543 28.852 103.803 208.801 1.00 35.35 O
ANISOU 4267 O ALA A 543 4770 6154 2507 -12 378 123 O
ATOM 4268 CB ALA A 543 27.923 105.849 211.042 1.00 34.22 C
ANISOU 4268 CB ALA A 543 4485 6041 2474 -31 319 184 C
ATOM 4269 N GLU A 544 30.353 105.432 208.920 1.00 35.24 N
ANISOU 4269 N GLU A 544 4624 6177 2589 39 428 132 N
ATOM 4270 CA GLU A 544 30.754 105.228 207.524 1.00 35.80 C
ANISOU 4270 CA GLU A 544 4730 6260 2612 35 482 120 C
ATOM 4271 C GLU A 544 31.506 103.898 207.409 1.00 36.34 C
ANISOU 4271 C GLU A 544 4854 6289 2665 86 508 68 C
ATOM 4272 O GLU A 544 31.339 103.178 206.410 1.00 36.84 O
ANISOU 4272 O GLU A 544 4998 6340 2658 71 535 48 O
ATOM 4273 CB GLU A 544 31.666 106.357 207.065 1.00 35.96 C
ANISOU 4273 CB GLU A 544 4676 6313 2675 46 535 132 C
ATOM 4274 CG GLU A 544 31.082 107.742 207.114 1.00 35.58 C
ANISOU 4274 CG GLU A 544 4578 6292 2649 5 518 184 C
ATOM 4275 CD GLU A 544 30.999 108.330 205.733 1.00 37.16 C
ANISOU 4275 CD GLU A 544 4799 6520 2801 -31 559 212 C
ATOM 4276 OE1 GLU A 544 30.426 107.631 204.856 1.00 38.69 O
ANISOU 4276 OE1 GLU A 544 5073 6715 2912 -58 557 209 O
ATOM 4277 OE2 GLU A 544 31.513 109.471 205.513 1.00 37.94 O
ANISOU 4277 OE2 GLU A 544 4841 6635 2937 -38 593 237 O
ATOM 4278 N HIS A 545 32.317 103.602 208.450 1.00 36.32 N
ANISOU 4278 N HIS A 545 4811 6264 2727 146 496 47 N
ATOM 4279 CA HIS A 545 33.089 102.342 208.597 1.00 36.90 C
ANISOU 4279 CA HIS A 545 4926 6290 2804 213 510 3 C
ATOM 4280 C HIS A 545 32.147 101.185 208.627 1.00 36.96 C
ANISOU 4280 C HIS A 545 5048 6249 2745 188 476 -8 C
ATOM 4281 O HIS A 545 32.409 100.152 208.021 1.00 37.59 O
ANISOU 4281 O HIS A 545 5207 6289 2788 213 508 -45 O
ATOM 4282 CB HIS A 545 33.940 102.294 209.893 1.00 36.87 C
ANISOU 4282 CB HIS A 545 4856 6272 2881 277 476 -4 C
ATOM 4283 CG HIS A 545 34.669 100.985 210.117 1.00 38.63 C
ANISOU 4283 CG HIS A 545 5122 6440 3115 356 480 -41 C
ATOM 4284 ND1 HIS A 545 35.981 100.778 209.727 1.00 41.06 N
ANISOU 4284 ND1 HIS A 545 5378 6751 3471 432 534 -72 N
ATOM 4285 CD2 HIS A 545 34.270 99.825 210.700 1.00 37.97 C
ANISOU 4285 CD2 HIS A 545 5130 6294 3004 374 437 -50 C
ATOM 4286 CE1 HIS A 545 36.343 99.544 210.038 1.00 39.59 C
ANISOU 4286 CE1 HIS A 545 5249 6503 3289 500 524 -98 C
ATOM 4287 NE2 HIS A 545 35.323 98.944 210.624 1.00 38.51 N
ANISOU 4287 NE2 HIS A 545 5206 6323 3104 464 464 -85 N
ATOM 4288 N LEU A 546 31.049 101.335 209.344 1.00 36.38 N
ANISOU 4288 N LEU A 546 4988 6177 2659 135 417 22 N
ATOM 4289 CA LEU A 546 30.120 100.238 209.375 1.00 36.52 C
ANISOU 4289 CA LEU A 546 5112 6150 2615 98 386 14 C
ATOM 4290 C LEU A 546 29.567 99.965 207.970 1.00 36.92 C
ANISOU 4290 C LEU A 546 5233 6209 2585 43 412 5 C
ATOM 4291 O LEU A 546 29.425 98.804 207.572 1.00 37.47 O
ANISOU 4291 O LEU A 546 5407 6228 2601 37 419 -28 O
ATOM 4292 CB LEU A 546 29.051 100.444 210.452 1.00 35.95 C
ANISOU 4292 CB LEU A 546 5031 6080 2547 49 326 48 C
ATOM 4293 CG LEU A 546 29.600 100.042 211.829 1.00 35.90 C
ANISOU 4293 CG LEU A 546 5020 6035 2586 103 295 42 C
ATOM 4294 CD1 LEU A 546 28.821 100.600 213.003 1.00 35.34 C
ANISOU 4294 CD1 LEU A 546 4917 5980 2532 65 252 74 C
ATOM 4295 CD2 LEU A 546 29.643 98.549 211.898 1.00 36.47 C
ANISOU 4295 CD2 LEU A 546 5203 6034 2621 122 288 15 C
ATOM 4296 N ILE A 547 29.343 101.028 207.199 1.00 36.76 N
ANISOU 4296 N ILE A 547 5164 6247 2554 6 429 32 N
ATOM 4297 CA ILE A 547 28.743 100.895 205.861 1.00 37.18 C
ANISOU 4297 CA ILE A 547 5286 6319 2523 -54 441 32 C
ATOM 4298 C ILE A 547 29.702 100.348 204.814 1.00 37.98 C
ANISOU 4298 C ILE A 547 5445 6400 2587 -18 515 -15 C
ATOM 4299 O ILE A 547 29.356 99.432 204.087 1.00 38.57 O
ANISOU 4299 O ILE A 547 5628 6444 2583 -49 521 -46 O
ATOM 4300 CB ILE A 547 28.042 102.203 205.396 1.00 36.85 C
ANISOU 4300 CB ILE A 547 5183 6343 2476 -109 423 87 C
ATOM 4301 CG1 ILE A 547 26.759 102.415 206.229 1.00 36.32 C
ANISOU 4301 CG1 ILE A 547 5089 6288 2424 -158 352 126 C
ATOM 4302 CG2 ILE A 547 27.727 102.167 203.919 1.00 37.46 C
ANISOU 4302 CG2 ILE A 547 5327 6443 2462 -160 440 89 C
ATOM 4303 CD1 ILE A 547 26.413 103.867 206.527 1.00 35.81 C
ANISOU 4303 CD1 ILE A 547 4923 6271 2412 -165 337 179 C
ATOM 4304 N SER A 548 30.904 100.898 204.765 1.00 38.09 N
ANISOU 4304 N SER A 548 5385 6430 2656 45 573 -24 N
ATOM 4305 CA SER A 548 31.906 100.458 203.789 1.00 38.95 C
ANISOU 4305 CA SER A 548 5533 6526 2740 87 659 -71 C
ATOM 4306 C SER A 548 32.595 99.109 204.121 1.00 39.54 C
ANISOU 4306 C SER A 548 5666 6529 2830 163 684 -128 C
ATOM 4307 O SER A 548 33.144 98.452 203.234 1.00 40.42 O
ANISOU 4307 O SER A 548 5845 6613 2899 190 755 -176 O
ATOM 4308 CB SER A 548 32.957 101.551 203.595 1.00 38.98 C
ANISOU 4308 CB SER A 548 5427 6579 2806 122 720 -59 C
ATOM 4309 OG SER A 548 33.696 101.714 204.784 1.00 38.67 O
ANISOU 4309 OG SER A 548 5291 6532 2869 187 703 -59 O
ATOM 4310 N SER A 549 32.580 98.689 205.376 1.00 39.18 N
ANISOU 4310 N SER A 549 5601 6446 2840 199 629 -124 N
ATOM 4311 CA SER A 549 33.081 97.358 205.668 1.00 39.83 C
ANISOU 4311 CA SER A 549 5756 6449 2929 268 642 -170 C
ATOM 4312 C SER A 549 31.991 96.347 205.317 1.00 40.09 C
ANISOU 4312 C SER A 549 5935 6428 2868 200 612 -187 C
ATOM 4313 O SER A 549 32.195 95.149 205.409 1.00 40.73 O
ANISOU 4313 O SER A 549 6111 6430 2935 240 621 -226 O
ATOM 4314 CB SER A 549 33.496 97.223 207.138 1.00 39.51 C
ANISOU 4314 CB SER A 549 5654 6383 2974 331 588 -155 C
ATOM 4315 OG SER A 549 32.372 97.038 207.971 1.00 38.92 O
ANISOU 4315 OG SER A 549 5620 6290 2876 271 509 -125 O
ATOM 4316 N GLY A 550 30.818 96.850 204.946 1.00 39.65 N
ANISOU 4316 N GLY A 550 5895 6416 2754 97 570 -153 N
ATOM 4317 CA GLY A 550 29.669 96.023 204.587 1.00 39.92 C
ANISOU 4317 CA GLY A 550 6053 6415 2700 12 531 -163 C
ATOM 4318 C GLY A 550 28.796 95.490 205.719 1.00 39.53 C
ANISOU 4318 C GLY A 550 6029 6328 2662 -24 455 -141 C
ATOM 4319 O GLY A 550 27.883 94.713 205.461 1.00 39.87 O
ANISOU 4319 O GLY A 550 6176 6338 2637 -99 424 -152 O
ATOM 4320 N LEU A 551 29.028 95.900 206.966 1.00 38.90 N
ANISOU 4320 N LEU A 551 5862 6256 2662 20 425 -111 N
ATOM 4321 CA LEU A 551 28.170 95.437 208.063 1.00 38.59 C
ANISOU 4321 CA LEU A 551 5852 6185 2627 -21 360 -88 C
ATOM 4322 C LEU A 551 26.727 95.896 207.935 1.00 38.21 C
ANISOU 4322 C LEU A 551 5790 6188 2538 -135 313 -50 C
ATOM 4323 O LEU A 551 25.813 95.199 208.352 1.00 38.33 O
ANISOU 4323 O LEU A 551 5869 6171 2522 -199 273 -45 O
ATOM 4324 CB LEU A 551 28.706 95.870 209.427 1.00 38.06 C
ANISOU 4324 CB LEU A 551 5698 6121 2643 43 337 -63 C
ATOM 4325 CG LEU A 551 30.023 95.355 209.991 1.00 38.46 C
ANISOU 4325 CG LEU A 551 5745 6119 2750 158 355 -87 C
ATOM 4326 CD1 LEU A 551 29.907 95.392 211.496 1.00 41.04 C
ANISOU 4326 CD1 LEU A 551 6045 6432 3117 172 298 -55 C
ATOM 4327 CD2 LEU A 551 30.375 93.940 209.546 1.00 42.55 C
ANISOU 4327 CD2 LEU A 551 6392 6543 3232 196 383 -134 C
ATOM 4328 N THR A 552 26.533 97.070 207.360 1.00 37.84 N
ANISOU 4328 N THR A 552 5659 6221 2496 -159 317 -21 N
ATOM 4329 CA THR A 552 25.243 97.732 207.319 1.00 37.48 C
ANISOU 4329 CA THR A 552 5569 6236 2435 -247 270 24 C
ATOM 4330 C THR A 552 25.204 98.655 206.103 1.00 37.55 C
ANISOU 4330 C THR A 552 5542 6311 2416 -270 286 42 C
ATOM 4331 O THR A 552 26.228 98.906 205.452 1.00 37.77 O
ANISOU 4331 O THR A 552 5566 6341 2444 -216 340 21 O
ATOM 4332 CB THR A 552 25.069 98.545 208.612 1.00 36.71 C
ANISOU 4332 CB THR A 552 5370 6166 2414 -228 247 63 C
ATOM 4333 OG1 THR A 552 24.791 97.632 209.662 1.00 37.20 O
ANISOU 4333 OG1 THR A 552 5485 6171 2479 -235 223 56 O
ATOM 4334 CG2 THR A 552 23.944 99.519 208.558 1.00 36.36 C
ANISOU 4334 CG2 THR A 552 5249 6190 2376 -291 214 113 C
ATOM 4335 N THR A 553 24.004 99.126 205.799 1.00 37.49 N
ANISOU 4335 N THR A 553 5507 6355 2382 -350 238 82 N
ATOM 4336 CA THR A 553 23.756 100.165 204.822 1.00 37.53 C
ANISOU 4336 CA THR A 553 5466 6428 2367 -375 234 118 C
ATOM 4337 C THR A 553 22.886 101.175 205.581 1.00 36.93 C
ANISOU 4337 C THR A 553 5279 6401 2354 -393 192 177 C
ATOM 4338 O THR A 553 22.212 100.818 206.524 1.00 36.73 O
ANISOU 4338 O THR A 553 5240 6363 2354 -416 162 183 O
ATOM 4339 CB THR A 553 23.005 99.600 203.577 1.00 38.33 C
ANISOU 4339 CB THR A 553 5659 6541 2364 -462 203 111 C
ATOM 4340 OG1 THR A 553 21.680 99.207 203.948 1.00 38.42 O
ANISOU 4340 OG1 THR A 553 5671 6564 2364 -544 135 132 O
ATOM 4341 CG2 THR A 553 23.722 98.391 203.028 1.00 39.02 C
ANISOU 4341 CG2 THR A 553 5876 6562 2388 -449 247 43 C
ATOM 4342 N PRO A 554 22.889 102.437 205.171 1.00 36.75 N
ANISOU 4342 N PRO A 554 5179 6429 2354 -381 195 220 N
ATOM 4343 CA PRO A 554 22.037 103.361 205.922 1.00 36.29 C
ANISOU 4343 CA PRO A 554 5020 6409 2360 -390 161 271 C
ATOM 4344 C PRO A 554 20.546 102.977 205.971 1.00 36.59 C
ANISOU 4344 C PRO A 554 5054 6472 2375 -470 97 296 C
ATOM 4345 O PRO A 554 19.921 103.194 206.989 1.00 36.27 O
ANISOU 4345 O PRO A 554 4951 6438 2390 -473 83 314 O
ATOM 4346 CB PRO A 554 22.214 104.697 205.187 1.00 36.29 C
ANISOU 4346 CB PRO A 554 4962 6452 2373 -373 170 316 C
ATOM 4347 CG PRO A 554 23.462 104.528 204.360 1.00 36.56 C
ANISOU 4347 CG PRO A 554 5054 6469 2369 -340 227 282 C
ATOM 4348 CD PRO A 554 23.530 103.072 204.007 1.00 37.05 C
ANISOU 4348 CD PRO A 554 5225 6493 2359 -367 229 228 C
ATOM 4349 N ALA A 555 19.947 102.421 204.927 1.00 37.27 N
ANISOU 4349 N ALA A 555 5203 6577 2383 -540 58 297 N
ATOM 4350 CA ALA A 555 18.530 102.039 205.088 1.00 37.63 C
ANISOU 4350 CA ALA A 555 5228 6651 2418 -622 -6 320 C
ATOM 4351 C ALA A 555 18.280 101.018 206.244 1.00 37.50 C
ANISOU 4351 C ALA A 555 5240 6587 2420 -642 0 287 C
ATOM 4352 O ALA A 555 17.139 100.801 206.679 1.00 37.72 O
ANISOU 4352 O ALA A 555 5230 6639 2462 -706 -39 308 O
ATOM 4353 CB ALA A 555 17.921 101.553 203.795 1.00 38.51 C
ANISOU 4353 CB ALA A 555 5406 6791 2436 -705 -59 323 C
ATOM 4354 N GLN A 556 19.346 100.412 206.743 1.00 37.23 N
ANISOU 4354 N GLN A 556 5270 6487 2389 -588 48 240 N
ATOM 4355 CA GLN A 556 19.242 99.413 207.800 1.00 37.20 C
ANISOU 4355 CA GLN A 556 5313 6427 2393 -602 54 212 C
ATOM 4356 C GLN A 556 19.909 99.884 209.094 1.00 36.49 C
ANISOU 4356 C GLN A 556 5171 6315 2378 -522 90 213 C
ATOM 4357 O GLN A 556 20.071 99.118 210.055 1.00 36.44 O
ANISOU 4357 O GLN A 556 5212 6256 2379 -515 100 191 O
ATOM 4358 CB GLN A 556 19.948 98.148 207.346 1.00 37.67 C
ANISOU 4358 CB GLN A 556 5510 6415 2389 -601 72 155 C
ATOM 4359 CG GLN A 556 19.467 97.552 206.024 1.00 38.50 C
ANISOU 4359 CG GLN A 556 5698 6527 2404 -681 42 139 C
ATOM 4360 CD GLN A 556 20.302 96.353 205.694 1.00 38.99 C
ANISOU 4360 CD GLN A 556 5900 6504 2412 -662 77 76 C
ATOM 4361 OE1 GLN A 556 20.069 95.250 206.194 1.00 39.33 O
ANISOU 4361 OE1 GLN A 556 6026 6482 2437 -697 70 49 O
ATOM 4362 NE2 GLN A 556 21.333 96.572 204.909 1.00 39.09 N
ANISOU 4362 NE2 GLN A 556 5940 6509 2403 -600 122 51 N
ATOM 4363 N LEU A 557 20.323 101.147 209.113 1.00 36.02 N
ANISOU 4363 N LEU A 557 5023 6292 2370 -465 109 238 N
ATOM 4364 CA LEU A 557 21.085 101.672 210.214 1.00 35.44 C
ANISOU 4364 CA LEU A 557 4905 6200 2360 -393 140 233 C
ATOM 4365 C LEU A 557 20.279 102.691 211.012 1.00 35.11 C
ANISOU 4365 C LEU A 557 4763 6199 2378 -399 134 273 C
ATOM 4366 O LEU A 557 19.616 103.562 210.448 1.00 35.18 O
ANISOU 4366 O LEU A 557 4704 6260 2402 -416 119 311 O
ATOM 4367 CB LEU A 557 22.345 102.311 209.690 1.00 35.25 C
ANISOU 4367 CB LEU A 557 4865 6177 2353 -322 174 223 C
ATOM 4368 CG LEU A 557 23.213 103.000 210.716 1.00 34.75 C
ANISOU 4368 CG LEU A 557 4745 6101 2357 -253 200 219 C
ATOM 4369 CD1 LEU A 557 23.887 102.004 211.614 1.00 34.78 C
ANISOU 4369 CD1 LEU A 557 4809 6045 2360 -219 203 183 C
ATOM 4370 CD2 LEU A 557 24.222 103.807 209.975 1.00 34.70 C
ANISOU 4370 CD2 LEU A 557 4705 6111 2369 -206 232 218 C
ATOM 4371 N SER A 558 20.367 102.562 212.334 1.00 34.84 N
ANISOU 4371 N SER A 558 4726 6138 2375 -380 147 263 N
ATOM 4372 CA SER A 558 19.771 103.487 213.266 1.00 34.58 C
ANISOU 4372 CA SER A 558 4611 6131 2397 -376 158 289 C
ATOM 4373 C SER A 558 20.796 103.928 214.302 1.00 34.16 C
ANISOU 4373 C SER A 558 4551 6047 2381 -309 183 270 C
ATOM 4374 O SER A 558 21.852 103.303 214.454 1.00 34.13 O
ANISOU 4374 O SER A 558 4606 6001 2361 -272 185 239 O
ATOM 4375 CB SER A 558 18.587 102.803 213.969 1.00 34.89 C
ANISOU 4375 CB SER A 558 4661 6172 2424 -444 149 296 C
ATOM 4376 OG SER A 558 18.991 101.635 214.681 1.00 35.76 O
ANISOU 4376 OG SER A 558 4867 6222 2499 -451 151 266 O
ATOM 4377 N CYS A 559 20.478 104.992 215.033 1.00 33.93 N
ANISOU 4377 N CYS A 559 4452 6039 2403 -293 201 286 N
ATOM 4378 CA CYS A 559 21.340 105.463 216.107 1.00 33.63 C
ANISOU 4378 CA CYS A 559 4410 5974 2395 -244 219 267 C
ATOM 4379 C CYS A 559 20.534 105.903 217.273 1.00 33.65 C
ANISOU 4379 C CYS A 559 4382 5982 2419 -261 238 275 C
ATOM 4380 O CYS A 559 19.387 106.258 217.136 1.00 33.83 O
ANISOU 4380 O CYS A 559 4356 6039 2460 -294 247 300 O
ATOM 4381 CB CYS A 559 22.209 106.632 215.660 1.00 33.39 C
ANISOU 4381 CB CYS A 559 4326 5955 2407 -194 232 270 C
ATOM 4382 SG CYS A 559 21.333 108.130 215.125 1.00 33.41 S
ANISOU 4382 SG CYS A 559 4234 6000 2459 -198 246 314 S
ATOM 4383 N GLU A 560 21.156 105.878 218.437 1.00 33.54 N
ANISOU 4383 N GLU A 560 4401 5937 2406 -236 245 252 N
ATOM 4384 CA GLU A 560 20.522 106.300 219.666 1.00 33.63 C
ANISOU 4384 CA GLU A 560 4401 5948 2429 -251 272 251 C
ATOM 4385 C GLU A 560 21.529 107.025 220.586 1.00 33.46 C
ANISOU 4385 C GLU A 560 4384 5904 2426 -206 277 228 C
ATOM 4386 O GLU A 560 22.737 106.636 220.687 1.00 33.38 O
ANISOU 4386 O GLU A 560 4413 5868 2403 -173 248 209 O
ATOM 4387 CB GLU A 560 19.914 105.089 220.352 1.00 33.95 C
ANISOU 4387 CB GLU A 560 4513 5969 2418 -301 270 248 C
ATOM 4388 CG GLU A 560 19.231 105.406 221.677 1.00 37.41 C
ANISOU 4388 CG GLU A 560 4952 6407 2855 -324 309 246 C
ATOM 4389 CD GLU A 560 18.848 104.165 222.492 1.00 42.70 C
ANISOU 4389 CD GLU A 560 5711 7047 3465 -375 309 243 C
ATOM 4390 OE1 GLU A 560 19.249 103.016 222.103 1.00 43.28 O
ANISOU 4390 OE1 GLU A 560 5856 7089 3499 -384 273 241 O
ATOM 4391 OE2 GLU A 560 18.148 104.372 223.532 1.00 44.63 O
ANISOU 4391 OE2 GLU A 560 5959 7296 3701 -404 352 242 O
ATOM 4392 N GLY A 561 21.008 108.089 221.220 1.00 33.51 N
ANISOU 4392 N GLY A 561 4346 5920 2465 -205 313 229 N
ATOM 4393 CA GLY A 561 21.702 108.896 222.236 1.00 33.49 C
ANISOU 4393 CA GLY A 561 4352 5896 2475 -179 323 203 C
ATOM 4394 C GLY A 561 20.732 109.408 223.295 1.00 33.79 C
ANISOU 4394 C GLY A 561 4388 5934 2515 -200 373 197 C
ATOM 4395 O GLY A 561 19.549 109.466 223.074 1.00 33.98 O
ANISOU 4395 O GLY A 561 4372 5983 2555 -224 406 217 O
ATOM 4396 N ARG A 562 21.252 109.779 224.457 1.00 33.92 N
ANISOU 4396 N ARG A 562 4448 5926 2515 -194 379 168 N
ATOM 4397 CA ARG A 562 20.453 110.313 225.540 1.00 34.31 C
ANISOU 4397 CA ARG A 562 4508 5970 2557 -212 436 153 C
ATOM 4398 C ARG A 562 21.267 111.432 226.198 1.00 34.37 C
ANISOU 4398 C ARG A 562 4525 5952 2581 -188 440 120 C
ATOM 4399 O ARG A 562 22.484 111.331 226.314 1.00 34.24 O
ANISOU 4399 O ARG A 562 4538 5921 2551 -173 386 105 O
ATOM 4400 CB ARG A 562 20.114 109.205 226.566 1.00 34.65 C
ANISOU 4400 CB ARG A 562 4639 6001 2526 -254 439 147 C
ATOM 4401 CG ARG A 562 18.695 108.529 226.406 1.00 36.22 C
ANISOU 4401 CG ARG A 562 4819 6226 2716 -301 481 172 C
ATOM 4402 CD ARG A 562 18.144 107.698 227.659 1.00 39.54 C
ANISOU 4402 CD ARG A 562 5327 6632 3063 -355 513 165 C
ATOM 4403 NE ARG A 562 18.741 108.195 228.914 1.00 43.40 N
ANISOU 4403 NE ARG A 562 5886 7092 3512 -346 523 132 N
ATOM 4404 CZ ARG A 562 18.124 108.920 229.850 1.00 44.61 C
ANISOU 4404 CZ ARG A 562 6046 7245 3658 -359 597 109 C
ATOM 4405 NH1 ARG A 562 16.817 109.230 229.750 1.00 44.76 N
ANISOU 4405 NH1 ARG A 562 5997 7294 3716 -377 677 118 N
ATOM 4406 NH2 ARG A 562 18.834 109.323 230.908 1.00 44.71 N
ANISOU 4406 NH2 ARG A 562 6136 7228 3624 -354 590 76 N
ATOM 4407 N SER A 563 20.577 112.484 226.642 1.00 34.67 N
ANISOU 4407 N SER A 563 4538 5985 2650 -184 504 107 N
ATOM 4408 CA SER A 563 21.164 113.595 227.363 1.00 34.89 C
ANISOU 4408 CA SER A 563 4587 5981 2688 -172 518 70 C
ATOM 4409 C SER A 563 22.188 114.266 226.476 1.00 34.55 C
ANISOU 4409 C SER A 563 4499 5931 2697 -143 477 75 C
ATOM 4410 O SER A 563 21.857 114.682 225.372 1.00 34.35 O
ANISOU 4410 O SER A 563 4404 5920 2728 -122 489 105 O
ATOM 4411 CB SER A 563 21.760 113.123 228.677 1.00 35.19 C
ANISOU 4411 CB SER A 563 4726 5998 2648 -198 493 36 C
ATOM 4412 OG SER A 563 22.028 114.217 229.544 1.00 35.60 O
ANISOU 4412 OG SER A 563 4810 6019 2698 -199 521 -6 O
ATOM 4413 N ALA A 564 23.432 114.367 226.922 1.00 34.57 N
ANISOU 4413 N ALA A 564 4539 5916 2680 -145 428 47 N
ATOM 4414 CA ALA A 564 24.478 114.826 226.009 1.00 34.30 C
ANISOU 4414 CA ALA A 564 4456 5884 2694 -125 390 55 C
ATOM 4415 C ALA A 564 24.565 114.006 224.717 1.00 33.88 C
ANISOU 4415 C ALA A 564 4359 5860 2652 -110 363 94 C
ATOM 4416 O ALA A 564 24.849 114.556 223.682 1.00 33.71 O
ANISOU 4416 O ALA A 564 4283 5845 2679 -95 365 113 O
ATOM 4417 CB ALA A 564 25.800 114.893 226.695 1.00 34.50 C
ANISOU 4417 CB ALA A 564 4516 5895 2698 -135 334 22 C
ATOM 4418 N GLY A 565 24.284 112.704 224.777 1.00 33.79 N
ANISOU 4418 N GLY A 565 4382 5864 2592 -119 341 105 N
ATOM 4419 CA GLY A 565 24.153 111.857 223.575 1.00 33.49 C
ANISOU 4419 CA GLY A 565 4319 5851 2557 -112 324 138 C
ATOM 4420 C GLY A 565 23.032 112.291 222.645 1.00 33.42 C
ANISOU 4420 C GLY A 565 4252 5863 2584 -113 363 171 C
ATOM 4421 O GLY A 565 23.081 112.040 221.427 1.00 33.23 O
ANISOU 4421 O GLY A 565 4196 5859 2573 -106 349 197 O
ATOM 4422 N GLY A 566 22.002 112.915 223.225 1.00 33.68 N
ANISOU 4422 N GLY A 566 4273 5892 2632 -122 413 170 N
ATOM 4423 CA GLY A 566 20.951 113.568 222.452 1.00 33.78 C
ANISOU 4423 CA GLY A 566 4218 5922 2693 -112 449 203 C
ATOM 4424 C GLY A 566 21.581 114.682 221.625 1.00 33.69 C
ANISOU 4424 C GLY A 566 4164 5899 2736 -83 446 215 C
ATOM 4425 O GLY A 566 21.242 114.868 220.415 1.00 33.64 O
ANISOU 4425 O GLY A 566 4110 5914 2757 -73 439 256 O
ATOM 4426 N LEU A 567 22.524 115.402 222.250 1.00 33.74 N
ANISOU 4426 N LEU A 567 4194 5873 2753 -77 447 182 N
ATOM 4427 CA LEU A 567 23.275 116.445 221.553 1.00 33.73 C
ANISOU 4427 CA LEU A 567 4162 5855 2801 -60 446 190 C
ATOM 4428 C LEU A 567 23.984 115.780 220.404 1.00 33.43 C
ANISOU 4428 C LEU A 567 4109 5844 2751 -60 406 212 C
ATOM 4429 O LEU A 567 23.962 116.280 219.268 1.00 33.43 O
ANISOU 4429 O LEU A 567 4071 5852 2780 -50 411 248 O
ATOM 4430 CB LEU A 567 24.305 117.105 222.486 1.00 33.92 C
ANISOU 4430 CB LEU A 567 4218 5841 2827 -69 442 144 C
ATOM 4431 CG LEU A 567 25.456 117.951 221.924 1.00 33.96 C
ANISOU 4431 CG LEU A 567 4201 5830 2873 -69 430 143 C
ATOM 4432 CD1 LEU A 567 24.948 119.185 221.128 1.00 34.17 C
ANISOU 4432 CD1 LEU A 567 4191 5831 2959 -53 471 177 C
ATOM 4433 CD2 LEU A 567 26.430 118.346 223.031 1.00 34.24 C
ANISOU 4433 CD2 LEU A 567 4272 5837 2900 -91 411 91 C
ATOM 4434 N LEU A 568 24.602 114.634 220.687 1.00 33.27 N
ANISOU 4434 N LEU A 568 4122 5835 2684 -68 369 193 N
ATOM 4435 CA LEU A 568 25.355 113.983 219.669 1.00 33.10 C
ANISOU 4435 CA LEU A 568 4091 5833 2651 -62 341 205 C
ATOM 4436 C LEU A 568 24.375 113.644 218.545 1.00 33.04 C
ANISOU 4436 C LEU A 568 4064 5853 2635 -66 348 246 C
ATOM 4437 O LEU A 568 24.639 113.988 217.388 1.00 33.04 O
ANISOU 4437 O LEU A 568 4038 5865 2651 -60 350 272 O
ATOM 4438 CB LEU A 568 26.102 112.790 220.236 1.00 33.06 C
ANISOU 4438 CB LEU A 568 4129 5829 2603 -60 302 178 C
ATOM 4439 CG LEU A 568 26.892 111.852 219.332 1.00 33.00 C
ANISOU 4439 CG LEU A 568 4122 5836 2579 -45 278 181 C
ATOM 4440 CD1 LEU A 568 27.817 110.964 220.151 1.00 33.13 C
ANISOU 4440 CD1 LEU A 568 4176 5840 2572 -30 236 152 C
ATOM 4441 CD2 LEU A 568 25.915 111.020 218.519 1.00 32.91 C
ANISOU 4441 CD2 LEU A 568 4128 5841 2534 -57 281 207 C
ATOM 4442 N VAL A 569 23.229 113.047 218.879 1.00 33.08 N
ANISOU 4442 N VAL A 569 4082 5869 2616 -82 351 255 N
ATOM 4443 CA VAL A 569 22.253 112.680 217.824 1.00 33.14 C
ANISOU 4443 CA VAL A 569 4067 5909 2615 -95 346 295 C
ATOM 4444 C VAL A 569 21.823 113.897 216.929 1.00 33.32 C
ANISOU 4444 C VAL A 569 4034 5939 2686 -79 362 336 C
ATOM 4445 O VAL A 569 21.852 113.847 215.674 1.00 33.37 O
ANISOU 4445 O VAL A 569 4029 5967 2682 -82 345 368 O
ATOM 4446 CB VAL A 569 20.998 111.920 218.381 1.00 33.30 C
ANISOU 4446 CB VAL A 569 4097 5944 2610 -124 350 299 C
ATOM 4447 CG1 VAL A 569 20.029 111.588 217.259 1.00 33.48 C
ANISOU 4447 CG1 VAL A 569 4088 6005 2627 -145 334 340 C
ATOM 4448 CG2 VAL A 569 21.393 110.635 219.043 1.00 33.21 C
ANISOU 4448 CG2 VAL A 569 4154 5921 2545 -143 330 269 C
ATOM 4449 N GLY A 570 21.451 114.980 217.609 1.00 33.50 N
ANISOU 4449 N GLY A 570 4033 5939 2757 -62 395 335 N
ATOM 4450 CA GLY A 570 20.917 116.166 216.962 1.00 33.80 C
ANISOU 4450 CA GLY A 570 4023 5972 2847 -39 412 377 C
ATOM 4451 C GLY A 570 21.915 116.830 216.044 1.00 33.78 C
ANISOU 4451 C GLY A 570 4021 5955 2857 -30 407 393 C
ATOM 4452 O GLY A 570 21.539 117.286 214.943 1.00 34.01 O
ANISOU 4452 O GLY A 570 4026 5998 2900 -22 399 444 O
ATOM 4453 N ALA A 571 23.179 116.891 216.478 1.00 33.59 N
ANISOU 4453 N ALA A 571 4024 5909 2830 -35 410 353 N
ATOM 4454 CA ALA A 571 24.217 117.429 215.616 1.00 33.64 C
ANISOU 4454 CA ALA A 571 4026 5908 2849 -35 412 365 C
ATOM 4455 C ALA A 571 24.348 116.498 214.406 1.00 33.56 C
ANISOU 4455 C ALA A 571 4023 5938 2789 -46 388 388 C
ATOM 4456 O ALA A 571 24.311 116.934 213.263 1.00 33.78 O
ANISOU 4456 O ALA A 571 4043 5974 2816 -48 390 430 O
ATOM 4457 CB ALA A 571 25.513 117.577 216.360 1.00 33.57 C
ANISOU 4457 CB ALA A 571 4031 5876 2849 -43 415 317 C
ATOM 4458 N VAL A 572 24.427 115.203 214.660 1.00 33.33 N
ANISOU 4458 N VAL A 572 4020 5929 2715 -56 367 360 N
ATOM 4459 CA VAL A 572 24.740 114.237 213.620 1.00 33.32 C
ANISOU 4459 CA VAL A 572 4041 5956 2663 -66 350 366 C
ATOM 4460 C VAL A 572 23.633 114.117 212.577 1.00 33.54 C
ANISOU 4460 C VAL A 572 4065 6013 2664 -81 333 415 C
ATOM 4461 O VAL A 572 23.917 113.933 211.384 1.00 33.72 O
ANISOU 4461 O VAL A 572 4104 6054 2652 -91 329 434 O
ATOM 4462 CB VAL A 572 25.016 112.892 214.254 1.00 33.13 C
ANISOU 4462 CB VAL A 572 4055 5933 2600 -70 331 325 C
ATOM 4463 CG1 VAL A 572 24.829 111.790 213.254 1.00 33.22 C
ANISOU 4463 CG1 VAL A 572 4100 5967 2554 -85 314 332 C
ATOM 4464 CG2 VAL A 572 26.413 112.879 214.878 1.00 33.07 C
ANISOU 4464 CG2 VAL A 572 4049 5907 2611 -52 335 284 C
ATOM 4465 N LEU A 573 22.372 114.211 213.031 1.00 33.62 N
ANISOU 4465 N LEU A 573 4053 6031 2690 -85 323 433 N
ATOM 4466 CA LEU A 573 21.244 114.377 212.103 1.00 33.98 C
ANISOU 4466 CA LEU A 573 4075 6108 2728 -96 299 488 C
ATOM 4467 C LEU A 573 21.268 115.709 211.368 1.00 34.31 C
ANISOU 4467 C LEU A 573 4090 6138 2806 -74 308 538 C
ATOM 4468 O LEU A 573 20.758 115.796 210.241 1.00 34.68 O
ANISOU 4468 O LEU A 573 4134 6213 2830 -85 280 588 O
ATOM 4469 CB LEU A 573 19.885 114.157 212.762 1.00 34.14 C
ANISOU 4469 CB LEU A 573 4060 6144 2765 -104 289 498 C
ATOM 4470 CG LEU A 573 19.557 112.781 213.393 1.00 33.98 C
ANISOU 4470 CG LEU A 573 4071 6138 2704 -138 277 462 C
ATOM 4471 CD1 LEU A 573 18.114 112.784 213.982 1.00 34.31 C
ANISOU 4471 CD1 LEU A 573 4061 6201 2774 -150 279 480 C
ATOM 4472 CD2 LEU A 573 19.761 111.544 212.491 1.00 34.01 C
ANISOU 4472 CD2 LEU A 573 4126 6161 2635 -175 243 456 C
ATOM 4473 N ASN A 574 21.846 116.754 211.957 1.00 34.26 N
ANISOU 4473 N ASN A 574 4073 6091 2854 -50 344 527 N
ATOM 4474 CA ASN A 574 21.991 117.999 211.194 1.00 34.65 C
ANISOU 4474 CA ASN A 574 4112 6118 2934 -34 356 576 C
ATOM 4475 C ASN A 574 22.982 117.832 210.048 1.00 34.72 C
ANISOU 4475 C ASN A 574 4155 6139 2896 -55 358 586 C
ATOM 4476 O ASN A 574 22.765 118.400 208.956 1.00 35.16 O
ANISOU 4476 O ASN A 574 4218 6201 2941 -57 348 644 O
ATOM 4477 CB ASN A 574 22.417 119.173 212.062 1.00 34.69 C
ANISOU 4477 CB ASN A 574 4107 6066 3007 -11 396 558 C
ATOM 4478 CG ASN A 574 21.257 119.907 212.621 1.00 35.01 C
ANISOU 4478 CG ASN A 574 4113 6087 3103 22 405 580 C
ATOM 4479 OD1 ASN A 574 20.197 119.935 211.995 1.00 35.38 O
ANISOU 4479 OD1 ASN A 574 4130 6160 3153 34 378 634 O
ATOM 4480 ND2 ASN A 574 21.419 120.481 213.822 1.00 34.98 N
ANISOU 4480 ND2 ASN A 574 4110 6037 3143 36 442 538 N
ATOM 4481 N MET A 575 24.043 117.044 210.276 1.00 34.38 N
ANISOU 4481 N MET A 575 4137 6101 2826 -68 371 532 N
ATOM 4482 CA MET A 575 25.138 116.957 209.300 1.00 34.54 C
ANISOU 4482 CA MET A 575 4183 6129 2812 -84 392 532 C
ATOM 4483 C MET A 575 25.002 115.856 208.290 1.00 34.66 C
ANISOU 4483 C MET A 575 4236 6184 2748 -104 372 536 C
ATOM 4484 O MET A 575 25.130 116.094 207.114 1.00 35.07 O
ANISOU 4484 O MET A 575 4312 6250 2761 -120 378 573 O
ATOM 4485 CB MET A 575 26.473 116.835 210.003 1.00 34.32 C
ANISOU 4485 CB MET A 575 4148 6083 2808 -81 422 475 C
ATOM 4486 CG MET A 575 26.581 117.727 211.229 1.00 34.21 C
ANISOU 4486 CG MET A 575 4107 6029 2862 -69 433 455 C
ATOM 4487 SD MET A 575 28.003 117.236 212.215 1.00 34.00 S
ANISOU 4487 SD MET A 575 4070 5997 2852 -70 441 384 S
ATOM 4488 CE MET A 575 28.233 118.699 213.257 1.00 34.15 C
ANISOU 4488 CE MET A 575 4069 5964 2944 -74 458 372 C
ATOM 4489 N ARG A 576 24.746 114.645 208.763 1.00 34.38 N
ANISOU 4489 N ARG A 576 4216 6163 2684 -109 350 498 N
ATOM 4490 CA ARG A 576 24.712 113.449 207.916 1.00 34.53 C
ANISOU 4490 CA ARG A 576 4286 6210 2625 -131 334 486 C
ATOM 4491 C ARG A 576 23.441 112.659 208.142 1.00 34.51 C
ANISOU 4491 C ARG A 576 4289 6226 2596 -151 286 492 C
ATOM 4492 O ARG A 576 23.472 111.461 208.394 1.00 34.39 O
ANISOU 4492 O ARG A 576 4310 6211 2545 -163 276 452 O
ATOM 4493 CB ARG A 576 25.933 112.553 208.184 1.00 34.37 C
ANISOU 4493 CB ARG A 576 4290 6179 2592 -119 363 425 C
ATOM 4494 CG ARG A 576 27.276 113.083 207.657 1.00 34.60 C
ANISOU 4494 CG ARG A 576 4310 6203 2634 -109 416 416 C
ATOM 4495 CD ARG A 576 27.203 113.509 206.187 1.00 35.13 C
ANISOU 4495 CD ARG A 576 4408 6290 2651 -134 432 462 C
ATOM 4496 NE ARG A 576 26.820 112.422 205.303 1.00 35.41 N
ANISOU 4496 NE ARG A 576 4507 6348 2599 -156 415 455 N
ATOM 4497 CZ ARG A 576 27.636 111.455 204.878 1.00 35.62 C
ANISOU 4497 CZ ARG A 576 4575 6376 2583 -152 449 408 C
ATOM 4498 NH1 ARG A 576 28.909 111.412 205.265 1.00 35.59 N
ANISOU 4498 NH1 ARG A 576 4543 6359 2621 -121 499 367 N
ATOM 4499 NH2 ARG A 576 27.172 110.529 204.046 1.00 35.96 N
ANISOU 4499 NH2 ARG A 576 4690 6433 2542 -178 432 401 N
ATOM 4500 N PRO A 577 22.302 113.333 208.030 1.00 34.73 N
ANISOU 4500 N PRO A 577 4281 6268 2646 -156 257 544 N
ATOM 4501 CA PRO A 577 21.016 112.677 208.250 1.00 34.83 C
ANISOU 4501 CA PRO A 577 4282 6308 2646 -181 212 554 C
ATOM 4502 C PRO A 577 20.809 111.481 207.330 1.00 35.13 C
ANISOU 4502 C PRO A 577 4379 6372 2596 -227 179 545 C
ATOM 4503 O PRO A 577 20.045 110.591 207.672 1.00 35.16 O
ANISOU 4503 O PRO A 577 4389 6389 2582 -258 150 531 O
ATOM 4504 CB PRO A 577 20.025 113.757 207.874 1.00 35.26 C
ANISOU 4504 CB PRO A 577 4283 6378 2737 -171 187 622 C
ATOM 4505 CG PRO A 577 20.797 114.694 206.928 1.00 35.51 C
ANISOU 4505 CG PRO A 577 4333 6398 2761 -157 206 656 C
ATOM 4506 CD PRO A 577 22.153 114.717 207.538 1.00 35.05 C
ANISOU 4506 CD PRO A 577 4291 6302 2722 -139 263 601 C
ATOM 4507 N ASP A 578 21.474 111.495 206.164 1.00 35.42 N
ANISOU 4507 N ASP A 578 4465 6416 2578 -236 188 553 N
ATOM 4508 CA ASP A 578 21.437 110.426 205.124 1.00 35.84 C
ANISOU 4508 CA ASP A 578 4594 6489 2535 -281 166 539 C
ATOM 4509 C ASP A 578 21.976 109.071 205.587 1.00 35.61 C
ANISOU 4509 C ASP A 578 4620 6434 2476 -287 184 469 C
ATOM 4510 O ASP A 578 21.726 108.064 204.959 1.00 35.98 O
ANISOU 4510 O ASP A 578 4733 6488 2450 -328 162 450 O
ATOM 4511 CB ASP A 578 22.317 110.836 203.959 1.00 36.21 C
ANISOU 4511 CB ASP A 578 4685 6537 2534 -280 198 551 C
ATOM 4512 CG ASP A 578 23.739 111.124 204.400 1.00 35.85 C
ANISOU 4512 CG ASP A 578 4632 6458 2530 -237 270 512 C
ATOM 4513 OD1 ASP A 578 23.960 112.236 204.906 1.00 35.63 O
ANISOU 4513 OD1 ASP A 578 4547 6416 2574 -208 290 535 O
ATOM 4514 OD2 ASP A 578 24.622 110.255 204.273 1.00 35.86 O
ANISOU 4514 OD2 ASP A 578 4680 6446 2498 -232 307 458 O
ATOM 4515 N LEU A 579 22.743 109.077 206.674 1.00 35.09 N
ANISOU 4515 N LEU A 579 4533 6335 2466 -244 222 431 N
ATOM 4516 CA LEU A 579 23.349 107.892 207.183 1.00 34.94 C
ANISOU 4516 CA LEU A 579 4563 6284 2429 -236 238 372 C
ATOM 4517 C LEU A 579 22.370 107.039 207.982 1.00 34.86 C
ANISOU 4517 C LEU A 579 4563 6268 2415 -267 201 361 C
ATOM 4518 O LEU A 579 22.632 105.846 208.233 1.00 34.92 O
ANISOU 4518 O LEU A 579 4633 6245 2389 -274 202 318 O
ATOM 4519 CB LEU A 579 24.555 108.269 208.029 1.00 34.55 C
ANISOU 4519 CB LEU A 579 4482 6206 2440 -180 281 342 C
ATOM 4520 CG LEU A 579 25.836 108.752 207.293 1.00 34.74 C
ANISOU 4520 CG LEU A 579 4505 6230 2467 -153 333 334 C
ATOM 4521 CD1 LEU A 579 26.966 108.824 208.266 1.00 34.47 C
ANISOU 4521 CD1 LEU A 579 4436 6170 2491 -105 361 297 C
ATOM 4522 CD2 LEU A 579 26.259 107.851 206.122 1.00 35.26 C
ANISOU 4522 CD2 LEU A 579 4647 6298 2454 -166 354 309 C
ATOM 4523 N PHE A 580 21.226 107.619 208.345 1.00 34.85 N
ANISOU 4523 N PHE A 580 4502 6293 2446 -287 171 402 N
ATOM 4524 CA PHE A 580 20.260 106.910 209.163 1.00 34.85 C
ANISOU 4524 CA PHE A 580 4500 6293 2450 -322 146 395 C
ATOM 4525 C PHE A 580 18.879 106.784 208.557 1.00 35.37 C
ANISOU 4525 C PHE A 580 4544 6404 2491 -384 94 434 C
ATOM 4526 O PHE A 580 18.437 107.624 207.736 1.00 35.68 O
ANISOU 4526 O PHE A 580 4541 6480 2534 -386 70 483 O
ATOM 4527 CB PHE A 580 20.230 107.576 210.522 1.00 34.43 C
ANISOU 4527 CB PHE A 580 4387 6225 2469 -287 170 394 C
ATOM 4528 CG PHE A 580 21.594 107.692 211.096 1.00 34.04 C
ANISOU 4528 CG PHE A 580 4356 6137 2442 -234 207 357 C
ATOM 4529 CD1 PHE A 580 22.202 106.592 211.674 1.00 33.96 C
ANISOU 4529 CD1 PHE A 580 4406 6090 2407 -227 211 313 C
ATOM 4530 CD2 PHE A 580 22.331 108.856 210.934 1.00 33.89 C
ANISOU 4530 CD2 PHE A 580 4295 6118 2464 -193 233 369 C
ATOM 4531 CE1 PHE A 580 23.492 106.672 212.131 1.00 33.74 C
ANISOU 4531 CE1 PHE A 580 4385 6033 2402 -176 235 282 C
ATOM 4532 CE2 PHE A 580 23.633 108.942 211.387 1.00 33.66 C
ANISOU 4532 CE2 PHE A 580 4273 6060 2457 -153 261 335 C
ATOM 4533 CZ PHE A 580 24.222 107.852 211.986 1.00 33.60 C
ANISOU 4533 CZ PHE A 580 4313 6023 2429 -141 259 292 C
ATOM 4534 N HIS A 581 18.192 105.722 208.961 1.00 35.57 N
ANISOU 4534 N HIS A 581 4598 6424 2491 -436 73 416 N
ATOM 4535 CA HIS A 581 16.824 105.511 208.537 1.00 36.15 C
ANISOU 4535 CA HIS A 581 4640 6547 2550 -504 20 450 C
ATOM 4536 C HIS A 581 15.863 105.830 209.675 1.00 36.12 C
ANISOU 4536 C HIS A 581 4550 6559 2614 -509 28 468 C
ATOM 4537 O HIS A 581 14.703 106.187 209.453 1.00 36.61 O
ANISOU 4537 O HIS A 581 4535 6672 2701 -541 -7 511 O
ATOM 4538 CB HIS A 581 16.643 104.078 208.069 1.00 36.60 C
ANISOU 4538 CB HIS A 581 4792 6589 2527 -576 -8 417 C
ATOM 4539 CG HIS A 581 15.334 103.839 207.397 1.00 37.36 C
ANISOU 4539 CG HIS A 581 4860 6740 2596 -659 -74 451 C
ATOM 4540 ND1 HIS A 581 15.033 104.350 206.147 1.00 37.87 N
ANISOU 4540 ND1 HIS A 581 4910 6851 2627 -677 -122 490 N
ATOM 4541 CD2 HIS A 581 14.238 103.161 207.807 1.00 37.81 C
ANISOU 4541 CD2 HIS A 581 4896 6815 2655 -734 -103 454 C
ATOM 4542 CE1 HIS A 581 13.810 103.988 205.815 1.00 38.60 C
ANISOU 4542 CE1 HIS A 581 4971 6993 2704 -757 -187 516 C
ATOM 4543 NE2 HIS A 581 13.304 103.267 206.805 1.00 38.58 N
ANISOU 4543 NE2 HIS A 581 4958 6975 2726 -795 -173 493 N
ATOM 4544 N VAL A 582 16.385 105.709 210.888 1.00 35.62 N
ANISOU 4544 N VAL A 582 4502 6453 2579 -476 75 435 N
ATOM 4545 CA VAL A 582 15.645 105.927 212.121 1.00 35.60 C
ANISOU 4545 CA VAL A 582 4439 6456 2630 -479 100 440 C
ATOM 4546 C VAL A 582 16.585 106.263 213.314 1.00 35.00 C
ANISOU 4546 C VAL A 582 4382 6331 2584 -418 152 408 C
ATOM 4547 O VAL A 582 17.759 105.897 213.338 1.00 34.66 O
ANISOU 4547 O VAL A 582 4408 6247 2514 -388 162 375 O
ATOM 4548 CB VAL A 582 14.713 104.745 212.454 1.00 36.06 C
ANISOU 4548 CB VAL A 582 4522 6522 2658 -563 83 431 C
ATOM 4549 CG1 VAL A 582 15.488 103.460 212.690 1.00 35.93 C
ANISOU 4549 CG1 VAL A 582 4629 6444 2579 -582 89 383 C
ATOM 4550 CG2 VAL A 582 13.811 105.100 213.648 1.00 36.20 C
ANISOU 4550 CG2 VAL A 582 4463 6556 2734 -570 119 443 C
ATOM 4551 N ALA A 583 16.038 106.955 214.304 1.00 34.98 N
ANISOU 4551 N ALA A 583 4316 6337 2638 -401 185 417 N
ATOM 4552 CA ALA A 583 16.842 107.680 215.259 1.00 34.53 C
ANISOU 4552 CA ALA A 583 4260 6245 2615 -342 228 396 C
ATOM 4553 C ALA A 583 16.082 107.932 216.570 1.00 34.69 C
ANISOU 4553 C ALA A 583 4244 6266 2669 -348 270 391 C
ATOM 4554 O ALA A 583 14.914 108.351 216.516 1.00 35.13 O
ANISOU 4554 O ALA A 583 4220 6362 2765 -364 278 421 O
ATOM 4555 CB ALA A 583 17.281 109.004 214.619 1.00 34.39 C
ANISOU 4555 CB ALA A 583 4192 6234 2640 -287 231 419 C
ATOM 4556 N LEU A 584 16.740 107.677 217.717 1.00 34.43 N
ANISOU 4556 N LEU A 584 4270 6191 2621 -334 297 355 N
ATOM 4557 CA LEU A 584 16.187 107.957 219.071 1.00 34.61 C
ANISOU 4557 CA LEU A 584 4280 6208 2664 -339 348 343 C
ATOM 4558 C LEU A 584 17.029 108.965 219.807 1.00 34.32 C
ANISOU 4558 C LEU A 584 4248 6139 2653 -281 376 320 C
ATOM 4559 O LEU A 584 18.235 108.848 219.838 1.00 33.96 O
ANISOU 4559 O LEU A 584 4255 6062 2586 -255 356 298 O
ATOM 4560 CB LEU A 584 16.136 106.702 219.931 1.00 34.76 C
ANISOU 4560 CB LEU A 584 4382 6201 2623 -388 352 321 C
ATOM 4561 CG LEU A 584 15.289 105.486 219.517 1.00 35.18 C
ANISOU 4561 CG LEU A 584 4456 6272 2640 -465 330 334 C
ATOM 4562 CD1 LEU A 584 15.496 104.329 220.514 1.00 35.32 C
ANISOU 4562 CD1 LEU A 584 4580 6244 2597 -504 339 312 C
ATOM 4563 CD2 LEU A 584 13.817 105.815 219.369 1.00 35.75 C
ANISOU 4563 CD2 LEU A 584 4427 6402 2755 -505 351 365 C
ATOM 4564 N ALA A 585 16.393 109.960 220.400 1.00 34.57 N
ANISOU 4564 N ALA A 585 4223 6177 2734 -262 425 323 N
ATOM 4565 CA ALA A 585 17.077 110.984 221.195 1.00 34.43 C
ANISOU 4565 CA ALA A 585 4217 6124 2740 -217 457 296 C
ATOM 4566 C ALA A 585 16.308 111.214 222.532 1.00 34.87 C
ANISOU 4566 C ALA A 585 4275 6174 2799 -229 523 276 C
ATOM 4567 O ALA A 585 15.381 112.009 222.594 1.00 35.29 O
ANISOU 4567 O ALA A 585 4256 6244 2907 -213 570 290 O
ATOM 4568 CB ALA A 585 17.146 112.245 220.409 1.00 34.41 C
ANISOU 4568 CB ALA A 585 4148 6125 2800 -170 459 319 C
ATOM 4569 N GLY A 586 16.646 110.500 223.590 1.00 34.89 N
ANISOU 4569 N GLY A 586 4362 6154 2743 -256 531 246 N
ATOM 4570 CA GLY A 586 15.995 110.763 224.853 1.00 35.39 C
ANISOU 4570 CA GLY A 586 4439 6209 2798 -271 601 224 C
ATOM 4571 C GLY A 586 16.578 111.985 225.515 1.00 35.40 C
ANISOU 4571 C GLY A 586 4455 6176 2822 -227 631 191 C
ATOM 4572 O GLY A 586 17.764 112.246 225.381 1.00 35.01 O
ANISOU 4572 O GLY A 586 4438 6099 2764 -203 587 177 O
ATOM 4573 N VAL A 587 15.734 112.729 226.240 1.00 35.97 N
ANISOU 4573 N VAL A 587 4499 6246 2922 -219 711 177 N
ATOM 4574 CA VAL A 587 16.140 113.915 227.018 1.00 36.18 C
ANISOU 4574 CA VAL A 587 4551 6230 2964 -184 754 138 C
ATOM 4575 C VAL A 587 17.340 114.665 226.411 1.00 35.69 C
ANISOU 4575 C VAL A 587 4492 6140 2930 -147 701 134 C
ATOM 4576 O VAL A 587 18.321 114.846 227.089 1.00 35.62 O
ANISOU 4576 O VAL A 587 4553 6097 2883 -150 682 98 O
ATOM 4577 CB VAL A 587 16.476 113.528 228.473 1.00 36.47 C
ANISOU 4577 CB VAL A 587 4699 6240 2917 -220 778 93 C
ATOM 4578 CG1 VAL A 587 15.174 113.329 229.307 1.00 37.23 C
ANISOU 4578 CG1 VAL A 587 4791 6355 3001 -250 873 86 C
ATOM 4579 CG2 VAL A 587 17.399 112.296 228.500 1.00 36.04 C
ANISOU 4579 CG2 VAL A 587 4722 6182 2788 -251 695 98 C
ATOM 4580 N PRO A 588 17.244 115.108 225.136 1.00 35.47 N
ANISOU 4580 N PRO A 588 4385 6127 2965 -116 676 174 N
ATOM 4581 CA PRO A 588 18.374 115.581 224.345 1.00 35.02 C
ANISOU 4581 CA PRO A 588 4326 6052 2928 -92 623 180 C
ATOM 4582 C PRO A 588 18.785 117.042 224.501 1.00 35.23 C
ANISOU 4582 C PRO A 588 4348 6032 3005 -57 652 161 C
ATOM 4583 O PRO A 588 17.987 117.938 224.273 1.00 35.63 O
ANISOU 4583 O PRO A 588 4347 6073 3119 -23 700 178 O
ATOM 4584 CB PRO A 588 17.890 115.359 222.908 1.00 34.86 C
ANISOU 4584 CB PRO A 588 4232 6071 2941 -84 591 236 C
ATOM 4585 CG PRO A 588 16.443 115.520 222.966 1.00 35.40 C
ANISOU 4585 CG PRO A 588 4235 6165 3048 -79 640 258 C
ATOM 4586 CD PRO A 588 15.998 115.157 224.352 1.00 35.76 C
ANISOU 4586 CD PRO A 588 4326 6204 3056 -105 696 219 C
ATOM 4587 N PHE A 589 20.062 117.245 224.810 1.00 35.02 N
ANISOU 4587 N PHE A 589 4374 5975 2955 -65 618 130 N
ATOM 4588 CA PHE A 589 20.620 118.555 225.040 1.00 35.27 C
ANISOU 4588 CA PHE A 589 4418 5956 3025 -47 639 105 C
ATOM 4589 C PHE A 589 20.751 119.138 223.697 1.00 35.10 C
ANISOU 4589 C PHE A 589 4336 5936 3064 -21 622 151 C
ATOM 4590 O PHE A 589 21.671 118.783 222.975 1.00 34.69 O
ANISOU 4590 O PHE A 589 4279 5900 3001 -31 569 164 O
ATOM 4591 CB PHE A 589 22.015 118.454 225.691 1.00 35.15 C
ANISOU 4591 CB PHE A 589 4468 5921 2966 -76 592 62 C
ATOM 4592 CG PHE A 589 22.691 119.799 225.944 1.00 35.49 C
ANISOU 4592 CG PHE A 589 4529 5909 3046 -73 607 31 C
ATOM 4593 CD1 PHE A 589 21.960 120.960 226.118 1.00 36.01 C
ANISOU 4593 CD1 PHE A 589 4589 5930 3162 -48 677 23 C
ATOM 4594 CD2 PHE A 589 24.063 119.891 226.050 1.00 35.40 C
ANISOU 4594 CD2 PHE A 589 4541 5889 3022 -98 552 8 C
ATOM 4595 CE1 PHE A 589 22.588 122.176 226.368 1.00 36.41 C
ANISOU 4595 CE1 PHE A 589 4669 5920 3244 -52 692 -8 C
ATOM 4596 CE2 PHE A 589 24.692 121.135 226.287 1.00 35.81 C
ANISOU 4596 CE2 PHE A 589 4611 5888 3108 -109 564 -23 C
ATOM 4597 CZ PHE A 589 23.948 122.260 226.450 1.00 36.30 C
ANISOU 4597 CZ PHE A 589 4681 5898 3214 -89 634 -32 C
ATOM 4598 N VAL A 590 19.842 120.021 223.305 1.00 35.50 N
ANISOU 4598 N VAL A 590 4338 5971 3178 17 668 178 N
ATOM 4599 CA VAL A 590 19.867 120.460 221.874 1.00 35.40 C
ANISOU 4599 CA VAL A 590 4270 5966 3213 41 642 237 C
ATOM 4600 C VAL A 590 19.748 121.956 221.577 1.00 35.90 C
ANISOU 4600 C VAL A 590 4319 5972 3351 81 679 253 C
ATOM 4601 O VAL A 590 20.020 122.349 220.465 1.00 35.85 O
ANISOU 4601 O VAL A 590 4287 5964 3371 92 653 299 O
ATOM 4602 CB VAL A 590 18.844 119.698 221.010 1.00 35.34 C
ANISOU 4602 CB VAL A 590 4201 6019 3207 47 623 291 C
ATOM 4603 CG1 VAL A 590 19.307 118.311 220.765 1.00 34.79 C
ANISOU 4603 CG1 VAL A 590 4153 5996 3070 7 569 289 C
ATOM 4604 CG2 VAL A 590 17.462 119.694 221.644 1.00 35.86 C
ANISOU 4604 CG2 VAL A 590 4231 6098 3297 64 677 291 C
ATOM 4605 N ASP A 591 19.353 122.774 222.545 1.00 36.47 N
ANISOU 4605 N ASP A 591 4415 5991 3450 101 742 215 N
ATOM 4606 CA ASP A 591 19.165 124.205 222.343 1.00 37.09 C
ANISOU 4606 CA ASP A 591 4490 6000 3602 144 785 227 C
ATOM 4607 C ASP A 591 20.390 124.884 222.936 1.00 37.15 C
ANISOU 4607 C ASP A 591 4573 5946 3597 110 786 173 C
ATOM 4608 O ASP A 591 20.278 125.662 223.891 1.00 37.73 O
ANISOU 4608 O ASP A 591 4695 5957 3685 118 842 123 O
ATOM 4609 CB ASP A 591 17.877 124.629 223.056 1.00 37.82 C
ANISOU 4609 CB ASP A 591 4563 6072 3736 191 862 215 C
ATOM 4610 CG ASP A 591 17.450 126.096 222.789 1.00 38.64 C
ANISOU 4610 CG ASP A 591 4656 6098 3929 255 912 236 C
ATOM 4611 OD1 ASP A 591 17.805 126.713 221.746 1.00 38.67 O
ANISOU 4611 OD1 ASP A 591 4646 6076 3970 272 880 288 O
ATOM 4612 OD2 ASP A 591 16.707 126.636 223.669 1.00 40.94 O
ANISOU 4612 OD2 ASP A 591 4956 6347 4251 292 992 200 O
ATOM 4613 N VAL A 592 21.563 124.580 222.373 1.00 36.65 N
ANISOU 4613 N VAL A 592 4517 5901 3508 71 727 180 N
ATOM 4614 CA VAL A 592 22.854 124.825 223.048 1.00 36.65 C
ANISOU 4614 CA VAL A 592 4576 5869 3480 20 708 123 C
ATOM 4615 C VAL A 592 23.196 126.288 223.250 1.00 37.32 C
ANISOU 4615 C VAL A 592 4701 5863 3615 20 747 101 C
ATOM 4616 O VAL A 592 23.496 126.714 224.371 1.00 37.73 O
ANISOU 4616 O VAL A 592 4816 5869 3650 -6 769 36 O
ATOM 4617 CB VAL A 592 24.015 124.137 222.316 1.00 36.08 C
ANISOU 4617 CB VAL A 592 4484 5844 3380 -16 641 139 C
ATOM 4618 CG1 VAL A 592 25.184 123.864 223.229 1.00 36.04 C
ANISOU 4618 CG1 VAL A 592 4523 5839 3332 -67 606 79 C
ATOM 4619 CG2 VAL A 592 23.535 122.846 221.810 1.00 35.54 C
ANISOU 4619 CG2 VAL A 592 4378 5850 3275 -6 611 173 C
ATOM 4620 N MET A 593 23.170 127.055 222.175 1.00 37.51 N
ANISOU 4620 N MET A 593 4699 5858 3697 43 753 156 N
ATOM 4621 CA MET A 593 23.418 128.477 222.299 1.00 38.26 C
ANISOU 4621 CA MET A 593 4838 5853 3844 44 793 142 C
ATOM 4622 C MET A 593 22.528 129.172 223.364 1.00 38.99 C
ANISOU 4622 C MET A 593 4976 5879 3960 81 866 96 C
ATOM 4623 O MET A 593 23.020 129.902 224.236 1.00 39.53 O
ANISOU 4623 O MET A 593 5117 5876 4025 49 893 32 O
ATOM 4624 CB MET A 593 23.266 129.142 220.936 1.00 38.46 C
ANISOU 4624 CB MET A 593 4831 5855 3925 74 793 223 C
ATOM 4625 CG MET A 593 24.221 128.606 219.918 1.00 37.92 C
ANISOU 4625 CG MET A 593 4733 5843 3832 32 737 260 C
ATOM 4626 SD MET A 593 25.875 129.161 220.334 1.00 38.13 S
ANISOU 4626 SD MET A 593 4806 5828 3854 -53 725 204 S
ATOM 4627 CE MET A 593 25.837 130.813 219.660 1.00 39.04 C
ANISOU 4627 CE MET A 593 4957 5832 4044 -42 770 247 C
ATOM 4628 N THR A 594 21.223 128.924 223.283 1.00 39.11 N
ANISOU 4628 N THR A 594 4945 5916 3996 146 900 127 N
ATOM 4629 CA THR A 594 20.239 129.657 224.085 1.00 39.96 C
ANISOU 4629 CA THR A 594 5079 5960 4144 199 985 95 C
ATOM 4630 C THR A 594 20.363 129.340 225.566 1.00 40.10 C
ANISOU 4630 C THR A 594 5164 5974 4097 160 1016 4 C
ATOM 4631 O THR A 594 20.322 130.239 226.405 1.00 40.90 O
ANISOU 4631 O THR A 594 5338 5990 4210 164 1077 -55 O
ATOM 4632 CB THR A 594 18.778 129.426 223.567 1.00 40.16 C
ANISOU 4632 CB THR A 594 5017 6024 4218 279 1011 156 C
ATOM 4633 OG1 THR A 594 18.654 129.999 222.261 1.00 40.32 O
ANISOU 4633 OG1 THR A 594 4994 6027 4299 319 984 240 O
ATOM 4634 CG2 THR A 594 17.702 130.056 224.531 1.00 41.15 C
ANISOU 4634 CG2 THR A 594 5157 6093 4385 340 1113 114 C
ATOM 4635 N THR A 595 20.532 128.057 225.863 1.00 39.39 N
ANISOU 4635 N THR A 595 5061 5972 3935 121 971 -6 N
ATOM 4636 CA THR A 595 20.693 127.596 227.210 1.00 39.50 C
ANISOU 4636 CA THR A 595 5144 5993 3873 79 986 -81 C
ATOM 4637 C THR A 595 22.040 128.008 227.712 1.00 39.60 C
ANISOU 4637 C THR A 595 5234 5964 3849 11 946 -135 C
ATOM 4638 O THR A 595 22.146 128.614 228.759 1.00 40.30 O
ANISOU 4638 O THR A 595 5407 5991 3913 -11 988 -205 O
ATOM 4639 CB THR A 595 20.544 126.107 227.269 1.00 38.78 C
ANISOU 4639 CB THR A 595 5019 6000 3717 57 942 -65 C
ATOM 4640 OG1 THR A 595 19.213 125.794 226.838 1.00 38.85 O
ANISOU 4640 OG1 THR A 595 4952 6046 3765 113 982 -17 O
ATOM 4641 CG2 THR A 595 20.813 125.546 228.716 1.00 38.94 C
ANISOU 4641 CG2 THR A 595 5126 6028 3643 6 947 -138 C
ATOM 4642 N MET A 596 23.070 127.745 226.940 1.00 39.03 N
ANISOU 4642 N MET A 596 5131 5923 3775 -25 868 -105 N
ATOM 4643 CA MET A 596 24.391 127.989 227.431 1.00 39.16 C
ANISOU 4643 CA MET A 596 5203 5917 3759 -97 820 -154 C
ATOM 4644 C MET A 596 24.751 129.452 227.689 1.00 40.04 C
ANISOU 4644 C MET A 596 5379 5922 3912 -116 859 -193 C
ATOM 4645 O MET A 596 25.712 129.720 228.421 1.00 40.40 O
ANISOU 4645 O MET A 596 5486 5942 3920 -185 826 -253 O
ATOM 4646 CB MET A 596 25.413 127.268 226.562 1.00 38.43 C
ANISOU 4646 CB MET A 596 5051 5892 3658 -128 734 -114 C
ATOM 4647 CG MET A 596 25.469 125.755 226.865 1.00 37.78 C
ANISOU 4647 CG MET A 596 4951 5899 3505 -137 682 -112 C
ATOM 4648 SD MET A 596 25.706 125.250 228.625 1.00 38.15 S
ANISOU 4648 SD MET A 596 5093 5949 3453 -184 665 -193 S
ATOM 4649 CE MET A 596 27.050 126.297 229.212 1.00 38.86 C
ANISOU 4649 CE MET A 596 5243 5979 3543 -256 628 -254 C
ATOM 4650 N CYS A 597 23.983 130.397 227.148 1.00 40.50 N
ANISOU 4650 N CYS A 597 5428 5914 4047 -57 925 -163 N
ATOM 4651 CA CYS A 597 24.311 131.807 227.361 1.00 41.43 C
ANISOU 4651 CA CYS A 597 5618 5916 4208 -75 965 -199 C
ATOM 4652 C CYS A 597 23.749 132.306 228.675 1.00 42.31 C
ANISOU 4652 C CYS A 597 5823 5959 4292 -68 1040 -280 C
ATOM 4653 O CYS A 597 24.204 133.313 229.221 1.00 43.16 O
ANISOU 4653 O CYS A 597 6020 5973 4405 -107 1065 -339 O
ATOM 4654 CB CYS A 597 23.780 132.679 226.233 1.00 41.73 C
ANISOU 4654 CB CYS A 597 5620 5896 4339 -11 1004 -128 C
ATOM 4655 SG CYS A 597 22.095 133.171 226.489 1.00 42.45 S
ANISOU 4655 SG CYS A 597 5709 5934 4485 100 1108 -121 S
ATOM 4656 N ASP A 598 22.753 131.584 229.162 1.00 42.17 N
ANISOU 4656 N ASP A 598 5788 5990 4244 -23 1079 -285 N
ATOM 4657 CA ASP A 598 21.852 132.019 230.245 1.00 43.08 C
ANISOU 4657 CA ASP A 598 5974 6048 4346 10 1179 -349 C
ATOM 4658 C ASP A 598 22.193 131.362 231.586 1.00 43.17 C
ANISOU 4658 C ASP A 598 6068 6093 4243 -57 1165 -427 C
ATOM 4659 O ASP A 598 21.988 130.175 231.758 1.00 42.53 O
ANISOU 4659 O ASP A 598 5950 6105 4106 -63 1134 -410 O
ATOM 4660 CB ASP A 598 20.422 131.626 229.832 1.00 42.98 C
ANISOU 4660 CB ASP A 598 5873 6077 4381 105 1239 -294 C
ATOM 4661 CG ASP A 598 19.378 131.929 230.879 1.00 43.94 C
ANISOU 4661 CG ASP A 598 6044 6156 4495 149 1355 -353 C
ATOM 4662 OD1 ASP A 598 19.715 132.135 232.047 1.00 44.52 O
ANISOU 4662 OD1 ASP A 598 6229 6189 4498 98 1384 -441 O
ATOM 4663 OD2 ASP A 598 18.184 131.949 230.534 1.00 44.21 O
ANISOU 4663 OD2 ASP A 598 6002 6201 4594 234 1419 -313 O
ATOM 4664 N PRO A 599 22.660 132.138 232.565 1.00 44.08 N
ANISOU 4664 N PRO A 599 6303 6127 4319 -109 1190 -513 N
ATOM 4665 CA PRO A 599 23.079 131.582 233.864 1.00 44.32 C
ANISOU 4665 CA PRO A 599 6428 6186 4228 -182 1164 -587 C
ATOM 4666 C PRO A 599 21.949 130.962 234.718 1.00 44.59 C
ANISOU 4666 C PRO A 599 6487 6252 4205 -146 1247 -612 C
ATOM 4667 O PRO A 599 22.218 130.198 235.655 1.00 44.61 O
ANISOU 4667 O PRO A 599 6551 6300 4097 -203 1215 -650 O
ATOM 4668 CB PRO A 599 23.638 132.794 234.574 1.00 45.47 C
ANISOU 4668 CB PRO A 599 6698 6218 4360 -235 1190 -671 C
ATOM 4669 CG PRO A 599 22.788 133.925 234.032 1.00 46.11 C
ANISOU 4669 CG PRO A 599 6769 6199 4550 -150 1296 -657 C
ATOM 4670 CD PRO A 599 22.699 133.608 232.563 1.00 45.11 C
ANISOU 4670 CD PRO A 599 6501 6127 4512 -98 1251 -548 C
ATOM 4671 N SER A 600 20.700 131.283 234.407 1.00 44.91 N
ANISOU 4671 N SER A 600 6476 6268 4319 -55 1353 -587 N
ATOM 4672 CA SER A 600 19.611 130.822 235.214 1.00 45.36 C
ANISOU 4672 CA SER A 600 6551 6350 4333 -24 1448 -615 C
ATOM 4673 C SER A 600 19.184 129.377 234.924 1.00 44.40 C
ANISOU 4673 C SER A 600 6337 6352 4182 -19 1408 -552 C
ATOM 4674 O SER A 600 18.542 128.748 235.795 1.00 44.73 O
ANISOU 4674 O SER A 600 6415 6429 4153 -28 1467 -581 O
ATOM 4675 CB SER A 600 18.444 131.738 235.045 1.00 46.25 C
ANISOU 4675 CB SER A 600 6637 6392 4544 74 1580 -616 C
ATOM 4676 OG SER A 600 17.808 131.433 233.836 1.00 45.59 O
ANISOU 4676 OG SER A 600 6405 6361 4557 147 1566 -519 O
ATOM 4677 N ILE A 601 19.514 128.833 233.745 1.00 43.32 N
ANISOU 4677 N ILE A 601 6092 6276 4092 -9 1317 -470 N
ATOM 4678 CA ILE A 601 19.126 127.448 233.484 1.00 42.50 C
ANISOU 4678 CA ILE A 601 5914 6280 3956 -11 1279 -416 C
ATOM 4679 C ILE A 601 19.976 126.440 234.291 1.00 42.16 C
ANISOU 4679 C ILE A 601 5947 6286 3786 -95 1198 -444 C
ATOM 4680 O ILE A 601 21.189 126.548 234.336 1.00 41.96 O
ANISOU 4680 O ILE A 601 5963 6250 3730 -148 1108 -462 O
ATOM 4681 CB ILE A 601 19.068 127.140 231.998 1.00 41.61 C
ANISOU 4681 CB ILE A 601 5671 6215 3924 28 1218 -323 C
ATOM 4682 CG1 ILE A 601 18.201 128.197 231.288 1.00 42.15 C
ANISOU 4682 CG1 ILE A 601 5675 6228 4113 115 1293 -291 C
ATOM 4683 CG2 ILE A 601 18.501 125.727 231.785 1.00 40.95 C
ANISOU 4683 CG2 ILE A 601 5520 6233 3807 25 1193 -275 C
ATOM 4684 CD1 ILE A 601 18.409 128.336 229.741 1.00 41.50 C
ANISOU 4684 CD1 ILE A 601 5493 6162 4113 148 1225 -204 C
ATOM 4685 N PRO A 602 19.325 125.484 234.981 1.00 42.24 N
ANISOU 4685 N PRO A 602 5977 6349 3724 -109 1231 -450 N
ATOM 4686 CA PRO A 602 20.056 124.720 236.020 1.00 42.30 C
ANISOU 4686 CA PRO A 602 6091 6381 3600 -186 1171 -488 C
ATOM 4687 C PRO A 602 21.508 124.213 235.815 1.00 41.63 C
ANISOU 4687 C PRO A 602 6019 6325 3474 -240 1021 -474 C
ATOM 4688 O PRO A 602 22.252 124.230 236.811 1.00 42.13 O
ANISOU 4688 O PRO A 602 6192 6372 3444 -301 978 -528 O
ATOM 4689 CB PRO A 602 19.080 123.613 236.423 1.00 42.30 C
ANISOU 4689 CB PRO A 602 6081 6443 3548 -187 1220 -468 C
ATOM 4690 CG PRO A 602 17.753 124.224 236.205 1.00 42.85 C
ANISOU 4690 CG PRO A 602 6086 6492 3703 -119 1353 -464 C
ATOM 4691 CD PRO A 602 17.865 125.320 235.151 1.00 42.71 C
ANISOU 4691 CD PRO A 602 5992 6426 3810 -60 1350 -441 C
ATOM 4692 N LEU A 603 21.962 123.797 234.638 1.00 40.69 N
ANISOU 4692 N LEU A 603 5797 6247 3415 -222 942 -409 N
ATOM 4693 CA LEU A 603 23.390 123.343 234.605 1.00 40.29 C
ANISOU 4693 CA LEU A 603 5762 6222 3323 -271 810 -406 C
ATOM 4694 C LEU A 603 24.400 124.205 233.803 1.00 40.12 C
ANISOU 4694 C LEU A 603 5695 6171 3377 -277 755 -400 C
ATOM 4695 O LEU A 603 25.535 123.811 233.581 1.00 39.79 O
ANISOU 4695 O LEU A 603 5635 6159 3323 -309 652 -388 O
ATOM 4696 CB LEU A 603 23.483 121.903 234.101 1.00 39.44 C
ANISOU 4696 CB LEU A 603 5599 6193 3195 -266 740 -345 C
ATOM 4697 CG LEU A 603 23.003 120.769 234.978 1.00 39.59 C
ANISOU 4697 CG LEU A 603 5681 6248 3114 -288 746 -346 C
ATOM 4698 CD1 LEU A 603 23.031 119.465 234.202 1.00 38.75 C
ANISOU 4698 CD1 LEU A 603 5507 6204 3012 -274 685 -280 C
ATOM 4699 CD2 LEU A 603 23.921 120.704 236.071 1.00 40.14 C
ANISOU 4699 CD2 LEU A 603 5859 6304 3087 -345 681 -393 C
ATOM 4700 N THR A 604 23.973 125.363 233.344 1.00 40.43 N
ANISOU 4700 N THR A 604 5713 6149 3498 -243 827 -405 N
ATOM 4701 CA THR A 604 24.770 126.206 232.459 1.00 40.31 C
ANISOU 4701 CA THR A 604 5653 6102 3563 -247 792 -389 C
ATOM 4702 C THR A 604 26.166 126.608 233.018 1.00 40.75 C
ANISOU 4702 C THR A 604 5768 6134 3580 -325 712 -440 C
ATOM 4703 O THR A 604 27.194 126.371 232.378 1.00 40.32 O
ANISOU 4703 O THR A 604 5656 6115 3550 -349 626 -411 O
ATOM 4704 CB THR A 604 23.927 127.433 232.002 1.00 40.78 C
ANISOU 4704 CB THR A 604 5699 6085 3712 -193 893 -385 C
ATOM 4705 OG1 THR A 604 22.717 126.966 231.386 1.00 40.40 O
ANISOU 4705 OG1 THR A 604 5572 6074 3705 -123 946 -329 O
ATOM 4706 CG2 THR A 604 24.680 128.300 231.049 1.00 40.74 C
ANISOU 4706 CG2 THR A 604 5654 6039 3785 -200 863 -361 C
ATOM 4707 N THR A 605 26.220 127.203 234.207 1.00 41.69 N
ANISOU 4707 N THR A 605 6002 6198 3640 -369 738 -516 N
ATOM 4708 CA THR A 605 27.509 127.727 234.707 1.00 42.28 C
ANISOU 4708 CA THR A 605 6132 6247 3685 -451 659 -567 C
ATOM 4709 C THR A 605 28.557 126.637 234.978 1.00 41.96 C
ANISOU 4709 C THR A 605 6074 6288 3580 -496 529 -554 C
ATOM 4710 O THR A 605 29.737 126.853 234.730 1.00 42.06 O
ANISOU 4710 O THR A 605 6053 6311 3616 -543 444 -556 O
ATOM 4711 CB THR A 605 27.370 128.677 235.925 1.00 43.51 C
ANISOU 4711 CB THR A 605 6430 6319 3785 -496 713 -659 C
ATOM 4712 OG1 THR A 605 26.864 127.943 237.034 1.00 43.80 O
ANISOU 4712 OG1 THR A 605 6550 6383 3710 -505 729 -690 O
ATOM 4713 CG2 THR A 605 26.449 129.879 235.612 1.00 44.00 C
ANISOU 4713 CG2 THR A 605 6508 6284 3926 -444 842 -673 C
ATOM 4714 N GLY A 606 28.139 125.472 235.475 1.00 41.67 N
ANISOU 4714 N GLY A 606 6057 6308 3467 -480 514 -539 N
ATOM 4715 CA GLY A 606 29.052 124.340 235.542 1.00 41.31 C
ANISOU 4715 CA GLY A 606 5982 6338 3378 -501 392 -511 C
ATOM 4716 C GLY A 606 29.726 124.147 234.191 1.00 40.54 C
ANISOU 4716 C GLY A 606 5751 6279 3374 -475 343 -452 C
ATOM 4717 O GLY A 606 30.963 124.173 234.102 1.00 40.73 O
ANISOU 4717 O GLY A 606 5739 6324 3410 -516 250 -456 O
ATOM 4718 N GLU A 607 28.901 123.994 233.146 1.00 39.80 N
ANISOU 4718 N GLU A 607 5583 6193 3346 -411 410 -399 N
ATOM 4719 CA GLU A 607 29.335 123.668 231.765 1.00 39.03 C
ANISOU 4719 CA GLU A 607 5366 6137 3326 -380 380 -336 C
ATOM 4720 C GLU A 607 29.886 124.795 230.889 1.00 39.15 C
ANISOU 4720 C GLU A 607 5329 6115 3433 -393 393 -329 C
ATOM 4721 O GLU A 607 30.146 124.573 229.707 1.00 38.59 O
ANISOU 4721 O GLU A 607 5167 6075 3420 -367 383 -277 O
ATOM 4722 CB GLU A 607 28.203 122.967 230.998 1.00 38.27 C
ANISOU 4722 CB GLU A 607 5221 6071 3251 -313 435 -279 C
ATOM 4723 CG GLU A 607 27.934 121.611 231.608 1.00 38.06 C
ANISOU 4723 CG GLU A 607 5226 6092 3142 -308 402 -271 C
ATOM 4724 CD GLU A 607 26.814 120.830 230.995 1.00 37.45 C
ANISOU 4724 CD GLU A 607 5109 6046 3074 -258 450 -221 C
ATOM 4725 OE1 GLU A 607 26.196 121.261 230.004 1.00 37.14 O
ANISOU 4725 OE1 GLU A 607 5006 6000 3106 -222 504 -187 O
ATOM 4726 OE2 GLU A 607 26.547 119.754 231.550 1.00 37.38 O
ANISOU 4726 OE2 GLU A 607 5139 6067 2995 -261 430 -216 O
ATOM 4727 N TRP A 608 30.059 125.994 231.438 1.00 39.96 N
ANISOU 4727 N TRP A 608 5495 6146 3543 -437 420 -383 N
ATOM 4728 CA TRP A 608 30.926 126.942 230.782 1.00 40.25 C
ANISOU 4728 CA TRP A 608 5491 6151 3652 -475 406 -381 C
ATOM 4729 C TRP A 608 32.353 126.354 230.689 1.00 40.24 C
ANISOU 4729 C TRP A 608 5427 6216 3647 -521 295 -376 C
ATOM 4730 O TRP A 608 33.147 126.748 229.843 1.00 40.26 O
ANISOU 4730 O TRP A 608 5356 6224 3716 -543 278 -354 O
ATOM 4731 CB TRP A 608 30.915 128.306 231.471 1.00 41.26 C
ANISOU 4731 CB TRP A 608 5711 6182 3783 -524 450 -446 C
ATOM 4732 CG TRP A 608 29.660 129.070 231.270 1.00 41.38 C
ANISOU 4732 CG TRP A 608 5762 6124 3837 -468 565 -442 C
ATOM 4733 CD1 TRP A 608 28.705 128.842 230.325 1.00 40.73 C
ANISOU 4733 CD1 TRP A 608 5616 6054 3803 -388 623 -378 C
ATOM 4734 CD2 TRP A 608 29.222 130.218 232.008 1.00 42.35 C
ANISOU 4734 CD2 TRP A 608 5990 6145 3955 -485 637 -505 C
ATOM 4735 NE1 TRP A 608 27.699 129.769 230.429 1.00 41.23 N
ANISOU 4735 NE1 TRP A 608 5729 6036 3902 -347 722 -391 N
ATOM 4736 CE2 TRP A 608 27.993 130.620 231.463 1.00 42.23 C
ANISOU 4736 CE2 TRP A 608 5962 6087 3997 -402 738 -471 C
ATOM 4737 CE3 TRP A 608 29.750 130.949 233.076 1.00 43.40 C
ANISOU 4737 CE3 TRP A 608 6230 6217 4042 -563 624 -588 C
ATOM 4738 CZ2 TRP A 608 27.295 131.724 231.947 1.00 43.13 C
ANISOU 4738 CZ2 TRP A 608 6163 6096 4131 -385 833 -518 C
ATOM 4739 CZ3 TRP A 608 29.062 132.040 233.543 1.00 44.27 C
ANISOU 4739 CZ3 TRP A 608 6436 6220 4163 -554 720 -638 C
ATOM 4740 CH2 TRP A 608 27.849 132.420 232.983 1.00 44.14 C
ANISOU 4740 CH2 TRP A 608 6401 6158 4210 -461 827 -603 C
ATOM 4741 N GLU A 609 32.688 125.407 231.553 1.00 40.31 N
ANISOU 4741 N GLU A 609 5463 6275 3579 -533 220 -394 N
ATOM 4742 CA GLU A 609 33.974 124.701 231.430 1.00 40.34 C
ANISOU 4742 CA GLU A 609 5393 6349 3586 -556 112 -380 C
ATOM 4743 C GLU A 609 33.830 123.321 230.796 1.00 39.47 C
ANISOU 4743 C GLU A 609 5217 6309 3473 -488 91 -322 C
ATOM 4744 O GLU A 609 34.592 122.431 231.073 1.00 39.56 O
ANISOU 4744 O GLU A 609 5199 6374 3457 -488 4 -316 O
ATOM 4745 CB GLU A 609 34.675 124.599 232.785 1.00 41.22 C
ANISOU 4745 CB GLU A 609 5573 6468 3620 -619 20 -435 C
ATOM 4746 CG GLU A 609 35.323 125.861 233.228 1.00 42.21 C
ANISOU 4746 CG GLU A 609 5736 6542 3762 -706 5 -491 C
ATOM 4747 CD GLU A 609 36.133 125.643 234.493 1.00 43.15 C
ANISOU 4747 CD GLU A 609 5912 6685 3800 -773 -109 -539 C
ATOM 4748 OE1 GLU A 609 36.195 124.477 234.949 1.00 42.98 O
ANISOU 4748 OE1 GLU A 609 5895 6719 3715 -742 -175 -519 O
ATOM 4749 OE2 GLU A 609 36.707 126.624 235.041 1.00 44.15 O
ANISOU 4749 OE2 GLU A 609 6083 6770 3922 -860 -137 -595 O
ATOM 4750 N GLU A 610 32.830 123.149 229.961 1.00 38.74 N
ANISOU 4750 N GLU A 610 5103 6211 3407 -430 170 -280 N
ATOM 4751 CA GLU A 610 32.677 121.911 229.221 1.00 37.98 C
ANISOU 4751 CA GLU A 610 4947 6172 3311 -372 156 -228 C
ATOM 4752 C GLU A 610 32.586 122.263 227.725 1.00 37.50 C
ANISOU 4752 C GLU A 610 4804 6114 3331 -344 209 -181 C
ATOM 4753 O GLU A 610 33.517 122.002 226.991 1.00 37.43 O
ANISOU 4753 O GLU A 610 4718 6144 3362 -346 175 -160 O
ATOM 4754 CB GLU A 610 31.473 121.092 229.728 1.00 37.62 C
ANISOU 4754 CB GLU A 610 4966 6131 3199 -334 188 -219 C
ATOM 4755 CG GLU A 610 31.141 119.839 228.947 1.00 36.89 C
ANISOU 4755 CG GLU A 610 4826 6086 3103 -281 183 -167 C
ATOM 4756 CD GLU A 610 32.149 118.696 229.131 1.00 36.93 C
ANISOU 4756 CD GLU A 610 4810 6141 3082 -274 88 -159 C
ATOM 4757 OE1 GLU A 610 32.975 118.782 230.060 1.00 37.57 O
ANISOU 4757 OE1 GLU A 610 4920 6223 3132 -310 17 -192 O
ATOM 4758 OE2 GLU A 610 32.094 117.694 228.363 1.00 36.42 O
ANISOU 4758 OE2 GLU A 610 4703 6110 3024 -230 81 -119 O
ATOM 4759 N TRP A 611 31.500 122.873 227.274 1.00 37.28 N
ANISOU 4759 N TRP A 611 4793 6046 3328 -320 293 -163 N
ATOM 4760 CA TRP A 611 31.389 123.205 225.869 1.00 36.94 C
ANISOU 4760 CA TRP A 611 4683 6003 3349 -295 335 -113 C
ATOM 4761 C TRP A 611 32.144 124.489 225.633 1.00 37.52 C
ANISOU 4761 C TRP A 611 4745 6032 3480 -345 347 -128 C
ATOM 4762 O TRP A 611 32.792 124.628 224.618 1.00 37.47 O
ANISOU 4762 O TRP A 611 4673 6044 3520 -353 347 -96 O
ATOM 4763 CB TRP A 611 29.917 123.387 225.472 1.00 36.62 C
ANISOU 4763 CB TRP A 611 4660 5938 3317 -247 409 -82 C
ATOM 4764 CG TRP A 611 29.042 122.595 226.327 1.00 36.46 C
ANISOU 4764 CG TRP A 611 4688 5932 3235 -226 413 -96 C
ATOM 4765 CD1 TRP A 611 28.266 123.056 227.336 1.00 36.87 C
ANISOU 4765 CD1 TRP A 611 4810 5940 3259 -229 457 -133 C
ATOM 4766 CD2 TRP A 611 28.901 121.174 226.320 1.00 35.98 C
ANISOU 4766 CD2 TRP A 611 4616 5928 3125 -204 376 -76 C
ATOM 4767 NE1 TRP A 611 27.629 122.018 227.952 1.00 36.66 N
ANISOU 4767 NE1 TRP A 611 4814 5946 3170 -215 452 -135 N
ATOM 4768 CE2 TRP A 611 27.997 120.846 227.341 1.00 36.10 C
ANISOU 4768 CE2 TRP A 611 4698 5935 3086 -200 400 -99 C
ATOM 4769 CE3 TRP A 611 29.460 120.144 225.554 1.00 35.53 C
ANISOU 4769 CE3 TRP A 611 4508 5926 3066 -188 331 -44 C
ATOM 4770 CZ2 TRP A 611 27.629 119.527 227.624 1.00 35.80 C
ANISOU 4770 CZ2 TRP A 611 4676 5937 2988 -187 376 -86 C
ATOM 4771 CZ3 TRP A 611 29.076 118.825 225.822 1.00 35.22 C
ANISOU 4771 CZ3 TRP A 611 4488 5921 2971 -168 306 -34 C
ATOM 4772 CH2 TRP A 611 28.174 118.537 226.852 1.00 35.35 C
ANISOU 4772 CH2 TRP A 611 4572 5925 2933 -171 326 -53 C
ATOM 4773 N GLY A 612 32.067 125.389 226.613 1.00 38.17 N
ANISOU 4773 N GLY A 612 4899 6053 3552 -384 359 -179 N
ATOM 4774 CA GLY A 612 32.492 126.770 226.509 1.00 38.86 C
ANISOU 4774 CA GLY A 612 5002 6072 3690 -434 386 -198 C
ATOM 4775 C GLY A 612 31.328 127.642 226.969 1.00 39.17 C
ANISOU 4775 C GLY A 612 5124 6029 3730 -413 463 -218 C
ATOM 4776 O GLY A 612 30.313 127.105 227.409 1.00 38.88 O
ANISOU 4776 O GLY A 612 5119 6001 3652 -365 489 -219 O
ATOM 4777 N ASN A 613 31.487 128.972 226.851 1.00 39.85 N
ANISOU 4777 N ASN A 613 5244 6033 3865 -447 503 -233 N
ATOM 4778 CA ASN A 613 30.496 130.000 227.208 1.00 40.37 C
ANISOU 4778 CA ASN A 613 5389 6002 3949 -424 584 -254 C
ATOM 4779 C ASN A 613 30.191 130.948 226.030 1.00 40.51 C
ANISOU 4779 C ASN A 613 5386 5960 4048 -397 643 -198 C
ATOM 4780 O ASN A 613 31.045 131.735 225.634 1.00 41.00 O
ANISOU 4780 O ASN A 613 5445 5983 4151 -455 637 -197 O
ATOM 4781 CB ASN A 613 31.067 130.822 228.333 1.00 41.35 C
ANISOU 4781 CB ASN A 613 5602 6061 4050 -500 573 -335 C
ATOM 4782 CG ASN A 613 30.142 131.903 228.803 1.00 42.06 C
ANISOU 4782 CG ASN A 613 5786 6041 4156 -477 662 -369 C
ATOM 4783 OD1 ASN A 613 29.023 132.070 228.315 1.00 41.87 O
ANISOU 4783 OD1 ASN A 613 5753 5989 4166 -396 733 -329 O
ATOM 4784 ND2 ASN A 613 30.602 132.639 229.789 1.00 43.01 N
ANISOU 4784 ND2 ASN A 613 5998 6096 4248 -548 657 -446 N
ATOM 4785 N PRO A 614 28.971 130.903 225.477 1.00 40.20 N
ANISOU 4785 N PRO A 614 5331 5911 4030 -313 698 -148 N
ATOM 4786 CA PRO A 614 28.801 131.654 224.247 1.00 40.33 C
ANISOU 4786 CA PRO A 614 5321 5885 4116 -288 734 -81 C
ATOM 4787 C PRO A 614 28.601 133.133 224.453 1.00 41.33 C
ANISOU 4787 C PRO A 614 5527 5883 4294 -296 794 -102 C
ATOM 4788 O PRO A 614 28.408 133.859 223.491 1.00 41.60 O
ANISOU 4788 O PRO A 614 5554 5866 4386 -272 826 -43 O
ATOM 4789 CB PRO A 614 27.578 131.013 223.597 1.00 39.73 C
ANISOU 4789 CB PRO A 614 5196 5853 4044 -197 756 -18 C
ATOM 4790 CG PRO A 614 26.803 130.462 224.713 1.00 39.65 C
ANISOU 4790 CG PRO A 614 5217 5860 3988 -169 772 -65 C
ATOM 4791 CD PRO A 614 27.804 130.054 225.772 1.00 39.71 C
ANISOU 4791 CD PRO A 614 5260 5893 3934 -243 719 -138 C
ATOM 4792 N ASN A 615 28.683 133.600 225.685 1.00 41.99 N
ANISOU 4792 N ASN A 615 5694 5908 4352 -331 809 -184 N
ATOM 4793 CA ASN A 615 28.759 135.038 225.935 1.00 43.10 C
ANISOU 4793 CA ASN A 615 5922 5916 4537 -359 861 -217 C
ATOM 4794 C ASN A 615 30.141 135.609 225.577 1.00 43.53 C
ANISOU 4794 C ASN A 615 5976 5948 4614 -464 821 -223 C
ATOM 4795 O ASN A 615 30.395 136.810 225.729 1.00 44.52 O
ANISOU 4795 O ASN A 615 6178 5960 4777 -508 855 -250 O
ATOM 4796 CB ASN A 615 28.447 135.311 227.409 1.00 43.76 C
ANISOU 4796 CB ASN A 615 6107 5946 4575 -374 891 -313 C
ATOM 4797 CG ASN A 615 27.006 134.989 227.767 1.00 43.63 C
ANISOU 4797 CG ASN A 615 6096 5932 4550 -272 956 -311 C
ATOM 4798 OD1 ASN A 615 26.067 135.645 227.273 1.00 43.99 O
ANISOU 4798 OD1 ASN A 615 6144 5910 4660 -191 1026 -271 O
ATOM 4799 ND2 ASN A 615 26.815 133.980 228.629 1.00 43.22 N
ANISOU 4799 ND2 ASN A 615 6045 5956 4419 -274 933 -349 N
ATOM 4800 N GLU A 616 31.038 134.742 225.119 1.00 42.87 N
ANISOU 4800 N GLU A 616 5806 5971 4513 -505 752 -198 N
ATOM 4801 CA GLU A 616 32.415 135.117 224.848 1.00 43.31 C
ANISOU 4801 CA GLU A 616 5839 6029 4589 -609 711 -207 C
ATOM 4802 C GLU A 616 32.798 134.966 223.375 1.00 42.92 C
ANISOU 4802 C GLU A 616 5704 6023 4580 -604 711 -120 C
ATOM 4803 O GLU A 616 32.457 133.945 222.737 1.00 42.00 O
ANISOU 4803 O GLU A 616 5514 5997 4445 -542 696 -68 O
ATOM 4804 CB GLU A 616 33.326 134.222 225.658 1.00 43.11 C
ANISOU 4804 CB GLU A 616 5778 6096 4506 -669 626 -261 C
ATOM 4805 CG GLU A 616 32.960 134.107 227.102 1.00 43.41 C
ANISOU 4805 CG GLU A 616 5899 6115 4480 -673 615 -341 C
ATOM 4806 CD GLU A 616 34.084 133.570 227.964 1.00 43.64 C
ANISOU 4806 CD GLU A 616 5914 6211 4459 -758 519 -398 C
ATOM 4807 OE1 GLU A 616 35.003 132.922 227.444 1.00 43.31 O
ANISOU 4807 OE1 GLU A 616 5771 6256 4427 -785 458 -368 O
ATOM 4808 OE2 GLU A 616 34.051 133.792 229.193 1.00 44.27 O
ANISOU 4808 OE2 GLU A 616 6083 6254 4483 -796 504 -473 O
ATOM 4809 N TYR A 617 33.543 135.934 222.831 1.00 43.68 N
ANISOU 4809 N TYR A 617 5812 6057 4726 -677 729 -105 N
ATOM 4810 CA TYR A 617 34.039 135.781 221.465 1.00 43.44 C
ANISOU 4810 CA TYR A 617 5706 6073 4725 -687 733 -26 C
ATOM 4811 C TYR A 617 34.744 134.432 221.221 1.00 42.63 C
ANISOU 4811 C TYR A 617 5494 6116 4589 -692 674 -19 C
ATOM 4812 O TYR A 617 34.620 133.842 220.177 1.00 42.05 O
ANISOU 4812 O TYR A 617 5361 6104 4514 -649 682 46 O
ATOM 4813 CB TYR A 617 35.005 136.885 221.107 1.00 44.47 C
ANISOU 4813 CB TYR A 617 5859 6133 4906 -792 752 -25 C
ATOM 4814 CG TYR A 617 34.503 138.284 221.272 1.00 45.46 C
ANISOU 4814 CG TYR A 617 6100 6101 5070 -799 812 -30 C
ATOM 4815 CD1 TYR A 617 33.535 138.807 220.421 1.00 45.52 C
ANISOU 4815 CD1 TYR A 617 6147 6039 5110 -717 869 46 C
ATOM 4816 CD2 TYR A 617 35.038 139.115 222.259 1.00 46.46 C
ANISOU 4816 CD2 TYR A 617 6303 6145 5205 -891 807 -112 C
ATOM 4817 CE1 TYR A 617 33.088 140.114 220.573 1.00 46.55 C
ANISOU 4817 CE1 TYR A 617 6390 6015 5284 -715 925 43 C
ATOM 4818 CE2 TYR A 617 34.614 140.418 222.409 1.00 47.49 C
ANISOU 4818 CE2 TYR A 617 6551 6118 5374 -898 866 -122 C
ATOM 4819 CZ TYR A 617 33.646 140.920 221.559 1.00 47.54 C
ANISOU 4819 CZ TYR A 617 6594 6050 5417 -807 928 -43 C
ATOM 4820 OH TYR A 617 33.214 142.222 221.718 1.00 48.66 O
ANISOU 4820 OH TYR A 617 6859 6027 5604 -804 989 -51 O
ATOM 4821 N LYS A 618 35.487 133.950 222.194 1.00 42.71 N
ANISOU 4821 N LYS A 618 5481 6175 4570 -744 612 -87 N
ATOM 4822 CA LYS A 618 36.268 132.740 222.028 1.00 42.16 C
ANISOU 4822 CA LYS A 618 5308 6232 4479 -748 554 -84 C
ATOM 4823 C LYS A 618 35.406 131.570 221.652 1.00 41.07 C
ANISOU 4823 C LYS A 618 5140 6164 4302 -644 552 -44 C
ATOM 4824 O LYS A 618 35.896 130.674 221.011 1.00 40.62 O
ANISOU 4824 O LYS A 618 5001 6195 4238 -631 530 -16 O
ATOM 4825 CB LYS A 618 37.049 132.431 223.321 1.00 42.53 C
ANISOU 4825 CB LYS A 618 5351 6313 4496 -809 476 -164 C
ATOM 4826 CG LYS A 618 37.835 131.090 223.413 1.00 42.09 C
ANISOU 4826 CG LYS A 618 5192 6383 4415 -800 402 -168 C
ATOM 4827 CD LYS A 618 38.673 131.023 224.761 1.00 42.77 C
ANISOU 4827 CD LYS A 618 5286 6490 4476 -873 314 -245 C
ATOM 4828 CE LYS A 618 39.355 129.667 225.085 1.00 42.46 C
ANISOU 4828 CE LYS A 618 5159 6566 4408 -851 227 -252 C
ATOM 4829 NZ LYS A 618 40.539 129.435 224.230 1.00 42.74 N
ANISOU 4829 NZ LYS A 618 5066 6672 4503 -884 214 -224 N
ATOM 4830 N PHE A 619 34.121 131.600 222.011 1.00 40.76 N
ANISOU 4830 N PHE A 619 5164 6082 4239 -573 580 -43 N
ATOM 4831 CA PHE A 619 33.237 130.405 221.959 1.00 39.81 C
ANISOU 4831 CA PHE A 619 5021 6030 4074 -486 569 -20 C
ATOM 4832 C PHE A 619 31.918 130.527 221.199 1.00 39.46 C
ANISOU 4832 C PHE A 619 4994 5960 4040 -404 622 42 C
ATOM 4833 O PHE A 619 31.351 129.510 220.784 1.00 38.72 O
ANISOU 4833 O PHE A 619 4862 5934 3917 -346 610 76 O
ATOM 4834 CB PHE A 619 32.871 129.977 223.370 1.00 39.75 C
ANISOU 4834 CB PHE A 619 5063 6027 4015 -477 538 -85 C
ATOM 4835 CG PHE A 619 33.931 129.219 224.075 1.00 39.78 C
ANISOU 4835 CG PHE A 619 5032 6099 3984 -524 461 -130 C
ATOM 4836 CD1 PHE A 619 34.304 127.956 223.647 1.00 39.15 C
ANISOU 4836 CD1 PHE A 619 4875 6115 3883 -496 418 -104 C
ATOM 4837 CD2 PHE A 619 34.549 129.768 225.204 1.00 40.56 C
ANISOU 4837 CD2 PHE A 619 5180 6162 4070 -597 426 -200 C
ATOM 4838 CE1 PHE A 619 35.273 127.261 224.339 1.00 39.30 C
ANISOU 4838 CE1 PHE A 619 4862 6193 3877 -529 341 -142 C
ATOM 4839 CE2 PHE A 619 35.530 129.082 225.899 1.00 40.73 C
ANISOU 4839 CE2 PHE A 619 5167 6248 4059 -639 341 -237 C
ATOM 4840 CZ PHE A 619 35.894 127.838 225.478 1.00 40.11 C
ANISOU 4840 CZ PHE A 619 5007 6265 3968 -601 297 -206 C
ATOM 4841 N PHE A 620 31.412 131.755 221.060 1.00 40.09 N
ANISOU 4841 N PHE A 620 5131 5938 4162 -398 675 57 N
ATOM 4842 CA PHE A 620 30.223 132.044 220.208 1.00 39.99 C
ANISOU 4842 CA PHE A 620 5127 5894 4173 -319 720 128 C
ATOM 4843 C PHE A 620 30.161 131.222 218.904 1.00 39.35 C
ANISOU 4843 C PHE A 620 4978 5897 4078 -288 705 202 C
ATOM 4844 O PHE A 620 29.386 130.283 218.831 1.00 38.71 O
ANISOU 4844 O PHE A 620 4869 5876 3964 -231 690 219 O
ATOM 4845 CB PHE A 620 30.081 133.550 219.898 1.00 40.93 C
ANISOU 4845 CB PHE A 620 5309 5890 4352 -329 773 150 C
ATOM 4846 CG PHE A 620 28.812 133.899 219.215 1.00 41.01 C
ANISOU 4846 CG PHE A 620 5330 5861 4390 -239 811 220 C
ATOM 4847 CD1 PHE A 620 27.625 133.999 219.943 1.00 41.11 C
ANISOU 4847 CD1 PHE A 620 5372 5839 4410 -166 839 199 C
ATOM 4848 CD2 PHE A 620 28.781 134.090 217.845 1.00 41.06 C
ANISOU 4848 CD2 PHE A 620 5314 5873 4414 -225 816 309 C
ATOM 4849 CE1 PHE A 620 26.389 134.309 219.291 1.00 41.31 C
ANISOU 4849 CE1 PHE A 620 5390 5834 4471 -74 869 270 C
ATOM 4850 CE2 PHE A 620 27.579 134.402 217.172 1.00 41.24 C
ANISOU 4850 CE2 PHE A 620 5343 5865 4463 -138 837 382 C
ATOM 4851 CZ PHE A 620 26.372 134.517 217.902 1.00 41.38 C
ANISOU 4851 CZ PHE A 620 5376 5848 4499 -59 860 363 C
ATOM 4852 N ASP A 621 30.994 131.548 217.916 1.00 39.61 N
ANISOU 4852 N ASP A 621 4988 5932 4129 -334 711 242 N
ATOM 4853 CA ASP A 621 30.923 130.903 216.587 1.00 39.19 C
ANISOU 4853 CA ASP A 621 4888 5947 4056 -309 707 314 C
ATOM 4854 C ASP A 621 31.020 129.384 216.571 1.00 38.34 C
ANISOU 4854 C ASP A 621 4723 5950 3895 -288 665 301 C
ATOM 4855 O ASP A 621 30.257 128.684 215.868 1.00 37.88 O
ANISOU 4855 O ASP A 621 4646 5938 3807 -236 658 347 O
ATOM 4856 CB ASP A 621 31.943 131.476 215.595 1.00 39.72 C
ANISOU 4856 CB ASP A 621 4945 6003 4144 -374 730 351 C
ATOM 4857 CG ASP A 621 31.824 130.844 214.201 1.00 39.41 C
ANISOU 4857 CG ASP A 621 4872 6029 4072 -350 734 423 C
ATOM 4858 OD1 ASP A 621 32.386 129.728 213.995 1.00 39.19 O
ANISOU 4858 OD1 ASP A 621 4789 6094 4008 -357 711 407 O
ATOM 4859 OD2 ASP A 621 31.170 131.439 213.298 1.00 39.74 O
ANISOU 4859 OD2 ASP A 621 4949 6030 4121 -322 757 497 O
ATOM 4860 N TYR A 622 31.981 128.884 217.320 1.00 38.25 N
ANISOU 4860 N TYR A 622 4684 5977 3872 -332 634 239 N
ATOM 4861 CA TYR A 622 32.239 127.451 217.342 1.00 37.58 C
ANISOU 4861 CA TYR A 622 4550 5988 3742 -313 593 224 C
ATOM 4862 C TYR A 622 31.009 126.660 217.764 1.00 36.99 C
ANISOU 4862 C TYR A 622 4490 5934 3628 -247 577 224 C
ATOM 4863 O TYR A 622 30.576 125.775 217.045 1.00 36.51 O
ANISOU 4863 O TYR A 622 4407 5929 3536 -211 569 260 O
ATOM 4864 CB TYR A 622 33.393 127.129 218.281 1.00 37.74 C
ANISOU 4864 CB TYR A 622 4542 6036 3762 -362 552 158 C
ATOM 4865 CG TYR A 622 33.900 125.754 218.106 1.00 37.27 C
ANISOU 4865 CG TYR A 622 4426 6066 3668 -343 514 151 C
ATOM 4866 CD1 TYR A 622 33.374 124.708 218.823 1.00 36.73 C
ANISOU 4866 CD1 TYR A 622 4370 6032 3555 -300 476 128 C
ATOM 4867 CD2 TYR A 622 34.935 125.499 217.227 1.00 37.46 C
ANISOU 4867 CD2 TYR A 622 4389 6137 3707 -368 523 167 C
ATOM 4868 CE1 TYR A 622 33.862 123.429 218.661 1.00 36.39 C
ANISOU 4868 CE1 TYR A 622 4284 6060 3483 -279 442 122 C
ATOM 4869 CE2 TYR A 622 35.433 124.217 217.061 1.00 37.14 C
ANISOU 4869 CE2 TYR A 622 4298 6172 3641 -342 494 158 C
ATOM 4870 CZ TYR A 622 34.888 123.193 217.778 1.00 36.60 C
ANISOU 4870 CZ TYR A 622 4249 6129 3529 -295 451 136 C
ATOM 4871 OH TYR A 622 35.364 121.927 217.602 1.00 36.37 O
ANISOU 4871 OH TYR A 622 4180 6162 3476 -265 424 129 O
ATOM 4872 N MET A 623 30.460 126.993 218.930 1.00 37.11 N
ANISOU 4872 N MET A 623 4549 5906 3645 -238 578 182 N
ATOM 4873 CA MET A 623 29.273 126.353 219.425 1.00 36.70 C
ANISOU 4873 CA MET A 623 4512 5870 3562 -184 576 179 C
ATOM 4874 C MET A 623 28.118 126.511 218.458 1.00 36.62 C
ANISOU 4874 C MET A 623 4495 5855 3565 -131 603 248 C
ATOM 4875 O MET A 623 27.343 125.593 218.226 1.00 36.17 O
ANISOU 4875 O MET A 623 4417 5849 3476 -94 589 270 O
ATOM 4876 CB MET A 623 28.927 126.955 220.769 1.00 37.09 C
ANISOU 4876 CB MET A 623 4617 5859 3614 -190 591 122 C
ATOM 4877 CG MET A 623 29.931 126.577 221.847 1.00 37.17 C
ANISOU 4877 CG MET A 623 4640 5889 3594 -241 546 54 C
ATOM 4878 SD MET A 623 29.310 126.919 223.492 1.00 37.57 S
ANISOU 4878 SD MET A 623 4770 5887 3616 -243 562 -16 S
ATOM 4879 CE MET A 623 30.475 128.166 223.874 1.00 38.42 C
ANISOU 4879 CE MET A 623 4912 5928 3759 -322 557 -61 C
ATOM 4880 N ASN A 624 28.012 127.680 217.869 1.00 37.17 N
ANISOU 4880 N ASN A 624 4581 5860 3680 -130 637 286 N
ATOM 4881 CA ASN A 624 27.003 127.887 216.880 1.00 37.24 C
ANISOU 4881 CA ASN A 624 4581 5865 3703 -80 651 360 C
ATOM 4882 C ASN A 624 27.024 126.837 215.736 1.00 36.75 C
ANISOU 4882 C ASN A 624 4478 5888 3596 -74 621 407 C
ATOM 4883 O ASN A 624 25.997 126.432 215.250 1.00 36.60 O
ANISOU 4883 O ASN A 624 4444 5898 3564 -31 610 450 O
ATOM 4884 CB ASN A 624 27.094 129.309 216.368 1.00 38.01 C
ANISOU 4884 CB ASN A 624 4713 5875 3855 -85 687 398 C
ATOM 4885 CG ASN A 624 25.914 129.675 215.548 1.00 38.29 C
ANISOU 4885 CG ASN A 624 4744 5892 3911 -22 697 475 C
ATOM 4886 OD1 ASN A 624 24.778 129.625 216.006 1.00 38.33 O
ANISOU 4886 OD1 ASN A 624 4742 5890 3931 36 704 476 O
ATOM 4887 ND2 ASN A 624 26.157 129.982 214.293 1.00 38.54 N
ANISOU 4887 ND2 ASN A 624 4777 5923 3942 -31 694 545 N
ATOM 4888 N SER A 625 28.202 126.386 215.341 1.00 36.58 N
ANISOU 4888 N SER A 625 4440 5907 3553 -119 608 395 N
ATOM 4889 CA SER A 625 28.374 125.515 214.189 1.00 36.29 C
ANISOU 4889 CA SER A 625 4378 5938 3473 -119 592 434 C
ATOM 4890 C SER A 625 27.907 124.093 214.426 1.00 35.66 C
ANISOU 4890 C SER A 625 4280 5926 3343 -95 557 415 C
ATOM 4891 O SER A 625 27.789 123.293 213.467 1.00 35.45 O
ANISOU 4891 O SER A 625 4243 5953 3274 -89 543 446 O
ATOM 4892 CB SER A 625 29.829 125.481 213.763 1.00 36.45 C
ANISOU 4892 CB SER A 625 4379 5977 3492 -172 601 419 C
ATOM 4893 OG SER A 625 30.654 124.838 214.721 1.00 36.21 O
ANISOU 4893 OG SER A 625 4327 5975 3456 -192 578 351 O
ATOM 4894 N TYR A 626 27.676 123.746 215.688 1.00 35.43 N
ANISOU 4894 N TYR A 626 4256 5893 3311 -87 544 361 N
ATOM 4895 CA TYR A 626 27.131 122.450 215.976 1.00 34.92 C
ANISOU 4895 CA TYR A 626 4186 5883 3201 -67 515 347 C
ATOM 4896 C TYR A 626 25.835 122.453 216.788 1.00 34.90 C
ANISOU 4896 C TYR A 626 4193 5866 3203 -36 521 341 C
ATOM 4897 O TYR A 626 25.219 121.386 216.933 1.00 34.57 O
ANISOU 4897 O TYR A 626 4145 5867 3122 -25 501 339 O
ATOM 4898 CB TYR A 626 28.175 121.584 216.634 1.00 34.67 C
ANISOU 4898 CB TYR A 626 4150 5880 3143 -89 489 292 C
ATOM 4899 CG TYR A 626 28.661 122.034 218.009 1.00 34.86 C
ANISOU 4899 CG TYR A 626 4193 5868 3184 -109 484 234 C
ATOM 4900 CD1 TYR A 626 28.028 121.589 219.173 1.00 34.72 C
ANISOU 4900 CD1 TYR A 626 4203 5848 3141 -98 473 199 C
ATOM 4901 CD2 TYR A 626 29.795 122.826 218.150 1.00 35.26 C
ANISOU 4901 CD2 TYR A 626 4237 5892 3269 -148 489 211 C
ATOM 4902 CE1 TYR A 626 28.469 121.948 220.421 1.00 34.98 C
ANISOU 4902 CE1 TYR A 626 4265 5850 3175 -121 466 145 C
ATOM 4903 CE2 TYR A 626 30.237 123.178 219.392 1.00 35.52 C
ANISOU 4903 CE2 TYR A 626 4291 5896 3309 -174 475 156 C
ATOM 4904 CZ TYR A 626 29.552 122.734 220.535 1.00 35.38 C
ANISOU 4904 CZ TYR A 626 4310 5874 3256 -158 462 122 C
ATOM 4905 OH TYR A 626 29.968 123.070 221.789 1.00 35.72 O
ANISOU 4905 OH TYR A 626 4389 5890 3293 -188 446 66 O
ATOM 4906 N SER A 627 25.424 123.616 217.314 1.00 35.35 N
ANISOU 4906 N SER A 627 4265 5859 3307 -23 555 337 N
ATOM 4907 CA SER A 627 24.193 123.712 218.106 1.00 35.49 C
ANISOU 4907 CA SER A 627 4286 5861 3336 11 577 328 C
ATOM 4908 C SER A 627 23.042 123.102 217.299 1.00 35.38 C
ANISOU 4908 C SER A 627 4235 5896 3312 42 562 385 C
ATOM 4909 O SER A 627 22.776 123.565 216.189 1.00 35.63 O
ANISOU 4909 O SER A 627 4248 5926 3363 58 557 446 O
ATOM 4910 CB SER A 627 23.890 125.157 218.462 1.00 36.14 C
ANISOU 4910 CB SER A 627 4391 5861 3480 31 623 327 C
ATOM 4911 OG SER A 627 22.907 125.223 219.472 1.00 36.36 O
ANISOU 4911 OG SER A 627 4427 5871 3517 60 656 299 O
ATOM 4912 N PRO A 628 22.402 122.018 217.818 1.00 35.08 N
ANISOU 4912 N PRO A 628 4188 5905 3236 42 549 366 N
ATOM 4913 CA PRO A 628 21.447 121.375 216.920 1.00 35.04 C
ANISOU 4913 CA PRO A 628 4144 5952 3217 55 524 420 C
ATOM 4914 C PRO A 628 20.301 122.258 216.502 1.00 35.63 C
ANISOU 4914 C PRO A 628 4180 6009 3348 101 542 474 C
ATOM 4915 O PRO A 628 20.158 122.494 215.306 1.00 35.82 O
ANISOU 4915 O PRO A 628 4186 6046 3377 110 517 535 O
ATOM 4916 CB PRO A 628 21.024 120.127 217.689 1.00 34.72 C
ANISOU 4916 CB PRO A 628 4108 5954 3131 38 514 385 C
ATOM 4917 CG PRO A 628 22.294 119.733 218.277 1.00 34.38 C
ANISOU 4917 CG PRO A 628 4108 5901 3053 9 502 333 C
ATOM 4918 CD PRO A 628 22.817 121.063 218.850 1.00 34.72 C
ANISOU 4918 CD PRO A 628 4171 5880 3143 15 537 308 C
ATOM 4919 N ILE A 629 19.531 122.783 217.444 1.00 36.02 N
ANISOU 4919 N ILE A 629 4220 6026 3440 131 587 453 N
ATOM 4920 CA ILE A 629 18.432 123.656 217.044 1.00 36.72 C
ANISOU 4920 CA ILE A 629 4263 6094 3595 187 605 508 C
ATOM 4921 C ILE A 629 18.853 124.721 215.984 1.00 37.08 C
ANISOU 4921 C ILE A 629 4320 6095 3675 206 594 564 C
ATOM 4922 O ILE A 629 18.082 125.042 215.074 1.00 37.56 O
ANISOU 4922 O ILE A 629 4340 6167 3764 242 571 636 O
ATOM 4923 CB ILE A 629 17.736 124.287 218.259 1.00 37.24 C
ANISOU 4923 CB ILE A 629 4326 6114 3711 225 673 468 C
ATOM 4924 CG1 ILE A 629 16.894 123.219 218.929 1.00 37.12 C
ANISOU 4924 CG1 ILE A 629 4279 6159 3668 212 682 445 C
ATOM 4925 CG2 ILE A 629 16.820 125.402 217.841 1.00 38.11 C
ANISOU 4925 CG2 ILE A 629 4394 6183 3904 296 698 522 C
ATOM 4926 CD1 ILE A 629 15.919 123.754 219.986 1.00 37.82 C
ANISOU 4926 CD1 ILE A 629 4347 6217 3806 254 759 416 C
ATOM 4927 N ASP A 630 20.083 125.221 216.093 1.00 36.94 N
ANISOU 4927 N ASP A 630 4355 6028 3650 176 606 534 N
ATOM 4928 CA ASP A 630 20.522 126.356 215.312 1.00 37.40 C
ANISOU 4928 CA ASP A 630 4438 6029 3745 187 612 580 C
ATOM 4929 C ASP A 630 20.953 125.938 213.941 1.00 37.21 C
ANISOU 4929 C ASP A 630 4411 6052 3677 160 565 636 C
ATOM 4930 O ASP A 630 21.143 126.741 213.047 1.00 37.68 O
ANISOU 4930 O ASP A 630 4487 6075 3753 167 562 693 O
ATOM 4931 CB ASP A 630 21.642 127.052 216.052 1.00 37.44 C
ANISOU 4931 CB ASP A 630 4498 5965 3762 154 647 521 C
ATOM 4932 CG ASP A 630 21.138 127.716 217.356 1.00 37.87 C
ANISOU 4932 CG ASP A 630 4574 5956 3861 184 702 467 C
ATOM 4933 OD1 ASP A 630 20.271 128.643 217.263 1.00 41.45 O
ANISOU 4933 OD1 ASP A 630 5018 6352 4378 245 734 503 O
ATOM 4934 OD2 ASP A 630 21.583 127.308 218.475 1.00 40.85 O
ANISOU 4934 OD2 ASP A 630 4977 6335 4207 151 715 391 O
ATOM 4935 N ASN A 631 21.068 124.642 213.768 1.00 36.61 N
ANISOU 4935 N ASN A 631 4321 6053 3537 128 530 620 N
ATOM 4936 CA ASN A 631 21.511 124.102 212.514 1.00 36.46 C
ANISOU 4936 CA ASN A 631 4308 6081 3463 99 492 660 C
ATOM 4937 C ASN A 631 20.513 123.249 211.785 1.00 36.48 C
ANISOU 4937 C ASN A 631 4277 6154 3430 106 444 705 C
ATOM 4938 O ASN A 631 20.862 122.654 210.772 1.00 36.37 O
ANISOU 4938 O ASN A 631 4279 6183 3357 75 412 729 O
ATOM 4939 CB ASN A 631 22.853 123.424 212.680 1.00 35.90 C
ANISOU 4939 CB ASN A 631 4265 6029 3347 48 496 604 C
ATOM 4940 CG ASN A 631 23.925 124.407 212.857 1.00 36.12 C
ANISOU 4940 CG ASN A 631 4320 5996 3407 29 530 586 C
ATOM 4941 OD1 ASN A 631 24.528 124.815 211.900 1.00 36.38 O
ANISOU 4941 OD1 ASN A 631 4369 6021 3432 9 535 624 O
ATOM 4942 ND2 ASN A 631 24.113 124.874 214.055 1.00 36.14 N
ANISOU 4942 ND2 ASN A 631 4334 5952 3447 30 558 533 N
ATOM 4943 N VAL A 632 19.273 123.232 212.269 1.00 36.74 N
ANISOU 4943 N VAL A 632 4263 6197 3498 142 440 715 N
ATOM 4944 CA VAL A 632 18.142 122.649 211.533 1.00 37.02 C
ANISOU 4944 CA VAL A 632 4253 6297 3517 149 388 769 C
ATOM 4945 C VAL A 632 17.913 123.345 210.191 1.00 37.68 C
ANISOU 4945 C VAL A 632 4339 6377 3601 167 350 859 C
ATOM 4946 O VAL A 632 17.818 124.577 210.128 1.00 38.26 O
ANISOU 4946 O VAL A 632 4415 6387 3735 211 371 896 O
ATOM 4947 CB VAL A 632 16.847 122.670 212.356 1.00 37.37 C
ANISOU 4947 CB VAL A 632 4231 6351 3617 189 401 766 C
ATOM 4948 CG1 VAL A 632 15.655 122.622 211.463 1.00 38.04 C
ANISOU 4948 CG1 VAL A 632 4254 6485 3714 210 346 844 C
ATOM 4949 CG2 VAL A 632 16.792 121.488 213.246 1.00 36.80 C
ANISOU 4949 CG2 VAL A 632 4158 6319 3507 151 411 701 C
ATOM 4950 N ARG A 633 17.823 122.583 209.107 1.00 37.70 N
ANISOU 4950 N ARG A 633 4349 6441 3533 132 293 894 N
ATOM 4951 CA ARG A 633 17.633 123.254 207.823 1.00 38.42 C
ANISOU 4951 CA ARG A 633 4456 6530 3613 145 253 983 C
ATOM 4952 C ARG A 633 16.745 122.522 206.787 1.00 38.85 C
ANISOU 4952 C ARG A 633 4487 6662 3610 125 170 1039 C
ATOM 4953 O ARG A 633 16.362 121.378 206.965 1.00 38.52 O
ANISOU 4953 O ARG A 633 4425 6681 3532 90 145 1005 O
ATOM 4954 CB ARG A 633 19.001 123.653 207.295 1.00 38.27 C
ANISOU 4954 CB ARG A 633 4511 6472 3557 113 285 978 C
ATOM 4955 CG ARG A 633 19.688 122.601 206.421 1.00 37.95 C
ANISOU 4955 CG ARG A 633 4517 6488 3413 51 264 965 C
ATOM 4956 CD ARG A 633 21.157 122.865 206.319 1.00 37.69 C
ANISOU 4956 CD ARG A 633 4537 6420 3362 20 320 931 C
ATOM 4957 NE ARG A 633 21.829 121.947 207.218 1.00 36.89 N
ANISOU 4957 NE ARG A 633 4431 6334 3251 -2 348 841 N
ATOM 4958 CZ ARG A 633 23.012 122.163 207.769 1.00 39.37 C
ANISOU 4958 CZ ARG A 633 4760 6614 3584 -17 399 788 C
ATOM 4959 NH1 ARG A 633 23.676 123.274 207.504 1.00 42.11 N
ANISOU 4959 NH1 ARG A 633 5129 6908 3961 -21 434 813 N
ATOM 4960 NH2 ARG A 633 23.532 121.269 208.603 1.00 41.67 N
ANISOU 4960 NH2 ARG A 633 5044 6923 3866 -30 410 713 N
ATOM 4961 N ALA A 634 16.388 123.186 205.712 1.00 39.67 N
ANISOU 4961 N ALA A 634 4600 6765 3706 142 123 1128 N
ATOM 4962 CA ALA A 634 15.555 122.529 204.714 1.00 40.20 C
ANISOU 4962 CA ALA A 634 4650 6909 3714 117 34 1183 C
ATOM 4963 C ALA A 634 16.234 121.318 204.058 1.00 39.73 C
ANISOU 4963 C ALA A 634 4658 6901 3537 37 18 1144 C
ATOM 4964 O ALA A 634 17.003 121.500 203.113 1.00 39.91 O
ANISOU 4964 O ALA A 634 4756 6914 3492 10 20 1169 O
ATOM 4965 CB ALA A 634 15.173 123.521 203.664 1.00 41.25 C
ANISOU 4965 CB ALA A 634 4796 7026 3851 150 -17 1289 C
ATOM 4966 N GLN A 635 15.953 120.101 204.542 1.00 39.24 N
ANISOU 4966 N GLN A 635 4574 6888 3449 0 8 1084 N
ATOM 4967 CA GLN A 635 16.540 118.854 203.998 1.00 38.87 C
ANISOU 4967 CA GLN A 635 4594 6881 3294 -70 -3 1040 C
ATOM 4968 C GLN A 635 15.819 117.643 204.557 1.00 38.62 C
ANISOU 4968 C GLN A 635 4524 6898 3253 -104 -29 994 C
ATOM 4969 O GLN A 635 15.146 117.755 205.604 1.00 38.51 O
ANISOU 4969 O GLN A 635 4436 6880 3318 -74 -13 979 O
ATOM 4970 CB GLN A 635 18.007 118.742 204.400 1.00 38.09 C
ANISOU 4970 CB GLN A 635 4554 6738 3181 -80 78 970 C
ATOM 4971 CG GLN A 635 18.286 118.214 205.852 1.00 37.26 C
ANISOU 4971 CG GLN A 635 4422 6614 3122 -72 129 885 C
ATOM 4972 CD GLN A 635 19.718 118.514 206.301 1.00 36.72 C
ANISOU 4972 CD GLN A 635 4392 6494 3065 -67 201 833 C
ATOM 4973 OE1 GLN A 635 20.556 118.895 205.489 1.00 36.90 O
ANISOU 4973 OE1 GLN A 635 4463 6505 3054 -79 220 851 O
ATOM 4974 NE2 GLN A 635 19.995 118.379 207.583 1.00 36.16 N
ANISOU 4974 NE2 GLN A 635 4299 6397 3041 -52 240 772 N
ATOM 4975 N ASP A 636 15.985 116.476 203.933 1.00 38.58 N
ANISOU 4975 N ASP A 636 4576 6932 3151 -168 -60 967 N
ATOM 4976 CA ASP A 636 15.482 115.245 204.573 1.00 38.29 C
ANISOU 4976 CA ASP A 636 4520 6926 3102 -209 -71 913 C
ATOM 4977 C ASP A 636 16.145 114.860 205.914 1.00 37.38 C
ANISOU 4977 C ASP A 636 4409 6771 3025 -195 4 832 C
ATOM 4978 O ASP A 636 17.353 114.881 206.022 1.00 36.88 O
ANISOU 4978 O ASP A 636 4400 6668 2943 -186 56 792 O
ATOM 4979 CB ASP A 636 15.556 114.089 203.597 1.00 38.54 C
ANISOU 4979 CB ASP A 636 4627 6997 3019 -282 -118 898 C
ATOM 4980 CG ASP A 636 14.807 114.391 202.297 1.00 39.56 C
ANISOU 4980 CG ASP A 636 4758 7175 3099 -306 -207 978 C
ATOM 4981 OD1 ASP A 636 14.077 115.420 202.276 1.00 40.09 O
ANISOU 4981 OD1 ASP A 636 4749 7248 3235 -260 -239 1049 O
ATOM 4982 OD2 ASP A 636 14.946 113.617 201.309 1.00 39.93 O
ANISOU 4982 OD2 ASP A 636 4885 7249 3037 -369 -246 971 O
ATOM 4983 N TYR A 637 15.346 114.539 206.937 1.00 37.29 N
ANISOU 4983 N TYR A 637 4335 6769 3065 -194 9 812 N
ATOM 4984 CA TYR A 637 15.813 113.858 208.169 1.00 36.58 C
ANISOU 4984 CA TYR A 637 4262 6650 2985 -199 64 736 C
ATOM 4985 C TYR A 637 15.124 112.463 208.289 1.00 36.69 C
ANISOU 4985 C TYR A 637 4285 6703 2953 -265 29 710 C
ATOM 4986 O TYR A 637 14.112 112.226 207.631 1.00 37.36 O
ANISOU 4986 O TYR A 637 4334 6839 3022 -302 -33 751 O
ATOM 4987 CB TYR A 637 15.459 114.712 209.372 1.00 36.48 C
ANISOU 4987 CB TYR A 637 4182 6610 3068 -147 111 732 C
ATOM 4988 CG TYR A 637 16.173 116.061 209.497 1.00 36.37 C
ANISOU 4988 CG TYR A 637 4169 6543 3106 -87 155 745 C
ATOM 4989 CD1 TYR A 637 15.670 117.188 208.871 1.00 37.00 C
ANISOU 4989 CD1 TYR A 637 4207 6620 3230 -47 134 815 C
ATOM 4990 CD2 TYR A 637 17.333 116.220 210.297 1.00 35.74 C
ANISOU 4990 CD2 TYR A 637 4132 6412 3035 -71 213 688 C
ATOM 4991 CE1 TYR A 637 16.298 118.427 208.993 1.00 36.99 C
ANISOU 4991 CE1 TYR A 637 4217 6561 3278 1 176 827 C
ATOM 4992 CE2 TYR A 637 17.965 117.477 210.445 1.00 35.74 C
ANISOU 4992 CE2 TYR A 637 4134 6361 3086 -28 251 697 C
ATOM 4993 CZ TYR A 637 17.431 118.575 209.786 1.00 36.37 C
ANISOU 4993 CZ TYR A 637 4180 6432 3206 6 236 766 C
ATOM 4994 OH TYR A 637 18.003 119.840 209.868 1.00 36.49 O
ANISOU 4994 OH TYR A 637 4206 6388 3272 44 274 780 O
ATOM 4995 N PRO A 638 15.622 111.531 209.141 1.00 36.15 N
ANISOU 4995 N PRO A 638 4264 6609 2864 -285 64 645 N
ATOM 4996 CA PRO A 638 14.897 110.249 209.181 1.00 36.41 C
ANISOU 4996 CA PRO A 638 4312 6670 2852 -354 31 627 C
ATOM 4997 C PRO A 638 13.808 110.203 210.248 1.00 36.61 C
ANISOU 4997 C PRO A 638 4260 6714 2937 -364 46 629 C
ATOM 4998 O PRO A 638 13.629 111.160 210.978 1.00 36.55 O
ANISOU 4998 O PRO A 638 4190 6694 3004 -311 86 639 O
ATOM 4999 CB PRO A 638 15.997 109.255 209.570 1.00 35.84 C
ANISOU 4999 CB PRO A 638 4338 6553 2728 -365 63 560 C
ATOM 5000 CG PRO A 638 16.946 110.041 210.393 1.00 35.26 C
ANISOU 5000 CG PRO A 638 4260 6435 2703 -300 121 538 C
ATOM 5001 CD PRO A 638 16.710 111.528 210.131 1.00 35.45 C
ANISOU 5001 CD PRO A 638 4214 6467 2789 -252 126 589 C
ATOM 5002 N HIS A 639 13.088 109.094 210.339 1.00 36.94 N
ANISOU 5002 N HIS A 639 4308 6782 2946 -436 19 616 N
ATOM 5003 CA HIS A 639 12.155 108.885 211.431 1.00 37.17 C
ANISOU 5003 CA HIS A 639 4274 6825 3023 -456 48 609 C
ATOM 5004 C HIS A 639 12.854 109.137 212.775 1.00 36.52 C
ANISOU 5004 C HIS A 639 4219 6688 2969 -409 125 565 C
ATOM 5005 O HIS A 639 13.917 108.563 213.046 1.00 35.96 O
ANISOU 5005 O HIS A 639 4242 6570 2851 -407 142 521 O
ATOM 5006 CB HIS A 639 11.570 107.466 211.354 1.00 37.56 C
ANISOU 5006 CB HIS A 639 4360 6894 3015 -554 15 591 C
ATOM 5007 CG HIS A 639 10.818 107.219 210.088 1.00 38.33 C
ANISOU 5007 CG HIS A 639 4431 7050 3081 -612 -69 632 C
ATOM 5008 ND1 HIS A 639 9.570 107.757 209.846 1.00 39.14 N
ANISOU 5008 ND1 HIS A 639 4408 7220 3243 -622 -107 687 N
ATOM 5009 CD2 HIS A 639 11.165 106.552 208.961 1.00 38.50 C
ANISOU 5009 CD2 HIS A 639 4537 7074 3018 -659 -124 626 C
ATOM 5010 CE1 HIS A 639 9.175 107.416 208.636 1.00 39.78 C
ANISOU 5010 CE1 HIS A 639 4497 7346 3274 -678 -192 716 C
ATOM 5011 NE2 HIS A 639 10.119 106.678 208.080 1.00 39.41 N
ANISOU 5011 NE2 HIS A 639 4582 7258 3133 -705 -202 677 N
ATOM 5012 N LEU A 640 12.264 110.000 213.603 1.00 36.70 N
ANISOU 5012 N LEU A 640 4160 6715 3068 -369 171 577 N
ATOM 5013 CA LEU A 640 12.863 110.323 214.887 1.00 36.22 C
ANISOU 5013 CA LEU A 640 4129 6605 3028 -329 241 535 C
ATOM 5014 C LEU A 640 11.862 110.337 216.015 1.00 36.65 C
ANISOU 5014 C LEU A 640 4124 6674 3126 -342 295 528 C
ATOM 5015 O LEU A 640 10.821 110.968 215.926 1.00 37.29 O
ANISOU 5015 O LEU A 640 4100 6794 3272 -327 302 565 O
ATOM 5016 CB LEU A 640 13.529 111.697 214.813 1.00 35.96 C
ANISOU 5016 CB LEU A 640 4080 6541 3043 -249 264 545 C
ATOM 5017 CG LEU A 640 14.042 112.322 216.105 1.00 35.65 C
ANISOU 5017 CG LEU A 640 4059 6451 3034 -206 333 505 C
ATOM 5018 CD1 LEU A 640 15.300 111.623 216.524 1.00 35.01 C
ANISOU 5018 CD1 LEU A 640 4080 6329 2892 -218 335 456 C
ATOM 5019 CD2 LEU A 640 14.309 113.774 215.885 1.00 35.70 C
ANISOU 5019 CD2 LEU A 640 4030 6433 3101 -138 351 527 C
ATOM 5020 N MET A 641 12.195 109.665 217.102 1.00 36.38 N
ANISOU 5020 N MET A 641 4159 6608 3057 -367 335 483 N
ATOM 5021 CA MET A 641 11.420 109.791 218.345 1.00 36.79 C
ANISOU 5021 CA MET A 641 4172 6663 3142 -374 406 468 C
ATOM 5022 C MET A 641 12.230 110.510 219.391 1.00 36.38 C
ANISOU 5022 C MET A 641 4168 6557 3099 -319 464 430 C
ATOM 5023 O MET A 641 13.356 110.106 219.668 1.00 35.81 O
ANISOU 5023 O MET A 641 4192 6441 2972 -317 452 398 O
ATOM 5024 CB MET A 641 10.995 108.429 218.884 1.00 37.03 C
ANISOU 5024 CB MET A 641 4250 6701 3118 -460 413 450 C
ATOM 5025 CG MET A 641 10.123 108.515 220.123 1.00 38.13 C
ANISOU 5025 CG MET A 641 4351 6852 3287 -478 495 438 C
ATOM 5026 SD MET A 641 9.405 106.917 220.528 1.00 43.21 S
ANISOU 5026 SD MET A 641 5036 7512 3871 -597 498 432 S
ATOM 5027 CE MET A 641 9.298 107.096 222.298 1.00 43.32 C
ANISOU 5027 CE MET A 641 5088 7494 3876 -594 607 395 C
ATOM 5028 N ILE A 642 11.664 111.577 219.949 1.00 36.78 N
ANISOU 5028 N ILE A 642 4150 6609 3217 -272 524 433 N
ATOM 5029 CA ILE A 642 12.265 112.281 221.074 1.00 36.60 C
ANISOU 5029 CA ILE A 642 4174 6533 3198 -230 586 391 C
ATOM 5030 C ILE A 642 11.464 111.985 222.344 1.00 37.15 C
ANISOU 5030 C ILE A 642 4243 6610 3264 -262 665 366 C
ATOM 5031 O ILE A 642 10.251 112.058 222.306 1.00 37.87 O
ANISOU 5031 O ILE A 642 4239 6747 3404 -273 697 390 O
ATOM 5032 CB ILE A 642 12.212 113.779 220.845 1.00 36.79 C
ANISOU 5032 CB ILE A 642 4137 6541 3302 -153 611 406 C
ATOM 5033 CG1 ILE A 642 12.793 114.122 219.474 1.00 36.45 C
ANISOU 5033 CG1 ILE A 642 4083 6499 3266 -128 539 444 C
ATOM 5034 CG2 ILE A 642 12.882 114.527 222.029 1.00 36.68 C
ANISOU 5034 CG2 ILE A 642 4186 6465 3285 -118 674 355 C
ATOM 5035 CD1 ILE A 642 12.158 115.294 218.820 1.00 36.97 C
ANISOU 5035 CD1 ILE A 642 4057 6574 3416 -68 541 491 C
ATOM 5036 N GLN A 643 12.144 111.683 223.449 1.00 36.92 N
ANISOU 5036 N GLN A 643 4315 6538 3174 -277 695 320 N
ATOM 5037 CA GLN A 643 11.523 111.373 224.752 1.00 37.48 C
ANISOU 5037 CA GLN A 643 4413 6608 3220 -313 776 292 C
ATOM 5038 C GLN A 643 11.969 112.452 225.705 1.00 37.55 C
ANISOU 5038 C GLN A 643 4459 6570 3239 -261 837 251 C
ATOM 5039 O GLN A 643 13.162 112.585 225.931 1.00 37.01 O
ANISOU 5039 O GLN A 643 4475 6456 3130 -245 803 225 O
ATOM 5040 CB GLN A 643 12.018 110.012 225.272 1.00 37.24 C
ANISOU 5040 CB GLN A 643 4498 6560 3093 -381 749 275 C
ATOM 5041 CG GLN A 643 11.389 109.505 226.572 1.00 39.64 C
ANISOU 5041 CG GLN A 643 4848 6863 3352 -434 828 253 C
ATOM 5042 CD GLN A 643 12.113 109.977 227.888 1.00 44.79 C
ANISOU 5042 CD GLN A 643 5602 7462 3954 -413 874 205 C
ATOM 5043 OE1 GLN A 643 13.255 109.563 228.173 1.00 48.07 O
ANISOU 5043 OE1 GLN A 643 6124 7837 4304 -414 819 188 O
ATOM 5044 NE2 GLN A 643 11.432 110.819 228.692 1.00 42.19 N
ANISOU 5044 NE2 GLN A 643 5240 7135 3656 -394 973 182 N
ATOM 5045 N ALA A 644 11.035 113.203 226.284 1.00 38.32 N
ANISOU 5045 N ALA A 644 4494 6675 3390 -237 929 242 N
ATOM 5046 CA ALA A 644 11.378 114.253 227.259 1.00 38.56 C
ANISOU 5046 CA ALA A 644 4571 6653 3425 -192 999 195 C
ATOM 5047 C ALA A 644 10.627 114.057 228.565 1.00 39.37 C
ANISOU 5047 C ALA A 644 4703 6760 3497 -226 1105 160 C
ATOM 5048 O ALA A 644 9.673 113.295 228.610 1.00 39.86 O
ANISOU 5048 O ALA A 644 4716 6870 3558 -275 1135 181 O
ATOM 5049 CB ALA A 644 11.114 115.641 226.693 1.00 38.82 C
ANISOU 5049 CB ALA A 644 4516 6672 3559 -110 1020 209 C
ATOM 5050 N GLY A 645 11.058 114.737 229.628 1.00 39.62 N
ANISOU 5050 N GLY A 645 4817 6740 3497 -207 1165 107 N
ATOM 5051 CA GLY A 645 10.377 114.678 230.926 1.00 40.52 C
ANISOU 5051 CA GLY A 645 4972 6852 3573 -237 1280 68 C
ATOM 5052 C GLY A 645 10.145 116.079 231.474 1.00 41.20 C
ANISOU 5052 C GLY A 645 5047 6896 3711 -170 1376 26 C
ATOM 5053 O GLY A 645 11.082 116.875 231.574 1.00 40.87 O
ANISOU 5053 O GLY A 645 5069 6798 3663 -134 1349 -4 O
ATOM 5054 N LEU A 646 8.902 116.387 231.849 1.00 42.25 N
ANISOU 5054 N LEU A 646 5099 7054 3899 -154 1493 21 N
ATOM 5055 CA LEU A 646 8.568 117.743 232.316 1.00 43.06 C
ANISOU 5055 CA LEU A 646 5184 7112 4065 -79 1597 -20 C
ATOM 5056 C LEU A 646 9.422 118.310 233.455 1.00 43.20 C
ANISOU 5056 C LEU A 646 5360 7055 3999 -84 1636 -94 C
ATOM 5057 O LEU A 646 9.800 119.472 233.413 1.00 43.31 O
ANISOU 5057 O LEU A 646 5389 7010 4059 -22 1649 -121 O
ATOM 5058 CB LEU A 646 7.087 117.883 232.659 1.00 44.34 C
ANISOU 5058 CB LEU A 646 5235 7316 4295 -62 1730 -19 C
ATOM 5059 CG LEU A 646 6.614 119.332 232.838 1.00 45.27 C
ANISOU 5059 CG LEU A 646 5301 7387 4511 39 1833 -49 C
ATOM 5060 CD1 LEU A 646 6.719 120.110 231.551 1.00 44.88 C
ANISOU 5060 CD1 LEU A 646 5152 7327 4574 121 1753 2 C
ATOM 5061 CD2 LEU A 646 5.179 119.373 233.363 1.00 46.70 C
ANISOU 5061 CD2 LEU A 646 5378 7613 4752 52 1981 -57 C
ATOM 5062 N HIS A 647 9.715 117.529 234.477 1.00 43.30 N
ANISOU 5062 N HIS A 647 5496 7067 3890 -159 1652 -126 N
ATOM 5063 CA HIS A 647 10.457 118.120 235.595 1.00 43.63 C
ANISOU 5063 CA HIS A 647 5688 7040 3847 -167 1687 -198 C
ATOM 5064 C HIS A 647 11.984 117.865 235.572 1.00 42.65 C
ANISOU 5064 C HIS A 647 5678 6884 3643 -198 1550 -205 C
ATOM 5065 O HIS A 647 12.628 117.760 236.625 1.00 42.90 O
ANISOU 5065 O HIS A 647 5854 6882 3563 -243 1550 -253 O
ATOM 5066 CB HIS A 647 9.798 117.745 236.924 1.00 44.71 C
ANISOU 5066 CB HIS A 647 5905 7185 3898 -220 1813 -242 C
ATOM 5067 CG HIS A 647 8.335 118.051 236.954 1.00 45.80 C
ANISOU 5067 CG HIS A 647 5918 7358 4126 -186 1956 -239 C
ATOM 5068 ND1 HIS A 647 7.846 119.301 237.272 1.00 46.76 N
ANISOU 5068 ND1 HIS A 647 6012 7437 4318 -111 2074 -285 N
ATOM 5069 CD2 HIS A 647 7.257 117.291 236.635 1.00 46.15 C
ANISOU 5069 CD2 HIS A 647 5845 7476 4214 -212 1996 -192 C
ATOM 5070 CE1 HIS A 647 6.526 119.287 237.180 1.00 47.69 C
ANISOU 5070 CE1 HIS A 647 5995 7604 4521 -86 2184 -267 C
ATOM 5071 NE2 HIS A 647 6.144 118.080 236.797 1.00 47.34 N
ANISOU 5071 NE2 HIS A 647 5891 7635 4462 -151 2137 -210 N
ATOM 5072 N ASP A 648 12.542 117.815 234.356 1.00 41.66 N
ANISOU 5072 N ASP A 648 5483 6770 3577 -172 1436 -157 N
ATOM 5073 CA ASP A 648 13.921 117.406 234.098 1.00 40.73 C
ANISOU 5073 CA ASP A 648 5435 6637 3402 -197 1302 -150 C
ATOM 5074 C ASP A 648 14.890 118.526 234.485 1.00 40.81 C
ANISOU 5074 C ASP A 648 5521 6580 3405 -175 1288 -202 C
ATOM 5075 O ASP A 648 15.047 119.518 233.767 1.00 40.67 O
ANISOU 5075 O ASP A 648 5443 6533 3476 -120 1281 -197 O
ATOM 5076 CB ASP A 648 14.038 116.979 232.616 1.00 39.82 C
ANISOU 5076 CB ASP A 648 5212 6561 3357 -177 1208 -82 C
ATOM 5077 CG ASP A 648 15.419 116.422 232.232 1.00 38.90 C
ANISOU 5077 CG ASP A 648 5151 6438 3192 -198 1076 -70 C
ATOM 5078 OD1 ASP A 648 16.412 116.798 232.860 1.00 38.91 O
ANISOU 5078 OD1 ASP A 648 5243 6397 3142 -207 1045 -111 O
ATOM 5079 OD2 ASP A 648 15.503 115.632 231.252 1.00 38.26 O
ANISOU 5079 OD2 ASP A 648 5015 6394 3128 -204 1004 -20 O
ATOM 5080 N PRO A 649 15.554 118.374 235.639 1.00 41.13 N
ANISOU 5080 N PRO A 649 5702 6593 3334 -224 1279 -252 N
ATOM 5081 CA PRO A 649 16.377 119.490 236.129 1.00 41.44 C
ANISOU 5081 CA PRO A 649 5819 6567 3361 -216 1274 -311 C
ATOM 5082 C PRO A 649 17.719 119.569 235.426 1.00 40.59 C
ANISOU 5082 C PRO A 649 5705 6449 3268 -215 1139 -293 C
ATOM 5083 O PRO A 649 18.559 120.374 235.805 1.00 40.82 O
ANISOU 5083 O PRO A 649 5799 6429 3281 -224 1113 -339 O
ATOM 5084 CB PRO A 649 16.586 119.153 237.600 1.00 42.18 C
ANISOU 5084 CB PRO A 649 6066 6644 3316 -279 1300 -364 C
ATOM 5085 CG PRO A 649 16.516 117.662 237.647 1.00 41.80 C
ANISOU 5085 CG PRO A 649 6032 6651 3200 -324 1248 -318 C
ATOM 5086 CD PRO A 649 15.651 117.184 236.500 1.00 41.29 C
ANISOU 5086 CD PRO A 649 5820 6636 3231 -293 1261 -253 C
ATOM 5087 N ARG A 650 17.910 118.733 234.417 1.00 39.71 N
ANISOU 5087 N ARG A 650 5517 6385 3187 -210 1058 -231 N
ATOM 5088 CA ARG A 650 19.182 118.582 233.733 1.00 38.94 C
ANISOU 5088 CA ARG A 650 5408 6289 3098 -212 935 -210 C
ATOM 5089 C ARG A 650 19.097 119.091 232.275 1.00 38.38 C
ANISOU 5089 C ARG A 650 5214 6225 3143 -160 919 -164 C
ATOM 5090 O ARG A 650 19.806 120.033 231.883 1.00 38.30 O
ANISOU 5090 O ARG A 650 5193 6179 3181 -143 894 -175 O
ATOM 5091 CB ARG A 650 19.624 117.117 233.805 1.00 38.50 C
ANISOU 5091 CB ARG A 650 5386 6275 2967 -250 851 -180 C
ATOM 5092 CG ARG A 650 20.146 116.704 235.200 1.00 39.06 C
ANISOU 5092 CG ARG A 650 5596 6330 2914 -302 828 -221 C
ATOM 5093 CD ARG A 650 20.445 115.203 235.275 1.00 38.75 C
ANISOU 5093 CD ARG A 650 5595 6324 2805 -331 752 -182 C
ATOM 5094 NE ARG A 650 20.729 114.709 236.624 1.00 39.42 N
ANISOU 5094 NE ARG A 650 5818 6396 2765 -381 736 -209 N
ATOM 5095 CZ ARG A 650 21.664 113.811 236.852 1.00 39.30 C
ANISOU 5095 CZ ARG A 650 5860 6386 2685 -398 627 -190 C
ATOM 5096 NH1 ARG A 650 22.375 113.362 235.832 1.00 38.55 N
ANISOU 5096 NH1 ARG A 650 5692 6308 2646 -368 539 -152 N
ATOM 5097 NH2 ARG A 650 21.915 113.370 238.059 1.00 40.00 N
ANISOU 5097 NH2 ARG A 650 6079 6462 2656 -442 604 -207 N
ATOM 5098 N VAL A 651 18.231 118.469 231.481 1.00 38.08 N
ANISOU 5098 N VAL A 651 5089 6234 3145 -143 932 -111 N
ATOM 5099 CA VAL A 651 17.924 118.973 230.199 1.00 37.77 C
ANISOU 5099 CA VAL A 651 4942 6203 3205 -95 927 -66 C
ATOM 5100 C VAL A 651 16.478 119.450 230.335 1.00 38.47 C
ANISOU 5100 C VAL A 651 4974 6295 3349 -61 1036 -62 C
ATOM 5101 O VAL A 651 15.590 118.641 230.541 1.00 38.66 O
ANISOU 5101 O VAL A 651 4974 6363 3353 -80 1071 -46 O
ATOM 5102 CB VAL A 651 18.092 117.857 229.129 1.00 36.99 C
ANISOU 5102 CB VAL A 651 4790 6160 3106 -105 846 -8 C
ATOM 5103 CG1 VAL A 651 17.689 118.348 227.749 1.00 36.77 C
ANISOU 5103 CG1 VAL A 651 4655 6146 3171 -60 838 44 C
ATOM 5104 CG2 VAL A 651 19.509 117.387 229.089 1.00 36.47 C
ANISOU 5104 CG2 VAL A 651 4776 6090 2992 -129 751 -16 C
ATOM 5105 N ALA A 652 16.244 120.764 230.238 1.00 38.96 N
ANISOU 5105 N ALA A 652 5012 6307 3484 -11 1093 -77 N
ATOM 5106 CA ALA A 652 14.897 121.358 230.265 1.00 39.76 C
ANISOU 5106 CA ALA A 652 5042 6405 3660 41 1197 -70 C
ATOM 5107 C ALA A 652 13.948 120.848 229.206 1.00 39.61 C
ANISOU 5107 C ALA A 652 4895 6451 3704 64 1183 2 C
ATOM 5108 O ALA A 652 14.269 120.771 228.032 1.00 39.01 O
ANISOU 5108 O ALA A 652 4764 6395 3664 77 1104 54 O
ATOM 5109 CB ALA A 652 14.980 122.833 230.184 1.00 40.28 C
ANISOU 5109 CB ALA A 652 5111 6396 3798 97 1242 -91 C
ATOM 5110 N TYR A 653 12.749 120.515 229.648 1.00 40.27 N
ANISOU 5110 N TYR A 653 4931 6571 3799 66 1263 3 N
ATOM 5111 CA TYR A 653 11.686 120.039 228.762 1.00 40.37 C
ANISOU 5111 CA TYR A 653 4813 6652 3876 81 1256 67 C
ATOM 5112 C TYR A 653 11.518 120.873 227.463 1.00 40.35 C
ANISOU 5112 C TYR A 653 4711 6642 3978 151 1215 125 C
ATOM 5113 O TYR A 653 11.105 120.344 226.439 1.00 40.10 O
ANISOU 5113 O TYR A 653 4592 6670 3976 148 1154 187 O
ATOM 5114 CB TYR A 653 10.353 119.992 229.558 1.00 41.46 C
ANISOU 5114 CB TYR A 653 4900 6815 4037 87 1379 50 C
ATOM 5115 CG TYR A 653 9.668 121.339 229.627 1.00 42.44 C
ANISOU 5115 CG TYR A 653 4965 6895 4265 178 1472 39 C
ATOM 5116 CD1 TYR A 653 8.944 121.824 228.520 1.00 42.74 C
ANISOU 5116 CD1 TYR A 653 4865 6956 4419 246 1452 105 C
ATOM 5117 CD2 TYR A 653 9.770 122.132 230.762 1.00 43.15 C
ANISOU 5117 CD2 TYR A 653 5143 6916 4335 197 1573 -34 C
ATOM 5118 CE1 TYR A 653 8.346 123.050 228.555 1.00 43.72 C
ANISOU 5118 CE1 TYR A 653 4936 7031 4643 339 1532 100 C
ATOM 5119 CE2 TYR A 653 9.154 123.348 230.823 1.00 44.14 C
ANISOU 5119 CE2 TYR A 653 5222 6990 4558 285 1663 -47 C
ATOM 5120 CZ TYR A 653 8.448 123.806 229.709 1.00 44.41 C
ANISOU 5120 CZ TYR A 653 5114 7045 4716 360 1642 23 C
ATOM 5121 OH TYR A 653 7.852 125.027 229.722 1.00 45.48 O
ANISOU 5121 OH TYR A 653 5202 7122 4955 459 1726 17 O
ATOM 5122 N TRP A 654 11.798 122.175 227.517 1.00 40.71 N
ANISOU 5122 N TRP A 654 4778 6614 4077 211 1250 105 N
ATOM 5123 CA TRP A 654 11.484 123.027 226.377 1.00 40.93 C
ANISOU 5123 CA TRP A 654 4717 6628 4207 283 1224 165 C
ATOM 5124 C TRP A 654 12.453 122.775 225.241 1.00 39.96 C
ANISOU 5124 C TRP A 654 4605 6516 4062 259 1105 210 C
ATOM 5125 O TRP A 654 12.100 122.918 224.046 1.00 39.96 O
ANISOU 5125 O TRP A 654 4522 6544 4119 292 1052 280 O
ATOM 5126 CB TRP A 654 11.417 124.516 226.726 1.00 41.76 C
ANISOU 5126 CB TRP A 654 4845 6640 4383 358 1301 136 C
ATOM 5127 CG TRP A 654 12.624 125.108 227.401 1.00 41.54 C
ANISOU 5127 CG TRP A 654 4954 6530 4301 332 1306 70 C
ATOM 5128 CD1 TRP A 654 13.763 125.557 226.804 1.00 40.97 C
ANISOU 5128 CD1 TRP A 654 4930 6414 4222 320 1232 80 C
ATOM 5129 CD2 TRP A 654 12.789 125.348 228.815 1.00 42.05 C
ANISOU 5129 CD2 TRP A 654 5122 6545 4310 309 1390 -18 C
ATOM 5130 NE1 TRP A 654 14.631 126.051 227.758 1.00 41.08 N
ANISOU 5130 NE1 TRP A 654 5064 6359 4186 288 1259 5 N
ATOM 5131 CE2 TRP A 654 14.063 125.929 228.994 1.00 41.73 C
ANISOU 5131 CE2 TRP A 654 5188 6436 4233 281 1351 -57 C
ATOM 5132 CE3 TRP A 654 11.998 125.089 229.940 1.00 42.79 C
ANISOU 5132 CE3 TRP A 654 5233 6652 4376 302 1495 -67 C
ATOM 5133 CZ2 TRP A 654 14.560 126.257 230.236 1.00 42.14 C
ANISOU 5133 CZ2 TRP A 654 5362 6431 4218 245 1401 -142 C
ATOM 5134 CZ3 TRP A 654 12.486 125.432 231.181 1.00 43.20 C
ANISOU 5134 CZ3 TRP A 654 5415 6644 4356 270 1554 -153 C
ATOM 5135 CH2 TRP A 654 13.758 126.014 231.320 1.00 42.88 C
ANISOU 5135 CH2 TRP A 654 5481 6534 4276 242 1502 -190 C
ATOM 5136 N GLU A 655 13.656 122.341 225.606 1.00 39.22 N
ANISOU 5136 N GLU A 655 4611 6407 3882 201 1061 170 N
ATOM 5137 CA GLU A 655 14.673 122.044 224.599 1.00 38.35 C
ANISOU 5137 CA GLU A 655 4515 6309 3748 176 959 204 C
ATOM 5138 C GLU A 655 14.227 121.068 223.524 1.00 37.98 C
ANISOU 5138 C GLU A 655 4393 6341 3697 158 891 268 C
ATOM 5139 O GLU A 655 14.219 121.429 222.355 1.00 37.93 O
ANISOU 5139 O GLU A 655 4336 6341 3733 186 844 325 O
ATOM 5140 CB GLU A 655 16.024 121.660 225.220 1.00 37.75 C
ANISOU 5140 CB GLU A 655 4545 6211 3587 119 922 152 C
ATOM 5141 CG GLU A 655 16.624 122.768 226.099 1.00 38.17 C
ANISOU 5141 CG GLU A 655 4677 6181 3644 128 970 91 C
ATOM 5142 CD GLU A 655 18.142 122.756 226.082 1.00 43.25 C
ANISOU 5142 CD GLU A 655 5389 6802 4241 85 902 67 C
ATOM 5143 OE1 GLU A 655 18.714 122.330 225.027 1.00 44.31 O
ANISOU 5143 OE1 GLU A 655 5492 6970 4376 74 829 111 O
ATOM 5144 OE2 GLU A 655 18.755 123.151 227.123 1.00 44.28 O
ANISOU 5144 OE2 GLU A 655 5605 6885 4334 59 922 3 O
ATOM 5145 N PRO A 656 13.850 119.842 223.883 1.00 37.81 N
ANISOU 5145 N PRO A 656 4370 6375 3620 107 885 261 N
ATOM 5146 CA PRO A 656 13.478 119.028 222.763 1.00 37.54 C
ANISOU 5146 CA PRO A 656 4273 6407 3584 87 816 319 C
ATOM 5147 C PRO A 656 12.185 119.515 222.175 1.00 38.31 C
ANISOU 5147 C PRO A 656 4254 6535 3768 135 836 372 C
ATOM 5148 O PRO A 656 11.931 119.300 220.989 1.00 38.25 O
ANISOU 5148 O PRO A 656 4188 6569 3777 136 768 432 O
ATOM 5149 CB PRO A 656 13.251 117.665 223.383 1.00 37.37 C
ANISOU 5149 CB PRO A 656 4281 6429 3490 20 816 297 C
ATOM 5150 CG PRO A 656 13.048 117.917 224.752 1.00 37.81 C
ANISOU 5150 CG PRO A 656 4381 6454 3532 19 901 243 C
ATOM 5151 CD PRO A 656 13.960 119.028 225.080 1.00 37.75 C
ANISOU 5151 CD PRO A 656 4433 6374 3535 55 916 208 C
ATOM 5152 N ALA A 657 11.375 120.190 222.992 1.00 39.14 N
ANISOU 5152 N ALA A 657 4324 6618 3928 177 927 351 N
ATOM 5153 CA ALA A 657 10.085 120.691 222.527 1.00 40.06 C
ANISOU 5153 CA ALA A 657 4315 6766 4142 234 952 402 C
ATOM 5154 C ALA A 657 10.217 121.611 221.285 1.00 40.18 C
ANISOU 5154 C ALA A 657 4288 6758 4219 296 893 466 C
ATOM 5155 O ALA A 657 9.430 121.517 220.328 1.00 40.59 O
ANISOU 5155 O ALA A 657 4241 6864 4317 314 842 534 O
ATOM 5156 CB ALA A 657 9.399 121.396 223.654 1.00 40.98 C
ANISOU 5156 CB ALA A 657 4416 6847 4308 280 1072 358 C
ATOM 5157 N LYS A 658 11.221 122.491 221.326 1.00 39.90 N
ANISOU 5157 N LYS A 658 4334 6643 4182 321 897 444 N
ATOM 5158 CA LYS A 658 11.511 123.443 220.248 1.00 40.03 C
ANISOU 5158 CA LYS A 658 4339 6622 4249 372 851 501 C
ATOM 5159 C LYS A 658 12.082 122.727 219.019 1.00 39.31 C
ANISOU 5159 C LYS A 658 4255 6579 4101 324 745 549 C
ATOM 5160 O LYS A 658 11.850 123.085 217.866 1.00 39.58 O
ANISOU 5160 O LYS A 658 4245 6627 4168 353 688 621 O
ATOM 5161 CB LYS A 658 12.560 124.456 220.728 1.00 39.91 C
ANISOU 5161 CB LYS A 658 4424 6506 4234 389 889 455 C
ATOM 5162 CG LYS A 658 12.240 125.283 221.987 1.00 40.65 C
ANISOU 5162 CG LYS A 658 4545 6530 4368 432 999 393 C
ATOM 5163 CD LYS A 658 13.334 126.331 222.090 1.00 40.58 C
ANISOU 5163 CD LYS A 658 4633 6422 4362 439 1008 365 C
ATOM 5164 CE LYS A 658 13.205 127.237 223.264 1.00 41.33 C
ANISOU 5164 CE LYS A 658 4783 6433 4488 474 1111 296 C
ATOM 5165 NZ LYS A 658 14.100 128.396 222.985 1.00 41.46 N
ANISOU 5165 NZ LYS A 658 4873 6351 4530 489 1106 293 N
ATOM 5166 N TRP A 659 12.872 121.709 219.291 1.00 38.45 N
ANISOU 5166 N TRP A 659 4212 6493 3904 251 720 508 N
ATOM 5167 CA TRP A 659 13.700 121.102 218.271 1.00 37.75 C
ANISOU 5167 CA TRP A 659 4157 6431 3754 207 637 534 C
ATOM 5168 C TRP A 659 12.741 120.300 217.459 1.00 37.98 C
ANISOU 5168 C TRP A 659 4110 6543 3780 187 582 587 C
ATOM 5169 O TRP A 659 12.786 120.368 216.242 1.00 38.03 O
ANISOU 5169 O TRP A 659 4098 6570 3781 189 516 645 O
ATOM 5170 CB TRP A 659 14.818 120.276 218.949 1.00 36.92 C
ANISOU 5170 CB TRP A 659 4143 6319 3565 146 634 468 C
ATOM 5171 CG TRP A 659 15.659 119.405 218.083 1.00 36.24 C
ANISOU 5171 CG TRP A 659 4094 6265 3412 99 563 480 C
ATOM 5172 CD1 TRP A 659 16.332 119.751 216.925 1.00 36.08 C
ANISOU 5172 CD1 TRP A 659 4085 6238 3387 104 517 519 C
ATOM 5173 CD2 TRP A 659 15.969 118.038 218.331 1.00 35.73 C
ANISOU 5173 CD2 TRP A 659 4067 6236 3272 42 536 450 C
ATOM 5174 NE1 TRP A 659 17.002 118.654 216.427 1.00 35.52 N
ANISOU 5174 NE1 TRP A 659 4051 6201 3243 55 470 511 N
ATOM 5175 CE2 TRP A 659 16.802 117.593 217.277 1.00 35.29 C
ANISOU 5175 CE2 TRP A 659 4040 6196 3174 20 478 469 C
ATOM 5176 CE3 TRP A 659 15.599 117.131 219.325 1.00 35.69 C
ANISOU 5176 CE3 TRP A 659 4080 6250 3231 7 560 412 C
ATOM 5177 CZ2 TRP A 659 17.269 116.270 217.202 1.00 34.83 C
ANISOU 5177 CZ2 TRP A 659 4027 6165 3043 -29 443 447 C
ATOM 5178 CZ3 TRP A 659 16.060 115.834 219.245 1.00 35.22 C
ANISOU 5178 CZ3 TRP A 659 4069 6215 3098 -45 519 396 C
ATOM 5179 CH2 TRP A 659 16.897 115.414 218.200 1.00 34.80 C
ANISOU 5179 CH2 TRP A 659 4042 6171 3009 -58 461 412 C
ATOM 5180 N ALA A 660 11.808 119.627 218.135 1.00 38.29 N
ANISOU 5180 N ALA A 660 4101 6625 3822 166 613 570 N
ATOM 5181 CA ALA A 660 10.746 118.890 217.456 1.00 38.72 C
ANISOU 5181 CA ALA A 660 4068 6760 3882 140 563 620 C
ATOM 5182 C ALA A 660 9.846 119.779 216.587 1.00 39.63 C
ANISOU 5182 C ALA A 660 4082 6892 4083 205 535 696 C
ATOM 5183 O ALA A 660 9.531 119.406 215.454 1.00 39.80 O
ANISOU 5183 O ALA A 660 4066 6967 4089 183 450 754 O
ATOM 5184 CB ALA A 660 9.945 118.065 218.409 1.00 38.98 C
ANISOU 5184 CB ALA A 660 4070 6834 3908 99 611 586 C
ATOM 5185 N SER A 661 9.487 120.955 217.081 1.00 40.27 N
ANISOU 5185 N SER A 661 4129 6923 4250 285 600 697 N
ATOM 5186 CA SER A 661 8.652 121.874 216.323 1.00 41.27 C
ANISOU 5186 CA SER A 661 4160 7053 4467 362 575 773 C
ATOM 5187 C SER A 661 9.396 122.494 215.138 1.00 41.08 C
ANISOU 5187 C SER A 661 4187 6995 4427 382 504 828 C
ATOM 5188 O SER A 661 8.804 122.755 214.077 1.00 41.74 O
ANISOU 5188 O SER A 661 4206 7113 4542 410 432 909 O
ATOM 5189 CB SER A 661 8.106 122.969 217.243 1.00 42.10 C
ANISOU 5189 CB SER A 661 4227 7100 4671 450 676 753 C
ATOM 5190 OG SER A 661 7.402 123.970 216.528 1.00 43.14 O
ANISOU 5190 OG SER A 661 4276 7219 4898 540 652 829 O
ATOM 5191 N LYS A 662 10.695 122.716 215.321 1.00 40.27 N
ANISOU 5191 N LYS A 662 4198 6829 4274 362 523 785 N
ATOM 5192 CA LYS A 662 11.534 123.298 214.286 1.00 40.09 C
ANISOU 5192 CA LYS A 662 4234 6769 4230 370 472 828 C
ATOM 5193 C LYS A 662 11.859 122.302 213.183 1.00 39.62 C
ANISOU 5193 C LYS A 662 4196 6777 4083 300 383 858 C
ATOM 5194 O LYS A 662 11.939 122.687 212.002 1.00 39.94 O
ANISOU 5194 O LYS A 662 4241 6821 4114 312 321 927 O
ATOM 5195 CB LYS A 662 12.831 123.819 214.872 1.00 39.48 C
ANISOU 5195 CB LYS A 662 4261 6608 4131 362 524 769 C
ATOM 5196 CG LYS A 662 13.240 125.076 214.210 1.00 39.91 C
ANISOU 5196 CG LYS A 662 4346 6591 4226 411 519 817 C
ATOM 5197 CD LYS A 662 14.711 125.294 214.224 1.00 39.22 C
ANISOU 5197 CD LYS A 662 4361 6451 4091 369 532 779 C
ATOM 5198 CE LYS A 662 15.021 126.692 213.756 1.00 39.83 C
ANISOU 5198 CE LYS A 662 4473 6441 4221 417 545 823 C
ATOM 5199 NZ LYS A 662 16.442 127.044 214.077 1.00 39.31 N
ANISOU 5199 NZ LYS A 662 4499 6314 4125 374 577 770 N
ATOM 5200 N LEU A 663 12.050 121.034 213.562 1.00 38.96 N
ANISOU 5200 N LEU A 663 4134 6740 3930 229 378 807 N
ATOM 5201 CA LEU A 663 12.305 119.992 212.584 1.00 38.61 C
ANISOU 5201 CA LEU A 663 4117 6754 3799 161 301 825 C
ATOM 5202 C LEU A 663 11.085 119.923 211.678 1.00 39.51 C
ANISOU 5202 C LEU A 663 4139 6934 3937 168 229 903 C
ATOM 5203 O LEU A 663 11.190 119.994 210.460 1.00 39.74 O
ANISOU 5203 O LEU A 663 4185 6985 3931 158 158 960 O
ATOM 5204 CB LEU A 663 12.555 118.653 213.263 1.00 37.94 C
ANISOU 5204 CB LEU A 663 4068 6698 3648 91 313 758 C
ATOM 5205 CG LEU A 663 13.956 118.367 213.840 1.00 37.02 C
ANISOU 5205 CG LEU A 663 4053 6535 3479 66 349 690 C
ATOM 5206 CD1 LEU A 663 13.932 117.288 214.966 1.00 36.62 C
ANISOU 5206 CD1 LEU A 663 4026 6497 3391 21 380 624 C
ATOM 5207 CD2 LEU A 663 15.006 117.986 212.790 1.00 36.57 C
ANISOU 5207 CD2 LEU A 663 4065 6481 3349 33 302 698 C
ATOM 5208 N ARG A 664 9.907 119.838 212.275 1.00 40.13 N
ANISOU 5208 N ARG A 664 4120 7049 4080 186 249 907 N
ATOM 5209 CA ARG A 664 8.711 119.688 211.482 1.00 41.09 C
ANISOU 5209 CA ARG A 664 4139 7245 4230 186 174 979 C
ATOM 5210 C ARG A 664 8.487 120.899 210.613 1.00 41.89 C
ANISOU 5210 C ARG A 664 4209 7322 4386 263 132 1062 C
ATOM 5211 O ARG A 664 7.907 120.803 209.510 1.00 42.59 O
ANISOU 5211 O ARG A 664 4254 7467 4463 253 35 1137 O
ATOM 5212 CB ARG A 664 7.512 119.469 212.375 1.00 41.74 C
ANISOU 5212 CB ARG A 664 4107 7368 4385 195 217 965 C
ATOM 5213 CG ARG A 664 7.543 118.143 212.999 1.00 41.18 C
ANISOU 5213 CG ARG A 664 4063 7334 4251 105 237 903 C
ATOM 5214 CD ARG A 664 6.164 117.693 213.352 1.00 42.09 C
ANISOU 5214 CD ARG A 664 4049 7523 4422 85 241 916 C
ATOM 5215 NE ARG A 664 6.202 116.628 214.347 1.00 41.62 N
ANISOU 5215 NE ARG A 664 4025 7474 4317 11 298 846 N
ATOM 5216 CZ ARG A 664 6.315 116.839 215.644 1.00 41.44 C
ANISOU 5216 CZ ARG A 664 4020 7408 4318 34 405 788 C
ATOM 5217 NH1 ARG A 664 6.390 118.071 216.158 1.00 41.68 N
ANISOU 5217 NH1 ARG A 664 4037 7379 4422 129 474 783 N
ATOM 5218 NH2 ARG A 664 6.340 115.791 216.420 1.00 41.10 N
ANISOU 5218 NH2 ARG A 664 4018 7378 4221 -42 442 735 N
ATOM 5219 N GLU A 665 8.961 122.035 211.111 1.00 41.87 N
ANISOU 5219 N GLU A 665 4238 7231 4439 336 201 1051 N
ATOM 5220 CA GLU A 665 8.761 123.283 210.424 1.00 42.71 C
ANISOU 5220 CA GLU A 665 4326 7295 4608 418 174 1130 C
ATOM 5221 C GLU A 665 9.598 123.380 209.152 1.00 42.49 C
ANISOU 5221 C GLU A 665 4389 7258 4498 386 103 1178 C
ATOM 5222 O GLU A 665 9.109 123.876 208.140 1.00 43.38 O
ANISOU 5222 O GLU A 665 4472 7387 4625 419 27 1269 O
ATOM 5223 CB GLU A 665 9.071 124.438 211.346 1.00 42.80 C
ANISOU 5223 CB GLU A 665 4361 7204 4697 495 274 1097 C
ATOM 5224 CG GLU A 665 8.367 125.683 210.934 1.00 44.05 C
ANISOU 5224 CG GLU A 665 4460 7321 4956 600 261 1179 C
ATOM 5225 CD GLU A 665 9.047 126.925 211.454 1.00 50.41 C
ANISOU 5225 CD GLU A 665 5340 8002 5811 662 343 1156 C
ATOM 5226 OE1 GLU A 665 9.706 126.852 212.535 1.00 52.88 O
ANISOU 5226 OE1 GLU A 665 5713 8269 6109 638 430 1063 O
ATOM 5227 OE2 GLU A 665 8.923 127.982 210.781 1.00 53.04 O
ANISOU 5227 OE2 GLU A 665 5679 8279 6195 733 316 1232 O
ATOM 5228 N LEU A 666 10.844 122.896 209.210 1.00 41.40 N
ANISOU 5228 N LEU A 666 4360 7098 4274 323 128 1119 N
ATOM 5229 CA LEU A 666 11.779 123.075 208.105 1.00 41.22 C
ANISOU 5229 CA LEU A 666 4430 7056 4175 295 87 1153 C
ATOM 5230 C LEU A 666 12.000 121.814 207.290 1.00 40.85 C
ANISOU 5230 C LEU A 666 4421 7084 4015 206 21 1148 C
ATOM 5231 O LEU A 666 12.209 121.888 206.079 1.00 41.20 O
ANISOU 5231 O LEU A 666 4510 7145 3998 185 -42 1206 O
ATOM 5232 CB LEU A 666 13.116 123.650 208.581 1.00 40.51 C
ANISOU 5232 CB LEU A 666 4434 6880 4080 296 165 1101 C
ATOM 5233 CG LEU A 666 13.140 125.064 209.179 1.00 40.97 C
ANISOU 5233 CG LEU A 666 4491 6841 4236 377 229 1109 C
ATOM 5234 CD1 LEU A 666 14.451 125.371 209.928 1.00 40.20 C
ANISOU 5234 CD1 LEU A 666 4477 6670 4127 355 307 1032 C
ATOM 5235 CD2 LEU A 666 12.881 126.135 208.167 1.00 41.96 C
ANISOU 5235 CD2 LEU A 666 4621 6930 4392 430 185 1210 C
ATOM 5236 N LYS A 667 11.926 120.659 207.932 1.00 40.25 N
ANISOU 5236 N LYS A 667 4336 7050 3907 151 37 1080 N
ATOM 5237 CA LYS A 667 12.215 119.411 207.253 1.00 39.90 C
ANISOU 5237 CA LYS A 667 4343 7062 3755 66 -15 1062 C
ATOM 5238 C LYS A 667 11.419 119.250 205.916 1.00 40.84 C
ANISOU 5238 C LYS A 667 4436 7248 3833 42 -124 1145 C
ATOM 5239 O LYS A 667 10.249 119.605 205.842 1.00 41.74 O
ANISOU 5239 O LYS A 667 4451 7398 4013 77 -169 1202 O
ATOM 5240 CB LYS A 667 11.995 118.239 208.206 1.00 39.37 C
ANISOU 5240 CB LYS A 667 4258 7025 3674 17 13 987 C
ATOM 5241 CG LYS A 667 10.585 117.779 208.371 1.00 40.07 C
ANISOU 5241 CG LYS A 667 4242 7181 3801 3 -26 1011 C
ATOM 5242 CD LYS A 667 10.493 116.704 209.435 1.00 39.53 C
ANISOU 5242 CD LYS A 667 4174 7127 3720 -47 19 935 C
ATOM 5243 CE LYS A 667 9.193 115.904 209.302 1.00 40.27 C
ANISOU 5243 CE LYS A 667 4179 7302 3819 -99 -36 957 C
ATOM 5244 NZ LYS A 667 8.894 115.363 207.899 1.00 40.82 N
ANISOU 5244 NZ LYS A 667 4262 7432 3815 -159 -147 1007 N
ATOM 5245 N THR A 668 12.058 118.736 204.867 1.00 40.73 N
ANISOU 5245 N THR A 668 4513 7253 3711 -15 -166 1151 N
ATOM 5246 CA THR A 668 11.436 118.630 203.551 1.00 41.68 C
ANISOU 5246 CA THR A 668 4633 7432 3774 -45 -273 1228 C
ATOM 5247 C THR A 668 11.006 117.200 203.306 1.00 41.70 C
ANISOU 5247 C THR A 668 4640 7505 3700 -135 -327 1194 C
ATOM 5248 O THR A 668 10.235 116.944 202.398 1.00 42.60 O
ANISOU 5248 O THR A 668 4733 7681 3772 -172 -426 1250 O
ATOM 5249 CB THR A 668 12.388 119.030 202.414 1.00 41.78 C
ANISOU 5249 CB THR A 668 4757 7418 3701 -58 -285 1262 C
ATOM 5250 OG1 THR A 668 13.575 118.249 202.520 1.00 40.84 O
ANISOU 5250 OG1 THR A 668 4732 7279 3506 -108 -225 1180 O
ATOM 5251 CG2 THR A 668 12.758 120.474 202.509 1.00 41.97 C
ANISOU 5251 CG2 THR A 668 4783 7368 3794 21 -241 1307 C
ATOM 5252 N ASP A 669 11.508 116.261 204.098 1.00 40.80 N
ANISOU 5252 N ASP A 669 4560 7378 3563 -174 -267 1105 N
ATOM 5253 CA ASP A 669 11.022 114.878 204.051 1.00 40.86 C
ANISOU 5253 CA ASP A 669 4572 7441 3512 -261 -309 1067 C
ATOM 5254 C ASP A 669 9.642 114.728 204.727 1.00 41.43 C
ANISOU 5254 C ASP A 669 4511 7563 3667 -262 -333 1083 C
ATOM 5255 O ASP A 669 9.071 115.673 205.321 1.00 41.75 O
ANISOU 5255 O ASP A 669 4452 7593 3817 -188 -308 1117 O
ATOM 5256 CB ASP A 669 11.993 113.998 204.804 1.00 39.79 C
ANISOU 5256 CB ASP A 669 4515 7265 3340 -289 -232 972 C
ATOM 5257 CG ASP A 669 12.023 114.346 206.283 1.00 40.99 C
ANISOU 5257 CG ASP A 669 4611 7377 3587 -238 -148 932 C
ATOM 5258 OD1 ASP A 669 12.478 115.464 206.602 1.00 43.69 O
ANISOU 5258 OD1 ASP A 669 4944 7670 3988 -166 -99 945 O
ATOM 5259 OD2 ASP A 669 11.543 113.545 207.126 1.00 45.48 O
ANISOU 5259 OD2 ASP A 669 5150 7961 4170 -272 -130 890 O
ATOM 5260 N SER A 670 9.124 113.511 204.689 1.00 41.62 N
ANISOU 5260 N SER A 670 4534 7636 3643 -349 -373 1054 N
ATOM 5261 CA SER A 670 7.879 113.255 205.370 1.00 42.18 C
ANISOU 5261 CA SER A 670 4480 7758 3791 -365 -385 1062 C
ATOM 5262 C SER A 670 7.985 112.053 206.262 1.00 41.60 C
ANISOU 5262 C SER A 670 4439 7675 3691 -432 -333 981 C
ATOM 5263 O SER A 670 7.076 111.252 206.304 1.00 42.45 O
ANISOU 5263 O SER A 670 4495 7837 3795 -505 -375 980 O
ATOM 5264 CB SER A 670 6.747 113.054 204.378 1.00 43.48 C
ANISOU 5264 CB SER A 670 4573 8008 3938 -417 -509 1130 C
ATOM 5265 OG SER A 670 7.090 111.979 203.530 1.00 45.12 O
ANISOU 5265 OG SER A 670 4892 8233 4017 -516 -565 1102 O
ATOM 5266 N ASN A 671 9.077 111.932 207.004 1.00 40.52 N
ANISOU 5266 N ASN A 671 4387 7468 3540 -408 -245 916 N
ATOM 5267 CA ASN A 671 9.160 110.870 208.012 1.00 40.02 C
ANISOU 5267 CA ASN A 671 4356 7388 3462 -458 -192 845 C
ATOM 5268 C ASN A 671 8.626 111.383 209.343 1.00 40.00 C
ANISOU 5268 C ASN A 671 4259 7376 3562 -410 -116 836 C
ATOM 5269 O ASN A 671 8.385 112.574 209.496 1.00 40.24 O
ANISOU 5269 O ASN A 671 4214 7401 3673 -329 -96 874 O
ATOM 5270 CB ASN A 671 10.585 110.332 208.086 1.00 39.04 C
ANISOU 5270 CB ASN A 671 4373 7199 3262 -462 -148 782 C
ATOM 5271 CG ASN A 671 11.102 109.882 206.696 1.00 39.22 C
ANISOU 5271 CG ASN A 671 4491 7230 3180 -505 -211 790 C
ATOM 5272 OD1 ASN A 671 10.460 109.079 206.003 1.00 41.55 O
ANISOU 5272 OD1 ASN A 671 4797 7571 3419 -586 -281 799 O
ATOM 5273 ND2 ASN A 671 12.244 110.423 206.281 1.00 38.73 N
ANISOU 5273 ND2 ASN A 671 4498 7126 3092 -457 -183 785 N
ATOM 5274 N GLU A 672 8.390 110.508 210.303 1.00 39.83 N
ANISOU 5274 N GLU A 672 4244 7353 3537 -460 -72 787 N
ATOM 5275 CA GLU A 672 7.804 111.015 211.516 1.00 39.98 C
ANISOU 5275 CA GLU A 672 4175 7369 3647 -419 4 780 C
ATOM 5276 C GLU A 672 8.856 111.404 212.496 1.00 39.06 C
ANISOU 5276 C GLU A 672 4131 7175 3533 -361 92 729 C
ATOM 5277 O GLU A 672 9.862 110.708 212.711 1.00 38.30 O
ANISOU 5277 O GLU A 672 4150 7035 3367 -386 107 679 O
ATOM 5278 CB GLU A 672 6.718 110.109 212.137 1.00 40.61 C
ANISOU 5278 CB GLU A 672 4191 7496 3741 -499 16 768 C
ATOM 5279 CG GLU A 672 7.151 108.707 212.621 1.00 40.49 C
ANISOU 5279 CG GLU A 672 4290 7453 3643 -586 34 707 C
ATOM 5280 CD GLU A 672 5.977 107.672 212.607 1.00 46.56 C
ANISOU 5280 CD GLU A 672 5002 8283 4405 -699 2 715 C
ATOM 5281 OE1 GLU A 672 4.917 107.923 211.952 1.00 49.41 O
ANISOU 5281 OE1 GLU A 672 5241 8719 4811 -719 -60 768 O
ATOM 5282 OE2 GLU A 672 6.121 106.589 213.238 1.00 46.87 O
ANISOU 5282 OE2 GLU A 672 5120 8294 4392 -770 34 669 O
ATOM 5283 N VAL A 673 8.598 112.583 213.038 1.00 39.25 N
ANISOU 5283 N VAL A 673 4083 7185 3646 -280 143 745 N
ATOM 5284 CA VAL A 673 9.215 113.083 214.234 1.00 38.70 C
ANISOU 5284 CA VAL A 673 4051 7053 3601 -230 235 697 C
ATOM 5285 C VAL A 673 8.209 113.053 215.402 1.00 39.26 C
ANISOU 5285 C VAL A 673 4043 7143 3731 -234 308 681 C
ATOM 5286 O VAL A 673 7.431 113.984 215.568 1.00 39.96 O
ANISOU 5286 O VAL A 673 4027 7246 3909 -174 337 711 O
ATOM 5287 CB VAL A 673 9.642 114.490 213.949 1.00 38.67 C
ANISOU 5287 CB VAL A 673 4033 7009 3649 -138 247 724 C
ATOM 5288 CG1 VAL A 673 10.146 115.170 215.188 1.00 38.31 C
ANISOU 5288 CG1 VAL A 673 4017 6900 3639 -86 340 676 C
ATOM 5289 CG2 VAL A 673 10.699 114.441 212.928 1.00 38.14 C
ANISOU 5289 CG2 VAL A 673 4053 6922 3517 -144 193 733 C
ATOM 5290 N LEU A 674 8.196 111.983 216.190 1.00 39.07 N
ANISOU 5290 N LEU A 674 4068 7119 3658 -303 340 636 N
ATOM 5291 CA LEU A 674 7.313 111.921 217.393 1.00 39.64 C
ANISOU 5291 CA LEU A 674 4080 7206 3775 -315 425 615 C
ATOM 5292 C LEU A 674 8.004 112.450 218.646 1.00 39.17 C
ANISOU 5292 C LEU A 674 4089 7080 3716 -267 517 562 C
ATOM 5293 O LEU A 674 9.196 112.279 218.812 1.00 38.33 O
ANISOU 5293 O LEU A 674 4097 6919 3548 -263 510 528 O
ATOM 5294 CB LEU A 674 6.770 110.494 217.631 1.00 39.92 C
ANISOU 5294 CB LEU A 674 4131 7278 3758 -426 416 601 C
ATOM 5295 CG LEU A 674 6.342 109.742 216.343 1.00 40.28 C
ANISOU 5295 CG LEU A 674 4150 7380 3773 -496 310 641 C
ATOM 5296 CD1 LEU A 674 5.833 108.332 216.571 1.00 40.63 C
ANISOU 5296 CD1 LEU A 674 4222 7450 3765 -615 302 624 C
ATOM 5297 CD2 LEU A 674 5.315 110.539 215.572 1.00 41.21 C
ANISOU 5297 CD2 LEU A 674 4116 7565 3978 -461 268 705 C
ATOM 5298 N LEU A 675 7.279 113.117 219.525 1.00 39.81 N
ANISOU 5298 N LEU A 675 4099 7163 3865 -228 604 554 N
ATOM 5299 CA LEU A 675 7.889 113.589 220.772 1.00 39.50 C
ANISOU 5299 CA LEU A 675 4137 7059 3814 -193 692 497 C
ATOM 5300 C LEU A 675 7.101 113.149 221.982 1.00 40.13 C
ANISOU 5300 C LEU A 675 4199 7156 3893 -234 785 467 C
ATOM 5301 O LEU A 675 6.055 113.701 222.226 1.00 41.06 O
ANISOU 5301 O LEU A 675 4204 7306 4092 -203 845 481 O
ATOM 5302 CB LEU A 675 7.976 115.105 220.762 1.00 39.72 C
ANISOU 5302 CB LEU A 675 4123 7047 3920 -90 728 505 C
ATOM 5303 CG LEU A 675 7.918 115.865 222.085 1.00 40.06 C
ANISOU 5303 CG LEU A 675 4186 7042 3992 -45 843 455 C
ATOM 5304 CD1 LEU A 675 9.211 115.724 222.916 1.00 39.23 C
ANISOU 5304 CD1 LEU A 675 4233 6871 3802 -61 860 394 C
ATOM 5305 CD2 LEU A 675 7.671 117.297 221.730 1.00 40.56 C
ANISOU 5305 CD2 LEU A 675 4180 7079 4153 56 863 482 C
ATOM 5306 N LYS A 676 7.615 112.177 222.740 1.00 39.72 N
ANISOU 5306 N LYS A 676 4260 7080 3751 -301 801 426 N
ATOM 5307 CA LYS A 676 6.981 111.702 223.992 1.00 40.33 C
ANISOU 5307 CA LYS A 676 4350 7165 3807 -350 896 395 C
ATOM 5308 C LYS A 676 7.362 112.483 225.267 1.00 40.40 C
ANISOU 5308 C LYS A 676 4424 7117 3808 -303 995 342 C
ATOM 5309 O LYS A 676 8.474 112.381 225.768 1.00 39.71 O
ANISOU 5309 O LYS A 676 4466 6973 3648 -303 982 306 O
ATOM 5310 CB LYS A 676 7.200 110.197 224.201 1.00 40.08 C
ANISOU 5310 CB LYS A 676 4413 7135 3679 -453 865 385 C
ATOM 5311 CG LYS A 676 6.219 109.612 225.205 1.00 43.20 C
ANISOU 5311 CG LYS A 676 4791 7559 4064 -523 957 372 C
ATOM 5312 CD LYS A 676 6.585 108.196 225.691 1.00 49.24 C
ANISOU 5312 CD LYS A 676 5688 8301 4722 -621 941 357 C
ATOM 5313 CE LYS A 676 5.847 107.860 227.011 1.00 52.14 C
ANISOU 5313 CE LYS A 676 6071 8675 5063 -679 1058 334 C
ATOM 5314 NZ LYS A 676 6.155 108.877 228.107 1.00 54.67 N
ANISOU 5314 NZ LYS A 676 6433 8956 5384 -610 1152 291 N
ATOM 5315 N MET A 677 6.405 113.247 225.780 1.00 41.35 N
ANISOU 5315 N MET A 677 4451 7255 4004 -263 1092 337 N
ATOM 5316 CA MET A 677 6.556 114.022 226.995 1.00 42.84 C
ANISOU 5316 CA MET A 677 4695 7393 4188 -222 1200 284 C
ATOM 5317 C MET A 677 5.819 113.367 228.187 1.00 44.67 C
ANISOU 5317 C MET A 677 4948 7647 4379 -290 1307 254 C
ATOM 5318 O MET A 677 4.589 113.472 228.282 1.00 45.82 O
ANISOU 5318 O MET A 677 4967 7846 4597 -291 1381 270 O
ATOM 5319 CB MET A 677 5.972 115.403 226.715 1.00 43.82 C
ANISOU 5319 CB MET A 677 4704 7513 4431 -119 1248 297 C
ATOM 5320 CG MET A 677 6.098 116.369 227.819 1.00 45.20 C
ANISOU 5320 CG MET A 677 4932 7628 4614 -65 1360 239 C
ATOM 5321 SD MET A 677 7.830 116.822 227.908 1.00 49.03 S
ANISOU 5321 SD MET A 677 5581 8024 5026 -45 1294 202 S
ATOM 5322 CE MET A 677 7.907 118.276 226.864 1.00 46.59 C
ANISOU 5322 CE MET A 677 5189 7681 4831 67 1262 238 C
ATOM 5323 N ASP A 678 6.548 112.691 229.087 1.00 45.88 N
ANISOU 5323 N ASP A 678 5254 7761 4418 -347 1316 216 N
ATOM 5324 CA ASP A 678 5.957 112.242 230.360 1.00 48.18 C
ANISOU 5324 CA ASP A 678 5591 8059 4657 -406 1432 183 C
ATOM 5325 C ASP A 678 5.948 113.422 231.298 1.00 48.89 C
ANISOU 5325 C ASP A 678 5706 8105 4765 -340 1544 131 C
ATOM 5326 O ASP A 678 6.994 113.836 231.783 1.00 48.55 O
ANISOU 5326 O ASP A 678 5787 7998 4662 -315 1526 92 O
ATOM 5327 CB ASP A 678 6.671 111.034 231.027 1.00 48.68 C
ANISOU 5327 CB ASP A 678 5819 8094 4584 -495 1400 168 C
ATOM 5328 CG ASP A 678 5.938 110.536 232.394 1.00 53.50 C
ANISOU 5328 CG ASP A 678 6484 8713 5130 -569 1532 140 C
ATOM 5329 OD1 ASP A 678 4.733 110.845 232.655 1.00 55.25 O
ANISOU 5329 OD1 ASP A 678 6591 8982 5419 -571 1645 140 O
ATOM 5330 OD2 ASP A 678 6.562 109.804 233.213 1.00 55.74 O
ANISOU 5330 OD2 ASP A 678 6926 8959 5295 -628 1525 121 O
ATOM 5331 N LEU A 679 4.758 113.965 231.533 1.00 50.49 N
ANISOU 5331 N LEU A 679 5786 8345 5054 -310 1657 130 N
ATOM 5332 CA LEU A 679 4.577 115.113 232.406 1.00 51.76 C
ANISOU 5332 CA LEU A 679 5961 8462 5242 -241 1783 76 C
ATOM 5333 C LEU A 679 4.701 114.709 233.876 1.00 52.74 C
ANISOU 5333 C LEU A 679 6232 8560 5247 -306 1883 19 C
ATOM 5334 O LEU A 679 4.430 115.513 234.755 1.00 54.00 O
ANISOU 5334 O LEU A 679 6418 8688 5412 -267 2008 -33 O
ATOM 5335 CB LEU A 679 3.203 115.766 232.169 1.00 52.98 C
ANISOU 5335 CB LEU A 679 5926 8667 5536 -181 1879 95 C
ATOM 5336 CG LEU A 679 2.501 115.749 230.799 1.00 53.22 C
ANISOU 5336 CG LEU A 679 5769 8765 5685 -152 1798 169 C
ATOM 5337 CD1 LEU A 679 0.993 115.568 230.954 1.00 52.90 C
ANISOU 5337 CD1 LEU A 679 5561 8807 5733 -167 1901 189 C
ATOM 5338 CD2 LEU A 679 2.808 116.985 229.967 1.00 52.99 C
ANISOU 5338 CD2 LEU A 679 5686 8697 5751 -33 1746 189 C
ATOM 5339 N GLU A 680 5.111 113.474 234.146 1.00 53.09 N
ANISOU 5339 N GLU A 680 6381 8611 5180 -404 1829 29 N
ATOM 5340 CA GLU A 680 5.164 112.974 235.520 1.00 54.93 C
ANISOU 5340 CA GLU A 680 6758 8823 5290 -476 1918 -13 C
ATOM 5341 C GLU A 680 6.585 112.789 236.051 1.00 54.01 C
ANISOU 5341 C GLU A 680 6838 8638 5046 -494 1835 -42 C
ATOM 5342 O GLU A 680 6.805 112.783 237.265 1.00 54.79 O
ANISOU 5342 O GLU A 680 7074 8702 5041 -528 1906 -89 O
ATOM 5343 CB GLU A 680 4.423 111.644 235.630 1.00 56.17 C
ANISOU 5343 CB GLU A 680 6898 9037 5408 -586 1938 22 C
ATOM 5344 CG GLU A 680 2.956 111.638 235.134 1.00 59.94 C
ANISOU 5344 CG GLU A 680 7170 9596 6009 -590 2013 56 C
ATOM 5345 CD GLU A 680 1.971 112.242 236.123 1.00 64.44 C
ANISOU 5345 CD GLU A 680 7693 10183 6608 -576 2205 14 C
ATOM 5346 OE1 GLU A 680 2.033 113.476 236.375 1.00 65.69 O
ANISOU 5346 OE1 GLU A 680 7838 10305 6818 -478 2270 -28 O
ATOM 5347 OE2 GLU A 680 1.120 111.476 236.636 1.00 66.13 O
ANISOU 5347 OE2 GLU A 680 7884 10445 6798 -666 2296 22 O
ATOM 5348 N SER A 681 7.532 112.662 235.122 1.00 52.75 N
ANISOU 5348 N SER A 681 6685 8462 4896 -470 1686 -14 N
ATOM 5349 CA SER A 681 8.936 112.332 235.395 1.00 51.50 C
ANISOU 5349 CA SER A 681 6684 8251 4633 -486 1581 -28 C
ATOM 5350 C SER A 681 9.953 113.424 235.077 1.00 50.47 C
ANISOU 5350 C SER A 681 6571 8071 4534 -407 1519 -54 C
ATOM 5351 O SER A 681 9.610 114.465 234.520 1.00 49.77 O
ANISOU 5351 O SER A 681 6376 7981 4552 -335 1549 -55 O
ATOM 5352 CB SER A 681 9.322 111.094 234.588 1.00 50.81 C
ANISOU 5352 CB SER A 681 6602 8182 4520 -533 1456 25 C
ATOM 5353 OG SER A 681 9.238 111.337 233.197 1.00 50.31 O
ANISOU 5353 OG SER A 681 6406 8147 4563 -486 1384 63 O
ATOM 5354 N GLY A 682 11.212 113.149 235.419 1.00 50.21 N
ANISOU 5354 N GLY A 682 6670 7996 4410 -424 1428 -69 N
ATOM 5355 CA GLY A 682 12.314 114.078 235.175 1.00 50.75 C
ANISOU 5355 CA GLY A 682 6766 8019 4498 -367 1360 -94 C
ATOM 5356 C GLY A 682 13.285 113.680 234.057 1.00 50.48 C
ANISOU 5356 C GLY A 682 6707 7987 4486 -352 1215 -54 C
ATOM 5357 O GLY A 682 12.893 113.433 232.897 1.00 49.69 O
ANISOU 5357 O GLY A 682 6495 7924 4462 -335 1179 -6 O
ATOM 5358 N HIS A 683 14.565 113.623 234.421 1.00 50.68 N
ANISOU 5358 N HIS A 683 6839 7976 4443 -358 1132 -75 N
ATOM 5359 CA HIS A 683 15.625 113.286 233.499 1.00 50.15 C
ANISOU 5359 CA HIS A 683 6758 7906 4391 -341 1005 -46 C
ATOM 5360 C HIS A 683 15.765 111.798 233.316 1.00 51.15 C
ANISOU 5360 C HIS A 683 6922 8053 4460 -387 939 -8 C
ATOM 5361 O HIS A 683 15.815 111.284 232.188 1.00 51.33 O
ANISOU 5361 O HIS A 683 6877 8099 4528 -377 879 33 O
ATOM 5362 CB HIS A 683 16.962 113.811 233.998 1.00 49.15 C
ANISOU 5362 CB HIS A 683 6719 7736 4221 -331 941 -84 C
ATOM 5363 CG HIS A 683 18.068 113.610 233.015 1.00 47.97 C
ANISOU 5363 CG HIS A 683 6537 7587 4102 -306 824 -58 C
ATOM 5364 ND1 HIS A 683 18.244 114.433 231.921 1.00 46.15 N
ANISOU 5364 ND1 HIS A 683 6209 7358 3969 -257 808 -45 N
ATOM 5365 CD2 HIS A 683 19.006 112.639 232.916 1.00 46.24 C
ANISOU 5365 CD2 HIS A 683 6367 7369 3832 -321 724 -40 C
ATOM 5366 CE1 HIS A 683 19.268 113.997 231.214 1.00 45.85 C
ANISOU 5366 CE1 HIS A 683 6162 7324 3934 -248 710 -24 C
ATOM 5367 NE2 HIS A 683 19.751 112.912 231.798 1.00 46.11 N
ANISOU 5367 NE2 HIS A 683 6280 7358 3883 -282 657 -22 N
ATOM 5368 N PHE A 684 15.878 111.110 234.438 1.00 52.85 N
ANISOU 5368 N PHE A 684 7258 8253 4569 -438 947 -21 N
ATOM 5369 CA PHE A 684 16.303 109.736 234.430 1.00 54.04 C
ANISOU 5369 CA PHE A 684 7480 8401 4652 -476 870 11 C
ATOM 5370 C PHE A 684 15.147 108.871 234.265 1.00 55.67 C
ANISOU 5370 C PHE A 684 7656 8638 4858 -525 924 43 C
ATOM 5371 O PHE A 684 15.264 107.736 233.823 1.00 56.40 O
ANISOU 5371 O PHE A 684 7769 8731 4927 -552 865 79 O
ATOM 5372 CB PHE A 684 16.946 109.376 235.737 1.00 53.77 C
ANISOU 5372 CB PHE A 684 7599 8332 4497 -510 848 -11 C
ATOM 5373 CG PHE A 684 18.356 109.721 235.779 1.00 54.07 C
ANISOU 5373 CG PHE A 684 7678 8344 4522 -474 745 -28 C
ATOM 5374 CD1 PHE A 684 19.244 109.089 234.915 1.00 53.65 C
ANISOU 5374 CD1 PHE A 684 7599 8290 4494 -446 636 3 C
ATOM 5375 CD2 PHE A 684 18.809 110.710 236.639 1.00 53.95 C
ANISOU 5375 CD2 PHE A 684 7718 8305 4474 -469 760 -77 C
ATOM 5376 CE1 PHE A 684 20.578 109.402 234.929 1.00 54.70 C
ANISOU 5376 CE1 PHE A 684 7753 8406 4625 -413 542 -11 C
ATOM 5377 CE2 PHE A 684 20.132 111.029 236.674 1.00 55.13 C
ANISOU 5377 CE2 PHE A 684 7895 8436 4615 -445 659 -92 C
ATOM 5378 CZ PHE A 684 21.034 110.369 235.814 1.00 56.04 C
ANISOU 5378 CZ PHE A 684 7973 8558 4763 -416 549 -57 C
ATOM 5379 N SER A 685 14.010 109.404 234.652 1.00 57.96 N
ANISOU 5379 N SER A 685 7898 8951 5175 -538 1043 28 N
ATOM 5380 CA SER A 685 12.859 108.568 234.815 1.00 59.43 C
ANISOU 5380 CA SER A 685 8068 9166 5345 -603 1112 53 C
ATOM 5381 C SER A 685 12.552 107.905 233.468 1.00 59.66 C
ANISOU 5381 C SER A 685 7998 9228 5441 -608 1052 101 C
ATOM 5382 O SER A 685 13.138 106.875 233.138 1.00 59.52 O
ANISOU 5382 O SER A 685 8041 9193 5380 -631 965 126 O
ATOM 5383 CB SER A 685 11.701 109.373 235.409 1.00 59.90 C
ANISOU 5383 CB SER A 685 8071 9250 5438 -606 1257 26 C
ATOM 5384 OG SER A 685 12.225 110.461 236.178 1.00 59.36 O
ANISOU 5384 OG SER A 685 8061 9145 5347 -566 1290 -27 O
ATOM 5385 N ALA A 686 11.710 108.525 232.657 1.00 60.50 N
ANISOU 5385 N ALA A 686 7957 9379 5653 -581 1092 113 N
ATOM 5386 CA ALA A 686 10.710 107.733 231.960 1.00 61.53 C
ANISOU 5386 CA ALA A 686 8004 9555 5820 -633 1099 153 C
ATOM 5387 C ALA A 686 9.861 107.249 233.178 1.00 62.68 C
ANISOU 5387 C ALA A 686 8206 9707 5901 -709 1209 143 C
ATOM 5388 O ALA A 686 8.732 107.729 233.368 1.00 64.26 O
ANISOU 5388 O ALA A 686 8308 9949 6157 -716 1315 138 O
ATOM 5389 CB ALA A 686 11.340 106.561 231.130 1.00 60.42 C
ANISOU 5389 CB ALA A 686 7908 9401 5647 -660 982 185 C
ATOM 5390 N SER A 687 10.418 106.365 234.019 1.00 62.40 N
ANISOU 5390 N SER A 687 8329 9630 5750 -760 1188 140 N
ATOM 5391 CA SER A 687 9.984 106.225 235.431 1.00 63.03 C
ANISOU 5391 CA SER A 687 8506 9697 5744 -816 1293 118 C
ATOM 5392 C SER A 687 10.846 105.330 236.361 1.00 62.61 C
ANISOU 5392 C SER A 687 8650 9587 5552 -860 1243 119 C
ATOM 5393 O SER A 687 11.925 104.818 235.996 1.00 61.65 O
ANISOU 5393 O SER A 687 8596 9429 5401 -837 1121 134 O
ATOM 5394 CB SER A 687 8.489 105.874 235.539 1.00 64.18 C
ANISOU 5394 CB SER A 687 8566 9897 5923 -888 1407 134 C
ATOM 5395 OG SER A 687 8.137 104.820 234.655 1.00 64.98 O
ANISOU 5395 OG SER A 687 8625 10020 6046 -944 1347 179 O
ATOM 5396 N ASP A 688 10.329 105.162 237.572 1.00 63.37 N
ANISOU 5396 N ASP A 688 8835 9678 5565 -921 1345 105 N
ATOM 5397 CA ASP A 688 10.944 104.408 238.660 1.00 63.43 C
ANISOU 5397 CA ASP A 688 9039 9634 5429 -969 1320 109 C
ATOM 5398 C ASP A 688 10.119 103.158 238.959 1.00 63.82 C
ANISOU 5398 C ASP A 688 9141 9686 5423 -1077 1371 148 C
ATOM 5399 O ASP A 688 10.003 102.768 240.107 1.00 64.77 O
ANISOU 5399 O ASP A 688 9399 9782 5429 -1139 1428 147 O
ATOM 5400 CB ASP A 688 10.976 105.331 239.857 1.00 64.26 C
ANISOU 5400 CB ASP A 688 9215 9729 5473 -959 1408 58 C
ATOM 5401 CG ASP A 688 10.006 106.518 239.690 1.00 65.80 C
ANISOU 5401 CG ASP A 688 9258 9970 5772 -923 1535 22 C
ATOM 5402 OD1 ASP A 688 9.679 106.867 238.525 1.00 64.70 O
ANISOU 5402 OD1 ASP A 688 8955 9867 5761 -877 1513 36 O
ATOM 5403 OD2 ASP A 688 9.567 107.116 240.704 1.00 68.24 O
ANISOU 5403 OD2 ASP A 688 9613 10279 6036 -937 1657 -20 O
ATOM 5404 N ARG A 689 9.608 102.515 237.897 1.00 63.19 N
ANISOU 5404 N ARG A 689 8961 9631 5417 -1104 1341 184 N
ATOM 5405 CA ARG A 689 8.628 101.435 237.957 1.00 63.46 C
ANISOU 5405 CA ARG A 689 9005 9679 5429 -1215 1397 219 C
ATOM 5406 C ARG A 689 8.923 100.212 237.045 1.00 62.20 C
ANISOU 5406 C ARG A 689 8872 9488 5272 -1248 1284 263 C
ATOM 5407 O ARG A 689 10.061 99.826 236.817 1.00 60.99 O
ANISOU 5407 O ARG A 689 8810 9280 5082 -1201 1165 272 O
ATOM 5408 CB ARG A 689 7.258 102.014 237.569 1.00 64.16 C
ANISOU 5408 CB ARG A 689 8902 9848 5628 -1234 1513 212 C
ATOM 5409 CG ARG A 689 6.173 101.931 238.611 1.00 67.51 C
ANISOU 5409 CG ARG A 689 9341 10301 6011 -1321 1675 204 C
ATOM 5410 CD ARG A 689 4.801 101.630 237.994 1.00 72.39 C
ANISOU 5410 CD ARG A 689 9789 10990 6725 -1391 1746 228 C
ATOM 5411 NE ARG A 689 4.376 100.233 238.200 1.00 79.12 N
ANISOU 5411 NE ARG A 689 10729 11826 7509 -1523 1755 268 N
ATOM 5412 CZ ARG A 689 3.193 99.697 237.825 1.00 82.30 C
ANISOU 5412 CZ ARG A 689 11016 12283 7969 -1620 1815 293 C
ATOM 5413 NH1 ARG A 689 2.275 100.434 237.195 1.00 83.02 N
ANISOU 5413 NH1 ARG A 689 10887 12460 8195 -1593 1868 286 N
ATOM 5414 NH2 ARG A 689 2.913 98.408 238.082 1.00 82.25 N
ANISOU 5414 NH2 ARG A 689 11116 12247 7889 -1747 1821 329 N
ATOM 5415 N TYR A 690 7.824 99.577 236.620 1.00 61.98 N
ANISOU 5415 N TYR A 690 8769 9498 5284 -1337 1334 288 N
ATOM 5416 CA TYR A 690 7.712 98.654 235.497 1.00 59.79 C
ANISOU 5416 CA TYR A 690 8457 9214 5045 -1375 1252 321 C
ATOM 5417 C TYR A 690 7.356 99.517 234.313 1.00 59.03 C
ANISOU 5417 C TYR A 690 8159 9187 5083 -1314 1232 310 C
ATOM 5418 O TYR A 690 7.302 99.059 233.184 1.00 58.33 O
ANISOU 5418 O TYR A 690 8012 9107 5043 -1325 1156 329 O
ATOM 5419 CB TYR A 690 6.494 97.748 235.710 1.00 60.65 C
ANISOU 5419 CB TYR A 690 8561 9344 5140 -1515 1335 348 C
ATOM 5420 CG TYR A 690 6.714 96.526 236.565 1.00 59.17 C
ANISOU 5420 CG TYR A 690 8580 9079 4825 -1604 1337 376 C
ATOM 5421 CD1 TYR A 690 6.783 96.619 237.951 1.00 56.60 C
ANISOU 5421 CD1 TYR A 690 8383 8728 4396 -1627 1417 370 C
ATOM 5422 CD2 TYR A 690 6.835 95.266 235.982 1.00 57.21 C
ANISOU 5422 CD2 TYR A 690 8408 8776 4553 -1666 1259 409 C
ATOM 5423 CE1 TYR A 690 6.982 95.499 238.715 1.00 56.12 C
ANISOU 5423 CE1 TYR A 690 8518 8591 4213 -1708 1413 403 C
ATOM 5424 CE2 TYR A 690 7.038 94.141 236.750 1.00 55.79 C
ANISOU 5424 CE2 TYR A 690 8426 8515 4258 -1744 1258 440 C
ATOM 5425 CZ TYR A 690 7.112 94.266 238.108 1.00 55.89 C
ANISOU 5425 CZ TYR A 690 8560 8505 4171 -1763 1332 440 C
ATOM 5426 OH TYR A 690 7.323 93.141 238.860 1.00 58.14 O
ANISOU 5426 OH TYR A 690 9051 8704 4337 -1839 1325 478 O
ATOM 5427 N LYS A 691 7.047 100.775 234.581 1.00 59.05 N
ANISOU 5427 N LYS A 691 8058 9238 5142 -1253 1306 281 N
ATOM 5428 CA LYS A 691 6.668 101.690 233.525 1.00 58.81 C
ANISOU 5428 CA LYS A 691 7837 9270 5239 -1189 1292 277 C
ATOM 5429 C LYS A 691 7.886 102.223 232.767 1.00 57.52 C
ANISOU 5429 C LYS A 691 7679 9077 5100 -1079 1175 267 C
ATOM 5430 O LYS A 691 7.802 102.602 231.587 1.00 57.11 O
ANISOU 5430 O LYS A 691 7505 9061 5135 -1037 1120 277 O
ATOM 5431 CB LYS A 691 5.736 102.783 234.063 1.00 59.62 C
ANISOU 5431 CB LYS A 691 7819 9431 5404 -1167 1427 253 C
ATOM 5432 CG LYS A 691 4.296 102.266 234.371 1.00 62.25 C
ANISOU 5432 CG LYS A 691 8074 9821 5757 -1279 1540 271 C
ATOM 5433 CD LYS A 691 3.635 101.547 233.139 1.00 63.75 C
ANISOU 5433 CD LYS A 691 8148 10056 6016 -1342 1473 310 C
ATOM 5434 CE LYS A 691 2.772 100.333 233.526 1.00 64.44 C
ANISOU 5434 CE LYS A 691 8272 10155 6059 -1494 1530 336 C
ATOM 5435 NZ LYS A 691 1.350 100.726 233.671 1.00 66.33 N
ANISOU 5435 NZ LYS A 691 8332 10485 6387 -1539 1654 339 N
ATOM 5436 N TYR A 692 9.027 102.215 233.438 1.00 57.10 N
ANISOU 5436 N TYR A 692 7770 8960 4965 -1039 1135 250 N
ATOM 5437 CA TYR A 692 10.288 102.458 232.779 1.00 55.93 C
ANISOU 5437 CA TYR A 692 7646 8778 4827 -952 1020 244 C
ATOM 5438 C TYR A 692 10.358 101.520 231.605 1.00 55.58 C
ANISOU 5438 C TYR A 692 7586 8729 4802 -979 931 274 C
ATOM 5439 O TYR A 692 10.550 101.944 230.467 1.00 55.49 O
ANISOU 5439 O TYR A 692 7478 8742 4864 -927 874 277 O
ATOM 5440 CB TYR A 692 11.439 102.162 233.730 1.00 55.97 C
ANISOU 5440 CB TYR A 692 7825 8714 4727 -934 977 232 C
ATOM 5441 CG TYR A 692 12.811 102.345 233.133 1.00 56.53 C
ANISOU 5441 CG TYR A 692 7918 8751 4808 -847 860 226 C
ATOM 5442 CD1 TYR A 692 13.426 101.313 232.425 1.00 58.18 C
ANISOU 5442 CD1 TYR A 692 8180 8924 5001 -849 764 250 C
ATOM 5443 CD2 TYR A 692 13.505 103.550 233.276 1.00 56.90 C
ANISOU 5443 CD2 TYR A 692 7936 8801 4884 -766 850 194 C
ATOM 5444 CE1 TYR A 692 14.691 101.474 231.874 1.00 58.22 C
ANISOU 5444 CE1 TYR A 692 8197 8903 5022 -767 666 242 C
ATOM 5445 CE2 TYR A 692 14.770 103.718 232.732 1.00 56.85 C
ANISOU 5445 CE2 TYR A 692 7940 8768 4891 -694 747 189 C
ATOM 5446 CZ TYR A 692 15.356 102.676 232.035 1.00 57.90 C
ANISOU 5446 CZ TYR A 692 8116 8873 5011 -693 659 213 C
ATOM 5447 OH TYR A 692 16.609 102.823 231.489 1.00 58.35 O
ANISOU 5447 OH TYR A 692 8175 8908 5087 -620 568 207 O
ATOM 5448 N LEU A 693 10.182 100.238 231.885 1.00 56.16 N
ANISOU 5448 N LEU A 693 7766 8767 4806 -1064 924 295 N
ATOM 5449 CA LEU A 693 10.263 99.214 230.851 1.00 56.30 C
ANISOU 5449 CA LEU A 693 7797 8765 4828 -1099 844 318 C
ATOM 5450 C LEU A 693 9.224 99.390 229.732 1.00 56.46 C
ANISOU 5450 C LEU A 693 7654 8858 4939 -1134 851 331 C
ATOM 5451 O LEU A 693 9.505 99.107 228.577 1.00 55.68 O
ANISOU 5451 O LEU A 693 7528 8758 4869 -1119 770 338 O
ATOM 5452 CB LEU A 693 10.188 97.814 231.469 1.00 56.74 C
ANISOU 5452 CB LEU A 693 8009 8758 4790 -1192 845 340 C
ATOM 5453 CG LEU A 693 11.373 97.301 232.309 1.00 56.56 C
ANISOU 5453 CG LEU A 693 8170 8649 4671 -1157 796 341 C
ATOM 5454 CD1 LEU A 693 11.141 95.818 232.670 1.00 57.18 C
ANISOU 5454 CD1 LEU A 693 8396 8662 4669 -1256 792 372 C
ATOM 5455 CD2 LEU A 693 12.771 97.496 231.675 1.00 54.37 C
ANISOU 5455 CD2 LEU A 693 7911 8337 4409 -1045 686 329 C
ATOM 5456 N ARG A 694 8.040 99.870 230.098 1.00 57.44 N
ANISOU 5456 N ARG A 694 7671 9047 5108 -1178 948 333 N
ATOM 5457 CA ARG A 694 6.969 100.148 229.162 1.00 57.96 C
ANISOU 5457 CA ARG A 694 7563 9191 5267 -1207 957 348 C
ATOM 5458 C ARG A 694 7.396 101.244 228.201 1.00 56.97 C
ANISOU 5458 C ARG A 694 7329 9096 5220 -1098 901 342 C
ATOM 5459 O ARG A 694 7.197 101.126 226.992 1.00 56.55 O
ANISOU 5459 O ARG A 694 7200 9074 5212 -1103 833 360 O
ATOM 5460 CB ARG A 694 5.758 100.639 229.934 1.00 59.31 C
ANISOU 5460 CB ARG A 694 7634 9423 5476 -1249 1085 347 C
ATOM 5461 CG ARG A 694 4.443 100.116 229.432 1.00 62.42 C
ANISOU 5461 CG ARG A 694 7910 9884 5922 -1354 1109 374 C
ATOM 5462 CD ARG A 694 3.959 99.045 230.360 1.00 66.45 C
ANISOU 5462 CD ARG A 694 8524 10369 6356 -1479 1178 382 C
ATOM 5463 NE ARG A 694 2.992 98.164 229.717 1.00 70.72 N
ANISOU 5463 NE ARG A 694 8999 10949 6924 -1602 1162 409 N
ATOM 5464 CZ ARG A 694 2.388 97.152 230.332 1.00 72.43 C
ANISOU 5464 CZ ARG A 694 9284 11151 7087 -1734 1220 422 C
ATOM 5465 NH1 ARG A 694 2.637 96.889 231.617 1.00 73.89 N
ANISOU 5465 NH1 ARG A 694 9610 11282 7183 -1758 1300 415 N
ATOM 5466 NH2 ARG A 694 1.530 96.407 229.661 1.00 72.28 N
ANISOU 5466 NH2 ARG A 694 9195 11169 7098 -1850 1197 445 N
ATOM 5467 N GLU A 695 7.967 102.309 228.772 1.00 56.47 N
ANISOU 5467 N GLU A 695 7269 9020 5166 -1005 933 318 N
ATOM 5468 CA GLU A 695 8.519 103.461 228.041 1.00 55.39 C
ANISOU 5468 CA GLU A 695 7053 8898 5097 -897 889 311 C
ATOM 5469 C GLU A 695 9.595 103.053 227.067 1.00 52.99 C
ANISOU 5469 C GLU A 695 6806 8556 4771 -863 775 315 C
ATOM 5470 O GLU A 695 9.647 103.523 225.938 1.00 52.27 O
ANISOU 5470 O GLU A 695 6628 8495 4738 -822 722 327 O
ATOM 5471 CB GLU A 695 9.142 104.447 229.036 1.00 56.17 C
ANISOU 5471 CB GLU A 695 7196 8966 5181 -823 940 277 C
ATOM 5472 CG GLU A 695 8.259 105.646 229.434 1.00 59.99 C
ANISOU 5472 CG GLU A 695 7559 9495 5740 -787 1042 265 C
ATOM 5473 CD GLU A 695 8.677 106.931 228.727 1.00 63.15 C
ANISOU 5473 CD GLU A 695 7874 9901 6219 -682 1011 260 C
ATOM 5474 OE1 GLU A 695 9.108 106.854 227.541 1.00 63.11 O
ANISOU 5474 OE1 GLU A 695 7837 9901 6240 -657 917 282 O
ATOM 5475 OE2 GLU A 695 8.570 108.013 229.366 1.00 65.46 O
ANISOU 5475 OE2 GLU A 695 8140 10189 6544 -627 1086 234 O
ATOM 5476 N ASN A 696 10.458 102.164 227.535 1.00 51.55 N
ANISOU 5476 N ASN A 696 6775 8307 4503 -879 740 306 N
ATOM 5477 CA ASN A 696 11.618 101.738 226.786 1.00 49.60 C
ANISOU 5477 CA ASN A 696 6597 8016 4231 -837 643 304 C
ATOM 5478 C ASN A 696 11.227 100.888 225.609 1.00 48.43 C
ANISOU 5478 C ASN A 696 6430 7881 4091 -892 588 324 C
ATOM 5479 O ASN A 696 11.948 100.792 224.637 1.00 47.61 O
ANISOU 5479 O ASN A 696 6335 7763 3993 -851 518 323 O
ATOM 5480 CB ASN A 696 12.534 100.957 227.712 1.00 49.93 C
ANISOU 5480 CB ASN A 696 6805 7983 4185 -838 624 294 C
ATOM 5481 CG ASN A 696 13.747 100.435 227.009 1.00 51.03 C
ANISOU 5481 CG ASN A 696 7013 8073 4303 -789 532 291 C
ATOM 5482 OD1 ASN A 696 13.835 99.249 226.697 1.00 54.26 O
ANISOU 5482 OD1 ASN A 696 7504 8441 4670 -833 494 301 O
ATOM 5483 ND2 ASN A 696 14.681 101.317 226.721 1.00 52.87 N
ANISOU 5483 ND2 ASN A 696 7211 8307 4568 -699 500 275 N
ATOM 5484 N ALA A 697 10.058 100.278 225.728 1.00 48.45 N
ANISOU 5484 N ALA A 697 6404 7912 4092 -991 627 341 N
ATOM 5485 CA ALA A 697 9.552 99.299 224.788 1.00 47.85 C
ANISOU 5485 CA ALA A 697 6328 7844 4009 -1072 579 357 C
ATOM 5486 C ALA A 697 9.056 99.961 223.486 1.00 47.57 C
ANISOU 5486 C ALA A 697 6145 7880 4048 -1055 539 372 C
ATOM 5487 O ALA A 697 9.281 99.457 222.371 1.00 46.55 O
ANISOU 5487 O ALA A 697 6034 7744 3907 -1070 465 376 O
ATOM 5488 CB ALA A 697 8.454 98.502 225.448 1.00 48.14 C
ANISOU 5488 CB ALA A 697 6378 7890 4022 -1193 638 371 C
ATOM 5489 N ILE A 698 8.396 101.104 223.646 1.00 47.55 N
ANISOU 5489 N ILE A 698 6005 7941 4119 -1019 589 380 N
ATOM 5490 CA ILE A 698 7.904 101.891 222.523 1.00 47.51 C
ANISOU 5490 CA ILE A 698 5857 8005 4191 -989 551 402 C
ATOM 5491 C ILE A 698 9.070 102.409 221.671 1.00 46.43 C
ANISOU 5491 C ILE A 698 5748 7842 4053 -895 484 395 C
ATOM 5492 O ILE A 698 9.068 102.348 220.451 1.00 46.03 O
ANISOU 5492 O ILE A 698 5665 7815 4011 -899 415 410 O
ATOM 5493 CB ILE A 698 7.000 103.010 223.053 1.00 47.80 C
ANISOU 5493 CB ILE A 698 5751 8103 4310 -957 630 412 C
ATOM 5494 CG1 ILE A 698 5.527 102.620 222.869 1.00 49.91 C
ANISOU 5494 CG1 ILE A 698 5901 8442 4619 -1054 651 439 C
ATOM 5495 CG2 ILE A 698 7.267 104.288 222.348 1.00 47.17 C
ANISOU 5495 CG2 ILE A 698 5580 8047 4297 -853 604 422 C
ATOM 5496 CD1 ILE A 698 4.988 101.551 223.869 1.00 52.44 C
ANISOU 5496 CD1 ILE A 698 6291 8748 4888 -1167 716 431 C
ATOM 5497 N GLN A 699 10.087 102.894 222.358 1.00 46.07 N
ANISOU 5497 N GLN A 699 5768 7748 3990 -818 506 371 N
ATOM 5498 CA GLN A 699 11.327 103.265 221.743 1.00 44.81 C
ANISOU 5498 CA GLN A 699 5649 7554 3822 -738 452 360 C
ATOM 5499 C GLN A 699 11.874 102.186 220.822 1.00 43.69 C
ANISOU 5499 C GLN A 699 5592 7381 3626 -769 380 357 C
ATOM 5500 O GLN A 699 12.273 102.486 219.688 1.00 43.39 O
ANISOU 5500 O GLN A 699 5529 7356 3601 -734 330 364 O
ATOM 5501 CB GLN A 699 12.326 103.646 222.835 1.00 44.76 C
ANISOU 5501 CB GLN A 699 5720 7495 3792 -677 484 331 C
ATOM 5502 CG GLN A 699 12.499 105.165 222.899 1.00 47.74 C
ANISOU 5502 CG GLN A 699 6013 7892 4234 -594 512 328 C
ATOM 5503 CD GLN A 699 12.415 105.718 224.278 1.00 50.36 C
ANISOU 5503 CD GLN A 699 6361 8209 4565 -577 587 306 C
ATOM 5504 OE1 GLN A 699 13.180 105.326 225.152 1.00 53.03 O
ANISOU 5504 OE1 GLN A 699 6808 8497 4842 -575 589 283 O
ATOM 5505 NE2 GLN A 699 11.486 106.647 224.493 1.00 51.47 N
ANISOU 5505 NE2 GLN A 699 6396 8389 4769 -563 649 313 N
ATOM 5506 N GLN A 700 11.884 100.937 221.291 1.00 42.76 N
ANISOU 5506 N GLN A 700 5583 7218 3447 -835 380 347 N
ATOM 5507 CA GLN A 700 12.468 99.854 220.502 1.00 41.66 C
ANISOU 5507 CA GLN A 700 5543 7032 3253 -858 319 338 C
ATOM 5508 C GLN A 700 11.470 99.507 219.419 1.00 41.66 C
ANISOU 5508 C GLN A 700 5483 7083 3263 -938 284 357 C
ATOM 5509 O GLN A 700 11.828 99.228 218.273 1.00 40.97 O
ANISOU 5509 O GLN A 700 5420 6991 3157 -936 228 353 O
ATOM 5510 CB GLN A 700 12.849 98.656 221.373 1.00 41.41 C
ANISOU 5510 CB GLN A 700 5658 6923 3153 -895 328 324 C
ATOM 5511 CG GLN A 700 13.895 99.000 222.444 1.00 42.63 C
ANISOU 5511 CG GLN A 700 5874 7030 3291 -815 347 309 C
ATOM 5512 CD GLN A 700 14.550 97.784 223.099 1.00 43.88 C
ANISOU 5512 CD GLN A 700 6191 7101 3379 -828 331 300 C
ATOM 5513 OE1 GLN A 700 13.993 97.164 224.001 1.00 45.74 O
ANISOU 5513 OE1 GLN A 700 6489 7314 3577 -896 365 310 O
ATOM 5514 NE2 GLN A 700 15.753 97.462 222.662 1.00 43.96 N
ANISOU 5514 NE2 GLN A 700 6268 7061 3373 -760 283 285 N
ATOM 5515 N ALA A 701 10.200 99.593 219.789 1.00 41.99 N
ANISOU 5515 N ALA A 701 5439 7179 3337 -1008 319 377 N
ATOM 5516 CA ALA A 701 9.121 99.322 218.864 1.00 42.07 C
ANISOU 5516 CA ALA A 701 5371 7250 3365 -1093 282 399 C
ATOM 5517 C ALA A 701 9.239 100.260 217.694 1.00 41.35 C
ANISOU 5517 C ALA A 701 5189 7210 3314 -1032 232 416 C
ATOM 5518 O ALA A 701 9.237 99.811 216.559 1.00 42.15 O
ANISOU 5518 O ALA A 701 5312 7318 3384 -1069 166 418 O
ATOM 5519 CB ALA A 701 7.786 99.485 219.534 1.00 42.85 C
ANISOU 5519 CB ALA A 701 5362 7410 3510 -1160 337 420 C
ATOM 5520 N PHE A 702 9.380 101.551 217.980 1.00 40.29 N
ANISOU 5520 N PHE A 702 4967 7101 3239 -941 264 426 N
ATOM 5521 CA PHE A 702 9.433 102.592 216.955 1.00 39.17 C
ANISOU 5521 CA PHE A 702 4736 7005 3143 -878 223 450 C
ATOM 5522 C PHE A 702 10.539 102.313 215.948 1.00 38.24 C
ANISOU 5522 C PHE A 702 4711 6849 2970 -847 166 435 C
ATOM 5523 O PHE A 702 10.319 102.392 214.748 1.00 38.36 O
ANISOU 5523 O PHE A 702 4696 6901 2979 -864 107 455 O
ATOM 5524 CB PHE A 702 9.604 103.958 217.621 1.00 38.39 C
ANISOU 5524 CB PHE A 702 4563 6914 3111 -780 279 455 C
ATOM 5525 CG PHE A 702 9.860 105.097 216.662 1.00 37.97 C
ANISOU 5525 CG PHE A 702 4440 6888 3100 -704 244 481 C
ATOM 5526 CD1 PHE A 702 8.849 105.603 215.857 1.00 38.62 C
ANISOU 5526 CD1 PHE A 702 4399 7042 3234 -716 206 526 C
ATOM 5527 CD2 PHE A 702 11.111 105.702 216.600 1.00 37.18 C
ANISOU 5527 CD2 PHE A 702 4393 6741 2991 -620 247 464 C
ATOM 5528 CE1 PHE A 702 9.096 106.679 214.997 1.00 38.47 C
ANISOU 5528 CE1 PHE A 702 4326 7039 3250 -643 173 557 C
ATOM 5529 CE2 PHE A 702 11.351 106.784 215.725 1.00 37.01 C
ANISOU 5529 CE2 PHE A 702 4315 6740 3009 -555 220 492 C
ATOM 5530 CZ PHE A 702 10.346 107.256 214.936 1.00 37.65 C
ANISOU 5530 CZ PHE A 702 4289 6884 3133 -566 184 539 C
ATOM 5531 N VAL A 703 11.700 101.927 216.457 1.00 37.48 N
ANISOU 5531 N VAL A 703 4728 6679 2832 -806 186 400 N
ATOM 5532 CA VAL A 703 12.868 101.625 215.642 1.00 37.03 C
ANISOU 5532 CA VAL A 703 4761 6579 2729 -768 149 379 C
ATOM 5533 C VAL A 703 12.607 100.387 214.809 1.00 38.09 C
ANISOU 5533 C VAL A 703 4973 6701 2800 -853 101 370 C
ATOM 5534 O VAL A 703 12.558 100.465 213.586 1.00 38.57 O
ANISOU 5534 O VAL A 703 5023 6790 2843 -866 53 379 O
ATOM 5535 CB VAL A 703 14.098 101.333 216.519 1.00 36.48 C
ANISOU 5535 CB VAL A 703 4791 6435 2635 -710 178 345 C
ATOM 5536 CG1 VAL A 703 15.170 100.660 215.718 1.00 36.29 C
ANISOU 5536 CG1 VAL A 703 4867 6363 2560 -686 146 319 C
ATOM 5537 CG2 VAL A 703 14.621 102.590 217.220 1.00 36.12 C
ANISOU 5537 CG2 VAL A 703 4688 6393 2641 -622 217 346 C
ATOM 5538 N LEU A 704 12.444 99.245 215.477 1.00 39.02 N
ANISOU 5538 N LEU A 704 5177 6770 2878 -916 114 351 N
ATOM 5539 CA LEU A 704 12.166 97.980 214.817 1.00 40.23 C
ANISOU 5539 CA LEU A 704 5420 6896 2968 -1008 75 336 C
ATOM 5540 C LEU A 704 11.044 98.099 213.769 1.00 42.06 C
ANISOU 5540 C LEU A 704 5569 7207 3207 -1089 22 363 C
ATOM 5541 O LEU A 704 11.124 97.494 212.681 1.00 41.97 O
ANISOU 5541 O LEU A 704 5621 7185 3140 -1133 -29 350 O
ATOM 5542 CB LEU A 704 11.779 96.927 215.850 1.00 40.64 C
ANISOU 5542 CB LEU A 704 5550 6898 2994 -1081 104 327 C
ATOM 5543 CG LEU A 704 12.866 96.420 216.787 1.00 38.96 C
ANISOU 5543 CG LEU A 704 5458 6593 2751 -1022 135 302 C
ATOM 5544 CD1 LEU A 704 12.205 95.674 217.874 1.00 39.15 C
ANISOU 5544 CD1 LEU A 704 5528 6589 2758 -1102 169 308 C
ATOM 5545 CD2 LEU A 704 13.823 95.534 216.049 1.00 38.60 C
ANISOU 5545 CD2 LEU A 704 5543 6473 2650 -1001 104 269 C
ATOM 5546 N LYS A 705 10.007 98.869 214.102 1.00 43.23 N
ANISOU 5546 N LYS A 705 5574 7431 3421 -1106 34 400 N
ATOM 5547 CA LYS A 705 9.027 99.200 213.119 1.00 45.43 C
ANISOU 5547 CA LYS A 705 5750 7793 3719 -1159 -24 434 C
ATOM 5548 C LYS A 705 9.765 99.779 211.936 1.00 45.92 C
ANISOU 5548 C LYS A 705 5826 7862 3760 -1093 -69 437 C
ATOM 5549 O LYS A 705 9.743 99.198 210.839 1.00 47.11 O
ANISOU 5549 O LYS A 705 6037 8015 3849 -1150 -129 429 O
ATOM 5550 CB LYS A 705 7.975 100.199 213.601 1.00 46.06 C
ANISOU 5550 CB LYS A 705 5657 7954 3890 -1148 0 476 C
ATOM 5551 CG LYS A 705 6.968 100.533 212.452 1.00 48.50 C
ANISOU 5551 CG LYS A 705 5852 8354 4221 -1199 -80 519 C
ATOM 5552 CD LYS A 705 5.910 101.584 212.790 1.00 51.42 C
ANISOU 5552 CD LYS A 705 6035 8809 4695 -1173 -63 566 C
ATOM 5553 CE LYS A 705 5.244 102.118 211.504 1.00 52.79 C
ANISOU 5553 CE LYS A 705 6107 9065 4887 -1185 -158 616 C
ATOM 5554 NZ LYS A 705 4.308 103.283 211.726 1.00 53.16 N
ANISOU 5554 NZ LYS A 705 5964 9188 5045 -1132 -147 668 N
ATOM 5555 N HIS A 706 10.435 100.905 212.128 1.00 45.69 N
ANISOU 5555 N HIS A 706 5753 7834 3775 -981 -37 447 N
ATOM 5556 CA HIS A 706 11.048 101.546 210.957 1.00 46.49 C
ANISOU 5556 CA HIS A 706 5858 7949 3858 -927 -76 459 C
ATOM 5557 C HIS A 706 12.085 100.724 210.196 1.00 46.75 C
ANISOU 5557 C HIS A 706 6036 7922 3804 -929 -91 417 C
ATOM 5558 O HIS A 706 12.147 100.800 208.958 1.00 47.18 O
ANISOU 5558 O HIS A 706 6111 8001 3815 -944 -141 426 O
ATOM 5559 CB HIS A 706 11.489 102.959 211.263 1.00 45.59 C
ANISOU 5559 CB HIS A 706 5665 7847 3812 -817 -40 481 C
ATOM 5560 CG HIS A 706 10.332 103.850 211.546 1.00 46.96 C
ANISOU 5560 CG HIS A 706 5687 8088 4066 -814 -40 528 C
ATOM 5561 ND1 HIS A 706 9.306 104.025 210.643 1.00 50.05 N
ANISOU 5561 ND1 HIS A 706 5995 8552 4468 -863 -108 573 N
ATOM 5562 CD2 HIS A 706 9.992 104.555 212.646 1.00 47.67 C
ANISOU 5562 CD2 HIS A 706 5697 8185 4232 -770 20 537 C
ATOM 5563 CE1 HIS A 706 8.396 104.824 211.168 1.00 51.00 C
ANISOU 5563 CE1 HIS A 706 5978 8722 4676 -840 -89 610 C
ATOM 5564 NE2 HIS A 706 8.788 105.160 212.383 1.00 48.85 N
ANISOU 5564 NE2 HIS A 706 5709 |
