*** VIRAL PROTEIN 22-AUG-22 8ASY ***
Job options:
ID = 230302032218128949
JOBID = VIRAL PROTEIN 22-AUG-22 8ASY
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER VIRAL PROTEIN 22-AUG-22 8ASY
TITLE SARS-COV-2 OMICRON BA.2.75 RBD IN COMPLEX WITH ACE2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROCESSED ANGIOTENSIN-CONVERTING ENZYME 2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SPIKE PROTEIN S1;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACE2, UNQ868/PRO1885;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: S, 2;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS SARS COV-2, OMICRON, BA.2.75, ACE2, COMPLEX, SPIKE, RBD, VIRAL
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.ZHOU,J.HUO,J.REN,D.I.STUART
REVDAT 1 11-JAN-23 8ASY 0
JRNL AUTH J.HUO,A.DIJOKAITE-GURALIUC,C.LIU,D.ZHOU,H.M.GINN,R.DAS,
JRNL AUTH 2 P.SUPASA,M.SELVARAJ,R.NUTALAI,A.TUEKPRAKHON,
JRNL AUTH 3 H.M.E.DUYVESTEYN,A.J.MENTZER,D.SKELLY,T.G.RITTER,A.AMINI,
JRNL AUTH 4 S.BIBI,S.ADELE,S.A.JOHNSON,N.G.PATERSON,M.A.WILLIAMS,
JRNL AUTH 5 D.R.HALL,M.PLOWRIGHT,T.A.H.NEWMAN,H.HORNSBY,T.I.DE SILVA,
JRNL AUTH 6 N.TEMPERTON,P.KLENERMAN,E.BARNES,S.J.DUNACHIE,A.J.POLLARD,
JRNL AUTH 7 T.LAMBE,P.GOULDER,E.E.FRY,J.MONGKOLSAPAYA,J.REN,D.I.STUART,
JRNL AUTH 8 G.R.SCREATON
JRNL TITL A DELICATE BALANCE BETWEEN ANTIBODY EVASION AND ACE2
JRNL TITL 2 AFFINITY FOR OMICRON BA.2.75.
JRNL REF CELL REP 11903 2022
JRNL REFN ESSN 2211-1247
JRNL PMID 36586406
JRNL DOI 10.1016/J.CELREP.2022.111903
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 29528
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 76.1800 - 6.1400 1.00 3067 149 0.1873 0.2394
REMARK 3 2 6.1400 - 4.8700 1.00 2896 143 0.1979 0.2449
REMARK 3 3 4.8700 - 4.2600 1.00 2840 154 0.1743 0.2164
REMARK 3 4 4.2600 - 3.8700 1.00 2829 142 0.1900 0.2151
REMARK 3 5 3.8700 - 3.5900 1.00 2816 132 0.2267 0.2648
REMARK 3 6 3.5900 - 3.3800 1.00 2797 127 0.2394 0.3063
REMARK 3 7 3.3800 - 3.2100 1.00 2761 164 0.2678 0.3603
REMARK 3 8 3.2100 - 3.0700 1.00 2794 130 0.3259 0.3704
REMARK 3 9 3.0700 - 2.9500 1.00 2749 160 0.3432 0.3782
REMARK 3 10 2.9500 - 2.8500 0.92 2540 138 0.3643 0.3821
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.494
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 6802
REMARK 3 ANGLE : 0.434 9219
REMARK 3 CHIRALITY : 0.039 974
REMARK 3 PLANARITY : 0.003 1178
REMARK 3 DIHEDRAL : 11.550 2463
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.3535 29.7496 -11.3510
REMARK 3 T TENSOR
REMARK 3 T11: 0.7016 T22: 0.9308
REMARK 3 T33: 0.7877 T12: -0.0083
REMARK 3 T13: 0.1024 T23: -0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 0.1595 L22: 0.8101
REMARK 3 L33: 1.2342 L12: -0.3830
REMARK 3 L13: 0.2387 L23: 0.6509
REMARK 3 S TENSOR
REMARK 3 S11: -0.1178 S12: 0.0014 S13: 0.0814
REMARK 3 S21: 0.0463 S22: 0.0036 S23: 0.2766
REMARK 3 S31: -0.2504 S32: -0.1597 S33: -0.0473
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 193 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.0463 10.9272 -37.8029
REMARK 3 T TENSOR
REMARK 3 T11: 0.6087 T22: 0.6959
REMARK 3 T33: 0.6645 T12: -0.0165
REMARK 3 T13: -0.0849 T23: -0.0727
REMARK 3 L TENSOR
REMARK 3 L11: 1.4192 L22: 1.6077
REMARK 3 L33: 1.7796 L12: -1.4407
REMARK 3 L13: -0.6431 L23: -0.0750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.1860 S13: -0.0696
REMARK 3 S21: -0.0152 S22: -0.2023 S23: 0.0390
REMARK 3 S31: 0.1807 S32: -0.5124 S33: 0.0572
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 194 THROUGH 293 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7138 15.6473 -33.9064
REMARK 3 T TENSOR
REMARK 3 T11: 0.5409 T22: 0.6772
REMARK 3 T33: 0.6048 T12: -0.0524
REMARK 3 T13: 0.0287 T23: -0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 1.0147 L22: 1.7363
REMARK 3 L33: 1.4252 L12: 0.0307
REMARK 3 L13: 0.0900 L23: -0.2199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0347 S12: 0.1164 S13: 0.0512
REMARK 3 S21: -0.2017 S22: 0.0682 S23: 0.1190
REMARK 3 S31: -0.0436 S32: 0.1843 S33: -0.0283
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 431 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0966 6.6274 -8.9016
REMARK 3 T TENSOR
REMARK 3 T11: 0.7424 T22: 0.8706
REMARK 3 T33: 0.6786 T12: -0.0224
REMARK 3 T13: 0.0489 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 0.2826 L22: 0.6383
REMARK 3 L33: 0.5923 L12: -0.0734
REMARK 3 L13: -0.0436 L23: 0.2224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0328 S12: -0.0013 S13: -0.1920
REMARK 3 S21: 0.2400 S22: -0.1566 S23: 0.2170
REMARK 3 S31: 0.2774 S32: 0.0866 S33: 0.0312
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 432 THROUGH 614 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3124 17.0054 -30.1161
REMARK 3 T TENSOR
REMARK 3 T11: 0.5752 T22: 0.7094
REMARK 3 T33: 0.6063 T12: -0.0457
REMARK 3 T13: 0.0279 T23: -0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 0.8922 L22: 0.9333
REMARK 3 L33: 0.6204 L12: -0.3268
REMARK 3 L13: 0.0673 L23: -0.3115
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -0.1518 S13: 0.1483
REMARK 3 S21: 0.0209 S22: -0.0096 S23: -0.0784
REMARK 3 S31: -0.0961 S32: 0.0802 S33: -0.0151
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 334 THROUGH 364 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3622 23.0125 31.9432
REMARK 3 T TENSOR
REMARK 3 T11: 0.8747 T22: 0.9595
REMARK 3 T33: 0.7812 T12: 0.1482
REMARK 3 T13: 0.0869 T23: -0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 1.1332 L22: 1.0575
REMARK 3 L33: 0.6182 L12: 0.2789
REMARK 3 L13: 0.1062 L23: 0.4784
REMARK 3 S TENSOR
REMARK 3 S11: -0.2401 S12: -0.1711 S13: -0.6182
REMARK 3 S21: 0.0569 S22: 0.4017 S23: 0.1282
REMARK 3 S31: 0.7259 S32: 0.0866 S33: -0.0273
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 365 THROUGH 380 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6930 15.7296 29.2319
REMARK 3 T TENSOR
REMARK 3 T11: 1.2441 T22: 1.2376
REMARK 3 T33: 1.1118 T12: 0.2035
REMARK 3 T13: -0.0464 T23: -0.1693
REMARK 3 L TENSOR
REMARK 3 L11: 0.0975 L22: 0.1495
REMARK 3 L33: 0.0070 L12: -0.1359
REMARK 3 L13: 0.0402 L23: -0.0292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.4322 S13: 0.0804
REMARK 3 S21: -0.0872 S22: -0.3510 S23: 0.0819
REMARK 3 S31: 1.2826 S32: 0.5704 S33: 0.0309
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 393 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1792 22.0477 39.8508
REMARK 3 T TENSOR
REMARK 3 T11: 1.0090 T22: 1.0026
REMARK 3 T33: 1.0195 T12: 0.1729
REMARK 3 T13: -0.0740 T23: -0.1484
REMARK 3 L TENSOR
REMARK 3 L11: 1.1487 L22: 1.2651
REMARK 3 L33: 0.6077 L12: -0.5367
REMARK 3 L13: 0.6332 L23: -0.8298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: -1.3840 S13: -0.6633
REMARK 3 S21: 0.5513 S22: 0.8462 S23: 1.5438
REMARK 3 S31: -0.0699 S32: -0.7265 S33: -0.0156
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 394 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.4546 29.6002 20.1743
REMARK 3 T TENSOR
REMARK 3 T11: 0.8719 T22: 0.9736
REMARK 3 T33: 0.7796 T12: -0.1151
REMARK 3 T13: 0.0299 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 0.7343 L22: 0.4898
REMARK 3 L33: 0.6217 L12: -0.4111
REMARK 3 L13: -0.4530 L23: 0.1607
REMARK 3 S TENSOR
REMARK 3 S11: -0.3449 S12: 0.0934 S13: -0.2191
REMARK 3 S21: -0.0510 S22: -0.1153 S23: -0.2866
REMARK 3 S31: 0.3914 S32: 0.8369 S33: -0.0368
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 422 THROUGH 516 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2382 31.2964 15.0806
REMARK 3 T TENSOR
REMARK 3 T11: 0.7490 T22: 0.7993
REMARK 3 T33: 0.7892 T12: -0.1047
REMARK 3 T13: 0.0385 T23: -0.0818
REMARK 3 L TENSOR
REMARK 3 L11: 1.1813 L22: 2.2204
REMARK 3 L33: 1.4886 L12: -0.7062
REMARK 3 L13: -0.6361 L23: 0.4556
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: -0.0565 S13: -0.0850
REMARK 3 S21: 0.1850 S22: 0.1502 S23: -0.1297
REMARK 3 S31: -0.1425 S32: 0.2964 S33: -0.0717
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 517 THROUGH 533 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1671 25.6054 48.8857
REMARK 3 T TENSOR
REMARK 3 T11: 1.4758 T22: 1.4231
REMARK 3 T33: 0.9429 T12: 0.0765
REMARK 3 T13: -0.0584 T23: -0.0796
REMARK 3 L TENSOR
REMARK 3 L11: 0.0210 L22: 5.2467
REMARK 3 L33: 5.2901 L12: -0.5302
REMARK 3 L13: 0.4783 L23: -5.2317
REMARK 3 S TENSOR
REMARK 3 S11: 0.1322 S12: -0.2092 S13: -0.4686
REMARK 3 S21: 0.5734 S22: 0.6216 S23: 0.2210
REMARK 3 S31: 0.0358 S32: -0.2738 S33: -0.0311
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8ASY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1292125075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97628
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 76.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 26.80
REMARK 200 R MERGE (I) : 0.44300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.6000
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) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 7ZF7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1% (W/V) N-OCTYL-B-D-GLUCOSIDE, 0.1
REMARK 280 M SODIUM CITRATE TRIBASIC DIHYDRATE PH 5.5 AND 22% (W/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.37650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.63050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.63050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.18825
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.63050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.63050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 165.56475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.63050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.63050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 55.18825
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.63050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.63050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 165.56475
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.37650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 ASP A 615
REMARK 465 ARG A 616
REMARK 465 HIS A 617
REMARK 465 HIS A 618
REMARK 465 HIS A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 HIS A 622
REMARK 465 THR B 333
REMARK 465 PHE B 535
REMARK 465 GLU B 536
REMARK 465 ALA B 537
REMARK 465 GLN B 538
REMARK 465 LYS B 539
REMARK 465 ILE B 540
REMARK 465 GLU B 541
REMARK 465 TRP B 542
REMARK 465 HIS B 543
REMARK 465 GLU B 544
REMARK 465 LYS B 545
REMARK 465 HIS B 546
REMARK 465 HIS B 547
REMARK 465 HIS B 548
REMARK 465 HIS B 549
REMARK 465 HIS B 550
REMARK 465 HIS B 551
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 527 CG CD CE NZ
REMARK 470 LYS B 528 CG CD CE NZ
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 ASN A 53 76.44 -151.49
REMARK 500 ILE A 54 94.99 -66.66
REMARK 500 ASN A 338 -123.61 59.91
REMARK 500 CYS A 498 64.23 -152.48
REMARK 500 ASP A 509 67.06 62.43
REMARK 500 ASN B 343 34.30 -97.07
REMARK 500 ALA B 352 56.37 -109.90
REMARK 500 LEU B 368 -80.63 -56.31
REMARK 500 LYS B 386 55.99 -104.16
REMARK 500 LEU B 387 -74.96 -73.99
REMARK 500 ASN B 388 46.66 -73.48
REMARK 500 ASP B 428 42.78 -97.80
REMARK 500 ASN B 481 14.53 59.87
REMARK 500 SER B 529 33.99 -71.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8ASY A 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615
DBREF 8ASY B 333 526 UNP P0DTC2 SPIKE_SARS2 333 526
SEQADV 8ASY ARG A 616 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 617 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 618 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 619 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 620 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 621 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS A 622 UNP Q9BYF1 EXPRESSION TAG
SEQADV 8ASY HIS B 339 UNP P0DTC2 GLY 339 VARIANT
SEQADV 8ASY PHE B 371 UNP P0DTC2 SER 371 VARIANT
SEQADV 8ASY PRO B 373 UNP P0DTC2 SER 373 VARIANT
SEQADV 8ASY PHE B 375 UNP P0DTC2 SER 375 VARIANT
SEQADV 8ASY ALA B 376 UNP P0DTC2 THR 376 VARIANT
SEQADV 8ASY ASN B 405 UNP P0DTC2 ASP 405 VARIANT
SEQADV 8ASY SER B 408 UNP P0DTC2 ARG 408 VARIANT
SEQADV 8ASY ASN B 417 UNP P0DTC2 LYS 417 VARIANT
SEQADV 8ASY LYS B 440 UNP P0DTC2 ASN 440 VARIANT
SEQADV 8ASY SER B 446 UNP P0DTC2 GLY 446 VARIANT
SEQADV 8ASY LYS B 460 UNP P0DTC2 ASN 460 VARIANT
SEQADV 8ASY ASN B 477 UNP P0DTC2 SER 477 VARIANT
SEQADV 8ASY LYS B 478 UNP P0DTC2 THR 478 VARIANT
SEQADV 8ASY ALA B 484 UNP P0DTC2 GLU 484 VARIANT
SEQADV 8ASY ARG B 498 UNP P0DTC2 GLN 498 VARIANT
SEQADV 8ASY TYR B 501 UNP P0DTC2 ASN 501 VARIANT
SEQADV 8ASY HIS B 505 UNP P0DTC2 TYR 505 VARIANT
SEQADV 8ASY LYS B 527 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY LYS B 528 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY SER B 529 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY LEU B 530 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY LEU B 531 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY ASN B 532 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY ASP B 533 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY ILE B 534 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY PHE B 535 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY GLU B 536 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY ALA B 537 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY GLN B 538 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY LYS B 539 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY ILE B 540 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY GLU B 541 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY TRP B 542 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 543 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY GLU B 544 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY LYS B 545 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 546 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 547 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 548 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 549 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 550 UNP P0DTC2 EXPRESSION TAG
SEQADV 8ASY HIS B 551 UNP P0DTC2 EXPRESSION TAG
SEQRES 1 A 604 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS
SEQRES 2 A 604 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER
SEQRES 3 A 604 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU
SEQRES 4 A 604 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER
SEQRES 5 A 604 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR
SEQRES 6 A 604 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN
SEQRES 7 A 604 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER
SEQRES 8 A 604 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR
SEQRES 9 A 604 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO
SEQRES 10 A 604 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU
SEQRES 11 A 604 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG
SEQRES 12 A 604 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS
SEQRES 13 A 604 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS
SEQRES 14 A 604 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY
SEQRES 15 A 604 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP
SEQRES 16 A 604 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL
SEQRES 17 A 604 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS
SEQRES 18 A 604 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR
SEQRES 19 A 604 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS
SEQRES 20 A 604 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU
SEQRES 21 A 604 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE
SEQRES 22 A 604 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA
SEQRES 23 A 604 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER
SEQRES 24 A 604 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN
SEQRES 25 A 604 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL
SEQRES 26 A 604 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE
SEQRES 27 A 604 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE
SEQRES 28 A 604 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP
SEQRES 29 A 604 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY
SEQRES 30 A 604 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET
SEQRES 31 A 604 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE
SEQRES 32 A 604 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR
SEQRES 33 A 604 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL
SEQRES 34 A 604 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG
SEQRES 35 A 604 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP
SEQRES 36 A 604 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY
SEQRES 37 A 604 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP
SEQRES 38 A 604 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE
SEQRES 39 A 604 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE
SEQRES 40 A 604 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO
SEQRES 41 A 604 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY
SEQRES 42 A 604 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU
SEQRES 43 A 604 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS
SEQRES 44 A 604 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO
SEQRES 45 A 604 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE
SEQRES 46 A 604 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP ARG
SEQRES 47 A 604 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 219 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR
SEQRES 2 B 219 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE
SEQRES 3 B 219 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE
SEQRES 4 B 219 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO
SEQRES 5 B 219 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA
SEQRES 6 B 219 ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN ILE
SEQRES 7 B 219 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR
SEQRES 8 B 219 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP
SEQRES 9 B 219 ASN SER ASN LYS LEU ASP SER LYS VAL SER GLY ASN TYR
SEQRES 10 B 219 ASN TYR LEU TYR ARG LEU PHE ARG LYS SER LYS LEU LYS
SEQRES 11 B 219 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA
SEQRES 12 B 219 GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PHE ASN CYS
SEQRES 13 B 219 TYR PHE PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR
SEQRES 14 B 219 GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER
SEQRES 15 B 219 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY LYS
SEQRES 16 B 219 LYS SER LEU LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE
SEQRES 17 B 219 GLU TRP HIS GLU LYS HIS HIS HIS HIS HIS HIS
HET GOL A 701 6
HET NAG A 702 14
HET GOL A 703 6
HET NAG A 704 14
HET NAG A 705 14
HET NAG A 706 14
HET NAG A 707 14
HET NAG A 708 14
HET GOL A 709 6
HET CL A 710 1
HET GOL A 711 6
HET GOL A 712 6
HET GOL A 713 6
HET GOL A 714 6
HET GOL A 715 6
HET PGE A 716 10
HET GOL A 717 6
HET GOL A 718 6
HET GOL B 601 6
HET GOL B 602 6
HETNAM GOL GLYCEROL
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 GOL 12(C3 H8 O3)
FORMUL 4 NAG 6(C8 H15 N O6)
FORMUL 12 CL CL 1-
FORMUL 18 PGE C6 H14 O4
HELIX 1 AA1 THR A 20 THR A 52 1 33
HELIX 2 AA2 THR A 55 GLN A 81 1 27
HELIX 3 AA3 MET A 82 TYR A 83 5 2
HELIX 4 AA4 PRO A 84 ILE A 88 5 5
HELIX 5 AA5 ASN A 90 GLN A 102 1 13
HELIX 6 AA6 ASN A 103 LEU A 108 5 6
HELIX 7 AA7 SER A 109 GLY A 130 1 22
HELIX 8 AA8 PRO A 146 SER A 155 1 10
HELIX 9 AA9 ASP A 157 VAL A 172 1 16
HELIX 10 AB1 VAL A 172 ASN A 194 1 23
HELIX 11 AB2 ASP A 198 ARG A 204 1 7
HELIX 12 AB3 GLY A 205 GLU A 208 5 4
HELIX 13 AB4 SER A 218 TYR A 252 1 35
HELIX 14 AB5 TRP A 275 ASN A 277 5 3
HELIX 15 AB6 LEU A 278 VAL A 283 1 6
HELIX 16 AB7 VAL A 293 GLN A 300 1 8
HELIX 17 AB8 ASP A 303 VAL A 318 1 16
HELIX 18 AB9 THR A 324 SER A 331 1 8
HELIX 19 AC1 THR A 365 TYR A 385 1 21
HELIX 20 AC2 ALA A 386 GLN A 388 5 3
HELIX 21 AC3 PRO A 389 ARG A 393 5 5
HELIX 22 AC4 GLY A 399 ALA A 413 1 15
HELIX 23 AC5 THR A 414 ILE A 421 1 8
HELIX 24 AC6 ASP A 431 ILE A 446 1 16
HELIX 25 AC7 THR A 449 LYS A 465 1 17
HELIX 26 AC8 PRO A 469 ASP A 471 5 3
HELIX 27 AC9 GLN A 472 ILE A 484 1 13
HELIX 28 AD1 CYS A 498 SER A 502 5 5
HELIX 29 AD2 LEU A 503 ASN A 508 1 6
HELIX 30 AD3 ILE A 513 ALA A 533 1 21
HELIX 31 AD4 PRO A 538 CYS A 542 5 5
HELIX 32 AD5 SER A 547 ARG A 559 1 13
HELIX 33 AD6 PRO A 565 GLY A 575 1 11
HELIX 34 AD7 VAL A 581 PHE A 588 1 8
HELIX 35 AD8 PHE A 588 ASN A 599 1 12
HELIX 36 AD9 PRO B 337 ASN B 343 1 7
HELIX 37 AE1 ASP B 364 ALA B 372 1 9
HELIX 38 AE2 ASN B 405 ILE B 410 5 6
HELIX 39 AE3 GLY B 416 ASN B 422 1 7
HELIX 40 AE4 SER B 438 SER B 443 1 6
HELIX 41 AE5 GLY B 502 HIS B 505 5 4
HELIX 42 AE6 LYS B 528 ILE B 534 5 7
SHEET 1 AA1 2 LYS A 131 CYS A 133 0
SHEET 2 AA1 2 CYS A 141 LEU A 143 -1 O LEU A 142 N VAL A 132
SHEET 1 AA2 2 LEU A 262 PRO A 263 0
SHEET 2 AA2 2 VAL A 487 VAL A 488 1 O VAL A 488 N LEU A 262
SHEET 1 AA3 2 THR A 347 GLY A 352 0
SHEET 2 AA3 2 ASP A 355 LEU A 359 -1 O ARG A 357 N TRP A 349
SHEET 1 AA4 5 ASN B 354 ILE B 358 0
SHEET 2 AA4 5 ASN B 394 ARG B 403 -1 O VAL B 395 N ILE B 358
SHEET 3 AA4 5 PRO B 507 GLU B 516 -1 O VAL B 512 N ASP B 398
SHEET 4 AA4 5 GLY B 431 ASN B 437 -1 N ILE B 434 O VAL B 511
SHEET 5 AA4 5 ALA B 376 TYR B 380 -1 N TYR B 380 O GLY B 431
SHEET 1 AA5 3 CYS B 361 VAL B 362 0
SHEET 2 AA5 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361
SHEET 3 AA5 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524
SHEET 1 AA6 2 LEU B 452 ARG B 454 0
SHEET 2 AA6 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453
SHEET 1 AA7 2 TYR B 473 GLN B 474 0
SHEET 2 AA7 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473
SSBOND 1 CYS A 133 CYS A 141 1555 1555 2.03
SSBOND 2 CYS A 344 CYS A 361 1555 1555 2.03
SSBOND 3 CYS A 530 CYS A 542 1555 1555 2.03
SSBOND 4 CYS B 336 CYS B 361 1555 1555 2.03
SSBOND 5 CYS B 379 CYS B 432 1555 1555 2.03
SSBOND 6 CYS B 391 CYS B 525 1555 1555 2.03
SSBOND 7 CYS B 480 CYS B 488 1555 1555 2.03
LINK ND2 ASN A 53 C1 NAG A 706 1555 1555 1.44
LINK ND2 ASN A 90 C1 NAG A 707 1555 1555 1.44
LINK ND2 ASN A 103 C1 NAG A 708 1555 1555 1.43
LINK ND2 ASN A 322 C1 NAG A 702 1555 1555 1.44
LINK ND2 ASN A 432 C1 NAG A 705 1555 1555 1.44
LINK ND2 ASN A 546 C1 NAG A 704 1555 1555 1.44
CISPEP 1 GLU A 145 PRO A 146 0 0.54
CRYST1 105.261 105.261 220.753 90.00 90.00 90.00 P 41 21 2 8
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 0.009500 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009500 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004530 0.00000
ATOM 1 N SER A 19 -31.269 53.129 3.367 1.00 97.89 N
ANISOU 1 N SER A 19 13520 12045 11630 658 3 -840 N
ATOM 2 CA SER A 19 -30.704 51.915 2.792 1.00101.38 C
ANISOU 2 CA SER A 19 13833 12588 12100 539 94 -825 C
ATOM 3 C SER A 19 -30.542 52.049 1.281 1.00107.74 C
ANISOU 3 C SER A 19 14660 13375 12900 397 79 -775 C
ATOM 4 O SER A 19 -31.453 52.499 0.586 1.00101.47 O
ANISOU 4 O SER A 19 13917 12545 12091 440 38 -745 O
ATOM 5 CB SER A 19 -31.580 50.704 3.123 1.00101.55 C
ANISOU 5 CB SER A 19 13715 12724 12144 638 186 -825 C
ATOM 6 OG SER A 19 -32.871 50.836 2.555 1.00102.73 O
ANISOU 6 OG SER A 19 13858 12880 12295 715 173 -799 O
ATOM 7 N THR A 20 -29.375 51.654 0.779 1.00106.57 N
ANISOU 7 N THR A 20 14477 13255 12760 234 112 -772 N
ATOM 8 CA THR A 20 -29.093 51.735 -0.644 1.00 97.99 C
ANISOU 8 CA THR A 20 13413 12156 11664 88 109 -726 C
ATOM 9 C THR A 20 -29.811 50.617 -1.398 1.00 99.22 C
ANISOU 9 C THR A 20 13446 12414 11840 101 175 -692 C
ATOM 10 O THR A 20 -30.357 49.681 -0.809 1.00 94.26 O
ANISOU 10 O THR A 20 12706 11872 11236 197 235 -707 O
ATOM 11 CB THR A 20 -27.588 51.660 -0.901 1.00 97.05 C
ANISOU 11 CB THR A 20 13283 12045 11546 -91 128 -741 C
ATOM 12 OG1 THR A 20 -27.106 50.360 -0.540 1.00102.05 O
ANISOU 12 OG1 THR A 20 13765 12802 12206 -103 211 -769 O
ATOM 13 CG2 THR A 20 -26.855 52.709 -0.081 1.00 98.72 C
ANISOU 13 CG2 THR A 20 13603 12160 11746 -106 64 -785 C
ATOM 14 N ILE A 21 -29.800 50.727 -2.728 1.00100.70 N
ANISOU 14 N ILE A 21 13663 12585 12014 1 164 -646 N
ATOM 15 CA ILE A 21 -30.413 49.701 -3.568 1.00100.28 C
ANISOU 15 CA ILE A 21 13500 12622 11980 2 219 -615 C
ATOM 16 C ILE A 21 -29.686 48.372 -3.402 1.00102.26 C
ANISOU 16 C ILE A 21 13603 12992 12258 -63 309 -630 C
ATOM 17 O ILE A 21 -30.311 47.304 -3.376 1.00100.30 O
ANISOU 17 O ILE A 21 13238 12835 12036 -4 367 -628 O
ATOM 18 CB ILE A 21 -30.436 50.162 -5.039 1.00102.74 C
ANISOU 18 CB ILE A 21 13892 12882 12262 -94 182 -565 C
ATOM 19 CG1 ILE A 21 -31.575 51.157 -5.265 1.00 98.40 C
ANISOU 19 CG1 ILE A 21 13464 12239 11686 21 97 -553 C
ATOM 20 CG2 ILE A 21 -30.565 48.973 -5.983 1.00104.65 C
ANISOU 20 CG2 ILE A 21 14010 13228 12525 -145 246 -537 C
ATOM 21 CD1 ILE A 21 -32.951 50.563 -5.061 1.00 99.27 C
ANISOU 21 CD1 ILE A 21 13477 12416 11824 180 112 -565 C
ATOM 22 N GLU A 22 -28.357 48.415 -3.275 1.00105.87 N
ANISOU 22 N GLU A 22 14066 13452 12708 -184 319 -653 N
ATOM 23 CA GLU A 22 -27.593 47.183 -3.101 1.00104.88 C
ANISOU 23 CA GLU A 22 13810 13440 12601 -238 394 -677 C
ATOM 24 C GLU A 22 -27.931 46.508 -1.777 1.00 91.64 C
ANISOU 24 C GLU A 22 12065 11814 10942 -104 432 -719 C
ATOM 25 O GLU A 22 -27.979 45.274 -1.692 1.00 88.23 O
ANISOU 25 O GLU A 22 11520 11479 10524 -88 500 -725 O
ATOM 26 CB GLU A 22 -26.095 47.476 -3.194 1.00 99.46 C
ANISOU 26 CB GLU A 22 13144 12747 11902 -388 388 -707 C
ATOM 27 CG GLU A 22 -25.209 46.267 -2.930 1.00 94.42 C
ANISOU 27 CG GLU A 22 12376 12225 11273 -431 452 -749 C
ATOM 28 CD GLU A 22 -23.764 46.501 -3.328 1.00109.54 C
ANISOU 28 CD GLU A 22 14292 14153 13177 -597 450 -780 C
ATOM 29 OE1 GLU A 22 -23.527 47.238 -4.308 1.00128.22 O
ANISOU 29 OE1 GLU A 22 16729 16463 15525 -714 426 -744 O
ATOM 30 OE2 GLU A 22 -22.865 45.946 -2.661 1.00105.01 O
ANISOU 30 OE2 GLU A 22 13648 13644 12608 -610 473 -845 O
ATOM 31 N GLU A 23 -28.177 47.301 -0.731 1.00100.96 N
ANISOU 31 N GLU A 23 13320 12924 12116 -4 390 -748 N
ATOM 32 CA GLU A 23 -28.539 46.729 0.562 1.00 94.83 C
ANISOU 32 CA GLU A 23 12495 12187 11349 132 428 -786 C
ATOM 33 C GLU A 23 -29.936 46.123 0.531 1.00 92.68 C
ANISOU 33 C GLU A 23 12161 11960 11093 244 471 -759 C
ATOM 34 O GLU A 23 -30.181 45.081 1.151 1.00 89.42 O
ANISOU 34 O GLU A 23 11664 11621 10691 306 542 -775 O
ATOM 35 CB GLU A 23 -28.441 47.795 1.651 1.00 87.75 C
ANISOU 35 CB GLU A 23 11702 11201 10438 213 367 -824 C
ATOM 36 CG GLU A 23 -27.020 48.245 1.945 1.00100.97 C
ANISOU 36 CG GLU A 23 13417 12842 12103 115 333 -869 C
ATOM 37 CD GLU A 23 -26.974 49.442 2.870 1.00116.60 C
ANISOU 37 CD GLU A 23 15515 14718 14070 188 257 -902 C
ATOM 38 OE1 GLU A 23 -27.966 50.200 2.907 1.00108.42 O
ANISOU 38 OE1 GLU A 23 14556 13615 13024 280 212 -876 O
ATOM 39 OE2 GLU A 23 -25.950 49.625 3.562 1.00117.60 O
ANISOU 39 OE2 GLU A 23 15656 14830 14194 160 238 -959 O
ATOM 40 N GLN A 24 -30.868 46.763 -0.180 1.00 91.35 N
ANISOU 40 N GLN A 24 12037 11746 10924 272 428 -724 N
ATOM 41 CA GLN A 24 -32.201 46.191 -0.330 1.00 87.36 C
ANISOU 41 CA GLN A 24 11459 11292 10441 368 466 -708 C
ATOM 42 C GLN A 24 -32.164 44.897 -1.131 1.00 87.03 C
ANISOU 42 C GLN A 24 11298 11347 10421 293 536 -684 C
ATOM 43 O GLN A 24 -32.967 43.990 -0.880 1.00 89.34 O
ANISOU 43 O GLN A 24 11498 11710 10738 360 601 -687 O
ATOM 44 CB GLN A 24 -33.136 47.200 -0.998 1.00 95.36 C
ANISOU 44 CB GLN A 24 12550 12236 11445 416 390 -686 C
ATOM 45 CG GLN A 24 -33.251 48.524 -0.264 1.00 94.20 C
ANISOU 45 CG GLN A 24 12533 11987 11270 499 309 -709 C
ATOM 46 CD GLN A 24 -33.940 49.590 -1.093 1.00 98.91 C
ANISOU 46 CD GLN A 24 13235 12502 11845 526 218 -688 C
ATOM 47 OE1 GLN A 24 -34.685 49.282 -2.025 1.00 94.19 O
ANISOU 47 OE1 GLN A 24 12594 11936 11257 531 221 -665 O
ATOM 48 NE2 GLN A 24 -33.691 50.851 -0.763 1.00 99.97 N
ANISOU 48 NE2 GLN A 24 13515 12526 11944 547 132 -698 N
ATOM 49 N ALA A 25 -31.244 44.792 -2.092 1.00 89.51 N
ANISOU 49 N ALA A 25 11615 11668 10727 152 527 -663 N
ATOM 50 CA ALA A 25 -31.135 43.570 -2.882 1.00 90.48 C
ANISOU 50 CA ALA A 25 11630 11882 10865 81 586 -642 C
ATOM 51 C ALA A 25 -30.522 42.439 -2.067 1.00 84.81 C
ANISOU 51 C ALA A 25 10834 11241 10150 82 658 -674 C
ATOM 52 O ALA A 25 -30.906 41.274 -2.226 1.00 83.47 O
ANISOU 52 O ALA A 25 10569 11148 9997 92 721 -666 O
ATOM 53 CB ALA A 25 -30.315 43.833 -4.144 1.00 87.44 C
ANISOU 53 CB ALA A 25 11277 11483 10463 -65 556 -612 C
ATOM 54 N LYS A 26 -29.562 42.759 -1.194 1.00 81.02 N
ANISOU 54 N LYS A 26 10397 10737 9650 74 646 -715 N
ATOM 55 CA LYS A 26 -28.994 41.738 -0.319 1.00 81.74 C
ANISOU 55 CA LYS A 26 10432 10892 9735 97 704 -755 C
ATOM 56 C LYS A 26 -30.053 41.172 0.617 1.00 84.50 C
ANISOU 56 C LYS A 26 10749 11262 10094 233 761 -762 C
ATOM 57 O LYS A 26 -30.066 39.968 0.898 1.00 81.76 O
ANISOU 57 O LYS A 26 10335 10985 9746 248 830 -771 O
ATOM 58 CB LYS A 26 -27.825 42.314 0.480 1.00 83.28 C
ANISOU 58 CB LYS A 26 10686 11050 9908 79 668 -808 C
ATOM 59 CG LYS A 26 -26.591 42.626 -0.349 1.00 88.66 C
ANISOU 59 CG LYS A 26 11375 11733 10578 -74 634 -816 C
ATOM 60 CD LYS A 26 -25.417 43.016 0.537 1.00 90.51 C
ANISOU 60 CD LYS A 26 11646 11948 10797 -87 605 -884 C
ATOM 61 CE LYS A 26 -24.161 43.263 -0.284 1.00105.28 C
ANISOU 61 CE LYS A 26 13507 13835 12659 -250 582 -901 C
ATOM 62 NZ LYS A 26 -22.980 43.554 0.577 1.00101.41 N
ANISOU 62 NZ LYS A 26 13032 13339 12158 -266 554 -983 N
ATOM 63 N THR A 27 -30.953 42.027 1.109 1.00 86.15 N
ANISOU 63 N THR A 27 11011 11414 10309 334 733 -761 N
ATOM 64 CA THR A 27 -32.049 41.547 1.944 1.00 83.42 C
ANISOU 64 CA THR A 27 10630 11094 9973 459 794 -768 C
ATOM 65 C THR A 27 -33.089 40.800 1.118 1.00 83.87 C
ANISOU 65 C THR A 27 10596 11208 10062 452 840 -734 C
ATOM 66 O THR A 27 -33.673 39.821 1.597 1.00 84.35 O
ANISOU 66 O THR A 27 10592 11324 10132 501 922 -740 O
ATOM 67 CB THR A 27 -32.693 42.719 2.686 1.00 87.46 C
ANISOU 67 CB THR A 27 11220 11534 10478 572 746 -784 C
ATOM 68 OG1 THR A 27 -31.679 43.467 3.367 1.00 87.55 O
ANISOU 68 OG1 THR A 27 11320 11484 10463 570 692 -817 O
ATOM 69 CG2 THR A 27 -33.706 42.218 3.704 1.00 86.98 C
ANISOU 69 CG2 THR A 27 11123 11506 10421 702 819 -800 C
ATOM 70 N PHE A 28 -33.327 41.240 -0.119 1.00 89.51 N
ANISOU 70 N PHE A 28 11310 11909 10792 392 789 -702 N
ATOM 71 CA PHE A 28 -34.254 40.533 -0.996 1.00 85.97 C
ANISOU 71 CA PHE A 28 10773 11516 10377 382 822 -676 C
ATOM 72 C PHE A 28 -33.729 39.145 -1.342 1.00 83.93 C
ANISOU 72 C PHE A 28 10433 11335 10123 303 888 -667 C
ATOM 73 O PHE A 28 -34.468 38.156 -1.276 1.00 75.59 O
ANISOU 73 O PHE A 28 9294 10336 9089 330 957 -664 O
ATOM 74 CB PHE A 28 -34.504 41.352 -2.263 1.00 88.14 C
ANISOU 74 CB PHE A 28 11084 11749 10656 339 743 -646 C
ATOM 75 CG PHE A 28 -35.157 40.576 -3.369 1.00 92.09 C
ANISOU 75 CG PHE A 28 11495 12307 11188 306 765 -621 C
ATOM 76 CD1 PHE A 28 -36.498 40.237 -3.299 1.00 92.13 C
ANISOU 76 CD1 PHE A 28 11427 12349 11228 392 796 -633 C
ATOM 77 CD2 PHE A 28 -34.430 40.189 -4.482 1.00 88.35 C
ANISOU 77 CD2 PHE A 28 11008 11854 10708 189 753 -592 C
ATOM 78 CE1 PHE A 28 -37.099 39.522 -4.317 1.00 88.51 C
ANISOU 78 CE1 PHE A 28 10884 11943 10804 363 811 -617 C
ATOM 79 CE2 PHE A 28 -35.025 39.475 -5.502 1.00 91.77 C
ANISOU 79 CE2 PHE A 28 11362 12337 11168 165 767 -571 C
ATOM 80 CZ PHE A 28 -36.362 39.141 -5.420 1.00 91.11 C
ANISOU 80 CZ PHE A 28 11207 12286 11124 252 793 -584 C
ATOM 81 N LEU A 29 -32.449 39.053 -1.717 1.00 89.72 N
ANISOU 81 N LEU A 29 11188 12072 10832 202 866 -665 N
ATOM 82 CA LEU A 29 -31.848 37.750 -1.983 1.00 82.97 C
ANISOU 82 CA LEU A 29 10264 11292 9971 136 919 -665 C
ATOM 83 C LEU A 29 -31.778 36.898 -0.722 1.00 84.30 C
ANISOU 83 C LEU A 29 10419 11489 10123 203 990 -698 C
ATOM 84 O LEU A 29 -31.794 35.665 -0.808 1.00 82.89 O
ANISOU 84 O LEU A 29 10180 11370 9943 185 1049 -695 O
ATOM 85 CB LEU A 29 -30.452 37.924 -2.581 1.00 68.60 C
ANISOU 85 CB LEU A 29 8468 9474 8123 22 877 -668 C
ATOM 86 CG LEU A 29 -30.364 38.528 -3.983 1.00 81.75 C
ANISOU 86 CG LEU A 29 10149 11120 9793 -68 822 -629 C
ATOM 87 CD1 LEU A 29 -28.914 38.779 -4.357 1.00 86.96 C
ANISOU 87 CD1 LEU A 29 10836 11782 10422 -182 793 -643 C
ATOM 88 CD2 LEU A 29 -31.035 37.620 -5.003 1.00 85.90 C
ANISOU 88 CD2 LEU A 29 10592 11702 10342 -90 849 -595 C
ATOM 89 N ASP A 30 -31.697 37.534 0.449 1.00 86.87 N
ANISOU 89 N ASP A 30 10809 11766 10430 283 982 -729 N
ATOM 90 CA ASP A 30 -31.704 36.784 1.700 1.00 89.00 C
ANISOU 90 CA ASP A 30 11085 12055 10678 361 1051 -760 C
ATOM 91 C ASP A 30 -33.061 36.132 1.937 1.00 87.35 C
ANISOU 91 C ASP A 30 10821 11875 10494 425 1129 -745 C
ATOM 92 O ASP A 30 -33.136 34.983 2.387 1.00 84.30 O
ANISOU 92 O ASP A 30 10407 11528 10094 438 1207 -751 O
ATOM 93 CB ASP A 30 -31.336 37.707 2.862 1.00 92.50 C
ANISOU 93 CB ASP A 30 11616 12434 11094 439 1018 -798 C
ATOM 94 CG ASP A 30 -30.603 36.984 3.974 1.00107.59 C
ANISOU 94 CG ASP A 30 13557 14360 12963 484 1059 -842 C
ATOM 95 OD1 ASP A 30 -30.709 35.743 4.052 1.00122.78 O
ANISOU 95 OD1 ASP A 30 15440 16335 14875 482 1130 -840 O
ATOM 96 OD2 ASP A 30 -29.922 37.660 4.773 1.00109.30 O
ANISOU 96 OD2 ASP A 30 13843 14530 13153 526 1016 -883 O
ATOM 97 N LYS A 31 -34.144 36.852 1.636 1.00 90.02 N
ANISOU 97 N LYS A 31 11144 12193 10867 466 1110 -729 N
ATOM 98 CA LYS A 31 -35.478 36.272 1.743 1.00 79.41 C
ANISOU 98 CA LYS A 31 9729 10888 9556 517 1183 -722 C
ATOM 99 C LYS A 31 -35.711 35.222 0.664 1.00 87.81 C
ANISOU 99 C LYS A 31 10704 12012 10650 434 1213 -696 C
ATOM 100 O LYS A 31 -36.397 34.221 0.901 1.00 88.73 O
ANISOU 100 O LYS A 31 10759 12172 10781 446 1298 -696 O
ATOM 101 CB LYS A 31 -36.533 37.375 1.652 1.00 79.72 C
ANISOU 101 CB LYS A 31 9771 10896 9622 590 1140 -726 C
ATOM 102 CG LYS A 31 -37.972 36.891 1.741 1.00 69.73 C
ANISOU 102 CG LYS A 31 8419 9680 8397 645 1211 -732 C
ATOM 103 CD LYS A 31 -38.398 36.703 3.184 1.00 87.75 C
ANISOU 103 CD LYS A 31 10718 11964 10658 741 1293 -760 C
ATOM 104 CE LYS A 31 -39.903 36.520 3.298 1.00101.40 C
ANISOU 104 CE LYS A 31 12359 13739 12428 801 1356 -776 C
ATOM 105 NZ LYS A 31 -40.287 35.088 3.424 1.00105.09 N
ANISOU 105 NZ LYS A 31 12752 14268 12912 758 1474 -771 N
ATOM 106 N PHE A 32 -35.147 35.434 -0.528 1.00 91.94 N
ANISOU 106 N PHE A 32 11220 12534 11178 346 1146 -673 N
ATOM 107 CA PHE A 32 -35.361 34.497 -1.626 1.00 85.04 C
ANISOU 107 CA PHE A 32 10265 11716 10331 273 1163 -648 C
ATOM 108 C PHE A 32 -34.701 33.152 -1.350 1.00 86.11 C
ANISOU 108 C PHE A 32 10381 11896 10439 231 1226 -653 C
ATOM 109 O PHE A 32 -35.293 32.101 -1.620 1.00 94.11 O
ANISOU 109 O PHE A 32 11328 12956 11476 214 1284 -643 O
ATOM 110 CB PHE A 32 -34.837 35.090 -2.935 1.00 79.98 C
ANISOU 110 CB PHE A 32 9637 11060 9692 194 1077 -623 C
ATOM 111 CG PHE A 32 -34.816 34.112 -4.079 1.00 85.92 C
ANISOU 111 CG PHE A 32 10316 11868 10461 116 1086 -598 C
ATOM 112 CD1 PHE A 32 -35.956 33.879 -4.830 1.00 89.33 C
ANISOU 112 CD1 PHE A 32 10677 12323 10941 129 1090 -586 C
ATOM 113 CD2 PHE A 32 -33.654 33.428 -4.403 1.00 80.79 C
ANISOU 113 CD2 PHE A 32 9667 11250 9778 36 1087 -594 C
ATOM 114 CE1 PHE A 32 -35.940 32.980 -5.881 1.00 83.10 C
ANISOU 114 CE1 PHE A 32 9824 11582 10168 62 1092 -566 C
ATOM 115 CE2 PHE A 32 -33.633 32.527 -5.450 1.00 83.15 C
ANISOU 115 CE2 PHE A 32 9903 11601 10089 -28 1091 -573 C
ATOM 116 CZ PHE A 32 -34.777 32.304 -6.191 1.00 87.21 C
ANISOU 116 CZ PHE A 32 10352 12132 10652 -16 1093 -556 C
ATOM 117 N ASN A 33 -33.477 33.164 -0.815 1.00 79.63 N
ANISOU 117 N ASN A 33 9623 11063 9570 217 1211 -673 N
ATOM 118 CA ASN A 33 -32.740 31.920 -0.612 1.00 78.76 C
ANISOU 118 CA ASN A 33 9507 10994 9423 185 1254 -684 C
ATOM 119 C ASN A 33 -33.487 30.967 0.312 1.00 83.38 C
ANISOU 119 C ASN A 33 10085 11593 10004 245 1353 -693 C
ATOM 120 O ASN A 33 -33.544 29.759 0.055 1.00 73.80 O
ANISOU 120 O ASN A 33 8837 10420 8785 209 1400 -684 O
ATOM 121 CB ASN A 33 -31.348 32.218 -0.055 1.00 75.23 C
ANISOU 121 CB ASN A 33 9129 10531 8923 180 1215 -721 C
ATOM 122 CG ASN A 33 -30.413 32.792 -1.098 1.00 76.70 C
ANISOU 122 CG ASN A 33 9312 10724 9107 88 1136 -715 C
ATOM 123 OD1 ASN A 33 -30.499 32.454 -2.279 1.00 82.48 O
ANISOU 123 OD1 ASN A 33 9989 11491 9858 17 1121 -684 O
ATOM 124 ND2 ASN A 33 -29.510 33.664 -0.667 1.00 85.25 N
ANISOU 124 ND2 ASN A 33 10454 11772 10166 87 1085 -746 N
ATOM 125 N HIS A 34 -34.074 31.491 1.390 1.00 81.90 N
ANISOU 125 N HIS A 34 9936 11369 9815 334 1386 -709 N
ATOM 126 CA HIS A 34 -34.723 30.622 2.367 1.00 78.59 C
ANISOU 126 CA HIS A 34 9523 10957 9381 388 1491 -718 C
ATOM 127 C HIS A 34 -36.049 30.085 1.844 1.00 75.95 C
ANISOU 127 C HIS A 34 9095 10658 9103 369 1550 -696 C
ATOM 128 O HIS A 34 -36.409 28.934 2.119 1.00 74.34 O
ANISOU 128 O HIS A 34 8876 10477 8892 356 1636 -693 O
ATOM 129 CB HIS A 34 -34.920 31.371 3.684 1.00 96.43 C
ANISOU 129 CB HIS A 34 11853 13169 11616 494 1510 -744 C
ATOM 130 CG HIS A 34 -33.638 31.772 4.346 1.00109.72 C
ANISOU 130 CG HIS A 34 13628 14818 13243 522 1458 -776 C
ATOM 131 ND1 HIS A 34 -32.894 32.858 3.934 1.00109.73 N
ANISOU 131 ND1 HIS A 34 13651 14792 13248 498 1357 -784 N
ATOM 132 CD2 HIS A 34 -32.962 31.227 5.385 1.00 98.17 C
ANISOU 132 CD2 HIS A 34 12244 13340 11717 571 1491 -808 C
ATOM 133 CE1 HIS A 34 -31.819 32.967 4.695 1.00105.42 C
ANISOU 133 CE1 HIS A 34 13181 14224 12651 528 1331 -823 C
ATOM 134 NE2 HIS A 34 -31.837 31.990 5.583 1.00 98.39 N
ANISOU 134 NE2 HIS A 34 12326 13339 11717 580 1407 -840 N
ATOM 135 N GLU A 35 -36.791 30.899 1.091 1.00 82.33 N
ANISOU 135 N GLU A 35 9845 11468 9967 367 1504 -685 N
ATOM 136 CA GLU A 35 -38.048 30.427 0.523 1.00 82.79 C
ANISOU 136 CA GLU A 35 9804 11568 10086 351 1549 -676 C
ATOM 137 C GLU A 35 -37.826 29.516 -0.676 1.00 89.18 C
ANISOU 137 C GLU A 35 10554 12416 10914 256 1533 -653 C
ATOM 138 O GLU A 35 -38.610 28.585 -0.894 1.00 82.32 O
ANISOU 138 O GLU A 35 9615 11584 10079 230 1599 -650 O
ATOM 139 CB GLU A 35 -38.930 31.612 0.125 1.00 81.55 C
ANISOU 139 CB GLU A 35 9608 11400 9976 398 1494 -683 C
ATOM 140 CG GLU A 35 -39.988 31.954 1.158 1.00 97.39 C
ANISOU 140 CG GLU A 35 11604 13406 11996 491 1560 -712 C
ATOM 141 CD GLU A 35 -40.772 33.202 0.807 1.00109.97 C
ANISOU 141 CD GLU A 35 13172 14988 13624 553 1489 -728 C
ATOM 142 OE1 GLU A 35 -40.851 33.542 -0.392 1.00121.84 O
ANISOU 142 OE1 GLU A 35 14641 16495 15157 516 1410 -716 O
ATOM 143 OE2 GLU A 35 -41.304 33.846 1.734 1.00117.86 O
ANISOU 143 OE2 GLU A 35 14194 15973 14615 645 1510 -754 O
ATOM 144 N ALA A 36 -36.769 29.761 -1.457 1.00 92.85 N
ANISOU 144 N ALA A 36 11046 12877 11358 203 1450 -639 N
ATOM 145 CA ALA A 36 -36.506 28.924 -2.622 1.00 85.53 C
ANISOU 145 CA ALA A 36 10065 11988 10442 120 1429 -617 C
ATOM 146 C ALA A 36 -36.039 27.534 -2.212 1.00 83.46 C
ANISOU 146 C ALA A 36 9821 11751 10141 92 1494 -620 C
ATOM 147 O ALA A 36 -36.464 26.535 -2.801 1.00 88.06 O
ANISOU 147 O ALA A 36 10344 12367 10746 46 1524 -608 O
ATOM 148 CB ALA A 36 -35.475 29.593 -3.531 1.00 76.98 C
ANISOU 148 CB ALA A 36 9010 10898 9340 70 1330 -603 C
ATOM 149 N GLU A 37 -35.168 27.449 -1.201 1.00 78.12 N
ANISOU 149 N GLU A 37 9231 11052 9400 124 1511 -640 N
ATOM 150 CA GLU A 37 -34.665 26.149 -0.767 1.00 69.76 C
ANISOU 150 CA GLU A 37 8209 10007 8288 110 1564 -649 C
ATOM 151 C GLU A 37 -35.793 25.249 -0.282 1.00 73.58 C
ANISOU 151 C GLU A 37 8669 10495 8793 121 1671 -644 C
ATOM 152 O GLU A 37 -35.752 24.030 -0.484 1.00 81.16 O
ANISOU 152 O GLU A 37 9627 11474 9736 79 1709 -638 O
ATOM 153 CB GLU A 37 -33.613 26.323 0.328 1.00 68.75 C
ANISOU 153 CB GLU A 37 8185 9849 8086 163 1558 -682 C
ATOM 154 CG GLU A 37 -32.277 26.844 -0.166 1.00 77.43 C
ANISOU 154 CG GLU A 37 9306 10959 9156 131 1462 -697 C
ATOM 155 CD GLU A 37 -31.194 26.764 0.891 1.00 86.86 C
ANISOU 155 CD GLU A 37 10594 12134 10275 183 1456 -743 C
ATOM 156 OE1 GLU A 37 -31.419 26.103 1.927 1.00103.15 O
ANISOU 156 OE1 GLU A 37 12718 14177 12299 242 1526 -759 O
ATOM 157 OE2 GLU A 37 -30.118 27.363 0.686 1.00 92.60 O
ANISOU 157 OE2 GLU A 37 11336 12866 10980 164 1381 -768 O
ATOM 158 N ASP A 38 -36.809 25.826 0.360 1.00 73.48 N
ANISOU 158 N ASP A 38 8640 10465 8815 174 1722 -651 N
ATOM 159 CA ASP A 38 -37.941 25.019 0.800 1.00 78.82 C
ANISOU 159 CA ASP A 38 9281 11150 9516 173 1834 -651 C
ATOM 160 C ASP A 38 -38.785 24.575 -0.387 1.00 79.56 C
ANISOU 160 C ASP A 38 9257 11287 9685 105 1829 -636 C
ATOM 161 O ASP A 38 -39.070 23.382 -0.546 1.00 71.13 O
ANISOU 161 O ASP A 38 8171 10236 8620 54 1888 -630 O
ATOM 162 CB ASP A 38 -38.784 25.796 1.812 1.00 85.18 C
ANISOU 162 CB ASP A 38 10092 11935 10335 251 1890 -669 C
ATOM 163 CG ASP A 38 -39.957 24.985 2.343 1.00 86.91 C
ANISOU 163 CG ASP A 38 10273 12169 10578 244 2020 -674 C
ATOM 164 OD1 ASP A 38 -39.724 23.980 3.048 1.00 68.40 O
ANISOU 164 OD1 ASP A 38 8004 9807 8178 234 2101 -672 O
ATOM 165 OD2 ASP A 38 -41.114 25.357 2.054 1.00 87.20 O
ANISOU 165 OD2 ASP A 38 10210 12237 10687 247 2042 -685 O
ATOM 166 N LEU A 39 -39.178 25.522 -1.246 1.00 82.99 N
ANISOU 166 N LEU A 39 9620 11735 10177 108 1754 -634 N
ATOM 167 CA LEU A 39 -40.024 25.190 -2.389 1.00 80.67 C
ANISOU 167 CA LEU A 39 9213 11480 9956 59 1740 -629 C
ATOM 168 C LEU A 39 -39.303 24.305 -3.397 1.00 82.00 C
ANISOU 168 C LEU A 39 9376 11670 10111 -17 1694 -606 C
ATOM 169 O LEU A 39 -39.936 23.454 -4.031 1.00 80.82 O
ANISOU 169 O LEU A 39 9154 11551 10005 -66 1719 -603 O
ATOM 170 CB LEU A 39 -40.517 26.470 -3.064 1.00 76.28 C
ANISOU 170 CB LEU A 39 8606 10927 9451 94 1657 -636 C
ATOM 171 CG LEU A 39 -41.615 27.221 -2.310 1.00 82.45 C
ANISOU 171 CG LEU A 39 9355 11706 10267 170 1700 -667 C
ATOM 172 CD1 LEU A 39 -41.894 28.558 -2.965 1.00 79.39 C
ANISOU 172 CD1 LEU A 39 8948 11307 9908 216 1598 -676 C
ATOM 173 CD2 LEU A 39 -42.877 26.378 -2.253 1.00 78.43 C
ANISOU 173 CD2 LEU A 39 8744 11239 9816 149 1796 -689 C
ATOM 174 N PHE A 40 -37.992 24.493 -3.571 1.00 79.48 N
ANISOU 174 N PHE A 40 9127 11340 9732 -27 1627 -595 N
ATOM 175 CA PHE A 40 -37.247 23.621 -4.471 1.00 74.79 C
ANISOU 175 CA PHE A 40 8530 10773 9115 -91 1585 -579 C
ATOM 176 C PHE A 40 -37.154 22.205 -3.919 1.00 71.95 C
ANISOU 176 C PHE A 40 8207 10415 8715 -113 1663 -582 C
ATOM 177 O PHE A 40 -37.155 21.240 -4.691 1.00 80.41 O
ANISOU 177 O PHE A 40 9246 11513 9794 -167 1654 -571 O
ATOM 178 CB PHE A 40 -35.850 24.187 -4.728 1.00 83.93 C
ANISOU 178 CB PHE A 40 9747 11926 10215 -97 1501 -576 C
ATOM 179 CG PHE A 40 -35.015 23.348 -5.657 1.00 83.48 C
ANISOU 179 CG PHE A 40 9684 11906 10128 -157 1455 -566 C
ATOM 180 CD1 PHE A 40 -35.162 23.455 -7.030 1.00 78.40 C
ANISOU 180 CD1 PHE A 40 8974 11291 9523 -201 1391 -544 C
ATOM 181 CD2 PHE A 40 -34.078 22.457 -5.158 1.00 87.92 C
ANISOU 181 CD2 PHE A 40 10312 12476 10616 -160 1471 -580 C
ATOM 182 CE1 PHE A 40 -34.396 22.685 -7.887 1.00 81.82 C
ANISOU 182 CE1 PHE A 40 9401 11762 9924 -251 1348 -535 C
ATOM 183 CE2 PHE A 40 -33.309 21.685 -6.009 1.00 81.18 C
ANISOU 183 CE2 PHE A 40 9451 11663 9729 -207 1424 -576 C
ATOM 184 CZ PHE A 40 -33.467 21.800 -7.375 1.00 82.01 C
ANISOU 184 CZ PHE A 40 9484 11800 9875 -254 1364 -552 C
ATOM 185 N TYR A 41 -37.079 22.059 -2.594 1.00 78.32 N
ANISOU 185 N TYR A 41 9093 11189 9475 -68 1737 -598 N
ATOM 186 CA TYR A 41 -37.027 20.724 -2.012 1.00 80.73 C
ANISOU 186 CA TYR A 41 9457 11484 9732 -84 1815 -600 C
ATOM 187 C TYR A 41 -38.361 20.007 -2.167 1.00 81.49 C
ANISOU 187 C TYR A 41 9478 11591 9893 -127 1898 -595 C
ATOM 188 O TYR A 41 -38.393 18.801 -2.440 1.00 77.31 O
ANISOU 188 O TYR A 41 8957 11066 9350 -178 1926 -587 O
ATOM 189 CB TYR A 41 -36.624 20.800 -0.539 1.00 79.51 C
ANISOU 189 CB TYR A 41 9420 11286 9504 -18 1872 -620 C
ATOM 190 CG TYR A 41 -36.269 19.451 0.050 1.00 71.36 C
ANISOU 190 CG TYR A 41 8486 10232 8396 -25 1933 -624 C
ATOM 191 CD1 TYR A 41 -37.255 18.594 0.522 1.00 68.26 C
ANISOU 191 CD1 TYR A 41 8099 9821 8015 -50 2048 -618 C
ATOM 192 CD2 TYR A 41 -34.948 19.031 0.123 1.00 72.37 C
ANISOU 192 CD2 TYR A 41 8703 10357 8437 -8 1876 -641 C
ATOM 193 CE1 TYR A 41 -36.937 17.360 1.050 1.00 72.20 C
ANISOU 193 CE1 TYR A 41 8708 10289 8436 -59 2103 -620 C
ATOM 194 CE2 TYR A 41 -34.620 17.799 0.653 1.00 73.45 C
ANISOU 194 CE2 TYR A 41 8944 10469 8494 -4 1922 -649 C
ATOM 195 CZ TYR A 41 -35.618 16.968 1.115 1.00 74.58 C
ANISOU 195 CZ TYR A 41 9109 10583 8646 -30 2035 -635 C
ATOM 196 OH TYR A 41 -35.298 15.739 1.644 1.00 80.92 O
ANISOU 196 OH TYR A 41 10036 11349 9360 -27 2081 -642 O
ATOM 197 N GLN A 42 -39.472 20.728 -1.990 1.00 85.05 N
ANISOU 197 N GLN A 42 9855 12047 10414 -105 1936 -604 N
ATOM 198 CA GLN A 42 -40.786 20.121 -2.183 1.00 86.67 C
ANISOU 198 CA GLN A 42 9967 12273 10691 -149 2013 -611 C
ATOM 199 C GLN A 42 -40.949 19.615 -3.609 1.00 86.60 C
ANISOU 199 C GLN A 42 9868 12301 10736 -214 1948 -601 C
ATOM 200 O GLN A 42 -41.493 18.527 -3.834 1.00 85.89 O
ANISOU 200 O GLN A 42 9744 12219 10670 -274 2002 -601 O
ATOM 201 CB GLN A 42 -41.888 21.126 -1.850 1.00 77.56 C
ANISOU 201 CB GLN A 42 8735 11132 9604 -103 2046 -634 C
ATOM 202 CG GLN A 42 -41.744 21.786 -0.495 1.00 75.19 C
ANISOU 202 CG GLN A 42 8520 10798 9252 -26 2097 -645 C
ATOM 203 CD GLN A 42 -42.884 22.734 -0.182 1.00 89.02 C
ANISOU 203 CD GLN A 42 10189 12569 11066 25 2128 -674 C
ATOM 204 OE1 GLN A 42 -42.671 23.921 0.066 1.00 88.77 O
ANISOU 204 OE1 GLN A 42 10180 12524 11025 97 2071 -681 O
ATOM 205 NE2 GLN A 42 -44.105 22.212 -0.186 1.00 89.59 N
ANISOU 205 NE2 GLN A 42 10166 12674 11202 -11 2216 -695 N
ATOM 206 N SER A 43 -40.477 20.390 -4.587 1.00 84.65 N
ANISOU 206 N SER A 43 9588 12071 10504 -203 1832 -592 N
ATOM 207 CA SER A 43 -40.606 19.985 -5.981 1.00 86.68 C
ANISOU 207 CA SER A 43 9766 12361 10806 -254 1762 -582 C
ATOM 208 C SER A 43 -39.660 18.837 -6.315 1.00 93.43 C
ANISOU 208 C SER A 43 10683 13218 11600 -300 1742 -564 C
ATOM 209 O SER A 43 -40.010 17.945 -7.096 1.00 98.34 O
ANISOU 209 O SER A 43 11253 13860 12254 -352 1734 -559 O
ATOM 210 CB SER A 43 -40.349 21.182 -6.895 1.00 81.78 C
ANISOU 210 CB SER A 43 9113 11752 10209 -226 1649 -576 C
ATOM 211 OG SER A 43 -40.536 20.836 -8.255 1.00 93.69 O
ANISOU 211 OG SER A 43 10548 13290 11760 -266 1582 -568 O
ATOM 212 N SER A 44 -38.460 18.840 -5.732 1.00 93.09 N
ANISOU 212 N SER A 44 10750 13156 11466 -276 1727 -559 N
ATOM 213 CA SER A 44 -37.505 17.772 -6.009 1.00 82.88 C
ANISOU 213 CA SER A 44 9520 11869 10104 -307 1699 -551 C
ATOM 214 C SER A 44 -37.930 16.463 -5.354 1.00 93.50 C
ANISOU 214 C SER A 44 10913 13189 11425 -334 1795 -554 C
ATOM 215 O SER A 44 -37.751 15.386 -5.935 1.00 90.22 O
ANISOU 215 O SER A 44 10505 12783 10992 -378 1778 -547 O
ATOM 216 CB SER A 44 -36.108 18.179 -5.541 1.00 83.22 C
ANISOU 216 CB SER A 44 9660 11905 10057 -266 1652 -559 C
ATOM 217 OG SER A 44 -35.646 19.317 -6.247 1.00 77.02 O
ANISOU 217 OG SER A 44 8836 11139 9289 -258 1564 -554 O
ATOM 218 N LEU A 45 -38.490 16.533 -4.144 1.00 93.72 N
ANISOU 218 N LEU A 45 10982 13181 11446 -310 1899 -565 N
ATOM 219 CA LEU A 45 -38.950 15.318 -3.479 1.00 85.04 C
ANISOU 219 CA LEU A 45 9942 12050 10321 -344 2003 -566 C
ATOM 220 C LEU A 45 -40.163 14.730 -4.190 1.00 87.48 C
ANISOU 220 C LEU A 45 10137 12378 10723 -417 2040 -565 C
ATOM 221 O LEU A 45 -40.263 13.508 -4.351 1.00 91.73 O
ANISOU 221 O LEU A 45 10707 12902 11244 -472 2071 -560 O
ATOM 222 CB LEU A 45 -39.270 15.608 -2.013 1.00 93.49 C
ANISOU 222 CB LEU A 45 11086 13077 11358 -299 2111 -577 C
ATOM 223 CG LEU A 45 -39.619 14.398 -1.142 1.00 90.02 C
ANISOU 223 CG LEU A 45 10745 12591 10869 -330 2231 -576 C
ATOM 224 CD1 LEU A 45 -38.472 13.398 -1.132 1.00 77.82 C
ANISOU 224 CD1 LEU A 45 9334 11019 9216 -326 2188 -573 C
ATOM 225 CD2 LEU A 45 -39.970 14.832 0.275 1.00 99.24 C
ANISOU 225 CD2 LEU A 45 11983 13720 12005 -278 2337 -587 C
ATOM 226 N ALA A 46 -41.094 15.584 -4.625 1.00 91.16 N
ANISOU 226 N ALA A 46 10473 12877 11288 -414 2032 -576 N
ATOM 227 CA ALA A 46 -42.244 15.101 -5.380 1.00 94.00 C
ANISOU 227 CA ALA A 46 10707 13263 11745 -477 2054 -588 C
ATOM 228 C ALA A 46 -41.825 14.527 -6.726 1.00 89.46 C
ANISOU 228 C ALA A 46 10098 12713 11181 -514 1950 -574 C
ATOM 229 O ALA A 46 -42.451 13.581 -7.218 1.00 98.27 O
ANISOU 229 O ALA A 46 11163 13834 12340 -578 1973 -580 O
ATOM 230 CB ALA A 46 -43.259 16.226 -5.576 1.00 91.95 C
ANISOU 230 CB ALA A 46 10318 13038 11582 -446 2050 -614 C
ATOM 231 N SER A 47 -40.776 15.084 -7.334 1.00 90.48 N
ANISOU 231 N SER A 47 10253 12857 11269 -478 1838 -559 N
ATOM 232 CA SER A 47 -40.264 14.529 -8.581 1.00 96.34 C
ANISOU 232 CA SER A 47 10974 13625 12005 -506 1741 -545 C
ATOM 233 C SER A 47 -39.544 13.207 -8.346 1.00 95.64 C
ANISOU 233 C SER A 47 10993 13514 11831 -535 1756 -535 C
ATOM 234 O SER A 47 -39.578 12.321 -9.208 1.00 91.45 O
ANISOU 234 O SER A 47 10438 12996 11311 -577 1715 -530 O
ATOM 235 CB SER A 47 -39.331 15.535 -9.255 1.00 86.13 C
ANISOU 235 CB SER A 47 9683 12357 10687 -465 1629 -532 C
ATOM 236 OG SER A 47 -38.754 14.994 -10.429 1.00 81.31 O
ANISOU 236 OG SER A 47 9058 11774 10060 -489 1540 -519 O
ATOM 237 N TRP A 48 -38.892 13.055 -7.192 1.00102.53 N
ANISOU 237 N TRP A 48 11992 14351 12614 -505 1807 -537 N
ATOM 238 CA TRP A 48 -38.229 11.795 -6.873 1.00 99.47 C
ANISOU 238 CA TRP A 48 11726 13935 12134 -519 1820 -534 C
ATOM 239 C TRP A 48 -39.242 10.678 -6.658 1.00104.02 C
ANISOU 239 C TRP A 48 12304 14477 12741 -588 1914 -535 C
ATOM 240 O TRP A 48 -39.053 9.559 -7.150 1.00103.81 O
ANISOU 240 O TRP A 48 12314 14442 12686 -626 1888 -530 O
ATOM 241 CB TRP A 48 -37.349 11.961 -5.633 1.00 95.47 C
ANISOU 241 CB TRP A 48 11359 13393 11522 -459 1852 -544 C
ATOM 242 CG TRP A 48 -36.836 10.664 -5.078 1.00 88.80 C
ANISOU 242 CG TRP A 48 10661 12505 10574 -462 1882 -548 C
ATOM 243 CD1 TRP A 48 -37.460 9.854 -4.173 1.00 95.07 C
ANISOU 243 CD1 TRP A 48 11540 13239 11344 -488 1997 -548 C
ATOM 244 CD2 TRP A 48 -35.591 10.028 -5.393 1.00 84.65 C
ANISOU 244 CD2 TRP A 48 10223 11992 9949 -434 1794 -558 C
ATOM 245 NE1 TRP A 48 -36.682 8.753 -3.907 1.00104.57 N
ANISOU 245 NE1 TRP A 48 12890 14406 12434 -476 1982 -554 N
ATOM 246 CE2 TRP A 48 -35.530 8.836 -4.643 1.00 90.15 C
ANISOU 246 CE2 TRP A 48 11064 12628 10561 -437 1854 -564 C
ATOM 247 CE3 TRP A 48 -34.522 10.350 -6.236 1.00 80.43 C
ANISOU 247 CE3 TRP A 48 9659 11514 9385 -406 1672 -566 C
ATOM 248 CZ2 TRP A 48 -34.443 7.967 -4.711 1.00 92.09 C
ANISOU 248 CZ2 TRP A 48 11428 12870 10693 -402 1786 -582 C
ATOM 249 CZ3 TRP A 48 -33.444 9.485 -6.301 1.00 74.17 C
ANISOU 249 CZ3 TRP A 48 8969 10729 8484 -377 1611 -586 C
ATOM 250 CH2 TRP A 48 -33.413 8.308 -5.543 1.00 82.03 C
ANISOU 250 CH2 TRP A 48 10108 11663 9395 -369 1663 -596 C
ATOM 251 N ASN A 49 -40.322 10.961 -5.926 1.00101.32 N
ANISOU 251 N ASN A 49 11922 14116 12458 -606 2025 -544 N
ATOM 252 CA ASN A 49 -41.305 9.928 -5.618 1.00107.31 C
ANISOU 252 CA ASN A 49 12684 14842 13247 -683 2132 -548 C
ATOM 253 C ASN A 49 -42.027 9.426 -6.860 1.00111.76 C
ANISOU 253 C ASN A 49 13120 15438 13906 -750 2089 -554 C
ATOM 254 O ASN A 49 -42.590 8.326 -6.833 1.00116.63 O
ANISOU 254 O ASN A 49 13754 16025 14534 -825 2151 -557 O
ATOM 255 CB ASN A 49 -42.317 10.450 -4.599 1.00 98.68 C
ANISOU 255 CB ASN A 49 11557 13736 12200 -687 2263 -564 C
ATOM 256 CG ASN A 49 -41.694 10.719 -3.246 1.00 99.46 C
ANISOU 256 CG ASN A 49 11805 13789 12197 -624 2323 -559 C
ATOM 257 OD1 ASN A 49 -40.716 10.078 -2.861 1.00 97.71 O
ANISOU 257 OD1 ASN A 49 11735 13527 11863 -600 2305 -549 O
ATOM 258 ND2 ASN A 49 -42.258 11.673 -2.514 1.00111.33 N
ANISOU 258 ND2 ASN A 49 13266 15300 13735 -588 2388 -572 N
ATOM 259 N TYR A 50 -42.026 10.201 -7.946 1.00104.83 N
ANISOU 259 N TYR A 50 12121 14615 13093 -725 1983 -557 N
ATOM 260 CA TYR A 50 -42.615 9.720 -9.190 1.00109.00 C
ANISOU 260 CA TYR A 50 12537 15174 13704 -774 1925 -565 C
ATOM 261 C TYR A 50 -41.638 8.846 -9.967 1.00105.85 C
ANISOU 261 C TYR A 50 12209 14774 13235 -779 1828 -546 C
ATOM 262 O TYR A 50 -41.999 7.757 -10.424 1.00111.53 O
ANISOU 262 O TYR A 50 12923 15480 13973 -839 1829 -548 O
ATOM 263 CB TYR A 50 -43.073 10.893 -10.055 1.00102.65 C
ANISOU 263 CB TYR A 50 11586 14424 12992 -737 1850 -580 C
ATOM 264 CG TYR A 50 -43.305 10.497 -11.494 1.00107.16 C
ANISOU 264 CG TYR A 50 12066 15027 13624 -761 1752 -585 C
ATOM 265 CD1 TYR A 50 -44.362 9.667 -11.842 1.00111.36 C
ANISOU 265 CD1 TYR A 50 12514 15559 14238 -831 1790 -611 C
ATOM 266 CD2 TYR A 50 -42.460 10.940 -12.503 1.00101.89 C
ANISOU 266 CD2 TYR A 50 11395 14389 12928 -716 1622 -566 C
ATOM 267 CE1 TYR A 50 -44.574 9.294 -13.153 1.00109.46 C
ANISOU 267 CE1 TYR A 50 12193 15345 14051 -845 1693 -620 C
ATOM 268 CE2 TYR A 50 -42.666 10.574 -13.819 1.00 91.38 C
ANISOU 268 CE2 TYR A 50 9989 13086 11646 -729 1532 -570 C
ATOM 269 CZ TYR A 50 -43.726 9.750 -14.138 1.00 95.26 C
ANISOU 269 CZ TYR A 50 10400 13575 12220 -789 1563 -598 C
ATOM 270 OH TYR A 50 -43.941 9.379 -15.445 1.00 93.90 O
ANISOU 270 OH TYR A 50 10153 13427 12096 -796 1467 -606 O
ATOM 271 N ASN A 51 -40.398 9.311 -10.131 1.00102.69 N
ANISOU 271 N ASN A 51 11871 14391 12754 -716 1742 -530 N
ATOM 272 CA ASN A 51 -39.418 8.553 -10.902 1.00 92.95 C
ANISOU 272 CA ASN A 51 10696 13170 11449 -710 1643 -518 C
ATOM 273 C ASN A 51 -39.010 7.256 -10.217 1.00 96.42 C
ANISOU 273 C ASN A 51 11284 13557 11793 -731 1688 -516 C
ATOM 274 O ASN A 51 -38.406 6.396 -10.865 1.00 84.75 O
ANISOU 274 O ASN A 51 9853 12086 10262 -734 1613 -512 O
ATOM 275 CB ASN A 51 -38.182 9.411 -11.172 1.00 91.46 C
ANISOU 275 CB ASN A 51 10533 13020 11198 -643 1552 -510 C
ATOM 276 CG ASN A 51 -38.467 10.554 -12.126 1.00 95.43 C
ANISOU 276 CG ASN A 51 10908 13569 11781 -626 1484 -507 C
ATOM 277 OD1 ASN A 51 -38.237 10.444 -13.331 1.00 93.39 O
ANISOU 277 OD1 ASN A 51 10599 13348 11537 -628 1390 -500 O
ATOM 278 ND2 ASN A 51 -38.975 11.658 -11.593 1.00106.44 N
ANISOU 278 ND2 ASN A 51 12260 14959 13225 -604 1529 -513 N
ATOM 279 N THR A 52 -39.319 7.097 -8.931 1.00104.56 N
ANISOU 279 N THR A 52 12400 14535 12794 -741 1806 -520 N
ATOM 280 CA THR A 52 -39.083 5.847 -8.223 1.00102.13 C
ANISOU 280 CA THR A 52 12250 14161 12392 -764 1861 -519 C
ATOM 281 C THR A 52 -40.360 5.053 -7.985 1.00113.06 C
ANISOU 281 C THR A 52 13614 15501 13843 -859 1972 -522 C
ATOM 282 O THR A 52 -40.280 3.887 -7.583 1.00118.66 O
ANISOU 282 O THR A 52 14455 16148 14482 -896 2013 -518 O
ATOM 283 CB THR A 52 -38.397 6.116 -6.878 1.00108.51 C
ANISOU 283 CB THR A 52 13203 14930 13096 -703 1917 -523 C
ATOM 284 OG1 THR A 52 -39.209 7.003 -6.096 1.00108.50 O
ANISOU 284 OG1 THR A 52 13146 14922 13158 -705 2019 -526 O
ATOM 285 CG2 THR A 52 -37.033 6.747 -7.095 1.00 80.12 C
ANISOU 285 CG2 THR A 52 9636 11379 9427 -616 1806 -530 C
ATOM 286 N ASN A 53 -41.530 5.655 -8.226 1.00118.83 N
ANISOU 286 N ASN A 53 14185 16260 14704 -900 2018 -533 N
ATOM 287 CA ASN A 53 -42.821 5.010 -7.997 1.00120.27 C
ANISOU 287 CA ASN A 53 14320 16412 14965 -998 2132 -547 C
ATOM 288 C ASN A 53 -43.810 5.627 -8.990 1.00114.86 C
ANISOU 288 C ASN A 53 13420 15791 14429 -1022 2095 -571 C
ATOM 289 O ASN A 53 -44.643 6.468 -8.649 1.00122.23 O
ANISOU 289 O ASN A 53 14247 16751 15443 -1021 2160 -592 O
ATOM 290 CB ASN A 53 -43.289 5.175 -6.551 1.00129.65 C
ANISOU 290 CB ASN A 53 15577 17554 16129 -1012 2288 -550 C
ATOM 291 CG ASN A 53 -44.247 4.087 -6.120 1.00133.35 C
ANISOU 291 CG ASN A 53 16078 17968 16621 -1125 2418 -557 C
ATOM 292 OD1 ASN A 53 -44.442 3.098 -6.826 1.00128.66 O
ANISOU 292 OD1 ASN A 53 15482 17358 16047 -1192 2385 -558 O
ATOM 293 ND2 ASN A 53 -44.849 4.261 -4.947 1.00134.85 N
ANISOU 293 ND2 ASN A 53 16304 18127 16808 -1150 2567 -563 N
ATOM 294 N ILE A 54 -43.704 5.200 -10.247 1.00103.07 N
ANISOU 294 N ILE A 54 11868 14326 12970 -1034 1984 -572 N
ATOM 295 CA ILE A 54 -44.528 5.745 -11.320 1.00102.30 C
ANISOU 295 CA ILE A 54 11579 14287 13003 -1040 1924 -598 C
ATOM 296 C ILE A 54 -45.986 5.366 -11.094 1.00102.34 C
ANISOU 296 C ILE A 54 11479 14285 13118 -1132 2035 -637 C
ATOM 297 O ILE A 54 -46.424 4.273 -11.468 1.00 96.27 O
ANISOU 297 O ILE A 54 10707 13493 12380 -1212 2046 -648 O
ATOM 298 CB ILE A 54 -44.040 5.262 -12.699 1.00 96.74 C
ANISOU 298 CB ILE A 54 10853 13608 12298 -1028 1780 -590 C
ATOM 299 CG1 ILE A 54 -42.583 5.673 -12.921 1.00 92.81 C
ANISOU 299 CG1 ILE A 54 10446 13128 11690 -942 1678 -558 C
ATOM 300 CG2 ILE A 54 -44.920 5.823 -13.805 1.00 89.34 C
ANISOU 300 CG2 ILE A 54 9728 12726 11492 -1024 1715 -622 C
ATOM 301 CD1 ILE A 54 -42.045 5.285 -14.276 1.00 78.01 C
ANISOU 301 CD1 ILE A 54 8549 11286 9805 -922 1537 -550 C
ATOM 302 N THR A 55 -46.738 6.262 -10.466 1.00108.90 N
ANISOU 302 N THR A 55 12226 15141 14011 -1122 2118 -663 N
ATOM 303 CA THR A 55 -48.172 6.114 -10.262 1.00110.01 C
ANISOU 303 CA THR A 55 12236 15296 14268 -1200 2224 -714 C
ATOM 304 C THR A 55 -48.884 7.323 -10.859 1.00112.65 C
ANISOU 304 C THR A 55 12385 15705 14712 -1143 2170 -758 C
ATOM 305 O THR A 55 -48.256 8.253 -11.369 1.00106.73 O
ANISOU 305 O THR A 55 11628 14984 13941 -1049 2059 -742 O
ATOM 306 CB THR A 55 -48.512 5.968 -8.774 1.00105.80 C
ANISOU 306 CB THR A 55 11783 14721 13694 -1244 2398 -713 C
ATOM 307 OG1 THR A 55 -48.341 7.230 -8.118 1.00121.08 O
ANISOU 307 OG1 THR A 55 13713 16682 15611 -1156 2415 -711 O
ATOM 308 CG2 THR A 55 -47.611 4.934 -8.113 1.00103.08 C
ANISOU 308 CG2 THR A 55 11659 14294 13213 -1271 2436 -665 C
ATOM 309 N GLU A 56 -50.215 7.307 -10.791 1.00133.30 N
ANISOU 309 N GLU A 56 14852 18352 17443 -1201 2249 -819 N
ATOM 310 CA GLU A 56 -50.979 8.461 -11.248 1.00130.84 C
ANISOU 310 CA GLU A 56 14368 18112 17231 -1137 2202 -874 C
ATOM 311 C GLU A 56 -51.033 9.544 -10.178 1.00130.03 C
ANISOU 311 C GLU A 56 14282 18022 17101 -1075 2277 -876 C
ATOM 312 O GLU A 56 -50.995 10.738 -10.495 1.00123.11 O
ANISOU 312 O GLU A 56 13348 17184 16243 -978 2197 -888 O
ATOM 313 CB GLU A 56 -52.390 8.034 -11.654 1.00140.10 C
ANISOU 313 CB GLU A 56 15362 19327 18544 -1214 2246 -955 C
ATOM 314 CG GLU A 56 -52.825 8.565 -13.010 1.00128.20 C
ANISOU 314 CG GLU A 56 13700 17878 17131 -1152 2100 -1004 C
ATOM 315 CD GLU A 56 -52.774 10.078 -13.088 1.00129.15 C
ANISOU 315 CD GLU A 56 13776 18040 17254 -1026 2033 -1016 C
ATOM 316 OE1 GLU A 56 -53.272 10.741 -12.155 1.00141.70 O
ANISOU 316 OE1 GLU A 56 15332 19651 18855 -1008 2128 -1043 O
ATOM 317 OE2 GLU A 56 -52.227 10.604 -14.080 1.00121.15 O
ANISOU 317 OE2 GLU A 56 12769 17036 16227 -945 1886 -997 O
ATOM 318 N GLU A 57 -51.111 9.144 -8.906 1.00139.25 N
ANISOU 318 N GLU A 57 15538 19151 18218 -1128 2428 -862 N
ATOM 319 CA GLU A 57 -51.101 10.115 -7.818 1.00137.25 C
ANISOU 319 CA GLU A 57 15317 18905 17928 -1064 2501 -860 C
ATOM 320 C GLU A 57 -49.773 10.858 -7.744 1.00136.01 C
ANISOU 320 C GLU A 57 15291 18723 17665 -961 2405 -802 C
ATOM 321 O GLU A 57 -49.745 12.042 -7.388 1.00145.90 O
ANISOU 321 O GLU A 57 16524 19998 18913 -875 2390 -810 O
ATOM 322 CB GLU A 57 -51.393 9.416 -6.490 1.00136.24 C
ANISOU 322 CB GLU A 57 15279 18732 17755 -1144 2685 -854 C
ATOM 323 CG GLU A 57 -51.535 10.353 -5.302 1.00140.24 C
ANISOU 323 CG GLU A 57 15810 19248 18228 -1081 2775 -859 C
ATOM 324 CD GLU A 57 -51.663 9.610 -3.986 1.00152.03 C
ANISOU 324 CD GLU A 57 17426 20685 19654 -1153 2954 -842 C
ATOM 325 OE1 GLU A 57 -51.337 8.405 -3.948 1.00159.99 O
ANISOU 325 OE1 GLU A 57 18548 21631 20612 -1237 2991 -810 O
ATOM 326 OE2 GLU A 57 -52.091 10.230 -2.990 1.00160.65 O
ANISOU 326 OE2 GLU A 57 18509 21792 20738 -1122 3058 -860 O
ATOM 327 N ASN A 58 -48.668 10.188 -8.075 1.00128.44 N
ANISOU 327 N ASN A 58 14462 17720 16621 -968 2338 -750 N
ATOM 328 CA ASN A 58 -47.365 10.839 -8.050 1.00115.40 C
ANISOU 328 CA ASN A 58 12925 16052 14872 -878 2246 -703 C
ATOM 329 C ASN A 58 -47.165 11.791 -9.221 1.00109.29 C
ANISOU 329 C ASN A 58 12061 15324 14140 -808 2096 -709 C
ATOM 330 O ASN A 58 -46.361 12.722 -9.114 1.00108.02 O
ANISOU 330 O ASN A 58 11956 15162 13923 -730 2035 -685 O
ATOM 331 CB ASN A 58 -46.250 9.791 -8.033 1.00108.21 C
ANISOU 331 CB ASN A 58 12175 15087 13851 -904 2221 -656 C
ATOM 332 CG ASN A 58 -46.211 9.008 -6.735 1.00112.91 C
ANISOU 332 CG ASN A 58 12909 15620 14370 -949 2362 -643 C
ATOM 333 OD1 ASN A 58 -46.613 9.508 -5.684 1.00116.12 O
ANISOU 333 OD1 ASN A 58 13327 16020 14772 -933 2467 -654 O
ATOM 334 ND2 ASN A 58 -45.726 7.774 -6.802 1.00114.47 N
ANISOU 334 ND2 ASN A 58 13222 15770 14502 -1001 2363 -620 N
ATOM 335 N VAL A 59 -47.873 11.580 -10.333 1.00120.27 N
ANISOU 335 N VAL A 59 13319 16751 15626 -833 2035 -742 N
ATOM 336 CA VAL A 59 -47.806 12.528 -11.441 1.00121.03 C
ANISOU 336 CA VAL A 59 13336 16888 15763 -761 1897 -751 C
ATOM 337 C VAL A 59 -48.429 13.858 -11.039 1.00123.39 C
ANISOU 337 C VAL A 59 13561 17216 16106 -690 1912 -787 C
ATOM 338 O VAL A 59 -47.866 14.928 -11.301 1.00117.18 O
ANISOU 338 O VAL A 59 12804 16433 15288 -611 1826 -769 O
ATOM 339 CB VAL A 59 -48.484 11.942 -12.693 1.00107.40 C
ANISOU 339 CB VAL A 59 11489 15190 14127 -797 1828 -786 C
ATOM 340 CG1 VAL A 59 -48.626 13.006 -13.769 1.00111.29 C
ANISOU 340 CG1 VAL A 59 11897 15721 14668 -713 1697 -806 C
ATOM 341 CG2 VAL A 59 -47.693 10.764 -13.221 1.00 95.68 C
ANISOU 341 CG2 VAL A 59 10091 13676 12586 -846 1783 -746 C
ATOM 342 N GLN A 60 -49.595 13.815 -10.390 1.00123.37 N
ANISOU 342 N GLN A 60 13466 17235 16173 -720 2022 -840 N
ATOM 343 CA GLN A 60 -50.259 15.048 -9.983 1.00122.69 C
ANISOU 343 CA GLN A 60 13305 17183 16127 -646 2035 -883 C
ATOM 344 C GLN A 60 -49.471 15.768 -8.897 1.00121.39 C
ANISOU 344 C GLN A 60 13270 16984 15867 -591 2072 -842 C
ATOM 345 O GLN A 60 -49.306 16.992 -8.953 1.00123.24 O
ANISOU 345 O GLN A 60 13506 17228 16092 -502 2004 -845 O
ATOM 346 CB GLN A 60 -51.680 14.745 -9.508 1.00145.47 C
ANISOU 346 CB GLN A 60 16054 20110 19108 -696 2154 -957 C
ATOM 347 CG GLN A 60 -52.540 13.993 -10.518 1.00145.49 C
ANISOU 347 CG GLN A 60 15916 20149 19215 -757 2124 -1011 C
ATOM 348 CD GLN A 60 -53.097 14.885 -11.617 1.00151.01 C
ANISOU 348 CD GLN A 60 16486 20900 19992 -672 1992 -1068 C
ATOM 349 OE1 GLN A 60 -52.435 15.814 -12.082 1.00141.37 O
ANISOU 349 OE1 GLN A 60 15321 19668 18726 -581 1878 -1038 O
ATOM 350 NE2 GLN A 60 -54.326 14.605 -12.034 1.00151.84 N
ANISOU 350 NE2 GLN A 60 16421 21060 20212 -701 2008 -1156 N
ATOM 351 N ASN A 61 -48.975 15.028 -7.902 1.00119.59 N
ANISOU 351 N ASN A 61 13162 16713 15565 -640 2175 -806 N
ATOM 352 CA ASN A 61 -48.180 15.650 -6.848 1.00111.42 C
ANISOU 352 CA ASN A 61 12257 15642 14435 -582 2205 -771 C
ATOM 353 C ASN A 61 -46.890 16.240 -7.399 1.00108.63 C
ANISOU 353 C ASN A 61 11992 15270 14012 -524 2073 -725 C
ATOM 354 O ASN A 61 -46.401 17.252 -6.885 1.00107.43 O
ANISOU 354 O ASN A 61 11898 15105 13814 -452 2051 -714 O
ATOM 355 CB ASN A 61 -47.876 14.635 -5.747 1.00 99.68 C
ANISOU 355 CB ASN A 61 10893 14106 12874 -641 2334 -744 C
ATOM 356 CG ASN A 61 -49.121 14.179 -5.015 1.00107.83 C
ANISOU 356 CG ASN A 61 11853 15154 13963 -703 2487 -788 C
ATOM 357 OD1 ASN A 61 -50.088 14.930 -4.883 1.00116.22 O
ANISOU 357 OD1 ASN A 61 12793 16266 15100 -671 2516 -839 O
ATOM 358 ND2 ASN A 61 -49.104 12.942 -4.533 1.00115.41 N
ANISOU 358 ND2 ASN A 61 12892 16071 14886 -791 2588 -771 N
ATOM 359 N MET A 62 -46.325 15.626 -8.441 1.00107.13 N
ANISOU 359 N MET A 62 11813 15078 13812 -556 1984 -701 N
ATOM 360 CA MET A 62 -45.153 16.204 -9.089 1.00 99.40 C
ANISOU 360 CA MET A 62 10901 14093 12775 -508 1860 -664 C
ATOM 361 C MET A 62 -45.522 17.461 -9.867 1.00 99.67 C
ANISOU 361 C MET A 62 10850 14155 12865 -444 1764 -684 C
ATOM 362 O MET A 62 -44.750 18.426 -9.901 1.00103.82 O
ANISOU 362 O MET A 62 11437 14667 13341 -388 1697 -662 O
ATOM 363 CB MET A 62 -44.501 15.173 -10.009 1.00 95.92 C
ANISOU 363 CB MET A 62 10489 13650 12307 -557 1795 -637 C
ATOM 364 CG MET A 62 -43.284 15.684 -10.760 1.00 95.25 C
ANISOU 364 CG MET A 62 10462 13567 12160 -519 1673 -603 C
ATOM 365 SD MET A 62 -42.624 14.465 -11.913 1.00 86.89 S
ANISOU 365 SD MET A 62 9423 12519 11074 -568 1594 -579 S
ATOM 366 CE MET A 62 -41.263 15.382 -12.628 1.00 73.39 C
ANISOU 366 CE MET A 62 7771 10822 9293 -518 1470 -547 C
ATOM 367 N ASN A 63 -46.701 17.470 -10.493 1.00108.18 N
ANISOU 367 N ASN A 63 11791 15270 14043 -448 1754 -732 N
ATOM 368 CA ASN A 63 -47.135 18.653 -11.228 1.00108.00 C
ANISOU 368 CA ASN A 63 11697 15269 14068 -375 1658 -760 C
ATOM 369 C ASN A 63 -47.528 19.779 -10.281 1.00111.14 C
ANISOU 369 C ASN A 63 12097 15666 14465 -307 1700 -784 C
ATOM 370 O ASN A 63 -47.192 20.944 -10.524 1.00109.50 O
ANISOU 370 O ASN A 63 11924 15447 14235 -236 1617 -776 O
ATOM 371 CB ASN A 63 -48.297 18.300 -12.156 1.00117.58 C
ANISOU 371 CB ASN A 63 12762 16525 15388 -389 1629 -816 C
ATOM 372 CG ASN A 63 -47.888 17.357 -13.271 1.00109.64 C
ANISOU 372 CG ASN A 63 11756 15520 14383 -438 1560 -793 C
ATOM 373 OD1 ASN A 63 -46.752 17.393 -13.744 1.00 76.48 O
ANISOU 373 OD1 ASN A 63 7650 11298 10110 -433 1488 -739 O
ATOM 374 ND2 ASN A 63 -48.814 16.505 -13.696 1.00117.12 N
ANISOU 374 ND2 ASN A 63 12594 16494 15413 -488 1582 -837 N
ATOM 375 N ASN A 64 -48.237 19.454 -9.198 1.00114.60 N
ANISOU 375 N ASN A 64 12504 16114 14924 -328 1828 -814 N
ATOM 376 CA ASN A 64 -48.636 20.479 -8.238 1.00114.45 C
ANISOU 376 CA ASN A 64 12487 16098 14901 -257 1872 -840 C
ATOM 377 C ASN A 64 -47.418 21.127 -7.591 1.00115.00 C
ANISOU 377 C ASN A 64 12707 16118 14869 -216 1851 -787 C
ATOM 378 O ASN A 64 -47.341 22.356 -7.475 1.00112.37 O
ANISOU 378 O ASN A 64 12396 15776 14523 -136 1795 -793 O
ATOM 379 CB ASN A 64 -49.554 19.877 -7.173 1.00120.30 C
ANISOU 379 CB ASN A 64 13175 16860 15674 -298 2028 -877 C
ATOM 380 CG ASN A 64 -50.857 19.362 -7.751 1.00119.63 C
ANISOU 380 CG ASN A 64 12921 16832 15700 -339 2054 -945 C
ATOM 381 OD1 ASN A 64 -51.270 19.765 -8.838 1.00108.25 O
ANISOU 381 OD1 ASN A 64 11390 15421 14318 -303 1947 -980 O
ATOM 382 ND2 ASN A 64 -51.514 18.467 -7.021 1.00120.72 N
ANISOU 382 ND2 ASN A 64 13020 16984 15864 -415 2196 -969 N
ATOM 383 N ALA A 65 -46.451 20.312 -7.165 1.00119.82 N
ANISOU 383 N ALA A 65 13426 16694 15407 -266 1890 -739 N
ATOM 384 CA ALA A 65 -45.239 20.858 -6.565 1.00122.87 C
ANISOU 384 CA ALA A 65 13949 17037 15698 -228 1866 -699 C
ATOM 385 C ALA A 65 -44.391 21.588 -7.599 1.00105.37 C
ANISOU 385 C ALA A 65 11764 14814 13460 -203 1726 -672 C
ATOM 386 O ALA A 65 -43.744 22.593 -7.283 1.00104.13 O
ANISOU 386 O ALA A 65 11679 14630 13255 -151 1681 -659 O
ATOM 387 CB ALA A 65 -44.433 19.744 -5.898 1.00117.68 C
ANISOU 387 CB ALA A 65 13399 16350 14965 -280 1935 -667 C
ATOM 388 N GLY A 66 -44.384 21.098 -8.840 1.00100.81 N
ANISOU 388 N GLY A 66 11134 14255 12912 -242 1656 -666 N
ATOM 389 CA GLY A 66 -43.621 21.768 -9.880 1.00 95.45 C
ANISOU 389 CA GLY A 66 10487 13571 12210 -223 1531 -640 C
ATOM 390 C GLY A 66 -44.241 23.085 -10.303 1.00105.61 C
ANISOU 390 C GLY A 66 11731 14858 13538 -153 1461 -665 C
ATOM 391 O GLY A 66 -43.530 24.037 -10.637 1.00102.22 O
ANISOU 391 O GLY A 66 11369 14404 13067 -122 1381 -642 O
ATOM 392 N ASP A 67 -45.574 23.161 -10.297 1.00108.59 N
ANISOU 392 N ASP A 67 11999 15266 13996 -126 1490 -718 N
ATOM 393 CA ASP A 67 -46.242 24.408 -10.657 1.00107.45 C
ANISOU 393 CA ASP A 67 11817 15123 13886 -44 1418 -754 C
ATOM 394 C ASP A 67 -46.025 25.477 -9.595 1.00103.57 C
ANISOU 394 C ASP A 67 11401 14601 13351 19 1438 -753 C
ATOM 395 O ASP A 67 -45.810 26.650 -9.923 1.00101.51 O
ANISOU 395 O ASP A 67 11191 14312 13068 78 1349 -749 O
ATOM 396 CB ASP A 67 -47.735 24.164 -10.877 1.00112.82 C
ANISOU 396 CB ASP A 67 12348 15853 14664 -26 1444 -825 C
ATOM 397 CG ASP A 67 -48.016 23.358 -12.130 1.00113.22 C
ANISOU 397 CG ASP A 67 12322 15930 14765 -68 1392 -834 C
ATOM 398 OD1 ASP A 67 -47.053 23.025 -12.852 1.00114.24 O
ANISOU 398 OD1 ASP A 67 12518 16039 14850 -106 1334 -782 O
ATOM 399 OD2 ASP A 67 -49.199 23.058 -12.392 1.00117.33 O
ANISOU 399 OD2 ASP A 67 12714 16495 15372 -62 1408 -899 O
ATOM 400 N LYS A 68 -46.082 25.094 -8.316 1.00101.36 N
ANISOU 400 N LYS A 68 11138 14320 13052 8 1552 -757 N
ATOM 401 CA LYS A 68 -45.828 26.055 -7.247 1.00 89.45 C
ANISOU 401 CA LYS A 68 9707 12780 11498 72 1570 -757 C
ATOM 402 C LYS A 68 -44.399 26.578 -7.293 1.00 88.44 C
ANISOU 402 C LYS A 68 9712 12602 11289 68 1504 -704 C
ATOM 403 O LYS A 68 -44.155 27.747 -6.974 1.00 82.41 O
ANISOU 403 O LYS A 68 9012 11805 10496 130 1456 -705 O
ATOM 404 CB LYS A 68 -46.117 25.420 -5.886 1.00 97.31 C
ANISOU 404 CB LYS A 68 10707 13784 12483 59 1711 -768 C
ATOM 405 CG LYS A 68 -47.580 25.074 -5.651 1.00104.71 C
ANISOU 405 CG LYS A 68 11511 14775 13500 63 1794 -829 C
ATOM 406 CD LYS A 68 -47.794 24.514 -4.253 1.00110.16 C
ANISOU 406 CD LYS A 68 12225 15465 14166 47 1942 -834 C
ATOM 407 CE LYS A 68 -49.260 24.204 -3.996 1.00113.36 C
ANISOU 407 CE LYS A 68 12490 15932 14651 42 2035 -900 C
ATOM 408 NZ LYS A 68 -49.485 23.687 -2.617 1.00107.88 N
ANISOU 408 NZ LYS A 68 11829 15234 13926 24 2190 -903 N
ATOM 409 N TRP A 69 -43.445 25.733 -7.690 1.00 90.74 N
ANISOU 409 N TRP A 69 10044 12889 11542 -4 1497 -664 N
ATOM 410 CA TRP A 69 -42.060 26.180 -7.799 1.00 90.42 C
ANISOU 410 CA TRP A 69 10115 12814 11428 -15 1434 -624 C
ATOM 411 C TRP A 69 -41.862 27.076 -9.015 1.00 94.72 C
ANISOU 411 C TRP A 69 10666 13345 11977 -4 1314 -612 C
ATOM 412 O TRP A 69 -41.088 28.039 -8.964 1.00 87.26 O
ANISOU 412 O TRP A 69 9808 12362 10985 13 1259 -594 O
ATOM 413 CB TRP A 69 -41.123 24.973 -7.857 1.00 88.53 C
ANISOU 413 CB TRP A 69 9910 12583 11143 -88 1462 -596 C
ATOM 414 CG TRP A 69 -39.740 25.304 -8.330 1.00 85.05 C
ANISOU 414 CG TRP A 69 9551 12126 10638 -113 1385 -564 C
ATOM 415 CD1 TRP A 69 -39.154 24.901 -9.494 1.00 87.13 C
ANISOU 415 CD1 TRP A 69 9806 12410 10890 -164 1321 -541 C
ATOM 416 CD2 TRP A 69 -38.771 26.115 -7.653 1.00 91.20 C
ANISOU 416 CD2 TRP A 69 10426 12870 11355 -90 1366 -558 C
ATOM 417 NE1 TRP A 69 -37.879 25.405 -9.582 1.00 86.54 N
ANISOU 417 NE1 TRP A 69 9811 12319 10750 -180 1271 -522 N
ATOM 418 CE2 TRP A 69 -37.620 26.155 -8.465 1.00 90.20 C
ANISOU 418 CE2 TRP A 69 10339 12749 11186 -138 1295 -534 C
ATOM 419 CE3 TRP A 69 -38.764 26.810 -6.440 1.00 93.71 C
ANISOU 419 CE3 TRP A 69 10799 13155 11652 -34 1402 -574 C
ATOM 420 CZ2 TRP A 69 -36.474 26.861 -8.103 1.00 82.47 C
ANISOU 420 CZ2 TRP A 69 9444 11744 10147 -139 1262 -530 C
ATOM 421 CZ3 TRP A 69 -37.626 27.510 -6.082 1.00 87.59 C
ANISOU 421 CZ3 TRP A 69 10114 12349 10817 -28 1361 -568 C
ATOM 422 CH2 TRP A 69 -36.497 27.531 -6.911 1.00 76.56 C
ANISOU 422 CH2 TRP A 69 8747 10960 9383 -84 1293 -548 C
ATOM 423 N SER A 70 -42.551 26.774 -10.118 1.00104.02 N
ANISOU 423 N SER A 70 11763 14551 13210 -14 1274 -623 N
ATOM 424 CA SER A 70 -42.442 27.612 -11.307 1.00 94.77 C
ANISOU 424 CA SER A 70 10610 13362 12038 4 1160 -612 C
ATOM 425 C SER A 70 -43.113 28.962 -11.094 1.00 99.36 C
ANISOU 425 C SER A 70 11207 13912 12632 92 1117 -642 C
ATOM 426 O SER A 70 -42.629 29.988 -11.587 1.00 99.83 O
ANISOU 426 O SER A 70 11348 13928 12654 112 1033 -623 O
ATOM 427 CB SER A 70 -43.048 26.894 -12.512 1.00 88.44 C
ANISOU 427 CB SER A 70 9718 12596 11289 -17 1125 -622 C
ATOM 428 OG SER A 70 -42.404 25.654 -12.745 1.00101.82 O
ANISOU 428 OG SER A 70 11407 14316 12966 -94 1156 -595 O
ATOM 429 N ALA A 71 -44.229 28.982 -10.361 1.00108.47 N
ANISOU 429 N ALA A 71 12289 15090 13835 146 1174 -691 N
ATOM 430 CA ALA A 71 -44.913 30.243 -10.090 1.00108.80 C
ANISOU 430 CA ALA A 71 12344 15110 13885 242 1131 -728 C
ATOM 431 C ALA A 71 -44.109 31.111 -9.132 1.00100.28 C
ANISOU 431 C ALA A 71 11383 13978 12741 266 1134 -706 C
ATOM 432 O ALA A 71 -44.115 32.343 -9.248 1.00 95.63 O
ANISOU 432 O ALA A 71 10862 13344 12129 327 1056 -711 O
ATOM 433 CB ALA A 71 -46.309 29.973 -9.530 1.00112.24 C
ANISOU 433 CB ALA A 71 12658 15597 14390 292 1199 -795 C
ATOM 434 N PHE A 72 -43.413 30.488 -8.179 1.00100.31 N
ANISOU 434 N PHE A 72 11419 13983 12711 222 1217 -684 N
ATOM 435 CA PHE A 72 -42.589 31.247 -7.243 1.00 94.20 C
ANISOU 435 CA PHE A 72 10756 13160 11876 245 1218 -668 C
ATOM 436 C PHE A 72 -41.448 31.956 -7.962 1.00 94.42 C
ANISOU 436 C PHE A 72 10884 13139 11852 210 1124 -628 C
ATOM 437 O PHE A 72 -41.135 33.113 -7.656 1.00 88.86 O
ANISOU 437 O PHE A 72 10267 12382 11114 251 1073 -627 O
ATOM 438 CB PHE A 72 -42.053 30.318 -6.154 1.00 80.86 C
ANISOU 438 CB PHE A 72 9084 11482 10157 208 1322 -658 C
ATOM 439 CG PHE A 72 -40.967 30.926 -5.313 1.00 80.87 C
ANISOU 439 CG PHE A 72 9202 11435 10091 220 1313 -642 C
ATOM 440 CD1 PHE A 72 -41.270 31.831 -4.310 1.00 79.99 C
ANISOU 440 CD1 PHE A 72 9132 11293 9967 302 1322 -666 C
ATOM 441 CD2 PHE A 72 -39.641 30.577 -5.515 1.00 86.31 C
ANISOU 441 CD2 PHE A 72 9953 12113 10730 152 1293 -611 C
ATOM 442 CE1 PHE A 72 -40.270 32.385 -3.531 1.00 87.23 C
ANISOU 442 CE1 PHE A 72 10156 12164 10825 316 1308 -656 C
ATOM 443 CE2 PHE A 72 -38.638 31.128 -4.740 1.00 86.45 C
ANISOU 443 CE2 PHE A 72 10068 12091 10690 163 1282 -607 C
ATOM 444 CZ PHE A 72 -38.952 32.033 -3.747 1.00 83.08 C
ANISOU 444 CZ PHE A 72 9685 11627 10253 244 1288 -629 C
ATOM 445 N LEU A 73 -40.817 31.280 -8.925 1.00 93.32 N
ANISOU 445 N LEU A 73 10737 13018 11705 131 1100 -597 N
ATOM 446 CA LEU A 73 -39.727 31.901 -9.672 1.00 89.81 C
ANISOU 446 CA LEU A 73 10379 12534 11209 85 1021 -560 C
ATOM 447 C LEU A 73 -40.227 33.057 -10.529 1.00 98.36 C
ANISOU 447 C LEU A 73 11498 13575 12299 132 925 -564 C
ATOM 448 O LEU A 73 -39.554 34.089 -10.638 1.00 97.11 O
ANISOU 448 O LEU A 73 11444 13359 12094 126 867 -545 O
ATOM 449 CB LEU A 73 -39.024 30.859 -10.540 1.00 86.24 C
ANISOU 449 CB LEU A 73 9902 12120 10746 -2 1022 -531 C
ATOM 450 CG LEU A 73 -38.051 29.923 -9.826 1.00 85.99 C
ANISOU 450 CG LEU A 73 9883 12114 10676 -55 1087 -522 C
ATOM 451 CD1 LEU A 73 -37.472 28.915 -10.803 1.00 77.75 C
ANISOU 451 CD1 LEU A 73 8809 11113 9621 -129 1075 -499 C
ATOM 452 CD2 LEU A 73 -36.945 30.726 -9.162 1.00 83.69 C
ANISOU 452 CD2 LEU A 73 9692 11782 10326 -63 1071 -517 C
ATOM 453 N LYS A 74 -41.400 32.903 -11.148 1.00 99.31 N
ANISOU 453 N LYS A 74 11538 13721 12474 178 905 -592 N
ATOM 454 CA LYS A 74 -41.936 33.972 -11.983 1.00 96.99 C
ANISOU 454 CA LYS A 74 11285 13385 12180 238 806 -602 C
ATOM 455 C LYS A 74 -42.272 35.206 -11.156 1.00101.54 C
ANISOU 455 C LYS A 74 11931 13912 12740 324 781 -628 C
ATOM 456 O LYS A 74 -42.103 36.337 -11.628 1.00 98.66 O
ANISOU 456 O LYS A 74 11669 13480 12336 352 693 -619 O
ATOM 457 CB LYS A 74 -43.171 33.480 -12.738 1.00115.91 C
ANISOU 457 CB LYS A 74 13569 15828 14642 282 789 -642 C
ATOM 458 CG LYS A 74 -43.709 34.464 -13.767 1.00129.76 C
ANISOU 458 CG LYS A 74 15372 17539 16390 350 675 -658 C
ATOM 459 CD LYS A 74 -44.960 33.929 -14.447 1.00142.34 C
ANISOU 459 CD LYS A 74 16841 19186 18055 403 656 -712 C
ATOM 460 CE LYS A 74 -45.518 34.931 -15.446 1.00138.83 C
ANISOU 460 CE LYS A 74 16456 18695 17596 490 534 -737 C
ATOM 461 NZ LYS A 74 -46.782 34.452 -16.071 1.00144.61 N
ANISOU 461 NZ LYS A 74 17060 19483 18401 554 507 -806 N
ATOM 462 N GLU A 75 -42.738 35.013 -9.920 1.00108.20 N
ANISOU 462 N GLU A 75 12725 14781 13604 368 856 -660 N
ATOM 463 CA GLU A 75 -43.016 36.149 -9.047 1.00 92.34 C
ANISOU 463 CA GLU A 75 10782 12728 11574 456 834 -686 C
ATOM 464 C GLU A 75 -41.728 36.799 -8.560 1.00 88.94 C
ANISOU 464 C GLU A 75 10482 12232 11077 414 818 -647 C
ATOM 465 O GLU A 75 -41.635 38.030 -8.490 1.00 80.41 O
ANISOU 465 O GLU A 75 9507 11084 9962 462 745 -649 O
ATOM 466 CB GLU A 75 -43.869 35.704 -7.860 1.00 99.40 C
ANISOU 466 CB GLU A 75 11586 13674 12506 513 928 -732 C
ATOM 467 CG GLU A 75 -45.253 35.201 -8.233 1.00120.50 C
ANISOU 467 CG GLU A 75 14119 16414 15251 559 947 -787 C
ATOM 468 CD GLU A 75 -46.016 34.666 -7.036 1.00136.02 C
ANISOU 468 CD GLU A 75 15994 18437 17251 594 1060 -829 C
ATOM 469 OE1 GLU A 75 -45.387 34.439 -5.980 1.00127.88 O
ANISOU 469 OE1 GLU A 75 15007 17393 16186 570 1133 -807 O
ATOM 470 OE2 GLU A 75 -47.245 34.475 -7.150 1.00139.10 O
ANISOU 470 OE2 GLU A 75 16268 18884 17700 645 1077 -889 O
ATOM 471 N GLN A 76 -40.724 35.989 -8.215 1.00 94.27 N
ANISOU 471 N GLN A 76 11157 12928 11734 328 880 -617 N
ATOM 472 CA GLN A 76 -39.464 36.541 -7.730 1.00 91.58 C
ANISOU 472 CA GLN A 76 10926 12534 11335 285 866 -592 C
ATOM 473 C GLN A 76 -38.665 37.191 -8.851 1.00 91.17 C
ANISOU 473 C GLN A 76 10961 12433 11245 219 781 -555 C
ATOM 474 O GLN A 76 -37.904 38.134 -8.600 1.00 83.85 O
ANISOU 474 O GLN A 76 10143 11442 10273 203 740 -544 O
ATOM 475 CB GLN A 76 -38.637 35.450 -7.051 1.00 87.87 C
ANISOU 475 CB GLN A 76 10427 12106 10852 223 951 -582 C
ATOM 476 CG GLN A 76 -39.253 34.922 -5.769 1.00 94.15 C
ANISOU 476 CG GLN A 76 11173 12932 11666 284 1042 -614 C
ATOM 477 CD GLN A 76 -39.366 35.984 -4.693 1.00 85.86 C
ANISOU 477 CD GLN A 76 10196 11833 10595 368 1029 -637 C
ATOM 478 OE1 GLN A 76 -38.369 36.586 -4.292 1.00 93.76 O
ANISOU 478 OE1 GLN A 76 11290 12785 11550 351 998 -628 O
ATOM 479 NE2 GLN A 76 -40.584 36.225 -4.224 1.00 71.66 N
ANISOU 479 NE2 GLN A 76 8350 10048 8828 462 1050 -672 N
ATOM 480 N SER A 77 -38.815 36.704 -10.085 1.00 98.56 N
ANISOU 480 N SER A 77 11856 13396 12197 177 757 -537 N
ATOM 481 CA SER A 77 -38.139 37.338 -11.212 1.00 98.46 C
ANISOU 481 CA SER A 77 11932 13334 12142 117 682 -501 C
ATOM 482 C SER A 77 -38.643 38.760 -11.424 1.00 99.32 C
ANISOU 482 C SER A 77 12146 13360 12230 189 594 -510 C
ATOM 483 O SER A 77 -37.854 39.670 -11.702 1.00 90.26 O
ANISOU 483 O SER A 77 11122 12142 11031 143 544 -483 O
ATOM 484 CB SER A 77 -38.330 36.504 -12.479 1.00104.96 C
ANISOU 484 CB SER A 77 12689 14204 12985 76 672 -484 C
ATOM 485 OG SER A 77 -37.632 37.071 -13.575 1.00110.80 O
ANISOU 485 OG SER A 77 13522 14899 13679 14 609 -446 O
ATOM 486 N THR A 78 -39.955 38.970 -11.289 1.00102.69 N
ANISOU 486 N THR A 78 12528 13795 12695 301 575 -551 N
ATOM 487 CA THR A 78 -40.509 40.313 -11.424 1.00 95.54 C
ANISOU 487 CA THR A 78 11726 12811 11763 390 484 -569 C
ATOM 488 C THR A 78 -40.054 41.213 -10.282 1.00 99.53 C
ANISOU 488 C THR A 78 12325 13258 12234 414 481 -575 C
ATOM 489 O THR A 78 -39.732 42.387 -10.499 1.00 97.36 O
ANISOU 489 O THR A 78 12192 12892 11909 420 404 -562 O
ATOM 490 CB THR A 78 -42.036 40.247 -11.481 1.00 80.65 C
ANISOU 490 CB THR A 78 9751 10964 9928 513 466 -627 C
ATOM 491 OG1 THR A 78 -42.440 39.381 -12.550 1.00 96.16 O
ANISOU 491 OG1 THR A 78 11626 12982 11929 490 465 -627 O
ATOM 492 CG2 THR A 78 -42.624 41.632 -11.711 1.00 81.22 C
ANISOU 492 CG2 THR A 78 9940 10956 9966 618 358 -653 C
ATOM 493 N LEU A 79 -40.015 40.679 -9.058 1.00100.12 N
ANISOU 493 N LEU A 79 12331 13378 12331 428 563 -594 N
ATOM 494 CA LEU A 79 -39.560 41.468 -7.918 1.00 93.96 C
ANISOU 494 CA LEU A 79 11636 12546 11518 457 560 -603 C
ATOM 495 C LEU A 79 -38.070 41.770 -8.011 1.00 95.27 C
ANISOU 495 C LEU A 79 11900 12663 11637 342 549 -563 C
ATOM 496 O LEU A 79 -37.625 42.852 -7.609 1.00 88.81 O
ANISOU 496 O LEU A 79 11200 11764 10779 351 498 -563 O
ATOM 497 CB LEU A 79 -39.880 40.738 -6.615 1.00 89.62 C
ANISOU 497 CB LEU A 79 10994 12059 11000 503 656 -633 C
ATOM 498 CG LEU A 79 -41.360 40.611 -6.255 1.00 87.87 C
ANISOU 498 CG LEU A 79 10679 11886 10823 622 677 -684 C
ATOM 499 CD1 LEU A 79 -41.533 39.773 -5.001 1.00 78.70 C
ANISOU 499 CD1 LEU A 79 9435 10785 9684 643 790 -705 C
ATOM 500 CD2 LEU A 79 -41.981 41.988 -6.074 1.00 86.80 C
ANISOU 500 CD2 LEU A 79 10632 11684 10662 737 588 -715 C
ATOM 501 N ALA A 80 -37.282 40.826 -8.533 1.00 98.72 N
ANISOU 501 N ALA A 80 12284 13148 12076 232 593 -534 N
ATOM 502 CA ALA A 80 -35.850 41.060 -8.678 1.00 96.21 C
ANISOU 502 CA ALA A 80 12041 12799 11715 117 586 -507 C
ATOM 503 C ALA A 80 -35.562 42.155 -9.696 1.00102.70 C
ANISOU 503 C ALA A 80 12992 13536 12495 73 500 -478 C
ATOM 504 O ALA A 80 -34.574 42.886 -9.559 1.00 95.55 O
ANISOU 504 O ALA A 80 12185 12571 11549 4 477 -466 O
ATOM 505 CB ALA A 80 -35.140 39.767 -9.076 1.00 83.41 C
ANISOU 505 CB ALA A 80 10330 11261 10103 20 648 -490 C
ATOM 506 N GLN A 81 -36.410 42.289 -10.714 1.00 99.97 N
ANISOU 506 N GLN A 81 12650 13180 12156 112 453 -469 N
ATOM 507 CA GLN A 81 -36.251 43.322 -11.734 1.00100.99 C
ANISOU 507 CA GLN A 81 12919 13218 12236 83 370 -441 C
ATOM 508 C GLN A 81 -36.573 44.721 -11.222 1.00 98.66 C
ANISOU 508 C GLN A 81 12761 12819 11908 161 297 -458 C
ATOM 509 O GLN A 81 -36.562 45.665 -12.023 1.00107.74 O
ANISOU 509 O GLN A 81 14049 13879 13010 152 220 -437 O
ATOM 510 CB GLN A 81 -37.121 42.989 -12.947 1.00106.71 C
ANISOU 510 CB GLN A 81 13609 13963 12974 121 335 -434 C
ATOM 511 CG GLN A 81 -36.628 41.789 -13.744 1.00104.92 C
ANISOU 511 CG GLN A 81 13286 13816 12762 26 387 -407 C
ATOM 512 CD GLN A 81 -37.629 41.321 -14.784 1.00110.62 C
ANISOU 512 CD GLN A 81 13951 14569 13510 84 356 -413 C
ATOM 513 OE1 GLN A 81 -38.637 41.981 -15.035 1.00115.18 O
ANISOU 513 OE1 GLN A 81 14572 15103 14088 191 288 -438 O
ATOM 514 NE2 GLN A 81 -37.355 40.173 -15.392 1.00118.23 N
ANISOU 514 NE2 GLN A 81 14817 15611 14496 20 400 -396 N
ATOM 515 N MET A 82 -36.861 44.890 -9.933 1.00105.69 N
ANISOU 515 N MET A 82 13627 13713 12816 241 315 -494 N
ATOM 516 CA MET A 82 -37.051 46.208 -9.344 1.00 97.10 C
ANISOU 516 CA MET A 82 12673 12528 11693 315 244 -512 C
ATOM 517 C MET A 82 -35.769 46.774 -8.749 1.00100.23 C
ANISOU 517 C MET A 82 13161 12866 12056 222 248 -499 C
ATOM 518 O MET A 82 -35.805 47.854 -8.151 1.00 96.80 O
ANISOU 518 O MET A 82 12841 12345 11592 275 190 -514 O
ATOM 519 CB MET A 82 -38.139 46.159 -8.267 1.00 87.74 C
ANISOU 519 CB MET A 82 11416 11379 10542 466 257 -564 C
ATOM 520 CG MET A 82 -39.521 45.806 -8.789 1.00 84.10 C
ANISOU 520 CG MET A 82 10868 10970 10116 572 242 -594 C
ATOM 521 SD MET A 82 -40.794 45.972 -7.523 1.00108.21 S
ANISOU 521 SD MET A 82 13852 14062 13200 750 252 -663 S
ATOM 522 CE MET A 82 -42.253 45.474 -8.434 1.00 85.43 C
ANISOU 522 CE MET A 82 10852 11248 10361 839 233 -702 C
ATOM 523 N TYR A 83 -34.649 46.076 -8.892 1.00106.75 N
ANISOU 523 N TYR A 83 13938 13739 12885 89 308 -478 N
ATOM 524 CA TYR A 83 -33.355 46.549 -8.401 1.00103.05 C
ANISOU 524 CA TYR A 83 13539 13226 12388 -11 313 -477 C
ATOM 525 C TYR A 83 -32.417 46.753 -9.582 1.00107.66 C
ANISOU 525 C TYR A 83 14191 13780 12935 -164 302 -435 C
ATOM 526 O TYR A 83 -32.012 45.764 -10.223 1.00113.37 O
ANISOU 526 O TYR A 83 14820 14586 13671 -243 355 -418 O
ATOM 527 CB TYR A 83 -32.755 45.558 -7.404 1.00 97.69 C
ANISOU 527 CB TYR A 83 12741 12637 11740 -29 396 -504 C
ATOM 528 CG TYR A 83 -33.643 45.265 -6.214 1.00101.06 C
ANISOU 528 CG TYR A 83 13103 13098 12199 115 423 -542 C
ATOM 529 CD1 TYR A 83 -33.671 46.116 -5.117 1.00 97.15 C
ANISOU 529 CD1 TYR A 83 12683 12540 11690 190 390 -571 C
ATOM 530 CD2 TYR A 83 -34.451 44.135 -6.186 1.00101.54 C
ANISOU 530 CD2 TYR A 83 13028 13251 12300 171 484 -549 C
ATOM 531 CE1 TYR A 83 -34.479 45.853 -4.028 1.00 90.09 C
ANISOU 531 CE1 TYR A 83 11731 11679 10818 322 422 -606 C
ATOM 532 CE2 TYR A 83 -35.262 43.863 -5.099 1.00 96.02 C
ANISOU 532 CE2 TYR A 83 12271 12584 11626 292 520 -584 C
ATOM 533 CZ TYR A 83 -35.272 44.725 -4.023 1.00 86.98 C
ANISOU 533 CZ TYR A 83 11203 11381 10464 369 491 -611 C
ATOM 534 OH TYR A 83 -36.078 44.459 -2.940 1.00 85.28 O
ANISOU 534 OH TYR A 83 10933 11201 10269 491 534 -646 O
ATOM 535 N PRO A 84 -32.046 47.990 -9.914 1.00102.03 N
ANISOU 535 N PRO A 84 13644 12951 12173 -213 237 -418 N
ATOM 536 CA PRO A 84 -31.194 48.218 -11.091 1.00109.94 C
ANISOU 536 CA PRO A 84 14719 13920 13132 -365 235 -377 C
ATOM 537 C PRO A 84 -29.788 47.677 -10.869 1.00118.62 C
ANISOU 537 C PRO A 84 15748 15083 14238 -510 303 -386 C
ATOM 538 O PRO A 84 -29.127 48.012 -9.884 1.00115.55 O
ANISOU 538 O PRO A 84 15372 14678 13854 -530 308 -419 O
ATOM 539 CB PRO A 84 -31.198 49.743 -11.241 1.00102.39 C
ANISOU 539 CB PRO A 84 13972 12812 12121 -371 150 -364 C
ATOM 540 CG PRO A 84 -31.490 50.254 -9.869 1.00104.17 C
ANISOU 540 CG PRO A 84 14214 13004 12362 -264 122 -407 C
ATOM 541 CD PRO A 84 -32.413 49.248 -9.240 1.00104.81 C
ANISOU 541 CD PRO A 84 14132 13193 12500 -130 163 -436 C
ATOM 542 N LEU A 85 -29.332 46.842 -11.808 1.00117.07 N
ANISOU 542 N LEU A 85 15478 14963 14040 -604 350 -361 N
ATOM 543 CA LEU A 85 -28.031 46.194 -11.662 1.00112.35 C
ANISOU 543 CA LEU A 85 14794 14447 13447 -730 414 -379 C
ATOM 544 C LEU A 85 -26.889 47.201 -11.658 1.00116.06 C
ANISOU 544 C LEU A 85 15377 14842 13879 -867 400 -384 C
ATOM 545 O LEU A 85 -25.858 46.966 -11.017 1.00114.23 O
ANISOU 545 O LEU A 85 15085 14660 13658 -938 436 -426 O
ATOM 546 CB LEU A 85 -27.817 45.171 -12.779 1.00105.30 C
ANISOU 546 CB LEU A 85 13812 13646 12551 -798 458 -352 C
ATOM 547 CG LEU A 85 -28.442 43.787 -12.604 1.00 99.43 C
ANISOU 547 CG LEU A 85 12909 13016 11853 -710 499 -364 C
ATOM 548 CD1 LEU A 85 -27.966 42.852 -13.705 1.00 90.31 C
ANISOU 548 CD1 LEU A 85 11679 11948 10688 -798 537 -340 C
ATOM 549 CD2 LEU A 85 -28.108 43.221 -11.235 1.00113.88 C
ANISOU 549 CD2 LEU A 85 14648 14906 13716 -668 538 -416 C
ATOM 550 N GLN A 86 -27.048 48.324 -12.365 1.00122.18 N
ANISOU 550 N GLN A 86 16319 15497 14607 -905 347 -347 N
ATOM 551 CA GLN A 86 -25.959 49.289 -12.474 1.00121.93 C
ANISOU 551 CA GLN A 86 16403 15388 14537 -1056 341 -347 C
ATOM 552 C GLN A 86 -25.586 49.875 -11.119 1.00118.68 C
ANISOU 552 C GLN A 86 16014 14935 14145 -1032 319 -400 C
ATOM 553 O GLN A 86 -24.432 50.264 -10.908 1.00120.92 O
ANISOU 553 O GLN A 86 16318 15207 14420 -1165 337 -426 O
ATOM 554 CB GLN A 86 -26.337 50.409 -13.444 1.00121.07 C
ANISOU 554 CB GLN A 86 16494 15140 14366 -1086 284 -294 C
ATOM 555 CG GLN A 86 -27.060 49.935 -14.695 1.00132.19 C
ANISOU 555 CG GLN A 86 17903 16570 15755 -1052 282 -245 C
ATOM 556 CD GLN A 86 -28.569 49.972 -14.541 1.00126.57 C
ANISOU 556 CD GLN A 86 17204 15828 15058 -855 219 -245 C
ATOM 557 OE1 GLN A 86 -29.125 50.927 -13.997 1.00129.61 O
ANISOU 557 OE1 GLN A 86 17707 16111 15429 -768 151 -256 O
ATOM 558 NE2 GLN A 86 -29.239 48.929 -15.016 1.00124.77 N
ANISOU 558 NE2 GLN A 86 16854 15695 14859 -783 240 -237 N
ATOM 559 N GLU A 87 -26.536 49.940 -10.190 1.00120.77 N
ANISOU 559 N GLU A 87 16270 15182 14436 -863 282 -420 N
ATOM 560 CA GLU A 87 -26.282 50.499 -8.870 1.00135.35 C
ANISOU 560 CA GLU A 87 18143 16984 16298 -817 256 -469 C
ATOM 561 C GLU A 87 -25.754 49.471 -7.878 1.00126.36 C
ANISOU 561 C GLU A 87 16839 15966 15204 -794 313 -525 C
ATOM 562 O GLU A 87 -25.449 49.834 -6.737 1.00117.26 O
ANISOU 562 O GLU A 87 15700 14788 14066 -753 295 -573 O
ATOM 563 CB GLU A 87 -27.555 51.152 -8.327 1.00126.92 C
ANISOU 563 CB GLU A 87 17159 15835 15228 -640 185 -468 C
ATOM 564 CG GLU A 87 -28.064 52.291 -9.197 1.00130.04 C
ANISOU 564 CG GLU A 87 17745 16096 15568 -646 111 -423 C
ATOM 565 CD GLU A 87 -29.330 52.921 -8.658 1.00144.15 C
ANISOU 565 CD GLU A 87 19609 17813 17349 -458 34 -432 C
ATOM 566 OE1 GLU A 87 -29.865 52.412 -7.652 1.00148.93 O
ANISOU 566 OE1 GLU A 87 20107 18483 17995 -328 49 -469 O
ATOM 567 OE2 GLU A 87 -29.789 53.926 -9.241 1.00157.42 O
ANISOU 567 OE2 GLU A 87 21462 19374 18978 -439 -41 -405 O
ATOM 568 N ILE A 88 -25.637 48.206 -8.277 1.00123.59 N
ANISOU 568 N ILE A 88 16345 15741 14873 -812 377 -522 N
ATOM 569 CA ILE A 88 -25.016 47.173 -7.456 1.00116.72 C
ANISOU 569 CA ILE A 88 15332 14984 14034 -801 431 -576 C
ATOM 570 C ILE A 88 -23.567 47.019 -7.894 1.00119.42 C
ANISOU 570 C ILE A 88 15637 15377 14362 -976 466 -601 C
ATOM 571 O ILE A 88 -23.284 46.871 -9.089 1.00122.60 O
ANISOU 571 O ILE A 88 16038 15802 14742 -1085 487 -564 O
ATOM 572 CB ILE A 88 -25.773 45.838 -7.566 1.00118.70 C
ANISOU 572 CB ILE A 88 15452 15339 14309 -710 478 -564 C
ATOM 573 CG1 ILE A 88 -27.048 45.868 -6.720 1.00102.57 C
ANISOU 573 CG1 ILE A 88 13413 13270 12290 -532 460 -567 C
ATOM 574 CG2 ILE A 88 -24.886 44.677 -7.139 1.00117.36 C
ANISOU 574 CG2 ILE A 88 15148 15291 14153 -743 537 -612 C
ATOM 575 CD1 ILE A 88 -28.306 46.106 -7.514 1.00113.72 C
ANISOU 575 CD1 ILE A 88 14866 14642 13699 -463 429 -518 C
ATOM 576 N GLN A 89 -22.647 47.062 -6.931 1.00112.50 N
ANISOU 576 N GLN A 89 14727 14521 13496 -999 470 -670 N
ATOM 577 CA GLN A 89 -21.225 46.917 -7.211 1.00116.66 C
ANISOU 577 CA GLN A 89 15203 15110 14015 -1158 501 -715 C
ATOM 578 C GLN A 89 -20.645 45.589 -6.754 1.00113.67 C
ANISOU 578 C GLN A 89 14665 14874 13652 -1133 549 -773 C
ATOM 579 O GLN A 89 -19.687 45.108 -7.362 1.00117.25 O
ANISOU 579 O GLN A 89 15044 15413 14092 -1253 586 -797 O
ATOM 580 CB GLN A 89 -20.438 48.062 -6.561 1.00113.39 C
ANISOU 580 CB GLN A 89 14874 14610 13598 -1227 461 -764 C
ATOM 581 CG GLN A 89 -20.854 49.435 -7.063 1.00130.75 C
ANISOU 581 CG GLN A 89 17250 16658 15771 -1272 410 -709 C
ATOM 582 CD GLN A 89 -19.959 50.544 -6.553 1.00142.74 C
ANISOU 582 CD GLN A 89 18855 18092 17286 -1369 375 -758 C
ATOM 583 OE1 GLN A 89 -19.131 50.331 -5.668 1.00152.13 O
ANISOU 583 OE1 GLN A 89 19969 19334 18500 -1377 380 -839 O
ATOM 584 NE2 GLN A 89 -20.119 51.737 -7.113 1.00138.19 N
ANISOU 584 NE2 GLN A 89 18445 17382 16678 -1442 335 -712 N
ATOM 585 N ASN A 90 -21.198 44.991 -5.701 1.00110.92 N
ANISOU 585 N ASN A 90 14270 14550 13323 -979 551 -799 N
ATOM 586 CA ASN A 90 -20.810 43.645 -5.297 1.00107.42 C
ANISOU 586 CA ASN A 90 13696 14233 12885 -936 594 -847 C
ATOM 587 C ASN A 90 -21.182 42.656 -6.395 1.00106.25 C
ANISOU 587 C ASN A 90 13477 14164 12731 -958 636 -795 C
ATOM 588 O ASN A 90 -22.366 42.458 -6.689 1.00105.89 O
ANISOU 588 O ASN A 90 13445 14095 12695 -876 638 -735 O
ATOM 589 CB ASN A 90 -21.499 43.292 -3.977 1.00106.30 C
ANISOU 589 CB ASN A 90 13550 14081 12760 -761 591 -872 C
ATOM 590 CG ASN A 90 -21.068 41.945 -3.407 1.00106.21 C
ANISOU 590 CG ASN A 90 13428 14182 12743 -706 632 -928 C
ATOM 591 OD1 ASN A 90 -20.814 40.984 -4.133 1.00108.83 O
ANISOU 591 OD1 ASN A 90 13678 14607 13065 -753 668 -920 O
ATOM 592 ND2 ASN A 90 -20.996 41.878 -2.081 1.00 96.10 N
ANISOU 592 ND2 ASN A 90 12159 12890 11465 -597 622 -986 N
ATOM 593 N LEU A 91 -20.167 42.034 -7.000 1.00 99.28 N
ANISOU 593 N LEU A 91 12512 13380 11831 -1065 665 -825 N
ATOM 594 CA LEU A 91 -20.408 41.171 -8.152 1.00102.66 C
ANISOU 594 CA LEU A 91 12879 13881 12248 -1099 698 -776 C
ATOM 595 C LEU A 91 -21.136 39.889 -7.766 1.00101.41 C
ANISOU 595 C LEU A 91 12643 13787 12101 -969 724 -772 C
ATOM 596 O LEU A 91 -21.932 39.372 -8.560 1.00 98.36 O
ANISOU 596 O LEU A 91 12238 13417 11719 -948 738 -712 O
ATOM 597 CB LEU A 91 -19.088 40.846 -8.849 1.00 97.08 C
ANISOU 597 CB LEU A 91 12102 13269 11514 -1243 723 -816 C
ATOM 598 CG LEU A 91 -18.412 42.021 -9.560 1.00 95.45 C
ANISOU 598 CG LEU A 91 11970 13005 11291 -1404 714 -806 C
ATOM 599 CD1 LEU A 91 -17.105 41.585 -10.203 1.00105.72 C
ANISOU 599 CD1 LEU A 91 13181 14421 12567 -1543 749 -856 C
ATOM 600 CD2 LEU A 91 -19.348 42.625 -10.597 1.00 97.42 C
ANISOU 600 CD2 LEU A 91 12319 13165 11530 -1422 703 -706 C
ATOM 601 N THR A 92 -20.881 39.358 -6.567 1.00 93.59 N
ANISOU 601 N THR A 92 11615 12830 11114 -883 730 -837 N
ATOM 602 CA THR A 92 -21.593 38.161 -6.131 1.00 99.35 C
ANISOU 602 CA THR A 92 12290 13608 11849 -763 761 -832 C
ATOM 603 C THR A 92 -23.083 38.431 -5.969 1.00 99.78 C
ANISOU 603 C THR A 92 12393 13587 11932 -662 760 -769 C
ATOM 604 O THR A 92 -23.907 37.540 -6.210 1.00 91.28 O
ANISOU 604 O THR A 92 11270 12545 10866 -604 789 -736 O
ATOM 605 CB THR A 92 -20.997 37.638 -4.822 1.00 91.22 C
ANISOU 605 CB THR A 92 11236 12616 10808 -686 766 -916 C
ATOM 606 OG1 THR A 92 -19.579 37.492 -4.969 1.00106.54 O
ANISOU 606 OG1 THR A 92 13127 14630 12724 -778 758 -989 O
ATOM 607 CG2 THR A 92 -21.598 36.286 -4.461 1.00 75.57 C
ANISOU 607 CG2 THR A 92 9204 10687 8820 -582 805 -912 C
ATOM 608 N VAL A 93 -23.449 39.651 -5.575 1.00 98.03 N
ANISOU 608 N VAL A 93 12262 13263 11722 -640 724 -759 N
ATOM 609 CA VAL A 93 -24.859 40.016 -5.510 1.00 96.30 C
ANISOU 609 CA VAL A 93 12086 12976 11526 -544 715 -707 C
ATOM 610 C VAL A 93 -25.415 40.239 -6.910 1.00 98.61 C
ANISOU 610 C VAL A 93 12395 13252 11822 -601 702 -639 C
ATOM 611 O VAL A 93 -26.555 39.861 -7.209 1.00 95.14 O
ANISOU 611 O VAL A 93 11932 12814 11402 -530 712 -601 O
ATOM 612 CB VAL A 93 -25.046 41.257 -4.618 1.00106.80 C
ANISOU 612 CB VAL A 93 13515 14202 12860 -490 671 -723 C
ATOM 613 CG1 VAL A 93 -26.505 41.689 -4.597 1.00102.00 C
ANISOU 613 CG1 VAL A 93 12952 13532 12272 -386 656 -678 C
ATOM 614 CG2 VAL A 93 -24.549 40.974 -3.208 1.00 92.26 C
ANISOU 614 CG2 VAL A 93 11662 12378 11014 -417 683 -793 C
ATOM 615 N LYS A 94 -24.618 40.848 -7.794 1.00104.99 N
ANISOU 615 N LYS A 94 13240 14044 12606 -731 681 -628 N
ATOM 616 CA LYS A 94 -25.080 41.105 -9.154 1.00106.83 C
ANISOU 616 CA LYS A 94 13506 14253 12831 -785 667 -564 C
ATOM 617 C LYS A 94 -25.316 39.806 -9.916 1.00107.85 C
ANISOU 617 C LYS A 94 13533 14480 12966 -785 704 -542 C
ATOM 618 O LYS A 94 -26.253 39.714 -10.717 1.00126.46 O
ANISOU 618 O LYS A 94 15895 16822 15332 -754 694 -493 O
ATOM 619 CB LYS A 94 -24.073 41.987 -9.894 1.00109.62 C
ANISOU 619 CB LYS A 94 13928 14570 13151 -935 649 -558 C
ATOM 620 CG LYS A 94 -24.467 42.306 -11.330 1.00115.53 C
ANISOU 620 CG LYS A 94 14733 15286 13880 -994 634 -491 C
ATOM 621 CD LYS A 94 -23.428 43.173 -12.022 1.00121.89 C
ANISOU 621 CD LYS A 94 15616 16052 14646 -1154 629 -484 C
ATOM 622 CE LYS A 94 -23.343 44.551 -11.389 1.00112.68 C
ANISOU 622 CE LYS A 94 14578 14762 13472 -1164 585 -496 C
ATOM 623 NZ LYS A 94 -22.393 45.436 -12.119 1.00120.02 N
ANISOU 623 NZ LYS A 94 15598 15643 14363 -1333 584 -486 N
ATOM 624 N LEU A 95 -24.481 38.790 -9.678 1.00 96.28 N
ANISOU 624 N LEU A 95 11977 13114 11491 -813 741 -584 N
ATOM 625 CA LEU A 95 -24.669 37.508 -10.350 1.00107.14 C
ANISOU 625 CA LEU A 95 13260 14582 12868 -809 772 -567 C
ATOM 626 C LEU A 95 -25.997 36.870 -9.962 1.00 96.75 C
ANISOU 626 C LEU A 95 11912 13263 11588 -682 787 -548 C
ATOM 627 O LEU A 95 -26.692 36.298 -10.810 1.00 90.12 O
ANISOU 627 O LEU A 95 11033 12448 10760 -670 791 -510 O
ATOM 628 CB LEU A 95 -23.511 36.563 -10.025 1.00 94.74 C
ANISOU 628 CB LEU A 95 11610 13114 11274 -846 800 -627 C
ATOM 629 CG LEU A 95 -22.184 36.796 -10.747 1.00 84.86 C
ANISOU 629 CG LEU A 95 10347 11910 9986 -986 798 -649 C
ATOM 630 CD1 LEU A 95 -21.156 35.762 -10.318 1.00 84.42 C
ANISOU 630 CD1 LEU A 95 10203 11966 9907 -993 819 -722 C
ATOM 631 CD2 LEU A 95 -22.385 36.762 -12.253 1.00 79.61 C
ANISOU 631 CD2 LEU A 95 9685 11257 9308 -1058 797 -587 C
ATOM 632 N GLN A 96 -26.367 36.960 -8.683 1.00 91.85 N
ANISOU 632 N GLN A 96 11303 12612 10983 -588 796 -579 N
ATOM 633 CA GLN A 96 -27.612 36.348 -8.234 1.00 89.36 C
ANISOU 633 CA GLN A 96 10951 12299 10700 -476 823 -567 C
ATOM 634 C GLN A 96 -28.821 37.146 -8.705 1.00 87.40 C
ANISOU 634 C GLN A 96 10748 11981 10479 -430 790 -525 C
ATOM 635 O GLN A 96 -29.856 36.565 -9.053 1.00 87.49 O
ANISOU 635 O GLN A 96 10709 12013 10521 -377 805 -504 O
ATOM 636 CB GLN A 96 -27.601 36.213 -6.712 1.00 89.21 C
ANISOU 636 CB GLN A 96 10940 12272 10683 -390 849 -614 C
ATOM 637 CG GLN A 96 -26.417 35.418 -6.189 1.00 88.07 C
ANISOU 637 CG GLN A 96 10761 12195 10507 -417 872 -666 C
ATOM 638 CD GLN A 96 -26.275 35.500 -4.685 1.00 85.97 C
ANISOU 638 CD GLN A 96 10528 11904 10232 -331 886 -717 C
ATOM 639 OE1 GLN A 96 -27.156 35.069 -3.942 1.00 81.73 O
ANISOU 639 OE1 GLN A 96 9987 11358 9710 -234 923 -714 O
ATOM 640 NE2 GLN A 96 -25.161 36.058 -4.227 1.00 90.57 N
ANISOU 640 NE2 GLN A 96 11144 12476 10790 -367 858 -766 N
ATOM 641 N LEU A 97 -28.712 38.475 -8.729 1.00 89.92 N
ANISOU 641 N LEU A 97 11163 12215 10786 -447 742 -518 N
ATOM 642 CA LEU A 97 -29.799 39.286 -9.268 1.00 98.11 C
ANISOU 642 CA LEU A 97 12257 13182 11838 -399 698 -484 C
ATOM 643 C LEU A 97 -29.944 39.086 -10.771 1.00 99.03 C
ANISOU 643 C LEU A 97 12365 13314 11947 -459 680 -441 C
ATOM 644 O LEU A 97 -31.064 38.986 -11.283 1.00 95.80 O
ANISOU 644 O LEU A 97 11939 12897 11562 -394 664 -421 O
ATOM 645 CB LEU A 97 -29.569 40.762 -8.948 1.00 95.89 C
ANISOU 645 CB LEU A 97 12101 12798 11535 -405 644 -488 C
ATOM 646 CG LEU A 97 -30.327 41.338 -7.752 1.00 93.03 C
ANISOU 646 CG LEU A 97 11776 12382 11190 -281 630 -513 C
ATOM 647 CD1 LEU A 97 -30.102 42.837 -7.665 1.00 99.47 C
ANISOU 647 CD1 LEU A 97 12729 13088 11979 -295 564 -511 C
ATOM 648 CD2 LEU A 97 -31.811 41.021 -7.853 1.00100.52 C
ANISOU 648 CD2 LEU A 97 12677 13342 12172 -169 635 -503 C
ATOM 649 N GLN A 98 -28.822 39.019 -11.492 1.00102.52 N
ANISOU 649 N GLN A 98 12815 13783 12355 -580 682 -431 N
ATOM 650 CA GLN A 98 -28.880 38.873 -12.942 1.00100.84 C
ANISOU 650 CA GLN A 98 12605 13582 12126 -639 666 -388 C
ATOM 651 C GLN A 98 -29.506 37.542 -13.341 1.00103.31 C
ANISOU 651 C GLN A 98 12806 13979 12469 -595 695 -382 C
ATOM 652 O GLN A 98 -30.300 37.483 -14.286 1.00115.44 O
ANISOU 652 O GLN A 98 14343 15505 14016 -569 669 -351 O
ATOM 653 CB GLN A 98 -27.479 39.013 -13.537 1.00104.25 C
ANISOU 653 CB GLN A 98 13059 14038 12513 -781 675 -386 C
ATOM 654 CG GLN A 98 -27.446 39.201 -15.043 1.00105.43 C
ANISOU 654 CG GLN A 98 13251 14175 12631 -851 654 -337 C
ATOM 655 CD GLN A 98 -26.068 39.583 -15.545 1.00114.29 C
ANISOU 655 CD GLN A 98 14412 15310 13705 -1000 669 -338 C
ATOM 656 OE1 GLN A 98 -25.095 39.570 -14.791 1.00100.43 O
ANISOU 656 OE1 GLN A 98 12628 13587 11944 -1052 693 -382 O
ATOM 657 NE2 GLN A 98 -25.979 39.933 -16.824 1.00114.66 N
ANISOU 657 NE2 GLN A 98 14522 15329 13714 -1069 654 -292 N
ATOM 658 N ALA A 99 -29.167 36.465 -12.627 1.00 90.82 N
ANISOU 658 N ALA A 99 11133 12475 10898 -584 745 -413 N
ATOM 659 CA ALA A 99 -29.754 35.165 -12.932 1.00 98.97 C
ANISOU 659 CA ALA A 99 12066 13580 11958 -547 774 -408 C
ATOM 660 C ALA A 99 -31.240 35.127 -12.604 1.00 91.08 C
ANISOU 660 C ALA A 99 11043 12554 11010 -435 773 -408 C
ATOM 661 O ALA A 99 -32.003 34.412 -13.263 1.00 97.57 O
ANISOU 661 O ALA A 99 11802 13410 11859 -409 775 -394 O
ATOM 662 CB ALA A 99 -29.015 34.062 -12.173 1.00 93.06 C
ANISOU 662 CB ALA A 99 11248 12910 11199 -557 824 -445 C
ATOM 663 N LEU A 100 -31.668 35.887 -11.595 1.00 90.91 N
ANISOU 663 N LEU A 100 11066 12475 11000 -368 769 -428 N
ATOM 664 CA LEU A 100 -33.077 35.907 -11.222 1.00 92.35 C
ANISOU 664 CA LEU A 100 11220 12641 11229 -259 773 -437 C
ATOM 665 C LEU A 100 -33.882 36.868 -12.086 1.00 94.66 C
ANISOU 665 C LEU A 100 11569 12870 11526 -225 705 -417 C
ATOM 666 O LEU A 100 -35.078 36.645 -12.303 1.00 93.98 O
ANISOU 666 O LEU A 100 11433 12794 11482 -149 698 -425 O
ATOM 667 CB LEU A 100 -33.218 36.274 -9.743 1.00 91.88 C
ANISOU 667 CB LEU A 100 11182 12554 11176 -190 799 -470 C
ATOM 668 CG LEU A 100 -34.597 36.101 -9.103 1.00 86.58 C
ANISOU 668 CG LEU A 100 10461 11886 10550 -79 826 -491 C
ATOM 669 CD1 LEU A 100 -35.104 34.682 -9.295 1.00 74.67 C
ANISOU 669 CD1 LEU A 100 8840 10456 9077 -78 883 -493 C
ATOM 670 CD2 LEU A 100 -34.540 36.453 -7.625 1.00 89.65 C
ANISOU 670 CD2 LEU A 100 10881 12249 10932 -17 856 -522 C
ATOM 671 N GLN A 101 -33.251 37.929 -12.591 1.00 98.21 N
ANISOU 671 N GLN A 101 12128 13253 11932 -279 653 -396 N
ATOM 672 CA GLN A 101 -33.942 38.884 -13.448 1.00101.14 C
ANISOU 672 CA GLN A 101 12582 13553 12295 -244 582 -378 C
ATOM 673 C GLN A 101 -34.139 38.378 -14.870 1.00108.71 C
ANISOU 673 C GLN A 101 13514 14539 13250 -275 561 -349 C
ATOM 674 O GLN A 101 -34.846 39.032 -15.643 1.00112.93 O
ANISOU 674 O GLN A 101 14113 15019 13778 -228 498 -338 O
ATOM 675 CB GLN A 101 -33.179 40.211 -13.483 1.00 91.96 C
ANISOU 675 CB GLN A 101 11564 12297 11078 -299 537 -363 C
ATOM 676 CG GLN A 101 -33.280 41.018 -12.201 1.00 96.36 C
ANISOU 676 CG GLN A 101 12175 12799 11636 -238 528 -392 C
ATOM 677 CD GLN A 101 -32.383 42.240 -12.209 1.00101.78 C
ANISOU 677 CD GLN A 101 13003 13396 12272 -311 488 -380 C
ATOM 678 OE1 GLN A 101 -31.677 42.500 -13.183 1.00101.45 O
ANISOU 678 OE1 GLN A 101 13022 13333 12192 -415 473 -348 O
ATOM 679 NE2 GLN A 101 -32.405 42.997 -11.117 1.00107.11 N
ANISOU 679 NE2 GLN A 101 13735 14017 12946 -260 472 -407 N
ATOM 680 N GLN A 102 -33.538 37.241 -15.230 1.00112.59 N
ANISOU 680 N GLN A 102 13922 15114 13744 -343 605 -340 N
ATOM 681 CA GLN A 102 -33.641 36.717 -16.587 1.00112.05 C
ANISOU 681 CA GLN A 102 13830 15075 13670 -372 584 -312 C
ATOM 682 C GLN A 102 -35.096 36.494 -16.974 1.00124.44 C
ANISOU 682 C GLN A 102 15349 16646 15288 -266 553 -326 C
ATOM 683 O GLN A 102 -35.766 35.620 -16.415 1.00115.90 O
ANISOU 683 O GLN A 102 14156 15621 14261 -214 593 -355 O
ATOM 684 CB GLN A 102 -32.853 35.411 -16.727 1.00103.05 C
ANISOU 684 CB GLN A 102 12595 14033 12528 -443 638 -310 C
ATOM 685 CG GLN A 102 -31.349 35.570 -16.604 1.00100.56 C
ANISOU 685 CG GLN A 102 12317 13732 12160 -554 661 -304 C
ATOM 686 CD GLN A 102 -30.738 36.347 -17.755 1.00122.53 C
ANISOU 686 CD GLN A 102 15198 16472 14887 -636 624 -267 C
ATOM 687 OE1 GLN A 102 -31.338 36.485 -18.823 1.00137.70 O
ANISOU 687 OE1 GLN A 102 17150 18366 16802 -613 583 -240 O
ATOM 688 NE2 GLN A 102 -29.532 36.859 -17.542 1.00113.60 N
ANISOU 688 NE2 GLN A 102 14118 15332 13712 -733 640 -269 N
ATOM 689 N ASN A 103 -35.591 37.293 -17.920 1.00128.33 N
ANISOU 689 N ASN A 103 15926 17073 15760 -232 482 -312 N
ATOM 690 CA ASN A 103 -36.970 37.155 -18.373 1.00126.31 C
ANISOU 690 CA ASN A 103 15623 16819 15549 -124 439 -337 C
ATOM 691 C ASN A 103 -37.199 35.798 -19.024 1.00138.20 C
ANISOU 691 C ASN A 103 17006 18412 17093 -136 463 -338 C
ATOM 692 O ASN A 103 -38.007 34.991 -18.549 1.00142.86 O
ANISOU 692 O ASN A 103 17475 19057 17746 -83 495 -373 O
ATOM 693 CB ASN A 103 -37.315 38.270 -19.357 1.00129.39 C
ANISOU 693 CB ASN A 103 16150 17118 15894 -85 349 -323 C
ATOM 694 CG ASN A 103 -37.700 39.563 -18.677 1.00131.05 C
ANISOU 694 CG ASN A 103 16466 17241 16087 -16 306 -342 C
ATOM 695 OD1 ASN A 103 -38.425 39.578 -17.683 1.00123.46 O
ANISOU 695 OD1 ASN A 103 15443 16295 15170 65 321 -385 O
ATOM 696 ND2 ASN A 103 -37.206 40.666 -19.223 1.00148.33 N
ANISOU 696 ND2 ASN A 103 18821 19333 18204 -51 254 -310 N
ATOM 697 N GLY A 104 -36.490 35.532 -20.116 1.00128.15 N
ANISOU 697 N GLY A 104 15762 17149 15778 -209 448 -299 N
ATOM 698 CA GLY A 104 -36.786 34.344 -20.895 1.00119.82 C
ANISOU 698 CA GLY A 104 14606 16165 14754 -208 452 -300 C
ATOM 699 C GLY A 104 -38.023 34.586 -21.737 1.00111.97 C
ANISOU 699 C GLY A 104 13614 15143 13788 -106 377 -321 C
ATOM 700 O GLY A 104 -38.192 35.652 -22.339 1.00100.95 O
ANISOU 700 O GLY A 104 12341 13666 12349 -72 310 -311 O
ATOM 701 N SER A 105 -38.915 33.595 -21.767 1.00121.31 N
ANISOU 701 N SER A 105 14664 16388 15041 -55 387 -357 N
ATOM 702 CA SER A 105 -40.145 33.717 -22.538 1.00115.83 C
ANISOU 702 CA SER A 105 13948 15678 14384 49 315 -394 C
ATOM 703 C SER A 105 -41.104 34.754 -21.965 1.00117.38 C
ANISOU 703 C SER A 105 14179 15821 14598 154 276 -440 C
ATOM 704 O SER A 105 -42.047 35.147 -22.661 1.00110.01 O
ANISOU 704 O SER A 105 13261 14861 13677 252 197 -476 O
ATOM 705 CB SER A 105 -40.848 32.359 -22.625 1.00110.22 C
ANISOU 705 CB SER A 105 13074 15054 13752 67 341 -428 C
ATOM 706 OG SER A 105 -42.061 32.459 -23.353 1.00109.41 O
ANISOU 706 OG SER A 105 12936 14943 13692 171 268 -477 O
ATOM 707 N SER A 106 -40.890 35.208 -20.728 1.00125.05 N
ANISOU 707 N SER A 106 15166 16779 15568 146 323 -446 N
ATOM 708 CA SER A 106 -41.788 36.177 -20.108 1.00123.78 C
ANISOU 708 CA SER A 106 15036 16574 15421 252 286 -493 C
ATOM 709 C SER A 106 -41.652 37.578 -20.691 1.00117.85 C
ANISOU 709 C SER A 106 14466 15716 14596 288 196 -476 C
ATOM 710 O SER A 106 -42.369 38.482 -20.246 1.00122.94 O
ANISOU 710 O SER A 106 15157 16315 15240 386 151 -516 O
ATOM 711 CB SER A 106 -41.551 36.222 -18.597 1.00121.01 C
ANISOU 711 CB SER A 106 14655 16238 15085 235 364 -502 C
ATOM 712 OG SER A 106 -40.220 36.603 -18.296 1.00120.05 O
ANISOU 712 OG SER A 106 14634 16079 14900 138 390 -449 O
ATOM 713 N VAL A 107 -40.760 37.784 -21.660 1.00108.84 N
ANISOU 713 N VAL A 107 13434 14534 13388 214 171 -418 N
ATOM 714 CA VAL A 107 -40.636 39.086 -22.305 1.00106.60 C
ANISOU 714 CA VAL A 107 13341 14139 13025 240 88 -397 C
ATOM 715 C VAL A 107 -41.573 39.226 -23.501 1.00105.17 C
ANISOU 715 C VAL A 107 13190 13931 12839 345 -8 -425 C
ATOM 716 O VAL A 107 -41.860 40.355 -23.925 1.00 95.23 O
ANISOU 716 O VAL A 107 12088 12575 11522 414 -93 -430 O
ATOM 717 CB VAL A 107 -39.179 39.337 -22.737 1.00100.13 C
ANISOU 717 CB VAL A 107 12637 13280 12126 100 114 -322 C
ATOM 718 CG1 VAL A 107 -38.850 38.543 -23.992 1.00 94.64 C
ANISOU 718 CG1 VAL A 107 11919 12624 11416 51 111 -290 C
ATOM 719 CG2 VAL A 107 -38.920 40.824 -22.937 1.00 96.64 C
ANISOU 719 CG2 VAL A 107 12407 12711 11601 105 53 -300 C
ATOM 720 N LEU A 108 -42.063 38.117 -24.049 1.00103.94 N
ANISOU 720 N LEU A 108 12897 13855 12741 365 -2 -448 N
ATOM 721 CA LEU A 108 -43.006 38.155 -25.153 1.00 85.91 C
ANISOU 721 CA LEU A 108 10624 11555 10462 475 -97 -487 C
ATOM 722 C LEU A 108 -44.406 38.490 -24.645 1.00 84.89 C
ANISOU 722 C LEU A 108 10427 11436 10392 624 -146 -580 C
ATOM 723 O LEU A 108 -44.678 38.500 -23.442 1.00 99.74 O
ANISOU 723 O LEU A 108 12228 13352 12318 635 -94 -611 O
ATOM 724 CB LEU A 108 -43.022 36.816 -25.891 1.00 86.23 C
ANISOU 724 CB LEU A 108 10534 11680 10549 441 -76 -484 C
ATOM 725 CG LEU A 108 -41.748 36.378 -26.615 1.00 81.85 C
ANISOU 725 CG LEU A 108 10035 11131 9935 313 -40 -403 C
ATOM 726 CD1 LEU A 108 -41.839 34.909 -27.004 1.00 68.94 C
ANISOU 726 CD1 LEU A 108 8239 9595 8362 285 -8 -411 C
ATOM 727 CD2 LEU A 108 -41.510 37.242 -27.842 1.00 76.27 C
ANISOU 727 CD2 LEU A 108 9519 10328 9134 334 -122 -368 C
ATOM 728 N SER A 109 -45.303 38.768 -25.586 1.00 78.08 N
ANISOU 728 N SER A 109 9596 10546 9524 746 -250 -630 N
ATOM 729 CA SER A 109 -46.702 38.945 -25.240 1.00 73.28 C
ANISOU 729 CA SER A 109 8896 9967 8979 895 -302 -735 C
ATOM 730 C SER A 109 -47.289 37.624 -24.753 1.00 72.94 C
ANISOU 730 C SER A 109 8609 10053 9054 878 -227 -784 C
ATOM 731 O SER A 109 -46.775 36.540 -25.045 1.00 78.13 O
ANISOU 731 O SER A 109 9184 10765 9738 779 -167 -744 O
ATOM 732 CB SER A 109 -47.492 39.464 -26.441 1.00 74.35 C
ANISOU 732 CB SER A 109 9119 10049 9080 1034 -438 -785 C
ATOM 733 OG SER A 109 -47.488 38.521 -27.499 1.00 78.43 O
ANISOU 733 OG SER A 109 9572 10607 9620 1014 -450 -778 O
ATOM 734 N GLU A 110 -48.379 37.724 -23.988 1.00 77.55 N
ANISOU 734 N GLU A 110 9080 10683 9703 975 -228 -874 N
ATOM 735 CA GLU A 110 -49.026 36.516 -23.486 1.00 83.48 C
ANISOU 735 CA GLU A 110 9603 11551 10565 956 -150 -927 C
ATOM 736 C GLU A 110 -49.522 35.640 -24.629 1.00 77.02 C
ANISOU 736 C GLU A 110 8693 10777 9795 979 -196 -962 C
ATOM 737 O GLU A 110 -49.553 34.411 -24.503 1.00 81.83 O
ANISOU 737 O GLU A 110 9148 11466 10475 904 -120 -963 O
ATOM 738 CB GLU A 110 -50.176 36.884 -22.548 1.00 77.78 C
ANISOU 738 CB GLU A 110 8782 10872 9900 1063 -148 -1027 C
ATOM 739 CG GLU A 110 -50.800 35.694 -21.836 1.00 89.89 C
ANISOU 739 CG GLU A 110 10087 12523 11544 1025 -44 -1079 C
ATOM 740 CD GLU A 110 -51.921 36.094 -20.898 1.00110.35 C
ANISOU 740 CD GLU A 110 12578 15162 14186 1128 -33 -1180 C
ATOM 741 OE1 GLU A 110 -52.169 37.309 -20.748 1.00112.05 O
ANISOU 741 OE1 GLU A 110 12906 15321 14348 1234 -110 -1208 O
ATOM 742 OE2 GLU A 110 -52.555 35.191 -20.312 1.00137.47 O
ANISOU 742 OE2 GLU A 110 15827 18694 17712 1101 54 -1232 O
ATOM 743 N ASP A 111 -49.894 36.252 -25.755 1.00 83.00 N
ANISOU 743 N ASP A 111 9552 11476 10509 1083 -322 -989 N
ATOM 744 CA ASP A 111 -50.331 35.481 -26.914 1.00 86.50 C
ANISOU 744 CA ASP A 111 9923 11952 10989 1116 -378 -1023 C
ATOM 745 C ASP A 111 -49.163 34.738 -27.553 1.00 84.53 C
ANISOU 745 C ASP A 111 9718 11696 10703 983 -336 -919 C
ATOM 746 O ASP A 111 -49.271 33.549 -27.873 1.00 89.41 O
ANISOU 746 O ASP A 111 10200 12385 11386 937 -304 -927 O
ATOM 747 CB ASP A 111 -51.004 36.404 -27.930 1.00 81.22 C
ANISOU 747 CB ASP A 111 9375 11215 10271 1277 -532 -1082 C
ATOM 748 CG ASP A 111 -51.564 35.653 -29.122 1.00 80.38 C
ANISOU 748 CG ASP A 111 9192 11142 10207 1334 -603 -1132 C
ATOM 749 OD1 ASP A 111 -52.560 34.921 -28.949 1.00 82.51 O
ANISOU 749 OD1 ASP A 111 9260 11505 10586 1376 -596 -1230 O
ATOM 750 OD2 ASP A 111 -51.012 35.799 -30.232 1.00 84.71 O
ANISOU 750 OD2 ASP A 111 9882 11623 10678 1334 -665 -1077 O
ATOM 751 N LYS A 112 -48.033 35.425 -27.746 1.00 74.07 N
ANISOU 751 N LYS A 112 8582 10289 9273 918 -334 -824 N
ATOM 752 CA LYS A 112 -46.895 34.798 -28.411 1.00 71.77 C
ANISOU 752 CA LYS A 112 8337 9996 8937 798 -298 -731 C
ATOM 753 C LYS A 112 -46.223 33.757 -27.525 1.00 75.97 C
ANISOU 753 C LYS A 112 8745 10606 9515 659 -168 -690 C
ATOM 754 O LYS A 112 -45.735 32.739 -28.031 1.00 76.71 O
ANISOU 754 O LYS A 112 8782 10745 9618 585 -138 -654 O
ATOM 755 CB LYS A 112 -45.884 35.858 -28.842 1.00 71.91 C
ANISOU 755 CB LYS A 112 8586 9907 8829 759 -326 -649 C
ATOM 756 CG LYS A 112 -46.362 36.725 -29.992 1.00 74.08 C
ANISOU 756 CG LYS A 112 9017 10093 9037 884 -456 -673 C
ATOM 757 CD LYS A 112 -45.252 37.618 -30.511 1.00 73.13 C
ANISOU 757 CD LYS A 112 9131 9867 8788 817 -467 -580 C
ATOM 758 CE LYS A 112 -45.711 38.408 -31.723 1.00 77.67 C
ANISOU 758 CE LYS A 112 9880 10346 9286 941 -596 -599 C
ATOM 759 NZ LYS A 112 -44.626 39.266 -32.266 1.00 88.09 N
ANISOU 759 NZ LYS A 112 11439 11557 10475 864 -596 -505 N
ATOM 760 N SER A 113 -46.177 33.989 -26.211 1.00 73.96 N
ANISOU 760 N SER A 113 8455 10366 9282 630 -94 -695 N
ATOM 761 CA SER A 113 -45.629 32.976 -25.316 1.00 81.30 C
ANISOU 761 CA SER A 113 9272 11367 10253 514 26 -666 C
ATOM 762 C SER A 113 -46.518 31.740 -25.272 1.00 78.61 C
ANISOU 762 C SER A 113 8734 11116 10017 527 54 -728 C
ATOM 763 O SER A 113 -46.010 30.616 -25.180 1.00 76.08 O
ANISOU 763 O SER A 113 8339 10850 9720 432 122 -696 O
ATOM 764 CB SER A 113 -45.438 33.553 -23.912 1.00 80.28 C
ANISOU 764 CB SER A 113 9159 11225 10118 494 93 -663 C
ATOM 765 OG SER A 113 -46.682 33.805 -23.283 1.00 88.47 O
ANISOU 765 OG SER A 113 10107 12288 11221 596 84 -750 O
ATOM 766 N LYS A 114 -47.838 31.924 -25.347 1.00 71.69 N
ANISOU 766 N LYS A 114 7776 10258 9206 643 1 -823 N
ATOM 767 CA LYS A 114 -48.741 30.780 -25.415 1.00 70.75 C
ANISOU 767 CA LYS A 114 7468 10223 9191 652 22 -891 C
ATOM 768 C LYS A 114 -48.586 30.036 -26.736 1.00 80.57 C
ANISOU 768 C LYS A 114 8704 11475 10434 643 -37 -876 C
ATOM 769 O LYS A 114 -48.694 28.805 -26.777 1.00 81.44 O
ANISOU 769 O LYS A 114 8688 11648 10607 584 9 -884 O
ATOM 770 CB LYS A 114 -50.185 31.237 -25.211 1.00 71.61 C
ANISOU 770 CB LYS A 114 7486 10356 9368 783 -27 -1008 C
ATOM 771 CG LYS A 114 -50.580 31.395 -23.751 1.00 91.26 C
ANISOU 771 CG LYS A 114 9898 12880 11896 775 66 -1043 C
ATOM 772 CD LYS A 114 -51.784 32.312 -23.585 1.00 89.01 C
ANISOU 772 CD LYS A 114 9584 12598 11639 923 -4 -1150 C
ATOM 773 CE LYS A 114 -52.972 31.843 -24.405 1.00 79.20 C
ANISOU 773 CE LYS A 114 8204 11409 10478 1010 -76 -1257 C
ATOM 774 NZ LYS A 114 -54.142 32.748 -24.232 1.00 85.45 N
ANISOU 774 NZ LYS A 114 8963 12213 11293 1165 -149 -1374 N
ATOM 775 N ARG A 115 -48.334 30.766 -27.827 1.00 93.46 N
ANISOU 775 N ARG A 115 10478 13039 11992 701 -139 -853 N
ATOM 776 CA ARG A 115 -48.035 30.108 -29.096 1.00 74.23 C
ANISOU 776 CA ARG A 115 8058 10607 9541 691 -192 -826 C
ATOM 777 C ARG A 115 -46.719 29.347 -29.020 1.00 77.27 C
ANISOU 777 C ARG A 115 8466 11011 9882 547 -112 -728 C
ATOM 778 O ARG A 115 -46.615 28.224 -29.525 1.00 73.78 O
ANISOU 778 O ARG A 115 7944 10617 9472 506 -104 -722 O
ATOM 779 CB ARG A 115 -47.982 31.131 -30.231 1.00 71.00 C
ANISOU 779 CB ARG A 115 7822 10111 9045 784 -311 -816 C
ATOM 780 CG ARG A 115 -49.297 31.818 -30.550 1.00 77.33 C
ANISOU 780 CG ARG A 115 8611 10893 9879 949 -418 -924 C
ATOM 781 CD ARG A 115 -49.190 32.566 -31.871 1.00 79.78 C
ANISOU 781 CD ARG A 115 9100 11116 10097 1039 -540 -909 C
ATOM 782 NE ARG A 115 -50.344 33.418 -32.131 1.00 97.88 N
ANISOU 782 NE ARG A 115 11418 13373 12397 1211 -654 -1012 N
ATOM 783 CZ ARG A 115 -50.587 34.010 -33.292 1.00109.58 C
ANISOU 783 CZ ARG A 115 13037 14783 13813 1328 -779 -1032 C
ATOM 784 NH1 ARG A 115 -49.790 33.841 -34.334 1.00130.31 N
ANISOU 784 NH1 ARG A 115 15784 17366 16362 1289 -803 -953 N
ATOM 785 NH2 ARG A 115 -51.659 34.788 -33.413 1.00101.30 N
ANISOU 785 NH2 ARG A 115 12010 13708 12771 1493 -884 -1136 N
ATOM 786 N LEU A 116 -45.703 29.943 -28.390 1.00 73.25 N
ANISOU 786 N LEU A 116 8065 10466 9300 473 -55 -658 N
ATOM 787 CA LEU A 116 -44.395 29.301 -28.317 1.00 67.66 C
ANISOU 787 CA LEU A 116 7383 9781 8544 344 16 -575 C
ATOM 788 C LEU A 116 -44.447 28.028 -27.480 1.00 76.32 C
ANISOU 788 C LEU A 116 8326 10957 9713 273 108 -589 C
ATOM 789 O LEU A 116 -43.869 27.005 -27.865 1.00 74.85 O
ANISOU 789 O LEU A 116 8106 10813 9521 207 129 -556 O
ATOM 790 CB LEU A 116 -43.364 30.280 -27.755 1.00 67.46 C
ANISOU 790 CB LEU A 116 7497 9701 8432 284 53 -513 C
ATOM 791 CG LEU A 116 -41.920 29.784 -27.648 1.00 66.52 C
ANISOU 791 CG LEU A 116 7413 9607 8254 154 122 -436 C
ATOM 792 CD1 LEU A 116 -41.440 29.230 -28.978 1.00 66.33 C
ANISOU 792 CD1 LEU A 116 7417 9596 8188 135 77 -401 C
ATOM 793 CD2 LEU A 116 -41.006 30.905 -27.177 1.00 66.55 C
ANISOU 793 CD2 LEU A 116 7557 9551 8177 104 145 -388 C
ATOM 794 N ASN A 117 -45.138 28.066 -26.337 1.00 79.45 N
ANISOU 794 N ASN A 117 8639 11376 10174 288 164 -638 N
ATOM 795 CA ASN A 117 -45.240 26.872 -25.503 1.00 83.23 C
ANISOU 795 CA ASN A 117 8988 11921 10716 220 258 -651 C
ATOM 796 C ASN A 117 -46.045 25.774 -26.187 1.00 81.98 C
ANISOU 796 C ASN A 117 8701 11811 10636 239 230 -701 C
ATOM 797 O ASN A 117 -45.808 24.587 -25.937 1.00 89.90 O
ANISOU 797 O ASN A 117 9632 12861 11666 164 290 -689 O
ATOM 798 CB ASN A 117 -45.858 27.222 -24.148 1.00 82.45 C
ANISOU 798 CB ASN A 117 8834 11830 10663 237 328 -695 C
ATOM 799 CG ASN A 117 -44.969 28.131 -23.319 1.00 89.08 C
ANISOU 799 CG ASN A 117 9792 12626 11429 206 367 -644 C
ATOM 800 OD1 ASN A 117 -43.758 28.203 -23.534 1.00 86.73 O
ANISOU 800 OD1 ASN A 117 9591 12308 11054 138 373 -575 O
ATOM 801 ND2 ASN A 117 -45.568 28.827 -22.359 1.00 90.42 N
ANISOU 801 ND2 ASN A 117 9950 12785 11622 255 393 -685 N
ATOM 802 N THR A 118 -46.994 26.145 -27.051 1.00 70.36 N
ANISOU 802 N THR A 118 7206 10327 9199 342 134 -761 N
ATOM 803 CA THR A 118 -47.751 25.143 -27.794 1.00 77.55 C
ANISOU 803 CA THR A 118 7998 11282 10187 365 94 -815 C
ATOM 804 C THR A 118 -46.894 24.496 -28.875 1.00 75.84 C
ANISOU 804 C THR A 118 7836 11064 9917 326 52 -754 C
ATOM 805 O THR A 118 -46.987 23.284 -29.108 1.00 77.74 O
ANISOU 805 O THR A 118 7985 11350 10203 284 66 -764 O
ATOM 806 CB THR A 118 -49.002 25.775 -28.408 1.00 71.79 C
ANISOU 806 CB THR A 118 7230 10541 9507 500 -7 -909 C
ATOM 807 OG1 THR A 118 -49.815 26.338 -27.371 1.00 72.28 O
ANISOU 807 OG1 THR A 118 7230 10617 9619 540 34 -973 O
ATOM 808 CG2 THR A 118 -49.812 24.735 -29.167 1.00 69.57 C
ANISOU 808 CG2 THR A 118 6813 10306 9312 525 -53 -975 C
ATOM 809 N ILE A 119 -46.054 25.288 -29.546 1.00 69.86 N
ANISOU 809 N ILE A 119 7230 10254 9058 338 2 -692 N
ATOM 810 CA ILE A 119 -45.146 24.734 -30.546 1.00 69.61 C
ANISOU 810 CA ILE A 119 7258 10227 8964 298 -29 -631 C
ATOM 811 C ILE A 119 -44.153 23.783 -29.892 1.00 73.86 C
ANISOU 811 C ILE A 119 7771 10810 9482 176 66 -576 C
ATOM 812 O ILE A 119 -43.854 22.708 -30.427 1.00 74.96 O
ANISOU 812 O ILE A 119 7870 10988 9624 142 58 -562 O
ATOM 813 CB ILE A 119 -44.430 25.871 -31.300 1.00 66.87 C
ANISOU 813 CB ILE A 119 7086 9812 8507 324 -86 -576 C
ATOM 814 CG1 ILE A 119 -45.441 26.725 -32.066 1.00 67.94 C
ANISOU 814 CG1 ILE A 119 7262 9897 8654 460 -196 -635 C
ATOM 815 CG2 ILE A 119 -43.381 25.313 -32.248 1.00 66.29 C
ANISOU 815 CG2 ILE A 119 7074 9753 8361 272 -102 -508 C
ATOM 816 CD1 ILE A 119 -44.846 27.977 -32.660 1.00 68.28 C
ANISOU 816 CD1 ILE A 119 7499 9858 8586 488 -245 -584 C
ATOM 817 N LEU A 120 -43.636 24.158 -28.718 1.00 71.51 N
ANISOU 817 N LEU A 120 7502 10507 9160 118 151 -550 N
ATOM 818 CA LEU A 120 -42.661 23.319 -28.029 1.00 64.48 C
ANISOU 818 CA LEU A 120 6601 9657 8241 14 237 -506 C
ATOM 819 C LEU A 120 -43.276 21.996 -27.588 1.00 66.50 C
ANISOU 819 C LEU A 120 6723 9963 8580 -14 282 -546 C
ATOM 820 O LEU A 120 -42.641 20.942 -27.707 1.00 72.92 O
ANISOU 820 O LEU A 120 7522 10812 9372 -74 303 -519 O
ATOM 821 CB LEU A 120 -42.086 24.069 -26.828 1.00 64.26 C
ANISOU 821 CB LEU A 120 6633 9608 8176 -28 311 -482 C
ATOM 822 CG LEU A 120 -41.280 25.330 -27.140 1.00 64.34 C
ANISOU 822 CG LEU A 120 6786 9565 8095 -28 280 -434 C
ATOM 823 CD1 LEU A 120 -41.027 26.132 -25.875 1.00 64.33 C
ANISOU 823 CD1 LEU A 120 6827 9537 8079 -50 344 -430 C
ATOM 824 CD2 LEU A 120 -39.971 24.971 -27.822 1.00 63.74 C
ANISOU 824 CD2 LEU A 120 6775 9509 7933 -97 277 -373 C
ATOM 825 N ASN A 121 -44.508 22.029 -27.075 1.00 65.02 N
ANISOU 825 N ASN A 121 6440 9781 8486 28 298 -615 N
ATOM 826 CA ASN A 121 -45.149 20.796 -26.632 1.00 76.79 C
ANISOU 826 CA ASN A 121 7806 11314 10058 -10 350 -657 C
ATOM 827 C ASN A 121 -45.495 19.897 -27.811 1.00 75.64 C
ANISOU 827 C ASN A 121 7602 11189 9947 8 276 -678 C
ATOM 828 O ASN A 121 -45.399 18.668 -27.710 1.00 80.62 O
ANISOU 828 O ASN A 121 8180 11852 10601 -51 310 -676 O
ATOM 829 CB ASN A 121 -46.400 21.115 -25.813 1.00 68.44 C
ANISOU 829 CB ASN A 121 6652 10263 9090 26 391 -732 C
ATOM 830 CG ASN A 121 -46.071 21.647 -24.434 1.00 83.69 C
ANISOU 830 CG ASN A 121 8622 12182 10994 -7 486 -713 C
ATOM 831 OD1 ASN A 121 -45.070 21.261 -23.829 1.00 94.18 O
ANISOU 831 OD1 ASN A 121 10007 13512 12264 -80 550 -657 O
ATOM 832 ND2 ASN A 121 -46.914 22.538 -23.927 1.00100.23 N
ANISOU 832 ND2 ASN A 121 10688 14266 13128 56 491 -764 N
ATOM 833 N THR A 122 -45.896 20.488 -28.937 1.00 75.41 N
ANISOU 833 N THR A 122 7594 11140 9919 96 170 -700 N
ATOM 834 CA THR A 122 -46.246 19.684 -30.102 1.00 69.39 C
ANISOU 834 CA THR A 122 6781 10395 9190 126 89 -724 C
ATOM 835 C THR A 122 -45.019 18.995 -30.687 1.00 68.86 C
ANISOU 835 C THR A 122 6786 10340 9038 72 78 -650 C
ATOM 836 O THR A 122 -45.073 17.809 -31.029 1.00 71.78 O
ANISOU 836 O THR A 122 7097 10740 9438 44 67 -658 O
ATOM 837 CB THR A 122 -46.930 20.551 -31.158 1.00 66.65 C
ANISOU 837 CB THR A 122 6456 10016 8851 246 -27 -767 C
ATOM 838 OG1 THR A 122 -47.986 21.302 -30.548 1.00 78.57 O
ANISOU 838 OG1 THR A 122 7908 11519 10427 305 -19 -840 O
ATOM 839 CG2 THR A 122 -47.517 19.679 -32.258 1.00 70.34 C
ANISOU 839 CG2 THR A 122 6849 10505 9374 290 -112 -813 C
ATOM 840 N MET A 123 -43.901 19.717 -30.800 1.00 64.52 N
ANISOU 840 N MET A 123 6363 9769 8383 56 80 -580 N
ATOM 841 CA MET A 123 -42.687 19.110 -31.336 1.00 72.14 C
ANISOU 841 CA MET A 123 7390 10758 9262 6 72 -516 C
ATOM 842 C MET A 123 -42.167 18.012 -30.417 1.00 73.81 C
ANISOU 842 C MET A 123 7562 11008 9472 -84 158 -501 C
ATOM 843 O MET A 123 -41.664 16.985 -30.888 1.00 73.34 O
ANISOU 843 O MET A 123 7497 10981 9386 -112 139 -483 O
ATOM 844 CB MET A 123 -41.614 20.175 -31.562 1.00 68.99 C
ANISOU 844 CB MET A 123 7128 10332 8754 -5 69 -453 C
ATOM 845 CG MET A 123 -41.972 21.200 -32.625 1.00 73.61 C
ANISOU 845 CG MET A 123 7785 10867 9314 83 -21 -457 C
ATOM 846 SD MET A 123 -40.550 22.156 -33.190 1.00 76.03 S
ANISOU 846 SD MET A 123 8262 11148 9480 48 -26 -374 S
ATOM 847 CE MET A 123 -39.977 22.869 -31.652 1.00 63.67 C
ANISOU 847 CE MET A 123 6728 9570 7894 -28 79 -354 C
ATOM 848 N SER A 124 -42.277 18.211 -29.102 1.00 79.66 N
ANISOU 848 N SER A 124 8286 11745 10237 -124 248 -510 N
ATOM 849 CA SER A 124 -41.883 17.163 -28.167 1.00 81.00 C
ANISOU 849 CA SER A 124 8430 11942 10404 -201 330 -502 C
ATOM 850 C SER A 124 -42.827 15.971 -28.254 1.00 83.75 C
ANISOU 850 C SER A 124 8672 12308 10842 -209 328 -551 C
ATOM 851 O SER A 124 -42.397 14.819 -28.119 1.00 90.49 O
ANISOU 851 O SER A 124 9522 13184 11676 -260 350 -538 O
ATOM 852 CB SER A 124 -41.844 17.717 -26.744 1.00 72.07 C
ANISOU 852 CB SER A 124 7314 10796 9275 -232 426 -504 C
ATOM 853 OG SER A 124 -41.478 16.711 -25.816 1.00 91.16 O
ANISOU 853 OG SER A 124 9721 13233 11682 -298 505 -498 O
ATOM 854 N THR A 125 -44.117 16.228 -28.485 1.00 78.42 N
ANISOU 854 N THR A 125 7910 11622 10263 -157 299 -614 N
ATOM 855 CA THR A 125 -45.077 15.139 -28.630 1.00 71.52 C
ANISOU 855 CA THR A 125 6926 10765 9484 -169 294 -670 C
ATOM 856 C THR A 125 -44.872 14.396 -29.944 1.00 77.15 C
ANISOU 856 C THR A 125 7640 11491 10183 -145 196 -663 C
ATOM 857 O THR A 125 -44.935 13.162 -29.982 1.00 74.19 O
ANISOU 857 O THR A 125 7225 11132 9832 -190 203 -672 O
ATOM 858 CB THR A 125 -46.503 15.681 -28.537 1.00 65.21 C
ANISOU 858 CB THR A 125 6023 9960 8792 -116 286 -751 C
ATOM 859 OG1 THR A 125 -46.690 16.320 -27.268 1.00 70.20 O
ANISOU 859 OG1 THR A 125 6654 10586 9435 -137 381 -759 O
ATOM 860 CG2 THR A 125 -47.516 14.556 -28.685 1.00 66.33 C
ANISOU 860 CG2 THR A 125 6038 10124 9040 -140 286 -818 C
ATOM 861 N ILE A 126 -44.625 15.131 -31.031 1.00 77.95 N
ANISOU 861 N ILE A 126 7796 11581 10240 -72 103 -646 N
ATOM 862 CA ILE A 126 -44.369 14.493 -32.320 1.00 68.43 C
ANISOU 862 CA ILE A 126 6603 10388 9009 -39 6 -635 C
ATOM 863 C ILE A 126 -43.120 13.626 -32.245 1.00 72.84 C
ANISOU 863 C ILE A 126 7224 10973 9478 -104 32 -574 C
ATOM 864 O ILE A 126 -43.073 12.526 -32.810 1.00 68.53 O
ANISOU 864 O ILE A 126 6654 10446 8937 -110 -12 -579 O
ATOM 865 CB ILE A 126 -44.259 15.556 -33.429 1.00 64.56 C
ANISOU 865 CB ILE A 126 6184 9874 8472 52 -87 -622 C
ATOM 866 CG1 ILE A 126 -45.620 16.205 -33.683 1.00 65.18 C
ANISOU 866 CG1 ILE A 126 6192 9929 8643 138 -138 -701 C
ATOM 867 CG2 ILE A 126 -43.711 14.947 -34.711 1.00 76.58 C
ANISOU 867 CG2 ILE A 126 7746 11411 9939 82 -175 -594 C
ATOM 868 CD1 ILE A 126 -45.590 17.287 -34.734 1.00 65.54 C
ANISOU 868 CD1 ILE A 126 6326 9939 8637 237 -233 -693 C
ATOM 869 N TYR A 127 -42.096 14.094 -31.531 1.00 71.75 N
ANISOU 869 N TYR A 127 7167 10839 9256 -149 97 -522 N
ATOM 870 CA TYR A 127 -40.843 13.349 -31.460 1.00 71.18 C
ANISOU 870 CA TYR A 127 7155 10800 9090 -200 115 -473 C
ATOM 871 C TYR A 127 -40.997 12.091 -30.612 1.00 74.44 C
ANISOU 871 C TYR A 127 7526 11223 9534 -262 174 -492 C
ATOM 872 O TYR A 127 -40.555 11.006 -31.008 1.00 73.07 O
ANISOU 872 O TYR A 127 7364 11074 9327 -276 142 -482 O
ATOM 873 CB TYR A 127 -39.737 14.247 -30.907 1.00 65.82 C
ANISOU 873 CB TYR A 127 6566 10124 8318 -229 166 -425 C
ATOM 874 CG TYR A 127 -38.370 13.604 -30.890 1.00 60.72 C
ANISOU 874 CG TYR A 127 5980 9523 7567 -272 177 -386 C
ATOM 875 CD1 TYR A 127 -37.541 13.661 -32.002 1.00 68.26 C
ANISOU 875 CD1 TYR A 127 6986 10509 8441 -249 112 -353 C
ATOM 876 CD2 TYR A 127 -37.905 12.947 -29.760 1.00 60.18 C
ANISOU 876 CD2 TYR A 127 5921 9469 7477 -328 252 -386 C
ATOM 877 CE1 TYR A 127 -36.289 13.076 -31.989 1.00 66.25 C
ANISOU 877 CE1 TYR A 127 6776 10307 8089 -283 120 -327 C
ATOM 878 CE2 TYR A 127 -36.656 12.360 -29.738 1.00 68.17 C
ANISOU 878 CE2 TYR A 127 6986 10527 8389 -355 253 -362 C
ATOM 879 CZ TYR A 127 -35.852 12.427 -30.855 1.00 70.28 C
ANISOU 879 CZ TYR A 127 7290 10833 8580 -332 186 -335 C
ATOM 880 OH TYR A 127 -34.606 11.844 -30.836 1.00 72.58 O
ANISOU 880 OH TYR A 127 7624 11182 8770 -354 185 -322 O
ATOM 881 N SER A 128 -41.632 12.213 -29.444 1.00 74.57 N
ANISOU 881 N SER A 128 7502 11219 9612 -298 261 -519 N
ATOM 882 CA SER A 128 -41.757 11.083 -28.529 1.00 78.16 C
ANISOU 882 CA SER A 128 7939 11673 10087 -364 332 -532 C
ATOM 883 C SER A 128 -42.824 10.084 -28.963 1.00 73.45 C
ANISOU 883 C SER A 128 7252 11071 9586 -369 301 -582 C
ATOM 884 O SER A 128 -42.742 8.908 -28.595 1.00 78.01 O
ANISOU 884 O SER A 128 7835 11646 10159 -423 331 -585 O
ATOM 885 CB SER A 128 -42.062 11.584 -27.115 1.00 69.47 C
ANISOU 885 CB SER A 128 6833 10551 9012 -400 444 -543 C
ATOM 886 OG SER A 128 -43.267 12.329 -27.090 1.00 69.05 O
ANISOU 886 OG SER A 128 6697 10481 9056 -367 448 -590 O
ATOM 887 N THR A 129 -43.828 10.520 -29.727 1.00 67.89 N
ANISOU 887 N THR A 129 6468 10360 8967 -314 239 -627 N
ATOM 888 CA THR A 129 -44.899 9.634 -30.161 1.00 73.53 C
ANISOU 888 CA THR A 129 7083 11072 9784 -319 205 -686 C
ATOM 889 C THR A 129 -44.835 9.272 -31.637 1.00 80.15 C
ANISOU 889 C THR A 129 7918 11921 10614 -256 76 -689 C
ATOM 890 O THR A 129 -45.612 8.418 -32.079 1.00 70.64 O
ANISOU 890 O THR A 129 6637 10714 9488 -260 35 -739 O
ATOM 891 CB THR A 129 -46.273 10.257 -29.867 1.00 69.62 C
ANISOU 891 CB THR A 129 6477 10568 9409 -300 231 -759 C
ATOM 892 OG1 THR A 129 -46.436 11.453 -30.640 1.00 66.91 O
ANISOU 892 OG1 THR A 129 6138 10223 9063 -204 153 -767 O
ATOM 893 CG2 THR A 129 -46.404 10.592 -28.390 1.00 80.92 C
ANISOU 893 CG2 THR A 129 7908 11990 10849 -358 362 -759 C
ATOM 894 N GLY A 130 -43.943 9.893 -32.407 1.00 76.08 N
ANISOU 894 N GLY A 130 8872 10455 9581 -595 -639 -870 N
ATOM 895 CA GLY A 130 -43.825 9.600 -33.822 1.00 71.90 C
ANISOU 895 CA GLY A 130 8300 9959 9060 -618 -690 -934 C
ATOM 896 C GLY A 130 -43.469 8.155 -34.098 1.00 80.33 C
ANISOU 896 C GLY A 130 9430 10912 10179 -762 -662 -970 C
ATOM 897 O GLY A 130 -42.422 7.671 -33.658 1.00 87.83 O
ANISOU 897 O GLY A 130 10518 11692 11161 -769 -642 -916 O
ATOM 898 N LYS A 131 -44.337 7.456 -34.822 1.00 79.12 N
ANISOU 898 N LYS A 131 9176 10851 10034 -875 -663 -1068 N
ATOM 899 CA LYS A 131 -44.142 6.051 -35.136 1.00 90.11 C
ANISOU 899 CA LYS A 131 10626 12132 11480 -1025 -633 -1121 C
ATOM 900 C LYS A 131 -44.073 5.855 -36.645 1.00 90.57 C
ANISOU 900 C LYS A 131 10651 12244 11515 -1012 -714 -1216 C
ATOM 901 O LYS A 131 -44.676 6.607 -37.417 1.00 87.44 O
ANISOU 901 O LYS A 131 10135 12024 11064 -930 -781 -1267 O
ATOM 902 CB LYS A 131 -45.263 5.184 -34.544 1.00 87.99 C
ANISOU 902 CB LYS A 131 10274 11893 11264 -1202 -549 -1169 C
ATOM 903 CG LYS A 131 -46.653 5.502 -35.070 1.00 96.92 C
ANISOU 903 CG LYS A 131 11192 13251 12382 -1242 -584 -1266 C
ATOM 904 CD LYS A 131 -47.710 4.661 -34.369 1.00104.60 C
ANISOU 904 CD LYS A 131 12072 14238 13434 -1426 -482 -1296 C
ATOM 905 CE LYS A 131 -49.099 4.921 -34.934 1.00119.96 C
ANISOU 905 CE LYS A 131 13778 16422 15378 -1474 -526 -1404 C
ATOM 906 NZ LYS A 131 -49.205 4.519 -36.364 1.00118.69 N
ANISOU 906 NZ LYS A 131 13557 16328 15213 -1517 -636 -1553 N
ATOM 907 N VAL A 132 -43.323 4.835 -37.052 1.00 99.05 N
ANISOU 907 N VAL A 132 11846 13169 12621 -1075 -706 -1235 N
ATOM 908 CA VAL A 132 -43.145 4.477 -38.453 1.00 85.07 C
ANISOU 908 CA VAL A 132 10080 11422 10820 -1056 -778 -1325 C
ATOM 909 C VAL A 132 -43.585 3.032 -38.630 1.00 88.48 C
ANISOU 909 C VAL A 132 10526 11782 11308 -1253 -747 -1435 C
ATOM 910 O VAL A 132 -43.110 2.142 -37.915 1.00 93.10 O
ANISOU 910 O VAL A 132 11235 12187 11951 -1348 -661 -1389 O
ATOM 911 CB VAL A 132 -41.686 4.668 -38.907 1.00 74.95 C
ANISOU 911 CB VAL A 132 8947 10012 9519 -918 -796 -1239 C
ATOM 912 CG1 VAL A 132 -41.415 3.859 -40.158 1.00 88.55 C
ANISOU 912 CG1 VAL A 132 10725 11704 11217 -927 -838 -1327 C
ATOM 913 CG2 VAL A 132 -41.395 6.141 -39.145 1.00 76.09 C
ANISOU 913 CG2 VAL A 132 9048 10247 9617 -725 -839 -1165 C
ATOM 914 N CYS A 133 -44.488 2.801 -39.577 1.00 94.42 N
ANISOU 914 N CYS A 133 11155 12675 12044 -1309 -817 -1584 N
ATOM 915 CA CYS A 133 -45.047 1.480 -39.824 1.00105.38 C
ANISOU 915 CA CYS A 133 12532 14007 13502 -1513 -801 -1719 C
ATOM 916 C CYS A 133 -44.384 0.866 -41.050 1.00105.89 C
ANISOU 916 C CYS A 133 12708 14001 13524 -1473 -870 -1800 C
ATOM 917 O CYS A 133 -44.222 1.536 -42.076 1.00 92.13 O
ANISOU 917 O CYS A 133 10938 12380 11685 -1309 -967 -1829 O
ATOM 918 CB CYS A 133 -46.563 1.569 -40.014 1.00107.97 C
ANISOU 918 CB CYS A 133 12627 14544 13852 -1618 -844 -1853 C
ATOM 919 SG CYS A 133 -47.413 2.458 -38.679 1.00138.77 S
ANISOU 919 SG CYS A 133 16385 18565 17777 -1618 -764 -1748 S
ATOM 920 N ASN A 134 -43.989 -0.399 -40.934 1.00113.13 N
ANISOU 920 N ASN A 134 13762 14717 14504 -1607 -809 -1829 N
ATOM 921 CA ASN A 134 -43.353 -1.086 -42.048 1.00121.68 C
ANISOU 921 CA ASN A 134 14974 15715 15543 -1570 -864 -1908 C
ATOM 922 C ASN A 134 -44.337 -1.201 -43.211 1.00127.43 C
ANISOU 922 C ASN A 134 15562 16620 16236 -1604 -992 -2117 C
ATOM 923 O ASN A 134 -45.550 -1.300 -42.989 1.00131.78 O
ANISOU 923 O ASN A 134 15933 17288 16848 -1753 -1006 -2225 O
ATOM 924 CB ASN A 134 -42.863 -2.470 -41.604 1.00121.04 C
ANISOU 924 CB ASN A 134 15069 15377 15543 -1719 -760 -1903 C
ATOM 925 CG ASN A 134 -42.394 -3.337 -42.761 1.00129.34 C
ANISOU 925 CG ASN A 134 16254 16337 16553 -1706 -815 -2015 C
ATOM 926 OD1 ASN A 134 -41.236 -3.268 -43.177 1.00134.37 O
ANISOU 926 OD1 ASN A 134 17046 16891 17118 -1543 -818 -1926 O
ATOM 927 ND2 ASN A 134 -43.291 -4.170 -43.277 1.00134.76 N
ANISOU 927 ND2 ASN A 134 16878 17034 17289 -1878 -857 -2214 N
ATOM 928 N PRO A 135 -43.864 -1.142 -44.457 1.00129.18 N
ANISOU 928 N PRO A 135 15849 16880 16352 -1454 -1088 -2177 N
ATOM 929 CA PRO A 135 -44.780 -1.277 -45.595 1.00138.93 C
ANISOU 929 CA PRO A 135 16959 18296 17533 -1464 -1226 -2392 C
ATOM 930 C PRO A 135 -45.448 -2.643 -45.621 1.00147.46 C
ANISOU 930 C PRO A 135 18030 19278 18722 -1726 -1227 -2580 C
ATOM 931 O PRO A 135 -44.892 -3.644 -45.162 1.00145.21 O
ANISOU 931 O PRO A 135 17910 18746 18515 -1848 -1128 -2548 O
ATOM 932 CB PRO A 135 -43.871 -1.071 -46.814 1.00131.15 C
ANISOU 932 CB PRO A 135 16108 17315 16407 -1226 -1298 -2384 C
ATOM 933 CG PRO A 135 -42.478 -1.275 -46.304 1.00118.82 C
ANISOU 933 CG PRO A 135 14761 15520 14867 -1167 -1184 -2193 C
ATOM 934 CD PRO A 135 -42.502 -0.793 -44.891 1.00116.12 C
ANISOU 934 CD PRO A 135 14367 15138 14614 -1238 -1080 -2042 C
ATOM 935 N ASP A 136 -46.669 -2.663 -46.157 1.00152.11 N
ANISOU 935 N ASP A 136 18416 20063 19317 -1810 -1339 -2779 N
ATOM 936 CA ASP A 136 -47.535 -3.835 -46.275 1.00175.31 C
ANISOU 936 CA ASP A 136 21284 22950 22377 -2076 -1365 -2996 C
ATOM 937 C ASP A 136 -48.047 -4.352 -44.935 1.00174.29 C
ANISOU 937 C ASP A 136 21095 22694 22435 -2332 -1210 -2939 C
ATOM 938 O ASP A 136 -48.663 -5.423 -44.894 1.00182.00 O
ANISOU 938 O ASP A 136 22033 23570 23547 -2579 -1192 -3093 O
ATOM 939 CB ASP A 136 -46.853 -4.979 -47.037 1.00168.77 C
ANISOU 939 CB ASP A 136 20673 21919 21532 -2104 -1391 -3105 C
ATOM 940 CG ASP A 136 -46.689 -4.676 -48.514 1.00162.12 C
ANISOU 940 CG ASP A 136 19854 21232 20512 -1884 -1564 -3231 C
ATOM 941 OD1 ASP A 136 -47.213 -3.639 -48.971 1.00161.19 O
ANISOU 941 OD1 ASP A 136 19568 21386 20292 -1727 -1666 -3252 O
ATOM 942 OD2 ASP A 136 -46.035 -5.473 -49.218 1.00166.03 O
ANISOU 942 OD2 ASP A 136 20546 21578 20960 -1850 -1591 -3304 O
ATOM 943 N ASN A 137 -47.818 -3.634 -43.837 1.00155.49 N
ANISOU 943 N ASN A 137 18707 20306 20067 -2276 -1094 -2724 N
ATOM 944 CA ASN A 137 -48.505 -3.920 -42.576 1.00151.64 C
ANISOU 944 CA ASN A 137 18122 19761 19735 -2480 -953 -2666 C
ATOM 945 C ASN A 137 -48.710 -2.613 -41.824 1.00153.21 C
ANISOU 945 C ASN A 137 18206 20127 19881 -2343 -922 -2502 C
ATOM 946 O ASN A 137 -47.843 -2.172 -41.060 1.00146.03 O
ANISOU 946 O ASN A 137 17434 19115 18937 -2226 -832 -2302 O
ATOM 947 CB ASN A 137 -47.757 -4.945 -41.719 1.00140.69 C
ANISOU 947 CB ASN A 137 16956 18055 18445 -2597 -778 -2558 C
ATOM 948 CG ASN A 137 -46.249 -4.778 -41.759 1.00144.31 C
ANISOU 948 CG ASN A 137 17669 18370 18793 -2393 -753 -2399 C
ATOM 949 OD1 ASN A 137 -45.727 -3.674 -41.642 1.00147.24 O
ANISOU 949 OD1 ASN A 137 18043 18842 19060 -2184 -780 -2262 O
ATOM 950 ND2 ASN A 137 -45.540 -5.890 -41.917 1.00142.00 N
ANISOU 950 ND2 ASN A 137 17588 17836 18531 -2455 -695 -2417 N
ATOM 951 N PRO A 138 -49.867 -1.962 -42.014 1.00162.27 N
ANISOU 951 N PRO A 138 19097 21538 21022 -2350 -1000 -2588 N
ATOM 952 CA PRO A 138 -50.134 -0.705 -41.297 1.00164.02 C
ANISOU 952 CA PRO A 138 19212 21919 21188 -2213 -966 -2437 C
ATOM 953 C PRO A 138 -50.218 -0.877 -39.785 1.00166.72 C
ANISOU 953 C PRO A 138 19578 22130 21638 -2320 -784 -2281 C
ATOM 954 O PRO A 138 -50.423 0.105 -39.064 1.00185.25 O
ANISOU 954 O PRO A 138 21859 24586 23942 -2211 -744 -2152 O
ATOM 955 CB PRO A 138 -51.480 -0.249 -41.881 1.00162.87 C
ANISOU 955 CB PRO A 138 18779 22078 21028 -2231 -1083 -2593 C
ATOM 956 CG PRO A 138 -51.584 -0.948 -43.202 1.00163.51 C
ANISOU 956 CG PRO A 138 18852 22187 21087 -2275 -1229 -2819 C
ATOM 957 CD PRO A 138 -50.933 -2.279 -42.977 1.00162.92 C
ANISOU 957 CD PRO A 138 18978 21800 21126 -2453 -1139 -2835 C
ATOM 958 N GLN A 139 -50.062 -2.108 -39.291 1.00151.19 N
ANISOU 958 N GLN A 139 17717 19926 19801 -2518 -665 -2288 N
ATOM 959 CA GLN A 139 -50.113 -2.388 -37.862 1.00152.05 C
ANISOU 959 CA GLN A 139 17872 19896 20006 -2606 -474 -2134 C
ATOM 960 C GLN A 139 -48.750 -2.636 -37.234 1.00144.48 C
ANISOU 960 C GLN A 139 17193 18693 19010 -2512 -377 -1967 C
ATOM 961 O GLN A 139 -48.577 -2.358 -36.045 1.00144.35 O
ANISOU 961 O GLN A 139 17229 18622 18997 -2466 -254 -1802 O
ATOM 962 CB GLN A 139 -51.015 -3.599 -37.588 1.00151.38 C
ANISOU 962 CB GLN A 139 17693 19713 20112 -2898 -371 -2238 C
ATOM 963 CG GLN A 139 -52.463 -3.417 -38.029 1.00146.86 C
ANISOU 963 CG GLN A 139 16805 19387 19608 -3019 -451 -2401 C
ATOM 964 CD GLN A 139 -52.667 -3.695 -39.507 1.00151.53 C
ANISOU 964 CD GLN A 139 17326 20077 20171 -3051 -647 -2641 C
ATOM 965 OE1 GLN A 139 -52.340 -4.776 -39.996 1.00153.71 O
ANISOU 965 OE1 GLN A 139 17722 20165 20515 -3183 -652 -2756 O
ATOM 966 NE2 GLN A 139 -53.206 -2.717 -40.226 1.00152.97 N
ANISOU 966 NE2 GLN A 139 17325 20554 20241 -2913 -807 -2718 N
ATOM 967 N GLU A 140 -47.779 -3.150 -37.993 1.00130.66 N
ANISOU 967 N GLU A 140 15624 16805 17215 -2470 -430 -2006 N
ATOM 968 CA GLU A 140 -46.430 -3.387 -37.473 1.00124.08 C
ANISOU 968 CA GLU A 140 15048 15758 16341 -2366 -349 -1851 C
ATOM 969 C GLU A 140 -45.649 -2.078 -37.551 1.00112.73 C
ANISOU 969 C GLU A 140 13640 14427 14766 -2109 -434 -1736 C
ATOM 970 O GLU A 140 -44.897 -1.810 -38.491 1.00114.09 O
ANISOU 970 O GLU A 140 13887 14611 14852 -1976 -536 -1757 O
ATOM 971 CB GLU A 140 -45.737 -4.505 -38.244 1.00123.80 C
ANISOU 971 CB GLU A 140 15190 15530 16318 -2423 -359 -1934 C
ATOM 972 CG GLU A 140 -44.346 -4.861 -37.721 1.00127.61 C
ANISOU 972 CG GLU A 140 15933 15793 16759 -2316 -268 -1774 C
ATOM 973 CD GLU A 140 -43.607 -5.834 -38.625 1.00137.66 C
ANISOU 973 CD GLU A 140 17386 16900 18018 -2329 -292 -1852 C
ATOM 974 OE1 GLU A 140 -44.206 -6.298 -39.618 1.00145.38 O
ANISOU 974 OE1 GLU A 140 18297 17917 19022 -2435 -378 -2042 O
ATOM 975 OE2 GLU A 140 -42.426 -6.133 -38.344 1.00134.36 O
ANISOU 975 OE2 GLU A 140 17177 16319 17555 -2225 -230 -1728 O
ATOM 976 N CYS A 141 -45.838 -1.245 -36.533 1.00100.60 N
ANISOU 976 N CYS A 141 12047 12963 13213 -2036 -381 -1611 N
ATOM 977 CA CYS A 141 -45.222 0.070 -36.467 1.00 98.85 C
ANISOU 977 CA CYS A 141 11837 12836 12884 -1812 -451 -1507 C
ATOM 978 C CYS A 141 -44.132 0.086 -35.404 1.00 95.91 C
ANISOU 978 C CYS A 141 11648 12296 12496 -1722 -364 -1340 C
ATOM 979 O CYS A 141 -44.169 -0.682 -34.438 1.00 94.95 O
ANISOU 979 O CYS A 141 11602 12040 12433 -1816 -232 -1282 O
ATOM 980 CB CYS A 141 -46.269 1.147 -36.168 1.00 97.08 C
ANISOU 980 CB CYS A 141 11410 12839 12636 -1769 -478 -1506 C
ATOM 981 SG CYS A 141 -47.730 1.061 -37.236 1.00133.02 S
ANISOU 981 SG CYS A 141 15710 17619 17212 -1885 -574 -1708 S
ATOM 982 N LEU A 142 -43.153 0.968 -35.595 1.00 86.52 N
ANISOU 982 N LEU A 142 10526 11118 11230 -1534 -436 -1263 N
ATOM 983 CA LEU A 142 -42.020 1.088 -34.691 1.00 88.33 C
ANISOU 983 CA LEU A 142 10912 11209 11440 -1430 -386 -1121 C
ATOM 984 C LEU A 142 -41.860 2.534 -34.251 1.00 85.87 C
ANISOU 984 C LEU A 142 10544 11007 11074 -1267 -442 -1044 C
ATOM 985 O LEU A 142 -41.981 3.458 -35.062 1.00 86.31 O
ANISOU 985 O LEU A 142 10509 11194 11091 -1175 -537 -1078 O
ATOM 986 CB LEU A 142 -40.719 0.608 -35.351 1.00 78.86 C
ANISOU 986 CB LEU A 142 9872 9868 10221 -1364 -414 -1098 C
ATOM 987 CG LEU A 142 -40.617 -0.865 -35.749 1.00 72.25 C
ANISOU 987 CG LEU A 142 9144 8880 9427 -1499 -352 -1161 C
ATOM 988 CD1 LEU A 142 -39.262 -1.149 -36.378 1.00 65.82 C
ANISOU 988 CD1 LEU A 142 8487 7947 8575 -1390 -382 -1117 C
ATOM 989 CD2 LEU A 142 -40.852 -1.764 -34.547 1.00 81.15 C
ANISOU 989 CD2 LEU A 142 10349 9874 10611 -1612 -202 -1108 C
ATOM 990 N LEU A 143 -41.592 2.724 -32.964 1.00 76.86 N
ANISOU 990 N LEU A 143 9467 9808 9927 -1221 -378 -943 N
ATOM 991 CA LEU A 143 -41.197 4.022 -32.446 1.00 70.29 C
ANISOU 991 CA LEU A 143 8624 9034 9050 -1060 -434 -871 C
ATOM 992 C LEU A 143 -39.691 4.202 -32.601 1.00 68.44 C
ANISOU 992 C LEU A 143 8515 8683 8806 -944 -484 -808 C
ATOM 993 O LEU A 143 -38.957 3.264 -32.921 1.00 70.46 O
ANISOU 993 O LEU A 143 8880 8812 9080 -978 -459 -800 O
ATOM 994 CB LEU A 143 -41.601 4.163 -30.978 1.00 87.93 C
ANISOU 994 CB LEU A 143 10873 11267 11269 -1047 -354 -804 C
ATOM 995 CG LEU A 143 -43.091 4.236 -30.646 1.00 74.38 C
ANISOU 995 CG LEU A 143 9014 9685 9562 -1130 -295 -839 C
ATOM 996 CD1 LEU A 143 -43.303 4.080 -29.151 1.00 61.15 C
ANISOU 996 CD1 LEU A 143 7399 7965 7869 -1108 -184 -751 C
ATOM 997 CD2 LEU A 143 -43.681 5.548 -31.135 1.00 81.99 C
ANISOU 997 CD2 LEU A 143 9834 10836 10484 -1041 -386 -873 C
ATOM 998 N LEU A 144 -39.227 5.432 -32.373 1.00 69.87 N
ANISOU 998 N LEU A 144 8676 8904 8966 -806 -552 -761 N
ATOM 999 CA LEU A 144 -37.789 5.672 -32.349 1.00 70.44 C
ANISOU 999 CA LEU A 144 8846 8867 9051 -701 -597 -696 C
ATOM 1000 C LEU A 144 -37.127 4.845 -31.255 1.00 65.91 C
ANISOU 1000 C LEU A 144 8408 8162 8474 -706 -536 -635 C
ATOM 1001 O LEU A 144 -36.174 4.099 -31.511 1.00 66.92 O
ANISOU 1001 O LEU A 144 8636 8176 8616 -701 -523 -605 O
ATOM 1002 CB LEU A 144 -37.504 7.162 -32.153 1.00 62.88 C
ANISOU 1002 CB LEU A 144 7836 7964 8092 -570 -673 -667 C
ATOM 1003 CG LEU A 144 -36.025 7.559 -32.164 1.00 67.53 C
ANISOU 1003 CG LEU A 144 8490 8447 8720 -468 -728 -606 C
ATOM 1004 CD1 LEU A 144 -35.379 7.206 -33.494 1.00 67.36 C
ANISOU 1004 CD1 LEU A 144 8478 8386 8727 -461 -740 -603 C
ATOM 1005 CD2 LEU A 144 -35.861 9.039 -31.865 1.00 68.75 C
ANISOU 1005 CD2 LEU A 144 8590 8640 8892 -360 -795 -591 C
ATOM 1006 N GLU A 145 -37.635 4.949 -30.028 1.00 68.53 N
ANISOU 1006 N GLU A 145 8749 8513 8776 -699 -490 -611 N
ATOM 1007 CA GLU A 145 -37.172 4.130 -28.918 1.00 73.86 C
ANISOU 1007 CA GLU A 145 9556 9080 9428 -686 -414 -551 C
ATOM 1008 C GLU A 145 -38.249 3.121 -28.556 1.00 72.67 C
ANISOU 1008 C GLU A 145 9411 8922 9280 -815 -281 -562 C
ATOM 1009 O GLU A 145 -39.369 3.524 -28.207 1.00 56.12 O
ANISOU 1009 O GLU A 145 7219 6930 7175 -847 -250 -582 O
ATOM 1010 CB GLU A 145 -36.828 4.998 -27.709 1.00 62.18 C
ANISOU 1010 CB GLU A 145 8105 7617 7903 -551 -458 -508 C
ATOM 1011 CG GLU A 145 -36.411 4.208 -26.477 1.00 55.16 C
ANISOU 1011 CG GLU A 145 7356 6639 6965 -503 -381 -444 C
ATOM 1012 CD GLU A 145 -35.067 3.526 -26.642 1.00 75.46 C
ANISOU 1012 CD GLU A 145 10036 9091 9544 -460 -396 -405 C
ATOM 1013 OE1 GLU A 145 -34.276 3.961 -27.506 1.00 85.64 O
ANISOU 1013 OE1 GLU A 145 11288 10371 10879 -435 -489 -419 O
ATOM 1014 OE2 GLU A 145 -34.798 2.553 -25.905 1.00 84.79 O
ANISOU 1014 OE2 GLU A 145 11344 10190 10684 -440 -303 -352 O
ATOM 1015 N PRO A 146 -37.967 1.814 -28.611 1.00 76.69 N
ANISOU 1015 N PRO A 146 10028 9304 9807 -890 -188 -546 N
ATOM 1016 CA PRO A 146 -36.692 1.189 -28.982 1.00 74.36 C
ANISOU 1016 CA PRO A 146 9857 8884 9514 -848 -202 -513 C
ATOM 1017 C PRO A 146 -36.636 0.727 -30.436 1.00 76.08 C
ANISOU 1017 C PRO A 146 10054 9081 9774 -933 -230 -580 C
ATOM 1018 O PRO A 146 -35.582 0.304 -30.904 1.00 80.12 O
ANISOU 1018 O PRO A 146 10658 9501 10283 -885 -247 -553 O
ATOM 1019 CB PRO A 146 -36.627 0.001 -28.019 1.00 74.16 C
ANISOU 1019 CB PRO A 146 9977 8734 9466 -867 -55 -450 C
ATOM 1020 CG PRO A 146 -38.069 -0.448 -27.941 1.00 58.18 C
ANISOU 1020 CG PRO A 146 7879 6742 7484 -1022 54 -492 C
ATOM 1021 CD PRO A 146 -38.904 0.819 -28.056 1.00 61.06 C
ANISOU 1021 CD PRO A 146 8070 7284 7847 -1010 -35 -539 C
ATOM 1022 N GLY A 147 -37.749 0.799 -31.166 1.00 65.61 N
ANISOU 1022 N GLY A 147 8605 7847 8478 -1046 -237 -670 N
ATOM 1023 CA GLY A 147 -37.853 0.222 -32.495 1.00 73.57 C
ANISOU 1023 CA GLY A 147 9601 8840 9514 -1131 -260 -753 C
ATOM 1024 C GLY A 147 -36.810 0.671 -33.499 1.00 76.40 C
ANISOU 1024 C GLY A 147 9979 9195 9856 -1019 -360 -744 C
ATOM 1025 O GLY A 147 -35.995 -0.137 -33.955 1.00 72.39 O
ANISOU 1025 O GLY A 147 9590 8569 9346 -1009 -338 -728 O
ATOM 1026 N LEU A 148 -36.826 1.957 -33.855 1.00 73.89 N
ANISOU 1026 N LEU A 148 9549 9000 9527 -926 -457 -747 N
ATOM 1027 CA LEU A 148 -35.897 2.448 -34.868 1.00 71.90 C
ANISOU 1027 CA LEU A 148 9303 8746 9271 -816 -534 -727 C
ATOM 1028 C LEU A 148 -34.471 2.529 -34.340 1.00 65.79 C
ANISOU 1028 C LEU A 148 8627 7865 8505 -704 -538 -621 C
ATOM 1029 O LEU A 148 -33.518 2.356 -35.110 1.00 71.66 O
ANISOU 1029 O LEU A 148 9422 8550 9255 -636 -558 -588 O
ATOM 1030 CB LEU A 148 -36.354 3.812 -35.382 1.00 68.43 C
ANISOU 1030 CB LEU A 148 8720 8458 8824 -743 -615 -751 C
ATOM 1031 CG LEU A 148 -37.672 3.825 -36.160 1.00 71.19 C
ANISOU 1031 CG LEU A 148 8952 8945 9153 -820 -634 -863 C
ATOM 1032 CD1 LEU A 148 -37.953 5.214 -36.711 1.00 67.20 C
ANISOU 1032 CD1 LEU A 148 8327 8582 8625 -706 -706 -866 C
ATOM 1033 CD2 LEU A 148 -37.652 2.791 -37.277 1.00 69.87 C
ANISOU 1033 CD2 LEU A 148 8835 8736 8975 -879 -633 -938 C
ATOM 1034 N ASN A 149 -34.299 2.788 -33.042 1.00 68.66 N
ANISOU 1034 N ASN A 149 9014 8210 8866 -672 -524 -568 N
ATOM 1035 CA ASN A 149 -32.953 2.861 -32.484 1.00 66.69 C
ANISOU 1035 CA ASN A 149 8843 7875 8623 -562 -544 -481 C
ATOM 1036 C ASN A 149 -32.269 1.501 -32.487 1.00 68.09 C
ANISOU 1036 C ASN A 149 9168 7921 8782 -576 -468 -443 C
ATOM 1037 O ASN A 149 -31.049 1.425 -32.673 1.00 72.58 O
ANISOU 1037 O ASN A 149 9789 8428 9361 -483 -491 -380 O
ATOM 1038 CB ASN A 149 -33.000 3.433 -31.067 1.00 68.57 C
ANISOU 1038 CB ASN A 149 9076 8135 8842 -511 -558 -452 C
ATOM 1039 CG ASN A 149 -33.264 4.923 -31.050 1.00 66.64 C
ANISOU 1039 CG ASN A 149 8709 7991 8620 -455 -647 -472 C
ATOM 1040 OD1 ASN A 149 -32.840 5.649 -31.950 1.00 64.62 O
ANISOU 1040 OD1 ASN A 149 8388 7756 8408 -407 -707 -471 O
ATOM 1041 ND2 ASN A 149 -33.973 5.389 -30.028 1.00 52.27 N
ANISOU 1041 ND2 ASN A 149 6866 6228 6768 -449 -643 -485 N
ATOM 1042 N GLU A 150 -33.030 0.423 -32.284 1.00 68.52 N
ANISOU 1042 N GLU A 150 9289 7928 8818 -690 -369 -477 N
ATOM 1043 CA GLU A 150 -32.443 -0.909 -32.367 1.00 74.76 C
ANISOU 1043 CA GLU A 150 10237 8578 9591 -705 -282 -445 C
ATOM 1044 C GLU A 150 -31.955 -1.209 -33.778 1.00 71.41 C
ANISOU 1044 C GLU A 150 9834 8123 9174 -694 -311 -468 C
ATOM 1045 O GLU A 150 -30.931 -1.880 -33.948 1.00 68.53 O
ANISOU 1045 O GLU A 150 9589 7657 8792 -626 -280 -408 O
ATOM 1046 CB GLU A 150 -33.458 -1.960 -31.906 1.00 62.73 C
ANISOU 1046 CB GLU A 150 8773 6994 8066 -846 -156 -482 C
ATOM 1047 CG GLU A 150 -32.872 -3.352 -31.676 1.00 69.54 C
ANISOU 1047 CG GLU A 150 9826 7689 8908 -850 -37 -432 C
ATOM 1048 CD GLU A 150 -32.763 -4.169 -32.951 1.00 76.97 C
ANISOU 1048 CD GLU A 150 10830 8552 9861 -913 -24 -490 C
ATOM 1049 OE1 GLU A 150 -33.593 -3.966 -33.863 1.00 74.66 O
ANISOU 1049 OE1 GLU A 150 10437 8329 9600 -1011 -73 -598 O
ATOM 1050 OE2 GLU A 150 -31.844 -5.009 -33.041 1.00 81.42 O
ANISOU 1050 OE2 GLU A 150 11549 8992 10396 -851 33 -432 O
ATOM 1051 N ILE A 151 -32.666 -0.717 -34.793 1.00 64.55 N
ANISOU 1051 N ILE A 151 8857 7348 8320 -740 -369 -552 N
ATOM 1052 CA ILE A 151 -32.240 -0.922 -36.172 1.00 76.45 C
ANISOU 1052 CA ILE A 151 10388 8842 9819 -701 -401 -577 C
ATOM 1053 C ILE A 151 -30.940 -0.177 -36.441 1.00 70.99 C
ANISOU 1053 C ILE A 151 9684 8152 9139 -538 -456 -477 C
ATOM 1054 O ILE A 151 -29.968 -0.750 -36.946 1.00 68.42 O
ANISOU 1054 O ILE A 151 9456 7741 8799 -464 -432 -423 O
ATOM 1055 CB ILE A 151 -33.348 -0.486 -37.147 1.00 71.02 C
ANISOU 1055 CB ILE A 151 9578 8279 9128 -763 -458 -693 C
ATOM 1056 CG1 ILE A 151 -34.580 -1.382 -37.001 1.00 67.60 C
ANISOU 1056 CG1 ILE A 151 9147 7834 8705 -943 -402 -802 C
ATOM 1057 CG2 ILE A 151 -32.834 -0.503 -38.582 1.00 71.53 C
ANISOU 1057 CG2 ILE A 151 9665 8349 9164 -676 -501 -708 C
ATOM 1058 CD1 ILE A 151 -35.736 -0.973 -37.888 1.00 75.60 C
ANISOU 1058 CD1 ILE A 151 10019 8992 9712 -1005 -470 -931 C
ATOM 1059 N MET A 152 -30.898 1.110 -36.097 1.00 60.66 N
ANISOU 1059 N MET A 152 8252 6933 7863 -478 -523 -450 N
ATOM 1060 CA MET A 152 -29.735 1.929 -36.406 1.00 60.80 C
ANISOU 1060 CA MET A 152 8230 6950 7922 -340 -573 -363 C
ATOM 1061 C MET A 152 -28.505 1.551 -35.592 1.00 66.90 C
ANISOU 1061 C MET A 152 9081 7629 8707 -269 -555 -268 C
ATOM 1062 O MET A 152 -27.408 2.014 -35.920 1.00 72.11 O
ANISOU 1062 O MET A 152 9712 8273 9414 -161 -586 -192 O
ATOM 1063 CB MET A 152 -30.065 3.406 -36.187 1.00 56.84 C
ANISOU 1063 CB MET A 152 7583 6550 7465 -308 -644 -369 C
ATOM 1064 CG MET A 152 -31.263 3.899 -36.983 1.00 66.96 C
ANISOU 1064 CG MET A 152 8773 7945 8723 -348 -665 -455 C
ATOM 1065 SD MET A 152 -31.112 3.612 -38.759 1.00 77.31 S
ANISOU 1065 SD MET A 152 10103 9270 10001 -287 -662 -472 S
ATOM 1066 CE MET A 152 -29.626 4.538 -39.136 1.00 66.68 C
ANISOU 1066 CE MET A 152 8724 7880 8730 -120 -676 -337 C
ATOM 1067 N ALA A 153 -28.649 0.719 -34.560 1.00 64.19 N
ANISOU 1067 N ALA A 153 8834 7230 8325 -317 -500 -267 N
ATOM 1068 CA ALA A 153 -27.536 0.379 -33.685 1.00 61.88 C
ANISOU 1068 CA ALA A 153 8614 6871 8025 -228 -489 -181 C
ATOM 1069 C ALA A 153 -27.053 -1.058 -33.823 1.00 72.91 C
ANISOU 1069 C ALA A 153 10181 8154 9368 -218 -393 -142 C
ATOM 1070 O ALA A 153 -25.973 -1.376 -33.313 1.00 70.74 O
ANISOU 1070 O ALA A 153 9967 7832 9078 -115 -383 -60 O
ATOM 1071 CB ALA A 153 -27.916 0.639 -32.220 1.00 73.43 C
ANISOU 1071 CB ALA A 153 10072 8362 9468 -238 -498 -189 C
ATOM 1072 N ASN A 154 -27.807 -1.931 -34.491 1.00 76.11 N
ANISOU 1072 N ASN A 154 10663 8513 9743 -317 -324 -204 N
ATOM 1073 CA ASN A 154 -27.422 -3.336 -34.566 1.00 81.10 C
ANISOU 1073 CA ASN A 154 11476 9014 10323 -314 -220 -175 C
ATOM 1074 C ASN A 154 -27.514 -3.887 -35.982 1.00 74.36 C
ANISOU 1074 C ASN A 154 10677 8119 9456 -338 -203 -223 C
ATOM 1075 O ASN A 154 -26.772 -4.807 -36.341 1.00 88.87 O
ANISOU 1075 O ASN A 154 12658 9854 11254 -276 -141 -175 O
ATOM 1076 CB ASN A 154 -28.294 -4.178 -33.632 1.00 82.38 C
ANISOU 1076 CB ASN A 154 11729 9112 10457 -424 -119 -208 C
ATOM 1077 CG ASN A 154 -28.244 -3.698 -32.199 1.00 73.65 C
ANISOU 1077 CG ASN A 154 10593 8051 9341 -376 -128 -160 C
ATOM 1078 OD1 ASN A 154 -29.128 -2.971 -31.746 1.00 70.66 O
ANISOU 1078 OD1 ASN A 154 10106 7758 8984 -438 -164 -209 O
ATOM 1079 ND2 ASN A 154 -27.206 -4.100 -31.476 1.00 69.27 N
ANISOU 1079 ND2 ASN A 154 10135 7444 8741 -248 -99 -65 N
ATOM 1080 N SER A 155 -28.421 -3.343 -36.789 1.00 67.36 N
ANISOU 1080 N SER A 155 9686 7318 8591 -412 -259 -320 N
ATOM 1081 CA SER A 155 -28.656 -3.893 -38.116 1.00 76.93 C
ANISOU 1081 CA SER A 155 10953 8503 9774 -433 -255 -392 C
ATOM 1082 C SER A 155 -27.464 -3.647 -39.030 1.00 74.66 C
ANISOU 1082 C SER A 155 10684 8212 9472 -264 -279 -305 C
ATOM 1083 O SER A 155 -26.878 -2.561 -39.042 1.00 69.47 O
ANISOU 1083 O SER A 155 9906 7631 8857 -164 -338 -232 O
ATOM 1084 CB SER A 155 -29.918 -3.290 -38.732 1.00 71.79 C
ANISOU 1084 CB SER A 155 10169 7972 9137 -528 -322 -520 C
ATOM 1085 OG SER A 155 -30.124 -3.780 -40.045 1.00 68.53 O
ANISOU 1085 OG SER A 155 9808 7549 8684 -527 -336 -603 O
ATOM 1086 N LEU A 156 -27.101 -4.676 -39.792 1.00 70.17 N
ANISOU 1086 N LEU A 156 10269 7545 8849 -230 -226 -312 N
ATOM 1087 CA LEU A 156 -26.074 -4.577 -40.817 1.00 74.83 C
ANISOU 1087 CA LEU A 156 10892 8130 9412 -63 -232 -233 C
ATOM 1088 C LEU A 156 -26.658 -4.521 -42.221 1.00 71.14 C
ANISOU 1088 C LEU A 156 10418 7712 8901 -54 -274 -334 C
ATOM 1089 O LEU A 156 -25.900 -4.421 -43.191 1.00 73.84 O
ANISOU 1089 O LEU A 156 10791 8056 9208 101 -272 -271 O
ATOM 1090 CB LEU A 156 -25.103 -5.756 -40.708 1.00 72.99 C
ANISOU 1090 CB LEU A 156 10852 7755 9128 15 -138 -150 C
ATOM 1091 CG LEU A 156 -24.272 -5.846 -39.427 1.00 61.03 C
ANISOU 1091 CG LEU A 156 9354 6202 7632 65 -99 -31 C
ATOM 1092 CD1 LEU A 156 -23.470 -7.137 -39.405 1.00 61.33 C
ANISOU 1092 CD1 LEU A 156 9603 6101 7599 145 6 38 C
ATOM 1093 CD2 LEU A 156 -23.355 -4.639 -39.296 1.00 54.89 C
ANISOU 1093 CD2 LEU A 156 8412 5522 6921 188 -167 79 C
ATOM 1094 N ASP A 157 -27.982 -4.584 -42.351 1.00 73.08 N
ANISOU 1094 N ASP A 157 10619 8004 9142 -202 -311 -488 N
ATOM 1095 CA ASP A 157 -28.634 -4.561 -43.654 1.00 81.09 C
ANISOU 1095 CA ASP A 157 11622 9086 10103 -191 -368 -610 C
ATOM 1096 C ASP A 157 -28.721 -3.124 -44.154 1.00 72.45 C
ANISOU 1096 C ASP A 157 10350 8152 9024 -90 -443 -579 C
ATOM 1097 O ASP A 157 -29.262 -2.252 -43.465 1.00 65.56 O
ANISOU 1097 O ASP A 157 9333 7369 8210 -155 -479 -584 O
ATOM 1098 CB ASP A 157 -30.024 -5.189 -43.563 1.00 73.98 C
ANISOU 1098 CB ASP A 157 10721 8184 9205 -396 -384 -794 C
ATOM 1099 CG ASP A 157 -30.707 -5.294 -44.912 1.00 77.27 C
ANISOU 1099 CG ASP A 157 11133 8672 9554 -382 -460 -946 C
ATOM 1100 OD1 ASP A 157 -30.316 -6.170 -45.711 1.00 84.04 O
ANISOU 1100 OD1 ASP A 157 12152 9436 10344 -322 -440 -982 O
ATOM 1101 OD2 ASP A 157 -31.636 -4.501 -45.174 1.00 84.63 O
ANISOU 1101 OD2 ASP A 157 11904 9760 10491 -418 -541 -1034 O
ATOM 1102 N TYR A 158 -28.188 -2.881 -45.354 1.00 63.87 N
ANISOU 1102 N TYR A 158 9288 7097 7881 82 -455 -541 N
ATOM 1103 CA TYR A 158 -28.190 -1.534 -45.917 1.00 62.82 C
ANISOU 1103 CA TYR A 158 9006 7100 7762 204 -501 -493 C
ATOM 1104 C TYR A 158 -29.612 -1.013 -46.089 1.00 76.50 C
ANISOU 1104 C TYR A 158 10615 8973 9478 109 -580 -643 C
ATOM 1105 O TYR A 158 -29.921 0.121 -45.705 1.00 71.34 O
ANISOU 1105 O TYR A 158 9811 8417 8877 110 -609 -612 O
ATOM 1106 CB TYR A 158 -27.445 -1.534 -47.254 1.00 63.13 C
ANISOU 1106 CB TYR A 158 9118 7141 7728 419 -480 -428 C
ATOM 1107 CG TYR A 158 -27.267 -0.170 -47.889 1.00 61.99 C
ANISOU 1107 CG TYR A 158 8839 7111 7601 578 -493 -342 C
ATOM 1108 CD1 TYR A 158 -28.245 0.367 -48.719 1.00 62.79 C
ANISOU 1108 CD1 TYR A 158 8872 7351 7632 618 -555 -449 C
ATOM 1109 CD2 TYR A 158 -26.113 0.570 -47.675 1.00 63.94 C
ANISOU 1109 CD2 TYR A 158 9028 7327 7941 694 -437 -154 C
ATOM 1110 CE1 TYR A 158 -28.082 1.609 -49.306 1.00 63.15 C
ANISOU 1110 CE1 TYR A 158 8811 7492 7690 780 -546 -358 C
ATOM 1111 CE2 TYR A 158 -25.940 1.812 -48.259 1.00 68.94 C
ANISOU 1111 CE2 TYR A 158 9544 8041 8607 835 -428 -68 C
ATOM 1112 CZ TYR A 158 -26.928 2.327 -49.073 1.00 68.15 C
ANISOU 1112 CZ TYR A 158 9396 8069 8428 884 -474 -164 C
ATOM 1113 OH TYR A 158 -26.758 3.563 -49.654 1.00 69.63 O
ANISOU 1113 OH TYR A 158 9482 8328 8644 1041 -445 -66 O
ATOM 1114 N ASN A 159 -30.497 -1.836 -46.658 1.00 74.91 N
ANISOU 1114 N ASN A 159 10472 8784 9205 26 -617 -813 N
ATOM 1115 CA ASN A 159 -31.853 -1.378 -46.947 1.00 77.83 C
ANISOU 1115 CA ASN A 159 10711 9310 9551 -49 -701 -965 C
ATOM 1116 C ASN A 159 -32.668 -1.194 -45.672 1.00 74.94 C
ANISOU 1116 C ASN A 159 10236 8966 9271 -245 -703 -1002 C
ATOM 1117 O ASN A 159 -33.491 -0.275 -45.585 1.00 74.16 O
ANISOU 1117 O ASN A 159 9982 9015 9181 -262 -754 -1042 O
ATOM 1118 CB ASN A 159 -32.547 -2.356 -47.895 1.00 77.56 C
ANISOU 1118 CB ASN A 159 10759 9282 9427 -91 -754 -1154 C
ATOM 1119 CG ASN A 159 -31.972 -2.312 -49.295 1.00 83.89 C
ANISOU 1119 CG ASN A 159 11648 10114 10115 140 -772 -1136 C
ATOM 1120 OD1 ASN A 159 -31.459 -1.283 -49.735 1.00 81.68 O
ANISOU 1120 OD1 ASN A 159 11306 9911 9816 330 -762 -1011 O
ATOM 1121 ND2 ASN A 159 -32.056 -3.430 -50.006 1.00100.76 N
ANISOU 1121 ND2 ASN A 159 13932 12179 12172 132 -792 -1260 N
ATOM 1122 N GLU A 160 -32.464 -2.059 -44.675 1.00 71.79 N
ANISOU 1122 N GLU A 160 9926 8426 8927 -379 -637 -982 N
ATOM 1123 CA GLU A 160 -33.191 -1.905 -43.419 1.00 76.12 C
ANISOU 1123 CA GLU A 160 10384 8990 9548 -543 -620 -1000 C
ATOM 1124 C GLU A 160 -32.788 -0.621 -42.706 1.00 76.47 C
ANISOU 1124 C GLU A 160 10317 9098 9642 -462 -626 -868 C
ATOM 1125 O GLU A 160 -33.645 0.101 -42.183 1.00 64.20 O
ANISOU 1125 O GLU A 160 8628 7652 8115 -526 -656 -904 O
ATOM 1126 CB GLU A 160 -32.956 -3.113 -42.514 1.00 74.88 C
ANISOU 1126 CB GLU A 160 10366 8657 9429 -668 -528 -985 C
ATOM 1127 CG GLU A 160 -33.730 -3.054 -41.206 1.00 70.05 C
ANISOU 1127 CG GLU A 160 9678 8054 8885 -824 -492 -995 C
ATOM 1128 CD GLU A 160 -33.310 -4.129 -40.224 1.00 84.00 C
ANISOU 1128 CD GLU A 160 11594 9641 10681 -900 -379 -938 C
ATOM 1129 OE1 GLU A 160 -32.301 -4.817 -40.489 1.00 87.38 O
ANISOU 1129 OE1 GLU A 160 12180 9943 11076 -817 -333 -874 O
ATOM 1130 OE2 GLU A 160 -33.988 -4.286 -39.187 1.00 75.83 O
ANISOU 1130 OE2 GLU A 160 10524 8594 9695 -1026 -326 -948 O
ATOM 1131 N ARG A 161 -31.488 -0.320 -42.675 1.00 74.42 N
ANISOU 1131 N ARG A 161 10108 8771 9398 -321 -596 -720 N
ATOM 1132 CA ARG A 161 -31.034 0.925 -42.066 1.00 70.64 C
ANISOU 1132 CA ARG A 161 9521 8339 8980 -246 -610 -609 C
ATOM 1133 C ARG A 161 -31.477 2.130 -42.885 1.00 69.12 C
ANISOU 1133 C ARG A 161 9199 8292 8772 -148 -666 -624 C
ATOM 1134 O ARG A 161 -31.842 3.169 -42.323 1.00 73.93 O
ANISOU 1134 O ARG A 161 9691 8978 9423 -153 -691 -606 O
ATOM 1135 CB ARG A 161 -29.515 0.912 -41.914 1.00 71.05 C
ANISOU 1135 CB ARG A 161 9641 8285 9068 -125 -569 -457 C
ATOM 1136 CG ARG A 161 -28.984 -0.212 -41.047 1.00 66.48 C
ANISOU 1136 CG ARG A 161 9196 7572 8493 -187 -509 -423 C
ATOM 1137 CD ARG A 161 -27.471 -0.158 -40.974 1.00 60.23 C
ANISOU 1137 CD ARG A 161 8447 6704 7733 -49 -479 -273 C
ATOM 1138 NE ARG A 161 -27.007 1.113 -40.434 1.00 65.58 N
ANISOU 1138 NE ARG A 161 8989 7433 8497 8 -519 -193 N
ATOM 1139 CZ ARG A 161 -26.819 1.353 -39.144 1.00 77.04 C
ANISOU 1139 CZ ARG A 161 10409 8869 9994 -33 -532 -165 C
ATOM 1140 NH1 ARG A 161 -27.036 0.421 -38.230 1.00 74.04 N
ANISOU 1140 NH1 ARG A 161 10125 8428 9577 -116 -495 -191 N
ATOM 1141 NH2 ARG A 161 -26.405 2.558 -38.761 1.00 70.54 N
ANISOU 1141 NH2 ARG A 161 9461 8087 9254 20 -581 -112 N
ATOM 1142 N LEU A 162 -31.444 2.012 -44.215 1.00 73.82 N
ANISOU 1142 N LEU A 162 9825 8926 9296 -42 -680 -654 N
ATOM 1143 CA LEU A 162 -31.913 3.101 -45.066 1.00 75.42 C
ANISOU 1143 CA LEU A 162 9919 9274 9463 75 -722 -668 C
ATOM 1144 C LEU A 162 -33.395 3.371 -44.845 1.00 70.22 C
ANISOU 1144 C LEU A 162 9147 8756 8779 -37 -779 -806 C
ATOM 1145 O LEU A 162 -33.829 4.529 -44.834 1.00 60.76 O
ANISOU 1145 O LEU A 162 7828 7671 7586 23 -802 -787 O
ATOM 1146 CB LEU A 162 -31.638 2.772 -46.533 1.00 75.08 C
ANISOU 1146 CB LEU A 162 9952 9251 9324 227 -724 -683 C
ATOM 1147 CG LEU A 162 -32.204 3.736 -47.578 1.00 64.29 C
ANISOU 1147 CG LEU A 162 8496 8046 7885 378 -762 -710 C
ATOM 1148 CD1 LEU A 162 -31.643 5.133 -47.379 1.00 62.84 C
ANISOU 1148 CD1 LEU A 162 8220 7874 7780 498 -721 -556 C
ATOM 1149 CD2 LEU A 162 -31.914 3.233 -48.982 1.00 62.03 C
ANISOU 1149 CD2 LEU A 162 8313 7772 7483 540 -764 -734 C
ATOM 1150 N TRP A 163 -34.187 2.312 -44.661 1.00 72.58 N
ANISOU 1150 N TRP A 163 9478 9045 9055 -200 -795 -941 N
ATOM 1151 CA TRP A 163 -35.617 2.484 -44.429 1.00 67.47 C
ANISOU 1151 CA TRP A 163 8704 8536 8397 -320 -844 -1073 C
ATOM 1152 C TRP A 163 -35.877 3.220 -43.121 1.00 73.40 C
ANISOU 1152 C TRP A 163 9365 9303 9220 -388 -823 -1011 C
ATOM 1153 O TRP A 163 -36.680 4.158 -43.073 1.00 72.58 O
ANISOU 1153 O TRP A 163 9129 9345 9103 -365 -858 -1037 O
ATOM 1154 CB TRP A 163 -36.315 1.125 -44.431 1.00 67.99 C
ANISOU 1154 CB TRP A 163 8821 8555 8456 -502 -850 -1224 C
ATOM 1155 CG TRP A 163 -37.726 1.180 -43.933 1.00 68.09 C
ANISOU 1155 CG TRP A 163 8692 8686 8492 -660 -880 -1343 C
ATOM 1156 CD1 TRP A 163 -38.829 1.562 -44.638 1.00 74.98 C
ANISOU 1156 CD1 TRP A 163 9429 9750 9311 -653 -962 -1473 C
ATOM 1157 CD2 TRP A 163 -38.187 0.840 -42.620 1.00 81.52 C
ANISOU 1157 CD2 TRP A 163 10367 10331 10275 -836 -821 -1336 C
ATOM 1158 NE1 TRP A 163 -39.949 1.483 -43.845 1.00 90.69 N
ANISOU 1158 NE1 TRP A 163 11297 11807 11355 -825 -958 -1546 N
ATOM 1159 CE2 TRP A 163 -39.581 1.042 -42.601 1.00 87.57 C
ANISOU 1159 CE2 TRP A 163 10972 11257 11045 -938 -865 -1460 C
ATOM 1160 CE3 TRP A 163 -37.555 0.385 -41.458 1.00 81.30 C
ANISOU 1160 CE3 TRP A 163 10437 10141 10311 -901 -732 -1234 C
ATOM 1161 CZ2 TRP A 163 -40.354 0.803 -41.468 1.00 84.52 C
ANISOU 1161 CZ2 TRP A 163 10518 10864 10731 -1106 -810 -1473 C
ATOM 1162 CZ3 TRP A 163 -38.326 0.149 -40.333 1.00 72.80 C
ANISOU 1162 CZ3 TRP A 163 9308 9058 9294 -1055 -679 -1250 C
ATOM 1163 CH2 TRP A 163 -39.710 0.359 -40.346 1.00 75.36 C
ANISOU 1163 CH2 TRP A 163 9470 9535 9629 -1158 -712 -1364 C
ATOM 1164 N ALA A 164 -35.201 2.809 -42.046 1.00 72.76 N
ANISOU 1164 N ALA A 164 9362 9079 9205 -454 -765 -929 N
ATOM 1165 CA ALA A 164 -35.402 3.462 -40.756 1.00 66.83 C
ANISOU 1165 CA ALA A 164 8545 8339 8509 -500 -749 -875 C
ATOM 1166 C ALA A 164 -34.912 4.904 -40.782 1.00 67.80 C
ANISOU 1166 C ALA A 164 8596 8512 8653 -350 -772 -778 C
ATOM 1167 O ALA A 164 -35.536 5.789 -40.185 1.00 68.52 O
ANISOU 1167 O ALA A 164 8589 8688 8756 -356 -788 -780 O
ATOM 1168 CB ALA A 164 -34.697 2.673 -39.653 1.00 76.06 C
ANISOU 1168 CB ALA A 164 9827 9348 9723 -570 -685 -809 C
ATOM 1169 N TRP A 165 -33.800 5.160 -41.474 1.00 70.35 N
ANISOU 1169 N TRP A 165 8968 8774 8986 -213 -764 -688 N
ATOM 1170 CA TRP A 165 -33.256 6.512 -41.539 1.00 64.36 C
ANISOU 1170 CA TRP A 165 8144 8036 8275 -78 -769 -589 C
ATOM 1171 C TRP A 165 -34.175 7.445 -42.319 1.00 73.16 C
ANISOU 1171 C TRP A 165 9153 9310 9334 3 -799 -636 C
ATOM 1172 O TRP A 165 -34.425 8.578 -41.892 1.00 64.16 O
ANISOU 1172 O TRP A 165 7932 8220 8225 44 -806 -604 O
ATOM 1173 CB TRP A 165 -31.863 6.475 -42.168 1.00 62.59 C
ANISOU 1173 CB TRP A 165 7987 7706 8086 47 -736 -475 C
ATOM 1174 CG TRP A 165 -31.136 7.786 -42.159 1.00 61.01 C
ANISOU 1174 CG TRP A 165 7721 7488 7973 167 -724 -362 C
ATOM 1175 CD1 TRP A 165 -30.227 8.211 -41.234 1.00 62.12 C
ANISOU 1175 CD1 TRP A 165 7850 7532 8221 162 -721 -279 C
ATOM 1176 CD2 TRP A 165 -31.242 8.837 -43.128 1.00 63.50 C
ANISOU 1176 CD2 TRP A 165 7972 7876 8281 312 -711 -323 C
ATOM 1177 NE1 TRP A 165 -29.766 9.463 -41.562 1.00 62.11 N
ANISOU 1177 NE1 TRP A 165 7775 7525 8298 274 -706 -197 N
ATOM 1178 CE2 TRP A 165 -30.374 9.870 -42.721 1.00 65.10 C
ANISOU 1178 CE2 TRP A 165 8127 8002 8608 372 -688 -212 C
ATOM 1179 CE3 TRP A 165 -31.989 9.006 -44.298 1.00 53.28 C
ANISOU 1179 CE3 TRP A 165 6656 6705 6884 406 -715 -374 C
ATOM 1180 CZ2 TRP A 165 -30.233 11.053 -43.441 1.00 60.48 C
ANISOU 1180 CZ2 TRP A 165 7481 7439 8059 515 -649 -138 C
ATOM 1181 CZ3 TRP A 165 -31.848 10.182 -45.012 1.00 57.32 C
ANISOU 1181 CZ3 TRP A 165 7113 7256 7409 570 -679 -295 C
ATOM 1182 CH2 TRP A 165 -30.977 11.191 -44.581 1.00 57.85 C
ANISOU 1182 CH2 TRP A 165 7141 7226 7614 620 -636 -173 C
ATOM 1183 N GLU A 166 -34.690 6.984 -43.461 1.00 73.57 N
ANISOU 1183 N GLU A 166 9212 9446 9297 39 -820 -717 N
ATOM 1184 CA GLU A 166 -35.515 7.834 -44.314 1.00 69.34 C
ANISOU 1184 CA GLU A 166 8582 9079 8686 150 -850 -760 C
ATOM 1185 C GLU A 166 -36.933 7.982 -43.772 1.00 69.67 C
ANISOU 1185 C GLU A 166 8514 9261 8696 41 -891 -872 C
ATOM 1186 O GLU A 166 -37.492 9.084 -43.792 1.00 61.85 O
ANISOU 1186 O GLU A 166 7429 8387 7685 124 -900 -859 O
ATOM 1187 CB GLU A 166 -35.540 7.272 -45.737 1.00 68.40 C
ANISOU 1187 CB GLU A 166 8511 9011 8465 250 -870 -818 C
ATOM 1188 CG GLU A 166 -36.606 7.874 -46.644 1.00 71.38 C
ANISOU 1188 CG GLU A 166 8793 9595 8732 358 -919 -903 C
ATOM 1189 CD GLU A 166 -36.337 9.326 -46.999 1.00 79.17 C
ANISOU 1189 CD GLU A 166 9730 10629 9721 558 -877 -782 C
ATOM 1190 OE1 GLU A 166 -35.180 9.774 -46.859 1.00 80.99 O
ANISOU 1190 OE1 GLU A 166 10011 10721 10041 630 -810 -634 O
ATOM 1191 OE2 GLU A 166 -37.288 10.018 -47.422 1.00 71.76 O
ANISOU 1191 OE2 GLU A 166 8700 9866 8700 644 -906 -834 O
ATOM 1192 N SER A 167 -37.529 6.888 -43.288 1.00 72.81 N
ANISOU 1192 N SER A 167 8922 9648 9095 -140 -905 -974 N
ATOM 1193 CA SER A 167 -38.906 6.948 -42.807 1.00 72.58 C
ANISOU 1193 CA SER A 167 8773 9757 9046 -251 -933 -1077 C
ATOM 1194 C SER A 167 -39.034 7.824 -41.569 1.00 76.24 C
ANISOU 1194 C SER A 167 9186 10217 9563 -267 -905 -1002 C
ATOM 1195 O SER A 167 -40.058 8.493 -41.389 1.00 77.13 O
ANISOU 1195 O SER A 167 9182 10481 9643 -259 -923 -1042 O
ATOM 1196 CB SER A 167 -39.424 5.541 -42.508 1.00 64.39 C
ANISOU 1196 CB SER A 167 7762 8675 8028 -454 -931 -1189 C
ATOM 1197 OG SER A 167 -39.286 4.689 -43.634 1.00 97.22 O
ANISOU 1197 OG SER A 167 11983 12820 12134 -442 -964 -1274 O
ATOM 1198 N TRP A 168 -38.014 7.834 -40.707 1.00 69.17 N
ANISOU 1198 N TRP A 168 8377 9160 8743 -278 -865 -899 N
ATOM 1199 CA TRP A 168 -38.066 8.680 -39.521 1.00 70.91 C
ANISOU 1199 CA TRP A 168 8566 9371 9006 -277 -851 -838 C
ATOM 1200 C TRP A 168 -38.051 10.158 -39.889 1.00 69.84 C
ANISOU 1200 C TRP A 168 8366 9308 8861 -116 -863 -784 C
ATOM 1201 O TRP A 168 -38.661 10.975 -39.190 1.00 72.89 O
ANISOU 1201 O TRP A 168 8690 9762 9243 -104 -865 -780 O
ATOM 1202 CB TRP A 168 -36.899 8.347 -38.587 1.00 73.04 C
ANISOU 1202 CB TRP A 168 8943 9459 9350 -306 -822 -753 C
ATOM 1203 CG TRP A 168 -36.798 9.267 -37.409 1.00 71.55 C
ANISOU 1203 CG TRP A 168 8735 9250 9199 -280 -824 -700 C
ATOM 1204 CD1 TRP A 168 -35.837 10.211 -37.185 1.00 66.30 C
ANISOU 1204 CD1 TRP A 168 8085 8509 8596 -179 -837 -617 C
ATOM 1205 CD2 TRP A 168 -37.701 9.344 -36.299 1.00 75.36 C
ANISOU 1205 CD2 TRP A 168 9181 9790 9664 -352 -813 -731 C
ATOM 1206 NE1 TRP A 168 -36.082 10.865 -36.001 1.00 74.86 N
ANISOU 1206 NE1 TRP A 168 9153 9595 9694 -183 -848 -609 N
ATOM 1207 CE2 TRP A 168 -37.222 10.351 -35.438 1.00 72.76 C
ANISOU 1207 CE2 TRP A 168 8861 9415 9370 -277 -829 -671 C
ATOM 1208 CE3 TRP A 168 -38.868 8.657 -35.948 1.00 65.07 C
ANISOU 1208 CE3 TRP A 168 7833 8567 8323 -471 -785 -803 C
ATOM 1209 CZ2 TRP A 168 -37.867 10.688 -34.250 1.00 63.71 C
ANISOU 1209 CZ2 TRP A 168 7699 8307 8202 -298 -822 -680 C
ATOM 1210 CZ3 TRP A 168 -39.507 8.991 -34.768 1.00 71.91 C
ANISOU 1210 CZ3 TRP A 168 8672 9473 9180 -495 -763 -796 C
ATOM 1211 CH2 TRP A 168 -39.005 9.998 -33.933 1.00 68.26 C
ANISOU 1211 CH2 TRP A 168 8236 8968 8731 -400 -783 -734 C
ATOM 1212 N ARG A 169 -37.382 10.516 -40.984 1.00 65.60 N
ANISOU 1212 N ARG A 169 7853 8756 8318 19 -861 -737 N
ATOM 1213 CA ARG A 169 -37.264 11.910 -41.385 1.00 71.26 C
ANISOU 1213 CA ARG A 169 8525 9514 9039 183 -848 -668 C
ATOM 1214 C ARG A 169 -38.370 12.364 -42.327 1.00 81.53 C
ANISOU 1214 C ARG A 169 9737 11013 10227 280 -867 -731 C
ATOM 1215 O ARG A 169 -38.651 13.566 -42.392 1.00 76.77 O
ANISOU 1215 O ARG A 169 9085 10473 9611 401 -849 -688 O
ATOM 1216 CB ARG A 169 -35.902 12.149 -42.045 1.00 62.80 C
ANISOU 1216 CB ARG A 169 7519 8310 8031 297 -812 -558 C
ATOM 1217 CG ARG A 169 -34.745 12.128 -41.065 1.00 67.89 C
ANISOU 1217 CG ARG A 169 8220 8776 8799 242 -800 -481 C
ATOM 1218 CD ARG A 169 -33.404 12.005 -41.765 1.00 59.33 C
ANISOU 1218 CD ARG A 169 7192 7569 7781 326 -762 -382 C
ATOM 1219 NE ARG A 169 -32.298 12.120 -40.823 1.00 60.27 N
ANISOU 1219 NE ARG A 169 7338 7536 8025 285 -762 -312 N
ATOM 1220 CZ ARG A 169 -31.909 11.154 -40.003 1.00 68.68 C
ANISOU 1220 CZ ARG A 169 8462 8529 9106 174 -782 -330 C
ATOM 1221 NH1 ARG A 169 -32.520 9.980 -39.978 1.00 64.89 N
ANISOU 1221 NH1 ARG A 169 8027 8090 8540 79 -789 -408 N
ATOM 1222 NH2 ARG A 169 -30.882 11.371 -39.186 1.00 70.75 N
ANISOU 1222 NH2 ARG A 169 8734 8672 9474 163 -792 -270 N
ATOM 1223 N SER A 170 -39.004 11.442 -43.055 1.00 90.13 N
ANISOU 1223 N SER A 170 10807 12204 11236 236 -904 -837 N
ATOM 1224 CA SER A 170 -40.054 11.813 -43.995 1.00 87.16 C
ANISOU 1224 CA SER A 170 10337 12040 10742 340 -938 -914 C
ATOM 1225 C SER A 170 -41.446 11.767 -43.386 1.00 87.33 C
ANISOU 1225 C SER A 170 10236 12219 10724 234 -973 -1015 C
ATOM 1226 O SER A 170 -42.369 12.371 -43.943 1.00 89.12 O
ANISOU 1226 O SER A 170 10364 12642 10858 340 -999 -1062 O
ATOM 1227 CB SER A 170 -40.016 10.901 -45.224 1.00 90.44 C
ANISOU 1227 CB SER A 170 10787 12498 11080 372 -977 -994 C
ATOM 1228 OG SER A 170 -40.452 9.592 -44.902 1.00111.07 O
ANISOU 1228 OG SER A 170 13400 15097 13705 169 -1016 -1114 O
ATOM 1229 N GLU A 171 -41.625 11.069 -42.266 1.00 83.12 N
ANISOU 1229 N GLU A 171 9708 11616 10258 42 -966 -1043 N
ATOM 1230 CA GLU A 171 -42.926 10.964 -41.621 1.00 88.70 C
ANISOU 1230 CA GLU A 171 10295 12463 10944 -67 -979 -1125 C
ATOM 1231 C GLU A 171 -43.007 11.695 -40.291 1.00 79.54 C
ANISOU 1231 C GLU A 171 9130 11262 9829 -82 -935 -1047 C
ATOM 1232 O GLU A 171 -44.092 12.140 -39.913 1.00 90.99 O
ANISOU 1232 O GLU A 171 10469 12864 11238 -82 -936 -1079 O
ATOM 1233 CB GLU A 171 -43.296 9.492 -41.406 1.00 96.44 C
ANISOU 1233 CB GLU A 171 11273 13410 11960 -280 -990 -1229 C
ATOM 1234 CG GLU A 171 -43.364 8.685 -42.694 1.00 88.87 C
ANISOU 1234 CG GLU A 171 10318 12500 10951 -280 -1048 -1340 C
ATOM 1235 CD GLU A 171 -43.668 7.221 -42.450 1.00110.65 C
ANISOU 1235 CD GLU A 171 13089 15188 13764 -504 -1048 -1446 C
ATOM 1236 OE1 GLU A 171 -44.125 6.885 -41.337 1.00127.90 O
ANISOU 1236 OE1 GLU A 171 15241 17338 16017 -656 -999 -1442 O
ATOM 1237 OE2 GLU A 171 -43.445 6.406 -43.370 1.00 99.20 O
ANISOU 1237 OE2 GLU A 171 11692 13712 12290 -519 -1089 -1530 O
ATOM 1238 N VAL A 172 -41.895 11.830 -39.578 1.00 73.91 N
ANISOU 1238 N VAL A 172 8532 10356 9194 -84 -903 -951 N
ATOM 1239 CA VAL A 172 -41.854 12.591 -38.337 1.00 79.01 C
ANISOU 1239 CA VAL A 172 9191 10953 9874 -73 -875 -885 C
ATOM 1240 C VAL A 172 -41.175 13.940 -38.531 1.00 76.33 C
ANISOU 1240 C VAL A 172 8886 10564 9553 99 -868 -795 C
ATOM 1241 O VAL A 172 -41.612 14.944 -37.968 1.00 79.77 O
ANISOU 1241 O VAL A 172 9291 11048 9971 169 -856 -770 O
ATOM 1242 CB VAL A 172 -41.157 11.769 -37.231 1.00 76.34 C
ANISOU 1242 CB VAL A 172 8954 10442 9611 -201 -852 -856 C
ATOM 1243 CG1 VAL A 172 -41.117 12.550 -35.927 1.00 68.30 C
ANISOU 1243 CG1 VAL A 172 7958 9380 8612 -171 -836 -802 C
ATOM 1244 CG2 VAL A 172 -41.863 10.436 -37.038 1.00 75.40 C
ANISOU 1244 CG2 VAL A 172 8809 10352 9488 -373 -834 -936 C
ATOM 1245 N GLY A 173 -40.113 13.980 -39.338 1.00 74.17 N
ANISOU 1245 N GLY A 173 8676 10187 9318 171 -864 -744 N
ATOM 1246 CA GLY A 173 -39.410 15.234 -39.558 1.00 68.17 C
ANISOU 1246 CA GLY A 173 7943 9355 8602 323 -839 -652 C
ATOM 1247 C GLY A 173 -40.224 16.237 -40.353 1.00 73.15 C
ANISOU 1247 C GLY A 173 8501 10146 9146 483 -824 -651 C
ATOM 1248 O GLY A 173 -40.128 17.446 -40.124 1.00 73.88 O
ANISOU 1248 O GLY A 173 8600 10210 9263 592 -792 -590 O
ATOM 1249 N LYS A 174 -41.034 15.755 -41.298 1.00 79.14 N
ANISOU 1249 N LYS A 174 9194 11076 9800 506 -847 -725 N
ATOM 1250 CA LYS A 174 -41.864 16.663 -42.083 1.00 69.81 C
ANISOU 1250 CA LYS A 174 7938 10074 8512 681 -836 -729 C
ATOM 1251 C LYS A 174 -42.961 17.295 -41.237 1.00 72.20 C
ANISOU 1251 C LYS A 174 8163 10501 8768 678 -836 -754 C
ATOM 1252 O LYS A 174 -43.402 18.411 -41.534 1.00 70.13 O
ANISOU 1252 O LYS A 174 7871 10330 8444 847 -804 -716 O
ATOM 1253 CB LYS A 174 -42.466 15.930 -43.282 1.00 69.52 C
ANISOU 1253 CB LYS A 174 7843 10208 8365 712 -882 -822 C
ATOM 1254 CG LYS A 174 -41.450 15.540 -44.345 1.00 74.79 C
ANISOU 1254 CG LYS A 174 8594 10780 9042 788 -870 -784 C
ATOM 1255 CD LYS A 174 -42.134 15.101 -45.630 1.00 69.48 C
ANISOU 1255 CD LYS A 174 7868 10302 8230 881 -921 -881 C
ATOM 1256 CE LYS A 174 -41.119 14.756 -46.707 1.00 74.91 C
ANISOU 1256 CE LYS A 174 8655 10898 8910 990 -901 -833 C
ATOM 1257 NZ LYS A 174 -41.778 14.407 -47.998 1.00 88.37 N
ANISOU 1257 NZ LYS A 174 10320 12801 10457 1116 -960 -935 N
ATOM 1258 N GLN A 175 -43.417 16.604 -40.188 1.00 71.77 N
ANISOU 1258 N GLN A 175 8082 10449 8737 504 -857 -808 N
ATOM 1259 CA GLN A 175 -44.376 17.211 -39.272 1.00 68.53 C
ANISOU 1259 CA GLN A 175 7610 10140 8287 510 -844 -814 C
ATOM 1260 C GLN A 175 -43.751 18.362 -38.496 1.00 65.99 C
ANISOU 1260 C GLN A 175 7376 9673 8023 595 -806 -723 C
ATOM 1261 O GLN A 175 -44.449 19.314 -38.128 1.00 60.16 O
ANISOU 1261 O GLN A 175 6607 9022 7228 695 -782 -705 O
ATOM 1262 CB GLN A 175 -44.920 16.166 -38.296 1.00 76.64 C
ANISOU 1262 CB GLN A 175 8600 11182 9337 311 -855 -876 C
ATOM 1263 CG GLN A 175 -45.597 14.970 -38.943 1.00 76.01 C
ANISOU 1263 CG GLN A 175 8427 11227 9227 193 -891 -984 C
ATOM 1264 CD GLN A 175 -46.248 14.057 -37.920 1.00 84.35 C
ANISOU 1264 CD GLN A 175 9436 12295 10320 2 -874 -1030 C
ATOM 1265 OE1 GLN A 175 -46.770 14.519 -36.905 1.00 78.34 O
ANISOU 1265 OE1 GLN A 175 8650 11565 9549 6 -838 -996 O
ATOM 1266 NE2 GLN A 175 -46.213 12.755 -38.179 1.00 87.65 N
ANISOU 1266 NE2 GLN A 175 9849 12674 10778 -158 -890 -1102 N
ATOM 1267 N LEU A 176 -42.443 18.293 -38.244 1.00 61.17 N
ANISOU 1267 N LEU A 176 6874 8842 7526 559 -803 -670 N
ATOM 1268 CA LEU A 176 -41.761 19.309 -37.454 1.00 63.26 C
ANISOU 1268 CA LEU A 176 7219 8950 7869 614 -784 -604 C
ATOM 1269 C LEU A 176 -41.323 20.510 -38.281 1.00 69.98 C
ANISOU 1269 C LEU A 176 8093 9752 8742 792 -736 -531 C
ATOM 1270 O LEU A 176 -41.017 21.559 -37.704 1.00 75.12 O
ANISOU 1270 O LEU A 176 8796 10297 9448 856 -714 -489 O
ATOM 1271 CB LEU A 176 -40.542 18.694 -36.762 1.00 67.84 C
ANISOU 1271 CB LEU A 176 7885 9323 8568 494 -810 -588 C
ATOM 1272 CG LEU A 176 -40.823 17.504 -35.844 1.00 63.99 C
ANISOU 1272 CG LEU A 176 7401 8846 8068 331 -836 -642 C
ATOM 1273 CD1 LEU A 176 -39.527 16.844 -35.406 1.00 61.82 C
ANISOU 1273 CD1 LEU A 176 7214 8380 7895 246 -857 -618 C
ATOM 1274 CD2 LEU A 176 -41.632 17.950 -34.639 1.00 59.34 C
ANISOU 1274 CD2 LEU A 176 6804 8313 7428 334 -832 -658 C
ATOM 1275 N ARG A 177 -41.286 20.382 -39.608 1.00 73.13 N
ANISOU 1275 N ARG A 177 8465 10221 9100 879 -716 -515 N
ATOM 1276 CA ARG A 177 -40.808 21.480 -40.447 1.00 68.37 C
ANISOU 1276 CA ARG A 177 7895 9559 8524 1063 -646 -426 C
ATOM 1277 C ARG A 177 -41.639 22.750 -40.302 1.00 67.40 C
ANISOU 1277 C ARG A 177 7757 9524 8329 1215 -599 -403 C
ATOM 1278 O ARG A 177 -41.047 23.825 -40.105 1.00 66.35 O
ANISOU 1278 O ARG A 177 7690 9234 8286 1296 -542 -331 O
ATOM 1279 CB ARG A 177 -40.732 21.016 -41.907 1.00 64.36 C
ANISOU 1279 CB ARG A 177 7365 9138 7951 1153 -630 -416 C
ATOM 1280 CG ARG A 177 -40.321 22.107 -42.884 1.00 57.32 C
ANISOU 1280 CG ARG A 177 6509 8202 7068 1372 -534 -309 C
ATOM 1281 CD ARG A 177 -39.004 22.747 -42.476 1.00 63.07 C
ANISOU 1281 CD ARG A 177 7314 8659 7989 1356 -479 -213 C
ATOM 1282 NE ARG A 177 -38.680 23.910 -43.293 1.00 58.76 N
ANISOU 1282 NE ARG A 177 6803 8051 7473 1561 -362 -99 N
ATOM 1283 CZ ARG A 177 -37.827 23.900 -44.308 1.00 69.51 C
ANISOU 1283 CZ ARG A 177 8193 9328 8888 1657 -288 -7 C
ATOM 1284 NH1 ARG A 177 -37.186 22.798 -44.661 1.00 65.04 N
ANISOU 1284 NH1 ARG A 177 7632 8734 8347 1572 -326 -18 N
ATOM 1285 NH2 ARG A 177 -37.610 25.025 -44.985 1.00 71.82 N
ANISOU 1285 NH2 ARG A 177 8519 9558 9210 1854 -160 108 N
ATOM 1286 N PRO A 178 -42.976 22.723 -40.388 1.00 64.41 N
ANISOU 1286 N PRO A 178 7292 9381 7798 1263 -615 -460 N
ATOM 1287 CA PRO A 178 -43.719 23.980 -40.205 1.00 66.45 C
ANISOU 1287 CA PRO A 178 7548 9716 7983 1426 -561 -427 C
ATOM 1288 C PRO A 178 -43.661 24.502 -38.782 1.00 72.45 C
ANISOU 1288 C PRO A 178 8366 10356 8806 1362 -567 -427 C
ATOM 1289 O PRO A 178 -43.660 25.723 -38.581 1.00 69.83 O
ANISOU 1289 O PRO A 178 8094 9955 8485 1494 -508 -375 O
ATOM 1290 CB PRO A 178 -45.149 23.609 -40.618 1.00 56.80 C
ANISOU 1290 CB PRO A 178 6197 8798 6585 1472 -592 -499 C
ATOM 1291 CG PRO A 178 -45.242 22.156 -40.352 1.00 56.44 C
ANISOU 1291 CG PRO A 178 6095 8792 6560 1256 -672 -589 C
ATOM 1292 CD PRO A 178 -43.886 21.597 -40.674 1.00 56.91 C
ANISOU 1292 CD PRO A 178 6238 8641 6743 1176 -678 -559 C
ATOM 1293 N LEU A 179 -43.607 23.614 -37.787 1.00 67.43 N
ANISOU 1293 N LEU A 179 7727 9687 8208 1176 -632 -486 N
ATOM 1294 CA LEU A 179 -43.507 24.062 -36.402 1.00 66.65 C
ANISOU 1294 CA LEU A 179 7696 9476 8154 1132 -646 -492 C
ATOM 1295 C LEU A 179 -42.158 24.710 -36.124 1.00 66.40 C
ANISOU 1295 C LEU A 179 7773 9172 8282 1131 -639 -448 C
ATOM 1296 O LEU A 179 -42.071 25.670 -35.351 1.00 69.26 O
ANISOU 1296 O LEU A 179 8206 9432 8677 1186 -629 -440 O
ATOM 1297 CB LEU A 179 -43.734 22.889 -35.450 1.00 69.60 C
ANISOU 1297 CB LEU A 179 8045 9879 8521 951 -704 -556 C
ATOM 1298 CG LEU A 179 -45.097 22.204 -35.523 1.00 64.97 C
ANISOU 1298 CG LEU A 179 7334 9545 7806 916 -707 -607 C
ATOM 1299 CD1 LEU A 179 -45.087 20.925 -34.705 1.00 68.79 C
ANISOU 1299 CD1 LEU A 179 7810 10008 8321 723 -742 -654 C
ATOM 1300 CD2 LEU A 179 -46.189 23.143 -35.039 1.00 64.81 C
ANISOU 1300 CD2 LEU A 179 7285 9662 7677 1047 -670 -597 C
ATOM 1301 N TYR A 180 -41.092 24.203 -36.744 1.00 63.74 N
ANISOU 1301 N TYR A 180 7449 8715 8054 1072 -645 -421 N
ATOM 1302 CA TYR A 180 -39.766 24.732 -36.451 1.00 63.81 C
ANISOU 1302 CA TYR A 180 7537 8470 8240 1050 -644 -383 C
ATOM 1303 C TYR A 180 -39.551 26.097 -37.093 1.00 71.44 C
ANISOU 1303 C TYR A 180 8538 9348 9258 1214 -553 -308 C
ATOM 1304 O TYR A 180 -38.741 26.891 -36.601 1.00 67.23 O
ANISOU 1304 O TYR A 180 8067 8607 8869 1211 -546 -291 O
ATOM 1305 CB TYR A 180 -38.692 23.745 -36.907 1.00 60.73 C
ANISOU 1305 CB TYR A 180 7140 7986 7948 943 -669 -367 C
ATOM 1306 CG TYR A 180 -37.380 23.900 -36.176 1.00 74.27 C
ANISOU 1306 CG TYR A 180 8911 9468 9842 860 -708 -361 C
ATOM 1307 CD1 TYR A 180 -37.172 23.293 -34.943 1.00 70.00 C
ANISOU 1307 CD1 TYR A 180 8397 8886 9312 736 -794 -426 C
ATOM 1308 CD2 TYR A 180 -36.348 24.654 -36.718 1.00 73.97 C
ANISOU 1308 CD2 TYR A 180 8890 9253 9962 912 -655 -289 C
ATOM 1309 CE1 TYR A 180 -35.973 23.434 -34.270 1.00 67.65 C
ANISOU 1309 CE1 TYR A 180 8140 8396 9169 672 -847 -433 C
ATOM 1310 CE2 TYR A 180 -35.147 24.800 -36.052 1.00 75.41 C
ANISOU 1310 CE2 TYR A 180 9100 9232 10322 828 -702 -294 C
ATOM 1311 CZ TYR A 180 -34.964 24.189 -34.831 1.00 68.58 C
ANISOU 1311 CZ TYR A 180 8257 8347 9453 710 -807 -373 C
ATOM 1312 OH TYR A 180 -33.765 24.339 -34.173 1.00 76.32 O
ANISOU 1312 OH TYR A 180 9254 9144 10602 639 -868 -391 O
ATOM 1313 N GLU A 181 -40.264 26.391 -38.182 1.00 74.54 N
ANISOU 1313 N GLU A 181 8891 9893 9539 1364 -481 -266 N
ATOM 1314 CA GLU A 181 -40.152 27.708 -38.801 1.00 67.11 C
ANISOU 1314 CA GLU A 181 7995 8874 8632 1546 -370 -180 C
ATOM 1315 C GLU A 181 -40.732 28.792 -37.899 1.00 73.05 C
ANISOU 1315 C GLU A 181 8803 9598 9354 1616 -354 -199 C
ATOM 1316 O GLU A 181 -40.110 29.844 -37.702 1.00 74.44 O
ANISOU 1316 O GLU A 181 9056 9566 9661 1665 -299 -159 O
ATOM 1317 CB GLU A 181 -40.845 27.706 -40.163 1.00 74.57 C
ANISOU 1317 CB GLU A 181 8888 10016 9430 1718 -300 -134 C
ATOM 1318 CG GLU A 181 -40.173 26.803 -41.187 1.00 80.47 C
ANISOU 1318 CG GLU A 181 9604 10764 10206 1691 -300 -106 C
ATOM 1319 CD GLU A 181 -40.814 26.901 -42.554 1.00 78.21 C
ANISOU 1319 CD GLU A 181 9282 10670 9764 1894 -235 -64 C
ATOM 1320 OE1 GLU A 181 -41.915 27.484 -42.652 1.00 79.21 O
ANISOU 1320 OE1 GLU A 181 9384 10972 9742 2035 -210 -74 O
ATOM 1321 OE2 GLU A 181 -40.214 26.402 -43.531 1.00 72.84 O
ANISOU 1321 OE2 GLU A 181 8600 9974 9102 1928 -210 -22 O
ATOM 1322 N GLU A 182 -41.921 28.550 -37.341 1.00 74.10 N
ANISOU 1322 N GLU A 182 8898 9933 9322 1622 -397 -260 N
ATOM 1323 CA GLU A 182 -42.510 29.468 -36.373 1.00 72.85 C
ANISOU 1323 CA GLU A 182 8801 9762 9118 1689 -389 -281 C
ATOM 1324 C GLU A 182 -41.770 29.456 -35.042 1.00 79.28 C
ANISOU 1324 C GLU A 182 9689 10377 10055 1549 -471 -341 C
ATOM 1325 O GLU A 182 -41.833 30.443 -34.300 1.00 74.88 O
ANISOU 1325 O GLU A 182 9220 9714 9516 1612 -460 -355 O
ATOM 1326 CB GLU A 182 -43.986 29.119 -36.157 1.00 70.80 C
ANISOU 1326 CB GLU A 182 8462 9789 8649 1735 -406 -321 C
ATOM 1327 CG GLU A 182 -44.804 30.222 -35.514 1.00 82.34 C
ANISOU 1327 CG GLU A 182 9982 11288 10016 1882 -361 -314 C
ATOM 1328 CD GLU A 182 -46.271 29.856 -35.388 1.00 94.71 C
ANISOU 1328 CD GLU A 182 11444 13158 11382 1934 -368 -341 C
ATOM 1329 OE1 GLU A 182 -46.654 28.757 -35.844 1.00 98.71 O
ANISOU 1329 OE1 GLU A 182 11828 13841 11837 1846 -411 -373 O
ATOM 1330 OE2 GLU A 182 -47.039 30.670 -34.834 1.00 89.90 O
ANISOU 1330 OE2 GLU A 182 10873 12610 10674 2064 -330 -331 O
ATOM 1331 N TYR A 183 -41.082 28.358 -34.722 1.00 75.68 N
ANISOU 1331 N TYR A 183 9207 9874 9675 1372 -555 -381 N
ATOM 1332 CA TYR A 183 -40.283 28.309 -33.503 1.00 56.67 C
ANISOU 1332 CA TYR A 183 6868 7286 7379 1256 -642 -441 C
ATOM 1333 C TYR A 183 -39.098 29.265 -33.585 1.00 65.86 C
ANISOU 1333 C TYR A 183 8097 8182 8747 1267 -621 -417 C
ATOM 1334 O TYR A 183 -38.759 29.927 -32.598 1.00 66.66 O
ANISOU 1334 O TYR A 183 8276 8134 8917 1256 -670 -472 O
ATOM 1335 CB TYR A 183 -39.828 26.869 -33.251 1.00 67.71 C
ANISOU 1335 CB TYR A 183 8221 8708 8798 1086 -722 -477 C
ATOM 1336 CG TYR A 183 -38.545 26.702 -32.458 1.00 66.01 C
ANISOU 1336 CG TYR A 183 8057 8282 8742 971 -805 -515 C
ATOM 1337 CD1 TYR A 183 -37.320 26.579 -33.103 1.00 70.20 C
ANISOU 1337 CD1 TYR A 183 8571 8661 9442 918 -800 -475 C
ATOM 1338 CD2 TYR A 183 -38.563 26.627 -31.071 1.00 60.75 C
ANISOU 1338 CD2 TYR A 183 7451 7582 8050 929 -890 -590 C
ATOM 1339 CE1 TYR A 183 -36.149 26.412 -32.391 1.00 69.22 C
ANISOU 1339 CE1 TYR A 183 8472 8363 9464 817 -883 -514 C
ATOM 1340 CE2 TYR A 183 -37.394 26.457 -30.350 1.00 66.48 C
ANISOU 1340 CE2 TYR A 183 8216 8135 8908 840 -980 -636 C
ATOM 1341 CZ TYR A 183 -36.190 26.350 -31.016 1.00 62.22 C
ANISOU 1341 CZ TYR A 183 7643 7455 8543 779 -980 -601 C
ATOM 1342 OH TYR A 183 -35.021 26.182 -30.309 1.00 67.52 O
ANISOU 1342 OH TYR A 183 8334 7973 9349 694 -1077 -650 O
ATOM 1343 N VAL A 184 -38.471 29.367 -34.759 1.00 75.39 N
ANISOU 1343 N VAL A 184 9270 9321 10052 1295 -546 -337 N
ATOM 1344 CA VAL A 184 -37.334 30.269 -34.921 1.00 68.58 C
ANISOU 1344 CA VAL A 184 8451 8196 9411 1298 -504 -300 C
ATOM 1345 C VAL A 184 -37.785 31.722 -34.846 1.00 65.25 C
ANISOU 1345 C VAL A 184 8109 7696 8988 1446 -418 -281 C
ATOM 1346 O VAL A 184 -37.091 32.573 -34.276 1.00 65.53 O
ANISOU 1346 O VAL A 184 8210 7501 9188 1420 -430 -312 O
ATOM 1347 CB VAL A 184 -36.603 29.966 -36.242 1.00 61.69 C
ANISOU 1347 CB VAL A 184 7522 7284 8634 1310 -421 -199 C
ATOM 1348 CG1 VAL A 184 -35.537 31.015 -36.520 1.00 57.48 C
ANISOU 1348 CG1 VAL A 184 7021 6481 8340 1330 -341 -139 C
ATOM 1349 CG2 VAL A 184 -35.981 28.579 -36.195 1.00 62.39 C
ANISOU 1349 CG2 VAL A 184 7553 7405 8748 1157 -509 -224 C
ATOM 1350 N VAL A 185 -38.956 32.031 -35.410 1.00 64.05 N
ANISOU 1350 N VAL A 185 7954 7732 8651 1607 -334 -235 N
ATOM 1351 CA VAL A 185 -39.444 33.409 -35.413 1.00 67.50 C
ANISOU 1351 CA VAL A 185 8478 8105 9066 1775 -234 -203 C
ATOM 1352 C VAL A 185 -39.710 33.884 -33.990 1.00 76.30 C
ANISOU 1352 C VAL A 185 9679 9153 10158 1749 -319 -305 C
ATOM 1353 O VAL A 185 -39.282 34.972 -33.589 1.00 74.40 O
ANISOU 1353 O VAL A 185 9535 8690 10043 1781 -291 -322 O
ATOM 1354 CB VAL A 185 -40.702 33.531 -36.292 1.00 63.87 C
ANISOU 1354 CB VAL A 185 7984 7901 8382 1968 -138 -136 C
ATOM 1355 CG1 VAL A 185 -41.285 34.933 -36.193 1.00 67.37 C
ANISOU 1355 CG1 VAL A 185 8529 8292 8776 2159 -32 -102 C
ATOM 1356 CG2 VAL A 185 -40.375 33.186 -37.735 1.00 63.25 C
ANISOU 1356 CG2 VAL A 185 7841 7871 8320 2027 -52 -39 C
ATOM 1357 N LEU A 186 -40.414 33.068 -33.202 1.00 75.28 N
ANISOU 1357 N LEU A 186 9521 9210 9873 1695 -418 -375 N
ATOM 1358 CA LEU A 186 -40.779 33.480 -31.851 1.00 65.40 C
ANISOU 1358 CA LEU A 186 8360 7926 8564 1704 -491 -464 C
ATOM 1359 C LEU A 186 -39.571 33.481 -30.921 1.00 71.28 C
ANISOU 1359 C LEU A 186 9157 8430 9495 1559 -608 -555 C
ATOM 1360 O LEU A 186 -39.464 34.339 -30.037 1.00 68.33 O
ANISOU 1360 O LEU A 186 8893 7911 9158 1594 -646 -625 O
ATOM 1361 CB LEU A 186 -41.880 32.570 -31.308 1.00 64.46 C
ANISOU 1361 CB LEU A 186 8187 8076 8229 1696 -543 -496 C
ATOM 1362 CG LEU A 186 -43.195 32.622 -32.086 1.00 61.00 C
ANISOU 1362 CG LEU A 186 7680 7902 7596 1845 -446 -428 C
ATOM 1363 CD1 LEU A 186 -44.196 31.622 -31.531 1.00 67.69 C
ANISOU 1363 CD1 LEU A 186 8448 9001 8271 1801 -497 -462 C
ATOM 1364 CD2 LEU A 186 -43.769 34.031 -32.064 1.00 65.49 C
ANISOU 1364 CD2 LEU A 186 8348 8433 8101 2048 -351 -395 C
ATOM 1365 N LYS A 187 -38.652 32.529 -31.099 1.00 69.62 N
ANISOU 1365 N LYS A 187 8873 8180 9400 1404 -672 -561 N
ATOM 1366 CA LYS A 187 -37.448 32.509 -30.272 1.00 68.73 C
ANISOU 1366 CA LYS A 187 8790 7855 9468 1274 -791 -648 C
ATOM 1367 C LYS A 187 -36.550 33.702 -30.573 1.00 67.64 C
ANISOU 1367 C LYS A 187 8695 7442 9564 1284 -741 -640 C
ATOM 1368 O LYS A 187 -35.904 34.243 -29.669 1.00 72.24 O
ANISOU 1368 O LYS A 187 9340 7836 10270 1233 -834 -742 O
ATOM 1369 CB LYS A 187 -36.685 31.199 -30.473 1.00 67.56 C
ANISOU 1369 CB LYS A 187 8548 7741 9381 1124 -856 -642 C
ATOM 1370 CG LYS A 187 -37.304 29.993 -29.782 1.00 61.92 C
ANISOU 1370 CG LYS A 187 7815 7227 8487 1074 -933 -683 C
ATOM 1371 CD LYS A 187 -37.184 30.084 -28.270 1.00 63.69 C
ANISOU 1371 CD LYS A 187 8125 7394 8682 1057 -1058 -798 C
ATOM 1372 CE LYS A 187 -37.665 28.804 -27.601 1.00 63.38 C
ANISOU 1372 CE LYS A 187 8068 7531 8484 1007 -1113 -820 C
ATOM 1373 NZ LYS A 187 -37.434 28.816 -26.128 1.00 67.73 N
ANISOU 1373 NZ LYS A 187 8710 8026 8998 1009 -1235 -925 N
ATOM 1374 N ASN A 188 -36.490 34.122 -31.839 1.00 70.29 N
ANISOU 1374 N ASN A 188 8997 7747 9965 1353 -592 -522 N
ATOM 1375 CA ASN A 188 -35.714 35.311 -32.178 1.00 67.19 C
ANISOU 1375 CA ASN A 188 8646 7080 9803 1372 -510 -495 C
ATOM 1376 C ASN A 188 -36.365 36.571 -31.622 1.00 73.52 C
ANISOU 1376 C ASN A 188 9582 7798 10554 1499 -471 -538 C
ATOM 1377 O ASN A 188 -35.668 37.487 -31.168 1.00 71.27 O
ANISOU 1377 O ASN A 188 9363 7251 10465 1462 -488 -602 O
ATOM 1378 CB ASN A 188 -35.534 35.414 -33.692 1.00 62.30 C
ANISOU 1378 CB ASN A 188 7967 6458 9246 1444 -338 -338 C
ATOM 1379 CG ASN A 188 -34.366 34.584 -34.192 1.00 72.31 C
ANISOU 1379 CG ASN A 188 9128 7663 10685 1304 -363 -301 C
ATOM 1380 OD1 ASN A 188 -33.404 34.347 -33.461 1.00 80.00 O
ANISOU 1380 OD1 ASN A 188 10076 8501 11820 1152 -486 -386 O
ATOM 1381 ND2 ASN A 188 -34.439 34.144 -35.444 1.00 74.08 N
ANISOU 1381 ND2 ASN A 188 9289 7993 10865 1370 -250 -174 N
ATOM 1382 N GLU A 189 -37.699 36.637 -31.646 1.00 70.97 N
ANISOU 1382 N GLU A 189 9298 7694 9975 1650 -420 -509 N
ATOM 1383 CA GLU A 189 -38.389 37.759 -31.020 1.00 69.04 C
ANISOU 1383 CA GLU A 189 9191 7390 9650 1787 -388 -551 C
ATOM 1384 C GLU A 189 -38.182 37.770 -29.511 1.00 75.02 C
ANISOU 1384 C GLU A 189 10026 8068 10408 1710 -562 -712 C
ATOM 1385 O GLU A 189 -38.096 38.845 -28.907 1.00 82.20 O
ANISOU 1385 O GLU A 189 11062 8787 11381 1762 -568 -784 O
ATOM 1386 CB GLU A 189 -39.882 37.715 -31.348 1.00 69.86 C
ANISOU 1386 CB GLU A 189 9296 7780 9466 1969 -303 -482 C
ATOM 1387 CG GLU A 189 -40.200 37.939 -32.814 1.00 81.57 C
ANISOU 1387 CG GLU A 189 10730 9345 10918 2101 -128 -332 C
ATOM 1388 CD GLU A 189 -41.688 37.991 -33.082 1.00 93.17 C
ANISOU 1388 CD GLU A 189 12193 11104 12103 2295 -57 -279 C
ATOM 1389 OE1 GLU A 189 -42.461 38.055 -32.104 1.00 92.65 O
ANISOU 1389 OE1 GLU A 189 12178 11139 11885 2337 -120 -347 O
ATOM 1390 OE2 GLU A 189 -42.085 37.967 -34.267 1.00 99.63 O
ANISOU 1390 OE2 GLU A 189 12952 12059 12846 2415 61 -169 O
ATOM 1391 N MET A 190 -38.099 36.593 -28.888 1.00 73.39 N
ANISOU 1391 N MET A 190 9755 8001 10127 1599 -700 -773 N
ATOM 1392 CA MET A 190 -37.839 36.536 -27.454 1.00 76.18 C
ANISOU 1392 CA MET A 190 10186 8289 10470 1546 -868 -923 C
ATOM 1393 C MET A 190 -36.416 36.977 -27.137 1.00 75.22 C
ANISOU 1393 C MET A 190 10074 7873 10633 1413 -961 -1019 C
ATOM 1394 O MET A 190 -36.192 37.741 -26.191 1.00 78.29 O
ANISOU 1394 O MET A 190 10576 8100 11071 1429 -1049 -1147 O
ATOM 1395 CB MET A 190 -38.100 35.123 -26.928 1.00 76.84 C
ANISOU 1395 CB MET A 190 10200 8595 10400 1474 -969 -945 C
ATOM 1396 CG MET A 190 -37.843 34.949 -25.435 1.00 78.08 C
ANISOU 1396 CG MET A 190 10439 8711 10516 1445 -1139 -1090 C
ATOM 1397 SD MET A 190 -36.150 34.476 -25.019 1.00 91.74 S
ANISOU 1397 SD MET A 190 12116 10248 12491 1253 -1305 -1194 S
ATOM 1398 CE MET A 190 -36.156 32.743 -25.471 1.00 85.71 C
ANISOU 1398 CE MET A 190 11213 9708 11646 1152 -1303 -1106 C
ATOM 1399 N ALA A 191 -35.441 36.508 -27.918 1.00 75.62 N
ANISOU 1399 N ALA A 191 10003 7852 10876 1286 -944 -963 N
ATOM 1400 CA ALA A 191 -34.049 36.845 -27.644 1.00 74.51 C
ANISOU 1400 CA ALA A 191 9838 7448 11024 1147 -1034 -1050 C
ATOM 1401 C ALA A 191 -33.763 38.309 -27.948 1.00 69.02 C
ANISOU 1401 C ALA A 191 9216 6482 10527 1187 -934 -1052 C
ATOM 1402 O ALA A 191 -33.024 38.968 -27.208 1.00 72.77 O
ANISOU 1402 O ALA A 191 9737 6730 11181 1116 -1039 -1190 O
ATOM 1403 CB ALA A 191 -33.121 35.937 -28.448 1.00 70.05 C
ANISOU 1403 CB ALA A 191 9117 6892 10605 1015 -1023 -970 C
ATOM 1404 N ARG A 192 -34.333 38.837 -29.033 1.00 79.74 N
ANISOU 1404 N ARG A 192 10586 7855 11856 1306 -729 -904 N
ATOM 1405 CA ARG A 192 -34.119 40.239 -29.372 1.00 81.11 C
ANISOU 1405 CA ARG A 192 10845 7762 12212 1363 -600 -885 C
ATOM 1406 C ARG A 192 -34.838 41.180 -28.417 1.00 80.05 C
ANISOU 1406 C ARG A 192 10888 7566 11961 1478 -636 -996 C
ATOM 1407 O ARG A 192 -34.431 42.339 -28.287 1.00 82.80 O
ANISOU 1407 O ARG A 192 11326 7633 12500 1480 -594 -1048 O
ATOM 1408 CB ARG A 192 -34.555 40.501 -30.815 1.00 76.73 C
ANISOU 1408 CB ARG A 192 10265 7259 11631 1491 -360 -683 C
ATOM 1409 CG ARG A 192 -33.585 39.930 -31.837 1.00 82.65 C
ANISOU 1409 CG ARG A 192 10865 7965 12574 1386 -295 -573 C
ATOM 1410 CD ARG A 192 -34.240 39.657 -33.179 1.00 88.19 C
ANISOU 1410 CD ARG A 192 11526 8853 13130 1534 -109 -384 C
ATOM 1411 NE ARG A 192 -33.351 38.891 -34.046 1.00102.27 N
ANISOU 1411 NE ARG A 192 13170 10634 15052 1440 -75 -290 N
ATOM 1412 CZ ARG A 192 -33.712 38.336 -35.195 1.00105.17 C
ANISOU 1412 CZ ARG A 192 13478 11184 15297 1538 41 -146 C
ATOM 1413 NH1 ARG A 192 -34.948 38.441 -35.655 1.00108.59 N
ANISOU 1413 NH1 ARG A 192 13961 11830 15469 1729 130 -81 N
ATOM 1414 NH2 ARG A 192 -32.811 37.655 -35.898 1.00 97.84 N
ANISOU 1414 NH2 ARG A 192 12437 10234 14506 1452 64 -70 N
ATOM 1415 N ALA A 193 -35.890 40.713 -27.743 1.00 84.43 N
ANISOU 1415 N ALA A 193 11497 8368 12214 1577 -706 -1030 N
ATOM 1416 CA ALA A 193 -36.522 41.528 -26.713 1.00 81.73 C
ANISOU 1416 CA ALA A 193 11331 7976 11748 1694 -757 -1144 C
ATOM 1417 C ALA A 193 -35.716 41.527 -25.421 1.00 82.57 C
ANISOU 1417 C ALA A 193 11481 7933 11959 1575 -984 -1353 C
ATOM 1418 O ALA A 193 -35.809 42.479 -24.638 1.00 78.15 O
ANISOU 1418 O ALA A 193 11076 7210 11409 1639 -1033 -1477 O
ATOM 1419 CB ALA A 193 -37.947 41.044 -26.454 1.00 86.74 C
ANISOU 1419 CB ALA A 193 11999 8933 12027 1854 -736 -1094 C
ATOM 1420 N ASN A 194 -34.928 40.478 -25.183 1.00 85.26 N
ANISOU 1420 N ASN A 194 10602 8974 12819 974 790 -504 N
ATOM 1421 CA ASN A 194 -33.961 40.443 -24.095 1.00 80.09 C
ANISOU 1421 CA ASN A 194 10078 8337 12015 892 882 -630 C
ATOM 1422 C ASN A 194 -32.623 41.061 -24.488 1.00 79.67 C
ANISOU 1422 C ASN A 194 10205 8225 11842 738 795 -645 C
ATOM 1423 O ASN A 194 -31.614 40.808 -23.819 1.00 90.54 O
ANISOU 1423 O ASN A 194 11667 9657 13077 626 829 -730 O
ATOM 1424 CB ASN A 194 -33.755 39.005 -23.612 1.00 79.35 C
ANISOU 1424 CB ASN A 194 9875 8441 11833 825 930 -656 C
ATOM 1425 CG ASN A 194 -34.853 38.544 -22.676 1.00 94.36 C
ANISOU 1425 CG ASN A 194 11654 10384 13816 963 1074 -688 C
ATOM 1426 OD1 ASN A 194 -34.865 38.893 -21.496 1.00115.63 O
ANISOU 1426 OD1 ASN A 194 14432 13031 16473 1020 1209 -792 O
ATOM 1427 ND2 ASN A 194 -35.780 37.750 -23.196 1.00 92.32 N
ANISOU 1427 ND2 ASN A 194 11198 10214 13666 1013 1049 -600 N
ATOM 1428 N HIS A 195 -32.599 41.848 -25.566 1.00 81.07 N
ANISOU 1428 N HIS A 195 10435 8294 12074 726 682 -557 N
ATOM 1429 CA HIS A 195 -31.418 42.599 -26.000 1.00 79.88 C
ANISOU 1429 CA HIS A 195 10457 8062 11831 584 605 -558 C
ATOM 1430 C HIS A 195 -30.284 41.676 -26.450 1.00 77.71 C
ANISOU 1430 C HIS A 195 10161 7955 11412 400 542 -541 C
ATOM 1431 O HIS A 195 -29.109 41.948 -26.201 1.00 80.34 O
ANISOU 1431 O HIS A 195 10615 8281 11631 266 536 -596 O
ATOM 1432 CB HIS A 195 -30.940 43.561 -24.909 1.00 89.33 C
ANISOU 1432 CB HIS A 195 11836 9119 12987 585 690 -684 C
ATOM 1433 CG HIS A 195 -32.033 44.406 -24.333 1.00 89.53 C
ANISOU 1433 CG HIS A 195 11889 8982 13146 779 777 -720 C
ATOM 1434 ND1 HIS A 195 -32.531 44.215 -23.062 1.00 99.78 N
ANISOU 1434 ND1 HIS A 195 13171 10294 14447 884 924 -829 N
ATOM 1435 CD2 HIS A 195 -32.736 45.436 -24.861 1.00 98.75 C
ANISOU 1435 CD2 HIS A 195 13098 9971 14450 895 741 -660 C
ATOM 1436 CE1 HIS A 195 -33.486 45.097 -22.828 1.00105.92 C
ANISOU 1436 CE1 HIS A 195 13975 10909 15359 1060 985 -840 C
ATOM 1437 NE2 HIS A 195 -33.630 45.850 -23.904 1.00 98.98 N
ANISOU 1437 NE2 HIS A 195 13130 9909 14569 1073 871 -738 N
ATOM 1438 N TYR A 196 -30.636 40.586 -27.123 1.00 80.88 N
ANISOU 1438 N TYR A 196 10405 8504 11820 394 494 -466 N
ATOM 1439 CA TYR A 196 -29.670 39.713 -27.771 1.00 84.18 C
ANISOU 1439 CA TYR A 196 10796 9072 12116 239 425 -434 C
ATOM 1440 C TYR A 196 -29.805 39.833 -29.284 1.00 89.03 C
ANISOU 1440 C TYR A 196 11393 9677 12758 209 295 -302 C
ATOM 1441 O TYR A 196 -30.840 40.259 -29.805 1.00 87.12 O
ANISOU 1441 O TYR A 196 11111 9353 12639 323 250 -228 O
ATOM 1442 CB TYR A 196 -29.857 38.253 -27.339 1.00 80.18 C
ANISOU 1442 CB TYR A 196 10143 8748 11573 242 472 -460 C
ATOM 1443 CG TYR A 196 -29.423 37.964 -25.920 1.00 83.55 C
ANISOU 1443 CG TYR A 196 10604 9217 11926 231 587 -584 C
ATOM 1444 CD1 TYR A 196 -30.308 38.107 -24.859 1.00 95.72 C
ANISOU 1444 CD1 TYR A 196 12122 10711 13536 365 701 -645 C
ATOM 1445 CD2 TYR A 196 -28.129 37.541 -25.641 1.00 78.50 C
ANISOU 1445 CD2 TYR A 196 10017 8667 11141 91 582 -635 C
ATOM 1446 CE1 TYR A 196 -29.915 37.842 -23.559 1.00 88.53 C
ANISOU 1446 CE1 TYR A 196 11258 9841 12539 354 804 -755 C
ATOM 1447 CE2 TYR A 196 -27.728 37.273 -24.345 1.00 80.45 C
ANISOU 1447 CE2 TYR A 196 10301 8955 11311 81 672 -742 C
ATOM 1448 CZ TYR A 196 -28.625 37.425 -23.309 1.00 86.22 C
ANISOU 1448 CZ TYR A 196 11026 9636 12099 211 782 -802 C
ATOM 1449 OH TYR A 196 -28.230 37.160 -22.017 1.00 97.35 O
ANISOU 1449 OH TYR A 196 12488 11087 13416 201 870 -907 O
ATOM 1450 N GLU A 197 -28.735 39.458 -29.989 1.00 81.76 N
ANISOU 1450 N GLU A 197 10505 8844 11717 57 234 -272 N
ATOM 1451 CA GLU A 197 -28.756 39.508 -31.449 1.00 66.98 C
ANISOU 1451 CA GLU A 197 8634 6977 9839 15 115 -150 C
ATOM 1452 C GLU A 197 -29.804 38.557 -32.012 1.00 75.86 C
ANISOU 1452 C GLU A 197 9600 8196 11027 95 64 -85 C
ATOM 1453 O GLU A 197 -30.639 38.947 -32.837 1.00 70.91 O
ANISOU 1453 O GLU A 197 8953 7502 10487 168 -21 10 O
ATOM 1454 CB GLU A 197 -27.373 39.166 -32.005 1.00 76.69 C
ANISOU 1454 CB GLU A 197 9917 8303 10918 -162 84 -141 C
ATOM 1455 CG GLU A 197 -26.255 40.070 -31.524 1.00 83.22 C
ANISOU 1455 CG GLU A 197 10888 9048 11684 -267 121 -198 C
ATOM 1456 CD GLU A 197 -24.902 39.645 -32.058 1.00100.10 C
ANISOU 1456 CD GLU A 197 13047 11302 13686 -438 100 -186 C
ATOM 1457 OE1 GLU A 197 -24.837 38.612 -32.760 1.00102.77 O
ANISOU 1457 OE1 GLU A 197 13296 11783 13970 -465 67 -144 O
ATOM 1458 OE2 GLU A 197 -23.904 40.341 -31.777 1.00101.47 O
ANISOU 1458 OE2 GLU A 197 13324 11422 13809 -546 119 -221 O
ATOM 1459 N ASP A 198 -29.772 37.303 -31.576 1.00 81.03 N
ANISOU 1459 N ASP A 198 10144 9002 11640 79 107 -134 N
ATOM 1460 CA ASP A 198 -30.719 36.290 -32.020 1.00 80.42 C
ANISOU 1460 CA ASP A 198 9914 9020 11621 138 61 -83 C
ATOM 1461 C ASP A 198 -30.783 35.212 -30.946 1.00 74.70 C
ANISOU 1461 C ASP A 198 9092 8408 10882 151 162 -169 C
ATOM 1462 O ASP A 198 -30.147 35.320 -29.895 1.00 70.69 O
ANISOU 1462 O ASP A 198 8640 7901 10319 126 258 -262 O
ATOM 1463 CB ASP A 198 -30.319 35.720 -33.385 1.00 71.55 C
ANISOU 1463 CB ASP A 198 8791 7982 10412 42 -54 -3 C
ATOM 1464 CG ASP A 198 -28.864 35.294 -33.437 1.00 69.06 C
ANISOU 1464 CG ASP A 198 8546 7760 9935 -105 -30 -47 C
ATOM 1465 OD1 ASP A 198 -28.528 34.245 -32.851 1.00 75.96 O
ANISOU 1465 OD1 ASP A 198 9354 8753 10756 -134 27 -112 O
ATOM 1466 OD2 ASP A 198 -28.055 36.010 -34.063 1.00 68.64 O
ANISOU 1466 OD2 ASP A 198 8609 7660 9811 -190 -65 -11 O
ATOM 1467 N TYR A 199 -31.565 34.165 -31.217 1.00 71.51 N
ANISOU 1467 N TYR A 199 8546 8098 10528 186 132 -135 N
ATOM 1468 CA TYR A 199 -31.699 33.090 -30.241 1.00 66.27 C
ANISOU 1468 CA TYR A 199 7788 7536 9855 197 225 -202 C
ATOM 1469 C TYR A 199 -30.402 32.307 -30.086 1.00 71.18 C
ANISOU 1469 C TYR A 199 8458 8268 10318 72 245 -256 C
ATOM 1470 O TYR A 199 -30.143 31.747 -29.014 1.00 71.73 O
ANISOU 1470 O TYR A 199 8509 8394 10350 70 340 -330 O
ATOM 1471 CB TYR A 199 -32.846 32.159 -30.632 1.00 65.77 C
ANISOU 1471 CB TYR A 199 7561 7538 9890 251 179 -146 C
ATOM 1472 CG TYR A 199 -33.206 31.160 -29.556 1.00 75.63 C
ANISOU 1472 CG TYR A 199 8707 8869 11160 279 287 -202 C
ATOM 1473 CD1 TYR A 199 -33.342 31.559 -28.232 1.00 71.57 C
ANISOU 1473 CD1 TYR A 199 8210 8313 10670 346 427 -276 C
ATOM 1474 CD2 TYR A 199 -33.421 29.823 -29.864 1.00 71.40 C
ANISOU 1474 CD2 TYR A 199 8069 8447 10614 236 251 -182 C
ATOM 1475 CE1 TYR A 199 -33.673 30.652 -27.243 1.00 72.46 C
ANISOU 1475 CE1 TYR A 199 8240 8501 10792 369 532 -319 C
ATOM 1476 CE2 TYR A 199 -33.754 28.909 -28.881 1.00 69.29 C
ANISOU 1476 CE2 TYR A 199 7714 8246 10366 256 352 -224 C
ATOM 1477 CZ TYR A 199 -33.878 29.329 -27.573 1.00 70.16 C
ANISOU 1477 CZ TYR A 199 7842 8320 10496 322 494 -288 C
ATOM 1478 OH TYR A 199 -34.209 28.423 -26.592 1.00 72.37 O
ANISOU 1478 OH TYR A 199 8045 8667 10784 339 600 -322 O
ATOM 1479 N GLY A 200 -29.578 32.256 -31.134 1.00 69.76 N
ANISOU 1479 N GLY A 200 8339 8122 10044 -28 159 -216 N
ATOM 1480 CA GLY A 200 -28.275 31.626 -31.003 1.00 66.38 C
ANISOU 1480 CA GLY A 200 7954 7793 9474 -140 182 -266 C
ATOM 1481 C GLY A 200 -27.333 32.436 -30.134 1.00 65.15 C
ANISOU 1481 C GLY A 200 7905 7588 9260 -181 253 -337 C
ATOM 1482 O GLY A 200 -26.567 31.877 -29.343 1.00 66.07 O
ANISOU 1482 O GLY A 200 8024 7780 9298 -227 312 -407 O
ATOM 1483 N ASP A 201 -27.374 33.764 -30.268 1.00 66.08 N
ANISOU 1483 N ASP A 201 8117 7573 9418 -167 239 -319 N
ATOM 1484 CA ASP A 201 -26.606 34.624 -29.375 1.00 68.04 C
ANISOU 1484 CA ASP A 201 8474 7752 9627 -204 300 -394 C
ATOM 1485 C ASP A 201 -27.119 34.533 -27.944 1.00 74.37 C
ANISOU 1485 C ASP A 201 9252 8537 10467 -116 405 -479 C
ATOM 1486 O ASP A 201 -26.336 34.661 -26.996 1.00 72.44 O
ANISOU 1486 O ASP A 201 9072 8302 10149 -162 462 -563 O
ATOM 1487 CB ASP A 201 -26.656 36.069 -29.875 1.00 77.95 C
ANISOU 1487 CB ASP A 201 9841 8848 10928 -202 259 -351 C
ATOM 1488 CG ASP A 201 -25.818 37.010 -29.033 1.00 73.80 C
ANISOU 1488 CG ASP A 201 9442 8237 10360 -257 309 -429 C
ATOM 1489 OD1 ASP A 201 -24.590 36.802 -28.950 1.00 77.40 O
ANISOU 1489 OD1 ASP A 201 9933 8765 10709 -382 309 -462 O
ATOM 1490 OD2 ASP A 201 -26.386 37.962 -28.459 1.00 70.69 O
ANISOU 1490 OD2 ASP A 201 9112 7703 10046 -175 346 -458 O
ATOM 1491 N TYR A 202 -28.425 34.314 -27.773 1.00 78.35 N
ANISOU 1491 N TYR A 202 9663 9021 11084 8 431 -457 N
ATOM 1492 CA TYR A 202 -28.980 34.095 -26.442 1.00 71.20 C
ANISOU 1492 CA TYR A 202 8725 8117 10211 94 546 -531 C
ATOM 1493 C TYR A 202 -28.376 32.856 -25.795 1.00 69.19 C
ANISOU 1493 C TYR A 202 8427 8007 9855 36 590 -581 C
ATOM 1494 O TYR A 202 -28.000 32.881 -24.617 1.00 68.71 O
ANISOU 1494 O TYR A 202 8418 7952 9734 37 673 -666 O
ATOM 1495 CB TYR A 202 -30.502 33.975 -26.532 1.00 69.96 C
ANISOU 1495 CB TYR A 202 8447 7930 10204 229 563 -482 C
ATOM 1496 CG TYR A 202 -31.200 33.688 -25.219 1.00 79.33 C
ANISOU 1496 CG TYR A 202 9583 9127 11432 325 698 -546 C
ATOM 1497 CD1 TYR A 202 -31.579 34.720 -24.372 1.00 75.77 C
ANISOU 1497 CD1 TYR A 202 9205 8554 11028 418 787 -604 C
ATOM 1498 CD2 TYR A 202 -31.497 32.384 -24.836 1.00 75.32 C
ANISOU 1498 CD2 TYR A 202 8960 8744 10913 325 741 -547 C
ATOM 1499 CE1 TYR A 202 -32.223 34.464 -23.176 1.00 91.52 C
ANISOU 1499 CE1 TYR A 202 11162 10563 13051 508 924 -662 C
ATOM 1500 CE2 TYR A 202 -32.140 32.119 -23.642 1.00 76.81 C
ANISOU 1500 CE2 TYR A 202 9106 8945 11133 408 874 -597 C
ATOM 1501 CZ TYR A 202 -32.501 33.162 -22.816 1.00 93.33 C
ANISOU 1501 CZ TYR A 202 11273 10925 13264 501 969 -655 C
ATOM 1502 OH TYR A 202 -33.142 32.905 -21.626 1.00108.07 O
ANISOU 1502 OH TYR A 202 13105 12808 15150 586 1115 -705 O
ATOM 1503 N TRP A 203 -28.269 31.762 -26.553 1.00 67.75 N
ANISOU 1503 N TRP A 203 8158 7937 9647 -12 530 -530 N
ATOM 1504 CA TRP A 203 -27.689 30.536 -26.013 1.00 59.59 C
ANISOU 1504 CA TRP A 203 7085 7033 8523 -61 564 -570 C
ATOM 1505 C TRP A 203 -26.222 30.726 -25.651 1.00 63.66 C
ANISOU 1505 C TRP A 203 7699 7580 8908 -164 563 -628 C
ATOM 1506 O TRP A 203 -25.742 30.165 -24.660 1.00 67.69 O
ANISOU 1506 O TRP A 203 8217 8155 9345 -179 620 -690 O
ATOM 1507 CB TRP A 203 -27.841 29.397 -27.017 1.00 55.83 C
ANISOU 1507 CB TRP A 203 6513 6652 8048 -92 491 -505 C
ATOM 1508 CG TRP A 203 -29.159 28.706 -26.949 1.00 64.56 C
ANISOU 1508 CG TRP A 203 7494 7773 9262 -9 510 -469 C
ATOM 1509 CD1 TRP A 203 -30.151 28.915 -26.037 1.00 65.98 C
ANISOU 1509 CD1 TRP A 203 7627 7907 9533 90 600 -487 C
ATOM 1510 CD2 TRP A 203 -29.631 27.683 -27.830 1.00 72.07 C
ANISOU 1510 CD2 TRP A 203 8348 8790 10245 -23 438 -409 C
ATOM 1511 NE1 TRP A 203 -31.215 28.085 -26.297 1.00 67.44 N
ANISOU 1511 NE1 TRP A 203 7678 8131 9814 134 590 -436 N
ATOM 1512 CE2 TRP A 203 -30.920 27.319 -27.394 1.00 76.83 C
ANISOU 1512 CE2 TRP A 203 8838 9386 10970 62 483 -389 C
ATOM 1513 CE3 TRP A 203 -29.090 27.041 -28.948 1.00 62.88 C
ANISOU 1513 CE3 TRP A 203 7185 7690 9016 -101 343 -374 C
ATOM 1514 CZ2 TRP A 203 -31.676 26.340 -28.036 1.00 70.44 C
ANISOU 1514 CZ2 TRP A 203 7914 8625 10223 61 424 -333 C
ATOM 1515 CZ3 TRP A 203 -29.841 26.072 -29.584 1.00 60.07 C
ANISOU 1515 CZ3 TRP A 203 6732 7379 8713 -94 285 -326 C
ATOM 1516 CH2 TRP A 203 -31.120 25.730 -29.127 1.00 67.89 C
ANISOU 1516 CH2 TRP A 203 7609 8357 9831 -19 319 -305 C
ATOM 1517 N ARG A 204 -25.491 31.511 -26.445 1.00 63.58 N
ANISOU 1517 N ARG A 204 7763 7528 8868 -239 497 -605 N
ATOM 1518 CA ARG A 204 -24.074 31.723 -26.182 1.00 65.68 C
ANISOU 1518 CA ARG A 204 8106 7828 9023 -348 490 -653 C
ATOM 1519 C ARG A 204 -23.823 32.574 -24.944 1.00 74.95 C
ANISOU 1519 C ARG A 204 9377 8925 10176 -341 550 -739 C
ATOM 1520 O ARG A 204 -22.664 32.729 -24.547 1.00 71.02 O
ANISOU 1520 O ARG A 204 8937 8458 9588 -434 541 -788 O
ATOM 1521 CB ARG A 204 -23.403 32.360 -27.400 1.00 66.98 C
ANISOU 1521 CB ARG A 204 8319 7964 9166 -438 412 -596 C
ATOM 1522 CG ARG A 204 -23.407 31.468 -28.633 1.00 72.50 C
ANISOU 1522 CG ARG A 204 8944 8755 9849 -463 352 -522 C
ATOM 1523 CD ARG A 204 -22.548 32.038 -29.753 1.00 75.05 C
ANISOU 1523 CD ARG A 204 9326 9069 10121 -565 292 -471 C
ATOM 1524 NE ARG A 204 -23.111 33.248 -30.342 1.00 70.08 N
ANISOU 1524 NE ARG A 204 8767 8301 9560 -543 254 -415 N
ATOM 1525 CZ ARG A 204 -23.932 33.263 -31.384 1.00 67.81 C
ANISOU 1525 CZ ARG A 204 8458 7984 9323 -500 193 -331 C
ATOM 1526 NH1 ARG A 204 -24.330 32.144 -31.966 1.00 60.12 N
ANISOU 1526 NH1 ARG A 204 7397 7106 8340 -478 161 -299 N
ATOM 1527 NH2 ARG A 204 -24.361 34.430 -31.855 1.00 74.84 N
ANISOU 1527 NH2 ARG A 204 9423 8740 10273 -479 155 -278 N
ATOM 1528 N GLY A 205 -24.870 33.119 -24.323 1.00 73.18 N
ANISOU 1528 N GLY A 205 9171 8602 10031 -233 610 -762 N
ATOM 1529 CA GLY A 205 -24.699 33.865 -23.090 1.00 75.18 C
ANISOU 1529 CA GLY A 205 9530 8780 10253 -216 675 -855 C
ATOM 1530 C GLY A 205 -24.298 33.023 -21.897 1.00 71.04 C
ANISOU 1530 C GLY A 205 9000 8357 9635 -223 734 -926 C
ATOM 1531 O GLY A 205 -24.017 33.584 -20.833 1.00 78.73 O
ANISOU 1531 O GLY A 205 10076 9281 10556 -223 779 -1011 O
ATOM 1532 N ASP A 206 -24.268 31.697 -22.044 1.00 70.11 N
ANISOU 1532 N ASP A 206 8776 8373 9490 -229 729 -893 N
ATOM 1533 CA ASP A 206 -23.895 30.843 -20.923 1.00 70.54 C
ANISOU 1533 CA ASP A 206 8828 8521 9452 -232 779 -949 C
ATOM 1534 C ASP A 206 -22.407 30.947 -20.613 1.00 73.76 C
ANISOU 1534 C ASP A 206 9303 8979 9742 -348 728 -998 C
ATOM 1535 O ASP A 206 -21.988 30.681 -19.480 1.00 85.22 O
ANISOU 1535 O ASP A 206 10800 10472 11106 -355 761 -1063 O
ATOM 1536 CB ASP A 206 -24.282 29.397 -21.217 1.00 61.09 C
ANISOU 1536 CB ASP A 206 7504 7438 8268 -207 783 -894 C
ATOM 1537 CG ASP A 206 -24.044 28.485 -20.036 1.00 78.52 C
ANISOU 1537 CG ASP A 206 9713 9731 10390 -197 841 -939 C
ATOM 1538 OD1 ASP A 206 -24.885 28.473 -19.110 1.00 84.35 O
ANISOU 1538 OD1 ASP A 206 10462 10441 11145 -114 935 -966 O
ATOM 1539 OD2 ASP A 206 -23.010 27.786 -20.027 1.00 71.07 O
ANISOU 1539 OD2 ASP A 206 8760 8884 9359 -268 794 -944 O
ATOM 1540 N TYR A 207 -21.604 31.342 -21.599 1.00 73.64 N
ANISOU 1540 N TYR A 207 9292 8963 9724 -442 648 -964 N
ATOM 1541 CA TYR A 207 -20.163 31.490 -21.459 1.00 73.74 C
ANISOU 1541 CA TYR A 207 9344 9028 9644 -562 594 -999 C
ATOM 1542 C TYR A 207 -19.743 32.942 -21.267 1.00 74.09 C
ANISOU 1542 C TYR A 207 9514 8948 9688 -623 573 -1044 C
ATOM 1543 O TYR A 207 -18.543 33.226 -21.190 1.00 79.62 O
ANISOU 1543 O TYR A 207 10246 9679 10326 -738 521 -1071 O
ATOM 1544 CB TYR A 207 -19.458 30.897 -22.683 1.00 71.29 C
ANISOU 1544 CB TYR A 207 8950 8811 9327 -636 530 -930 C
ATOM 1545 CG TYR A 207 -19.781 29.438 -22.949 1.00 71.47 C
ANISOU 1545 CG TYR A 207 8861 8947 9346 -586 541 -889 C
ATOM 1546 CD1 TYR A 207 -20.886 29.070 -23.712 1.00 58.54 C
ANISOU 1546 CD1 TYR A 207 7163 7289 7790 -514 548 -827 C
ATOM 1547 CD2 TYR A 207 -18.972 28.429 -22.444 1.00 71.13 C
ANISOU 1547 CD2 TYR A 207 8777 9026 9224 -612 535 -912 C
ATOM 1548 CE1 TYR A 207 -21.177 27.735 -23.955 1.00 56.74 C
ANISOU 1548 CE1 TYR A 207 6843 7153 7561 -479 552 -794 C
ATOM 1549 CE2 TYR A 207 -19.254 27.096 -22.683 1.00 67.66 C
ANISOU 1549 CE2 TYR A 207 8249 8674 8785 -567 544 -876 C
ATOM 1550 CZ TYR A 207 -20.356 26.753 -23.437 1.00 60.02 C
ANISOU 1550 CZ TYR A 207 7230 7679 7897 -505 553 -820 C
ATOM 1551 OH TYR A 207 -20.630 25.424 -23.670 1.00 60.08 O
ANISOU 1551 OH TYR A 207 7158 7764 7907 -471 556 -789 O
ATOM 1552 N GLU A 208 -20.699 33.865 -21.186 1.00 68.64 N
ANISOU 1552 N GLU A 208 8891 8116 9074 -548 611 -1053 N
ATOM 1553 CA GLU A 208 -20.383 35.283 -21.097 1.00 69.52 C
ANISOU 1553 CA GLU A 208 9133 8085 9196 -601 590 -1092 C
ATOM 1554 C GLU A 208 -19.905 35.648 -19.698 1.00 69.26 C
ANISOU 1554 C GLU A 208 9210 8027 9078 -625 613 -1206 C
ATOM 1555 O GLU A 208 -20.464 35.195 -18.695 1.00 75.01 O
ANISOU 1555 O GLU A 208 9947 8779 9773 -537 683 -1257 O
ATOM 1556 CB GLU A 208 -21.602 36.128 -21.465 1.00 70.29 C
ANISOU 1556 CB GLU A 208 9269 8030 9409 -496 623 -1064 C
ATOM 1557 CG GLU A 208 -21.300 37.611 -21.597 1.00 84.41 C
ANISOU 1557 CG GLU A 208 11197 9652 11225 -550 592 -1087 C
ATOM 1558 CD GLU A 208 -22.517 38.428 -21.982 1.00 91.41 C
ANISOU 1558 CD GLU A 208 12117 10382 12233 -431 621 -1052 C
ATOM 1559 OE1 GLU A 208 -23.632 37.867 -21.990 1.00 84.76 O
ANISOU 1559 OE1 GLU A 208 11186 9565 11454 -302 673 -1022 O
ATOM 1560 OE2 GLU A 208 -22.357 39.631 -22.279 1.00 97.09 O
ANISOU 1560 OE2 GLU A 208 12950 10950 12990 -468 590 -1051 O
ATOM 1561 N VAL A 209 -18.859 36.471 -19.638 1.00 65.62 N
ANISOU 1561 N VAL A 209 8837 7520 8577 -752 551 -1244 N
ATOM 1562 CA VAL A 209 -18.304 36.968 -18.383 1.00 77.32 C
ANISOU 1562 CA VAL A 209 10441 8964 9971 -797 548 -1356 C
ATOM 1563 C VAL A 209 -17.986 38.447 -18.556 1.00 82.66 C
ANISOU 1563 C VAL A 209 11255 9470 10683 -876 509 -1387 C
ATOM 1564 O VAL A 209 -17.314 38.833 -19.518 1.00 82.06 O
ANISOU 1564 O VAL A 209 11157 9383 10639 -986 443 -1327 O
ATOM 1565 CB VAL A 209 -17.040 36.193 -17.960 1.00 74.86 C
ANISOU 1565 CB VAL A 209 10077 8811 9553 -904 487 -1379 C
ATOM 1566 CG1 VAL A 209 -16.380 36.871 -16.769 1.00 79.14 C
ANISOU 1566 CG1 VAL A 209 10760 9303 10007 -975 457 -1493 C
ATOM 1567 CG2 VAL A 209 -17.379 34.746 -17.630 1.00 68.20 C
ANISOU 1567 CG2 VAL A 209 9124 8117 8670 -819 530 -1356 C
ATOM 1568 N ASN A 210 -18.467 39.274 -17.627 1.00 83.68 N
ANISOU 1568 N ASN A 210 11532 9460 10802 -819 554 -1481 N
ATOM 1569 CA ASN A 210 -18.238 40.711 -17.665 1.00 91.99 C
ANISOU 1569 CA ASN A 210 12740 10325 11888 -884 521 -1523 C
ATOM 1570 C ASN A 210 -17.825 41.213 -16.289 1.00 89.20 C
ANISOU 1570 C ASN A 210 12544 9914 11434 -921 520 -1663 C
ATOM 1571 O ASN A 210 -18.217 40.655 -15.260 1.00 97.29 O
ANISOU 1571 O ASN A 210 13587 10995 12384 -833 583 -1729 O
ATOM 1572 CB ASN A 210 -19.487 41.475 -18.129 1.00 83.07 C
ANISOU 1572 CB ASN A 210 11660 9025 10880 -751 582 -1492 C
ATOM 1573 CG ASN A 210 -19.840 41.195 -19.573 1.00 87.87 C
ANISOU 1573 CG ASN A 210 12139 9663 11583 -734 558 -1352 C
ATOM 1574 OD1 ASN A 210 -19.251 41.768 -20.490 1.00104.61 O
ANISOU 1574 OD1 ASN A 210 14275 11736 13736 -844 489 -1291 O
ATOM 1575 ND2 ASN A 210 -20.812 40.317 -19.786 1.00 81.79 N
ANISOU 1575 ND2 ASN A 210 11247 8974 10857 -602 615 -1299 N
ATOM 1576 N GLY A 211 -17.028 42.280 -16.283 1.00 84.57 N
ANISOU 1576 N GLY A 211 12080 9212 10842 -1057 446 -1707 N
ATOM 1577 CA GLY A 211 -16.662 42.962 -15.061 1.00 85.59 C
ANISOU 1577 CA GLY A 211 12389 9250 10882 -1102 430 -1847 C
ATOM 1578 C GLY A 211 -15.485 42.384 -14.307 1.00 89.18 C
ANISOU 1578 C GLY A 211 12823 9854 11207 -1229 350 -1902 C
ATOM 1579 O GLY A 211 -15.150 42.901 -13.233 1.00 99.52 O
ANISOU 1579 O GLY A 211 14289 11098 12426 -1273 324 -2024 O
ATOM 1580 N VAL A 212 -14.845 41.339 -14.822 1.00 83.00 N
ANISOU 1580 N VAL A 212 11859 9267 10411 -1285 306 -1818 N
ATOM 1581 CA VAL A 212 -13.709 40.703 -14.164 1.00 81.93 C
ANISOU 1581 CA VAL A 212 11679 9287 10164 -1395 223 -1856 C
ATOM 1582 C VAL A 212 -12.499 40.873 -15.071 1.00 90.93 C
ANISOU 1582 C VAL A 212 12721 10481 11346 -1576 120 -1788 C
ATOM 1583 O VAL A 212 -12.384 40.191 -16.097 1.00100.70 O
ANISOU 1583 O VAL A 212 13794 11830 12639 -1575 127 -1677 O
ATOM 1584 CB VAL A 212 -13.970 39.221 -13.865 1.00 79.64 C
ANISOU 1584 CB VAL A 212 11255 9188 9817 -1292 267 -1820 C
ATOM 1585 CG1 VAL A 212 -12.868 38.656 -12.980 1.00 79.28 C
ANISOU 1585 CG1 VAL A 212 11194 9283 9646 -1386 177 -1872 C
ATOM 1586 CG2 VAL A 212 -15.333 39.039 -13.213 1.00 66.01 C
ANISOU 1586 CG2 VAL A 212 9597 7406 8078 -1105 394 -1859 C
ATOM 1587 N ASP A 213 -11.598 41.779 -14.698 1.00 87.39 N
ANISOU 1587 N ASP A 213 12376 9956 10872 -1735 28 -1855 N
ATOM 1588 CA ASP A 213 -10.420 42.046 -15.512 1.00 94.99 C
ANISOU 1588 CA ASP A 213 13247 10963 11881 -1922 -63 -1792 C
ATOM 1589 C ASP A 213 -9.551 40.801 -15.630 1.00 98.45 C
ANISOU 1589 C ASP A 213 13484 11644 12277 -1963 -107 -1737 C
ATOM 1590 O ASP A 213 -9.202 40.173 -14.627 1.00107.33 O
ANISOU 1590 O ASP A 213 14603 12877 13302 -1952 -146 -1800 O
ATOM 1591 CB ASP A 213 -9.614 43.200 -14.914 1.00 99.53 C
ANISOU 1591 CB ASP A 213 13972 11414 12432 -2093 -160 -1886 C
ATOM 1592 CG ASP A 213 -10.311 44.535 -15.066 1.00117.02 C
ANISOU 1592 CG ASP A 213 16379 13369 14713 -2077 -125 -1921 C
ATOM 1593 OD1 ASP A 213 -11.395 44.714 -14.470 1.00116.45 O
ANISOU 1593 OD1 ASP A 213 16434 13190 14620 -1918 -43 -1987 O
ATOM 1594 OD2 ASP A 213 -9.775 45.408 -15.780 1.00137.75 O
ANISOU 1594 OD2 ASP A 213 19030 15895 17414 -2221 -174 -1880 O
ATOM 1595 N GLY A 214 -9.205 40.447 -16.866 1.00 93.42 N
ANISOU 1595 N GLY A 214 12691 11092 11714 -2004 -101 -1620 N
ATOM 1596 CA GLY A 214 -8.399 39.276 -17.132 1.00 95.66 C
ANISOU 1596 CA GLY A 214 12778 11597 11973 -2031 -130 -1562 C
ATOM 1597 C GLY A 214 -9.164 37.976 -17.231 1.00 94.73 C
ANISOU 1597 C GLY A 214 12561 11596 11836 -1856 -53 -1518 C
ATOM 1598 O GLY A 214 -8.555 36.942 -17.536 1.00 90.27 O
ANISOU 1598 O GLY A 214 11834 11207 11257 -1861 -69 -1464 O
ATOM 1599 N TYR A 215 -10.477 37.989 -16.988 1.00 89.54 N
ANISOU 1599 N TYR A 215 11994 10844 11185 -1700 32 -1537 N
ATOM 1600 CA TYR A 215 -11.284 36.778 -17.050 1.00 86.14 C
ANISOU 1600 CA TYR A 215 11474 10511 10743 -1541 107 -1495 C
ATOM 1601 C TYR A 215 -12.578 36.970 -17.832 1.00 86.58 C
ANISOU 1601 C TYR A 215 11548 10464 10886 -1421 196 -1440 C
ATOM 1602 O TYR A 215 -13.426 36.069 -17.829 1.00 83.50 O
ANISOU 1602 O TYR A 215 11099 10129 10498 -1285 262 -1411 O
ATOM 1603 CB TYR A 215 -11.601 36.272 -15.637 1.00 84.86 C
ANISOU 1603 CB TYR A 215 11382 10384 10479 -1456 122 -1582 C
ATOM 1604 CG TYR A 215 -10.389 35.777 -14.885 1.00 87.40 C
ANISOU 1604 CG TYR A 215 11658 10841 10707 -1548 26 -1619 C
ATOM 1605 CD1 TYR A 215 -9.968 34.459 -15.001 1.00 88.23 C
ANISOU 1605 CD1 TYR A 215 11608 11128 10786 -1515 14 -1564 C
ATOM 1606 CD2 TYR A 215 -9.661 36.627 -14.064 1.00 82.81 C
ANISOU 1606 CD2 TYR A 215 11191 10204 10068 -1666 -61 -1710 C
ATOM 1607 CE1 TYR A 215 -8.859 34.001 -14.319 1.00 84.28 C
ANISOU 1607 CE1 TYR A 215 11059 10754 10210 -1589 -82 -1591 C
ATOM 1608 CE2 TYR A 215 -8.551 36.178 -13.376 1.00 89.01 C
ANISOU 1608 CE2 TYR A 215 11927 11119 10772 -1752 -164 -1741 C
ATOM 1609 CZ TYR A 215 -8.154 34.863 -13.507 1.00 89.02 C
ANISOU 1609 CZ TYR A 215 11765 11305 10754 -1708 -175 -1678 C
ATOM 1610 OH TYR A 215 -7.048 34.410 -12.825 1.00 97.07 O
ANISOU 1610 OH TYR A 215 12727 12454 11700 -1782 -285 -1701 O
ATOM 1611 N ASP A 216 -12.752 38.107 -18.500 1.00 93.33 N
ANISOU 1611 N ASP A 216 12479 11168 11815 -1470 193 -1419 N
ATOM 1612 CA ASP A 216 -13.963 38.355 -19.266 1.00 82.92 C
ANISOU 1612 CA ASP A 216 11176 9746 10584 -1355 262 -1360 C
ATOM 1613 C ASP A 216 -14.029 37.441 -20.487 1.00 78.57 C
ANISOU 1613 C ASP A 216 10466 9316 10072 -1330 274 -1245 C
ATOM 1614 O ASP A 216 -13.021 36.911 -20.962 1.00 73.85 O
ANISOU 1614 O ASP A 216 9761 8850 9449 -1425 231 -1204 O
ATOM 1615 CB ASP A 216 -14.031 39.818 -19.706 1.00 76.65 C
ANISOU 1615 CB ASP A 216 10510 8756 9857 -1420 243 -1358 C
ATOM 1616 CG ASP A 216 -14.182 40.770 -18.537 1.00 78.09 C
ANISOU 1616 CG ASP A 216 10875 8788 10009 -1420 243 -1480 C
ATOM 1617 OD1 ASP A 216 -14.895 40.421 -17.574 1.00 80.92 O
ANISOU 1617 OD1 ASP A 216 11276 9146 10322 -1297 301 -1549 O
ATOM 1618 OD2 ASP A 216 -13.584 41.865 -18.580 1.00 88.34 O
ANISOU 1618 OD2 ASP A 216 12278 9965 11323 -1547 188 -1507 O
ATOM 1619 N TYR A 217 -15.246 37.264 -20.998 1.00 77.82 N
ANISOU 1619 N TYR A 217 10355 9172 10040 -1198 332 -1195 N
ATOM 1620 CA TYR A 217 -15.477 36.389 -22.145 1.00 77.28 C
ANISOU 1620 CA TYR A 217 10155 9205 10005 -1162 341 -1093 C
ATOM 1621 C TYR A 217 -16.757 36.838 -22.831 1.00 77.30 C
ANISOU 1621 C TYR A 217 10188 9084 10099 -1056 376 -1038 C
ATOM 1622 O TYR A 217 -17.806 36.916 -22.185 1.00 82.03 O
ANISOU 1622 O TYR A 217 10829 9612 10727 -932 430 -1076 O
ATOM 1623 CB TYR A 217 -15.576 34.929 -21.702 1.00 67.21 C
ANISOU 1623 CB TYR A 217 8770 8089 8679 -1087 367 -1100 C
ATOM 1624 CG TYR A 217 -15.352 33.931 -22.814 1.00 71.92 C
ANISOU 1624 CG TYR A 217 9231 8814 9281 -1091 357 -1013 C
ATOM 1625 CD1 TYR A 217 -14.074 33.486 -23.124 1.00 71.62 C
ANISOU 1625 CD1 TYR A 217 9115 8903 9196 -1198 316 -997 C
ATOM 1626 CD2 TYR A 217 -16.417 33.433 -23.551 1.00 74.84 C
ANISOU 1626 CD2 TYR A 217 9551 9179 9707 -988 389 -949 C
ATOM 1627 CE1 TYR A 217 -13.863 32.572 -24.139 1.00 83.94 C
ANISOU 1627 CE1 TYR A 217 10562 10575 10755 -1194 317 -925 C
ATOM 1628 CE2 TYR A 217 -16.217 32.520 -24.568 1.00 74.10 C
ANISOU 1628 CE2 TYR A 217 9352 9195 9609 -994 377 -879 C
ATOM 1629 CZ TYR A 217 -14.938 32.093 -24.858 1.00 75.02 C
ANISOU 1629 CZ TYR A 217 9404 9430 9669 -1093 346 -870 C
ATOM 1630 OH TYR A 217 -14.732 31.184 -25.869 1.00 70.75 O
ANISOU 1630 OH TYR A 217 8769 8995 9118 -1091 344 -808 O
ATOM 1631 N SER A 218 -16.675 37.135 -24.124 1.00 77.36 N
ANISOU 1631 N SER A 218 10173 9070 10150 -1102 348 -945 N
ATOM 1632 CA SER A 218 -17.824 37.621 -24.872 1.00 80.28 C
ANISOU 1632 CA SER A 218 10572 9322 10609 -1009 360 -881 C
ATOM 1633 C SER A 218 -18.561 36.466 -25.543 1.00 74.33 C
ANISOU 1633 C SER A 218 9695 8674 9874 -914 374 -814 C
ATOM 1634 O SER A 218 -18.017 35.377 -25.741 1.00 73.17 O
ANISOU 1634 O SER A 218 9446 8682 9671 -944 368 -801 O
ATOM 1635 CB SER A 218 -17.392 38.648 -25.920 1.00 75.33 C
ANISOU 1635 CB SER A 218 10010 8598 10013 -1112 314 -809 C
ATOM 1636 OG SER A 218 -16.518 38.070 -26.873 1.00 78.72 O
ANISOU 1636 OG SER A 218 10352 9159 10397 -1211 286 -741 O
ATOM 1637 N ARG A 219 -19.825 36.722 -25.893 1.00 74.61 N
ANISOU 1637 N ARG A 219 9738 8616 9995 -797 389 -773 N
ATOM 1638 CA ARG A 219 -20.641 35.685 -26.519 1.00 66.76 C
ANISOU 1638 CA ARG A 219 8630 7707 9030 -709 392 -711 C
ATOM 1639 C ARG A 219 -20.122 35.335 -27.908 1.00 80.71 C
ANISOU 1639 C ARG A 219 10349 9549 10768 -786 336 -620 C
ATOM 1640 O ARG A 219 -20.132 34.163 -28.303 1.00 83.12 O
ANISOU 1640 O ARG A 219 10555 9984 11043 -771 333 -595 O
ATOM 1641 CB ARG A 219 -22.102 36.130 -26.588 1.00 62.89 C
ANISOU 1641 CB ARG A 219 8149 7097 8650 -570 410 -683 C
ATOM 1642 CG ARG A 219 -22.734 36.405 -25.234 1.00 67.14 C
ANISOU 1642 CG ARG A 219 8728 7566 9215 -473 486 -773 C
ATOM 1643 CD ARG A 219 -24.243 36.546 -25.347 1.00 65.73 C
ANISOU 1643 CD ARG A 219 8510 7309 9156 -320 515 -737 C
ATOM 1644 NE ARG A 219 -24.637 37.672 -26.184 1.00 67.90 N
ANISOU 1644 NE ARG A 219 8851 7436 9511 -302 468 -673 N
ATOM 1645 CZ ARG A 219 -24.927 38.881 -25.724 1.00 71.65 C
ANISOU 1645 CZ ARG A 219 9441 7743 10039 -256 493 -711 C
ATOM 1646 NH1 ARG A 219 -24.870 39.160 -24.432 1.00 77.37 N
ANISOU 1646 NH1 ARG A 219 10234 8425 10737 -227 568 -821 N
ATOM 1647 NH2 ARG A 219 -25.284 39.833 -26.581 1.00 75.75 N
ANISOU 1647 NH2 ARG A 219 10018 8128 10636 -237 441 -638 N
ATOM 1648 N GLY A 220 -19.668 36.336 -28.665 1.00 84.63 N
ANISOU 1648 N GLY A 220 10925 9962 11271 -870 298 -570 N
ATOM 1649 CA GLY A 220 -19.099 36.075 -29.975 1.00 77.60 C
ANISOU 1649 CA GLY A 220 10006 9144 10337 -952 257 -485 C
ATOM 1650 C GLY A 220 -17.751 35.390 -29.931 1.00 74.93 C
ANISOU 1650 C GLY A 220 9608 8955 9905 -1064 267 -511 C
ATOM 1651 O GLY A 220 -17.326 34.815 -30.939 1.00 76.81 O
ANISOU 1651 O GLY A 220 9797 9291 10097 -1108 253 -452 O
ATOM 1652 N GLN A 221 -17.069 35.436 -28.784 1.00 71.00 N
ANISOU 1652 N GLN A 221 9119 8481 9379 -1105 289 -598 N
ATOM 1653 CA GLN A 221 -15.776 34.772 -28.660 1.00 78.65 C
ANISOU 1653 CA GLN A 221 10017 9597 10270 -1202 292 -623 C
ATOM 1654 C GLN A 221 -15.921 33.256 -28.678 1.00 74.93 C
ANISOU 1654 C GLN A 221 9430 9275 9764 -1130 309 -628 C
ATOM 1655 O GLN A 221 -14.991 32.551 -29.088 1.00 75.75 O
ANISOU 1655 O GLN A 221 9461 9510 9812 -1190 309 -615 O
ATOM 1656 CB GLN A 221 -15.075 35.228 -27.379 1.00 76.75 C
ANISOU 1656 CB GLN A 221 9816 9337 10008 -1261 293 -716 C
ATOM 1657 CG GLN A 221 -13.623 34.794 -27.268 1.00 81.56 C
ANISOU 1657 CG GLN A 221 10354 10085 10552 -1379 281 -735 C
ATOM 1658 CD GLN A 221 -12.748 35.402 -28.349 1.00104.28 C
ANISOU 1658 CD GLN A 221 13234 12964 13423 -1514 266 -664 C
ATOM 1659 OE1 GLN A 221 -13.003 36.510 -28.821 1.00107.98 O
ANISOU 1659 OE1 GLN A 221 13800 13294 13932 -1555 253 -623 O
ATOM 1660 NE2 GLN A 221 -11.711 34.674 -28.749 1.00104.48 N
ANISOU 1660 NE2 GLN A 221 13153 13144 13400 -1581 272 -645 N
ATOM 1661 N LEU A 222 -17.072 32.738 -28.241 1.00 71.44 N
ANISOU 1661 N LEU A 222 8970 8814 9361 -1003 327 -644 N
ATOM 1662 CA LEU A 222 -17.289 31.295 -28.261 1.00 65.08 C
ANISOU 1662 CA LEU A 222 8064 8132 8530 -938 341 -645 C
ATOM 1663 C LEU A 222 -17.250 30.749 -29.682 1.00 75.00 C
ANISOU 1663 C LEU A 222 9278 9451 9769 -953 317 -568 C
ATOM 1664 O LEU A 222 -16.705 29.666 -29.924 1.00 71.32 O
ANISOU 1664 O LEU A 222 8738 9110 9250 -961 324 -570 O
ATOM 1665 CB LEU A 222 -18.622 30.954 -27.597 1.00 62.23 C
ANISOU 1665 CB LEU A 222 7692 7724 8227 -809 368 -666 C
ATOM 1666 CG LEU A 222 -18.987 29.468 -27.580 1.00 67.58 C
ANISOU 1666 CG LEU A 222 8275 8511 8892 -743 382 -662 C
ATOM 1667 CD1 LEU A 222 -18.088 28.706 -26.617 1.00 59.38 C
ANISOU 1667 CD1 LEU A 222 7201 7576 7783 -766 403 -723 C
ATOM 1668 CD2 LEU A 222 -20.455 29.267 -27.235 1.00 65.79 C
ANISOU 1668 CD2 LEU A 222 8028 8224 8744 -626 406 -656 C
ATOM 1669 N ILE A 223 -17.824 31.485 -30.638 1.00 73.54 N
ANISOU 1669 N ILE A 223 9146 9176 9622 -952 288 -500 N
ATOM 1670 CA ILE A 223 -17.808 31.042 -32.029 1.00 68.57 C
ANISOU 1670 CA ILE A 223 8496 8599 8958 -970 260 -426 C
ATOM 1671 C ILE A 223 -16.377 30.937 -32.538 1.00 72.06 C
ANISOU 1671 C ILE A 223 8923 9140 9318 -1085 274 -417 C
ATOM 1672 O ILE A 223 -16.005 29.955 -33.191 1.00 72.03 O
ANISOU 1672 O ILE A 223 8863 9247 9257 -1088 282 -403 O
ATOM 1673 CB ILE A 223 -18.650 31.989 -32.904 1.00 70.77 C
ANISOU 1673 CB ILE A 223 8849 8753 9286 -953 216 -349 C
ATOM 1674 CG1 ILE A 223 -20.095 32.039 -32.409 1.00 75.16 C
ANISOU 1674 CG1 ILE A 223 9396 9222 9938 -827 205 -355 C
ATOM 1675 CG2 ILE A 223 -18.607 31.550 -34.360 1.00 70.96 C
ANISOU 1675 CG2 ILE A 223 8870 8835 9255 -977 181 -272 C
ATOM 1676 CD1 ILE A 223 -20.988 32.943 -33.231 1.00 76.94 C
ANISOU 1676 CD1 ILE A 223 9684 9325 10227 -792 152 -275 C
ATOM 1677 N GLU A 224 -15.550 31.941 -32.238 1.00 71.06 N
ANISOU 1677 N GLU A 224 8843 8970 9187 -1182 282 -427 N
ATOM 1678 CA GLU A 224 -14.176 31.933 -32.726 1.00 68.14 C
ANISOU 1678 CA GLU A 224 8444 8693 8752 -1301 302 -411 C
ATOM 1679 C GLU A 224 -13.352 30.843 -32.052 1.00 69.00 C
ANISOU 1679 C GLU A 224 8449 8947 8821 -1298 329 -475 C
ATOM 1680 O GLU A 224 -12.509 30.210 -32.696 1.00 67.08 O
ANISOU 1680 O GLU A 224 8143 8822 8522 -1338 352 -456 O
ATOM 1681 CB GLU A 224 -13.536 33.304 -32.507 1.00 77.47 C
ANISOU 1681 CB GLU A 224 9698 9784 9954 -1416 297 -406 C
ATOM 1682 CG GLU A 224 -14.226 34.432 -33.254 1.00 98.59 C
ANISOU 1682 CG GLU A 224 12485 12308 12666 -1425 269 -332 C
ATOM 1683 CD GLU A 224 -13.588 35.780 -32.991 1.00114.10 C
ANISOU 1683 CD GLU A 224 14532 14166 14655 -1544 263 -329 C
ATOM 1684 OE1 GLU A 224 -12.759 35.876 -32.062 1.00108.97 O
ANISOU 1684 OE1 GLU A 224 13854 13550 14001 -1610 272 -398 O
ATOM 1685 OE2 GLU A 224 -13.913 36.743 -33.717 1.00122.36 O
ANISOU 1685 OE2 GLU A 224 15676 15092 15724 -1575 242 -255 O
ATOM 1686 N ASP A 225 -13.582 30.606 -30.758 1.00 73.04 N
ANISOU 1686 N ASP A 225 8945 9450 9356 -1245 328 -548 N
ATOM 1687 CA ASP A 225 -12.809 29.591 -30.050 1.00 66.05 C
ANISOU 1687 CA ASP A 225 7968 8694 8432 -1236 344 -602 C
ATOM 1688 C ASP A 225 -13.214 28.185 -30.475 1.00 65.03 C
ANISOU 1688 C ASP A 225 7774 8652 8281 -1144 356 -592 C
ATOM 1689 O ASP A 225 -12.361 27.298 -30.595 1.00 58.89 O
ANISOU 1689 O ASP A 225 6919 7997 7459 -1153 373 -603 O
ATOM 1690 CB ASP A 225 -12.970 29.765 -28.540 1.00 71.01 C
ANISOU 1690 CB ASP A 225 8619 9285 9078 -1207 336 -678 C
ATOM 1691 CG ASP A 225 -12.257 30.999 -28.016 1.00 81.29 C
ANISOU 1691 CG ASP A 225 9977 10523 10386 -1317 317 -705 C
ATOM 1692 OD1 ASP A 225 -11.299 31.456 -28.674 1.00 81.38 O
ANISOU 1692 OD1 ASP A 225 9971 10566 10384 -1430 313 -671 O
ATOM 1693 OD2 ASP A 225 -12.650 31.508 -26.944 1.00 76.29 O
ANISOU 1693 OD2 ASP A 225 9409 9809 9771 -1294 308 -763 O
ATOM 1694 N VAL A 226 -14.510 27.959 -30.705 1.00 69.20 N
ANISOU 1694 N VAL A 226 8332 9115 8846 -1055 346 -573 N
ATOM 1695 CA VAL A 226 -14.962 26.647 -31.162 1.00 66.86 C
ANISOU 1695 CA VAL A 226 7984 8885 8534 -978 349 -563 C
ATOM 1696 C VAL A 226 -14.417 26.351 -32.553 1.00 72.42 C
ANISOU 1696 C VAL A 226 8679 9655 9182 -1021 352 -515 C
ATOM 1697 O VAL A 226 -13.964 25.235 -32.834 1.00 69.76 O
ANISOU 1697 O VAL A 226 8286 9419 8802 -997 370 -528 O
ATOM 1698 CB VAL A 226 -16.499 26.567 -31.124 1.00 63.79 C
ANISOU 1698 CB VAL A 226 7621 8408 8208 -886 329 -548 C
ATOM 1699 CG1 VAL A 226 -16.990 25.350 -31.892 1.00 53.13 C
ANISOU 1699 CG1 VAL A 226 6232 7111 6844 -832 316 -526 C
ATOM 1700 CG2 VAL A 226 -16.991 26.516 -29.686 1.00 60.64 C
ANISOU 1700 CG2 VAL A 226 7217 7973 7849 -828 349 -603 C
ATOM 1701 N GLU A 227 -14.443 27.345 -33.443 1.00 75.15 N
ANISOU 1701 N GLU A 227 9088 9940 9524 -1082 339 -458 N
ATOM 1702 CA GLU A 227 -13.939 27.137 -34.795 1.00 59.91 C
ANISOU 1702 CA GLU A 227 7165 8072 7526 -1127 351 -407 C
ATOM 1703 C GLU A 227 -12.420 27.009 -34.817 1.00 64.29 C
ANISOU 1703 C GLU A 227 7660 8738 8029 -1206 402 -422 C
ATOM 1704 O GLU A 227 -11.876 26.236 -35.614 1.00 71.68 O
ANISOU 1704 O GLU A 227 8562 9772 8903 -1206 434 -413 O
ATOM 1705 CB GLU A 227 -14.390 28.281 -35.702 1.00 56.84 C
ANISOU 1705 CB GLU A 227 6871 7583 7142 -1172 322 -332 C
ATOM 1706 CG GLU A 227 -15.888 28.319 -35.952 1.00 62.94 C
ANISOU 1706 CG GLU A 227 7688 8260 7966 -1087 265 -302 C
ATOM 1707 CD GLU A 227 -16.314 29.533 -36.754 1.00 86.75 C
ANISOU 1707 CD GLU A 227 10801 11166 10993 -1125 226 -223 C
ATOM 1708 OE1 GLU A 227 -15.488 30.456 -36.917 1.00 92.69 O
ANISOU 1708 OE1 GLU A 227 11595 11898 11725 -1222 250 -196 O
ATOM 1709 OE2 GLU A 227 -17.473 29.562 -37.220 1.00 83.53 O
ANISOU 1709 OE2 GLU A 227 10426 10692 10619 -1060 169 -183 O
ATOM 1710 N HIS A 228 -11.723 27.750 -33.953 1.00 63.95 N
ANISOU 1710 N HIS A 228 7601 8684 8013 -1274 408 -448 N
ATOM 1711 CA HIS A 228 -10.265 27.681 -33.933 1.00 65.25 C
ANISOU 1711 CA HIS A 228 7689 8959 8144 -1357 448 -459 C
ATOM 1712 C HIS A 228 -9.781 26.330 -33.420 1.00 65.40 C
ANISOU 1712 C HIS A 228 7606 9099 8143 -1288 467 -513 C
ATOM 1713 O HIS A 228 -8.870 25.730 -34.001 1.00 65.71 O
ANISOU 1713 O HIS A 228 7577 9252 8139 -1304 512 -506 O
ATOM 1714 CB HIS A 228 -9.698 28.814 -33.081 1.00 67.58 C
ANISOU 1714 CB HIS A 228 7995 9204 8478 -1453 432 -477 C
ATOM 1715 CG HIS A 228 -8.208 28.934 -33.150 1.00 85.28 C
ANISOU 1715 CG HIS A 228 10150 11552 10699 -1560 465 -475 C
ATOM 1716 ND1 HIS A 228 -7.362 28.182 -32.363 1.00 81.23 N
ANISOU 1716 ND1 HIS A 228 9526 11154 10184 -1547 469 -528 N
ATOM 1717 CD2 HIS A 228 -7.411 29.718 -33.915 1.00 95.04 C
ANISOU 1717 CD2 HIS A 228 11388 12801 11922 -1684 496 -420 C
ATOM 1718 CE1 HIS A 228 -6.110 28.497 -32.639 1.00 95.01 C
ANISOU 1718 CE1 HIS A 228 11195 12981 11922 -1655 498 -508 C
ATOM 1719 NE2 HIS A 228 -6.112 29.427 -33.578 1.00 97.48 N
ANISOU 1719 NE2 HIS A 228 11574 13235 12228 -1745 521 -443 N
ATOM 1720 N THR A 229 -10.376 25.836 -32.332 1.00 65.69 N
ANISOU 1720 N THR A 229 7636 9112 8213 -1207 438 -563 N
ATOM 1721 CA THR A 229 -9.991 24.526 -31.819 1.00 69.52 C
ANISOU 1721 CA THR A 229 8036 9696 8680 -1134 450 -606 C
ATOM 1722 C THR A 229 -10.428 23.406 -32.755 1.00 68.27 C
ANISOU 1722 C THR A 229 7877 9574 8490 -1057 468 -592 C
ATOM 1723 O THR A 229 -9.766 22.364 -32.821 1.00 67.72 O
ANISOU 1723 O THR A 229 7737 9602 8391 -1016 495 -613 O
ATOM 1724 CB THR A 229 -10.576 24.304 -30.424 1.00 64.82 C
ANISOU 1724 CB THR A 229 7450 9059 8120 -1072 419 -656 C
ATOM 1725 OG1 THR A 229 -12.003 24.432 -30.473 1.00 62.36 O
ANISOU 1725 OG1 THR A 229 7211 8640 7841 -1012 402 -643 O
ATOM 1726 CG2 THR A 229 -10.013 25.317 -29.441 1.00 63.40 C
ANISOU 1726 CG2 THR A 229 7279 8854 7957 -1149 396 -684 C
ATOM 1727 N PHE A 230 -11.530 23.600 -33.485 1.00 62.19 N
ANISOU 1727 N PHE A 230 7184 8721 7725 -1033 449 -557 N
ATOM 1728 CA PHE A 230 -11.991 22.569 -34.409 1.00 64.40 C
ANISOU 1728 CA PHE A 230 7475 9025 7968 -970 452 -547 C
ATOM 1729 C PHE A 230 -11.045 22.411 -35.592 1.00 63.27 C
ANISOU 1729 C PHE A 230 7321 8969 7751 -1014 502 -524 C
ATOM 1730 O PHE A 230 -10.947 21.317 -36.159 1.00 65.19 O
ANISOU 1730 O PHE A 230 7551 9269 7950 -958 523 -540 O
ATOM 1731 CB PHE A 230 -13.404 22.888 -34.897 1.00 63.85 C
ANISOU 1731 CB PHE A 230 7486 8849 7926 -942 404 -512 C
ATOM 1732 CG PHE A 230 -13.972 21.850 -35.822 1.00 66.87 C
ANISOU 1732 CG PHE A 230 7890 9247 8272 -886 389 -506 C
ATOM 1733 CD1 PHE A 230 -14.440 20.644 -35.326 1.00 67.43 C
ANISOU 1733 CD1 PHE A 230 7928 9329 8365 -805 378 -545 C
ATOM 1734 CD2 PHE A 230 -14.039 22.078 -37.186 1.00 66.52 C
ANISOU 1734 CD2 PHE A 230 7907 9201 8165 -919 382 -460 C
ATOM 1735 CE1 PHE A 230 -14.962 19.684 -36.173 1.00 66.10 C
ANISOU 1735 CE1 PHE A 230 7787 9164 8165 -762 357 -545 C
ATOM 1736 CE2 PHE A 230 -14.561 21.123 -38.038 1.00 70.08 C
ANISOU 1736 CE2 PHE A 230 8390 9662 8573 -872 359 -462 C
ATOM 1737 CZ PHE A 230 -15.023 19.924 -37.530 1.00 60.92 C
ANISOU 1737 CZ PHE A 230 7195 8507 7443 -796 344 -508 C
ATOM 1738 N GLU A 231 -10.348 23.482 -35.979 1.00 59.88 N
ANISOU 1738 N GLU A 231 6900 8545 7306 -1114 526 -486 N
ATOM 1739 CA GLU A 231 -9.367 23.370 -37.054 1.00 67.69 C
ANISOU 1739 CA GLU A 231 7870 9627 8223 -1162 592 -460 C
ATOM 1740 C GLU A 231 -8.235 22.423 -36.679 1.00 72.81 C
ANISOU 1740 C GLU A 231 8402 10402 8860 -1130 644 -506 C
ATOM 1741 O GLU A 231 -7.676 21.749 -37.552 1.00 87.09 O
ANISOU 1741 O GLU A 231 10191 12294 10606 -1110 704 -506 O
ATOM 1742 CB GLU A 231 -8.810 24.750 -37.409 1.00 68.78 C
ANISOU 1742 CB GLU A 231 8033 9743 8357 -1288 611 -405 C
ATOM 1743 CG GLU A 231 -9.760 25.614 -38.223 1.00 72.98 C
ANISOU 1743 CG GLU A 231 8691 10164 8876 -1317 573 -340 C
ATOM 1744 CD GLU A 231 -9.980 25.078 -39.626 1.00 94.12 C
ANISOU 1744 CD GLU A 231 11429 12873 11459 -1293 595 -306 C
ATOM 1745 OE1 GLU A 231 -9.079 24.390 -40.153 1.00 86.69 O
ANISOU 1745 OE1 GLU A 231 10439 12047 10454 -1293 669 -320 O
ATOM 1746 OE2 GLU A 231 -11.057 25.341 -40.202 1.00106.45 O
ANISOU 1746 OE2 GLU A 231 13089 14347 13010 -1272 536 -267 O
ATOM 1747 N GLU A 232 -7.890 22.351 -35.393 1.00 63.65 N
ANISOU 1747 N GLU A 232 7170 9258 7756 -1120 621 -547 N
ATOM 1748 CA GLU A 232 -6.847 21.440 -34.943 1.00 62.38 C
ANISOU 1748 CA GLU A 232 6892 9214 7595 -1079 655 -586 C
ATOM 1749 C GLU A 232 -7.349 20.010 -34.787 1.00 66.83 C
ANISOU 1749 C GLU A 232 7456 9785 8150 -950 646 -626 C
ATOM 1750 O GLU A 232 -6.532 19.083 -34.737 1.00 69.59 O
ANISOU 1750 O GLU A 232 7725 10229 8489 -896 683 -653 O
ATOM 1751 CB GLU A 232 -6.259 21.939 -33.623 1.00 74.24 C
ANISOU 1751 CB GLU A 232 8325 10731 9152 -1123 619 -610 C
ATOM 1752 CG GLU A 232 -6.024 23.442 -33.593 1.00 79.02 C
ANISOU 1752 CG GLU A 232 8957 11286 9779 -1255 607 -577 C
ATOM 1753 CD GLU A 232 -5.364 23.905 -32.312 1.00 88.92 C
ANISOU 1753 CD GLU A 232 10148 12558 11078 -1307 564 -609 C
ATOM 1754 OE1 GLU A 232 -4.318 23.331 -31.944 1.00 83.35 O
ANISOU 1754 OE1 GLU A 232 9323 11968 10378 -1298 576 -629 O
ATOM 1755 OE2 GLU A 232 -5.896 24.836 -31.669 1.00 98.51 O
ANISOU 1755 OE2 GLU A 232 11435 13671 12323 -1353 514 -615 O
ATOM 1756 N ILE A 233 -8.667 19.812 -34.707 1.00 61.31 N
ANISOU 1756 N ILE A 233 6843 8987 7465 -900 596 -628 N
ATOM 1757 CA ILE A 233 -9.229 18.467 -34.656 1.00 68.37 C
ANISOU 1757 CA ILE A 233 7749 9875 8355 -792 585 -660 C
ATOM 1758 C ILE A 233 -9.325 17.840 -36.041 1.00 73.76 C
ANISOU 1758 C ILE A 233 8479 10575 8969 -766 619 -654 C
ATOM 1759 O ILE A 233 -9.354 16.608 -36.156 1.00 71.64 O
ANISOU 1759 O ILE A 233 8207 10327 8685 -682 628 -689 O
ATOM 1760 CB ILE A 233 -10.615 18.491 -33.986 1.00 66.84 C
ANISOU 1760 CB ILE A 233 7613 9571 8212 -758 522 -662 C
ATOM 1761 CG1 ILE A 233 -10.556 19.248 -32.658 1.00 71.47 C
ANISOU 1761 CG1 ILE A 233 8175 10132 8849 -788 497 -671 C
ATOM 1762 CG2 ILE A 233 -11.140 17.080 -33.744 1.00 63.34 C
ANISOU 1762 CG2 ILE A 233 7172 9118 7776 -658 510 -692 C
ATOM 1763 CD1 ILE A 233 -11.889 19.317 -31.940 1.00 64.55 C
ANISOU 1763 CD1 ILE A 233 7350 9154 8023 -750 455 -673 C
ATOM 1764 N LYS A 234 -9.365 18.656 -37.096 1.00 68.07 N
ANISOU 1764 N LYS A 234 7816 9843 8203 -836 635 -612 N
ATOM 1765 CA LYS A 234 -9.548 18.147 -38.455 1.00 65.06 C
ANISOU 1765 CA LYS A 234 7507 9474 7740 -817 660 -606 C
ATOM 1766 C LYS A 234 -8.553 17.062 -38.851 1.00 67.25 C
ANISOU 1766 C LYS A 234 7733 9852 7965 -758 737 -647 C
ATOM 1767 O LYS A 234 -8.988 16.044 -39.410 1.00 68.11 O
ANISOU 1767 O LYS A 234 7899 9946 8033 -688 732 -678 O
ATOM 1768 CB LYS A 234 -9.504 19.315 -39.450 1.00 70.89 C
ANISOU 1768 CB LYS A 234 8310 10199 8426 -912 676 -544 C
ATOM 1769 CG LYS A 234 -10.711 20.236 -39.396 1.00 64.20 C
ANISOU 1769 CG LYS A 234 7544 9233 7618 -946 593 -500 C
ATOM 1770 CD LYS A 234 -10.636 21.290 -40.488 1.00 76.26 C
ANISOU 1770 CD LYS A 234 9149 10744 9083 -1034 606 -431 C
ATOM 1771 CE LYS A 234 -11.897 22.135 -40.539 1.00 67.64 C
ANISOU 1771 CE LYS A 234 8141 9527 8032 -1050 516 -384 C
ATOM 1772 NZ LYS A 234 -11.843 23.136 -41.641 1.00 82.88 N
ANISOU 1772 NZ LYS A 234 10161 11434 9896 -1130 522 -307 N
ATOM 1773 N PRO A 235 -7.240 17.195 -38.611 1.00 62.28 N
ANISOU 1773 N PRO A 235 6998 9324 7341 -779 807 -651 N
ATOM 1774 CA PRO A 235 -6.330 16.109 -39.021 1.00 60.86 C
ANISOU 1774 CA PRO A 235 6765 9240 7120 -704 886 -691 C
ATOM 1775 C PRO A 235 -6.637 14.779 -38.357 1.00 63.55 C
ANISOU 1775 C PRO A 235 7093 9557 7496 -586 852 -746 C
ATOM 1776 O PRO A 235 -6.604 13.737 -39.024 1.00 64.11 O
ANISOU 1776 O PRO A 235 7204 9638 7516 -508 887 -783 O
ATOM 1777 CB PRO A 235 -4.948 16.642 -38.617 1.00 54.91 C
ANISOU 1777 CB PRO A 235 5871 8594 6398 -756 948 -677 C
ATOM 1778 CG PRO A 235 -5.103 18.115 -38.602 1.00 62.56 C
ANISOU 1778 CG PRO A 235 6865 9525 7382 -884 923 -620 C
ATOM 1779 CD PRO A 235 -6.492 18.353 -38.092 1.00 60.01 C
ANISOU 1779 CD PRO A 235 6636 9072 7094 -876 820 -618 C
ATOM 1780 N LEU A 236 -6.939 14.783 -37.057 1.00 61.18 N
ANISOU 1780 N LEU A 236 6750 9219 7276 -571 787 -751 N
ATOM 1781 CA LEU A 236 -7.281 13.537 -36.380 1.00 61.47 C
ANISOU 1781 CA LEU A 236 6786 9224 7346 -466 754 -792 C
ATOM 1782 C LEU A 236 -8.592 12.965 -36.903 1.00 60.64 C
ANISOU 1782 C LEU A 236 6802 9017 7220 -435 707 -802 C
ATOM 1783 O LEU A 236 -8.711 11.750 -37.100 1.00 63.07 O
ANISOU 1783 O LEU A 236 7140 9309 7515 -350 711 -841 O
ATOM 1784 CB LEU A 236 -7.360 13.762 -34.870 1.00 67.46 C
ANISOU 1784 CB LEU A 236 7486 9966 8180 -467 697 -788 C
ATOM 1785 CG LEU A 236 -7.869 12.583 -34.036 1.00 51.00 C
ANISOU 1785 CG LEU A 236 5413 7832 6131 -370 656 -815 C
ATOM 1786 CD1 LEU A 236 -6.981 11.361 -34.225 1.00 52.61 C
ANISOU 1786 CD1 LEU A 236 5570 8099 6321 -271 704 -849 C
ATOM 1787 CD2 LEU A 236 -7.963 12.961 -32.568 1.00 50.51 C
ANISOU 1787 CD2 LEU A 236 5310 7756 6125 -384 605 -805 C
ATOM 1788 N TYR A 237 -9.586 13.824 -37.142 1.00 56.99 N
ANISOU 1788 N TYR A 237 6410 8482 6762 -502 655 -767 N
ATOM 1789 CA TYR A 237 -10.885 13.334 -37.591 1.00 60.54 C
ANISOU 1789 CA TYR A 237 6958 8837 7207 -481 595 -771 C
ATOM 1790 C TYR A 237 -10.827 12.833 -39.029 1.00 68.17 C
ANISOU 1790 C TYR A 237 8008 9817 8078 -468 623 -789 C
ATOM 1791 O TYR A 237 -11.494 11.851 -39.374 1.00 62.83 O
ANISOU 1791 O TYR A 237 7398 9086 7388 -419 587 -820 O
ATOM 1792 CB TYR A 237 -11.943 14.427 -37.446 1.00 55.09 C
ANISOU 1792 CB TYR A 237 6306 8069 6556 -548 530 -724 C
ATOM 1793 CG TYR A 237 -13.301 14.023 -37.974 1.00 53.47 C
ANISOU 1793 CG TYR A 237 6187 7775 6356 -535 458 -720 C
ATOM 1794 CD1 TYR A 237 -14.074 13.081 -37.308 1.00 56.25 C
ANISOU 1794 CD1 TYR A 237 6536 8069 6767 -480 416 -742 C
ATOM 1795 CD2 TYR A 237 -13.809 14.583 -39.139 1.00 60.04 C
ANISOU 1795 CD2 TYR A 237 7100 8579 7133 -582 428 -688 C
ATOM 1796 CE1 TYR A 237 -15.316 12.707 -37.788 1.00 55.24 C
ANISOU 1796 CE1 TYR A 237 6472 7862 6656 -478 344 -736 C
ATOM 1797 CE2 TYR A 237 -15.050 14.217 -39.626 1.00 56.73 C
ANISOU 1797 CE2 TYR A 237 6750 8082 6722 -575 346 -682 C
ATOM 1798 CZ TYR A 237 -15.798 13.280 -38.947 1.00 53.20 C
ANISOU 1798 CZ TYR A 237 6285 7582 6346 -526 304 -707 C
ATOM 1799 OH TYR A 237 -17.033 12.916 -39.431 1.00 59.07 O
ANISOU 1799 OH TYR A 237 7083 8251 7109 -528 218 -699 O
ATOM 1800 N GLU A 238 -10.040 13.493 -39.884 1.00 66.19 N
ANISOU 1800 N GLU A 238 7759 9635 7755 -517 687 -770 N
ATOM 1801 CA GLU A 238 -9.940 13.059 -41.274 1.00 68.51 C
ANISOU 1801 CA GLU A 238 8145 9948 7938 -506 725 -788 C
ATOM 1802 C GLU A 238 -9.313 11.675 -41.378 1.00 66.64 C
ANISOU 1802 C GLU A 238 7897 9748 7675 -404 782 -856 C
ATOM 1803 O GLU A 238 -9.730 10.857 -42.206 1.00 71.15 O
ANISOU 1803 O GLU A 238 8571 10282 8179 -365 770 -896 O
ATOM 1804 CB GLU A 238 -9.140 14.073 -42.093 1.00 77.68 C
ANISOU 1804 CB GLU A 238 9307 11184 9025 -582 800 -746 C
ATOM 1805 CG GLU A 238 -9.893 15.355 -42.405 1.00 82.18 C
ANISOU 1805 CG GLU A 238 9939 11695 9591 -678 740 -676 C
ATOM 1806 CD GLU A 238 -9.109 16.280 -43.315 1.00 86.64 C
ANISOU 1806 CD GLU A 238 10522 12326 10072 -758 819 -628 C
ATOM 1807 OE1 GLU A 238 -8.175 15.799 -43.989 1.00 96.78 O
ANISOU 1807 OE1 GLU A 238 11798 13698 11276 -734 921 -653 O
ATOM 1808 OE2 GLU A 238 -9.426 17.488 -43.352 1.00 90.73 O
ANISOU 1808 OE2 GLU A 238 11064 12804 10606 -842 784 -563 O
ATOM 1809 N HIS A 239 -8.307 11.393 -40.548 1.00 60.69 N
ANISOU 1809 N HIS A 239 7023 9062 6973 -358 836 -873 N
ATOM 1810 CA HIS A 239 -7.708 10.064 -40.546 1.00 65.10 C
ANISOU 1810 CA HIS A 239 7565 9647 7523 -246 887 -935 C
ATOM 1811 C HIS A 239 -8.612 9.035 -39.880 1.00 70.53 C
ANISOU 1811 C HIS A 239 8294 10233 8269 -182 805 -965 C
ATOM 1812 O HIS A 239 -8.616 7.867 -40.285 1.00 71.67 O
ANISOU 1812 O HIS A 239 8499 10348 8384 -101 819 -1019 O
ATOM 1813 CB HIS A 239 -6.341 10.099 -39.864 1.00 67.81 C
ANISOU 1813 CB HIS A 239 7754 10098 7911 -214 960 -934 C
ATOM 1814 CG HIS A 239 -5.250 10.640 -40.735 1.00 63.83 C
ANISOU 1814 CG HIS A 239 7205 9706 7341 -247 1074 -923 C
ATOM 1815 ND1 HIS A 239 -4.586 9.864 -41.660 1.00 69.56 N
ANISOU 1815 ND1 HIS A 239 7954 10485 7991 -172 1174 -969 N
ATOM 1816 CD2 HIS A 239 -4.713 11.879 -40.828 1.00 64.87 C
ANISOU 1816 CD2 HIS A 239 7272 9903 7470 -350 1109 -869 C
ATOM 1817 CE1 HIS A 239 -3.684 10.601 -42.284 1.00 67.27 C
ANISOU 1817 CE1 HIS A 239 7607 10297 7654 -227 1274 -940 C
ATOM 1818 NE2 HIS A 239 -3.740 11.827 -41.797 1.00 69.44 N
ANISOU 1818 NE2 HIS A 239 7829 10581 7976 -341 1234 -877 N
ATOM 1819 N LEU A 240 -9.375 9.440 -38.863 1.00 69.99 N
ANISOU 1819 N LEU A 240 8200 10108 8285 -218 725 -930 N
ATOM 1820 CA LEU A 240 -10.406 8.557 -38.329 1.00 62.78 C
ANISOU 1820 CA LEU A 240 7337 9092 7426 -177 649 -947 C
ATOM 1821 C LEU A 240 -11.506 8.328 -39.357 1.00 66.03 C
ANISOU 1821 C LEU A 240 7876 9422 7788 -205 593 -957 C
ATOM 1822 O LEU A 240 -11.980 7.199 -39.527 1.00 61.59 O
ANISOU 1822 O LEU A 240 7382 8792 7227 -154 562 -998 O
ATOM 1823 CB LEU A 240 -10.984 9.137 -37.039 1.00 56.00 C
ANISOU 1823 CB LEU A 240 6421 8198 6658 -213 592 -904 C
ATOM 1824 CG LEU A 240 -12.126 8.350 -36.392 1.00 61.74 C
ANISOU 1824 CG LEU A 240 7189 8822 7450 -185 522 -907 C
ATOM 1825 CD1 LEU A 240 -11.651 6.976 -35.942 1.00 66.40 C
ANISOU 1825 CD1 LEU A 240 7771 9402 8056 -86 542 -945 C
ATOM 1826 CD2 LEU A 240 -12.727 9.121 -35.225 1.00 56.44 C
ANISOU 1826 CD2 LEU A 240 6469 8123 6853 -228 482 -863 C
ATOM 1827 N HIS A 241 -11.915 9.389 -40.056 1.00 68.41 N
ANISOU 1827 N HIS A 241 8218 9726 8049 -288 571 -919 N
ATOM 1828 CA HIS A 241 -12.915 9.252 -41.110 1.00 62.45 C
ANISOU 1828 CA HIS A 241 7585 8904 7240 -320 504 -923 C
ATOM 1829 C HIS A 241 -12.405 8.370 -42.242 1.00 70.21 C
ANISOU 1829 C HIS A 241 8659 9908 8112 -272 554 -985 C
ATOM 1830 O HIS A 241 -13.134 7.507 -42.744 1.00 71.15 O
ANISOU 1830 O HIS A 241 8877 9952 8206 -254 494 -1024 O
ATOM 1831 CB HIS A 241 -13.306 10.635 -41.634 1.00 59.52 C
ANISOU 1831 CB HIS A 241 7235 8538 6841 -411 475 -861 C
ATOM 1832 CG HIS A 241 -14.286 10.606 -42.767 1.00 68.00 C
ANISOU 1832 CG HIS A 241 8433 9554 7850 -446 394 -856 C
ATOM 1833 ND1 HIS A 241 -13.910 10.365 -44.071 1.00 61.92 N
ANISOU 1833 ND1 HIS A 241 7766 8815 6944 -447 427 -883 N
ATOM 1834 CD2 HIS A 241 -15.625 10.801 -42.792 1.00 65.14 C
ANISOU 1834 CD2 HIS A 241 8105 9107 7538 -482 280 -825 C
ATOM 1835 CE1 HIS A 241 -14.977 10.403 -44.849 1.00 65.59 C
ANISOU 1835 CE1 HIS A 241 8333 9215 7371 -485 323 -870 C
ATOM 1836 NE2 HIS A 241 -16.031 10.668 -44.098 1.00 57.15 N
ANISOU 1836 NE2 HIS A 241 7216 8077 6422 -507 230 -833 N
ATOM 1837 N ALA A 242 -11.150 8.570 -42.655 1.00 66.97 N
ANISOU 1837 N ALA A 242 8216 9598 7633 -253 665 -997 N
ATOM 1838 CA ALA A 242 -10.596 7.776 -43.747 1.00 60.68 C
ANISOU 1838 CA ALA A 242 7508 8828 6722 -199 733 -1060 C
ATOM 1839 C ALA A 242 -10.482 6.306 -43.363 1.00 64.08 C
ANISOU 1839 C ALA A 242 7951 9210 7187 -93 739 -1130 C
ATOM 1840 O ALA A 242 -10.790 5.424 -44.172 1.00 72.04 O
ANISOU 1840 O ALA A 242 9085 10164 8124 -58 724 -1191 O
ATOM 1841 CB ALA A 242 -9.235 8.332 -44.163 1.00 68.13 C
ANISOU 1841 CB ALA A 242 8388 9897 7600 -199 868 -1050 C
ATOM 1842 N TYR A 243 -10.042 6.023 -42.134 1.00 67.64 N
ANISOU 1842 N TYR A 243 8283 9674 7743 -42 754 -1124 N
ATOM 1843 CA TYR A 243 -9.914 4.634 -41.703 1.00 63.13 C
ANISOU 1843 CA TYR A 243 7726 9048 7212 63 756 -1180 C
ATOM 1844 C TYR A 243 -11.275 3.955 -41.613 1.00 66.64 C
ANISOU 1844 C TYR A 243 8269 9357 7694 44 640 -1193 C
ATOM 1845 O TYR A 243 -11.426 2.800 -42.030 1.00 61.99 O
ANISOU 1845 O TYR A 243 7779 8698 7079 103 631 -1257 O
ATOM 1846 CB TYR A 243 -9.190 4.557 -40.358 1.00 64.09 C
ANISOU 1846 CB TYR A 243 7703 9215 7436 115 783 -1156 C
ATOM 1847 CG TYR A 243 -9.156 3.159 -39.778 1.00 64.73 C
ANISOU 1847 CG TYR A 243 7801 9224 7569 222 771 -1199 C
ATOM 1848 CD1 TYR A 243 -8.228 2.224 -40.222 1.00 63.10 C
ANISOU 1848 CD1 TYR A 243 7611 9040 7325 335 853 -1261 C
ATOM 1849 CD2 TYR A 243 -10.057 2.770 -38.793 1.00 60.36 C
ANISOU 1849 CD2 TYR A 243 7252 8576 7105 213 682 -1174 C
ATOM 1850 CE1 TYR A 243 -8.197 0.943 -39.701 1.00 58.54 C
ANISOU 1850 CE1 TYR A 243 7060 8383 6799 438 839 -1296 C
ATOM 1851 CE2 TYR A 243 -10.033 1.491 -38.267 1.00 62.02 C
ANISOU 1851 CE2 TYR A 243 7490 8712 7363 304 671 -1203 C
ATOM 1852 CZ TYR A 243 -9.101 0.582 -38.724 1.00 64.99 C
ANISOU 1852 CZ TYR A 243 7889 9102 7703 418 744 -1264 C
ATOM 1853 OH TYR A 243 -9.073 -0.692 -38.202 1.00 62.03 O
ANISOU 1853 OH TYR A 243 7550 8640 7380 514 730 -1290 O
ATOM 1854 N VAL A 244 -12.273 4.651 -41.064 1.00 66.23 N
ANISOU 1854 N VAL A 244 8190 9264 7710 -37 553 -1133 N
ATOM 1855 CA VAL A 244 -13.614 4.080 -40.964 1.00 61.56 C
ANISOU 1855 CA VAL A 244 7670 8552 7168 -66 443 -1135 C
ATOM 1856 C VAL A 244 -14.182 3.811 -42.351 1.00 67.20 C
ANISOU 1856 C VAL A 244 8530 9220 7783 -99 395 -1176 C
ATOM 1857 O VAL A 244 -14.807 2.770 -42.591 1.00 58.75 O
ANISOU 1857 O VAL A 244 7551 8053 6719 -85 335 -1222 O
ATOM 1858 CB VAL A 244 -14.531 5.007 -40.143 1.00 61.31 C
ANISOU 1858 CB VAL A 244 7567 8499 7229 -143 375 -1060 C
ATOM 1859 CG1 VAL A 244 -15.985 4.587 -40.287 1.00 55.40 C
ANISOU 1859 CG1 VAL A 244 6883 7640 6528 -190 262 -1055 C
ATOM 1860 CG2 VAL A 244 -14.121 4.995 -38.679 1.00 61.63 C
ANISOU 1860 CG2 VAL A 244 7493 8561 7362 -105 407 -1032 C
ATOM 1861 N ARG A 245 -13.962 4.737 -43.288 1.00 71.76 N
ANISOU 1861 N ARG A 245 9139 9863 8263 -149 417 -1160 N
ATOM 1862 CA ARG A 245 -14.470 4.556 -44.645 1.00 68.64 C
ANISOU 1862 CA ARG A 245 8895 9433 7752 -183 366 -1195 C
ATOM 1863 C ARG A 245 -13.850 3.334 -45.311 1.00 66.24 C
ANISOU 1863 C ARG A 245 8696 9112 7360 -100 425 -1292 C
ATOM 1864 O ARG A 245 -14.537 2.594 -46.024 1.00 63.61 O
ANISOU 1864 O ARG A 245 8498 8693 6976 -110 350 -1344 O
ATOM 1865 CB ARG A 245 -14.205 5.814 -45.474 1.00 67.33 C
ANISOU 1865 CB ARG A 245 8746 9349 7489 -246 394 -1149 C
ATOM 1866 CG ARG A 245 -14.637 5.711 -46.928 1.00 61.88 C
ANISOU 1866 CG ARG A 245 8224 8636 6653 -282 344 -1180 C
ATOM 1867 CD ARG A 245 -14.420 7.031 -47.648 1.00 67.55 C
ANISOU 1867 CD ARG A 245 8957 9429 7281 -350 369 -1115 C
ATOM 1868 NE ARG A 245 -13.039 7.486 -47.537 1.00 58.13 N
ANISOU 1868 NE ARG A 245 7683 8348 6054 -320 525 -1106 N
ATOM 1869 CZ ARG A 245 -12.630 8.713 -47.829 1.00 60.76 C
ANISOU 1869 CZ ARG A 245 7988 8755 6345 -380 572 -1038 C
ATOM 1870 NH1 ARG A 245 -13.475 9.642 -48.246 1.00 58.00 N
ANISOU 1870 NH1 ARG A 245 7687 8374 5976 -465 477 -970 N
ATOM 1871 NH2 ARG A 245 -11.342 9.016 -47.693 1.00 59.99 N
ANISOU 1871 NH2 ARG A 245 7804 8760 6230 -357 716 -1034 N
ATOM 1872 N ALA A 246 -12.554 3.104 -45.087 1.00 58.37 N
ANISOU 1872 N ALA A 246 7638 8191 6348 -14 558 -1319 N
ATOM 1873 CA ALA A 246 -11.893 1.954 -45.696 1.00 61.52 C
ANISOU 1873 CA ALA A 246 8131 8574 6669 84 630 -1415 C
ATOM 1874 C ALA A 246 -12.440 0.644 -45.144 1.00 65.33 C
ANISOU 1874 C ALA A 246 8660 8928 7235 134 563 -1462 C
ATOM 1875 O ALA A 246 -12.694 -0.298 -45.903 1.00 73.81 O
ANISOU 1875 O ALA A 246 9884 9921 8240 162 538 -1542 O
ATOM 1876 CB ALA A 246 -10.383 2.040 -45.479 1.00 67.52 C
ANISOU 1876 CB ALA A 246 8784 9452 7419 171 787 -1423 C
ATOM 1877 N LYS A 247 -12.628 0.565 -43.824 1.00 74.19 N
ANISOU 1877 N LYS A 247 9664 10024 8499 143 533 -1413 N
ATOM 1878 CA LYS A 247 -13.171 -0.651 -43.229 1.00 69.90 C
ANISOU 1878 CA LYS A 247 9164 9354 8042 182 472 -1442 C
ATOM 1879 C LYS A 247 -14.616 -0.874 -43.655 1.00 61.95 C
ANISOU 1879 C LYS A 247 8262 8233 7042 87 331 -1446 C
ATOM 1880 O LYS A 247 -15.018 -2.010 -43.932 1.00 65.58 O
ANISOU 1880 O LYS A 247 8838 8579 7500 108 283 -1509 O
ATOM 1881 CB LYS A 247 -13.060 -0.581 -41.706 1.00 69.90 C
ANISOU 1881 CB LYS A 247 9018 9362 8179 204 474 -1377 C
ATOM 1882 CG LYS A 247 -11.641 -0.401 -41.193 1.00 64.26 C
ANISOU 1882 CG LYS A 247 8186 8760 7470 295 593 -1370 C
ATOM 1883 CD LYS A 247 -10.812 -1.662 -41.381 1.00 71.29 C
ANISOU 1883 CD LYS A 247 9130 9616 8341 430 661 -1447 C
ATOM 1884 CE LYS A 247 -11.321 -2.793 -40.502 1.00 64.75 C
ANISOU 1884 CE LYS A 247 8334 8657 7613 472 599 -1448 C
ATOM 1885 NZ LYS A 247 -10.453 -3.999 -40.589 1.00 65.11 N
ANISOU 1885 NZ LYS A 247 8426 8661 7651 616 667 -1516 N
ATOM 1886 N LEU A 248 -15.412 0.196 -43.712 1.00 62.81 N
ANISOU 1886 N LEU A 248 8331 8369 7167 -18 260 -1378 N
ATOM 1887 CA LEU A 248 -16.793 0.060 -44.160 1.00 67.63 C
ANISOU 1887 CA LEU A 248 9021 8884 7791 -111 118 -1374 C
ATOM 1888 C LEU A 248 -16.870 -0.262 -45.647 1.00 72.64 C
ANISOU 1888 C LEU A 248 9829 9495 8274 -126 86 -1449 C
ATOM 1889 O LEU A 248 -17.823 -0.915 -46.088 1.00 66.76 O
ANISOU 1889 O LEU A 248 9189 8646 7532 -176 -31 -1482 O
ATOM 1890 CB LEU A 248 -17.578 1.335 -43.854 1.00 63.01 C
ANISOU 1890 CB LEU A 248 8340 8336 7264 -204 54 -1279 C
ATOM 1891 CG LEU A 248 -17.854 1.684 -42.389 1.00 69.05 C
ANISOU 1891 CG LEU A 248 8953 9102 8179 -209 59 -1205 C
ATOM 1892 CD1 LEU A 248 -18.727 2.927 -42.294 1.00 54.36 C
ANISOU 1892 CD1 LEU A 248 7024 7265 6366 -296 -8 -1124 C
ATOM 1893 CD2 LEU A 248 -18.499 0.515 -41.662 1.00 63.88 C
ANISOU 1893 CD2 LEU A 248 8307 8334 7631 -199 10 -1216 C
ATOM 1894 N MET A 249 -15.883 0.183 -46.430 1.00 81.08 N
ANISOU 1894 N MET A 249 10934 10662 9209 -88 188 -1475 N
ATOM 1895 CA MET A 249 -15.884 -0.119 -47.857 1.00 82.20 C
ANISOU 1895 CA MET A 249 11258 10789 9184 -97 172 -1550 C
ATOM 1896 C MET A 249 -15.632 -1.598 -48.115 1.00 78.29 C
ANISOU 1896 C MET A 249 10890 10198 8658 -16 191 -1661 C
ATOM 1897 O MET A 249 -16.112 -2.141 -49.115 1.00 87.87 O
ANISOU 1897 O MET A 249 12277 11340 9768 -44 118 -1732 O
ATOM 1898 CB MET A 249 -14.841 0.735 -48.578 1.00 78.27 C
ANISOU 1898 CB MET A 249 10762 10427 8551 -75 298 -1543 C
ATOM 1899 CG MET A 249 -15.003 0.771 -50.088 1.00 84.45 C
ANISOU 1899 CG MET A 249 11733 11212 9143 -111 270 -1594 C
ATOM 1900 SD MET A 249 -13.832 1.882 -50.891 1.00 83.66 S
ANISOU 1900 SD MET A 249 11627 11275 8886 -102 428 -1564 S
ATOM 1901 CE MET A 249 -12.281 1.071 -50.516 1.00 89.92 C
ANISOU 1901 CE MET A 249 12359 12122 9685 50 631 -1637 C
ATOM 1902 N ASN A 250 -14.886 -2.266 -47.232 1.00 70.08 N
ANISOU 1902 N ASN A 250 9776 9149 7703 86 281 -1679 N
ATOM 1903 CA ASN A 250 -14.712 -3.708 -47.366 1.00 62.96 C
ANISOU 1903 CA ASN A 250 8996 8133 6794 168 292 -1779 C
ATOM 1904 C ASN A 250 -15.985 -4.460 -47.000 1.00 74.23 C
ANISOU 1904 C ASN A 250 10475 9406 8324 97 137 -1779 C
ATOM 1905 O ASN A 250 -16.202 -5.578 -47.481 1.00 80.97 O
ANISOU 1905 O ASN A 250 11485 10138 9142 118 96 -1870 O
ATOM 1906 CB ASN A 250 -13.545 -4.184 -46.502 1.00 62.81 C
ANISOU 1906 CB ASN A 250 8875 8146 6843 304 425 -1786 C
ATOM 1907 CG ASN A 250 -12.203 -3.709 -47.022 1.00 75.92 C
ANISOU 1907 CG ASN A 250 10501 9949 8398 386 587 -1808 C
ATOM 1908 OD1 ASN A 250 -12.032 -3.487 -48.220 1.00 90.44 O
ANISOU 1908 OD1 ASN A 250 12456 11827 10082 374 622 -1858 O
ATOM 1909 ND2 ASN A 250 -11.241 -3.554 -46.121 1.00 92.97 N
ANISOU 1909 ND2 ASN A 250 12499 12189 10638 468 688 -1768 N
ATOM 1910 N ALA A 251 -16.835 -3.867 -46.160 1.00 70.69 N
ANISOU 1910 N ALA A 251 9900 8956 8004 10 54 -1681 N
ATOM 1911 CA ALA A 251 -18.101 -4.484 -45.784 1.00 69.09 C
ANISOU 1911 CA ALA A 251 9721 8620 7912 -71 -87 -1666 C
ATOM 1912 C ALA A 251 -19.223 -4.166 -46.761 1.00 73.94 C
ANISOU 1912 C ALA A 251 10425 9200 8469 -194 -235 -1670 C
ATOM 1913 O ALA A 251 -20.130 -4.987 -46.941 1.00 67.95 O
ANISOU 1913 O ALA A 251 9754 8313 7751 -255 -356 -1704 O
ATOM 1914 CB ALA A 251 -18.509 -4.040 -44.378 1.00 69.73 C
ANISOU 1914 CB ALA A 251 9619 8716 8160 -100 -96 -1558 C
ATOM 1915 N TYR A 252 -19.184 -2.994 -47.392 1.00 78.39 N
ANISOU 1915 N TYR A 252 10969 9873 8943 -236 -236 -1632 N
ATOM 1916 CA TYR A 252 -20.174 -2.586 -48.388 1.00 74.87 C
ANISOU 1916 CA TYR A 252 10610 9409 8428 -344 -381 -1628 C
ATOM 1917 C TYR A 252 -19.424 -2.046 -49.598 1.00 78.30 C
ANISOU 1917 C TYR A 252 11156 9936 8658 -320 -317 -1668 C
ATOM 1918 O TYR A 252 -19.333 -0.826 -49.795 1.00 83.88 O
ANISOU 1918 O TYR A 252 11798 10748 9325 -352 -300 -1595 O
ATOM 1919 CB TYR A 252 -21.137 -1.541 -47.822 1.00 73.42 C
ANISOU 1919 CB TYR A 252 10273 9259 8366 -434 -469 -1509 C
ATOM 1920 CG TYR A 252 -21.805 -1.961 -46.533 1.00 72.19 C
ANISOU 1920 CG TYR A 252 9989 9030 8408 -454 -501 -1457 C
ATOM 1921 CD1 TYR A 252 -22.997 -2.674 -46.547 1.00 80.66 C
ANISOU 1921 CD1 TYR A 252 11094 9986 9568 -538 -646 -1464 C
ATOM 1922 CD2 TYR A 252 -21.246 -1.644 -45.302 1.00 65.56 C
ANISOU 1922 CD2 TYR A 252 9000 8244 7667 -396 -388 -1401 C
ATOM 1923 CE1 TYR A 252 -23.612 -3.060 -45.372 1.00 73.31 C
ANISOU 1923 CE1 TYR A 252 10046 8991 8816 -561 -662 -1410 C
ATOM 1924 CE2 TYR A 252 -21.853 -2.025 -44.122 1.00 67.96 C
ANISOU 1924 CE2 TYR A 252 9200 8485 8137 -413 -408 -1351 C
ATOM 1925 CZ TYR A 252 -23.036 -2.733 -44.162 1.00 68.82 C
ANISOU 1925 CZ TYR A 252 9341 8478 8330 -495 -539 -1353 C
ATOM 1926 OH TYR A 252 -23.644 -3.114 -42.988 1.00 63.59 O
ANISOU 1926 OH TYR A 252 8574 7756 7831 -518 -546 -1296 O
ATOM 1927 N PRO A 253 -18.867 -2.930 -50.431 1.00 73.48 N
ANISOU 1927 N PRO A 253 10722 9286 7911 -261 -274 -1783 N
ATOM 1928 CA PRO A 253 -18.043 -2.449 -51.550 1.00 74.18 C
ANISOU 1928 CA PRO A 253 10918 9473 7796 -227 -182 -1823 C
ATOM 1929 C PRO A 253 -18.833 -1.698 -52.605 1.00 81.53 C
ANISOU 1929 C PRO A 253 11944 10426 8609 -335 -313 -1794 C
ATOM 1930 O PRO A 253 -18.288 -0.779 -53.229 1.00 82.14 O
ANISOU 1930 O PRO A 253 12037 10615 8558 -334 -240 -1762 O
ATOM 1931 CB PRO A 253 -17.428 -3.739 -52.109 1.00 73.48 C
ANISOU 1931 CB PRO A 253 11005 9309 7605 -136 -116 -1963 C
ATOM 1932 CG PRO A 253 -18.390 -4.812 -51.717 1.00 67.82 C
ANISOU 1932 CG PRO A 253 10335 8428 7004 -178 -256 -1999 C
ATOM 1933 CD PRO A 253 -18.945 -4.399 -50.385 1.00 66.49 C
ANISOU 1933 CD PRO A 253 9952 8261 7050 -221 -297 -1883 C
ATOM 1934 N SER A 254 -20.099 -2.048 -52.814 1.00 72.44 N
ANISOU 1934 N SER A 254 10850 9172 7501 -431 -507 -1796 N
ATOM 1935 CA SER A 254 -20.925 -1.421 -53.837 1.00 80.84 C
ANISOU 1935 CA SER A 254 12010 10248 8457 -533 -660 -1769 C
ATOM 1936 C SER A 254 -21.708 -0.221 -53.322 1.00 73.10 C
ANISOU 1936 C SER A 254 10856 9317 7602 -610 -746 -1629 C
ATOM 1937 O SER A 254 -22.498 0.353 -54.080 1.00 75.53 O
ANISOU 1937 O SER A 254 11222 9631 7847 -693 -892 -1588 O
ATOM 1938 CB SER A 254 -21.894 -2.450 -54.427 1.00101.74 C
ANISOU 1938 CB SER A 254 14817 12759 11080 -602 -842 -1851 C
ATOM 1939 OG SER A 254 -22.754 -2.963 -53.424 1.00 84.87 O
ANISOU 1939 OG SER A 254 12557 10526 9164 -646 -936 -1819 O
ATOM 1940 N TYR A 255 -21.513 0.177 -52.063 1.00 79.78 N
ANISOU 1940 N TYR A 255 11497 10195 8620 -578 -664 -1554 N
ATOM 1941 CA TYR A 255 -22.259 1.282 -51.478 1.00 77.06 C
ANISOU 1941 CA TYR A 255 10987 9885 8406 -639 -734 -1429 C
ATOM 1942 C TYR A 255 -21.412 2.486 -51.098 1.00 74.74 C
ANISOU 1942 C TYR A 255 10579 9712 8106 -600 -592 -1353 C
ATOM 1943 O TYR A 255 -21.980 3.558 -50.858 1.00 73.85 O
ANISOU 1943 O TYR A 255 10365 9631 8064 -650 -650 -1253 O
ATOM 1944 CB TYR A 255 -23.013 0.821 -50.220 1.00 64.34 C
ANISOU 1944 CB TYR A 255 9226 8198 7024 -657 -783 -1394 C
ATOM 1945 CG TYR A 255 -24.124 -0.165 -50.482 1.00 64.24 C
ANISOU 1945 CG TYR A 255 9285 8062 7063 -729 -953 -1438 C
ATOM 1946 CD1 TYR A 255 -25.267 0.216 -51.172 1.00 64.60 C
ANISOU 1946 CD1 TYR A 255 9358 8085 7102 -828 -1142 -1400 C
ATOM 1947 CD2 TYR A 255 -24.040 -1.473 -50.025 1.00 64.07 C
ANISOU 1947 CD2 TYR A 255 9300 7941 7102 -701 -933 -1512 C
ATOM 1948 CE1 TYR A 255 -26.288 -0.680 -51.410 1.00 65.71 C
ANISOU 1948 CE1 TYR A 255 9554 8115 7299 -906 -1309 -1438 C
ATOM 1949 CE2 TYR A 255 -25.056 -2.377 -50.256 1.00 65.16 C
ANISOU 1949 CE2 TYR A 255 9505 7958 7295 -781 -1092 -1551 C
ATOM 1950 CZ TYR A 255 -26.178 -1.975 -50.949 1.00 65.99 C
ANISOU 1950 CZ TYR A 255 9628 8050 7395 -888 -1281 -1515 C
ATOM 1951 OH TYR A 255 -27.192 -2.874 -51.180 1.00 70.92 O
ANISOU 1951 OH TYR A 255 10309 8556 8083 -978 -1449 -1553 O
ATOM 1952 N ILE A 256 -20.089 2.354 -51.031 1.00 68.08 N
ANISOU 1952 N ILE A 256 9746 8934 7189 -515 -413 -1396 N
ATOM 1953 CA ILE A 256 -19.230 3.389 -50.471 1.00 72.21 C
ANISOU 1953 CA ILE A 256 10137 9564 7737 -483 -275 -1326 C
ATOM 1954 C ILE A 256 -18.119 3.710 -51.459 1.00 65.44 C
ANISOU 1954 C ILE A 256 9383 8799 6682 -449 -150 -1358 C
ATOM 1955 O ILE A 256 -17.424 2.807 -51.936 1.00 73.38 O
ANISOU 1955 O ILE A 256 10497 9800 7586 -384 -68 -1456 O
ATOM 1956 CB ILE A 256 -18.643 2.959 -49.113 1.00 70.24 C
ANISOU 1956 CB ILE A 256 9741 9314 7633 -411 -168 -1330 C
ATOM 1957 CG1 ILE A 256 -19.755 2.895 -48.064 1.00 61.51 C
ANISOU 1957 CG1 ILE A 256 8516 8133 6720 -454 -274 -1276 C
ATOM 1958 CG2 ILE A 256 -17.534 3.906 -48.678 1.00 71.48 C
ANISOU 1958 CG2 ILE A 256 9785 9589 7786 -375 -17 -1280 C
ATOM 1959 CD1 ILE A 256 -19.320 2.316 -46.752 1.00 71.11 C
ANISOU 1959 CD1 ILE A 256 9618 9334 8068 -389 -190 -1281 C
ATOM 1960 N SER A 257 -17.953 4.999 -51.761 1.00 68.14 N
ANISOU 1960 N SER A 257 9694 9222 6974 -492 -127 -1273 N
ATOM 1961 CA SER A 257 -16.880 5.463 -52.629 1.00 64.81 C
ANISOU 1961 CA SER A 257 9350 8899 6375 -472 8 -1281 C
ATOM 1962 C SER A 257 -15.594 5.644 -51.824 1.00 72.67 C
ANISOU 1962 C SER A 257 10202 9979 7428 -403 196 -1275 C
ATOM 1963 O SER A 257 -15.638 6.087 -50.673 1.00 72.26 O
ANISOU 1963 O SER A 257 9983 9933 7540 -406 201 -1216 O
ATOM 1964 CB SER A 257 -17.264 6.782 -53.296 1.00 63.35 C
ANISOU 1964 CB SER A 257 9200 8756 6115 -555 -54 -1182 C
ATOM 1965 OG SER A 257 -16.138 7.407 -53.886 1.00 72.06 O
ANISOU 1965 OG SER A 257 10336 9965 7079 -544 102 -1164 O
ATOM 1966 N PRO A 258 -14.435 5.307 -52.400 1.00 69.24 N
ANISOU 1966 N PRO A 258 9827 9615 6864 -340 353 -1336 N
ATOM 1967 CA PRO A 258 -13.171 5.509 -51.676 1.00 67.36 C
ANISOU 1967 CA PRO A 258 9438 9470 6687 -277 527 -1325 C
ATOM 1968 C PRO A 258 -12.770 6.968 -51.533 1.00 72.40 C
ANISOU 1968 C PRO A 258 9973 10200 7337 -341 580 -1217 C
ATOM 1969 O PRO A 258 -11.800 7.253 -50.819 1.00 67.93 O
ANISOU 1969 O PRO A 258 9259 9708 6842 -308 702 -1197 O
ATOM 1970 CB PRO A 258 -12.154 4.737 -52.526 1.00 65.73 C
ANISOU 1970 CB PRO A 258 9339 9310 6326 -194 673 -1421 C
ATOM 1971 CG PRO A 258 -12.735 4.751 -53.895 1.00 65.87 C
ANISOU 1971 CG PRO A 258 9571 9301 6154 -246 600 -1446 C
ATOM 1972 CD PRO A 258 -14.226 4.663 -53.708 1.00 68.78 C
ANISOU 1972 CD PRO A 258 9976 9554 6602 -317 379 -1423 C
ATOM 1973 N ILE A 259 -13.473 7.897 -52.184 1.00 71.39 N
ANISOU 1973 N ILE A 259 9919 10064 7143 -433 487 -1145 N
ATOM 1974 CA ILE A 259 -13.180 9.319 -52.068 1.00 74.13 C
ANISOU 1974 CA ILE A 259 10185 10476 7505 -500 526 -1038 C
ATOM 1975 C ILE A 259 -14.386 10.137 -51.636 1.00 75.85 C
ANISOU 1975 C ILE A 259 10365 10624 7833 -574 362 -952 C
ATOM 1976 O ILE A 259 -14.262 11.349 -51.452 1.00 77.22 O
ANISOU 1976 O ILE A 259 10474 10829 8036 -630 378 -861 O
ATOM 1977 CB ILE A 259 -12.605 9.888 -53.382 1.00 69.36 C
ANISOU 1977 CB ILE A 259 9710 9948 6695 -537 611 -1014 C
ATOM 1978 CG1 ILE A 259 -13.663 9.849 -54.485 1.00 64.69 C
ANISOU 1978 CG1 ILE A 259 9316 9294 5971 -587 462 -1012 C
ATOM 1979 CG2 ILE A 259 -11.357 9.123 -53.800 1.00 67.15 C
ANISOU 1979 CG2 ILE A 259 9454 9748 6311 -456 796 -1099 C
ATOM 1980 CD1 ILE A 259 -13.373 10.785 -55.635 1.00 69.75 C
ANISOU 1980 CD1 ILE A 259 10077 9998 6428 -651 506 -944 C
ATOM 1981 N GLY A 260 -15.556 9.518 -51.469 1.00 69.49 N
ANISOU 1981 N GLY A 260 9592 9720 7093 -575 209 -977 N
ATOM 1982 CA GLY A 260 -16.760 10.230 -51.108 1.00 76.84 C
ANISOU 1982 CA GLY A 260 10480 10584 8132 -634 56 -898 C
ATOM 1983 C GLY A 260 -17.024 10.228 -49.608 1.00 74.19 C
ANISOU 1983 C GLY A 260 9968 10215 8007 -613 46 -881 C
ATOM 1984 O GLY A 260 -16.298 9.640 -48.810 1.00 66.34 O
ANISOU 1984 O GLY A 260 8887 9244 7074 -554 145 -928 O
ATOM 1985 N CYS A 261 -18.099 10.919 -49.236 1.00 73.82 N
ANISOU 1985 N CYS A 261 9871 10110 8066 -658 -75 -809 N
ATOM 1986 CA CYS A 261 -18.515 10.970 -47.844 1.00 62.68 C
ANISOU 1986 CA CYS A 261 8308 8662 6847 -641 -91 -789 C
ATOM 1987 C CYS A 261 -19.137 9.639 -47.424 1.00 67.03 C
ANISOU 1987 C CYS A 261 8853 9144 7472 -607 -152 -855 C
ATOM 1988 O CYS A 261 -19.381 8.745 -48.240 1.00 75.48 O
ANISOU 1988 O CYS A 261 10041 10183 8455 -604 -206 -915 O
ATOM 1989 CB CYS A 261 -19.510 12.110 -47.619 1.00 56.17 C
ANISOU 1989 CB CYS A 261 7435 7795 6114 -691 -193 -695 C
ATOM 1990 SG CYS A 261 -18.845 13.769 -47.900 1.00 73.56 S
ANISOU 1990 SG CYS A 261 9636 10053 8262 -737 -126 -605 S
ATOM 1991 N LEU A 262 -19.395 9.517 -46.125 1.00 69.09 N
ANISOU 1991 N LEU A 262 8983 9376 7891 -585 -143 -844 N
ATOM 1992 CA LEU A 262 -20.013 8.314 -45.575 1.00 64.79 C
ANISOU 1992 CA LEU A 262 8421 8760 7436 -560 -194 -891 C
ATOM 1993 C LEU A 262 -21.531 8.433 -45.636 1.00 66.84 C
ANISOU 1993 C LEU A 262 8668 8943 7786 -612 -351 -848 C
ATOM 1994 O LEU A 262 -22.079 9.469 -45.239 1.00 63.53 O
ANISOU 1994 O LEU A 262 8168 8521 7449 -638 -384 -772 O
ATOM 1995 CB LEU A 262 -19.574 8.091 -44.135 1.00 57.71 C
ANISOU 1995 CB LEU A 262 7396 7873 6659 -512 -108 -894 C
ATOM 1996 CG LEU A 262 -18.084 7.831 -43.910 1.00 66.88 C
ANISOU 1996 CG LEU A 262 8542 9110 7760 -452 37 -937 C
ATOM 1997 CD1 LEU A 262 -17.786 7.666 -42.428 1.00 52.85 C
ANISOU 1997 CD1 LEU A 262 6640 7338 6105 -411 95 -929 C
ATOM 1998 CD2 LEU A 262 -17.632 6.607 -44.691 1.00 57.76 C
ANISOU 1998 CD2 LEU A 262 7499 7943 6503 -408 60 -1024 C
ATOM 1999 N PRO A 263 -22.234 7.413 -46.132 1.00 65.88 N
ANISOU 1999 N PRO A 263 8622 8755 7656 -629 -450 -894 N
ATOM 2000 CA PRO A 263 -23.701 7.454 -46.117 1.00 69.22 C
ANISOU 2000 CA PRO A 263 9006 9107 8186 -682 -604 -850 C
ATOM 2001 C PRO A 263 -24.231 7.629 -44.701 1.00 64.94 C
ANISOU 2001 C PRO A 263 8302 8541 7832 -671 -581 -803 C
ATOM 2002 O PRO A 263 -23.769 6.982 -43.759 1.00 64.48 O
ANISOU 2002 O PRO A 263 8193 8478 7829 -629 -492 -834 O
ATOM 2003 CB PRO A 263 -24.100 6.098 -46.710 1.00 63.13 C
ANISOU 2003 CB PRO A 263 8341 8269 7378 -699 -688 -926 C
ATOM 2004 CG PRO A 263 -22.927 5.700 -47.550 1.00 62.89 C
ANISOU 2004 CG PRO A 263 8451 8282 7163 -662 -603 -1002 C
ATOM 2005 CD PRO A 263 -21.717 6.222 -46.827 1.00 61.38 C
ANISOU 2005 CD PRO A 263 8180 8169 6971 -603 -432 -989 C
ATOM 2006 N ALA A 264 -25.221 8.515 -44.563 1.00 68.45 N
ANISOU 2006 N ALA A 264 8668 8968 8371 -704 -663 -725 N
ATOM 2007 CA ALA A 264 -25.668 8.959 -43.247 1.00 64.09 C
ANISOU 2007 CA ALA A 264 7965 8404 7982 -688 -620 -674 C
ATOM 2008 C ALA A 264 -26.342 7.860 -42.434 1.00 63.67 C
ANISOU 2008 C ALA A 264 7847 8290 8055 -690 -636 -693 C
ATOM 2009 O ALA A 264 -26.403 7.971 -41.205 1.00 63.01 O
ANISOU 2009 O ALA A 264 7657 8205 8079 -663 -560 -669 O
ATOM 2010 CB ALA A 264 -26.621 10.147 -43.395 1.00 61.02 C
ANISOU 2010 CB ALA A 264 7515 8005 7667 -713 -705 -589 C
ATOM 2011 N HIS A 265 -26.845 6.809 -43.077 1.00 63.93 N
ANISOU 2011 N HIS A 265 7949 8269 8073 -727 -734 -734 N
ATOM 2012 CA HIS A 265 -27.586 5.764 -42.384 1.00 59.35 C
ANISOU 2012 CA HIS A 265 7311 7620 7620 -746 -761 -743 C
ATOM 2013 C HIS A 265 -26.715 4.585 -41.966 1.00 64.02 C
ANISOU 2013 C HIS A 265 7962 8192 8171 -707 -670 -814 C
ATOM 2014 O HIS A 265 -27.250 3.573 -41.501 1.00 62.66 O
ANISOU 2014 O HIS A 265 7770 7950 8088 -728 -695 -826 O
ATOM 2015 CB HIS A 265 -28.738 5.267 -43.260 1.00 58.19 C
ANISOU 2015 CB HIS A 265 7198 7412 7502 -821 -935 -743 C
ATOM 2016 CG HIS A 265 -28.291 4.594 -44.520 1.00 69.57 C
ANISOU 2016 CG HIS A 265 8815 8838 8780 -839 -998 -821 C
ATOM 2017 ND1 HIS A 265 -27.686 5.276 -45.554 1.00 71.83 N
ANISOU 2017 ND1 HIS A 265 9206 9180 8904 -830 -1005 -831 N
ATOM 2018 CD2 HIS A 265 -28.364 3.301 -44.913 1.00 61.91 C
ANISOU 2018 CD2 HIS A 265 7944 7799 7779 -867 -1051 -894 C
ATOM 2019 CE1 HIS A 265 -27.403 4.430 -46.529 1.00 67.42 C
ANISOU 2019 CE1 HIS A 265 8807 8595 8216 -846 -1055 -910 C
ATOM 2020 NE2 HIS A 265 -27.805 3.226 -46.165 1.00 69.34 N
ANISOU 2020 NE2 HIS A 265 9051 8759 8536 -867 -1086 -954 N
ATOM 2021 N LEU A 266 -25.396 4.689 -42.111 1.00 63.46 N
ANISOU 2021 N LEU A 266 7956 8179 7977 -649 -566 -856 N
ATOM 2022 CA LEU A 266 -24.472 3.606 -41.796 1.00 65.41 C
ANISOU 2022 CA LEU A 266 8260 8412 8180 -595 -479 -924 C
ATOM 2023 C LEU A 266 -23.441 4.043 -40.761 1.00 67.07 C
ANISOU 2023 C LEU A 266 8397 8690 8397 -527 -336 -908 C
ATOM 2024 O LEU A 266 -22.258 3.710 -40.859 1.00 68.41 O
ANISOU 2024 O LEU A 266 8618 8899 8478 -468 -250 -958 O
ATOM 2025 CB LEU A 266 -23.770 3.110 -43.059 1.00 55.61 C
ANISOU 2025 CB LEU A 266 7177 7177 6776 -582 -490 -1003 C
ATOM 2026 CG LEU A 266 -24.625 2.747 -44.274 1.00 60.93 C
ANISOU 2026 CG LEU A 266 7958 7793 7399 -651 -641 -1031 C
ATOM 2027 CD1 LEU A 266 -23.739 2.526 -45.490 1.00 65.48 C
ANISOU 2027 CD1 LEU A 266 8696 8400 7783 -625 -618 -1107 C
ATOM 2028 CD2 LEU A 266 -25.471 1.516 -43.999 1.00 57.24 C
ANISOU 2028 CD2 LEU A 266 7502 7216 7032 -690 -722 -1056 C
ATOM 2029 N LEU A 267 -23.875 4.787 -39.743 1.00 63.39 N
ANISOU 2029 N LEU A 267 7808 8240 8039 -533 -310 -842 N
ATOM 2030 CA LEU A 267 -22.946 5.428 -38.823 1.00 60.14 C
ANISOU 2030 CA LEU A 267 7331 7897 7623 -481 -193 -824 C
ATOM 2031 C LEU A 267 -23.062 4.967 -37.376 1.00 64.26 C
ANISOU 2031 C LEU A 267 7775 8395 8248 -453 -135 -803 C
ATOM 2032 O LEU A 267 -22.273 5.421 -36.539 1.00 64.77 O
ANISOU 2032 O LEU A 267 7790 8515 8303 -411 -47 -792 O
ATOM 2033 CB LEU A 267 -23.117 6.951 -38.884 1.00 65.93 C
ANISOU 2033 CB LEU A 267 8010 8680 8361 -505 -195 -769 C
ATOM 2034 CG LEU A 267 -22.652 7.613 -40.180 1.00 54.04 C
ANISOU 2034 CG LEU A 267 6584 7219 6730 -523 -219 -779 C
ATOM 2035 CD1 LEU A 267 -22.859 9.118 -40.123 1.00 62.70 C
ANISOU 2035 CD1 LEU A 267 7628 8347 7847 -546 -221 -715 C
ATOM 2036 CD2 LEU A 267 -21.193 7.278 -40.444 1.00 53.32 C
ANISOU 2036 CD2 LEU A 267 6548 7189 6520 -476 -123 -834 C
ATOM 2037 N GLY A 268 -24.010 4.093 -37.048 1.00 62.08 N
ANISOU 2037 N GLY A 268 7486 8037 8062 -481 -184 -792 N
ATOM 2038 CA GLY A 268 -24.126 3.540 -35.715 1.00 66.17 C
ANISOU 2038 CA GLY A 268 7948 8528 8667 -457 -125 -767 C
ATOM 2039 C GLY A 268 -25.373 3.952 -34.960 1.00 75.95 C
ANISOU 2039 C GLY A 268 9084 9738 10035 -499 -141 -699 C
ATOM 2040 O GLY A 268 -25.768 3.248 -34.021 1.00 71.76 O
ANISOU 2040 O GLY A 268 8520 9162 9582 -499 -110 -675 O
ATOM 2041 N ASP A 269 -25.999 5.066 -35.327 1.00 79.01 N
ANISOU 2041 N ASP A 269 9421 10150 10451 -530 -182 -664 N
ATOM 2042 CA ASP A 269 -27.263 5.458 -34.718 1.00 62.13 C
ANISOU 2042 CA ASP A 269 7176 7984 8446 -563 -198 -601 C
ATOM 2043 C ASP A 269 -28.103 6.176 -35.769 1.00 73.55 C
ANISOU 2043 C ASP A 269 8605 9425 9917 -609 -306 -578 C
ATOM 2044 O ASP A 269 -27.777 6.171 -36.960 1.00 75.38 O
ANISOU 2044 O ASP A 269 8921 9663 10055 -625 -377 -613 O
ATOM 2045 CB ASP A 269 -27.033 6.307 -33.458 1.00 65.94 C
ANISOU 2045 CB ASP A 269 7586 8511 8957 -520 -90 -567 C
ATOM 2046 CG ASP A 269 -26.216 7.559 -33.726 1.00 74.55 C
ANISOU 2046 CG ASP A 269 8692 9669 9964 -494 -63 -577 C
ATOM 2047 OD1 ASP A 269 -26.682 8.433 -34.486 1.00 77.94 O
ANISOU 2047 OD1 ASP A 269 9110 10102 10401 -517 -124 -557 O
ATOM 2048 OD2 ASP A 269 -25.112 7.677 -33.153 1.00 76.58 O
ANISOU 2048 OD2 ASP A 269 8970 9973 10152 -451 16 -600 O
ATOM 2049 N MET A 270 -29.194 6.797 -35.319 1.00 64.31 N
ANISOU 2049 N MET A 270 7323 8242 8869 -626 -319 -518 N
ATOM 2050 CA MET A 270 -30.157 7.389 -36.242 1.00 62.83 C
ANISOU 2050 CA MET A 270 7100 8041 8729 -666 -437 -485 C
ATOM 2051 C MET A 270 -29.579 8.583 -36.993 1.00 62.84 C
ANISOU 2051 C MET A 270 7152 8092 8634 -645 -454 -486 C
ATOM 2052 O MET A 270 -30.013 8.876 -38.113 1.00 66.62 O
ANISOU 2052 O MET A 270 7660 8562 9091 -678 -571 -474 O
ATOM 2053 CB MET A 270 -31.419 7.794 -35.479 1.00 62.80 C
ANISOU 2053 CB MET A 270 6950 8018 8893 -673 -428 -417 C
ATOM 2054 CG MET A 270 -32.477 8.487 -36.318 1.00 61.30 C
ANISOU 2054 CG MET A 270 6698 7816 8776 -703 -553 -370 C
ATOM 2055 SD MET A 270 -33.079 7.470 -37.676 1.00 67.68 S
ANISOU 2055 SD MET A 270 7562 8579 9577 -789 -736 -391 S
ATOM 2056 CE MET A 270 -34.034 6.242 -36.789 1.00 55.64 C
ANISOU 2056 CE MET A 270 5934 6996 8211 -840 -718 -368 C
ATOM 2057 N TRP A 271 -28.594 9.269 -36.413 1.00 54.40 N
ANISOU 2057 N TRP A 271 6097 7069 7502 -596 -347 -496 N
ATOM 2058 CA TRP A 271 -28.045 10.477 -37.013 1.00 59.08 C
ANISOU 2058 CA TRP A 271 6731 7702 8015 -584 -351 -488 C
ATOM 2059 C TRP A 271 -26.542 10.435 -37.226 1.00 68.33 C
ANISOU 2059 C TRP A 271 7994 8926 9040 -564 -283 -539 C
ATOM 2060 O TRP A 271 -26.005 11.352 -37.859 1.00 75.21 O
ANISOU 2060 O TRP A 271 8911 9831 9833 -567 -286 -532 O
ATOM 2061 CB TRP A 271 -28.373 11.706 -36.149 1.00 55.56 C
ANISOU 2061 CB TRP A 271 6201 7261 7649 -552 -292 -442 C
ATOM 2062 CG TRP A 271 -29.755 11.685 -35.576 1.00 60.57 C
ANISOU 2062 CG TRP A 271 6719 7853 8444 -554 -312 -394 C
ATOM 2063 CD1 TRP A 271 -30.857 12.320 -36.069 1.00 63.76 C
ANISOU 2063 CD1 TRP A 271 7059 8229 8939 -563 -402 -340 C
ATOM 2064 CD2 TRP A 271 -30.185 10.994 -34.396 1.00 64.79 C
ANISOU 2064 CD2 TRP A 271 7179 8370 9069 -543 -238 -389 C
ATOM 2065 NE1 TRP A 271 -31.946 12.067 -35.271 1.00 67.19 N
ANISOU 2065 NE1 TRP A 271 7370 8634 9524 -558 -381 -305 N
ATOM 2066 CE2 TRP A 271 -31.560 11.254 -34.238 1.00 67.74 C
ANISOU 2066 CE2 TRP A 271 7437 8710 9591 -550 -276 -333 C
ATOM 2067 CE3 TRP A 271 -29.541 10.178 -33.460 1.00 53.92 C
ANISOU 2067 CE3 TRP A 271 5822 7003 7661 -528 -142 -420 C
ATOM 2068 CZ2 TRP A 271 -32.303 10.730 -33.182 1.00 66.19 C
ANISOU 2068 CZ2 TRP A 271 7144 8494 9511 -547 -209 -309 C
ATOM 2069 CZ3 TRP A 271 -30.279 9.657 -32.414 1.00 50.98 C
ANISOU 2069 CZ3 TRP A 271 5369 6606 7395 -525 -85 -393 C
ATOM 2070 CH2 TRP A 271 -31.646 9.936 -32.283 1.00 64.81 C
ANISOU 2070 CH2 TRP A 271 7005 8327 9291 -538 -112 -338 C
ATOM 2071 N GLY A 272 -25.847 9.415 -36.732 1.00 64.28 N
ANISOU 2071 N GLY A 272 7507 8422 8494 -543 -221 -585 N
ATOM 2072 CA GLY A 272 -24.401 9.450 -36.738 1.00 67.32 C
ANISOU 2072 CA GLY A 272 7948 8867 8764 -513 -142 -627 C
ATOM 2073 C GLY A 272 -23.806 10.349 -35.683 1.00 69.23 C
ANISOU 2073 C GLY A 272 8137 9150 9016 -484 -49 -612 C
ATOM 2074 O GLY A 272 -22.675 10.817 -35.849 1.00 73.91 O
ANISOU 2074 O GLY A 272 8761 9800 9520 -474 1 -632 O
ATOM 2075 N ARG A 273 -24.543 10.619 -34.602 1.00 70.11 N
ANISOU 2075 N ARG A 273 8171 9234 9232 -474 -21 -578 N
ATOM 2076 CA ARG A 273 -24.007 11.444 -33.525 1.00 66.07 C
ANISOU 2076 CA ARG A 273 7624 8756 8723 -447 65 -572 C
ATOM 2077 C ARG A 273 -22.785 10.791 -32.893 1.00 64.93 C
ANISOU 2077 C ARG A 273 7502 8658 8512 -416 135 -613 C
ATOM 2078 O ARG A 273 -21.840 11.480 -32.493 1.00 55.94 O
ANISOU 2078 O ARG A 273 6362 7570 7323 -405 186 -624 O
ATOM 2079 CB ARG A 273 -25.085 11.703 -32.472 1.00 48.89 C
ANISOU 2079 CB ARG A 273 5371 6539 6665 -436 90 -535 C
ATOM 2080 CG ARG A 273 -24.636 12.631 -31.359 1.00 51.39 C
ANISOU 2080 CG ARG A 273 5667 6881 6979 -410 173 -535 C
ATOM 2081 CD ARG A 273 -25.679 12.747 -30.262 1.00 56.70 C
ANISOU 2081 CD ARG A 273 6273 7516 7756 -389 218 -505 C
ATOM 2082 NE ARG A 273 -25.211 13.588 -29.166 1.00 61.00 N
ANISOU 2082 NE ARG A 273 6818 8080 8280 -363 298 -516 N
ATOM 2083 CZ ARG A 273 -25.852 13.747 -28.016 1.00 57.78 C
ANISOU 2083 CZ ARG A 273 6370 7651 7931 -336 365 -502 C
ATOM 2084 NH1 ARG A 273 -26.991 13.123 -27.768 1.00 70.41 N
ANISOU 2084 NH1 ARG A 273 7912 9214 9626 -333 371 -468 N
ATOM 2085 NH2 ARG A 273 -25.335 14.551 -27.092 1.00 58.45 N
ANISOU 2085 NH2 ARG A 273 6478 7754 7978 -316 429 -522 N
ATOM 2086 N PHE A 274 -22.785 9.464 -32.796 1.00 59.98 N
ANISOU 2086 N PHE A 274 6892 8011 7888 -401 131 -633 N
ATOM 2087 CA PHE A 274 -21.635 8.709 -32.324 1.00 61.40 C
ANISOU 2087 CA PHE A 274 7094 8228 8006 -359 184 -668 C
ATOM 2088 C PHE A 274 -21.363 7.562 -33.284 1.00 63.86 C
ANISOU 2088 C PHE A 274 7471 8522 8271 -353 147 -706 C
ATOM 2089 O PHE A 274 -22.296 6.915 -33.770 1.00 69.38 O
ANISOU 2089 O PHE A 274 8190 9157 9015 -379 86 -702 O
ATOM 2090 CB PHE A 274 -21.857 8.153 -30.908 1.00 71.49 C
ANISOU 2090 CB PHE A 274 8339 9486 9338 -331 233 -651 C
ATOM 2091 CG PHE A 274 -22.242 9.194 -29.897 1.00 62.05 C
ANISOU 2091 CG PHE A 274 7093 8299 8185 -333 275 -620 C
ATOM 2092 CD1 PHE A 274 -21.294 10.060 -29.377 1.00 52.63 C
ANISOU 2092 CD1 PHE A 274 5895 7166 6937 -320 318 -633 C
ATOM 2093 CD2 PHE A 274 -23.551 9.296 -29.455 1.00 51.96 C
ANISOU 2093 CD2 PHE A 274 5771 6969 7004 -348 275 -581 C
ATOM 2094 CE1 PHE A 274 -21.647 11.015 -28.444 1.00 50.05 C
ANISOU 2094 CE1 PHE A 274 5539 6836 6641 -321 356 -615 C
ATOM 2095 CE2 PHE A 274 -23.910 10.248 -28.520 1.00 47.67 C
ANISOU 2095 CE2 PHE A 274 5189 6429 6496 -340 326 -560 C
ATOM 2096 CZ PHE A 274 -22.957 11.109 -28.015 1.00 51.79 C
ANISOU 2096 CZ PHE A 274 5725 7001 6951 -325 365 -581 C
ATOM 2097 N TRP A 275 -20.084 7.313 -33.558 1.00 62.28 N
ANISOU 2097 N TRP A 275 7303 8378 7985 -317 185 -746 N
ATOM 2098 CA TRP A 275 -19.672 6.172 -34.362 1.00 58.47 C
ANISOU 2098 CA TRP A 275 6889 7877 7450 -292 170 -793 C
ATOM 2099 C TRP A 275 -19.340 4.954 -33.507 1.00 58.36 C
ANISOU 2099 C TRP A 275 6881 7834 7459 -236 201 -806 C
ATOM 2100 O TRP A 275 -18.574 4.089 -33.946 1.00 62.40 O
ANISOU 2100 O TRP A 275 7443 8348 7918 -189 215 -851 O
ATOM 2101 CB TRP A 275 -18.473 6.544 -35.239 1.00 60.24 C
ANISOU 2101 CB TRP A 275 7143 8178 7568 -276 203 -828 C
ATOM 2102 CG TRP A 275 -18.765 7.619 -36.251 1.00 61.45 C
ANISOU 2102 CG TRP A 275 7317 8351 7682 -333 169 -812 C
ATOM 2103 CD1 TRP A 275 -19.966 8.227 -36.482 1.00 57.64 C
ANISOU 2103 CD1 TRP A 275 6828 7822 7253 -386 101 -772 C
ATOM 2104 CD2 TRP A 275 -17.834 8.210 -37.167 1.00 61.15 C
ANISOU 2104 CD2 TRP A 275 7307 8382 7544 -341 201 -828 C
ATOM 2105 NE1 TRP A 275 -19.840 9.159 -37.483 1.00 54.64 N
ANISOU 2105 NE1 TRP A 275 6480 7472 6808 -423 81 -760 N
ATOM 2106 CE2 TRP A 275 -18.541 9.168 -37.920 1.00 59.91 C
ANISOU 2106 CE2 TRP A 275 7174 8211 7377 -401 146 -793 C
ATOM 2107 CE3 TRP A 275 -16.472 8.022 -37.423 1.00 59.71 C
ANISOU 2107 CE3 TRP A 275 7128 8275 7283 -301 276 -864 C
ATOM 2108 CZ2 TRP A 275 -17.933 9.935 -38.911 1.00 62.63 C
ANISOU 2108 CZ2 TRP A 275 7559 8610 7627 -429 164 -789 C
ATOM 2109 CZ3 TRP A 275 -15.870 8.786 -38.406 1.00 56.94 C
ANISOU 2109 CZ3 TRP A 275 6805 7986 6845 -331 302 -863 C
ATOM 2110 CH2 TRP A 275 -16.600 9.730 -39.138 1.00 61.79 C
ANISOU 2110 CH2 TRP A 275 7456 8579 7442 -397 248 -824 C
ATOM 2111 N THR A 276 -19.911 4.869 -32.302 1.00 68.62 N
ANISOU 2111 N THR A 276 8135 9104 8834 -237 215 -765 N
ATOM 2112 CA THR A 276 -19.549 3.806 -31.368 1.00 72.48 C
ANISOU 2112 CA THR A 276 8632 9567 9339 -183 247 -764 C
ATOM 2113 C THR A 276 -19.872 2.428 -31.932 1.00 73.04 C
ANISOU 2113 C THR A 276 8777 9552 9424 -175 208 -790 C
ATOM 2114 O THR A 276 -19.056 1.504 -31.836 1.00 77.82 O
ANISOU 2114 O THR A 276 9422 10146 9997 -110 230 -819 O
ATOM 2115 CB THR A 276 -20.273 4.011 -30.035 1.00 68.19 C
ANISOU 2115 CB THR A 276 8039 9003 8866 -197 271 -708 C
ATOM 2116 OG1 THR A 276 -20.047 5.345 -29.564 1.00 66.95 O
ANISOU 2116 OG1 THR A 276 7828 8914 8694 -208 302 -693 O
ATOM 2117 CG2 THR A 276 -19.766 3.022 -28.996 1.00 75.77 C
ANISOU 2117 CG2 THR A 276 9016 9947 9826 -139 306 -697 C
ATOM 2118 N ASN A 277 -21.056 2.270 -32.527 1.00 73.59 N
ANISOU 2118 N ASN A 277 8864 9552 9545 -239 145 -782 N
ATOM 2119 CA ASN A 277 -21.499 0.961 -32.991 1.00 71.46 C
ANISOU 2119 CA ASN A 277 8668 9182 9299 -249 97 -807 C
ATOM 2120 C ASN A 277 -20.745 0.475 -34.221 1.00 66.06 C
ANISOU 2120 C ASN A 277 8076 8499 8524 -217 79 -881 C
ATOM 2121 O ASN A 277 -20.919 -0.684 -34.611 1.00 68.04 O
ANISOU 2121 O ASN A 277 8409 8662 8781 -212 44 -916 O
ATOM 2122 CB ASN A 277 -22.998 0.992 -33.281 1.00 76.76 C
ANISOU 2122 CB ASN A 277 9320 9786 10058 -337 23 -775 C
ATOM 2123 CG ASN A 277 -23.822 1.268 -32.043 1.00 79.84 C
ANISOU 2123 CG ASN A 277 9622 10165 10547 -363 56 -703 C
ATOM 2124 OD1 ASN A 277 -23.501 0.794 -30.953 1.00 67.74 O
ANISOU 2124 OD1 ASN A 277 8084 8626 9030 -323 116 -679 O
ATOM 2125 ND2 ASN A 277 -24.886 2.046 -32.200 1.00 96.83 N
ANISOU 2125 ND2 ASN A 277 11707 12318 12766 -423 20 -666 N
ATOM 2126 N LEU A 278 -19.920 1.318 -34.837 1.00 63.35 N
ANISOU 2126 N LEU A 278 7728 8248 8095 -198 106 -906 N
ATOM 2127 CA LEU A 278 -19.075 0.902 -35.949 1.00 63.41 C
ANISOU 2127 CA LEU A 278 7819 8271 8003 -157 115 -977 C
ATOM 2128 C LEU A 278 -17.855 0.111 -35.495 1.00 74.41 C
ANISOU 2128 C LEU A 278 9225 9681 9368 -55 186 -1008 C
ATOM 2129 O LEU A 278 -17.005 -0.216 -36.329 1.00 76.75 O
ANISOU 2129 O LEU A 278 9578 10002 9582 -2 216 -1069 O
ATOM 2130 CB LEU A 278 -18.622 2.123 -36.755 1.00 62.64 C
ANISOU 2130 CB LEU A 278 7707 8270 7825 -178 130 -982 C
ATOM 2131 CG LEU A 278 -19.700 3.032 -37.348 1.00 62.39 C
ANISOU 2131 CG LEU A 278 7667 8230 7808 -267 56 -948 C
ATOM 2132 CD1 LEU A 278 -19.064 4.166 -38.141 1.00 53.07 C
ANISOU 2132 CD1 LEU A 278 6488 7141 6536 -280 82 -950 C
ATOM 2133 CD2 LEU A 278 -20.662 2.239 -38.219 1.00 64.33 C
ANISOU 2133 CD2 LEU A 278 8001 8382 8061 -313 -41 -976 C
ATOM 2134 N TYR A 279 -17.757 -0.209 -34.202 1.00 73.23 N
ANISOU 2134 N TYR A 279 9024 9519 9280 -20 214 -967 N
ATOM 2135 CA TYR A 279 -16.546 -0.831 -33.676 1.00 72.84 C
ANISOU 2135 CA TYR A 279 8969 9497 9208 84 273 -984 C
ATOM 2136 C TYR A 279 -16.387 -2.264 -34.171 1.00 76.99 C
ANISOU 2136 C TYR A 279 9602 9924 9725 142 262 -1039 C
ATOM 2137 O TYR A 279 -15.264 -2.714 -34.429 1.00 70.20 O
ANISOU 2137 O TYR A 279 8761 9095 8817 238 312 -1084 O
ATOM 2138 CB TYR A 279 -16.560 -0.788 -32.147 1.00 67.82 C
ANISOU 2138 CB TYR A 279 8267 8870 8633 100 293 -919 C
ATOM 2139 CG TYR A 279 -15.340 -1.406 -31.507 1.00 66.94 C
ANISOU 2139 CG TYR A 279 8142 8790 8504 210 338 -924 C
ATOM 2140 CD1 TYR A 279 -14.122 -0.739 -31.502 1.00 67.59 C
ANISOU 2140 CD1 TYR A 279 8153 8993 8534 258 383 -937 C
ATOM 2141 CD2 TYR A 279 -15.405 -2.655 -30.904 1.00 61.29 C
ANISOU 2141 CD2 TYR A 279 7480 7978 7829 264 329 -911 C
ATOM 2142 CE1 TYR A 279 -13.002 -1.300 -30.919 1.00 63.66 C
ANISOU 2142 CE1 TYR A 279 7628 8530 8030 362 414 -938 C
ATOM 2143 CE2 TYR A 279 -14.291 -3.224 -30.317 1.00 63.10 C
ANISOU 2143 CE2 TYR A 279 7696 8233 8046 374 360 -909 C
ATOM 2144 CZ TYR A 279 -13.093 -2.543 -30.328 1.00 66.75 C
ANISOU 2144 CZ TYR A 279 8076 8825 8460 425 400 -923 C
ATOM 2145 OH TYR A 279 -11.982 -3.107 -29.745 1.00 74.16 O
ANISOU 2145 OH TYR A 279 8985 9795 9396 538 421 -918 O
ATOM 2146 N SER A 280 -17.495 -2.998 -34.311 1.00 79.54 N
ANISOU 2146 N SER A 280 9995 10124 10102 87 199 -1037 N
ATOM 2147 CA SER A 280 -17.405 -4.399 -34.714 1.00 68.39 C
ANISOU 2147 CA SER A 280 8700 8596 8689 136 182 -1091 C
ATOM 2148 C SER A 280 -16.808 -4.539 -36.109 1.00 73.46 C
ANISOU 2148 C SER A 280 9426 9254 9231 172 193 -1182 C
ATOM 2149 O SER A 280 -16.058 -5.485 -36.380 1.00 72.40 O
ANISOU 2149 O SER A 280 9367 9076 9066 267 226 -1240 O
ATOM 2150 CB SER A 280 -18.786 -5.051 -34.658 1.00 71.57 C
ANISOU 2150 CB SER A 280 9155 8864 9173 44 103 -1070 C
ATOM 2151 OG SER A 280 -19.674 -4.442 -35.579 1.00 78.26 O
ANISOU 2151 OG SER A 280 10011 9715 10008 -57 36 -1082 O
ATOM 2152 N LEU A 281 -17.126 -3.607 -37.006 1.00 73.85 N
ANISOU 2152 N LEU A 281 9471 9364 9225 101 169 -1195 N
ATOM 2153 CA LEU A 281 -16.629 -3.666 -38.374 1.00 74.80 C
ANISOU 2153 CA LEU A 281 9682 9505 9232 125 182 -1278 C
ATOM 2154 C LEU A 281 -15.314 -2.926 -38.569 1.00 77.22 C
ANISOU 2154 C LEU A 281 9924 9955 9462 194 281 -1289 C
ATOM 2155 O LEU A 281 -14.634 -3.159 -39.575 1.00 75.15 O
ANISOU 2155 O LEU A 281 9735 9715 9103 245 326 -1360 O
ATOM 2156 CB LEU A 281 -17.674 -3.097 -39.339 1.00 62.49 C
ANISOU 2156 CB LEU A 281 8170 7932 7643 10 94 -1282 C
ATOM 2157 CG LEU A 281 -19.006 -3.845 -39.406 1.00 74.09 C
ANISOU 2157 CG LEU A 281 9705 9261 9184 -73 -17 -1280 C
ATOM 2158 CD1 LEU A 281 -19.961 -3.153 -40.366 1.00 82.54 C
ANISOU 2158 CD1 LEU A 281 10801 10338 10222 -182 -113 -1277 C
ATOM 2159 CD2 LEU A 281 -18.788 -5.295 -39.813 1.00 57.61 C
ANISOU 2159 CD2 LEU A 281 7761 7052 7076 -19 -26 -1362 C
ATOM 2160 N THR A 282 -14.937 -2.047 -37.640 1.00 73.70 N
ANISOU 2160 N THR A 282 9344 9604 9053 194 319 -1223 N
ATOM 2161 CA THR A 282 -13.730 -1.242 -37.776 1.00 77.11 C
ANISOU 2161 CA THR A 282 9697 10176 9426 239 405 -1224 C
ATOM 2162 C THR A 282 -12.687 -1.558 -36.712 1.00 67.10 C
ANISOU 2162 C THR A 282 8341 8955 8200 338 465 -1205 C
ATOM 2163 O THR A 282 -11.724 -0.801 -36.562 1.00 72.66 O
ANISOU 2163 O THR A 282 8946 9781 8879 362 526 -1190 O
ATOM 2164 CB THR A 282 -14.078 0.247 -37.729 1.00 74.84 C
ANISOU 2164 CB THR A 282 9330 9971 9134 143 390 -1167 C
ATOM 2165 OG1 THR A 282 -14.674 0.560 -36.465 1.00 82.55 O
ANISOU 2165 OG1 THR A 282 10228 10930 10207 107 357 -1098 O
ATOM 2166 CG2 THR A 282 -15.049 0.601 -38.844 1.00 69.12 C
ANISOU 2166 CG2 THR A 282 8690 9209 8364 52 323 -1180 C
ATOM 2167 N VAL A 283 -12.853 -2.646 -35.972 1.00 66.94 N
ANISOU 2167 N VAL A 283 8351 8838 8244 393 444 -1200 N
ATOM 2168 CA VAL A 283 -11.888 -2.988 -34.921 1.00 74.03 C
ANISOU 2168 CA VAL A 283 9170 9777 9181 494 486 -1173 C
ATOM 2169 C VAL A 283 -10.540 -3.310 -35.561 1.00 70.99 C
ANISOU 2169 C VAL A 283 8774 9459 8739 608 568 -1232 C
ATOM 2170 O VAL A 283 -10.482 -4.119 -36.504 1.00 70.58 O
ANISOU 2170 O VAL A 283 8832 9341 8645 657 585 -1305 O
ATOM 2171 CB VAL A 283 -12.402 -4.161 -34.083 1.00 71.01 C
ANISOU 2171 CB VAL A 283 8846 9262 8872 528 443 -1150 C
ATOM 2172 CG1 VAL A 283 -12.904 -5.290 -34.976 1.00 73.97 C
ANISOU 2172 CG1 VAL A 283 9372 9498 9237 541 415 -1217 C
ATOM 2173 CG2 VAL A 283 -11.318 -4.656 -33.135 1.00 73.62 C
ANISOU 2173 CG2 VAL A 283 9115 9626 9232 651 479 -1126 C
ATOM 2174 N PRO A 284 -9.447 -2.687 -35.113 1.00 70.92 N
ANISOU 2174 N PRO A 284 8636 9583 8729 652 621 -1207 N
ATOM 2175 CA PRO A 284 -8.147 -2.949 -35.758 1.00 71.67 C
ANISOU 2175 CA PRO A 284 8698 9755 8779 762 711 -1260 C
ATOM 2176 C PRO A 284 -7.680 -4.388 -35.616 1.00 73.10 C
ANISOU 2176 C PRO A 284 8936 9849 8991 907 728 -1299 C
ATOM 2177 O PRO A 284 -7.337 -5.031 -36.617 1.00 88.79 O
ANISOU 2177 O PRO A 284 11004 11804 10927 979 781 -1376 O
ATOM 2178 CB PRO A 284 -7.206 -1.967 -35.046 1.00 65.82 C
ANISOU 2178 CB PRO A 284 7786 9167 8057 759 741 -1208 C
ATOM 2179 CG PRO A 284 -8.103 -0.902 -34.495 1.00 70.45 C
ANISOU 2179 CG PRO A 284 8346 9762 8660 622 679 -1148 C
ATOM 2180 CD PRO A 284 -9.366 -1.608 -34.116 1.00 70.53 C
ANISOU 2180 CD PRO A 284 8463 9625 8712 592 605 -1135 C
ATOM 2181 N PHE A 285 -7.655 -4.912 -34.395 1.00 77.72 N
ANISOU 2181 N PHE A 285 9489 10390 9652 956 685 -1246 N
ATOM 2182 CA PHE A 285 -7.173 -6.261 -34.108 1.00 80.63 C
ANISOU 2182 CA PHE A 285 9907 10669 10060 1102 693 -1267 C
ATOM 2183 C PHE A 285 -8.332 -7.032 -33.484 1.00 84.58 C
ANISOU 2183 C PHE A 285 10521 11004 10613 1060 610 -1234 C
ATOM 2184 O PHE A 285 -8.473 -7.086 -32.259 1.00 83.26 O
ANISOU 2184 O PHE A 285 10309 10824 10500 1058 566 -1158 O
ATOM 2185 CB PHE A 285 -5.949 -6.213 -33.195 1.00 77.88 C
ANISOU 2185 CB PHE A 285 9411 10426 9753 1209 716 -1222 C
ATOM 2186 CG PHE A 285 -4.901 -5.230 -33.642 1.00 71.27 C
ANISOU 2186 CG PHE A 285 8430 9769 8880 1213 789 -1234 C
ATOM 2187 CD1 PHE A 285 -3.947 -5.592 -34.578 1.00 61.63 C
ANISOU 2187 CD1 PHE A 285 7193 8594 7628 1322 885 -1302 C
ATOM 2188 CD2 PHE A 285 -4.876 -3.942 -33.131 1.00 70.15 C
ANISOU 2188 CD2 PHE A 285 8172 9745 8736 1104 768 -1177 C
ATOM 2189 CE1 PHE A 285 -2.985 -4.689 -34.993 1.00 66.91 C
ANISOU 2189 CE1 PHE A 285 7722 9433 8269 1316 961 -1306 C
ATOM 2190 CE2 PHE A 285 -3.917 -3.035 -33.543 1.00 67.10 C
ANISOU 2190 CE2 PHE A 285 7655 9518 8323 1093 834 -1183 C
ATOM 2191 CZ PHE A 285 -2.971 -3.410 -34.475 1.00 68.47 C
ANISOU 2191 CZ PHE A 285 7803 9743 8470 1195 932 -1243 C
ATOM 2192 N GLY A 286 -9.159 -7.633 -34.336 1.00 78.83 N
ANISOU 2192 N GLY A 286 9941 10148 9864 1022 589 -1292 N
ATOM 2193 CA GLY A 286 -10.393 -8.257 -33.898 1.00 82.89 C
ANISOU 2193 CA GLY A 286 10557 10507 10430 949 510 -1261 C
ATOM 2194 C GLY A 286 -10.245 -9.627 -33.269 1.00 83.39 C
ANISOU 2194 C GLY A 286 10698 10432 10555 1056 493 -1250 C
ATOM 2195 O GLY A 286 -11.229 -10.362 -33.141 1.00 76.32 O
ANISOU 2195 O GLY A 286 9915 9382 9701 1001 436 -1240 O
ATOM 2196 N GLN A 287 -9.025 -9.987 -32.871 1.00 86.89 N
ANISOU 2196 N GLN A 287 11080 10925 11011 1207 539 -1246 N
ATOM 2197 CA GLN A 287 -8.782 -11.252 -32.195 1.00 84.68 C
ANISOU 2197 CA GLN A 287 10866 10516 10791 1324 520 -1223 C
ATOM 2198 C GLN A 287 -8.357 -11.087 -30.743 1.00 97.55 C
ANISOU 2198 C GLN A 287 12389 12207 12467 1364 495 -1117 C
ATOM 2199 O GLN A 287 -8.230 -12.092 -30.036 1.00 99.79 O
ANISOU 2199 O GLN A 287 12731 12382 12801 1453 468 -1077 O
ATOM 2200 CB GLN A 287 -7.717 -12.064 -32.948 1.00 87.41 C
ANISOU 2200 CB GLN A 287 11253 10837 11121 1498 586 -1309 C
ATOM 2201 CG GLN A 287 -8.043 -12.288 -34.415 1.00103.05 C
ANISOU 2201 CG GLN A 287 13361 12757 13037 1472 617 -1424 C
ATOM 2202 CD GLN A 287 -7.843 -13.728 -34.847 1.00108.02 C
ANISOU 2202 CD GLN A 287 14150 13210 13683 1602 630 -1498 C
ATOM 2203 OE1 GLN A 287 -7.995 -14.654 -34.050 1.00113.70 O
ANISOU 2203 OE1 GLN A 287 14931 13795 14476 1655 586 -1452 O
ATOM 2204 NE2 GLN A 287 -7.497 -13.923 -36.114 1.00100.45 N
ANISOU 2204 NE2 GLN A 287 13269 12244 12651 1654 695 -1613 N
ATOM 2205 N LYS A 288 -8.138 -9.855 -30.280 1.00100.80 N
ANISOU 2205 N LYS A 288 12657 12783 12858 1299 498 -1071 N
ATOM 2206 CA LYS A 288 -7.805 -9.610 -28.886 1.00100.21 C
ANISOU 2206 CA LYS A 288 12493 12771 12811 1319 463 -974 C
ATOM 2207 C LYS A 288 -9.024 -9.056 -28.170 1.00112.79 C
ANISOU 2207 C LYS A 288 14104 14341 14412 1164 417 -907 C
ATOM 2208 O LYS A 288 -9.536 -7.996 -28.567 1.00111.56 O
ANISOU 2208 O LYS A 288 13904 14258 14226 1043 424 -921 O
ATOM 2209 CB LYS A 288 -6.633 -8.643 -28.774 1.00 91.48 C
ANISOU 2209 CB LYS A 288 11215 11863 11680 1359 495 -971 C
ATOM 2210 CG LYS A 288 -5.348 -9.215 -29.343 1.00 85.09 C
ANISOU 2210 CG LYS A 288 10363 11091 10878 1528 550 -1025 C
ATOM 2211 CD LYS A 288 -4.133 -8.386 -28.983 1.00 71.80 C
ANISOU 2211 CD LYS A 288 8489 9600 9191 1572 568 -1001 C
ATOM 2212 CE LYS A 288 -2.863 -9.162 -29.294 1.00 81.43 C
ANISOU 2212 CE LYS A 288 9655 10842 10442 1764 616 -1036 C
ATOM 2213 NZ LYS A 288 -1.640 -8.329 -29.162 1.00 99.73 N
ANISOU 2213 NZ LYS A 288 11769 13359 12763 1799 643 -1023 N
ATOM 2214 N PRO A 289 -9.519 -9.720 -27.131 1.00124.99 N
ANISOU 2214 N PRO A 289 15710 15785 15995 1165 375 -831 N
ATOM 2215 CA PRO A 289 -10.791 -9.318 -26.527 1.00124.92 C
ANISOU 2215 CA PRO A 289 15728 15737 15998 1020 347 -771 C
ATOM 2216 C PRO A 289 -10.658 -8.063 -25.678 1.00121.40 C
ANISOU 2216 C PRO A 289 15164 15443 15521 961 344 -718 C
ATOM 2217 O PRO A 289 -9.579 -7.704 -25.202 1.00113.98 O
ANISOU 2217 O PRO A 289 14131 14619 14558 1036 343 -703 O
ATOM 2218 CB PRO A 289 -11.162 -10.527 -25.662 1.00117.04 C
ANISOU 2218 CB PRO A 289 14837 14587 15046 1059 316 -702 C
ATOM 2219 CG PRO A 289 -9.843 -11.107 -25.275 1.00117.09 C
ANISOU 2219 CG PRO A 289 14817 14620 15052 1230 313 -690 C
ATOM 2220 CD PRO A 289 -8.926 -10.887 -26.454 1.00115.59 C
ANISOU 2220 CD PRO A 289 14570 14509 14840 1306 355 -790 C
ATOM 2221 N ASN A 290 -11.795 -7.398 -25.495 1.00129.49 N
ANISOU 2221 N ASN A 290 16192 16460 16548 823 339 -692 N
ATOM 2222 CA ASN A 290 -11.849 -6.214 -24.655 1.00127.37 C
ANISOU 2222 CA ASN A 290 15835 16311 16250 758 339 -647 C
ATOM 2223 C ASN A 290 -11.677 -6.591 -23.187 1.00119.96 C
ANISOU 2223 C ASN A 290 14911 15362 15305 802 317 -558 C
ATOM 2224 O ASN A 290 -11.791 -7.756 -22.794 1.00113.00 O
ANISOU 2224 O ASN A 290 14118 14365 14453 858 302 -518 O
ATOM 2225 CB ASN A 290 -13.176 -5.478 -24.843 1.00113.68 C
ANISOU 2225 CB ASN A 290 14106 14558 14529 612 346 -641 C
ATOM 2226 CG ASN A 290 -13.431 -5.089 -26.284 1.00135.86 C
ANISOU 2226 CG ASN A 290 16913 17372 17335 562 355 -720 C
ATOM 2227 OD1 ASN A 290 -13.002 -4.028 -26.737 1.00143.44 O
ANISOU 2227 OD1 ASN A 290 17795 18447 18258 538 370 -753 O
ATOM 2228 ND2 ASN A 290 -14.138 -5.945 -27.012 1.00145.15 N
ANISOU 2228 ND2 ASN A 290 18182 18422 18547 541 340 -748 N
ATOM 2229 N ILE A 291 -11.396 -5.579 -22.369 1.00115.83 N
ANISOU 2229 N ILE A 291 14311 14959 14739 772 312 -526 N
ATOM 2230 CA ILE A 291 -11.355 -5.746 -20.919 1.00104.27 C
ANISOU 2230 CA ILE A 291 12870 13500 13250 793 288 -441 C
ATOM 2231 C ILE A 291 -12.795 -5.652 -20.423 1.00 98.33 C
ANISOU 2231 C ILE A 291 12181 12670 12511 681 313 -393 C
ATOM 2232 O ILE A 291 -13.374 -4.566 -20.369 1.00 98.45 O
ANISOU 2232 O ILE A 291 12151 12743 12511 586 336 -403 O
ATOM 2233 CB ILE A 291 -10.455 -4.710 -20.244 1.00 97.79 C
ANISOU 2233 CB ILE A 291 11951 12835 12369 803 266 -434 C
ATOM 2234 CG1 ILE A 291 -9.015 -4.853 -20.734 1.00101.65 C
ANISOU 2234 CG1 ILE A 291 12358 13406 12860 913 244 -475 C
ATOM 2235 CG2 ILE A 291 -10.514 -4.859 -18.732 1.00 90.21 C
ANISOU 2235 CG2 ILE A 291 11035 11876 11364 814 237 -348 C
ATOM 2236 CD1 ILE A 291 -8.052 -3.914 -20.050 1.00 90.74 C
ANISOU 2236 CD1 ILE A 291 10870 12177 11430 919 207 -466 C
ATOM 2237 N ASP A 292 -13.383 -6.791 -20.075 1.00 93.55 N
ANISOU 2237 N ASP A 292 11675 11928 11940 692 313 -339 N
ATOM 2238 CA ASP A 292 -14.752 -6.856 -19.569 1.00 92.55 C
ANISOU 2238 CA ASP A 292 11603 11722 11839 588 345 -283 C
ATOM 2239 C ASP A 292 -14.708 -7.570 -18.223 1.00100.15 C
ANISOU 2239 C ASP A 292 12641 12638 12771 630 339 -182 C
ATOM 2240 O ASP A 292 -14.705 -8.804 -18.165 1.00110.65 O
ANISOU 2240 O ASP A 292 14060 13846 14136 682 324 -144 O
ATOM 2241 CB ASP A 292 -15.672 -7.568 -20.557 1.00105.46 C
ANISOU 2241 CB ASP A 292 13292 13224 13554 533 352 -311 C
ATOM 2242 CG ASP A 292 -17.132 -7.472 -20.165 1.00106.06 C
ANISOU 2242 CG ASP A 292 13388 13237 13672 411 388 -257 C
ATOM 2243 OD1 ASP A 292 -17.672 -6.345 -20.154 1.00106.15 O
ANISOU 2243 OD1 ASP A 292 13328 13327 13675 333 415 -270 O
ATOM 2244 OD2 ASP A 292 -17.741 -8.522 -19.871 1.00115.09 O
ANISOU 2244 OD2 ASP A 292 14617 14250 14863 392 392 -201 O
ATOM 2245 N VAL A 293 -14.676 -6.792 -17.142 1.00100.73 N
ANISOU 2245 N VAL A 293 12693 12804 12776 608 350 -138 N
ATOM 2246 CA VAL A 293 -14.555 -7.340 -15.796 1.00 96.81 C
ANISOU 2246 CA VAL A 293 12274 12284 12224 649 342 -40 C
ATOM 2247 C VAL A 293 -15.931 -7.715 -15.262 1.00 90.22 C
ANISOU 2247 C VAL A 293 11514 11348 11416 556 404 34 C
ATOM 2248 O VAL A 293 -16.097 -7.951 -14.060 1.00 93.20 O
ANISOU 2248 O VAL A 293 11960 11715 11735 558 420 123 O
ATOM 2249 CB VAL A 293 -13.853 -6.344 -14.854 1.00 82.24 C
ANISOU 2249 CB VAL A 293 10384 10586 10277 667 319 -31 C
ATOM 2250 CG1 VAL A 293 -12.432 -6.080 -15.326 1.00 85.49 C
ANISOU 2250 CG1 VAL A 293 10711 11098 10674 758 254 -91 C
ATOM 2251 CG2 VAL A 293 -14.643 -5.047 -14.771 1.00 74.91 C
ANISOU 2251 CG2 VAL A 293 9406 9726 9329 556 374 -61 C
ATOM 2252 N THR A 294 -16.925 -7.774 -16.151 1.00 96.36 N
ANISOU 2252 N THR A 294 12396 12747 11471 521 291 -532 N
ATOM 2253 CA THR A 294 -18.273 -8.146 -15.731 1.00 95.44 C
ANISOU 2253 CA THR A 294 12312 12520 11430 421 362 -579 C
ATOM 2254 C THR A 294 -18.306 -9.566 -15.176 1.00 90.84 C
ANISOU 2254 C THR A 294 11853 11806 10856 428 407 -562 C
ATOM 2255 O THR A 294 -18.952 -9.825 -14.154 1.00 87.78 O
ANISOU 2255 O THR A 294 11536 11332 10487 352 476 -547 O
ATOM 2256 CB THR A 294 -19.246 -8.003 -16.903 1.00 88.41 C
ANISOU 2256 CB THR A 294 11338 11631 10621 388 354 -680 C
ATOM 2257 OG1 THR A 294 -19.274 -6.637 -17.337 1.00 85.26 O
ANISOU 2257 OG1 THR A 294 10834 11349 10213 378 316 -692 O
ATOM 2258 CG2 THR A 294 -20.649 -8.428 -16.492 1.00 80.54 C
ANISOU 2258 CG2 THR A 294 10369 10522 9710 283 428 -735 C
ATOM 2259 N ASP A 295 -17.612 -10.498 -15.834 1.00 98.61 N
ANISOU 2259 N ASP A 295 12869 12771 11825 519 371 -564 N
ATOM 2260 CA ASP A 295 -17.560 -11.868 -15.332 1.00102.19 C
ANISOU 2260 CA ASP A 295 13447 13097 12282 535 410 -544 C
ATOM 2261 C ASP A 295 -16.881 -11.930 -13.970 1.00 92.91 C
ANISOU 2261 C ASP A 295 12365 11904 11031 548 428 -446 C
ATOM 2262 O ASP A 295 -17.263 -12.736 -13.114 1.00104.46 O
ANISOU 2262 O ASP A 295 13938 13249 12503 509 489 -425 O
ATOM 2263 CB ASP A 295 -16.839 -12.772 -16.332 1.00107.69 C
ANISOU 2263 CB ASP A 295 14157 13789 12972 641 360 -564 C
ATOM 2264 CG ASP A 295 -17.731 -13.200 -17.482 1.00 99.69 C
ANISOU 2264 CG ASP A 295 13100 12733 12044 617 363 -666 C
ATOM 2265 OD1 ASP A 295 -18.940 -12.887 -17.451 1.00 83.84 O
ANISOU 2265 OD1 ASP A 295 11058 10692 10107 515 405 -723 O
ATOM 2266 OD2 ASP A 295 -17.223 -13.854 -18.416 1.00109.09 O
ANISOU 2266 OD2 ASP A 295 14291 13926 13233 700 322 -693 O
ATOM 2267 N ALA A 296 -15.873 -11.083 -13.749 1.00 92.60 N
ANISOU 2267 N ALA A 296 12286 11982 10917 600 377 -386 N
ATOM 2268 CA ALA A 296 -15.178 -11.082 -12.466 1.00 92.90 C
ANISOU 2268 CA ALA A 296 12407 12014 10878 617 385 -294 C
ATOM 2269 C ALA A 296 -16.071 -10.549 -11.352 1.00 93.99 C
ANISOU 2269 C ALA A 296 12575 12110 11027 503 454 -281 C
ATOM 2270 O ALA A 296 -15.999 -11.022 -10.212 1.00 94.51 O
ANISOU 2270 O ALA A 296 12752 12101 11056 488 494 -224 O
ATOM 2271 CB ALA A 296 -13.893 -10.261 -12.563 1.00 72.35 C
ANISOU 2271 CB ALA A 296 9741 9552 8196 697 310 -242 C
ATOM 2272 N MET A 297 -16.917 -9.565 -11.661 1.00 88.52 N
ANISOU 2272 N MET A 297 11787 11465 10383 424 468 -332 N
ATOM 2273 CA MET A 297 -17.819 -9.025 -10.650 1.00 87.01 C
ANISOU 2273 CA MET A 297 11616 11236 10208 314 537 -326 C
ATOM 2274 C MET A 297 -18.864 -10.055 -10.237 1.00 93.34 C
ANISOU 2274 C MET A 297 12507 11887 11072 243 622 -358 C
ATOM 2275 O MET A 297 -19.229 -10.139 -9.058 1.00 93.39 O
ANISOU 2275 O MET A 297 12596 11827 11061 181 687 -320 O
ATOM 2276 CB MET A 297 -18.485 -7.753 -11.173 1.00 89.51 C
ANISOU 2276 CB MET A 297 11804 11638 10566 255 528 -381 C
ATOM 2277 CG MET A 297 -17.499 -6.646 -11.513 1.00 76.49 C
ANISOU 2277 CG MET A 297 10072 10137 8856 314 452 -348 C
ATOM 2278 SD MET A 297 -18.262 -5.266 -12.384 1.00 92.18 S
ANISOU 2278 SD MET A 297 11911 12217 10895 259 433 -419 S
ATOM 2279 CE MET A 297 -19.483 -4.750 -11.183 1.00 91.18 C
ANISOU 2279 CE MET A 297 11811 12030 10803 130 522 -425 C
ATOM 2280 N VAL A 298 -19.352 -10.851 -11.190 1.00 89.81 N
ANISOU 2280 N VAL A 298 12047 11382 10696 248 626 -428 N
ATOM 2281 CA VAL A 298 -20.286 -11.918 -10.850 1.00 94.19 C
ANISOU 2281 CA VAL A 298 12689 11787 11312 182 706 -460 C
ATOM 2282 C VAL A 298 -19.559 -13.062 -10.152 1.00 91.92 C
ANISOU 2282 C VAL A 298 12548 11410 10968 239 719 -390 C
ATOM 2283 O VAL A 298 -20.123 -13.718 -9.266 1.00 84.13 O
ANISOU 2283 O VAL A 298 11668 10305 9993 177 798 -373 O
ATOM 2284 CB VAL A 298 -21.029 -12.396 -12.112 1.00 82.47 C
ANISOU 2284 CB VAL A 298 11142 10271 9922 169 700 -561 C
ATOM 2285 CG1 VAL A 298 -22.026 -13.493 -11.766 1.00 72.64 C
ANISOU 2285 CG1 VAL A 298 9984 8870 8747 92 787 -599 C
ATOM 2286 CG2 VAL A 298 -21.734 -11.228 -12.784 1.00 89.27 C
ANISOU 2286 CG2 VAL A 298 11862 11223 10835 118 682 -628 C
ATOM 2287 N ASP A 299 -18.300 -13.315 -10.522 1.00 84.98 N
ANISOU 2287 N ASP A 299 11678 10585 10024 360 644 -347 N
ATOM 2288 CA ASP A 299 -17.528 -14.357 -9.851 1.00 87.91 C
ANISOU 2288 CA ASP A 299 12188 10878 10335 427 646 -277 C
ATOM 2289 C ASP A 299 -17.280 -14.020 -8.388 1.00 85.66 C
ANISOU 2289 C ASP A 299 11986 10585 9977 400 678 -191 C
ATOM 2290 O ASP A 299 -17.088 -14.924 -7.568 1.00 91.00 O
ANISOU 2290 O ASP A 299 12801 11158 10617 415 713 -139 O
ATOM 2291 CB ASP A 299 -16.195 -14.576 -10.570 1.00 89.48 C
ANISOU 2291 CB ASP A 299 12364 11155 10481 566 554 -252 C
ATOM 2292 CG ASP A 299 -16.347 -15.350 -11.863 1.00 94.83 C
ANISOU 2292 CG ASP A 299 13012 11801 11220 608 533 -325 C
ATOM 2293 OD1 ASP A 299 -17.475 -15.791 -12.165 1.00100.97 O
ANISOU 2293 OD1 ASP A 299 13794 12488 12081 529 588 -395 O
ATOM 2294 OD2 ASP A 299 -15.338 -15.516 -12.579 1.00 89.09 O
ANISOU 2294 OD2 ASP A 299 12254 11138 10457 719 462 -316 O
ATOM 2295 N GLN A 300 -17.279 -12.734 -8.041 1.00 87.04 N
ANISOU 2295 N GLN A 300 12083 10862 10125 363 666 -176 N
ATOM 2296 CA GLN A 300 -17.033 -12.289 -6.677 1.00 85.06 C
ANISOU 2296 CA GLN A 300 11903 10615 9800 336 691 -98 C
ATOM 2297 C GLN A 300 -18.307 -11.860 -5.961 1.00 82.41 C
ANISOU 2297 C GLN A 300 11577 10225 9510 201 784 -123 C
ATOM 2298 O GLN A 300 -18.225 -11.235 -4.899 1.00 74.21 O
ANISOU 2298 O GLN A 300 10574 9207 8415 166 805 -70 O
ATOM 2299 CB GLN A 300 -16.017 -11.146 -6.675 1.00 78.15 C
ANISOU 2299 CB GLN A 300 10944 9894 8854 394 610 -56 C
ATOM 2300 CG GLN A 300 -14.691 -11.508 -7.325 1.00 84.73 C
ANISOU 2300 CG GLN A 300 11762 10792 9641 528 520 -29 C
ATOM 2301 CD GLN A 300 -13.747 -10.328 -7.421 1.00 90.57 C
ANISOU 2301 CD GLN A 300 12405 11689 10321 575 445 3 C
ATOM 2302 OE1 GLN A 300 -13.897 -9.337 -6.705 1.00 91.61 O
ANISOU 2302 OE1 GLN A 300 12514 11870 10423 517 457 27 O
ATOM 2303 NE2 GLN A 300 -12.767 -10.425 -8.312 1.00 78.94 N
ANISOU 2303 NE2 GLN A 300 10872 10293 8828 678 368 1 N
ATOM 2304 N ALA A 301 -19.476 -12.177 -6.522 1.00 89.62 N
ANISOU 2304 N ALA A 301 12458 11071 10524 124 839 -206 N
ATOM 2305 CA ALA A 301 -20.768 -11.899 -5.891 1.00 90.96 C
ANISOU 2305 CA ALA A 301 12635 11178 10749 -7 935 -239 C
ATOM 2306 C ALA A 301 -20.934 -10.414 -5.572 1.00 87.30 C
ANISOU 2306 C ALA A 301 12078 10825 10268 -54 927 -237 C
ATOM 2307 O ALA A 301 -21.381 -10.040 -4.485 1.00 93.92 O
ANISOU 2307 O ALA A 301 12965 11635 11085 -127 992 -208 O
ATOM 2308 CB ALA A 301 -20.966 -12.751 -4.635 1.00 79.25 C
ANISOU 2308 CB ALA A 301 11317 9562 9231 -46 1018 -184 C
ATOM 2309 N TRP A 302 -20.572 -9.560 -6.525 1.00 88.33 N
ANISOU 2309 N TRP A 302 12077 11079 10405 -10 849 -266 N
ATOM 2310 CA TRP A 302 -20.767 -8.127 -6.371 1.00 79.46 C
ANISOU 2310 CA TRP A 302 10858 10061 9273 -53 838 -272 C
ATOM 2311 C TRP A 302 -22.233 -7.765 -6.563 1.00 86.17 C
ANISOU 2311 C TRP A 302 11641 10876 10223 -165 905 -356 C
ATOM 2312 O TRP A 302 -22.913 -8.307 -7.440 1.00 97.76 O
ANISOU 2312 O TRP A 302 13069 12300 11776 -182 916 -432 O
ATOM 2313 CB TRP A 302 -19.914 -7.352 -7.376 1.00 89.08 C
ANISOU 2313 CB TRP A 302 11961 11417 10467 28 735 -278 C
ATOM 2314 CG TRP A 302 -18.482 -7.187 -6.973 1.00 96.15 C
ANISOU 2314 CG TRP A 302 12892 12384 11257 120 669 -191 C
ATOM 2315 CD1 TRP A 302 -17.721 -8.069 -6.260 1.00 95.86 C
ANISOU 2315 CD1 TRP A 302 12977 12291 11155 176 667 -122 C
ATOM 2316 CD2 TRP A 302 -17.639 -6.060 -7.245 1.00 92.15 C
ANISOU 2316 CD2 TRP A 302 12296 12017 10698 166 594 -167 C
ATOM 2317 NE1 TRP A 302 -16.456 -7.564 -6.080 1.00 92.46 N
ANISOU 2317 NE1 TRP A 302 12532 11961 10636 256 592 -59 N
ATOM 2318 CE2 TRP A 302 -16.380 -6.331 -6.673 1.00 93.35 C
ANISOU 2318 CE2 TRP A 302 12517 12196 10758 248 548 -85 C
ATOM 2319 CE3 TRP A 302 -17.828 -4.848 -7.917 1.00 83.30 C
ANISOU 2319 CE3 TRP A 302 11048 11002 9600 146 560 -207 C
ATOM 2320 CZ2 TRP A 302 -15.315 -5.436 -6.755 1.00 88.64 C
ANISOU 2320 CZ2 TRP A 302 11857 11728 10094 306 473 -45 C
ATOM 2321 CZ3 TRP A 302 -16.769 -3.961 -7.997 1.00 80.04 C
ANISOU 2321 CZ3 TRP A 302 10581 10712 9119 202 488 -164 C
ATOM 2322 CH2 TRP A 302 -15.529 -4.260 -7.419 1.00 78.57 C
ANISOU 2322 CH2 TRP A 302 10458 10550 8844 278 447 -85 C
ATOM 2323 N ASP A 303 -22.717 -6.845 -5.739 1.00 80.17 N
ANISOU 2323 N ASP A 303 10868 10140 9452 -239 949 -346 N
ATOM 2324 CA ASP A 303 -24.051 -6.278 -5.881 1.00 86.88 C
ANISOU 2324 CA ASP A 303 11638 10979 10392 -340 1006 -425 C
ATOM 2325 C ASP A 303 -23.935 -4.778 -6.141 1.00 91.34 C
ANISOU 2325 C ASP A 303 12086 11675 10942 -338 955 -434 C
ATOM 2326 O ASP A 303 -22.837 -4.230 -6.262 1.00 86.09 O
ANISOU 2326 O ASP A 303 11402 11105 10202 -264 878 -382 O
ATOM 2327 CB ASP A 303 -24.909 -6.571 -4.645 1.00 94.12 C
ANISOU 2327 CB ASP A 303 12646 11792 11322 -440 1121 -414 C
ATOM 2328 CG ASP A 303 -24.248 -6.135 -3.352 1.00 84.88 C
ANISOU 2328 CG ASP A 303 11563 10642 10047 -436 1133 -322 C
ATOM 2329 OD1 ASP A 303 -23.105 -5.637 -3.399 1.00 91.70 O
ANISOU 2329 OD1 ASP A 303 12414 11598 10829 -354 1050 -266 O
ATOM 2330 OD2 ASP A 303 -24.875 -6.293 -2.284 1.00 87.96 O
ANISOU 2330 OD2 ASP A 303 12034 10954 10434 -515 1226 -306 O
ATOM 2331 N ALA A 304 -25.089 -4.113 -6.228 1.00 93.83 N
ANISOU 2331 N ALA A 304 12324 11994 11333 -423 1000 -502 N
ATOM 2332 CA ALA A 304 -25.092 -2.687 -6.538 1.00 85.02 C
ANISOU 2332 CA ALA A 304 11098 10994 10212 -424 954 -518 C
ATOM 2333 C ALA A 304 -24.450 -1.874 -5.422 1.00 86.28 C
ANISOU 2333 C ALA A 304 11302 11203 10276 -426 955 -438 C
ATOM 2334 O ALA A 304 -23.771 -0.876 -5.688 1.00 81.99 O
ANISOU 2334 O ALA A 304 10698 10770 9686 -383 885 -415 O
ATOM 2335 CB ALA A 304 -26.518 -2.209 -6.801 1.00 79.57 C
ANISOU 2335 CB ALA A 304 10321 10287 9625 -513 1005 -610 C
ATOM 2336 N GLN A 305 -24.655 -2.280 -4.166 1.00 88.87 N
ANISOU 2336 N GLN A 305 11741 11452 10574 -476 1033 -395 N
ATOM 2337 CA GLN A 305 -24.033 -1.564 -3.058 1.00102.32 C
ANISOU 2337 CA GLN A 305 13497 13198 12181 -477 1033 -319 C
ATOM 2338 C GLN A 305 -22.516 -1.683 -3.100 1.00 89.02 C
ANISOU 2338 C GLN A 305 11850 11576 10399 -372 944 -242 C
ATOM 2339 O GLN A 305 -21.812 -0.729 -2.748 1.00 90.36 O
ANISOU 2339 O GLN A 305 12000 11834 10498 -349 898 -197 O
ATOM 2340 CB GLN A 305 -24.571 -2.080 -1.723 1.00 97.67 C
ANISOU 2340 CB GLN A 305 13030 12503 11575 -550 1138 -289 C
ATOM 2341 CG GLN A 305 -24.068 -1.302 -0.518 1.00 87.74 C
ANISOU 2341 CG GLN A 305 11831 11286 10221 -560 1145 -218 C
ATOM 2342 CD GLN A 305 -24.514 -1.905 0.797 1.00 95.99 C
ANISOU 2342 CD GLN A 305 13012 12223 11238 -624 1247 -182 C
ATOM 2343 OE1 GLN A 305 -25.483 -2.661 0.851 1.00122.07 O
ANISOU 2343 OE1 GLN A 305 16346 15424 14612 -688 1332 -226 O
ATOM 2344 NE2 GLN A 305 -23.802 -1.576 1.869 1.00110.25 N
ANISOU 2344 NE2 GLN A 305 14903 14050 12938 -609 1241 -104 N
ATOM 2345 N ARG A 306 -21.995 -2.835 -3.529 1.00 83.89 N
ANISOU 2345 N ARG A 306 11251 10880 9745 -308 919 -228 N
ATOM 2346 CA ARG A 306 -20.551 -2.993 -3.653 1.00 86.62 C
ANISOU 2346 CA ARG A 306 11621 11287 10004 -202 832 -161 C
ATOM 2347 C ARG A 306 -19.985 -2.065 -4.720 1.00 86.20 C
ANISOU 2347 C ARG A 306 11439 11363 9951 -148 741 -182 C
ATOM 2348 O ARG A 306 -18.879 -1.536 -4.567 1.00 85.23 O
ANISOU 2348 O ARG A 306 11307 11327 9748 -89 676 -126 O
ATOM 2349 CB ARG A 306 -20.209 -4.449 -3.967 1.00 78.20 C
ANISOU 2349 CB ARG A 306 10632 10138 8943 -144 828 -151 C
ATOM 2350 CG ARG A 306 -18.732 -4.702 -4.218 1.00 76.76 C
ANISOU 2350 CG ARG A 306 10465 10017 8682 -26 736 -91 C
ATOM 2351 CD ARG A 306 -17.893 -4.406 -2.986 1.00 80.47 C
ANISOU 2351 CD ARG A 306 11017 10512 9045 -5 724 -2 C
ATOM 2352 NE ARG A 306 -16.471 -4.597 -3.245 1.00 81.57 N
ANISOU 2352 NE ARG A 306 11159 10720 9113 109 633 50 N
ATOM 2353 CZ ARG A 306 -15.848 -5.765 -3.178 1.00 77.70 C
ANISOU 2353 CZ ARG A 306 10758 10171 8594 182 616 87 C
ATOM 2354 NH1 ARG A 306 -16.492 -6.874 -2.854 1.00 79.57 N
ANISOU 2354 NH1 ARG A 306 11098 10274 8862 153 686 80 N
ATOM 2355 NH2 ARG A 306 -14.546 -5.823 -3.445 1.00 84.20 N
ANISOU 2355 NH2 ARG A 306 11567 11069 9355 288 530 129 N
ATOM 2356 N ILE A 307 -20.731 -1.854 -5.806 1.00 86.54 N
ANISOU 2356 N ILE A 307 11382 11420 10081 -169 737 -263 N
ATOM 2357 CA ILE A 307 -20.269 -0.963 -6.868 1.00 87.12 C
ANISOU 2357 CA ILE A 307 11336 11611 10154 -121 656 -285 C
ATOM 2358 C ILE A 307 -20.156 0.464 -6.349 1.00 89.30 C
ANISOU 2358 C ILE A 307 11567 11973 10389 -154 644 -263 C
ATOM 2359 O ILE A 307 -19.126 1.128 -6.518 1.00 87.98 O
ANISOU 2359 O ILE A 307 11364 11904 10159 -99 575 -222 O
ATOM 2360 CB ILE A 307 -21.207 -1.045 -8.085 1.00 79.94 C
ANISOU 2360 CB ILE A 307 10338 10690 9346 -141 656 -380 C
ATOM 2361 CG1 ILE A 307 -21.162 -2.441 -8.709 1.00 82.32 C
ANISOU 2361 CG1 ILE A 307 10681 10916 9682 -98 655 -402 C
ATOM 2362 CG2 ILE A 307 -20.837 0.013 -9.110 1.00 71.71 C
ANISOU 2362 CG2 ILE A 307 9178 9768 8301 -102 580 -403 C
ATOM 2363 CD1 ILE A 307 -22.095 -2.605 -9.891 1.00 84.73 C
ANISOU 2363 CD1 ILE A 307 10905 11204 10086 -117 654 -499 C
ATOM 2364 N PHE A 308 -21.217 0.959 -5.706 1.00 87.07 N
ANISOU 2364 N PHE A 308 11285 11654 10145 -247 715 -291 N
ATOM 2365 CA PHE A 308 -21.196 2.324 -5.193 1.00 78.53 C
ANISOU 2365 CA PHE A 308 10163 10646 9028 -282 709 -275 C
ATOM 2366 C PHE A 308 -20.246 2.469 -4.014 1.00 79.09 C
ANISOU 2366 C PHE A 308 10321 10736 8995 -265 701 -186 C
ATOM 2367 O PHE A 308 -19.700 3.556 -3.793 1.00 75.03 O
ANISOU 2367 O PHE A 308 9770 10309 8427 -259 661 -158 O
ATOM 2368 CB PHE A 308 -22.609 2.761 -4.809 1.00 70.29 C
ANISOU 2368 CB PHE A 308 9098 9554 8055 -383 790 -332 C
ATOM 2369 CG PHE A 308 -23.483 3.074 -5.990 1.00 87.62 C
ANISOU 2369 CG PHE A 308 11181 11766 10346 -399 779 -422 C
ATOM 2370 CD1 PHE A 308 -24.176 2.069 -6.645 1.00 86.97 C
ANISOU 2370 CD1 PHE A 308 11092 11610 10344 -407 804 -481 C
ATOM 2371 CD2 PHE A 308 -23.603 4.374 -6.453 1.00 88.67 C
ANISOU 2371 CD2 PHE A 308 11216 11987 10486 -405 740 -448 C
ATOM 2372 CE1 PHE A 308 -24.976 2.355 -7.735 1.00 72.21 C
ANISOU 2372 CE1 PHE A 308 9119 9758 8560 -418 787 -566 C
ATOM 2373 CE2 PHE A 308 -24.401 4.666 -7.542 1.00 80.76 C
ANISOU 2373 CE2 PHE A 308 10116 11001 9569 -414 725 -530 C
ATOM 2374 CZ PHE A 308 -25.089 3.656 -8.184 1.00 67.50 C
ANISOU 2374 CZ PHE A 308 8428 9250 7968 -419 746 -589 C
ATOM 2375 N LYS A 309 -20.032 1.394 -3.251 1.00 85.46 N
ANISOU 2375 N LYS A 309 11243 11459 9767 -255 736 -142 N
ATOM 2376 CA LYS A 309 -19.036 1.438 -2.185 1.00 85.83 C
ANISOU 2376 CA LYS A 309 11378 11526 9709 -225 717 -56 C
ATOM 2377 C LYS A 309 -17.630 1.556 -2.760 1.00 86.53 C
ANISOU 2377 C LYS A 309 11429 11710 9738 -124 614 -16 C
ATOM 2378 O LYS A 309 -16.794 2.295 -2.226 1.00 84.89 O
ANISOU 2378 O LYS A 309 11222 11578 9454 -104 571 34 O
ATOM 2379 CB LYS A 309 -19.152 0.195 -1.302 1.00 84.19 C
ANISOU 2379 CB LYS A 309 11309 11201 9480 -232 777 -20 C
ATOM 2380 CG LYS A 309 -19.152 0.482 0.192 1.00 85.45 C
ANISOU 2380 CG LYS A 309 11567 11333 9567 -278 825 35 C
ATOM 2381 CD LYS A 309 -20.473 1.088 0.637 1.00 83.62 C
ANISOU 2381 CD LYS A 309 11318 11064 9391 -388 914 -13 C
ATOM 2382 CE LYS A 309 -20.497 1.324 2.138 1.00 91.66 C
ANISOU 2382 CE LYS A 309 12444 12050 10334 -435 968 41 C
ATOM 2383 NZ LYS A 309 -21.800 1.886 2.588 1.00102.90 N
ANISOU 2383 NZ LYS A 309 13850 13435 11812 -541 1062 -9 N
ATOM 2384 N GLU A 310 -17.352 0.834 -3.848 1.00 82.42 N
ANISOU 2384 N GLU A 310 10874 11189 9253 -61 575 -41 N
ATOM 2385 CA GLU A 310 -16.060 0.967 -4.514 1.00 82.11 C
ANISOU 2385 CA GLU A 310 10787 11247 9166 34 482 -11 C
ATOM 2386 C GLU A 310 -15.898 2.352 -5.126 1.00 80.04 C
ANISOU 2386 C GLU A 310 10406 11100 8906 26 435 -33 C
ATOM 2387 O GLU A 310 -14.801 2.922 -5.103 1.00 74.25 O
ANISOU 2387 O GLU A 310 9644 10459 8107 74 371 10 O
ATOM 2388 CB GLU A 310 -15.903 -0.114 -5.583 1.00 80.14 C
ANISOU 2388 CB GLU A 310 10526 10965 8958 100 458 -40 C
ATOM 2389 CG GLU A 310 -15.702 -1.516 -5.032 1.00 77.79 C
ANISOU 2389 CG GLU A 310 10351 10565 8640 133 484 -5 C
ATOM 2390 CD GLU A 310 -14.355 -1.696 -4.357 1.00 85.54 C
ANISOU 2390 CD GLU A 310 11394 11586 9523 209 431 77 C
ATOM 2391 OE1 GLU A 310 -13.464 -0.843 -4.558 1.00 75.90 O
ANISOU 2391 OE1 GLU A 310 10104 10480 8256 248 364 100 O
ATOM 2392 OE2 GLU A 310 -14.187 -2.694 -3.626 1.00 98.17 O
ANISOU 2392 OE2 GLU A 310 13109 13100 11089 230 456 118 O
ATOM 2393 N ALA A 311 -16.977 2.905 -5.685 1.00 79.43 N
ANISOU 2393 N ALA A 311 10258 11017 8904 -34 466 -101 N
ATOM 2394 CA ALA A 311 -16.925 4.272 -6.188 1.00 73.56 C
ANISOU 2394 CA ALA A 311 9413 10374 8163 -48 428 -121 C
ATOM 2395 C ALA A 311 -16.681 5.260 -5.056 1.00 79.80 C
ANISOU 2395 C ALA A 311 10227 11203 8889 -91 436 -76 C
ATOM 2396 O ALA A 311 -15.919 6.221 -5.212 1.00 69.67 O
ANISOU 2396 O ALA A 311 8890 10018 7561 -70 380 -53 O
ATOM 2397 CB ALA A 311 -18.217 4.611 -6.931 1.00 67.77 C
ANISOU 2397 CB ALA A 311 8608 9617 7524 -104 462 -204 C
ATOM 2398 N GLU A 312 -17.315 5.033 -3.902 1.00 79.26 N
ANISOU 2398 N GLU A 312 10244 11057 8816 -152 507 -62 N
ATOM 2399 CA GLU A 312 -17.090 5.898 -2.750 1.00 72.17 C
ANISOU 2399 CA GLU A 312 9381 10188 7852 -192 517 -19 C
ATOM 2400 C GLU A 312 -15.637 5.843 -2.297 1.00 76.09 C
ANISOU 2400 C GLU A 312 9916 10744 8251 -124 451 56 C
ATOM 2401 O GLU A 312 -15.042 6.877 -1.972 1.00 71.54 O
ANISOU 2401 O GLU A 312 9310 10249 7621 -128 413 84 O
ATOM 2402 CB GLU A 312 -18.024 5.501 -1.607 1.00 87.39 C
ANISOU 2402 CB GLU A 312 11403 12012 9788 -265 611 -18 C
ATOM 2403 CG GLU A 312 -17.982 6.436 -0.410 1.00 84.79 C
ANISOU 2403 CG GLU A 312 11112 11706 9397 -316 632 17 C
ATOM 2404 CD GLU A 312 -18.830 5.935 0.742 1.00 83.90 C
ANISOU 2404 CD GLU A 312 11104 11488 9285 -384 728 23 C
ATOM 2405 OE1 GLU A 312 -18.922 4.702 0.920 1.00 86.82 O
ANISOU 2405 OE1 GLU A 312 11554 11774 9661 -368 761 36 O
ATOM 2406 OE2 GLU A 312 -19.410 6.773 1.465 1.00 84.40 O
ANISOU 2406 OE2 GLU A 312 11174 11552 9342 -452 775 14 O
ATOM 2407 N LYS A 313 -15.046 4.644 -2.276 1.00 78.64 N
ANISOU 2407 N LYS A 313 10302 11026 8550 -60 436 89 N
ATOM 2408 CA LYS A 313 -13.640 4.518 -1.907 1.00 72.32 C
ANISOU 2408 CA LYS A 313 9531 10284 7661 14 367 156 C
ATOM 2409 C LYS A 313 -12.738 5.259 -2.885 1.00 75.71 C
ANISOU 2409 C LYS A 313 9849 10835 8081 66 285 152 C
ATOM 2410 O LYS A 313 -11.684 5.773 -2.491 1.00 75.93 O
ANISOU 2410 O LYS A 313 9870 10942 8037 98 230 199 O
ATOM 2411 CB LYS A 313 -13.245 3.040 -1.832 1.00 73.82 C
ANISOU 2411 CB LYS A 313 9806 10403 7838 79 365 184 C
ATOM 2412 CG LYS A 313 -11.770 2.806 -1.530 1.00 74.66 C
ANISOU 2412 CG LYS A 313 9940 10571 7859 168 289 250 C
ATOM 2413 CD LYS A 313 -11.370 1.344 -1.683 1.00 83.65 C
ANISOU 2413 CD LYS A 313 11148 11642 8993 245 280 270 C
ATOM 2414 CE LYS A 313 -11.729 0.527 -0.453 1.00 80.85 C
ANISOU 2414 CE LYS A 313 10940 11176 8605 222 337 308 C
ATOM 2415 NZ LYS A 313 -11.124 -0.834 -0.503 1.00 86.73 N
ANISOU 2415 NZ LYS A 313 11762 11862 9328 309 316 340 N
ATOM 2416 N PHE A 314 -13.140 5.338 -4.157 1.00 74.55 N
ANISOU 2416 N PHE A 314 9615 10706 8004 74 277 95 N
ATOM 2417 CA PHE A 314 -12.329 6.028 -5.155 1.00 70.99 C
ANISOU 2417 CA PHE A 314 9062 10366 7544 120 207 89 C
ATOM 2418 C PHE A 314 -12.196 7.511 -4.829 1.00 74.94 C
ANISOU 2418 C PHE A 314 9512 10947 8014 72 191 97 C
ATOM 2419 O PHE A 314 -11.083 8.045 -4.758 1.00 73.66 O
ANISOU 2419 O PHE A 314 9321 10875 7793 108 132 135 O
ATOM 2420 CB PHE A 314 -12.933 5.831 -6.546 1.00 79.27 C
ANISOU 2420 CB PHE A 314 10038 11408 8673 131 208 22 C
ATOM 2421 CG PHE A 314 -12.387 6.771 -7.582 1.00 74.26 C
ANISOU 2421 CG PHE A 314 9295 10882 8036 157 151 7 C
ATOM 2422 CD1 PHE A 314 -11.137 6.558 -8.141 1.00 71.59 C
ANISOU 2422 CD1 PHE A 314 8924 10617 7658 240 87 35 C
ATOM 2423 CD2 PHE A 314 -13.124 7.868 -7.998 1.00 69.80 C
ANISOU 2423 CD2 PHE A 314 8665 10347 7511 100 162 -36 C
ATOM 2424 CE1 PHE A 314 -10.632 7.423 -9.093 1.00 68.91 C
ANISOU 2424 CE1 PHE A 314 8490 10376 7315 260 41 22 C
ATOM 2425 CE2 PHE A 314 -12.625 8.737 -8.950 1.00 73.40 C
ANISOU 2425 CE2 PHE A 314 9030 10898 7961 123 113 -48 C
ATOM 2426 CZ PHE A 314 -11.377 8.514 -9.498 1.00 69.38 C
ANISOU 2426 CZ PHE A 314 8492 10460 7410 201 54 -18 C
ATOM 2427 N PHE A 315 -13.325 8.195 -4.627 1.00 72.29 N
ANISOU 2427 N PHE A 315 9165 10580 7721 -9 243 58 N
ATOM 2428 CA PHE A 315 -13.272 9.618 -4.302 1.00 72.28 C
ANISOU 2428 CA PHE A 315 9123 10647 7695 -58 232 63 C
ATOM 2429 C PHE A 315 -12.605 9.861 -2.954 1.00 83.02 C
ANISOU 2429 C PHE A 315 10553 12022 8970 -69 225 125 C
ATOM 2430 O PHE A 315 -11.935 10.882 -2.770 1.00 81.87 O
ANISOU 2430 O PHE A 315 10371 11959 8778 -75 184 147 O
ATOM 2431 CB PHE A 315 -14.678 10.217 -4.316 1.00 66.20 C
ANISOU 2431 CB PHE A 315 8331 9831 6990 -139 294 6 C
ATOM 2432 CG PHE A 315 -15.362 10.125 -5.649 1.00 71.53 C
ANISOU 2432 CG PHE A 315 8932 10500 7747 -130 293 -59 C
ATOM 2433 CD1 PHE A 315 -15.049 11.010 -6.667 1.00 78.29 C
ANISOU 2433 CD1 PHE A 315 9695 11441 8611 -111 243 -79 C
ATOM 2434 CD2 PHE A 315 -16.323 9.157 -5.883 1.00 73.73 C
ANISOU 2434 CD2 PHE A 315 9234 10687 8093 -142 343 -102 C
ATOM 2435 CE1 PHE A 315 -15.678 10.927 -7.897 1.00 69.03 C
ANISOU 2435 CE1 PHE A 315 8458 10262 7507 -99 239 -139 C
ATOM 2436 CE2 PHE A 315 -16.954 9.067 -7.109 1.00 81.74 C
ANISOU 2436 CE2 PHE A 315 10179 11698 9182 -133 337 -165 C
ATOM 2437 CZ PHE A 315 -16.633 9.954 -8.117 1.00 76.93 C
ANISOU 2437 CZ PHE A 315 9481 11174 8576 -109 283 -184 C
ATOM 2438 N VAL A 316 -12.773 8.941 -2.002 1.00 82.69 N
ANISOU 2438 N VAL A 316 10616 11898 8905 -72 264 153 N
ATOM 2439 CA VAL A 316 -12.111 9.092 -0.710 1.00 72.07 C
ANISOU 2439 CA VAL A 316 9346 10564 7472 -75 252 213 C
ATOM 2440 C VAL A 316 -10.598 8.986 -0.868 1.00 74.48 C
ANISOU 2440 C VAL A 316 9630 10955 7714 7 166 260 C
ATOM 2441 O VAL A 316 -9.844 9.679 -0.172 1.00 82.53 O
ANISOU 2441 O VAL A 316 10656 12037 8666 4 128 298 O
ATOM 2442 CB VAL A 316 -12.658 8.057 0.292 1.00 69.47 C
ANISOU 2442 CB VAL A 316 9141 10122 7132 -93 316 233 C
ATOM 2443 CG1 VAL A 316 -11.801 8.013 1.548 1.00 64.12 C
ANISOU 2443 CG1 VAL A 316 8552 9458 6355 -76 290 301 C
ATOM 2444 CG2 VAL A 316 -14.098 8.386 0.656 1.00 73.28 C
ANISOU 2444 CG2 VAL A 316 9641 10533 7668 -187 405 189 C
ATOM 2445 N SER A 317 -10.127 8.150 -1.797 1.00 69.15 N
ANISOU 2445 N SER A 317 8924 10287 7062 81 132 255 N
ATOM 2446 CA SER A 317 -8.690 7.972 -1.981 1.00 77.23 C
ANISOU 2446 CA SER A 317 9923 11391 8030 165 53 296 C
ATOM 2447 C SER A 317 -7.998 9.246 -2.450 1.00 79.21 C
ANISOU 2447 C SER A 317 10072 11763 8263 159 -1 293 C
ATOM 2448 O SER A 317 -6.782 9.374 -2.275 1.00 81.72 O
ANISOU 2448 O SER A 317 10371 12157 8523 209 -64 332 O
ATOM 2449 CB SER A 317 -8.417 6.840 -2.974 1.00 85.27 C
ANISOU 2449 CB SER A 317 10924 12390 9083 244 35 283 C
ATOM 2450 OG SER A 317 -8.883 7.167 -4.271 1.00 70.79 O
ANISOU 2450 OG SER A 317 8999 10580 7319 237 38 227 O
ATOM 2451 N VAL A 318 -8.735 10.189 -3.037 1.00 76.31 N
ANISOU 2451 N VAL A 318 9637 11412 7944 101 23 248 N
ATOM 2452 CA VAL A 318 -8.149 11.436 -3.512 1.00 77.41 C
ANISOU 2452 CA VAL A 318 9685 11658 8069 90 -22 244 C
ATOM 2453 C VAL A 318 -8.439 12.598 -2.568 1.00 79.17 C
ANISOU 2453 C VAL A 318 9926 11894 8261 11 -4 252 C
ATOM 2454 O VAL A 318 -8.142 13.750 -2.899 1.00 82.62 O
ANISOU 2454 O VAL A 318 10294 12407 8691 -15 -31 244 O
ATOM 2455 CB VAL A 318 -8.614 11.761 -4.942 1.00 84.17 C
ANISOU 2455 CB VAL A 318 10452 12535 8993 90 -19 191 C
ATOM 2456 CG1 VAL A 318 -8.369 10.573 -5.860 1.00 70.38 C
ANISOU 2456 CG1 VAL A 318 8695 10771 7277 168 -33 179 C
ATOM 2457 CG2 VAL A 318 -10.080 12.165 -4.958 1.00 73.54 C
ANISOU 2457 CG2 VAL A 318 9112 11122 7708 15 45 142 C
ATOM 2458 N GLY A 319 -9.007 12.323 -1.397 1.00 74.53 N
ANISOU 2458 N GLY A 319 9433 11233 7653 -29 42 267 N
ATOM 2459 CA GLY A 319 -9.266 13.350 -0.411 1.00 64.81 C
ANISOU 2459 CA GLY A 319 8229 10009 6386 -101 60 276 C
ATOM 2460 C GLY A 319 -10.664 13.927 -0.407 1.00 70.50 C
ANISOU 2460 C GLY A 319 8948 10673 7164 -180 131 227 C
ATOM 2461 O GLY A 319 -10.891 14.942 0.263 1.00 73.35 O
ANISOU 2461 O GLY A 319 9318 11050 7502 -240 145 227 O
ATOM 2462 N LEU A 320 -11.613 13.318 -1.137 1.00 74.31 N
ANISOU 2462 N LEU A 320 9418 11093 7725 -181 174 183 N
ATOM 2463 CA LEU A 320 -12.981 13.811 -1.153 1.00 69.59 C
ANISOU 2463 CA LEU A 320 8812 10442 7188 -253 240 132 C
ATOM 2464 C LEU A 320 -13.809 13.127 -0.068 1.00 77.26 C
ANISOU 2464 C LEU A 320 9885 11310 8159 -294 315 136 C
ATOM 2465 O LEU A 320 -13.500 12.002 0.339 1.00 80.80 O
ANISOU 2465 O LEU A 320 10405 11712 8582 -257 320 168 O
ATOM 2466 CB LEU A 320 -13.617 13.569 -2.520 1.00 78.35 C
ANISOU 2466 CB LEU A 320 9848 11539 8383 -236 246 76 C
ATOM 2467 CG LEU A 320 -13.051 14.397 -3.674 1.00 72.28 C
ANISOU 2467 CG LEU A 320 8977 10863 7622 -209 186 62 C
ATOM 2468 CD1 LEU A 320 -13.800 14.096 -4.960 1.00 69.18 C
ANISOU 2468 CD1 LEU A 320 8525 10448 7311 -194 196 3 C
ATOM 2469 CD2 LEU A 320 -13.112 15.881 -3.346 1.00 70.43 C
ANISOU 2469 CD2 LEU A 320 8714 10679 7368 -264 182 59 C
ATOM 2470 N PRO A 321 -14.864 13.780 0.417 1.00 80.02 N
ANISOU 2470 N PRO A 321 10246 11622 8537 -369 377 104 N
ATOM 2471 CA PRO A 321 -15.655 13.193 1.503 1.00 80.64 C
ANISOU 2471 CA PRO A 321 10423 11604 8612 -415 456 108 C
ATOM 2472 C PRO A 321 -16.443 11.979 1.039 1.00 79.01 C
ANISOU 2472 C PRO A 321 10234 11311 8476 -407 505 76 C
ATOM 2473 O PRO A 321 -16.738 11.801 -0.145 1.00 77.70 O
ANISOU 2473 O PRO A 321 9993 11152 8379 -385 491 33 O
ATOM 2474 CB PRO A 321 -16.593 14.333 1.914 1.00 75.18 C
ANISOU 2474 CB PRO A 321 9716 10907 7944 -495 506 71 C
ATOM 2475 CG PRO A 321 -16.723 15.160 0.682 1.00 65.33 C
ANISOU 2475 CG PRO A 321 8352 9719 6752 -488 469 27 C
ATOM 2476 CD PRO A 321 -15.371 15.107 0.028 1.00 73.89 C
ANISOU 2476 CD PRO A 321 9395 10886 7793 -416 379 63 C
ATOM 2477 N ASN A 322 -16.776 11.129 2.007 1.00 78.73 N
ANISOU 2477 N ASN A 322 10304 11191 8420 -427 563 99 N
ATOM 2478 CA ASN A 322 -17.624 9.981 1.736 1.00 76.53 C
ANISOU 2478 CA ASN A 322 10054 10816 8208 -434 623 68 C
ATOM 2479 C ASN A 322 -19.074 10.426 1.556 1.00 74.87 C
ANISOU 2479 C ASN A 322 9800 10561 8085 -510 697 -3 C
ATOM 2480 O ASN A 322 -19.456 11.553 1.882 1.00 80.39 O
ANISOU 2480 O ASN A 322 10470 11291 8782 -559 713 -21 O
ATOM 2481 CB ASN A 322 -17.512 8.953 2.862 1.00 83.72 C
ANISOU 2481 CB ASN A 322 11100 11646 9065 -434 666 117 C
ATOM 2482 CG ASN A 322 -17.361 9.594 4.231 1.00106.93 C
ANISOU 2482 CG ASN A 322 14114 14590 11922 -476 688 158 C
ATOM 2483 OD1 ASN A 322 -17.471 10.811 4.380 1.00118.48 O
ANISOU 2483 OD1 ASN A 322 15531 16109 13378 -514 681 143 O
ATOM 2484 ND2 ASN A 322 -17.106 8.768 5.242 1.00115.43 N
ANISOU 2484 ND2 ASN A 322 15315 15606 12936 -468 714 209 N
ATOM 2485 N MET A 323 -19.885 9.522 1.015 1.00 72.90 N
ANISOU 2485 N MET A 323 9545 10240 7915 -517 742 -47 N
ATOM 2486 CA MET A 323 -21.294 9.816 0.811 1.00 76.60 C
ANISOU 2486 CA MET A 323 9968 10664 8475 -586 812 -120 C
ATOM 2487 C MET A 323 -22.005 9.972 2.150 1.00 80.29 C
ANISOU 2487 C MET A 323 10516 11070 8923 -663 904 -114 C
ATOM 2488 O MET A 323 -21.651 9.334 3.145 1.00 86.24 O
ANISOU 2488 O MET A 323 11381 11777 9611 -664 932 -60 O
ATOM 2489 CB MET A 323 -21.958 8.712 -0.011 1.00 71.26 C
ANISOU 2489 CB MET A 323 9272 9920 7885 -578 839 -168 C
ATOM 2490 CG MET A 323 -21.415 8.555 -1.426 1.00 74.90 C
ANISOU 2490 CG MET A 323 9649 10437 8373 -506 757 -186 C
ATOM 2491 SD MET A 323 -21.762 9.962 -2.502 1.00 89.02 S
ANISOU 2491 SD MET A 323 11298 12314 10213 -511 710 -245 S
ATOM 2492 CE MET A 323 -20.188 10.818 -2.484 1.00 66.73 C
ANISOU 2492 CE MET A 323 8462 9605 7285 -453 615 -176 C
ATOM 2493 N THR A 324 -23.016 10.836 2.167 1.00 83.02 N
ANISOU 2493 N THR A 324 10806 11414 9323 -725 950 -170 N
ATOM 2494 CA THR A 324 -23.777 11.072 3.383 1.00 81.69 C
ANISOU 2494 CA THR A 324 10704 11191 9143 -802 1043 -172 C
ATOM 2495 C THR A 324 -24.568 9.826 3.773 1.00 84.90 C
ANISOU 2495 C THR A 324 11182 11485 9592 -839 1134 -186 C
ATOM 2496 O THR A 324 -24.818 8.934 2.957 1.00 83.18 O
ANISOU 2496 O THR A 324 10937 11229 9437 -818 1132 -216 O
ATOM 2497 CB THR A 324 -24.730 12.255 3.203 1.00 73.74 C
ANISOU 2497 CB THR A 324 9612 10208 8196 -855 1071 -237 C
ATOM 2498 OG1 THR A 324 -25.764 11.902 2.276 1.00 66.71 O
ANISOU 2498 OG1 THR A 324 8643 9283 7422 -870 1100 -314 O
ATOM 2499 CG2 THR A 324 -23.978 13.467 2.675 1.00 64.78 C
ANISOU 2499 CG2 THR A 324 8405 9181 7029 -817 980 -227 C
ATOM 2500 N GLN A 325 -24.957 9.769 5.049 1.00 83.16 N
ANISOU 2500 N GLN A 325 11058 11208 9332 -897 1218 -165 N
ATOM 2501 CA GLN A 325 -25.798 8.668 5.507 1.00 85.87 C
ANISOU 2501 CA GLN A 325 11473 11439 9716 -945 1319 -180 C
ATOM 2502 C GLN A 325 -27.144 8.677 4.794 1.00 87.20 C
ANISOU 2502 C GLN A 325 11545 11573 10014 -996 1376 -275 C
ATOM 2503 O GLN A 325 -27.696 7.617 4.476 1.00 83.79 O
ANISOU 2503 O GLN A 325 11125 11065 9646 -1011 1421 -304 O
ATOM 2504 CB GLN A 325 -25.996 8.746 7.020 1.00 90.14 C
ANISOU 2504 CB GLN A 325 12134 11931 10186 -1002 1402 -142 C
ATOM 2505 CG GLN A 325 -26.805 7.593 7.592 1.00 84.59 C
ANISOU 2505 CG GLN A 325 11520 11107 9514 -1056 1514 -150 C
ATOM 2506 CD GLN A 325 -27.236 7.832 9.025 1.00108.16 C
ANISOU 2506 CD GLN A 325 14608 14044 12442 -1124 1611 -127 C
ATOM 2507 OE1 GLN A 325 -27.146 8.949 9.536 1.00116.95 O
ANISOU 2507 OE1 GLN A 325 15710 15213 13511 -1142 1603 -122 O
ATOM 2508 NE2 GLN A 325 -27.710 6.780 9.683 1.00109.79 N
ANISOU 2508 NE2 GLN A 325 14921 14145 12648 -1166 1705 -114 N
ATOM 2509 N GLY A 326 -27.686 9.868 4.531 1.00 88.91 N
ANISOU 2509 N GLY A 326 11666 11842 10271 -1023 1372 -326 N
ATOM 2510 CA GLY A 326 -28.925 9.970 3.784 1.00 85.70 C
ANISOU 2510 CA GLY A 326 11157 11416 9990 -1063 1412 -420 C
ATOM 2511 C GLY A 326 -28.802 9.508 2.348 1.00 86.40 C
ANISOU 2511 C GLY A 326 11160 11526 10144 -1007 1340 -455 C
ATOM 2512 O GLY A 326 -29.808 9.138 1.733 1.00 87.93 O
ANISOU 2512 O GLY A 326 11288 11678 10442 -1037 1377 -530 O
ATOM 2513 N PHE A 327 -27.587 9.521 1.796 1.00 81.35 N
ANISOU 2513 N PHE A 327 10516 10950 9444 -928 1237 -406 N
ATOM 2514 CA PHE A 327 -27.382 9.008 0.446 1.00 82.66 C
ANISOU 2514 CA PHE A 327 10611 11135 9661 -870 1169 -434 C
ATOM 2515 C PHE A 327 -27.677 7.515 0.383 1.00 83.11 C
ANISOU 2515 C PHE A 327 10724 11097 9757 -876 1216 -442 C
ATOM 2516 O PHE A 327 -28.432 7.054 -0.480 1.00 86.41 O
ANISOU 2516 O PHE A 327 11076 11484 10271 -885 1226 -511 O
ATOM 2517 CB PHE A 327 -25.952 9.299 -0.012 1.00 79.30 C
ANISOU 2517 CB PHE A 327 10179 10797 9155 -785 1058 -374 C
ATOM 2518 CG PHE A 327 -25.582 8.633 -1.303 1.00 83.13 C
ANISOU 2518 CG PHE A 327 10613 11298 9677 -719 990 -392 C
ATOM 2519 CD1 PHE A 327 -25.907 9.216 -2.516 1.00 89.98 C
ANISOU 2519 CD1 PHE A 327 11363 12218 10608 -699 940 -452 C
ATOM 2520 CD2 PHE A 327 -24.904 7.423 -1.306 1.00 75.71 C
ANISOU 2520 CD2 PHE A 327 9744 10318 8704 -674 977 -349 C
ATOM 2521 CE1 PHE A 327 -25.566 8.604 -3.708 1.00 87.48 C
ANISOU 2521 CE1 PHE A 327 11003 11916 10320 -637 879 -470 C
ATOM 2522 CE2 PHE A 327 -24.562 6.807 -2.493 1.00 81.68 C
ANISOU 2522 CE2 PHE A 327 10454 11087 9492 -612 917 -368 C
ATOM 2523 CZ PHE A 327 -24.893 7.399 -3.696 1.00 85.71 C
ANISOU 2523 CZ PHE A 327 10849 11653 10064 -594 869 -429 C
ATOM 2524 N TRP A 328 -27.089 6.739 1.298 1.00 83.04 N
ANISOU 2524 N TRP A 328 10840 11039 9673 -870 1243 -372 N
ATOM 2525 CA TRP A 328 -27.305 5.296 1.286 1.00 79.96 C
ANISOU 2525 CA TRP A 328 10516 10551 9312 -874 1288 -372 C
ATOM 2526 C TRP A 328 -28.731 4.933 1.683 1.00 86.21 C
ANISOU 2526 C TRP A 328 11314 11251 10191 -969 1407 -435 C
ATOM 2527 O TRP A 328 -29.230 3.873 1.288 1.00 88.16 O
ANISOU 2527 O TRP A 328 11570 11423 10503 -983 1443 -470 O
ATOM 2528 CB TRP A 328 -26.305 4.604 2.214 1.00 74.04 C
ANISOU 2528 CB TRP A 328 9906 9770 8454 -841 1286 -278 C
ATOM 2529 CG TRP A 328 -24.876 4.824 1.827 1.00 72.99 C
ANISOU 2529 CG TRP A 328 9767 9724 8240 -746 1171 -219 C
ATOM 2530 CD1 TRP A 328 -23.972 5.633 2.451 1.00 76.23 C
ANISOU 2530 CD1 TRP A 328 10204 10206 8554 -721 1124 -158 C
ATOM 2531 CD2 TRP A 328 -24.186 4.229 0.722 1.00 79.53 C
ANISOU 2531 CD2 TRP A 328 10558 10580 9081 -666 1090 -218 C
ATOM 2532 NE1 TRP A 328 -22.760 5.576 1.805 1.00 72.52 N
ANISOU 2532 NE1 TRP A 328 9710 9806 8037 -631 1020 -120 N
ATOM 2533 CE2 TRP A 328 -22.866 4.722 0.739 1.00 83.17 C
ANISOU 2533 CE2 TRP A 328 11020 11130 9450 -594 999 -155 C
ATOM 2534 CE3 TRP A 328 -24.557 3.328 -0.281 1.00 87.08 C
ANISOU 2534 CE3 TRP A 328 11478 11492 10116 -647 1087 -267 C
ATOM 2535 CZ2 TRP A 328 -21.916 4.343 -0.206 1.00 85.34 C
ANISOU 2535 CZ2 TRP A 328 11261 11454 9712 -506 909 -139 C
ATOM 2536 CZ3 TRP A 328 -23.612 2.953 -1.218 1.00 85.67 C
ANISOU 2536 CZ3 TRP A 328 11270 11359 9920 -557 996 -251 C
ATOM 2537 CH2 TRP A 328 -22.307 3.460 -1.175 1.00 87.23 C
ANISOU 2537 CH2 TRP A 328 11469 11648 10027 -487 910 -187 C
ATOM 2538 N GLU A 329 -29.401 5.792 2.451 1.00 82.90 N
ANISOU 2538 N GLU A 329 10887 10836 9775 -1035 1471 -453 N
ATOM 2539 CA GLU A 329 -30.743 5.491 2.932 1.00 80.74 C
ANISOU 2539 CA GLU A 329 10619 10478 9580 -1129 1592 -511 C
ATOM 2540 C GLU A 329 -31.839 5.919 1.966 1.00 85.16 C
ANISOU 2540 C GLU A 329 11035 11056 10266 -1158 1596 -616 C
ATOM 2541 O GLU A 329 -32.884 5.261 1.900 1.00 92.76 O
ANISOU 2541 O GLU A 329 11982 11942 11320 -1219 1676 -678 O
ATOM 2542 CB GLU A 329 -30.982 6.161 4.289 1.00 91.71 C
ANISOU 2542 CB GLU A 329 12075 11858 10912 -1189 1668 -483 C
ATOM 2543 CG GLU A 329 -30.129 5.614 5.421 1.00101.57 C
ANISOU 2543 CG GLU A 329 13482 13068 12041 -1176 1687 -386 C
ATOM 2544 CD GLU A 329 -30.348 6.361 6.723 1.00101.17 C
ANISOU 2544 CD GLU A 329 13496 13016 11929 -1232 1756 -360 C
ATOM 2545 OE1 GLU A 329 -30.960 7.450 6.688 1.00 95.89 O
ANISOU 2545 OE1 GLU A 329 12741 12393 11298 -1267 1771 -411 O
ATOM 2546 OE2 GLU A 329 -29.911 5.860 7.781 1.00106.97 O
ANISOU 2546 OE2 GLU A 329 14369 13701 12573 -1239 1796 -290 O
ATOM 2547 N ASN A 330 -31.631 7.001 1.215 1.00 88.87 N
ANISOU 2547 N ASN A 330 11401 11623 10744 -1117 1512 -639 N
ATOM 2548 CA ASN A 330 -32.684 7.560 0.376 1.00 86.52 C
ANISOU 2548 CA ASN A 330 10968 11347 10558 -1141 1511 -738 C
ATOM 2549 C ASN A 330 -32.530 7.239 -1.104 1.00 83.21 C
ANISOU 2549 C ASN A 330 10463 10960 10194 -1080 1422 -779 C
ATOM 2550 O ASN A 330 -33.526 7.290 -1.834 1.00 76.37 O
ANISOU 2550 O ASN A 330 9497 10085 9434 -1104 1431 -868 O
ATOM 2551 CB ASN A 330 -32.747 9.082 0.552 1.00 85.70 C
ANISOU 2551 CB ASN A 330 10805 11324 10434 -1144 1487 -746 C
ATOM 2552 CG ASN A 330 -33.061 9.491 1.976 1.00 86.34 C
ANISOU 2552 CG ASN A 330 10961 11374 10470 -1210 1581 -720 C
ATOM 2553 OD1 ASN A 330 -33.882 8.865 2.647 1.00 87.95 O
ANISOU 2553 OD1 ASN A 330 11209 11495 10714 -1281 1689 -744 O
ATOM 2554 ND2 ASN A 330 -32.405 10.544 2.447 1.00 90.52 N
ANISOU 2554 ND2 ASN A 330 11507 11970 10915 -1190 1542 -673 N
ATOM 2555 N SER A 331 -31.325 6.917 -1.567 1.00 86.80 N
ANISOU 2555 N SER A 331 10949 11451 10580 -1000 1334 -719 N
ATOM 2556 CA SER A 331 -31.128 6.634 -2.981 1.00 86.05 C
ANISOU 2556 CA SER A 331 10776 11390 10530 -938 1249 -756 C
ATOM 2557 C SER A 331 -31.774 5.305 -3.364 1.00 85.98 C
ANISOU 2557 C SER A 331 10777 11291 10601 -962 1294 -805 C
ATOM 2558 O SER A 331 -32.080 4.460 -2.519 1.00 99.57 O
ANISOU 2558 O SER A 331 12586 12922 12324 -1014 1382 -789 O
ATOM 2559 CB SER A 331 -29.639 6.598 -3.327 1.00 71.62 C
ANISOU 2559 CB SER A 331 8982 9624 8605 -847 1152 -679 C
ATOM 2560 OG SER A 331 -29.006 7.824 -3.011 1.00 75.88 O
ANISOU 2560 OG SER A 331 9511 10248 9072 -828 1108 -636 O
ATOM 2561 N MET A 332 -31.982 5.132 -4.666 1.00 79.84 N
ANISOU 2561 N MET A 332 9910 10535 9889 -924 1232 -866 N
ATOM 2562 CA MET A 332 -32.492 3.888 -5.238 1.00 86.34 C
ANISOU 2562 CA MET A 332 10733 11282 10789 -936 1254 -917 C
ATOM 2563 C MET A 332 -31.396 3.344 -6.150 1.00 85.85 C
ANISOU 2563 C MET A 332 10684 11252 10682 -842 1159 -882 C
ATOM 2564 O MET A 332 -31.331 3.685 -7.333 1.00 78.52 O
ANISOU 2564 O MET A 332 9667 10384 9782 -791 1078 -924 O
ATOM 2565 CB MET A 332 -33.800 4.111 -5.993 1.00 87.90 C
ANISOU 2565 CB MET A 332 10811 11474 11112 -977 1268 -1031 C
ATOM 2566 CG MET A 332 -34.570 2.830 -6.276 1.00 90.55 C
ANISOU 2566 CG MET A 332 11154 11713 11538 -1019 1321 -1092 C
ATOM 2567 SD MET A 332 -36.003 3.087 -7.337 1.00111.71 S
ANISOU 2567 SD MET A 332 13680 14400 14366 -1054 1313 -1232 S
ATOM 2568 CE MET A 332 -35.205 3.404 -8.907 1.00 91.71 C
ANISOU 2568 CE MET A 332 11077 11961 11809 -940 1163 -1240 C
ATOM 2569 N LEU A 333 -30.532 2.502 -5.591 1.00 84.38 N
ANISOU 2569 N LEU A 333 10612 11025 10423 -815 1168 -805 N
ATOM 2570 CA LEU A 333 -29.397 1.956 -6.324 1.00 84.36 C
ANISOU 2570 CA LEU A 333 10632 11052 10370 -722 1082 -764 C
ATOM 2571 C LEU A 333 -29.714 0.640 -7.023 1.00 86.30 C
ANISOU 2571 C LEU A 333 10889 11220 10680 -715 1090 -810 C
ATOM 2572 O LEU A 333 -28.820 0.057 -7.642 1.00 82.87 O
ANISOU 2572 O LEU A 333 10478 10800 10207 -637 1026 -781 O
ATOM 2573 CB LEU A 333 -28.205 1.766 -5.380 1.00 78.28 C
ANISOU 2573 CB LEU A 333 9977 10285 9481 -686 1077 -656 C
ATOM 2574 CG LEU A 333 -27.748 3.002 -4.602 1.00 67.73 C
ANISOU 2574 CG LEU A 333 8644 9023 8069 -690 1065 -603 C
ATOM 2575 CD1 LEU A 333 -26.487 2.698 -3.806 1.00 77.83 C
ANISOU 2575 CD1 LEU A 333 10031 10307 9231 -643 1045 -500 C
ATOM 2576 CD2 LEU A 333 -27.528 4.186 -5.532 1.00 67.10 C
ANISOU 2576 CD2 LEU A 333 8450 9054 7992 -649 980 -628 C
ATOM 2577 N THR A 334 -30.952 0.158 -6.938 1.00 87.21 N
ANISOU 2577 N THR A 334 10988 11255 10892 -794 1168 -883 N
ATOM 2578 CA THR A 334 -31.365 -1.053 -7.631 1.00 81.69 C
ANISOU 2578 CA THR A 334 10293 10480 10266 -797 1178 -938 C
ATOM 2579 C THR A 334 -32.739 -0.837 -8.246 1.00 93.08 C
ANISOU 2579 C THR A 334 11624 11911 11833 -858 1202 -1052 C
ATOM 2580 O THR A 334 -33.486 0.064 -7.853 1.00 93.81 O
ANISOU 2580 O THR A 334 11659 12028 11958 -914 1240 -1084 O
ATOM 2581 CB THR A 334 -31.410 -2.273 -6.698 1.00 78.85 C
ANISOU 2581 CB THR A 334 10065 10001 9895 -839 1267 -900 C
ATOM 2582 OG1 THR A 334 -32.134 -1.944 -5.505 1.00107.74 O
ANISOU 2582 OG1 THR A 334 13756 13617 13562 -931 1369 -895 O
ATOM 2583 CG2 THR A 334 -30.009 -2.730 -6.333 1.00 67.60 C
ANISOU 2583 CG2 THR A 334 8748 8580 8355 -761 1226 -796 C
ATOM 2584 N ASP A 335 -33.061 -1.676 -9.219 1.00 93.54 N
ANISOU 2584 N ASP A 335 11650 11931 11958 -844 1179 -1116 N
ATOM 2585 CA ASP A 335 -34.390 -1.656 -9.814 1.00102.93 C
ANISOU 2585 CA ASP A 335 12737 13098 13272 -904 1202 -1232 C
ATOM 2586 C ASP A 335 -35.415 -2.091 -8.771 1.00101.11 C
ANISOU 2586 C ASP A 335 12545 12770 13102 -1016 1331 -1257 C
ATOM 2587 O ASP A 335 -35.240 -3.142 -8.142 1.00 91.71 O
ANISOU 2587 O ASP A 335 11466 11486 11894 -1042 1394 -1218 O
ATOM 2588 CB ASP A 335 -34.435 -2.581 -11.031 1.00105.88 C
ANISOU 2588 CB ASP A 335 13084 13446 13699 -864 1148 -1291 C
ATOM 2589 CG ASP A 335 -35.652 -2.344 -11.912 1.00107.56 C
ANISOU 2589 CG ASP A 335 13169 13668 14031 -901 1135 -1414 C
ATOM 2590 OD1 ASP A 335 -36.777 -2.228 -11.381 1.00112.31 O
ANISOU 2590 OD1 ASP A 335 13734 14226 14711 -993 1217 -1470 O
ATOM 2591 OD2 ASP A 335 -35.480 -2.278 -13.147 1.00108.80 O
ANISOU 2591 OD2 ASP A 335 13260 13877 14203 -836 1042 -1456 O
ATOM 2592 N PRO A 336 -36.478 -1.314 -8.544 1.00107.98 N
ANISOU 2592 N PRO A 336 13330 13656 14042 -1084 1376 -1320 N
ATOM 2593 CA PRO A 336 -37.502 -1.748 -7.578 1.00110.73 C
ANISOU 2593 CA PRO A 336 13709 13910 14453 -1196 1507 -1352 C
ATOM 2594 C PRO A 336 -38.159 -3.061 -7.958 1.00111.14 C
ANISOU 2594 C PRO A 336 13772 13860 14596 -1243 1551 -1418 C
ATOM 2595 O PRO A 336 -38.559 -3.826 -7.070 1.00124.20 O
ANISOU 2595 O PRO A 336 15510 15414 16268 -1320 1661 -1407 O
ATOM 2596 CB PRO A 336 -38.508 -0.587 -7.583 1.00113.08 C
ANISOU 2596 CB PRO A 336 13883 14262 14818 -1242 1522 -1424 C
ATOM 2597 CG PRO A 336 -38.251 0.147 -8.866 1.00108.42 C
ANISOU 2597 CG PRO A 336 13186 13774 14233 -1159 1394 -1459 C
ATOM 2598 CD PRO A 336 -36.783 0.007 -9.118 1.00102.83 C
ANISOU 2598 CD PRO A 336 12554 13107 13411 -1062 1312 -1365 C
ATOM 2599 N GLY A 337 -38.287 -3.340 -9.253 1.00109.00 N
ANISOU 2599 N GLY A 337 13424 13610 14382 -1200 1471 -1487 N
ATOM 2600 CA GLY A 337 -38.779 -4.618 -9.722 1.00110.94 C
ANISOU 2600 CA GLY A 337 13684 13762 14708 -1233 1499 -1548 C
ATOM 2601 C GLY A 337 -40.239 -4.900 -9.431 1.00125.69 C
ANISOU 2601 C GLY A 337 15496 15559 16702 -1351 1600 -1646 C
ATOM 2602 O GLY A 337 -40.880 -4.207 -8.628 1.00130.78 O
ANISOU 2602 O GLY A 337 16111 16212 17368 -1417 1672 -1655 O
ATOM 2603 N ASN A 338 -40.773 -5.924 -10.100 1.00130.29 N
ANISOU 2603 N ASN A 338 16060 16072 17371 -1379 1606 -1722 N
ATOM 2604 CA ASN A 338 -42.127 -6.428 -9.859 1.00140.65 C
ANISOU 2604 CA ASN A 338 17328 17301 18811 -1497 1708 -1818 C
ATOM 2605 C ASN A 338 -43.128 -5.306 -10.120 1.00134.89 C
ANISOU 2605 C ASN A 338 16441 16647 18162 -1528 1697 -1907 C
ATOM 2606 O ASN A 338 -43.114 -4.741 -11.230 1.00126.43 O
ANISOU 2606 O ASN A 338 15266 15661 17110 -1461 1585 -1958 O
ATOM 2607 CB ASN A 338 -42.146 -7.060 -8.462 1.00147.11 C
ANISOU 2607 CB ASN A 338 18281 18015 19598 -1576 1844 -1752 C
ATOM 2608 CG ASN A 338 -41.458 -8.431 -8.433 1.00157.76 C
ANISOU 2608 CG ASN A 338 19770 19266 20905 -1557 1857 -1699 C
ATOM 2609 OD1 ASN A 338 -42.001 -9.415 -8.942 1.00162.45 O
ANISOU 2609 OD1 ASN A 338 20357 19782 21585 -1597 1878 -1771 O
ATOM 2610 ND2 ASN A 338 -40.293 -8.508 -7.799 1.00161.10 N
ANISOU 2610 ND2 ASN A 338 20322 19688 21200 -1497 1848 -1577 N
ATOM 2611 N VAL A 339 -43.988 -4.933 -9.166 1.00139.67 N
ANISOU 2611 N VAL A 339 17026 17228 18814 -1623 1806 -1929 N
ATOM 2612 CA VAL A 339 -45.074 -3.985 -9.445 1.00137.93 C
ANISOU 2612 CA VAL A 339 16649 17069 18689 -1658 1802 -2029 C
ATOM 2613 C VAL A 339 -44.537 -2.561 -9.552 1.00134.67 C
ANISOU 2613 C VAL A 339 16190 16779 18201 -1578 1719 -1985 C
ATOM 2614 O VAL A 339 -44.809 -1.843 -10.524 1.00127.65 O
ANISOU 2614 O VAL A 339 15180 15971 17350 -1528 1623 -2049 O
ATOM 2615 CB VAL A 339 -46.170 -4.086 -8.367 1.00134.69 C
ANISOU 2615 CB VAL A 339 16231 16589 18354 -1787 1954 -2069 C
ATOM 2616 CG1 VAL A 339 -47.298 -3.098 -8.631 1.00140.44 C
ANISOU 2616 CG1 VAL A 339 16794 17382 19184 -1819 1951 -2174 C
ATOM 2617 CG2 VAL A 339 -46.679 -5.511 -8.285 1.00119.74 C
ANISOU 2617 CG2 VAL A 339 14389 14571 16537 -1870 2039 -2112 C
ATOM 2618 N GLN A 340 -43.774 -2.136 -8.548 1.00132.35 N
ANISOU 2618 N GLN A 340 15995 16497 17796 -1565 1753 -1875 N
ATOM 2619 CA GLN A 340 -43.248 -0.780 -8.489 1.00130.00 C
ANISOU 2619 CA GLN A 340 15666 16306 17422 -1500 1687 -1827 C
ATOM 2620 C GLN A 340 -42.342 -0.485 -9.676 1.00122.41 C
ANISOU 2620 C GLN A 340 14678 15428 16406 -1382 1539 -1807 C
ATOM 2621 O GLN A 340 -41.256 -1.062 -9.799 1.00119.16 O
ANISOU 2621 O GLN A 340 14362 15005 15908 -1322 1498 -1729 O
ATOM 2622 CB GLN A 340 -42.492 -0.559 -7.178 1.00126.92 C
ANISOU 2622 CB GLN A 340 15404 15903 16916 -1509 1750 -1708 C
ATOM 2623 CG GLN A 340 -41.990 0.862 -6.995 1.00121.84 C
ANISOU 2623 CG GLN A 340 14734 15365 16196 -1454 1694 -1659 C
ATOM 2624 CD GLN A 340 -41.264 1.064 -5.683 1.00128.06 C
ANISOU 2624 CD GLN A 340 15648 16139 16870 -1465 1755 -1547 C
ATOM 2625 OE1 GLN A 340 -40.987 0.109 -4.958 1.00147.98 O
ANISOU 2625 OE1 GLN A 340 18292 18578 19358 -1499 1827 -1494 O
ATOM 2626 NE2 GLN A 340 -40.953 2.314 -5.369 1.00132.61 N
ANISOU 2626 NE2 GLN A 340 16202 16797 17386 -1434 1724 -1511 N
ATOM 2627 N LYS A 341 -42.783 0.411 -10.552 1.00111.14 N
ANISOU 2627 N LYS A 341 13121 14082 15025 -1345 1459 -1877 N
ATOM 2628 CA LYS A 341 -42.031 0.800 -11.734 1.00107.42 C
ANISOU 2628 CA LYS A 341 12614 13694 14507 -1236 1320 -1867 C
ATOM 2629 C LYS A 341 -41.284 2.103 -11.480 1.00108.40 C
ANISOU 2629 C LYS A 341 12744 13913 14532 -1178 1270 -1792 C
ATOM 2630 O LYS A 341 -41.631 2.885 -10.591 1.00118.20 O
ANISOU 2630 O LYS A 341 13976 15166 15767 -1221 1330 -1778 O
ATOM 2631 CB LYS A 341 -42.962 0.948 -12.939 1.00102.03 C
ANISOU 2631 CB LYS A 341 11792 13041 13934 -1227 1254 -1992 C
ATOM 2632 CG LYS A 341 -43.719 -0.322 -13.282 1.00119.74 C
ANISOU 2632 CG LYS A 341 14021 15194 16280 -1286 1295 -2077 C
ATOM 2633 CD LYS A 341 -44.610 -0.131 -14.495 1.00122.06 C
ANISOU 2633 CD LYS A 341 14175 15525 16678 -1271 1219 -2203 C
ATOM 2634 CE LYS A 341 -45.317 -1.423 -14.867 1.00106.01 C
ANISOU 2634 CE LYS A 341 12129 13403 14748 -1330 1255 -2289 C
ATOM 2635 NZ LYS A 341 -46.174 -1.258 -16.072 1.00106.75 N
ANISOU 2635 NZ LYS A 341 12084 13534 14941 -1313 1173 -2415 N
ATOM 2636 N ALA A 342 -40.243 2.328 -12.278 1.00 95.63 N
ANISOU 2636 N ALA A 342 11139 12360 12836 -1079 1161 -1744 N
ATOM 2637 CA ALA A 342 -39.383 3.486 -12.084 1.00 97.55 C
ANISOU 2637 CA ALA A 342 11396 12690 12977 -1020 1110 -1665 C
ATOM 2638 C ALA A 342 -38.694 3.820 -13.397 1.00 83.34 C
ANISOU 2638 C ALA A 342 9557 10971 11139 -918 979 -1665 C
ATOM 2639 O ALA A 342 -38.569 2.976 -14.287 1.00 93.66 O
ANISOU 2639 O ALA A 342 10861 12257 12468 -884 933 -1697 O
ATOM 2640 CB ALA A 342 -38.349 3.236 -10.980 1.00105.64 C
ANISOU 2640 CB ALA A 342 12556 13691 13892 -1021 1157 -1545 C
ATOM 2641 N VAL A 343 -38.249 5.072 -13.503 1.00 90.30 N
ANISOU 2641 N VAL A 343 10410 11941 11961 -870 922 -1628 N
ATOM 2642 CA VAL A 343 -37.507 5.551 -14.669 1.00 89.15 C
ANISOU 2642 CA VAL A 343 10232 11876 11763 -773 802 -1616 C
ATOM 2643 C VAL A 343 -36.043 5.178 -14.454 1.00 87.30 C
ANISOU 2643 C VAL A 343 10104 11655 11413 -719 780 -1506 C
ATOM 2644 O VAL A 343 -35.321 5.851 -13.717 1.00 83.04 O
ANISOU 2644 O VAL A 343 9612 11152 10789 -711 789 -1423 O
ATOM 2645 CB VAL A 343 -37.683 7.056 -14.879 1.00 84.08 C
ANISOU 2645 CB VAL A 343 9519 11319 11109 -748 754 -1626 C
ATOM 2646 CG1 VAL A 343 -36.870 7.522 -16.076 1.00 78.85 C
ANISOU 2646 CG1 VAL A 343 8835 10737 10387 -650 636 -1608 C
ATOM 2647 CG2 VAL A 343 -39.154 7.399 -15.060 1.00 80.27 C
ANISOU 2647 CG2 VAL A 343 8930 10823 10745 -797 776 -1739 C
ATOM 2648 N CYS A 344 -35.595 4.110 -15.109 1.00 91.59 N
ANISOU 2648 N CYS A 344 10680 12168 11950 -681 749 -1506 N
ATOM 2649 CA CYS A 344 -34.259 3.557 -14.891 1.00 91.64 C
ANISOU 2649 CA CYS A 344 10787 12175 11857 -631 734 -1409 C
ATOM 2650 C CYS A 344 -33.133 4.387 -15.506 1.00 99.16 C
ANISOU 2650 C CYS A 344 11731 13229 12715 -542 640 -1351 C
ATOM 2651 O CYS A 344 -32.021 3.848 -15.592 1.00 93.10 O
ANISOU 2651 O CYS A 344 11030 12468 11874 -488 613 -1284 O
ATOM 2652 CB CYS A 344 -34.196 2.128 -15.430 1.00 89.71 C
ANISOU 2652 CB CYS A 344 10580 11863 11644 -617 732 -1436 C
ATOM 2653 SG CYS A 344 -34.952 0.899 -14.349 1.00133.86 S
ANISOU 2653 SG CYS A 344 16241 17320 17300 -718 859 -1452 S
ATOM 2654 N HIS A 345 -33.318 5.630 -15.930 1.00103.02 N
ANISOU 2654 N HIS A 345 12146 13794 13201 -522 591 -1370 N
ATOM 2655 CA HIS A 345 -32.197 6.399 -16.457 1.00 98.74 C
ANISOU 2655 CA HIS A 345 11606 13345 12567 -444 510 -1309 C
ATOM 2656 C HIS A 345 -31.313 6.869 -15.306 1.00102.80 C
ANISOU 2656 C HIS A 345 12190 13879 12989 -453 542 -1207 C
ATOM 2657 O HIS A 345 -31.819 7.459 -14.344 1.00102.67 O
ANISOU 2657 O HIS A 345 12175 13850 12985 -513 601 -1202 O
ATOM 2658 CB HIS A 345 -32.692 7.594 -17.267 1.00100.54 C
ANISOU 2658 CB HIS A 345 11740 13642 12818 -421 449 -1361 C
ATOM 2659 CG HIS A 345 -31.596 8.355 -17.948 1.00110.24 C
ANISOU 2659 CG HIS A 345 12968 14962 13958 -342 366 -1306 C
ATOM 2660 ND1 HIS A 345 -30.801 7.797 -18.926 1.00125.31 N
ANISOU 2660 ND1 HIS A 345 14890 16896 15827 -270 304 -1294 N
ATOM 2661 CD2 HIS A 345 -31.160 9.627 -17.789 1.00107.94 C
ANISOU 2661 CD2 HIS A 345 12664 14741 13607 -327 340 -1261 C
ATOM 2662 CE1 HIS A 345 -29.924 8.694 -19.342 1.00115.58 C
ANISOU 2662 CE1 HIS A 345 13652 15747 14517 -215 245 -1244 C
ATOM 2663 NE2 HIS A 345 -30.121 9.813 -18.668 1.00103.54 N
ANISOU 2663 NE2 HIS A 345 12112 14250 12979 -249 264 -1223 N
ATOM 2664 N PRO A 346 -30.004 6.622 -15.359 1.00 94.16 N
ANISOU 2664 N PRO A 346 11155 12818 11805 -394 506 -1128 N
ATOM 2665 CA PRO A 346 -29.129 7.021 -14.246 1.00 88.84 C
ANISOU 2665 CA PRO A 346 10548 12164 11043 -401 532 -1032 C
ATOM 2666 C PRO A 346 -29.041 8.536 -14.127 1.00 87.19 C
ANISOU 2666 C PRO A 346 10295 12032 10799 -402 506 -1015 C
ATOM 2667 O PRO A 346 -28.708 9.231 -15.090 1.00 95.16 O
ANISOU 2667 O PRO A 346 11254 13115 11789 -349 432 -1022 O
ATOM 2668 CB PRO A 346 -27.773 6.406 -14.617 1.00 76.86 C
ANISOU 2668 CB PRO A 346 9082 10673 9447 -325 483 -967 C
ATOM 2669 CG PRO A 346 -28.089 5.347 -15.633 1.00 82.45 C
ANISOU 2669 CG PRO A 346 9773 11341 10212 -296 460 -1029 C
ATOM 2670 CD PRO A 346 -29.277 5.859 -16.385 1.00 80.27 C
ANISOU 2670 CD PRO A 346 9405 11072 10022 -319 445 -1125 C
ATOM 2671 N THR A 347 -29.342 9.043 -12.933 1.00 82.81 N
ANISOU 2671 N THR A 347 9768 11461 10237 -463 569 -990 N
ATOM 2672 CA THR A 347 -29.301 10.472 -12.658 1.00 83.98 C
ANISOU 2672 CA THR A 347 9884 11672 10353 -472 554 -973 C
ATOM 2673 C THR A 347 -28.751 10.703 -11.258 1.00 84.16 C
ANISOU 2673 C THR A 347 9984 11687 10305 -508 604 -895 C
ATOM 2674 O THR A 347 -28.786 9.819 -10.399 1.00 80.37 O
ANISOU 2674 O THR A 347 9574 11140 9822 -542 668 -871 O
ATOM 2675 CB THR A 347 -30.689 11.121 -12.783 1.00 85.99 C
ANISOU 2675 CB THR A 347 10062 11912 10698 -520 578 -1059 C
ATOM 2676 OG1 THR A 347 -31.655 10.328 -12.081 1.00 91.64 O
ANISOU 2676 OG1 THR A 347 10796 12540 11485 -589 665 -1101 O
ATOM 2677 CG2 THR A 347 -31.100 11.251 -14.244 1.00 77.43 C
ANISOU 2677 CG2 THR A 347 8896 10860 9666 -472 506 -1131 C
ATOM 2678 N ALA A 348 -28.239 11.913 -11.040 1.00 87.09 N
ANISOU 2678 N ALA A 348 10346 12127 10617 -498 575 -854 N
ATOM 2679 CA ALA A 348 -27.754 12.354 -9.739 1.00 78.46 C
ANISOU 2679 CA ALA A 348 9318 11038 9456 -532 614 -786 C
ATOM 2680 C ALA A 348 -28.627 13.501 -9.255 1.00 81.56 C
ANISOU 2680 C ALA A 348 9674 11437 9879 -586 649 -821 C
ATOM 2681 O ALA A 348 -28.829 14.480 -9.981 1.00 88.46 O
ANISOU 2681 O ALA A 348 10478 12363 10768 -565 601 -852 O
ATOM 2682 CB ALA A 348 -26.289 12.790 -9.810 1.00 75.34 C
ANISOU 2682 CB ALA A 348 8949 10719 8957 -477 550 -705 C
ATOM 2683 N TRP A 349 -29.139 13.383 -8.033 1.00 85.86 N
ANISOU 2683 N TRP A 349 10267 11927 10431 -652 734 -815 N
ATOM 2684 CA TRP A 349 -30.119 14.317 -7.496 1.00 80.68 C
ANISOU 2684 CA TRP A 349 9576 11262 9815 -708 782 -857 C
ATOM 2685 C TRP A 349 -29.498 15.164 -6.394 1.00 78.84 C
ANISOU 2685 C TRP A 349 9400 11058 9496 -729 798 -790 C
ATOM 2686 O TRP A 349 -28.856 14.634 -5.481 1.00 80.03 O
ANISOU 2686 O TRP A 349 9639 11187 9584 -741 829 -726 O
ATOM 2687 CB TRP A 349 -31.341 13.569 -6.961 1.00 87.13 C
ANISOU 2687 CB TRP A 349 10397 11991 10717 -775 876 -915 C
ATOM 2688 CG TRP A 349 -32.157 12.915 -8.032 1.00 89.07 C
ANISOU 2688 CG TRP A 349 10572 12210 11062 -765 862 -998 C
ATOM 2689 CD1 TRP A 349 -31.784 11.868 -8.823 1.00 89.39 C
ANISOU 2689 CD1 TRP A 349 10619 12235 11111 -723 824 -1000 C
ATOM 2690 CD2 TRP A 349 -33.491 13.259 -8.424 1.00 84.44 C
ANISOU 2690 CD2 TRP A 349 9898 11607 10580 -796 882 -1095 C
ATOM 2691 NE1 TRP A 349 -32.801 11.542 -9.687 1.00 83.18 N
ANISOU 2691 NE1 TRP A 349 9754 11424 10426 -728 819 -1093 N
ATOM 2692 CE2 TRP A 349 -33.861 12.380 -9.462 1.00 83.87 C
ANISOU 2692 CE2 TRP A 349 9780 11511 10575 -773 853 -1153 C
ATOM 2693 CE3 TRP A 349 -34.408 14.225 -7.999 1.00 89.22 C
ANISOU 2693 CE3 TRP A 349 10456 12216 11229 -840 922 -1141 C
ATOM 2694 CZ2 TRP A 349 -35.108 12.439 -10.080 1.00 93.26 C
ANISOU 2694 CZ2 TRP A 349 10878 12684 11874 -792 858 -1255 C
ATOM 2695 CZ3 TRP A 349 -35.645 14.282 -8.615 1.00 91.54 C
ANISOU 2695 CZ3 TRP A 349 10656 12493 11633 -856 928 -1242 C
ATOM 2696 CH2 TRP A 349 -35.983 13.395 -9.644 1.00 91.77 C
ANISOU 2696 CH2 TRP A 349 10640 12502 11728 -833 895 -1298 C
ATOM 2697 N ASP A 350 -29.697 16.477 -6.484 1.00 83.17 N
ANISOU 2697 N ASP A 350 9902 11655 10042 -732 776 -806 N
ATOM 2698 CA ASP A 350 -29.294 17.438 -5.458 1.00 83.96 C
ANISOU 2698 CA ASP A 350 10047 11782 10072 -760 794 -756 C
ATOM 2699 C ASP A 350 -30.559 18.163 -5.010 1.00 82.65 C
ANISOU 2699 C ASP A 350 9844 11589 9972 -816 855 -820 C
ATOM 2700 O ASP A 350 -30.846 19.277 -5.453 1.00 86.52 O
ANISOU 2700 O ASP A 350 10275 12120 10478 -805 821 -851 O
ATOM 2701 CB ASP A 350 -28.221 18.418 -5.995 1.00 87.46 C
ANISOU 2701 CB ASP A 350 10474 12313 10444 -709 705 -711 C
ATOM 2702 CG ASP A 350 -27.760 19.421 -4.946 1.00 92.36 C
ANISOU 2702 CG ASP A 350 11142 12961 10990 -738 719 -662 C
ATOM 2703 OD1 ASP A 350 -28.159 19.296 -3.769 1.00 98.84 O
ANISOU 2703 OD1 ASP A 350 12016 13734 11803 -793 795 -655 O
ATOM 2704 OD2 ASP A 350 -26.995 20.342 -5.304 1.00 95.20 O
ANISOU 2704 OD2 ASP A 350 11485 13388 11297 -708 656 -630 O
ATOM 2705 N LEU A 351 -31.321 17.516 -4.125 1.00 80.59 N
ANISOU 2705 N LEU A 351 9619 11255 9747 -876 950 -841 N
ATOM 2706 CA LEU A 351 -32.567 18.099 -3.643 1.00 80.26 C
ANISOU 2706 CA LEU A 351 9540 11183 9772 -932 1019 -906 C
ATOM 2707 C LEU A 351 -32.337 19.320 -2.763 1.00 85.00 C
ANISOU 2707 C LEU A 351 10171 11814 10310 -954 1033 -874 C
ATOM 2708 O LEU A 351 -33.279 20.084 -2.528 1.00 81.58 O
ANISOU 2708 O LEU A 351 9696 11374 9929 -987 1072 -930 O
ATOM 2709 CB LEU A 351 -33.380 17.057 -2.868 1.00 71.73 C
ANISOU 2709 CB LEU A 351 8496 10016 8742 -995 1125 -933 C
ATOM 2710 CG LEU A 351 -33.922 15.833 -3.613 1.00 75.19 C
ANISOU 2710 CG LEU A 351 8900 10406 9263 -992 1133 -984 C
ATOM 2711 CD1 LEU A 351 -32.867 14.742 -3.748 1.00 76.36 C
ANISOU 2711 CD1 LEU A 351 9118 10543 9351 -956 1102 -917 C
ATOM 2712 CD2 LEU A 351 -35.163 15.295 -2.915 1.00 86.46 C
ANISOU 2712 CD2 LEU A 351 10326 11754 10770 -1070 1247 -1042 C
ATOM 2713 N GLY A 352 -31.116 19.524 -2.278 1.00 80.81 N
ANISOU 2713 N GLY A 352 9711 11319 9672 -936 1000 -790 N
ATOM 2714 CA GLY A 352 -30.822 20.619 -1.382 1.00 73.81 C
ANISOU 2714 CA GLY A 352 8864 10459 8720 -960 1012 -756 C
ATOM 2715 C GLY A 352 -31.073 20.259 0.071 1.00 80.37 C
ANISOU 2715 C GLY A 352 9782 11233 9520 -1023 1110 -734 C
ATOM 2716 O GLY A 352 -31.642 19.217 0.405 1.00 81.52 O
ANISOU 2716 O GLY A 352 9953 11313 9706 -1056 1180 -752 O
ATOM 2717 N LYS A 353 -30.631 21.159 0.952 1.00 78.40 N
ANISOU 2717 N LYS A 353 9583 11009 9195 -1042 1116 -694 N
ATOM 2718 CA LYS A 353 -30.737 20.973 2.400 1.00 78.58 C
ANISOU 2718 CA LYS A 353 9701 10987 9170 -1099 1203 -665 C
ATOM 2719 C LYS A 353 -30.082 19.665 2.842 1.00 76.65 C
ANISOU 2719 C LYS A 353 9544 10706 8874 -1094 1218 -605 C
ATOM 2720 O LYS A 353 -30.630 18.917 3.655 1.00 68.16 O
ANISOU 2720 O LYS A 353 8526 9561 7809 -1142 1308 -609 O
ATOM 2721 CB LYS A 353 -32.194 21.042 2.867 1.00 70.10 C
ANISOU 2721 CB LYS A 353 8601 9855 8180 -1160 1306 -740 C
ATOM 2722 CG LYS A 353 -32.849 22.389 2.623 1.00 81.31 C
ANISOU 2722 CG LYS A 353 9947 11306 9642 -1164 1298 -796 C
ATOM 2723 CD LYS A 353 -34.223 22.471 3.260 1.00 77.65 C
ANISOU 2723 CD LYS A 353 9465 10787 9252 -1227 1408 -866 C
ATOM 2724 CE LYS A 353 -34.782 23.880 3.154 1.00 81.07 C
ANISOU 2724 CE LYS A 353 9836 11251 9716 -1227 1399 -916 C
ATOM 2725 NZ LYS A 353 -36.108 24.018 3.819 1.00 87.25 N
ANISOU 2725 NZ LYS A 353 10598 11984 10570 -1286 1509 -986 N
ATOM 2726 N GLY A 354 -28.900 19.386 2.297 1.00 76.67 N
ANISOU 2726 N GLY A 354 9556 10754 8821 -1036 1130 -550 N
ATOM 2727 CA GLY A 354 -28.135 18.221 2.692 1.00 75.46 C
ANISOU 2727 CA GLY A 354 9487 10574 8610 -1019 1130 -487 C
ATOM 2728 C GLY A 354 -28.604 16.905 2.119 1.00 74.81 C
ANISOU 2728 C GLY A 354 9392 10435 8598 -1012 1156 -516 C
ATOM 2729 O GLY A 354 -28.093 15.857 2.527 1.00 74.36 O
ANISOU 2729 O GLY A 354 9414 10340 8498 -1003 1168 -468 O
ATOM 2730 N ASP A 355 -29.551 16.921 1.183 1.00 79.74 N
ANISOU 2730 N ASP A 355 9921 11049 9328 -1014 1160 -594 N
ATOM 2731 CA ASP A 355 -30.111 15.706 0.603 1.00 80.78 C
ANISOU 2731 CA ASP A 355 10032 11123 9536 -1014 1186 -633 C
ATOM 2732 C ASP A 355 -29.473 15.473 -0.763 1.00 83.61 C
ANISOU 2732 C ASP A 355 10331 11530 9907 -940 1085 -632 C
ATOM 2733 O ASP A 355 -29.661 16.268 -1.689 1.00 83.22 O
ANISOU 2733 O ASP A 355 10191 11532 9895 -914 1029 -673 O
ATOM 2734 CB ASP A 355 -31.631 15.813 0.493 1.00 75.00 C
ANISOU 2734 CB ASP A 355 9233 10346 8918 -1068 1260 -726 C
ATOM 2735 CG ASP A 355 -32.291 14.482 0.177 1.00 82.34 C
ANISOU 2735 CG ASP A 355 10159 11201 9925 -1086 1308 -766 C
ATOM 2736 OD1 ASP A 355 -31.574 13.463 0.072 1.00 86.41 O
ANISOU 2736 OD1 ASP A 355 10733 11696 10404 -1056 1286 -719 O
ATOM 2737 OD2 ASP A 355 -33.533 14.455 0.037 1.00 78.52 O
ANISOU 2737 OD2 ASP A 355 9614 10680 9541 -1131 1367 -847 O
ATOM 2738 N PHE A 356 -28.716 14.383 -0.883 1.00 86.17 N
ANISOU 2738 N PHE A 356 10709 11838 10196 -904 1062 -586 N
ATOM 2739 CA PHE A 356 -28.080 13.988 -2.133 1.00 81.52 C
ANISOU 2739 CA PHE A 356 10072 11287 9614 -833 975 -584 C
ATOM 2740 C PHE A 356 -28.408 12.529 -2.403 1.00 85.04 C
ANISOU 2740 C PHE A 356 10541 11659 10110 -832 1007 -603 C
ATOM 2741 O PHE A 356 -28.184 11.672 -1.542 1.00 90.69 O
ANISOU 2741 O PHE A 356 11353 12318 10788 -851 1057 -560 O
ATOM 2742 CB PHE A 356 -26.560 14.188 -2.078 1.00 70.10 C
ANISOU 2742 CB PHE A 356 8666 9907 8061 -776 897 -500 C
ATOM 2743 CG PHE A 356 -26.143 15.591 -1.743 1.00 73.18 C
ANISOU 2743 CG PHE A 356 9043 10366 8395 -781 866 -476 C
ATOM 2744 CD1 PHE A 356 -26.075 16.562 -2.728 1.00 81.93 C
ANISOU 2744 CD1 PHE A 356 10064 11543 9524 -751 800 -504 C
ATOM 2745 CD2 PHE A 356 -25.811 15.938 -0.445 1.00 71.54 C
ANISOU 2745 CD2 PHE A 356 8916 10154 8113 -815 901 -426 C
ATOM 2746 CE1 PHE A 356 -25.689 17.853 -2.423 1.00 80.16 C
ANISOU 2746 CE1 PHE A 356 9831 11377 9249 -758 772 -482 C
ATOM 2747 CE2 PHE A 356 -25.425 17.229 -0.135 1.00 79.15 C
ANISOU 2747 CE2 PHE A 356 9868 11178 9026 -822 871 -407 C
ATOM 2748 CZ PHE A 356 -25.364 18.187 -1.125 1.00 67.71 C
ANISOU 2748 CZ PHE A 356 8331 9794 7601 -795 808 -435 C
ATOM 2749 N ARG A 357 -28.939 12.247 -3.591 1.00 83.89 N
ANISOU 2749 N ARG A 357 10314 11513 10048 -811 979 -668 N
ATOM 2750 CA ARG A 357 -29.363 10.900 -3.943 1.00 76.92 C
ANISOU 2750 CA ARG A 357 9444 10557 9224 -814 1009 -699 C
ATOM 2751 C ARG A 357 -28.894 10.563 -5.351 1.00 83.49 C
ANISOU 2751 C ARG A 357 10218 11429 10075 -741 920 -715 C
ATOM 2752 O ARG A 357 -28.528 11.441 -6.136 1.00 79.77 O
ANISOU 2752 O ARG A 357 9681 11036 9590 -698 845 -720 O
ATOM 2753 CB ARG A 357 -30.889 10.742 -3.850 1.00 80.23 C
ANISOU 2753 CB ARG A 357 9819 10912 9753 -885 1092 -786 C
ATOM 2754 CG ARG A 357 -31.493 11.210 -2.535 1.00 91.27 C
ANISOU 2754 CG ARG A 357 11260 12276 11143 -961 1186 -782 C
ATOM 2755 CD ARG A 357 -32.999 11.008 -2.509 1.00 82.92 C
ANISOU 2755 CD ARG A 357 10149 11157 10200 -1030 1270 -874 C
ATOM 2756 NE ARG A 357 -33.615 11.679 -1.370 1.00 82.80 N
ANISOU 2756 NE ARG A 357 10157 11124 10180 -1098 1354 -880 N
ATOM 2757 CZ ARG A 357 -34.897 11.581 -1.045 1.00 83.03 C
ANISOU 2757 CZ ARG A 357 10151 11097 10297 -1168 1446 -951 C
ATOM 2758 NH1 ARG A 357 -35.731 10.826 -1.741 1.00 75.18 N
ANISOU 2758 NH1 ARG A 357 9098 10059 9407 -1186 1465 -1025 N
ATOM 2759 NH2 ARG A 357 -35.353 12.256 0.006 1.00 84.85 N
ANISOU 2759 NH2 ARG A 357 10408 11319 10514 -1224 1520 -951 N
ATOM 2760 N ILE A 358 -28.909 9.268 -5.660 1.00 87.51 N
ANISOU 2760 N ILE A 358 10757 11879 10612 -728 932 -723 N
ATOM 2761 CA ILE A 358 -28.600 8.758 -6.991 1.00 76.54 C
ANISOU 2761 CA ILE A 358 9320 10513 9250 -664 859 -749 C
ATOM 2762 C ILE A 358 -29.665 7.739 -7.367 1.00 76.63 C
ANISOU 2762 C ILE A 358 9312 10441 9362 -698 908 -824 C
ATOM 2763 O ILE A 358 -29.895 6.773 -6.631 1.00 87.79 O
ANISOU 2763 O ILE A 358 10801 11771 10783 -738 980 -811 O
ATOM 2764 CB ILE A 358 -27.197 8.124 -7.061 1.00 78.86 C
ANISOU 2764 CB ILE A 358 9679 10828 9456 -594 806 -670 C
ATOM 2765 CG1 ILE A 358 -26.122 9.205 -7.176 1.00 78.49 C
ANISOU 2765 CG1 ILE A 358 9614 10883 9326 -546 732 -615 C
ATOM 2766 CG2 ILE A 358 -27.101 7.154 -8.229 1.00 72.11 C
ANISOU 2766 CG2 ILE A 358 8798 9957 8642 -542 764 -704 C
ATOM 2767 CD1 ILE A 358 -24.727 8.654 -7.375 1.00 73.24 C
ANISOU 2767 CD1 ILE A 358 8994 10252 8582 -472 673 -545 C
ATOM 2768 N LEU A 359 -30.314 7.956 -8.506 1.00 81.89 N
ANISOU 2768 N LEU A 359 9880 11129 10105 -684 868 -902 N
ATOM 2769 CA LEU A 359 -31.328 7.047 -9.023 1.00 89.77 C
ANISOU 2769 CA LEU A 359 10845 12057 11206 -713 901 -984 C
ATOM 2770 C LEU A 359 -30.704 6.217 -10.138 1.00 81.55 C
ANISOU 2770 C LEU A 359 9801 11024 10161 -641 831 -986 C
ATOM 2771 O LEU A 359 -30.207 6.772 -11.124 1.00 78.26 O
ANISOU 2771 O LEU A 359 9330 10684 9723 -577 744 -989 O
ATOM 2772 CB LEU A 359 -32.542 7.826 -9.532 1.00 82.75 C
ANISOU 2772 CB LEU A 359 9847 11186 10410 -746 903 -1078 C
ATOM 2773 CG LEU A 359 -33.893 7.115 -9.646 1.00 84.58 C
ANISOU 2773 CG LEU A 359 10038 11339 10760 -809 967 -1172 C
ATOM 2774 CD1 LEU A 359 -35.003 8.145 -9.756 1.00 87.61 C
ANISOU 2774 CD1 LEU A 359 10323 11748 11216 -846 979 -1248 C
ATOM 2775 CD2 LEU A 359 -33.934 6.172 -10.837 1.00 83.53 C
ANISOU 2775 CD2 LEU A 359 9876 11188 10675 -768 917 -1220 C
ATOM 2776 N MET A 360 -30.736 4.892 -9.985 1.00 86.66 N
ANISOU 2776 N MET A 360 10511 11590 10828 -652 871 -986 N
ATOM 2777 CA MET A 360 -30.076 4.010 -10.940 1.00 86.20 C
ANISOU 2777 CA MET A 360 10464 11531 10758 -582 810 -982 C
ATOM 2778 C MET A 360 -30.512 2.559 -10.769 1.00 89.79 C
ANISOU 2778 C MET A 360 10976 11876 11264 -614 870 -1007 C
ATOM 2779 O MET A 360 -30.420 2.002 -9.671 1.00 89.06 O
ANISOU 2779 O MET A 360 10977 11718 11144 -654 941 -959 O
ATOM 2780 CB MET A 360 -28.556 4.127 -10.789 1.00 70.40 C
ANISOU 2780 CB MET A 360 8521 9588 8642 -509 755 -884 C
ATOM 2781 CG MET A 360 -27.752 3.372 -11.831 1.00 91.93 C
ANISOU 2781 CG MET A 360 11251 12331 11348 -426 685 -878 C
ATOM 2782 SD MET A 360 -25.982 3.686 -11.677 1.00 73.46 S
ANISOU 2782 SD MET A 360 8959 10074 8877 -341 618 -768 S
ATOM 2783 CE MET A 360 -25.338 2.633 -12.972 1.00 83.57 C
ANISOU 2783 CE MET A 360 10238 11356 10160 -252 553 -784 C
ATOM 2784 N CYS A 361 -30.991 1.939 -11.851 1.00 87.52 N
ANISOU 2784 N CYS A 361 10638 11567 11050 -599 841 -1082 N
ATOM 2785 CA CYS A 361 -31.307 0.509 -11.855 1.00 86.98 C
ANISOU 2785 CA CYS A 361 10625 11396 11029 -621 887 -1107 C
ATOM 2786 C CYS A 361 -30.019 -0.248 -12.165 1.00 87.45 C
ANISOU 2786 C CYS A 361 10757 11461 11011 -536 835 -1041 C
ATOM 2787 O CYS A 361 -29.792 -0.741 -13.272 1.00 91.28 O
ANISOU 2787 O CYS A 361 11214 11955 11512 -479 774 -1075 O
ATOM 2788 CB CYS A 361 -32.405 0.199 -12.863 1.00 91.38 C
ANISOU 2788 CB CYS A 361 11094 11928 11700 -644 877 -1222 C
ATOM 2789 SG CYS A 361 -33.939 1.112 -12.601 1.00103.37 S
ANISOU 2789 SG CYS A 361 12512 13448 13317 -736 930 -1309 S
ATOM 2790 N THR A 362 -29.162 -0.339 -11.152 1.00 87.48 N
ANISOU 2790 N THR A 362 10856 11457 10927 -525 858 -946 N
ATOM 2791 CA THR A 362 -27.815 -0.853 -11.352 1.00 86.99 C
ANISOU 2791 CA THR A 362 10855 11417 10779 -436 802 -875 C
ATOM 2792 C THR A 362 -27.825 -2.359 -11.584 1.00 88.19 C
ANISOU 2792 C THR A 362 11075 11473 10962 -424 823 -890 C
ATOM 2793 O THR A 362 -28.517 -3.110 -10.890 1.00 79.48 O
ANISOU 2793 O THR A 362 10032 10267 9901 -493 908 -903 O
ATOM 2794 CB THR A 362 -26.938 -0.522 -10.144 1.00 79.00 C
ANISOU 2794 CB THR A 362 9926 10424 9667 -429 819 -773 C
ATOM 2795 OG1 THR A 362 -27.054 0.873 -9.836 1.00 79.72 O
ANISOU 2795 OG1 THR A 362 9958 10593 9737 -453 810 -765 O
ATOM 2796 CG2 THR A 362 -25.480 -0.849 -10.435 1.00 84.13 C
ANISOU 2796 CG2 THR A 362 10618 11120 10228 -328 748 -702 C
ATOM 2797 N LYS A 363 -27.052 -2.793 -12.574 1.00 85.10 N
ANISOU 2797 N LYS A 363 10675 11112 10546 -337 749 -888 N
ATOM 2798 CA LYS A 363 -26.795 -4.198 -12.837 1.00 82.28 C
ANISOU 2798 CA LYS A 363 10390 10673 10198 -305 755 -889 C
ATOM 2799 C LYS A 363 -25.321 -4.491 -12.588 1.00 79.34 C
ANISOU 2799 C LYS A 363 10094 10333 9721 -216 712 -794 C
ATOM 2800 O LYS A 363 -24.474 -3.593 -12.613 1.00 67.54 O
ANISOU 2800 O LYS A 363 8568 8939 8156 -166 657 -744 O
ATOM 2801 CB LYS A 363 -27.177 -4.569 -14.275 1.00 71.23 C
ANISOU 2801 CB LYS A 363 8918 9280 8867 -274 704 -977 C
ATOM 2802 CG LYS A 363 -28.511 -3.991 -14.729 1.00 93.94 C
ANISOU 2802 CG LYS A 363 11691 12160 11840 -344 718 -1075 C
ATOM 2803 CD LYS A 363 -29.676 -4.578 -13.948 1.00 94.72 C
ANISOU 2803 CD LYS A 363 11823 12148 12019 -449 820 -1116 C
ATOM 2804 CE LYS A 363 -30.932 -3.732 -14.112 1.00102.66 C
ANISOU 2804 CE LYS A 363 12721 13176 13109 -522 840 -1199 C
ATOM 2805 NZ LYS A 363 -31.257 -3.471 -15.542 1.00111.93 N
ANISOU 2805 NZ LYS A 363 13790 14404 14333 -482 761 -1283 N
ATOM 2806 N VAL A 364 -25.017 -5.763 -12.335 1.00 82.61 N
ANISOU 2806 N VAL A 364 10607 10656 10126 -195 738 -770 N
ATOM 2807 CA VAL A 364 -23.645 -6.167 -12.045 1.00 80.84 C
ANISOU 2807 CA VAL A 364 10460 10451 9806 -107 699 -681 C
ATOM 2808 C VAL A 364 -22.878 -6.301 -13.354 1.00 85.28 C
ANISOU 2808 C VAL A 364 10969 11080 10352 -7 610 -699 C
ATOM 2809 O VAL A 364 -22.543 -7.411 -13.785 1.00 82.74 O
ANISOU 2809 O VAL A 364 10700 10703 10036 44 598 -705 O
ATOM 2810 CB VAL A 364 -23.604 -7.477 -11.236 1.00 88.69 C
ANISOU 2810 CB VAL A 364 11590 11318 10792 -118 761 -645 C
ATOM 2811 CG1 VAL A 364 -22.210 -7.706 -10.662 1.00 80.96 C
ANISOU 2811 CG1 VAL A 364 10693 10363 9704 -34 725 -544 C
ATOM 2812 CG2 VAL A 364 -24.643 -7.445 -10.127 1.00 88.81 C
ANISOU 2812 CG2 VAL A 364 11650 11252 10844 -232 862 -651 C
ATOM 2813 N THR A 365 -22.605 -5.170 -14.000 1.00 87.47 N
ANISOU 2813 N THR A 365 11148 11475 10612 20 549 -708 N
ATOM 2814 CA THR A 365 -21.853 -5.127 -15.244 1.00 78.60 C
ANISOU 2814 CA THR A 365 9968 10428 9466 113 466 -723 C
ATOM 2815 C THR A 365 -20.752 -4.083 -15.124 1.00 80.11 C
ANISOU 2815 C THR A 365 10126 10741 9570 165 411 -655 C
ATOM 2816 O THR A 365 -20.724 -3.278 -14.189 1.00 85.27 O
ANISOU 2816 O THR A 365 10786 11424 10190 123 433 -610 O
ATOM 2817 CB THR A 365 -22.753 -4.806 -16.447 1.00 70.82 C
ANISOU 2817 CB THR A 365 8884 9465 8560 93 441 -822 C
ATOM 2818 OG1 THR A 365 -23.292 -3.485 -16.306 1.00 64.23 O
ANISOU 2818 OG1 THR A 365 7972 8696 7737 40 442 -837 O
ATOM 2819 CG2 THR A 365 -23.895 -5.807 -16.551 1.00 69.35 C
ANISOU 2819 CG2 THR A 365 8722 9160 8467 33 495 -896 C
ATOM 2820 N MET A 366 -19.835 -4.100 -16.093 1.00 82.73 N
ANISOU 2820 N MET A 366 10423 11145 9865 256 341 -650 N
ATOM 2821 CA MET A 366 -18.758 -3.117 -16.097 1.00 77.38 C
ANISOU 2821 CA MET A 366 9705 10587 9108 306 288 -591 C
ATOM 2822 C MET A 366 -19.260 -1.734 -16.495 1.00 78.28 C
ANISOU 2822 C MET A 366 9722 10782 9240 265 269 -624 C
ATOM 2823 O MET A 366 -18.720 -0.723 -16.031 1.00 78.41 O
ANISOU 2823 O MET A 366 9715 10876 9200 262 253 -573 O
ATOM 2824 CB MET A 366 -17.638 -3.568 -17.033 1.00 75.81 C
ANISOU 2824 CB MET A 366 9496 10440 8867 414 224 -578 C
ATOM 2825 CG MET A 366 -16.448 -2.627 -17.066 1.00 77.58 C
ANISOU 2825 CG MET A 366 9677 10789 9010 467 171 -519 C
ATOM 2826 SD MET A 366 -15.136 -3.205 -18.153 1.00 76.89 S
ANISOU 2826 SD MET A 366 9575 10762 8877 594 105 -508 S
ATOM 2827 CE MET A 366 -13.976 -1.846 -18.032 1.00 69.86 C
ANISOU 2827 CE MET A 366 8622 10019 7904 624 57 -443 C
ATOM 2828 N ASP A 367 -20.288 -1.668 -17.343 1.00 80.83 N
ANISOU 2828 N ASP A 367 9987 11087 9638 233 270 -709 N
ATOM 2829 CA ASP A 367 -20.818 -0.375 -17.765 1.00 76.17 C
ANISOU 2829 CA ASP A 367 9307 10568 9067 199 249 -744 C
ATOM 2830 C ASP A 367 -21.463 0.362 -16.597 1.00 79.29 C
ANISOU 2830 C ASP A 367 9709 10946 9471 112 303 -726 C
ATOM 2831 O ASP A 367 -21.229 1.561 -16.403 1.00 83.02 O
ANISOU 2831 O ASP A 367 10140 11497 9908 101 285 -699 O
ATOM 2832 CB ASP A 367 -21.819 -0.564 -18.905 1.00 86.33 C
ANISOU 2832 CB ASP A 367 10536 11832 10434 188 235 -843 C
ATOM 2833 CG ASP A 367 -21.162 -1.044 -20.185 1.00 87.98 C
ANISOU 2833 CG ASP A 367 10727 12078 10625 278 174 -863 C
ATOM 2834 OD1 ASP A 367 -19.988 -0.690 -20.422 1.00 85.99 O
ANISOU 2834 OD1 ASP A 367 10467 11907 10297 345 130 -809 O
ATOM 2835 OD2 ASP A 367 -21.820 -1.775 -20.956 1.00 83.32 O
ANISOU 2835 OD2 ASP A 367 10128 11434 10096 280 170 -937 O
ATOM 2836 N ASP A 368 -22.281 -0.339 -15.807 1.00 81.27 N
ANISOU 2836 N ASP A 368 10015 11093 9771 47 373 -742 N
ATOM 2837 CA ASP A 368 -22.883 0.285 -14.634 1.00 78.42 C
ANISOU 2837 CA ASP A 368 9669 10710 9416 -36 433 -724 C
ATOM 2838 C ASP A 368 -21.840 0.600 -13.570 1.00 81.13 C
ANISOU 2838 C ASP A 368 10072 11088 9667 -20 434 -626 C
ATOM 2839 O ASP A 368 -22.018 1.543 -12.789 1.00 80.42 O
ANISOU 2839 O ASP A 368 9974 11026 9557 -69 457 -602 O
ATOM 2840 CB ASP A 368 -23.976 -0.616 -14.058 1.00 85.36 C
ANISOU 2840 CB ASP A 368 10598 11467 10369 -110 513 -765 C
ATOM 2841 CG ASP A 368 -25.232 -0.623 -14.907 1.00 82.37 C
ANISOU 2841 CG ASP A 368 10144 11062 10092 -151 519 -870 C
ATOM 2842 OD1 ASP A 368 -25.263 0.092 -15.931 1.00 86.40 O
ANISOU 2842 OD1 ASP A 368 10568 11648 10612 -119 458 -908 O
ATOM 2843 OD2 ASP A 368 -26.189 -1.341 -14.548 1.00 79.81 O
ANISOU 2843 OD2 ASP A 368 9847 10640 9838 -216 585 -914 O
ATOM 2844 N PHE A 369 -20.756 -0.177 -13.519 1.00 78.42 N
ANISOU 2844 N PHE A 369 9788 10742 9266 51 409 -572 N
ATOM 2845 CA PHE A 369 -19.657 0.142 -12.614 1.00 71.77 C
ANISOU 2845 CA PHE A 369 8994 9944 8330 79 396 -481 C
ATOM 2846 C PHE A 369 -19.038 1.490 -12.959 1.00 84.21 C
ANISOU 2846 C PHE A 369 10492 11645 9860 102 339 -461 C
ATOM 2847 O PHE A 369 -18.752 2.299 -12.068 1.00 77.63 O
ANISOU 2847 O PHE A 369 9669 10848 8977 73 347 -412 O
ATOM 2848 CB PHE A 369 -18.603 -0.965 -12.663 1.00 72.27 C
ANISOU 2848 CB PHE A 369 9124 9988 8347 163 369 -436 C
ATOM 2849 CG PHE A 369 -17.336 -0.635 -11.923 1.00 86.83 C
ANISOU 2849 CG PHE A 369 11002 11894 10094 208 338 -347 C
ATOM 2850 CD1 PHE A 369 -17.248 -0.823 -10.554 1.00 83.30 C
ANISOU 2850 CD1 PHE A 369 10645 11398 9607 176 381 -290 C
ATOM 2851 CD2 PHE A 369 -16.228 -0.147 -12.600 1.00 82.23 C
ANISOU 2851 CD2 PHE A 369 10363 11419 9460 283 266 -322 C
ATOM 2852 CE1 PHE A 369 -16.083 -0.524 -9.872 1.00 86.30 C
ANISOU 2852 CE1 PHE A 369 11056 11838 9898 219 346 -212 C
ATOM 2853 CE2 PHE A 369 -15.061 0.155 -11.924 1.00 77.24 C
ANISOU 2853 CE2 PHE A 369 9756 10848 8744 323 235 -246 C
ATOM 2854 CZ PHE A 369 -14.988 -0.035 -10.559 1.00 88.63 C
ANISOU 2854 CZ PHE A 369 11286 12242 10148 293 272 -191 C
ATOM 2855 N LEU A 370 -18.824 1.751 -14.251 1.00 84.54 N
ANISOU 2855 N LEU A 370 10458 11750 9913 151 282 -498 N
ATOM 2856 CA LEU A 370 -18.262 3.030 -14.664 1.00 74.87 C
ANISOU 2856 CA LEU A 370 9161 10640 8646 170 231 -481 C
ATOM 2857 C LEU A 370 -19.289 4.152 -14.590 1.00 69.04 C
ANISOU 2857 C LEU A 370 8368 9915 7951 95 252 -522 C
ATOM 2858 O LEU A 370 -18.926 5.301 -14.319 1.00 71.70 O
ANISOU 2858 O LEU A 370 8674 10324 8244 83 234 -490 O
ATOM 2859 CB LEU A 370 -17.695 2.921 -16.080 1.00 76.48 C
ANISOU 2859 CB LEU A 370 9310 10904 8845 248 169 -506 C
ATOM 2860 CG LEU A 370 -16.535 1.938 -16.252 1.00 77.03 C
ANISOU 2860 CG LEU A 370 9422 10978 8867 334 140 -465 C
ATOM 2861 CD1 LEU A 370 -16.122 1.847 -17.711 1.00 60.59 C
ANISOU 2861 CD1 LEU A 370 7283 8952 6786 405 86 -500 C
ATOM 2862 CD2 LEU A 370 -15.355 2.342 -15.381 1.00 75.32 C
ANISOU 2862 CD2 LEU A 370 9232 10821 8566 357 123 -379 C
ATOM 2863 N THR A 371 -20.566 3.842 -14.828 1.00 70.41 N
ANISOU 2863 N THR A 371 8526 10018 8208 46 289 -594 N
ATOM 2864 CA THR A 371 -21.606 4.856 -14.696 1.00 73.92 C
ANISOU 2864 CA THR A 371 8919 10470 8699 -24 312 -638 C
ATOM 2865 C THR A 371 -21.757 5.309 -13.249 1.00 77.62 C
ANISOU 2865 C THR A 371 9435 10917 9142 -89 367 -593 C
ATOM 2866 O THR A 371 -22.027 6.488 -12.996 1.00 80.87 O
ANISOU 2866 O THR A 371 9806 11373 9548 -126 368 -594 O
ATOM 2867 CB THR A 371 -22.935 4.321 -15.236 1.00 82.77 C
ANISOU 2867 CB THR A 371 10011 11518 9920 -62 341 -729 C
ATOM 2868 OG1 THR A 371 -22.772 3.921 -16.602 1.00 87.94 O
ANISOU 2868 OG1 THR A 371 10626 12196 10593 1 285 -772 O
ATOM 2869 CG2 THR A 371 -24.019 5.390 -15.160 1.00 78.03 C
ANISOU 2869 CG2 THR A 371 9348 10929 9370 -127 360 -778 C
ATOM 2870 N ALA A 372 -21.573 4.395 -12.291 1.00 87.93 N
ANISOU 2870 N ALA A 372 10829 12152 10429 -101 413 -552 N
ATOM 2871 CA ALA A 372 -21.661 4.771 -10.883 1.00 88.45 C
ANISOU 2871 CA ALA A 372 10950 12196 10461 -159 466 -506 C
ATOM 2872 C ALA A 372 -20.586 5.784 -10.515 1.00 80.82 C
ANISOU 2872 C ALA A 372 9976 11324 9406 -133 421 -439 C
ATOM 2873 O ALA A 372 -20.840 6.717 -9.745 1.00 74.92 O
ANISOU 2873 O ALA A 372 9228 10595 8642 -185 446 -425 O
ATOM 2874 CB ALA A 372 -21.559 3.529 -9.999 1.00 81.38 C
ANISOU 2874 CB ALA A 372 10161 11207 9552 -166 517 -471 C
ATOM 2875 N HIS A 373 -19.375 5.616 -11.053 1.00 80.40 N
ANISOU 2875 N HIS A 373 9918 11333 9297 -53 357 -399 N
ATOM 2876 CA HIS A 373 -18.331 6.613 -10.836 1.00 77.40 C
ANISOU 2876 CA HIS A 373 9518 11052 8840 -29 311 -342 C
ATOM 2877 C HIS A 373 -18.646 7.915 -11.559 1.00 83.28 C
ANISOU 2877 C HIS A 373 10172 11868 9603 -45 281 -378 C
ATOM 2878 O HIS A 373 -18.292 8.995 -11.072 1.00 81.50 O
ANISOU 2878 O HIS A 373 9933 11700 9332 -67 270 -346 O
ATOM 2879 CB HIS A 373 -16.977 6.070 -11.291 1.00 68.93 C
ANISOU 2879 CB HIS A 373 8453 10028 7709 61 252 -298 C
ATOM 2880 CG HIS A 373 -16.466 4.936 -10.458 1.00 71.13 C
ANISOU 2880 CG HIS A 373 8827 10247 7953 86 272 -248 C
ATOM 2881 ND1 HIS A 373 -17.059 3.692 -10.449 1.00 73.24 N
ANISOU 2881 ND1 HIS A 373 9148 10413 8267 84 312 -275 N
ATOM 2882 CD2 HIS A 373 -15.415 4.858 -9.607 1.00 69.25 C
ANISOU 2882 CD2 HIS A 373 8641 10034 7635 116 254 -175 C
ATOM 2883 CE1 HIS A 373 -16.397 2.897 -9.628 1.00 84.50 C
ANISOU 2883 CE1 HIS A 373 10662 11802 9643 113 320 -217 C
ATOM 2884 NE2 HIS A 373 -15.394 3.580 -9.104 1.00 73.81 N
ANISOU 2884 NE2 HIS A 373 9307 10525 8211 135 283 -156 N
ATOM 2885 N HIS A 374 -19.307 7.834 -12.716 1.00 79.35 N
ANISOU 2885 N HIS A 374 9615 11365 9168 -34 267 -446 N
ATOM 2886 CA HIS A 374 -19.690 9.041 -13.440 1.00 75.06 C
ANISOU 2886 CA HIS A 374 8992 10883 8645 -47 238 -484 C
ATOM 2887 C HIS A 374 -20.761 9.819 -12.687 1.00 80.66 C
ANISOU 2887 C HIS A 374 9695 11561 9391 -129 288 -510 C
ATOM 2888 O HIS A 374 -20.705 11.053 -12.615 1.00 79.03 O
ANISOU 2888 O HIS A 374 9453 11412 9162 -148 272 -501 O
ATOM 2889 CB HIS A 374 -20.178 8.675 -14.843 1.00 78.76 C
ANISOU 2889 CB HIS A 374 9407 11348 9172 -12 208 -553 C
ATOM 2890 CG HIS A 374 -20.602 9.851 -15.667 1.00 79.48 C
ANISOU 2890 CG HIS A 374 9421 11496 9282 -17 175 -593 C
ATOM 2891 ND1 HIS A 374 -19.832 10.357 -16.692 1.00 84.96 N
ANISOU 2891 ND1 HIS A 374 10072 12272 9936 40 113 -584 N
ATOM 2892 CD2 HIS A 374 -21.718 10.616 -15.624 1.00 78.70 C
ANISOU 2892 CD2 HIS A 374 9285 11382 9236 -72 196 -643 C
ATOM 2893 CE1 HIS A 374 -20.453 11.386 -17.241 1.00 82.66 C
ANISOU 2893 CE1 HIS A 374 9725 12012 9671 22 96 -623 C
ATOM 2894 NE2 HIS A 374 -21.600 11.564 -16.610 1.00 82.16 N
ANISOU 2894 NE2 HIS A 374 9662 11890 9664 -43 143 -661 N
ATOM 2895 N GLU A 375 -21.742 9.117 -12.117 1.00 83.04 N
ANISOU 2895 N GLU A 375 10031 11771 9749 -179 353 -542 N
ATOM 2896 CA GLU A 375 -22.848 9.793 -11.448 1.00 79.99 C
ANISOU 2896 CA GLU A 375 9634 11352 9407 -257 407 -576 C
ATOM 2897 C GLU A 375 -22.457 10.278 -10.058 1.00 80.60 C
ANISOU 2897 C GLU A 375 9769 11433 9421 -296 441 -512 C
ATOM 2898 O GLU A 375 -22.884 11.359 -9.635 1.00 82.54 O
ANISOU 2898 O GLU A 375 9993 11701 9668 -341 457 -520 O
ATOM 2899 CB GLU A 375 -24.060 8.865 -11.371 1.00 98.07 C
ANISOU 2899 CB GLU A 375 11934 13543 11784 -301 468 -639 C
ATOM 2900 CG GLU A 375 -24.632 8.495 -12.729 1.00 86.40 C
ANISOU 2900 CG GLU A 375 10391 12060 10377 -272 434 -715 C
ATOM 2901 CD GLU A 375 -25.114 9.705 -13.507 1.00 89.23 C
ANISOU 2901 CD GLU A 375 10662 12479 10762 -272 394 -762 C
ATOM 2902 OE1 GLU A 375 -25.623 10.657 -12.876 1.00 97.87 O
ANISOU 2902 OE1 GLU A 375 11742 13582 11864 -322 423 -766 O
ATOM 2903 OE2 GLU A 375 -24.980 9.707 -14.748 1.00 87.94 O
ANISOU 2903 OE2 GLU A 375 10449 12353 10611 -219 335 -794 O
ATOM 2904 N MET A 376 -21.654 9.498 -9.330 1.00 77.14 N
ANISOU 2904 N MET A 376 9410 10973 8926 -277 451 -450 N
ATOM 2905 CA MET A 376 -21.179 9.956 -8.030 1.00 77.09 C
ANISOU 2905 CA MET A 376 9464 10976 8850 -307 474 -387 C
ATOM 2906 C MET A 376 -20.237 11.146 -8.159 1.00 78.41 C
ANISOU 2906 C MET A 376 9595 11247 8951 -282 413 -347 C
ATOM 2907 O MET A 376 -20.073 11.900 -7.194 1.00 78.61 O
ANISOU 2907 O MET A 376 9648 11290 8931 -320 429 -312 O
ATOM 2908 CB MET A 376 -20.495 8.809 -7.282 1.00 80.71 C
ANISOU 2908 CB MET A 376 10018 11389 9260 -283 490 -329 C
ATOM 2909 CG MET A 376 -20.267 9.082 -5.801 1.00 61.12 C
ANISOU 2909 CG MET A 376 7615 8892 6716 -324 528 -273 C
ATOM 2910 SD MET A 376 -19.634 7.654 -4.900 1.00 62.01 S
ANISOU 2910 SD MET A 376 7850 8934 6775 -297 552 -210 S
ATOM 2911 CE MET A 376 -21.026 6.532 -5.017 1.00 64.50 C
ANISOU 2911 CE MET A 376 8191 9125 7189 -344 635 -275 C
ATOM 2912 N GLY A 377 -19.622 11.334 -9.329 1.00 77.57 N
ANISOU 2912 N GLY A 377 9428 11207 8838 -223 346 -353 N
ATOM 2913 CA GLY A 377 -18.858 12.547 -9.562 1.00 72.35 C
ANISOU 2913 CA GLY A 377 8724 10642 8125 -208 294 -324 C
ATOM 2914 C GLY A 377 -19.734 13.785 -9.574 1.00 76.49 C
ANISOU 2914 C GLY A 377 9202 11178 8683 -262 310 -365 C
ATOM 2915 O GLY A 377 -19.325 14.851 -9.107 1.00 82.48 O
ANISOU 2915 O GLY A 377 9957 11987 9394 -282 297 -334 O
ATOM 2916 N HIS A 378 -20.952 13.662 -10.111 1.00 77.31 N
ANISOU 2916 N HIS A 378 9269 11235 8871 -284 335 -437 N
ATOM 2917 CA HIS A 378 -21.911 14.759 -10.025 1.00 70.53 C
ANISOU 2917 CA HIS A 378 8370 10376 8051 -335 356 -480 C
ATOM 2918 C HIS A 378 -22.270 15.057 -8.574 1.00 79.19 C
ANISOU 2918 C HIS A 378 9522 11435 9132 -402 420 -459 C
ATOM 2919 O HIS A 378 -22.476 16.219 -8.203 1.00 74.89 O
ANISOU 2919 O HIS A 378 8962 10919 8575 -437 425 -460 O
ATOM 2920 CB HIS A 378 -23.174 14.428 -10.823 1.00 69.83 C
ANISOU 2920 CB HIS A 378 8232 10241 8061 -344 373 -566 C
ATOM 2921 CG HIS A 378 -22.960 14.348 -12.303 1.00 78.12 C
ANISOU 2921 CG HIS A 378 9223 11332 9128 -282 308 -595 C
ATOM 2922 ND1 HIS A 378 -22.578 15.434 -13.060 1.00 69.81 N
ANISOU 2922 ND1 HIS A 378 8121 10355 8048 -255 252 -592 N
ATOM 2923 CD2 HIS A 378 -23.097 13.316 -13.169 1.00 83.24 C
ANISOU 2923 CD2 HIS A 378 9859 11954 9815 -243 292 -630 C
ATOM 2924 CE1 HIS A 378 -22.478 15.072 -14.327 1.00 74.48 C
ANISOU 2924 CE1 HIS A 378 8674 10967 8659 -201 205 -622 C
ATOM 2925 NE2 HIS A 378 -22.788 13.792 -14.420 1.00 85.89 N
ANISOU 2925 NE2 HIS A 378 10139 12352 10144 -192 227 -647 N
ATOM 2926 N ILE A 379 -22.352 14.017 -7.741 1.00 81.28 N
ANISOU 2926 N ILE A 379 9856 11633 9392 -420 471 -440 N
ATOM 2927 CA ILE A 379 -22.692 14.208 -6.333 1.00 73.57 C
ANISOU 2927 CA ILE A 379 8943 10616 8396 -483 536 -419 C
ATOM 2928 C ILE A 379 -21.578 14.959 -5.615 1.00 75.69 C
ANISOU 2928 C ILE A 379 9246 10946 8566 -477 505 -347 C
ATOM 2929 O ILE A 379 -21.832 15.888 -4.840 1.00 76.79 O
ANISOU 2929 O ILE A 379 9397 11093 8686 -525 531 -342 O
ATOM 2930 CB ILE A 379 -22.982 12.854 -5.663 1.00 70.20 C
ANISOU 2930 CB ILE A 379 8591 10099 7982 -500 597 -411 C
ATOM 2931 CG1 ILE A 379 -24.196 12.186 -6.313 1.00 72.36 C
ANISOU 2931 CG1 ILE A 379 8826 10308 8360 -519 634 -490 C
ATOM 2932 CG2 ILE A 379 -23.204 13.032 -4.171 1.00 67.75 C
ANISOU 2932 CG2 ILE A 379 8357 9749 7634 -561 664 -380 C
ATOM 2933 CD1 ILE A 379 -25.475 12.979 -6.176 1.00 72.33 C
ANISOU 2933 CD1 ILE A 379 8773 10284 8423 -581 681 -555 C
ATOM 2934 N GLN A 380 -20.325 14.564 -5.861 1.00 74.94 N
ANISOU 2934 N GLN A 380 9166 10897 8410 -418 449 -294 N
ATOM 2935 CA GLN A 380 -19.191 15.271 -5.274 1.00 69.19 C
ANISOU 2935 CA GLN A 380 8460 10236 7592 -409 410 -229 C
ATOM 2936 C GLN A 380 -19.185 16.737 -5.686 1.00 70.89 C
ANISOU 2936 C GLN A 380 8612 10519 7804 -424 378 -244 C
ATOM 2937 O GLN A 380 -18.859 17.616 -4.879 1.00 84.24 O
ANISOU 2937 O GLN A 380 10325 12239 9443 -456 379 -214 O
ATOM 2938 CB GLN A 380 -17.884 14.596 -5.684 1.00 69.23 C
ANISOU 2938 CB GLN A 380 8473 10286 7546 -336 350 -180 C
ATOM 2939 CG GLN A 380 -17.676 13.217 -5.082 1.00 70.59 C
ANISOU 2939 CG GLN A 380 8724 10394 7701 -316 376 -151 C
ATOM 2940 CD GLN A 380 -17.183 13.275 -3.651 1.00 73.20 C
ANISOU 2940 CD GLN A 380 9139 10716 7956 -340 394 -92 C
ATOM 2941 OE1 GLN A 380 -16.840 14.343 -3.143 1.00 67.98 O
ANISOU 2941 OE1 GLN A 380 8474 10107 7250 -366 379 -70 O
ATOM 2942 NE2 GLN A 380 -17.143 12.123 -2.992 1.00 81.99 N
ANISOU 2942 NE2 GLN A 380 10335 11762 9054 -331 426 -65 N
ATOM 2943 N TYR A 381 -19.543 17.019 -6.940 1.00 63.39 N
ANISOU 2943 N TYR A 381 7587 9592 6907 -400 348 -292 N
ATOM 2944 CA TYR A 381 -19.658 18.402 -7.387 1.00 74.12 C
ANISOU 2944 CA TYR A 381 8890 11005 8267 -414 321 -310 C
ATOM 2945 C TYR A 381 -20.739 19.139 -6.604 1.00 77.16 C
ANISOU 2945 C TYR A 381 9286 11349 8684 -482 379 -343 C
ATOM 2946 O TYR A 381 -20.538 20.281 -6.177 1.00 71.74 O
ANISOU 2946 O TYR A 381 8598 10699 7960 -510 371 -327 O
ATOM 2947 CB TYR A 381 -19.955 18.437 -8.888 1.00 75.64 C
ANISOU 2947 CB TYR A 381 9009 11219 8513 -372 282 -358 C
ATOM 2948 CG TYR A 381 -19.533 19.705 -9.604 1.00 72.89 C
ANISOU 2948 CG TYR A 381 8609 10946 8140 -359 231 -355 C
ATOM 2949 CD1 TYR A 381 -19.080 20.814 -8.901 1.00 77.51 C
ANISOU 2949 CD1 TYR A 381 9209 11569 8671 -393 226 -320 C
ATOM 2950 CD2 TYR A 381 -19.592 19.790 -10.989 1.00 60.90 C
ANISOU 2950 CD2 TYR A 381 7032 9457 6651 -315 187 -388 C
ATOM 2951 CE1 TYR A 381 -18.700 21.972 -9.558 1.00 79.05 C
ANISOU 2951 CE1 TYR A 381 9362 11828 8846 -384 182 -317 C
ATOM 2952 CE2 TYR A 381 -19.212 20.941 -11.655 1.00 66.85 C
ANISOU 2952 CE2 TYR A 381 7746 10274 7380 -304 144 -383 C
ATOM 2953 CZ TYR A 381 -18.766 22.029 -10.935 1.00 81.75 C
ANISOU 2953 CZ TYR A 381 9649 12196 9216 -340 142 -347 C
ATOM 2954 OH TYR A 381 -18.387 23.175 -11.595 1.00 77.32 O
ANISOU 2954 OH TYR A 381 9053 11693 8630 -332 102 -341 O
ATOM 2955 N ASP A 382 -21.887 18.491 -6.392 1.00 75.30 N
ANISOU 2955 N ASP A 382 9058 11036 8516 -512 439 -391 N
ATOM 2956 CA ASP A 382 -22.987 19.141 -5.686 1.00 80.82 C
ANISOU 2956 CA ASP A 382 9760 11694 9252 -576 499 -429 C
ATOM 2957 C ASP A 382 -22.642 19.385 -4.222 1.00 71.96 C
ANISOU 2957 C ASP A 382 8716 10562 8063 -619 538 -379 C
ATOM 2958 O ASP A 382 -22.917 20.466 -3.687 1.00 73.09 O
ANISOU 2958 O ASP A 382 8859 10717 8194 -658 554 -385 O
ATOM 2959 CB ASP A 382 -24.257 18.299 -5.803 1.00 84.27 C
ANISOU 2959 CB ASP A 382 10186 12052 9780 -599 558 -493 C
ATOM 2960 CG ASP A 382 -24.711 18.122 -7.238 1.00 82.42 C
ANISOU 2960 CG ASP A 382 9874 11827 9615 -559 518 -551 C
ATOM 2961 OD1 ASP A 382 -24.469 19.033 -8.056 1.00 82.14 O
ANISOU 2961 OD1 ASP A 382 9785 11851 9572 -531 461 -559 O
ATOM 2962 OD2 ASP A 382 -25.306 17.069 -7.549 1.00 80.95 O
ANISOU 2962 OD2 ASP A 382 9682 11586 9488 -557 544 -589 O
ATOM 2963 N MET A 383 -22.043 18.394 -3.556 1.00 71.78 N
ANISOU 2963 N MET A 383 8764 10515 7996 -610 551 -331 N
ATOM 2964 CA MET A 383 -21.688 18.563 -2.151 1.00 73.06 C
ANISOU 2964 CA MET A 383 9007 10666 8088 -647 584 -282 C
ATOM 2965 C MET A 383 -20.623 19.635 -1.968 1.00 81.79 C
ANISOU 2965 C MET A 383 10109 11853 9114 -637 526 -236 C
ATOM 2966 O MET A 383 -20.527 20.238 -0.893 1.00 90.74 O
ANISOU 2966 O MET A 383 11292 12987 10197 -678 550 -212 O
ATOM 2967 CB MET A 383 -21.204 17.237 -1.561 1.00 68.13 C
ANISOU 2967 CB MET A 383 8461 9999 7426 -629 602 -237 C
ATOM 2968 CG MET A 383 -22.201 16.094 -1.666 1.00 70.80 C
ANISOU 2968 CG MET A 383 8812 10249 7838 -644 664 -279 C
ATOM 2969 SD MET A 383 -21.616 14.589 -0.859 1.00 69.53 S
ANISOU 2969 SD MET A 383 8761 10030 7626 -625 689 -220 S
ATOM 2970 CE MET A 383 -19.966 14.452 -1.543 1.00 67.23 C
ANISOU 2970 CE MET A 383 8452 9826 7266 -537 582 -162 C
ATOM 2971 N ALA A 384 -19.821 19.892 -3.003 1.00 83.92 N
ANISOU 2971 N ALA A 384 10322 12191 9372 -586 452 -224 N
ATOM 2972 CA ALA A 384 -18.723 20.843 -2.872 1.00 77.06 C
ANISOU 2972 CA ALA A 384 9448 11402 8429 -578 396 -179 C
ATOM 2973 C ALA A 384 -19.230 22.280 -2.848 1.00 78.59 C
ANISOU 2973 C ALA A 384 9610 11615 8636 -620 401 -209 C
ATOM 2974 O ALA A 384 -18.826 23.073 -1.990 1.00 86.81 O
ANISOU 2974 O ALA A 384 10685 12679 9618 -652 400 -180 O
ATOM 2975 CB ALA A 384 -17.717 20.640 -4.003 1.00 76.60 C
ANISOU 2975 CB ALA A 384 9339 11409 8356 -512 322 -159 C
ATOM 2976 N TYR A 385 -20.113 22.641 -3.781 1.00 72.04 N
ANISOU 2976 N TYR A 385 8718 10776 7880 -618 405 -267 N
ATOM 2977 CA TYR A 385 -20.645 23.996 -3.841 1.00 76.69 C
ANISOU 2977 CA TYR A 385 9275 11378 8485 -651 408 -298 C
ATOM 2978 C TYR A 385 -21.961 24.146 -3.083 1.00 83.22 C
ANISOU 2978 C TYR A 385 10122 12136 9361 -705 486 -345 C
ATOM 2979 O TYR A 385 -22.673 25.137 -3.283 1.00 81.68 O
ANISOU 2979 O TYR A 385 9892 11940 9202 -726 494 -387 O
ATOM 2980 CB TYR A 385 -20.807 24.460 -5.294 1.00 78.73 C
ANISOU 2980 CB TYR A 385 9455 11671 8788 -613 360 -334 C
ATOM 2981 CG TYR A 385 -21.709 23.624 -6.191 1.00 74.94 C
ANISOU 2981 CG TYR A 385 8932 11149 8392 -587 372 -390 C
ATOM 2982 CD1 TYR A 385 -23.057 23.447 -5.901 1.00 70.98 C
ANISOU 2982 CD1 TYR A 385 8426 10580 7962 -622 434 -448 C
ATOM 2983 CD2 TYR A 385 -21.216 23.058 -7.359 1.00 78.54 C
ANISOU 2983 CD2 TYR A 385 9350 11636 8856 -529 321 -388 C
ATOM 2984 CE1 TYR A 385 -23.877 22.700 -6.726 1.00 81.98 C
ANISOU 2984 CE1 TYR A 385 9776 11937 9434 -601 441 -504 C
ATOM 2985 CE2 TYR A 385 -22.030 22.311 -8.193 1.00 78.01 C
ANISOU 2985 CE2 TYR A 385 9246 11531 8863 -505 328 -442 C
ATOM 2986 CZ TYR A 385 -23.359 22.136 -7.871 1.00 83.45 C
ANISOU 2986 CZ TYR A 385 9929 12153 9625 -542 386 -501 C
ATOM 2987 OH TYR A 385 -24.171 21.395 -8.699 1.00 81.27 O
ANISOU 2987 OH TYR A 385 9612 11841 9426 -522 390 -559 O
ATOM 2988 N ALA A 386 -22.301 23.186 -2.220 1.00 79.10 N
ANISOU 2988 N ALA A 386 9656 11555 8841 -728 544 -339 N
ATOM 2989 CA ALA A 386 -23.527 23.302 -1.441 1.00 77.59 C
ANISOU 2989 CA ALA A 386 9486 11300 8696 -784 626 -383 C
ATOM 2990 C ALA A 386 -23.484 24.491 -0.490 1.00 82.67 C
ANISOU 2990 C ALA A 386 10164 11958 9291 -829 644 -371 C
ATOM 2991 O ALA A 386 -24.541 25.005 -0.104 1.00 82.96 O
ANISOU 2991 O ALA A 386 10193 11956 9371 -870 700 -419 O
ATOM 2992 CB ALA A 386 -23.781 22.009 -0.662 1.00 76.79 C
ANISOU 2992 CB ALA A 386 9450 11132 8596 -801 688 -371 C
ATOM 2993 N ALA A 387 -22.286 24.945 -0.112 1.00 79.80 N
ANISOU 2993 N ALA A 387 9833 11648 8838 -821 596 -311 N
ATOM 2994 CA ALA A 387 -22.140 26.109 0.751 1.00 67.89 C
ANISOU 2994 CA ALA A 387 8358 10159 7280 -863 604 -298 C
ATOM 2995 C ALA A 387 -22.418 27.418 0.025 1.00 78.21 C
ANISOU 2995 C ALA A 387 9603 11499 8616 -863 573 -334 C
ATOM 2996 O ALA A 387 -22.626 28.443 0.684 1.00 94.70 O
ANISOU 2996 O ALA A 387 11712 13586 10682 -902 593 -341 O
ATOM 2997 CB ALA A 387 -20.732 26.146 1.347 1.00 73.52 C
ANISOU 2997 CB ALA A 387 9122 10921 7890 -854 556 -226 C
ATOM 2998 N GLN A 388 -22.414 27.411 -1.306 1.00 83.22 N
ANISOU 2998 N GLN A 388 10165 12159 9295 -819 526 -355 N
ATOM 2999 CA GLN A 388 -22.695 28.612 -2.071 1.00 81.35 C
ANISOU 2999 CA GLN A 388 9874 11949 9085 -813 494 -387 C
ATOM 3000 C GLN A 388 -24.157 29.021 -1.902 1.00 72.80 C
ANISOU 3000 C GLN A 388 8771 10811 8077 -843 554 -456 C
ATOM 3001 O GLN A 388 -24.994 28.213 -1.491 1.00 67.09 O
ANISOU 3001 O GLN A 388 8059 10032 7401 -861 616 -486 O
ATOM 3002 CB GLN A 388 -22.385 28.382 -3.550 1.00 72.23 C
ANISOU 3002 CB GLN A 388 8653 10830 7959 -756 432 -394 C
ATOM 3003 CG GLN A 388 -20.914 28.165 -3.862 1.00 63.32 C
ANISOU 3003 CG GLN A 388 7532 9767 6761 -723 369 -330 C
ATOM 3004 CD GLN A 388 -20.085 29.424 -3.686 1.00 74.47 C
ANISOU 3004 CD GLN A 388 8952 11234 8110 -740 331 -297 C
ATOM 3005 OE1 GLN A 388 -20.619 30.532 -3.629 1.00 77.31 O
ANISOU 3005 OE1 GLN A 388 9304 11586 8484 -766 340 -325 O
ATOM 3006 NE2 GLN A 388 -18.770 29.258 -3.598 1.00 71.59 N
ANISOU 3006 NE2 GLN A 388 8602 10924 7676 -725 287 -239 N
ATOM 3007 N PRO A 389 -24.486 30.279 -2.198 1.00 67.92 N
ANISOU 3007 N PRO A 389 8126 10208 7474 -849 539 -484 N
ATOM 3008 CA PRO A 389 -25.897 30.678 -2.239 1.00 66.44 C
ANISOU 3008 CA PRO A 389 7905 9974 7367 -865 586 -557 C
ATOM 3009 C PRO A 389 -26.681 29.835 -3.235 1.00 76.38 C
ANISOU 3009 C PRO A 389 9101 11208 8713 -831 586 -607 C
ATOM 3010 O PRO A 389 -26.121 29.190 -4.124 1.00 79.21 O
ANISOU 3010 O PRO A 389 9435 11593 9069 -787 536 -589 O
ATOM 3011 CB PRO A 389 -25.840 32.147 -2.671 1.00 79.86 C
ANISOU 3011 CB PRO A 389 9583 11704 9057 -860 546 -567 C
ATOM 3012 CG PRO A 389 -24.501 32.613 -2.208 1.00 85.64 C
ANISOU 3012 CG PRO A 389 10363 12484 9691 -872 508 -498 C
ATOM 3013 CD PRO A 389 -23.582 31.432 -2.360 1.00 71.15 C
ANISOU 3013 CD PRO A 389 8540 10673 7822 -848 483 -449 C
ATOM 3014 N PHE A 390 -28.008 29.856 -3.076 1.00 76.62 N
ANISOU 3014 N PHE A 390 9103 11188 8821 -850 642 -675 N
ATOM 3015 CA PHE A 390 -28.867 28.963 -3.849 1.00 77.75 C
ANISOU 3015 CA PHE A 390 9189 11301 9054 -828 652 -731 C
ATOM 3016 C PHE A 390 -28.705 29.185 -5.349 1.00 79.88 C
ANISOU 3016 C PHE A 390 9394 11608 9347 -767 571 -746 C
ATOM 3017 O PHE A 390 -28.640 28.223 -6.125 1.00 78.99 O
ANISOU 3017 O PHE A 390 9254 11496 9262 -734 547 -754 O
ATOM 3018 CB PHE A 390 -30.328 29.153 -3.434 1.00 75.80 C
ANISOU 3018 CB PHE A 390 8913 11000 8889 -861 723 -807 C
ATOM 3019 CG PHE A 390 -31.292 28.285 -4.192 1.00 76.32 C
ANISOU 3019 CG PHE A 390 8912 11033 9052 -844 735 -873 C
ATOM 3020 CD1 PHE A 390 -31.535 26.982 -3.790 1.00 70.50 C
ANISOU 3020 CD1 PHE A 390 8194 10253 8341 -867 789 -876 C
ATOM 3021 CD2 PHE A 390 -31.959 28.773 -5.306 1.00 85.54 C
ANISOU 3021 CD2 PHE A 390 10002 12211 10287 -804 690 -932 C
ATOM 3022 CE1 PHE A 390 -32.422 26.181 -4.486 1.00 81.31 C
ANISOU 3022 CE1 PHE A 390 9502 11591 9803 -856 800 -940 C
ATOM 3023 CE2 PHE A 390 -32.846 27.977 -6.006 1.00 76.27 C
ANISOU 3023 CE2 PHE A 390 8765 11010 9204 -788 696 -997 C
ATOM 3024 CZ PHE A 390 -33.079 26.680 -5.596 1.00 75.60 C
ANISOU 3024 CZ PHE A 390 8696 10883 9147 -816 751 -1002 C
ATOM 3025 N LEU A 391 -28.631 30.444 -5.778 1.00 77.54 N
ANISOU 3025 N LEU A 391 9081 11344 9038 -752 528 -752 N
ATOM 3026 CA LEU A 391 -28.542 30.758 -7.198 1.00 75.35 C
ANISOU 3026 CA LEU A 391 8750 11100 8780 -695 454 -768 C
ATOM 3027 C LEU A 391 -27.166 30.486 -7.792 1.00 78.94 C
ANISOU 3027 C LEU A 391 9222 11610 9164 -662 392 -701 C
ATOM 3028 O LEU A 391 -27.001 30.617 -9.009 1.00 91.91 O
ANISOU 3028 O LEU A 391 10825 13281 10816 -613 332 -710 O
ATOM 3029 CB LEU A 391 -28.923 32.222 -7.431 1.00 73.92 C
ANISOU 3029 CB LEU A 391 8553 10928 8605 -690 432 -793 C
ATOM 3030 CG LEU A 391 -30.387 32.563 -7.146 1.00 75.61 C
ANISOU 3030 CG LEU A 391 8731 11093 8903 -706 481 -872 C
ATOM 3031 CD1 LEU A 391 -30.622 34.061 -7.222 1.00 84.25 C
ANISOU 3031 CD1 LEU A 391 9825 12196 9991 -700 461 -888 C
ATOM 3032 CD2 LEU A 391 -31.298 31.826 -8.114 1.00 64.55 C
ANISOU 3032 CD2 LEU A 391 7260 9674 7593 -669 468 -939 C
ATOM 3033 N LEU A 392 -26.180 30.108 -6.977 1.00 75.22 N
ANISOU 3033 N LEU A 392 8806 11154 8622 -685 404 -637 N
ATOM 3034 CA LEU A 392 -24.832 29.839 -7.460 1.00 70.73 C
ANISOU 3034 CA LEU A 392 8249 10640 7986 -655 348 -574 C
ATOM 3035 C LEU A 392 -24.446 28.370 -7.314 1.00 75.17 C
ANISOU 3035 C LEU A 392 8827 11190 8542 -644 361 -551 C
ATOM 3036 O LEU A 392 -23.257 28.039 -7.341 1.00 78.84 O
ANISOU 3036 O LEU A 392 9314 11697 8943 -627 328 -492 O
ATOM 3037 CB LEU A 392 -23.823 30.728 -6.731 1.00 77.14 C
ANISOU 3037 CB LEU A 392 9108 11490 8712 -684 336 -515 C
ATOM 3038 CG LEU A 392 -24.096 32.233 -6.788 1.00 73.11 C
ANISOU 3038 CG LEU A 392 8594 10988 8198 -698 324 -532 C
ATOM 3039 CD1 LEU A 392 -23.019 33.005 -6.042 1.00 83.36 C
ANISOU 3039 CD1 LEU A 392 9940 12323 9409 -731 312 -472 C
ATOM 3040 CD2 LEU A 392 -24.201 32.707 -8.227 1.00 68.17 C
ANISOU 3040 CD2 LEU A 392 7917 10386 7598 -649 267 -554 C
ATOM 3041 N ARG A 393 -25.430 27.482 -7.165 1.00 70.46 N
ANISOU 3041 N ARG A 393 8219 10538 8014 -653 409 -598 N
ATOM 3042 CA ARG A 393 -25.175 26.053 -6.983 1.00 73.32 C
ANISOU 3042 CA ARG A 393 8604 10877 8377 -645 428 -580 C
ATOM 3043 C ARG A 393 -25.355 25.347 -8.324 1.00 81.34 C
ANISOU 3043 C ARG A 393 9566 11898 9443 -592 388 -612 C
ATOM 3044 O ARG A 393 -26.404 24.779 -8.629 1.00 85.57 O
ANISOU 3044 O ARG A 393 10069 12388 10058 -592 414 -674 O
ATOM 3045 CB ARG A 393 -26.098 25.475 -5.916 1.00 69.46 C
ANISOU 3045 CB ARG A 393 8146 10319 7928 -696 513 -607 C
ATOM 3046 CG ARG A 393 -25.869 26.027 -4.526 1.00 73.06 C
ANISOU 3046 CG ARG A 393 8666 10768 8327 -747 556 -572 C
ATOM 3047 CD ARG A 393 -27.006 25.629 -3.606 1.00 85.66 C
ANISOU 3047 CD ARG A 393 10281 12292 9972 -798 646 -613 C
ATOM 3048 NE ARG A 393 -26.843 26.165 -2.261 1.00 84.86 N
ANISOU 3048 NE ARG A 393 10247 12182 9814 -848 692 -582 N
ATOM 3049 CZ ARG A 393 -27.774 26.110 -1.320 1.00 81.69 C
ANISOU 3049 CZ ARG A 393 9871 11726 9443 -899 775 -615 C
ATOM 3050 NH1 ARG A 393 -28.956 25.560 -1.549 1.00 72.35 N
ANISOU 3050 NH1 ARG A 393 8647 10491 8351 -911 825 -680 N
ATOM 3051 NH2 ARG A 393 -27.516 26.623 -0.120 1.00 85.89 N
ANISOU 3051 NH2 ARG A 393 10470 12254 9911 -940 810 -582 N
ATOM 3052 N ASN A 394 -24.297 25.377 -9.128 1.00 77.07 N
ANISOU 3052 N ASN A 394 9016 11414 8853 -546 323 -573 N
ATOM 3053 CA ASN A 394 -24.296 24.739 -10.438 1.00 77.61 C
ANISOU 3053 CA ASN A 394 9040 11494 8954 -490 279 -597 C
ATOM 3054 C ASN A 394 -22.858 24.702 -10.935 1.00 74.72 C
ANISOU 3054 C ASN A 394 8683 11194 8513 -450 223 -534 C
ATOM 3055 O ASN A 394 -21.955 25.268 -10.315 1.00 80.00 O
ANISOU 3055 O ASN A 394 9385 11900 9113 -467 215 -478 O
ATOM 3056 CB ASN A 394 -25.204 25.480 -11.425 1.00 72.52 C
ANISOU 3056 CB ASN A 394 8337 10851 8369 -470 252 -661 C
ATOM 3057 CG ASN A 394 -25.850 24.553 -12.434 1.00 81.28 C
ANISOU 3057 CG ASN A 394 9401 11935 9546 -432 237 -717 C
ATOM 3058 OD1 ASN A 394 -25.218 23.623 -12.935 1.00 91.10 O
ANISOU 3058 OD1 ASN A 394 10650 13192 10773 -397 214 -696 O
ATOM 3059 ND2 ASN A 394 -27.121 24.797 -12.730 1.00 75.65 N
ANISOU 3059 ND2 ASN A 394 8644 11188 8912 -438 249 -791 N
ATOM 3060 N GLY A 395 -22.654 24.021 -12.060 1.00 72.13 N
ANISOU 3060 N GLY A 395 8325 10882 8201 -396 184 -547 N
ATOM 3061 CA GLY A 395 -21.349 24.030 -12.691 1.00 68.96 C
ANISOU 3061 CA GLY A 395 7922 10545 7734 -354 131 -495 C
ATOM 3062 C GLY A 395 -20.970 25.412 -13.185 1.00 69.05 C
ANISOU 3062 C GLY A 395 7915 10611 7709 -350 92 -481 C
ATOM 3063 O GLY A 395 -21.806 26.306 -13.320 1.00 70.08 O
ANISOU 3063 O GLY A 395 8028 10726 7874 -367 95 -520 O
ATOM 3064 N ALA A 396 -19.672 25.586 -13.454 1.00 64.69 N
ANISOU 3064 N ALA A 396 7368 10122 7088 -328 55 -425 N
ATOM 3065 CA ALA A 396 -19.178 26.882 -13.914 1.00 59.01 C
ANISOU 3065 CA ALA A 396 6638 9455 6329 -329 20 -406 C
ATOM 3066 C ALA A 396 -19.895 27.321 -15.186 1.00 67.60 C
ANISOU 3066 C ALA A 396 7686 10541 7457 -295 -10 -456 C
ATOM 3067 O ALA A 396 -20.337 28.470 -15.298 1.00 72.46 O
ANISOU 3067 O ALA A 396 8298 11156 8079 -312 -16 -472 O
ATOM 3068 CB ALA A 396 -17.666 26.822 -14.132 1.00 59.82 C
ANISOU 3068 CB ALA A 396 6743 9628 6358 -308 -13 -343 C
ATOM 3069 N ASN A 397 -20.022 26.418 -16.155 1.00 67.71 N
ANISOU 3069 N ASN A 397 7675 10552 7499 -244 -31 -482 N
ATOM 3070 CA ASN A 397 -20.904 26.628 -17.296 1.00 66.05 C
ANISOU 3070 CA ASN A 397 7430 10328 7337 -210 -57 -541 C
ATOM 3071 C ASN A 397 -21.567 25.294 -17.625 1.00 72.11 C
ANISOU 3071 C ASN A 397 8181 11053 8165 -184 -49 -588 C
ATOM 3072 O ASN A 397 -21.451 24.319 -16.875 1.00 65.58 O
ANISOU 3072 O ASN A 397 7373 10198 7345 -199 -15 -576 O
ATOM 3073 CB ASN A 397 -20.148 27.246 -18.485 1.00 67.90 C
ANISOU 3073 CB ASN A 397 7653 10623 7523 -168 -109 -519 C
ATOM 3074 CG ASN A 397 -18.969 26.406 -18.947 1.00 75.47 C
ANISOU 3074 CG ASN A 397 8612 11628 8437 -130 -127 -479 C
ATOM 3075 OD1 ASN A 397 -19.024 25.177 -18.964 1.00 81.70 O
ANISOU 3075 OD1 ASN A 397 9398 12396 9250 -108 -119 -492 O
ATOM 3076 ND2 ASN A 397 -17.892 27.078 -19.339 1.00 72.77 N
ANISOU 3076 ND2 ASN A 397 8272 11348 8028 -121 -152 -431 N
ATOM 3077 N GLU A 398 -22.266 25.250 -18.762 1.00 71.68 N
ANISOU 3077 N GLU A 398 8092 10989 8152 -143 -80 -643 N
ATOM 3078 CA GLU A 398 -23.070 24.083 -19.106 1.00 70.41 C
ANISOU 3078 CA GLU A 398 7911 10782 8058 -124 -73 -701 C
ATOM 3079 C GLU A 398 -22.232 22.835 -19.354 1.00 65.49 C
ANISOU 3079 C GLU A 398 7300 10171 7411 -91 -79 -674 C
ATOM 3080 O GLU A 398 -22.759 21.722 -19.249 1.00 66.18 O
ANISOU 3080 O GLU A 398 7385 10211 7548 -89 -58 -708 O
ATOM 3081 CB GLU A 398 -23.926 24.388 -20.335 1.00 69.40 C
ANISOU 3081 CB GLU A 398 7745 10651 7974 -83 -116 -766 C
ATOM 3082 CG GLU A 398 -23.133 24.835 -21.549 1.00 57.96 C
ANISOU 3082 CG GLU A 398 6294 9262 6468 -29 -173 -742 C
ATOM 3083 CD GLU A 398 -24.025 25.302 -22.681 1.00 79.60 C
ANISOU 3083 CD GLU A 398 9004 11997 9244 10 -217 -804 C
ATOM 3084 OE1 GLU A 398 -25.206 25.609 -22.413 1.00 73.05 O
ANISOU 3084 OE1 GLU A 398 8153 11124 8479 -10 -207 -860 O
ATOM 3085 OE2 GLU A 398 -23.548 25.358 -23.835 1.00 82.73 O
ANISOU 3085 OE2 GLU A 398 9399 12432 9603 62 -264 -799 O
ATOM 3086 N GLY A 399 -20.949 22.985 -19.676 1.00 67.45 N
ANISOU 3086 N GLY A 399 7561 10481 7586 -64 -105 -615 N
ATOM 3087 CA GLY A 399 -20.106 21.836 -19.937 1.00 71.72 C
ANISOU 3087 CA GLY A 399 8111 11038 8102 -26 -112 -590 C
ATOM 3088 C GLY A 399 -19.284 21.345 -18.769 1.00 72.46 C
ANISOU 3088 C GLY A 399 8241 11133 8159 -52 -80 -531 C
ATOM 3089 O GLY A 399 -18.626 20.307 -18.882 1.00 73.71 O
ANISOU 3089 O GLY A 399 8409 11296 8300 -19 -83 -511 O
ATOM 3090 N PHE A 400 -19.311 22.057 -17.641 1.00 69.53 N
ANISOU 3090 N PHE A 400 7891 10756 7772 -107 -50 -504 N
ATOM 3091 CA PHE A 400 -18.451 21.704 -16.515 1.00 67.78 C
ANISOU 3091 CA PHE A 400 7707 10542 7505 -130 -27 -445 C
ATOM 3092 C PHE A 400 -18.945 20.450 -15.804 1.00 69.23 C
ANISOU 3092 C PHE A 400 7919 10658 7728 -141 14 -460 C
ATOM 3093 O PHE A 400 -18.163 19.531 -15.534 1.00 64.02 O
ANISOU 3093 O PHE A 400 7284 10003 7039 -118 15 -424 O
ATOM 3094 CB PHE A 400 -18.368 22.873 -15.535 1.00 71.43 C
ANISOU 3094 CB PHE A 400 8187 11016 7936 -186 -9 -416 C
ATOM 3095 CG PHE A 400 -17.119 23.692 -15.671 1.00 70.87 C
ANISOU 3095 CG PHE A 400 8114 11023 7792 -181 -41 -359 C
ATOM 3096 CD1 PHE A 400 -16.954 24.556 -16.740 1.00 63.58 C
ANISOU 3096 CD1 PHE A 400 7161 10143 6854 -159 -78 -366 C
ATOM 3097 CD2 PHE A 400 -16.112 23.604 -14.724 1.00 61.08 C
ANISOU 3097 CD2 PHE A 400 6903 9810 6495 -199 -35 -301 C
ATOM 3098 CE1 PHE A 400 -15.806 25.315 -16.865 1.00 65.32 C
ANISOU 3098 CE1 PHE A 400 7379 10432 7008 -160 -102 -316 C
ATOM 3099 CE2 PHE A 400 -14.962 24.360 -14.843 1.00 63.31 C
ANISOU 3099 CE2 PHE A 400 7176 10166 6714 -198 -64 -253 C
ATOM 3100 CZ PHE A 400 -14.808 25.216 -15.915 1.00 67.61 C
ANISOU 3100 CZ PHE A 400 7689 10752 7247 -181 -94 -261 C
ATOM 3101 N HIS A 401 -20.241 20.401 -15.485 1.00 70.50 N
ANISOU 3101 N HIS A 401 8077 10755 7957 -177 50 -514 N
ATOM 3102 CA HIS A 401 -20.760 19.310 -14.666 1.00 67.80 C
ANISOU 3102 CA HIS A 401 7767 10342 7651 -201 100 -526 C
ATOM 3103 C HIS A 401 -20.569 17.961 -15.347 1.00 68.91 C
ANISOU 3103 C HIS A 401 7909 10465 7810 -151 88 -539 C
ATOM 3104 O HIS A 401 -20.127 16.995 -14.714 1.00 64.89 O
ANISOU 3104 O HIS A 401 7441 9929 7284 -148 110 -508 O
ATOM 3105 CB HIS A 401 -22.237 19.548 -14.350 1.00 66.12 C
ANISOU 3105 CB HIS A 401 7540 10067 7515 -248 142 -590 C
ATOM 3106 CG HIS A 401 -22.564 19.452 -12.893 1.00 68.59 C
ANISOU 3106 CG HIS A 401 7899 10333 7829 -309 205 -574 C
ATOM 3107 ND1 HIS A 401 -22.563 18.256 -12.208 1.00 67.06 N
ANISOU 3107 ND1 HIS A 401 7750 10087 7643 -320 247 -561 N
ATOM 3108 CD2 HIS A 401 -22.899 20.402 -11.989 1.00 73.86 C
ANISOU 3108 CD2 HIS A 401 8580 10995 8488 -361 237 -567 C
ATOM 3109 CE1 HIS A 401 -22.884 18.474 -10.945 1.00 75.89 C
ANISOU 3109 CE1 HIS A 401 8910 11171 8754 -378 302 -547 C
ATOM 3110 NE2 HIS A 401 -23.094 19.768 -10.786 1.00 76.58 N
ANISOU 3110 NE2 HIS A 401 8978 11288 8833 -403 297 -552 N
ATOM 3111 N GLU A 402 -20.886 17.876 -16.640 1.00 76.12 N
ANISOU 3111 N GLU A 402 8778 11389 8755 -109 50 -586 N
ATOM 3112 CA GLU A 402 -20.748 16.604 -17.337 1.00 80.48 C
ANISOU 3112 CA GLU A 402 9332 11922 9327 -60 37 -604 C
ATOM 3113 C GLU A 402 -19.285 16.254 -17.585 1.00 74.11 C
ANISOU 3113 C GLU A 402 8540 11172 8446 -9 5 -543 C
ATOM 3114 O GLU A 402 -18.948 15.072 -17.714 1.00 77.85 O
ANISOU 3114 O GLU A 402 9034 11623 8921 25 7 -538 O
ATOM 3115 CB GLU A 402 -21.523 16.640 -18.653 1.00 92.24 C
ANISOU 3115 CB GLU A 402 10772 13408 10868 -29 3 -675 C
ATOM 3116 CG GLU A 402 -21.970 15.271 -19.135 1.00 89.34 C
ANISOU 3116 CG GLU A 402 10406 12986 10553 -4 8 -722 C
ATOM 3117 CD GLU A 402 -22.961 14.623 -18.188 1.00 99.29 C
ANISOU 3117 CD GLU A 402 11686 14161 11877 -61 70 -754 C
ATOM 3118 OE1 GLU A 402 -23.846 15.337 -17.671 1.00101.33 O
ANISOU 3118 OE1 GLU A 402 11929 14398 12173 -112 98 -781 O
ATOM 3119 OE2 GLU A 402 -22.850 13.402 -17.951 1.00104.43 O
ANISOU 3119 OE2 GLU A 402 12372 14766 12542 -54 94 -751 O
ATOM 3120 N ALA A 403 -18.406 17.258 -17.649 1.00 73.05 N
ANISOU 3120 N ALA A 403 8396 11111 8249 -4 -22 -496 N
ATOM 3121 CA ALA A 403 -16.985 16.977 -17.826 1.00 69.77 C
ANISOU 3121 CA ALA A 403 7987 10756 7765 42 -50 -439 C
ATOM 3122 C ALA A 403 -16.384 16.367 -16.567 1.00 76.95 C
ANISOU 3122 C ALA A 403 8946 11647 8643 26 -22 -386 C
ATOM 3123 O ALA A 403 -15.490 15.517 -16.649 1.00 72.25 O
ANISOU 3123 O ALA A 403 8367 11069 8017 72 -36 -355 O
ATOM 3124 CB ALA A 403 -16.237 18.253 -18.213 1.00 63.52 C
ANISOU 3124 CB ALA A 403 7170 10047 6919 44 -83 -406 C
ATOM 3125 N VAL A 404 -16.860 16.791 -15.395 1.00 79.46 N
ANISOU 3125 N VAL A 404 9293 11931 8966 -36 16 -377 N
ATOM 3126 CA VAL A 404 -16.361 16.233 -14.142 1.00 72.67 C
ANISOU 3126 CA VAL A 404 8489 11050 8072 -53 43 -327 C
ATOM 3127 C VAL A 404 -16.754 14.766 -14.019 1.00 70.18 C
ANISOU 3127 C VAL A 404 8209 10660 7796 -35 70 -346 C
ATOM 3128 O VAL A 404 -15.974 13.939 -13.532 1.00 65.93 O
ANISOU 3128 O VAL A 404 7711 10117 7221 -8 70 -304 O
ATOM 3129 CB VAL A 404 -16.870 17.066 -12.951 1.00 68.90 C
ANISOU 3129 CB VAL A 404 8037 10551 7592 -126 80 -318 C
ATOM 3130 CG1 VAL A 404 -16.496 16.407 -11.632 1.00 57.86 C
ANISOU 3130 CG1 VAL A 404 6705 9119 6159 -144 112 -272 C
ATOM 3131 CG2 VAL A 404 -16.308 18.478 -13.018 1.00 70.83 C
ANISOU 3131 CG2 VAL A 404 8254 10869 7790 -141 51 -292 C
ATOM 3132 N GLY A 405 -17.960 14.415 -14.470 1.00 70.41 N
ANISOU 3132 N GLY A 405 8223 10629 7900 -49 92 -413 N
ATOM 3133 CA GLY A 405 -18.383 13.028 -14.414 1.00 71.49 C
ANISOU 3133 CA GLY A 405 8394 10692 8079 -37 120 -436 C
ATOM 3134 C GLY A 405 -17.643 12.133 -15.387 1.00 76.93 C
ANISOU 3134 C GLY A 405 9074 11401 8755 39 80 -434 C
ATOM 3135 O GLY A 405 -17.447 10.945 -15.114 1.00 75.48 O
ANISOU 3135 O GLY A 405 8935 11169 8574 61 96 -423 O
ATOM 3136 N GLU A 406 -17.217 12.683 -16.528 1.00 81.46 N
ANISOU 3136 N GLU A 406 9595 12043 9312 81 31 -443 N
ATOM 3137 CA GLU A 406 -16.560 11.865 -17.545 1.00 88.34 C
ANISOU 3137 CA GLU A 406 10456 12937 10173 155 -5 -447 C
ATOM 3138 C GLU A 406 -15.169 11.429 -17.102 1.00 82.95 C
ANISOU 3138 C GLU A 406 9802 12294 9421 197 -20 -378 C
ATOM 3139 O GLU A 406 -14.769 10.284 -17.340 1.00 89.60 O
ANISOU 3139 O GLU A 406 10669 13114 10263 248 -25 -375 O
ATOM 3140 CB GLU A 406 -16.483 12.630 -18.866 1.00 84.07 C
ANISOU 3140 CB GLU A 406 9855 12461 9627 187 -50 -475 C
ATOM 3141 CG GLU A 406 -17.803 12.726 -19.614 1.00 82.02 C
ANISOU 3141 CG GLU A 406 9564 12159 9439 171 -49 -554 C
ATOM 3142 CD GLU A 406 -18.215 11.411 -20.244 1.00 82.83 C
ANISOU 3142 CD GLU A 406 9676 12206 9590 207 -49 -603 C
ATOM 3143 OE1 GLU A 406 -17.332 10.558 -20.476 1.00 84.69 O
ANISOU 3143 OE1 GLU A 406 9933 12453 9794 261 -62 -576 O
ATOM 3144 OE2 GLU A 406 -19.422 11.231 -20.506 1.00 87.59 O
ANISOU 3144 OE2 GLU A 406 10265 12753 10264 181 -36 -670 O
ATOM 3145 N ILE A 407 -14.417 12.324 -16.457 1.00 64.13 N
ANISOU 3145 N ILE A 407 7417 9970 6980 178 -29 -324 N
ATOM 3146 CA ILE A 407 -13.046 12.001 -16.079 1.00 68.09 C
ANISOU 3146 CA ILE A 407 7936 10521 7415 221 -51 -260 C
ATOM 3147 C ILE A 407 -12.992 10.948 -14.982 1.00 72.45 C
ANISOU 3147 C ILE A 407 8559 11007 7963 219 -21 -233 C
ATOM 3148 O ILE A 407 -11.938 10.341 -14.763 1.00 66.23 O
ANISOU 3148 O ILE A 407 7791 10243 7130 270 -41 -189 O
ATOM 3149 CB ILE A 407 -12.288 13.268 -15.644 1.00 65.78 C
ANISOU 3149 CB ILE A 407 7621 10308 7065 195 -69 -214 C
ATOM 3150 CG1 ILE A 407 -12.827 13.788 -14.312 1.00 70.21 C
ANISOU 3150 CG1 ILE A 407 8220 10831 7624 121 -33 -198 C
ATOM 3151 CG2 ILE A 407 -12.406 14.342 -16.706 1.00 65.93 C
ANISOU 3151 CG2 ILE A 407 7579 10384 7087 192 -94 -240 C
ATOM 3152 CD1 ILE A 407 -12.157 15.058 -13.841 1.00 57.66 C
ANISOU 3152 CD1 ILE A 407 6613 9314 5981 89 -50 -158 C
ATOM 3153 N MET A 408 -14.104 10.714 -14.280 1.00 69.43 N
ANISOU 3153 N MET A 408 8216 10540 7627 163 28 -258 N
ATOM 3154 CA MET A 408 -14.117 9.677 -13.255 1.00 68.26 C
ANISOU 3154 CA MET A 408 8144 10319 7474 158 61 -232 C
ATOM 3155 C MET A 408 -14.142 8.289 -13.881 1.00 75.63 C
ANISOU 3155 C MET A 408 9098 11201 8437 214 60 -256 C
ATOM 3156 O MET A 408 -13.418 7.389 -13.440 1.00 72.97 O
ANISOU 3156 O MET A 408 8812 10847 8068 257 56 -216 O
ATOM 3157 CB MET A 408 -15.313 9.876 -12.324 1.00 74.29 C
ANISOU 3157 CB MET A 408 8943 11008 8276 76 121 -253 C
ATOM 3158 CG MET A 408 -15.417 11.284 -11.762 1.00 81.41 C
ANISOU 3158 CG MET A 408 9824 11955 9154 20 125 -238 C
ATOM 3159 SD MET A 408 -13.877 11.848 -11.009 1.00 79.27 S
ANISOU 3159 SD MET A 408 9566 11769 8783 40 85 -155 S
ATOM 3160 CE MET A 408 -14.267 13.566 -10.693 1.00 59.99 C
ANISOU 3160 CE MET A 408 7088 9371 6333 -31 90 -161 C
ATOM 3161 N SER A 409 -14.965 8.098 -14.914 1.00 81.38 N
ANISOU 3161 N SER A 409 9790 11903 9228 217 62 -322 N
ATOM 3162 CA SER A 409 -14.974 6.828 -15.629 1.00 76.01 C
ANISOU 3162 CA SER A 409 9125 11178 8576 272 56 -350 C
ATOM 3163 C SER A 409 -13.701 6.616 -16.437 1.00 74.28 C
ANISOU 3163 C SER A 409 8879 11034 8308 358 3 -324 C
ATOM 3164 O SER A 409 -13.391 5.473 -16.788 1.00 86.61 O
ANISOU 3164 O SER A 409 10469 12563 9876 414 -4 -329 O
ATOM 3165 CB SER A 409 -16.199 6.747 -16.542 1.00 69.05 C
ANISOU 3165 CB SER A 409 8208 10255 7774 250 66 -433 C
ATOM 3166 OG SER A 409 -16.263 7.861 -17.414 1.00 87.58 O
ANISOU 3166 OG SER A 409 10482 12675 10120 251 32 -457 O
ATOM 3167 N LEU A 410 -12.960 7.686 -16.738 1.00 70.95 N
ANISOU 3167 N LEU A 410 8406 10712 7841 369 -33 -298 N
ATOM 3168 CA LEU A 410 -11.687 7.534 -17.436 1.00 70.42 C
ANISOU 3168 CA LEU A 410 8310 10722 7724 447 -79 -271 C
ATOM 3169 C LEU A 410 -10.672 6.799 -16.571 1.00 81.85 C
ANISOU 3169 C LEU A 410 9807 12169 9123 487 -84 -211 C
ATOM 3170 O LEU A 410 -10.034 5.841 -17.022 1.00 84.89 O
ANISOU 3170 O LEU A 410 10204 12554 9499 560 -102 -207 O
ATOM 3171 CB LEU A 410 -11.146 8.903 -17.850 1.00 62.63 C
ANISOU 3171 CB LEU A 410 7259 9839 6699 438 -109 -255 C
ATOM 3172 CG LEU A 410 -11.775 9.569 -19.073 1.00 69.10 C
ANISOU 3172 CG LEU A 410 8023 10682 7550 432 -122 -310 C
ATOM 3173 CD1 LEU A 410 -11.103 10.905 -19.350 1.00 62.80 C
ANISOU 3173 CD1 LEU A 410 7174 9983 6705 423 -148 -283 C
ATOM 3174 CD2 LEU A 410 -11.680 8.656 -20.286 1.00 66.47 C
ANISOU 3174 CD2 LEU A 410 7678 10342 7235 502 -141 -349 C
ATOM 3175 N SER A 411 -10.506 7.237 -15.320 1.00 72.52 N
ANISOU 3175 N SER A 411 8658 10988 7909 443 -70 -164 N
ATOM 3176 CA SER A 411 -9.542 6.590 -14.436 1.00 77.97 C
ANISOU 3176 CA SER A 411 9398 11678 8548 483 -80 -106 C
ATOM 3177 C SER A 411 -10.039 5.224 -13.980 1.00 78.91 C
ANISOU 3177 C SER A 411 9600 11687 8697 495 -47 -112 C
ATOM 3178 O SER A 411 -9.252 4.277 -13.868 1.00 81.25 O
ANISOU 3178 O SER A 411 9931 11974 8965 563 -64 -84 O
ATOM 3179 CB SER A 411 -9.252 7.484 -13.230 1.00 72.27 C
ANISOU 3179 CB SER A 411 8692 10989 7780 431 -77 -57 C
ATOM 3180 OG SER A 411 -8.715 8.733 -13.630 1.00 75.27 O
ANISOU 3180 OG SER A 411 8999 11468 8131 419 -108 -48 O
ATOM 3181 N ALA A 412 -11.343 5.101 -13.720 1.00 78.28 N
ANISOU 3181 N ALA A 412 9550 11520 8673 430 2 -151 N
ATOM 3182 CA ALA A 412 -11.888 3.855 -13.193 1.00 78.47 C
ANISOU 3182 CA ALA A 412 9658 11432 8726 427 43 -157 C
ATOM 3183 C ALA A 412 -11.851 2.720 -14.208 1.00 81.96 C
ANISOU 3183 C ALA A 412 10102 11838 9201 493 31 -194 C
ATOM 3184 O ALA A 412 -11.928 1.553 -13.812 1.00 93.60 O
ANISOU 3184 O ALA A 412 11651 13229 10684 514 54 -186 O
ATOM 3185 CB ALA A 412 -13.323 4.073 -12.712 1.00 80.15 C
ANISOU 3185 CB ALA A 412 9892 11566 8996 334 103 -196 C
ATOM 3186 N ALA A 413 -11.733 3.030 -15.499 1.00 77.47 N
ANISOU 3186 N ALA A 413 9458 11328 8648 527 -2 -233 N
ATOM 3187 CA ALA A 413 -11.734 2.009 -16.538 1.00 80.52 C
ANISOU 3187 CA ALA A 413 9844 11684 9065 589 -14 -274 C
ATOM 3188 C ALA A 413 -10.339 1.545 -16.932 1.00 83.81 C
ANISOU 3188 C ALA A 413 10254 12162 9428 688 -60 -238 C
ATOM 3189 O ALA A 413 -10.218 0.549 -17.653 1.00 96.62 O
ANISOU 3189 O ALA A 413 11890 13752 11069 748 -68 -265 O
ATOM 3190 CB ALA A 413 -12.465 2.522 -17.784 1.00 72.81 C
ANISOU 3190 CB ALA A 413 8797 10730 8137 574 -24 -344 C
ATOM 3191 N THR A 414 -9.291 2.234 -16.487 1.00 84.99 N
ANISOU 3191 N THR A 414 10379 12400 9514 706 -89 -181 N
ATOM 3192 CA THR A 414 -7.939 1.846 -16.850 1.00 83.43 C
ANISOU 3192 CA THR A 414 10163 12269 9268 799 -132 -149 C
ATOM 3193 C THR A 414 -7.589 0.492 -16.235 1.00 75.41 C
ANISOU 3193 C THR A 414 9233 11178 8242 853 -126 -122 C
ATOM 3194 O THR A 414 -8.106 0.129 -15.176 1.00 82.85 O
ANISOU 3194 O THR A 414 10251 12038 9190 811 -92 -102 O
ATOM 3195 CB THR A 414 -6.932 2.894 -16.384 1.00 78.88 C
ANISOU 3195 CB THR A 414 9542 11800 8629 798 -162 -95 C
ATOM 3196 OG1 THR A 414 -6.977 3.001 -14.955 1.00 81.55 O
ANISOU 3196 OG1 THR A 414 9940 12105 8942 754 -146 -48 O
ATOM 3197 CG2 THR A 414 -7.247 4.247 -16.999 1.00 66.49 C
ANISOU 3197 CG2 THR A 414 7894 10301 7067 745 -168 -119 C
ATOM 3198 N PRO A 415 -6.720 -0.282 -16.890 1.00 77.92 N
ANISOU 3198 N PRO A 415 9544 11519 8543 948 -156 -121 N
ATOM 3199 CA PRO A 415 -6.285 -1.552 -16.287 1.00 93.65 C
ANISOU 3199 CA PRO A 415 11620 13442 10521 1009 -155 -90 C
ATOM 3200 C PRO A 415 -5.516 -1.358 -14.994 1.00 88.89 C
ANISOU 3200 C PRO A 415 11053 12864 9858 1014 -170 -18 C
ATOM 3201 O PRO A 415 -5.572 -2.224 -14.112 1.00 78.38 O
ANISOU 3201 O PRO A 415 9814 11448 8517 1026 -154 11 O
ATOM 3202 CB PRO A 415 -5.406 -2.178 -17.379 1.00 84.82 C
ANISOU 3202 CB PRO A 415 10466 12368 9392 1114 -191 -106 C
ATOM 3203 CG PRO A 415 -5.780 -1.470 -18.641 1.00 79.21 C
ANISOU 3203 CG PRO A 415 9672 11714 8710 1095 -196 -161 C
ATOM 3204 CD PRO A 415 -6.151 -0.083 -18.232 1.00 76.56 C
ANISOU 3204 CD PRO A 415 9293 11430 8368 1007 -189 -150 C
ATOM 3205 N LYS A 416 -4.796 -0.242 -14.859 1.00 86.52 N
ANISOU 3205 N LYS A 416 10684 12676 9514 1004 -200 12 N
ATOM 3206 CA LYS A 416 -4.094 0.053 -13.614 1.00 77.70 C
ANISOU 3206 CA LYS A 416 9595 11587 8338 1002 -218 76 C
ATOM 3207 C LYS A 416 -5.062 0.125 -12.440 1.00 88.08 C
ANISOU 3207 C LYS A 416 10992 12814 9662 917 -173 91 C
ATOM 3208 O LYS A 416 -4.762 -0.365 -11.345 1.00 84.33 O
ANISOU 3208 O LYS A 416 10596 12297 9150 931 -174 138 O
ATOM 3209 CB LYS A 416 -3.321 1.364 -13.759 1.00 84.91 C
ANISOU 3209 CB LYS A 416 10413 12634 9214 988 -253 95 C
ATOM 3210 CG LYS A 416 -2.800 1.948 -12.458 1.00 79.66 C
ANISOU 3210 CG LYS A 416 9770 12004 8494 961 -270 153 C
ATOM 3211 CD LYS A 416 -2.203 3.327 -12.693 1.00 86.17 C
ANISOU 3211 CD LYS A 416 10497 12953 9292 931 -298 161 C
ATOM 3212 CE LYS A 416 -1.819 4.001 -11.386 1.00113.66 C
ANISOU 3212 CE LYS A 416 13999 16464 12721 890 -312 211 C
ATOM 3213 NZ LYS A 416 -0.747 3.259 -10.668 1.00114.72 N
ANISOU 3213 NZ LYS A 416 14171 16611 12805 969 -353 260 N
ATOM 3214 N HIS A 417 -6.233 0.727 -12.651 1.00 85.49 N
ANISOU 3214 N HIS A 417 10647 12454 9381 829 -133 49 N
ATOM 3215 CA HIS A 417 -7.223 0.823 -11.585 1.00 82.40 C
ANISOU 3215 CA HIS A 417 10326 11979 9003 743 -83 56 C
ATOM 3216 C HIS A 417 -7.972 -0.491 -11.397 1.00 81.71 C
ANISOU 3216 C HIS A 417 10333 11758 8955 746 -39 39 C
ATOM 3217 O HIS A 417 -8.213 -0.914 -10.261 1.00 74.90 O
ANISOU 3217 O HIS A 417 9563 10821 8074 721 -9 73 O
ATOM 3218 CB HIS A 417 -8.206 1.955 -11.882 1.00 79.85 C
ANISOU 3218 CB HIS A 417 9946 11673 8720 652 -56 15 C
ATOM 3219 CG HIS A 417 -9.192 2.199 -10.783 1.00 78.98 C
ANISOU 3219 CG HIS A 417 9898 11489 8622 561 -2 20 C
ATOM 3220 ND1 HIS A 417 -8.912 3.002 -9.698 1.00 77.84 N
ANISOU 3220 ND1 HIS A 417 9770 11380 8427 520 -4 66 N
ATOM 3221 CD2 HIS A 417 -10.452 1.742 -10.597 1.00 84.11 C
ANISOU 3221 CD2 HIS A 417 10597 12034 9329 502 58 -17 C
ATOM 3222 CE1 HIS A 417 -9.959 3.033 -8.894 1.00 83.99 C
ANISOU 3222 CE1 HIS A 417 10607 12077 9228 441 54 58 C
ATOM 3223 NE2 HIS A 417 -10.907 2.275 -9.416 1.00 85.93 N
ANISOU 3223 NE2 HIS A 417 10871 12237 9541 428 94 8 N
ATOM 3224 N LEU A 418 -8.348 -1.147 -12.499 1.00 83.81 N
ANISOU 3224 N LEU A 418 10580 11991 9274 776 -34 -15 N
ATOM 3225 CA LEU A 418 -9.102 -2.393 -12.397 1.00 88.32 C
ANISOU 3225 CA LEU A 418 11238 12432 9889 774 9 -38 C
ATOM 3226 C LEU A 418 -8.285 -3.495 -11.735 1.00 88.93 C
ANISOU 3226 C LEU A 418 11406 12463 9921 850 -4 14 C
ATOM 3227 O LEU A 418 -8.854 -4.389 -11.097 1.00 81.59 O
ANISOU 3227 O LEU A 418 10577 11417 9007 830 40 20 O
ATOM 3228 CB LEU A 418 -9.575 -2.833 -13.783 1.00 77.01 C
ANISOU 3228 CB LEU A 418 9760 10981 8518 796 9 -110 C
ATOM 3229 CG LEU A 418 -10.619 -1.926 -14.436 1.00 84.57 C
ANISOU 3229 CG LEU A 418 10645 11958 9531 718 28 -170 C
ATOM 3230 CD1 LEU A 418 -10.980 -2.424 -15.828 1.00 75.22 C
ANISOU 3230 CD1 LEU A 418 9421 10761 8400 751 18 -240 C
ATOM 3231 CD2 LEU A 418 -11.858 -1.827 -13.558 1.00 71.18 C
ANISOU 3231 CD2 LEU A 418 8999 10173 7874 616 91 -183 C
ATOM 3232 N LYS A 419 -6.958 -3.453 -11.870 1.00 84.58 N
ANISOU 3232 N LYS A 419 10823 12000 9315 937 -64 52 N
ATOM 3233 CA LYS A 419 -6.119 -4.444 -11.206 1.00 80.28 C
ANISOU 3233 CA LYS A 419 10361 11419 8722 1018 -84 105 C
ATOM 3234 C LYS A 419 -5.920 -4.126 -9.731 1.00 96.12 C
ANISOU 3234 C LYS A 419 12433 13416 10671 985 -80 169 C
ATOM 3235 O LYS A 419 -5.744 -5.045 -8.923 1.00100.21 O
ANISOU 3235 O LYS A 419 13058 13855 11161 1019 -72 208 O
ATOM 3236 CB LYS A 419 -4.763 -4.547 -11.906 1.00 71.65 C
ANISOU 3236 CB LYS A 419 9204 10426 7595 1128 -151 117 C
ATOM 3237 CG LYS A 419 -4.830 -5.161 -13.292 1.00 94.82 C
ANISOU 3237 CG LYS A 419 12098 13353 10575 1182 -156 60 C
ATOM 3238 CD LYS A 419 -3.470 -5.156 -13.966 1.00 89.32 C
ANISOU 3238 CD LYS A 419 11331 12766 9842 1287 -216 72 C
ATOM 3239 CE LYS A 419 -3.572 -5.647 -15.398 1.00106.71 C
ANISOU 3239 CE LYS A 419 13489 14968 12087 1334 -218 11 C
ATOM 3240 NZ LYS A 419 -2.249 -5.672 -16.079 1.00122.17 N
ANISOU 3240 NZ LYS A 419 15377 17032 14010 1438 -271 20 N
ATOM 3241 N SER A 420 -5.948 -2.846 -9.360 1.00 91.91 N
ANISOU 3241 N SER A 420 11843 12960 10117 921 -85 180 N
ATOM 3242 CA SER A 420 -5.758 -2.457 -7.969 1.00 88.68 C
ANISOU 3242 CA SER A 420 11495 12550 9650 887 -83 238 C
ATOM 3243 C SER A 420 -6.980 -2.731 -7.102 1.00 78.97 C
ANISOU 3243 C SER A 420 10364 11198 8443 799 -9 235 C
ATOM 3244 O SER A 420 -6.876 -2.641 -5.874 1.00 90.82 O
ANISOU 3244 O SER A 420 11939 12675 9892 777 0 285 O
ATOM 3245 CB SER A 420 -5.390 -0.973 -7.880 1.00 83.03 C
ANISOU 3245 CB SER A 420 10687 11956 8906 845 -112 247 C
ATOM 3246 OG SER A 420 -6.457 -0.151 -8.318 1.00 87.18 O
ANISOU 3246 OG SER A 420 11160 12480 9486 753 -71 198 O
ATOM 3247 N ILE A 421 -8.126 -3.059 -7.699 1.00 83.81 N
ANISOU 3247 N ILE A 421 10978 11735 9132 749 45 177 N
ATOM 3248 CA ILE A 421 -9.343 -3.351 -6.951 1.00 69.63 C
ANISOU 3248 CA ILE A 421 9267 9821 7367 662 123 167 C
ATOM 3249 C ILE A 421 -9.748 -4.811 -7.047 1.00 73.26 C
ANISOU 3249 C ILE A 421 9821 10153 7861 689 159 154 C
ATOM 3250 O ILE A 421 -10.788 -5.191 -6.487 1.00 66.75 O
ANISOU 3250 O ILE A 421 9072 9222 7069 615 230 142 O
ATOM 3251 CB ILE A 421 -10.507 -2.445 -7.394 1.00 65.55 C
ANISOU 3251 CB ILE A 421 8677 9312 6915 562 164 106 C
ATOM 3252 CG1 ILE A 421 -10.929 -2.774 -8.828 1.00 81.68 C
ANISOU 3252 CG1 ILE A 421 10652 11351 9031 581 161 36 C
ATOM 3253 CG2 ILE A 421 -10.116 -0.979 -7.267 1.00 64.21 C
ANISOU 3253 CG2 ILE A 421 8424 9263 6711 533 131 121 C
ATOM 3254 CD1 ILE A 421 -12.122 -1.978 -9.313 1.00 69.37 C
ANISOU 3254 CD1 ILE A 421 9023 9793 7540 490 198 -28 C
ATOM 3255 N GLY A 422 -8.972 -5.640 -7.739 1.00 77.02 N
ANISOU 3255 N GLY A 422 10295 10636 8332 790 115 155 N
ATOM 3256 CA GLY A 422 -9.224 -7.065 -7.785 1.00 84.63 C
ANISOU 3256 CA GLY A 422 11357 11477 9320 825 144 148 C
ATOM 3257 C GLY A 422 -10.193 -7.536 -8.847 1.00 82.10 C
ANISOU 3257 C GLY A 422 11008 11095 9089 795 180 70 C
ATOM 3258 O GLY A 422 -10.625 -8.693 -8.792 1.00 89.50 O
ANISOU 3258 O GLY A 422 12035 11913 10056 801 218 58 O
ATOM 3259 N LEU A 423 -10.551 -6.686 -9.809 1.00 79.32 N
ANISOU 3259 N LEU A 423 10538 10818 8781 763 169 14 N
ATOM 3260 CA LEU A 423 -11.450 -7.089 -10.883 1.00 82.27 C
ANISOU 3260 CA LEU A 423 10876 11143 9239 738 194 -65 C
ATOM 3261 C LEU A 423 -10.722 -7.546 -12.137 1.00 86.44 C
ANISOU 3261 C LEU A 423 11352 11719 9773 838 139 -92 C
ATOM 3262 O LEU A 423 -11.285 -8.321 -12.917 1.00 89.14 O
ANISOU 3262 O LEU A 423 11703 11992 10174 843 157 -149 O
ATOM 3263 CB LEU A 423 -12.400 -5.943 -11.246 1.00 83.50 C
ANISOU 3263 CB LEU A 423 10940 11343 9443 645 216 -117 C
ATOM 3264 CG LEU A 423 -13.496 -5.636 -10.226 1.00 73.98 C
ANISOU 3264 CG LEU A 423 9782 10067 8261 532 288 -117 C
ATOM 3265 CD1 LEU A 423 -14.454 -4.590 -10.774 1.00 81.86 C
ANISOU 3265 CD1 LEU A 423 10680 11107 9318 453 304 -180 C
ATOM 3266 CD2 LEU A 423 -14.239 -6.908 -9.845 1.00 76.45 C
ANISOU 3266 CD2 LEU A 423 10204 10230 8615 505 352 -131 C
ATOM 3267 N LEU A 424 -9.493 -7.086 -12.353 1.00 88.39 N
ANISOU 3267 N LEU A 424 11543 12080 9961 915 74 -56 N
ATOM 3268 CA LEU A 424 -8.685 -7.500 -13.489 1.00 98.59 C
ANISOU 3268 CA LEU A 424 12785 13424 11250 1016 24 -77 C
ATOM 3269 C LEU A 424 -7.492 -8.305 -12.992 1.00 97.26 C
ANISOU 3269 C LEU A 424 12682 13252 11020 1120 -12 -16 C
ATOM 3270 O LEU A 424 -6.878 -7.961 -11.977 1.00 80.09 O
ANISOU 3270 O LEU A 424 10535 11110 8785 1127 -29 48 O
ATOM 3271 CB LEU A 424 -8.212 -6.290 -14.300 1.00 95.01 C
ANISOU 3271 CB LEU A 424 12201 13115 10784 1024 -21 -92 C
ATOM 3272 CG LEU A 424 -7.560 -6.583 -15.652 1.00 79.00 C
ANISOU 3272 CG LEU A 424 10108 11146 8761 1113 -64 -127 C
ATOM 3273 CD1 LEU A 424 -8.501 -7.389 -16.534 1.00 83.72 C
ANISOU 3273 CD1 LEU A 424 10724 11654 9430 1102 -36 -200 C
ATOM 3274 CD2 LEU A 424 -7.155 -5.290 -16.339 1.00 85.07 C
ANISOU 3274 CD2 LEU A 424 10757 12053 9513 1107 -99 -136 C
ATOM 3275 N SER A 425 -7.176 -9.380 -13.707 1.00114.19 N
ANISOU 3275 N SER A 425 14853 15355 13181 1202 -26 -38 N
ATOM 3276 CA SER A 425 -6.110 -10.272 -13.275 1.00117.02 C
ANISOU 3276 CA SER A 425 15281 15696 13487 1308 -59 14 C
ATOM 3277 C SER A 425 -4.756 -9.572 -13.377 1.00116.19 C
ANISOU 3277 C SER A 425 15090 15736 13320 1382 -126 52 C
ATOM 3278 O SER A 425 -4.506 -8.838 -14.337 1.00114.42 O
ANISOU 3278 O SER A 425 14754 15616 13105 1390 -152 19 O
ATOM 3279 CB SER A 425 -6.103 -11.546 -14.120 1.00120.87 C
ANISOU 3279 CB SER A 425 15809 16107 14010 1381 -58 -27 C
ATOM 3280 OG SER A 425 -5.013 -12.383 -13.774 1.00113.43 O
ANISOU 3280 OG SER A 425 14926 15154 13017 1494 -95 22 O
ATOM 3281 N PRO A 426 -3.868 -9.769 -12.398 1.00110.96 N
ANISOU 3281 N PRO A 426 14480 15086 12593 1437 -156 121 N
ATOM 3282 CA PRO A 426 -2.521 -9.190 -12.523 1.00113.67 C
ANISOU 3282 CA PRO A 426 14739 15570 12882 1514 -223 153 C
ATOM 3283 C PRO A 426 -1.727 -9.789 -13.670 1.00127.97 C
ANISOU 3283 C PRO A 426 16499 17422 14700 1625 -260 124 C
ATOM 3284 O PRO A 426 -0.929 -9.078 -14.294 1.00122.21 O
ANISOU 3284 O PRO A 426 15659 16822 13952 1661 -300 118 O
ATOM 3285 CB PRO A 426 -1.877 -9.498 -11.163 1.00102.17 C
ANISOU 3285 CB PRO A 426 13370 14090 11359 1550 -245 228 C
ATOM 3286 CG PRO A 426 -3.034 -9.748 -10.235 1.00 94.85 C
ANISOU 3286 CG PRO A 426 12555 13034 10448 1456 -181 238 C
ATOM 3287 CD PRO A 426 -4.082 -10.397 -11.085 1.00105.52 C
ANISOU 3287 CD PRO A 426 13926 14291 11876 1422 -130 173 C
ATOM 3288 N ASP A 427 -1.927 -11.075 -13.972 1.00137.78 N
ANISOU 3288 N ASP A 427 17823 18558 15969 1679 -244 103 N
ATOM 3289 CA ASP A 427 -1.246 -11.701 -15.099 1.00130.26 C
ANISOU 3289 CA ASP A 427 16829 17637 15026 1785 -274 70 C
ATOM 3290 C ASP A 427 -1.687 -11.120 -16.436 1.00135.47 C
ANISOU 3290 C ASP A 427 17386 18356 15732 1750 -265 0 C
ATOM 3291 O ASP A 427 -0.945 -11.226 -17.419 1.00143.96 O
ANISOU 3291 O ASP A 427 18392 19503 16802 1832 -296 -24 O
ATOM 3292 CB ASP A 427 -1.486 -13.214 -15.091 1.00127.45 C
ANISOU 3292 CB ASP A 427 16593 17139 14692 1842 -255 60 C
ATOM 3293 CG ASP A 427 -0.861 -13.898 -13.895 1.00142.16 C
ANISOU 3293 CG ASP A 427 18563 18949 16502 1903 -274 130 C
ATOM 3294 OD1 ASP A 427 -1.407 -13.771 -12.780 1.00127.50 O
ANISOU 3294 OD1 ASP A 427 16784 17029 14632 1831 -245 168 O
ATOM 3295 OD2 ASP A 427 0.180 -14.561 -14.071 1.00164.90 O
ANISOU 3295 OD2 ASP A 427 21450 21851 19354 2027 -318 147 O
ATOM 3296 N PHE A 428 -2.878 -10.524 -16.497 1.00134.31 N
ANISOU 3296 N PHE A 428 17228 18178 15628 1634 -222 -33 N
ATOM 3297 CA PHE A 428 -3.345 -9.864 -17.709 1.00130.64 C
ANISOU 3297 CA PHE A 428 16665 17770 15201 1596 -217 -97 C
ATOM 3298 C PHE A 428 -2.389 -8.744 -18.098 1.00133.15 C
ANISOU 3298 C PHE A 428 16864 18249 15478 1620 -260 -81 C
ATOM 3299 O PHE A 428 -2.277 -7.742 -17.386 1.00133.11 O
ANISOU 3299 O PHE A 428 16827 18304 15444 1564 -265 -43 O
ATOM 3300 CB PHE A 428 -4.760 -9.315 -17.510 1.00123.89 C
ANISOU 3300 CB PHE A 428 15819 16860 14394 1465 -168 -128 C
ATOM 3301 CG PHE A 428 -5.283 -8.532 -18.684 1.00121.58 C
ANISOU 3301 CG PHE A 428 15429 16629 14138 1423 -168 -190 C
ATOM 3302 CD1 PHE A 428 -5.120 -7.156 -18.751 1.00115.26 C
ANISOU 3302 CD1 PHE A 428 14536 15942 13316 1377 -183 -180 C
ATOM 3303 CD2 PHE A 428 -5.949 -9.171 -19.717 1.00131.87 C
ANISOU 3303 CD2 PHE A 428 16737 17873 15494 1430 -153 -261 C
ATOM 3304 CE1 PHE A 428 -5.602 -6.436 -19.829 1.00109.24 C
ANISOU 3304 CE1 PHE A 428 13691 15232 12582 1343 -184 -235 C
ATOM 3305 CE2 PHE A 428 -6.436 -8.455 -20.797 1.00113.50 C
ANISOU 3305 CE2 PHE A 428 14325 15602 13196 1395 -157 -319 C
ATOM 3306 CZ PHE A 428 -6.262 -7.085 -20.853 1.00 98.16 C
ANISOU 3306 CZ PHE A 428 12295 13772 11231 1353 -172 -304 C
ATOM 3307 N GLN A 429 -1.690 -8.905 -19.215 1.00139.39 N
ANISOU 3307 N GLN A 429 17590 19107 16264 1702 -287 -110 N
ATOM 3308 CA GLN A 429 -0.770 -7.889 -19.699 1.00140.89 C
ANISOU 3308 CA GLN A 429 17665 19449 16418 1725 -321 -100 C
ATOM 3309 C GLN A 429 -1.411 -7.103 -20.835 1.00132.33 C
ANISOU 3309 C GLN A 429 16504 18411 15366 1669 -308 -158 C
ATOM 3310 O GLN A 429 -2.240 -7.623 -21.587 1.00118.36 O
ANISOU 3310 O GLN A 429 14758 16570 13642 1658 -286 -216 O
ATOM 3311 CB GLN A 429 0.545 -8.514 -20.167 1.00144.21 C
ANISOU 3311 CB GLN A 429 18058 19928 16806 1856 -360 -91 C
ATOM 3312 CG GLN A 429 1.721 -7.550 -20.154 1.00145.67 C
ANISOU 3312 CG GLN A 429 18141 20265 16943 1883 -397 -56 C
ATOM 3313 CD GLN A 429 1.963 -6.950 -18.781 1.00143.73 C
ANISOU 3313 CD GLN A 429 17911 20040 16661 1838 -410 8 C
ATOM 3314 OE1 GLN A 429 1.557 -5.822 -18.502 1.00135.63 O
ANISOU 3314 OE1 GLN A 429 16845 19056 15632 1744 -400 16 O
ATOM 3315 NE2 GLN A 429 2.626 -7.707 -17.913 1.00134.33 N
ANISOU 3315 NE2 GLN A 429 16782 18818 15440 1908 -435 53 N
ATOM 3316 N GLU A 430 -1.021 -5.838 -20.950 1.00129.02 N
ANISOU 3316 N GLU A 430 15993 18108 14919 1634 -323 -143 N
ATOM 3317 CA GLU A 430 -1.560 -4.935 -21.958 1.00119.39 C
ANISOU 3317 CA GLU A 430 14701 16942 13721 1581 -313 -190 C
ATOM 3318 C GLU A 430 -0.482 -4.646 -22.995 1.00120.91 C
ANISOU 3318 C GLU A 430 14805 17254 13882 1656 -340 -199 C
ATOM 3319 O GLU A 430 0.600 -4.153 -22.655 1.00126.32 O
ANISOU 3319 O GLU A 430 15438 18035 14523 1686 -366 -155 O
ATOM 3320 CB GLU A 430 -2.072 -3.643 -21.317 1.00114.27 C
ANISOU 3320 CB GLU A 430 14022 16325 13068 1472 -303 -168 C
ATOM 3321 CG GLU A 430 -1.078 -2.951 -20.395 1.00116.65 C
ANISOU 3321 CG GLU A 430 14293 16713 13316 1474 -328 -102 C
ATOM 3322 CD GLU A 430 -1.723 -2.436 -19.125 1.00121.31 C
ANISOU 3322 CD GLU A 430 14928 17259 13905 1382 -310 -68 C
ATOM 3323 OE1 GLU A 430 -2.676 -3.081 -18.640 1.00126.74 O
ANISOU 3323 OE1 GLU A 430 15699 17829 14627 1346 -278 -80 O
ATOM 3324 OE2 GLU A 430 -1.278 -1.389 -18.611 1.00122.92 O
ANISOU 3324 OE2 GLU A 430 15085 17544 14074 1344 -324 -32 O
ATOM 3325 N ASP A 431 -0.773 -4.969 -24.249 1.00111.80 N
ANISOU 3325 N ASP A 431 13634 16092 12751 1685 -335 -259 N
ATOM 3326 CA ASP A 431 0.116 -4.695 -25.367 1.00106.84 C
ANISOU 3326 CA ASP A 431 12927 15572 12096 1751 -352 -276 C
ATOM 3327 C ASP A 431 -0.454 -3.562 -26.209 1.00105.20 C
ANISOU 3327 C ASP A 431 12657 15419 11895 1682 -343 -310 C
ATOM 3328 O ASP A 431 -1.611 -3.163 -26.053 1.00103.37 O
ANISOU 3328 O ASP A 431 12448 15132 11697 1595 -326 -330 O
ATOM 3329 CB ASP A 431 0.330 -5.955 -26.216 1.00 97.03 C
ANISOU 3329 CB ASP A 431 11716 14285 10866 1849 -354 -318 C
ATOM 3330 CG ASP A 431 -0.970 -6.653 -26.567 1.00101.07 C
ANISOU 3330 CG ASP A 431 12298 14672 11433 1815 -331 -375 C
ATOM 3331 OD1 ASP A 431 -2.051 -6.075 -26.330 1.00102.13 O
ANISOU 3331 OD1 ASP A 431 12441 14768 11597 1716 -314 -388 O
ATOM 3332 OD2 ASP A 431 -0.908 -7.792 -27.075 1.00109.92 O
ANISOU 3332 OD2 ASP A 431 13463 15734 12568 1887 -331 -408 O
ATOM 3333 N ASN A 432 0.376 -3.047 -27.118 1.00107.89 N
ANISOU 3333 N ASN A 432 12529 15006 13457 90 -44 -18 N
ATOM 3334 CA ASN A 432 -0.024 -1.901 -27.926 1.00100.17 C
ANISOU 3334 CA ASN A 432 11580 14001 12479 53 -4 -68 C
ATOM 3335 C ASN A 432 -1.162 -2.213 -28.888 1.00 90.71 C
ANISOU 3335 C ASN A 432 10480 12719 11266 73 20 -89 C
ATOM 3336 O ASN A 432 -1.740 -1.278 -29.453 1.00 87.05 O
ANISOU 3336 O ASN A 432 10050 12232 10794 39 45 -129 O
ATOM 3337 CB ASN A 432 1.179 -1.358 -28.700 1.00107.21 C
ANISOU 3337 CB ASN A 432 12414 14906 13413 70 45 -66 C
ATOM 3338 CG ASN A 432 1.894 -2.428 -29.496 1.00114.12 C
ANISOU 3338 CG ASN A 432 13291 15754 14315 158 80 -29 C
ATOM 3339 OD1 ASN A 432 1.666 -3.623 -29.303 1.00118.76 O
ANISOU 3339 OD1 ASN A 432 13910 16317 14895 205 58 -2 O
ATOM 3340 ND2 ASN A 432 2.772 -2.002 -30.396 1.00124.17 N
ANISOU 3340 ND2 ASN A 432 14530 17028 15621 184 139 -24 N
ATOM 3341 N GLU A 433 -1.504 -3.488 -29.088 1.00 94.16 N
ANISOU 3341 N GLU A 433 10964 13110 11704 125 9 -64 N
ATOM 3342 CA GLU A 433 -2.651 -3.811 -29.928 1.00 87.72 C
ANISOU 3342 CA GLU A 433 10241 12212 10876 138 16 -86 C
ATOM 3343 C GLU A 433 -3.965 -3.589 -29.186 1.00 85.12 C
ANISOU 3343 C GLU A 433 9941 11880 10520 80 -22 -96 C
ATOM 3344 O GLU A 433 -4.951 -3.149 -29.787 1.00 84.12 O
ANISOU 3344 O GLU A 433 9870 11708 10382 59 -12 -129 O
ATOM 3345 CB GLU A 433 -2.551 -5.252 -30.432 1.00 83.30 C
ANISOU 3345 CB GLU A 433 9724 11593 10334 212 13 -61 C
ATOM 3346 CG GLU A 433 -1.382 -5.494 -31.375 1.00 77.09 C
ANISOU 3346 CG GLU A 433 8924 10799 9569 283 63 -56 C
ATOM 3347 CD GLU A 433 -1.518 -6.787 -32.158 1.00 84.59 C
ANISOU 3347 CD GLU A 433 9944 11668 10528 360 65 -51 C
ATOM 3348 OE1 GLU A 433 -2.532 -7.491 -31.976 1.00 81.44 O
ANISOU 3348 OE1 GLU A 433 9603 11215 10127 352 22 -51 O
ATOM 3349 OE2 GLU A 433 -0.612 -7.096 -32.962 1.00 87.57 O
ANISOU 3349 OE2 GLU A 433 10320 12035 10918 431 110 -47 O
ATOM 3350 N THR A 434 -3.999 -3.883 -27.883 1.00 90.22 N
ANISOU 3350 N THR A 434 10549 12577 11155 58 -63 -65 N
ATOM 3351 CA THR A 434 -5.195 -3.591 -27.099 1.00 89.45 C
ANISOU 3351 CA THR A 434 10471 12488 11028 7 -90 -69 C
ATOM 3352 C THR A 434 -5.316 -2.103 -26.799 1.00 80.88 C
ANISOU 3352 C THR A 434 9363 11448 9920 -53 -79 -114 C
ATOM 3353 O THR A 434 -6.429 -1.599 -26.608 1.00 74.28 O
ANISOU 3353 O THR A 434 8559 10600 9064 -90 -82 -134 O
ATOM 3354 CB THR A 434 -5.193 -4.391 -25.795 1.00 80.52 C
ANISOU 3354 CB THR A 434 9310 11400 9884 9 -132 -16 C
ATOM 3355 OG1 THR A 434 -3.959 -4.177 -25.098 1.00 98.95 O
ANISOU 3355 OG1 THR A 434 11572 13813 12213 12 -144 -1 O
ATOM 3356 CG2 THR A 434 -5.368 -5.876 -26.077 1.00 81.79 C
ANISOU 3356 CG2 THR A 434 9505 11497 10074 61 -146 30 C
ATOM 3357 N GLU A 435 -4.189 -1.387 -26.748 1.00 80.46 N
ANISOU 3357 N GLU A 435 9253 11443 9876 -61 -66 -128 N
ATOM 3358 CA GLU A 435 -4.241 0.061 -26.572 1.00 79.79 C
ANISOU 3358 CA GLU A 435 9150 11387 9780 -118 -56 -175 C
ATOM 3359 C GLU A 435 -4.888 0.734 -27.776 1.00 75.02 C
ANISOU 3359 C GLU A 435 8598 10719 9186 -125 -14 -212 C
ATOM 3360 O GLU A 435 -5.689 1.663 -27.620 1.00 68.32 O
ANISOU 3360 O GLU A 435 7770 9867 8321 -168 -10 -246 O
ATOM 3361 CB GLU A 435 -2.834 0.616 -26.347 1.00 89.40 C
ANISOU 3361 CB GLU A 435 10289 12660 11019 -127 -55 -178 C
ATOM 3362 CG GLU A 435 -1.998 -0.146 -25.329 1.00 93.86 C
ANISOU 3362 CG GLU A 435 10796 13288 11579 -108 -99 -135 C
ATOM 3363 CD GLU A 435 -2.081 0.439 -23.935 1.00106.43 C
ANISOU 3363 CD GLU A 435 12356 14952 13130 -158 -147 -150 C
ATOM 3364 OE1 GLU A 435 -3.195 0.493 -23.371 1.00107.96 O
ANISOU 3364 OE1 GLU A 435 12594 15144 13280 -178 -160 -160 O
ATOM 3365 OE2 GLU A 435 -1.027 0.851 -23.405 1.00109.21 O
ANISOU 3365 OE2 GLU A 435 12640 15364 13492 -174 -172 -153 O
ATOM 3366 N ILE A 436 -4.550 0.278 -28.984 1.00 80.52 N
ANISOU 3366 N ILE A 436 9320 11367 9906 -77 19 -204 N
ATOM 3367 CA ILE A 436 -5.143 0.848 -30.189 1.00 74.15 C
ANISOU 3367 CA ILE A 436 8569 10503 9102 -75 57 -234 C
ATOM 3368 C ILE A 436 -6.620 0.486 -30.280 1.00 77.74 C
ANISOU 3368 C ILE A 436 9092 10909 9538 -81 36 -241 C
ATOM 3369 O ILE A 436 -7.447 1.303 -30.704 1.00 77.55 O
ANISOU 3369 O ILE A 436 9102 10859 9506 -108 49 -270 O
ATOM 3370 CB ILE A 436 -4.362 0.388 -31.434 1.00 71.74 C
ANISOU 3370 CB ILE A 436 8278 10164 8816 -12 99 -223 C
ATOM 3371 CG1 ILE A 436 -2.959 0.999 -31.435 1.00 78.29 C
ANISOU 3371 CG1 ILE A 436 9030 11042 9674 -14 130 -214 C
ATOM 3372 CG2 ILE A 436 -5.103 0.761 -32.710 1.00 65.18 C
ANISOU 3372 CG2 ILE A 436 7520 9272 7975 0 130 -250 C
ATOM 3373 CD1 ILE A 436 -2.954 2.513 -31.436 1.00 62.97 C
ANISOU 3373 CD1 ILE A 436 7065 9118 7742 -74 150 -245 C
ATOM 3374 N ASN A 437 -6.978 -0.737 -29.880 1.00 71.89 N
ANISOU 3374 N ASN A 437 8367 10153 8795 -58 2 -209 N
ATOM 3375 CA ASN A 437 -8.386 -1.122 -29.858 1.00 66.99 C
ANISOU 3375 CA ASN A 437 7798 9487 8167 -70 -23 -207 C
ATOM 3376 C ASN A 437 -9.181 -0.246 -28.899 1.00 70.76 C
ANISOU 3376 C ASN A 437 8258 10004 8623 -128 -33 -219 C
ATOM 3377 O ASN A 437 -10.316 0.144 -29.197 1.00 68.92 O
ANISOU 3377 O ASN A 437 8062 9737 8387 -149 -32 -235 O
ATOM 3378 CB ASN A 437 -8.527 -2.595 -29.477 1.00 66.21 C
ANISOU 3378 CB ASN A 437 7709 9366 8081 -39 -59 -162 C
ATOM 3379 CG ASN A 437 -8.291 -3.526 -30.649 1.00 70.21 C
ANISOU 3379 CG ASN A 437 8265 9802 8608 20 -54 -162 C
ATOM 3380 OD1 ASN A 437 -7.752 -3.122 -31.679 1.00 80.49 O
ANISOU 3380 OD1 ASN A 437 9585 11088 9909 47 -19 -190 O
ATOM 3381 ND2 ASN A 437 -8.698 -4.781 -30.499 1.00 74.51 N
ANISOU 3381 ND2 ASN A 437 8835 10302 9172 43 -89 -130 N
ATOM 3382 N PHE A 438 -8.600 0.077 -27.742 1.00 71.32 N
ANISOU 3382 N PHE A 438 8274 10146 8677 -151 -44 -212 N
ATOM 3383 CA PHE A 438 -9.289 0.937 -26.786 1.00 67.33 C
ANISOU 3383 CA PHE A 438 7756 9682 8142 -198 -51 -230 C
ATOM 3384 C PHE A 438 -9.395 2.364 -27.310 1.00 66.46 C
ANISOU 3384 C PHE A 438 7654 9563 8035 -229 -19 -282 C
ATOM 3385 O PHE A 438 -10.464 2.982 -27.243 1.00 69.97 O
ANISOU 3385 O PHE A 438 8124 9992 8468 -254 -13 -301 O
ATOM 3386 CB PHE A 438 -8.568 0.907 -25.437 1.00 70.26 C
ANISOU 3386 CB PHE A 438 8074 10135 8488 -209 -76 -214 C
ATOM 3387 CG PHE A 438 -9.087 1.915 -24.452 1.00 63.70 C
ANISOU 3387 CG PHE A 438 7233 9352 7617 -252 -80 -244 C
ATOM 3388 CD1 PHE A 438 -10.301 1.720 -23.815 1.00 56.47 C
ANISOU 3388 CD1 PHE A 438 6341 8441 6676 -261 -86 -227 C
ATOM 3389 CD2 PHE A 438 -8.358 3.056 -24.160 1.00 63.93 C
ANISOU 3389 CD2 PHE A 438 7231 9421 7639 -282 -78 -290 C
ATOM 3390 CE1 PHE A 438 -10.780 2.647 -22.910 1.00 59.70 C
ANISOU 3390 CE1 PHE A 438 6746 8895 7043 -291 -84 -256 C
ATOM 3391 CE2 PHE A 438 -8.832 3.986 -23.255 1.00 61.57 C
ANISOU 3391 CE2 PHE A 438 6931 9160 7301 -317 -84 -326 C
ATOM 3392 CZ PHE A 438 -10.044 3.781 -22.630 1.00 57.75 C
ANISOU 3392 CZ PHE A 438 6475 8684 6783 -318 -85 -310 C
ATOM 3393 N LEU A 439 -8.295 2.903 -27.841 1.00 63.03 N
ANISOU 3393 N LEU A 439 7193 9135 7619 -226 3 -300 N
ATOM 3394 CA LEU A 439 -8.307 4.281 -28.324 1.00 66.12 C
ANISOU 3394 CA LEU A 439 7588 9514 8021 -257 34 -343 C
ATOM 3395 C LEU A 439 -9.217 4.440 -29.538 1.00 66.40 C
ANISOU 3395 C LEU A 439 7683 9480 8065 -243 59 -352 C
ATOM 3396 O LEU A 439 -9.876 5.475 -29.693 1.00 55.62 O
ANISOU 3396 O LEU A 439 6336 8099 6699 -272 75 -382 O
ATOM 3397 CB LEU A 439 -6.883 4.734 -28.650 1.00 70.93 C
ANISOU 3397 CB LEU A 439 8148 10144 8659 -256 54 -348 C
ATOM 3398 CG LEU A 439 -6.222 5.671 -27.634 1.00 63.19 C
ANISOU 3398 CG LEU A 439 7111 9221 7678 -304 36 -375 C
ATOM 3399 CD1 LEU A 439 -6.382 5.142 -26.222 1.00 62.15 C
ANISOU 3399 CD1 LEU A 439 6961 9147 7507 -312 -12 -365 C
ATOM 3400 CD2 LEU A 439 -4.752 5.870 -27.961 1.00 65.25 C
ANISOU 3400 CD2 LEU A 439 7312 9502 7980 -301 50 -366 C
ATOM 3401 N LEU A 440 -9.270 3.427 -30.407 1.00 69.78 N
ANISOU 3401 N LEU A 440 8147 9867 8501 -198 59 -329 N
ATOM 3402 CA LEU A 440 -10.167 3.487 -31.558 1.00 63.43 C
ANISOU 3402 CA LEU A 440 7404 8998 7698 -182 72 -339 C
ATOM 3403 C LEU A 440 -11.625 3.475 -31.115 1.00 64.53 C
ANISOU 3403 C LEU A 440 7568 9121 7828 -206 46 -339 C
ATOM 3404 O LEU A 440 -12.447 4.230 -31.646 1.00 64.39 O
ANISOU 3404 O LEU A 440 7580 9073 7811 -219 59 -358 O
ATOM 3405 CB LEU A 440 -9.874 2.326 -32.512 1.00 69.45 C
ANISOU 3405 CB LEU A 440 8204 9719 8466 -125 69 -320 C
ATOM 3406 CG LEU A 440 -10.479 2.321 -33.922 1.00 68.47 C
ANISOU 3406 CG LEU A 440 8148 9530 8337 -95 81 -334 C
ATOM 3407 CD1 LEU A 440 -11.876 1.707 -33.944 1.00 52.61 C
ANISOU 3407 CD1 LEU A 440 6185 7478 6328 -101 37 -330 C
ATOM 3408 CD2 LEU A 440 -10.499 3.726 -34.511 1.00 71.33 C
ANISOU 3408 CD2 LEU A 440 8514 9891 8697 -115 122 -358 C
ATOM 3409 N LYS A 441 -11.962 2.620 -30.147 1.00 60.52 N
ANISOU 3409 N LYS A 441 7046 8634 7314 -210 13 -311 N
ATOM 3410 CA LYS A 441 -13.309 2.621 -29.587 1.00 52.71 C
ANISOU 3410 CA LYS A 441 6068 7640 6320 -233 -5 -301 C
ATOM 3411 C LYS A 441 -13.643 3.973 -28.969 1.00 59.45 C
ANISOU 3411 C LYS A 441 6902 8528 7158 -272 15 -332 C
ATOM 3412 O LYS A 441 -14.764 4.474 -29.115 1.00 62.29 O
ANISOU 3412 O LYS A 441 7282 8864 7520 -286 21 -341 O
ATOM 3413 CB LYS A 441 -13.435 1.507 -28.548 1.00 64.10 C
ANISOU 3413 CB LYS A 441 7489 9108 7758 -229 -37 -256 C
ATOM 3414 CG LYS A 441 -14.766 1.458 -27.815 1.00 60.62 C
ANISOU 3414 CG LYS A 441 7047 8672 7312 -252 -49 -234 C
ATOM 3415 CD LYS A 441 -15.806 0.677 -28.595 1.00 70.84 C
ANISOU 3415 CD LYS A 441 8380 9896 8642 -243 -72 -212 C
ATOM 3416 CE LYS A 441 -16.982 0.300 -27.708 1.00 70.45 C
ANISOU 3416 CE LYS A 441 8312 9856 8598 -262 -86 -169 C
ATOM 3417 NZ LYS A 441 -17.952 -0.579 -28.418 1.00 85.09 N
ANISOU 3417 NZ LYS A 441 10196 11637 10499 -258 -119 -142 N
ATOM 3418 N GLN A 442 -12.675 4.582 -28.279 1.00 65.85 N
ANISOU 3418 N GLN A 442 7674 9391 7954 -288 24 -352 N
ATOM 3419 CA GLN A 442 -12.901 5.890 -27.672 1.00 63.80 C
ANISOU 3419 CA GLN A 442 7402 9159 7680 -323 40 -390 C
ATOM 3420 C GLN A 442 -13.092 6.969 -28.731 1.00 58.28 C
ANISOU 3420 C GLN A 442 6727 8413 7004 -331 73 -422 C
ATOM 3421 O GLN A 442 -13.953 7.844 -28.584 1.00 62.19 O
ANISOU 3421 O GLN A 442 7235 8897 7495 -349 86 -445 O
ATOM 3422 CB GLN A 442 -11.734 6.249 -26.752 1.00 70.84 C
ANISOU 3422 CB GLN A 442 8247 10113 8557 -341 31 -408 C
ATOM 3423 CG GLN A 442 -11.640 5.406 -25.488 1.00 66.69 C
ANISOU 3423 CG GLN A 442 7696 9646 7996 -335 -1 -377 C
ATOM 3424 CD GLN A 442 -12.643 5.822 -24.432 1.00 57.30 C
ANISOU 3424 CD GLN A 442 6514 8490 6769 -352 -3 -386 C
ATOM 3425 OE1 GLN A 442 -13.786 5.366 -24.429 1.00 55.99 O
ANISOU 3425 OE1 GLN A 442 6369 8303 6601 -343 0 -357 O
ATOM 3426 NE2 GLN A 442 -12.218 6.696 -23.527 1.00 53.72 N
ANISOU 3426 NE2 GLN A 442 6040 8086 6284 -376 -9 -427 N
ATOM 3427 N ALA A 443 -12.298 6.925 -29.805 1.00 63.48 N
ANISOU 3427 N ALA A 443 7393 9043 7683 -312 90 -421 N
ATOM 3428 CA ALA A 443 -12.385 7.959 -30.831 1.00 64.66 C
ANISOU 3428 CA ALA A 443 7565 9151 7852 -316 125 -443 C
ATOM 3429 C ALA A 443 -13.699 7.890 -31.597 1.00 64.23 C
ANISOU 3429 C ALA A 443 7562 9046 7798 -302 123 -436 C
ATOM 3430 O ALA A 443 -14.207 8.925 -32.044 1.00 58.62 O
ANISOU 3430 O ALA A 443 6868 8309 7097 -313 146 -455 O
ATOM 3431 CB ALA A 443 -11.203 7.846 -31.793 1.00 54.81 C
ANISOU 3431 CB ALA A 443 6311 7891 6621 -292 149 -434 C
ATOM 3432 N LEU A 444 -14.261 6.688 -31.762 1.00 64.00 N
ANISOU 3432 N LEU A 444 7554 9000 7764 -278 93 -408 N
ATOM 3433 CA LEU A 444 -15.541 6.559 -32.450 1.00 63.05 C
ANISOU 3433 CA LEU A 444 7475 8831 7649 -268 80 -401 C
ATOM 3434 C LEU A 444 -16.646 7.314 -31.722 1.00 63.35 C
ANISOU 3434 C LEU A 444 7503 8880 7688 -297 82 -409 C
ATOM 3435 O LEU A 444 -17.559 7.847 -32.362 1.00 67.86 O
ANISOU 3435 O LEU A 444 8099 9415 8270 -296 87 -413 O
ATOM 3436 CB LEU A 444 -15.914 5.082 -32.594 1.00 63.88 C
ANISOU 3436 CB LEU A 444 7600 8915 7758 -245 38 -370 C
ATOM 3437 CG LEU A 444 -15.054 4.231 -33.532 1.00 60.75 C
ANISOU 3437 CG LEU A 444 7230 8492 7360 -204 34 -365 C
ATOM 3438 CD1 LEU A 444 -15.560 2.796 -33.571 1.00 48.97 C
ANISOU 3438 CD1 LEU A 444 5759 6967 5878 -185 -14 -339 C
ATOM 3439 CD2 LEU A 444 -15.027 4.833 -34.926 1.00 61.53 C
ANISOU 3439 CD2 LEU A 444 7373 8551 7453 -180 57 -384 C
ATOM 3440 N THR A 445 -16.578 7.374 -30.393 1.00 65.25 N
ANISOU 3440 N THR A 445 7706 9171 7914 -319 80 -410 N
ATOM 3441 CA THR A 445 -17.571 8.082 -29.594 1.00 67.06 C
ANISOU 3441 CA THR A 445 7926 9417 8137 -338 90 -418 C
ATOM 3442 C THR A 445 -17.174 9.533 -29.344 1.00 64.69 C
ANISOU 3442 C THR A 445 7618 9128 7834 -359 123 -465 C
ATOM 3443 O THR A 445 -17.991 10.443 -29.516 1.00 61.46 O
ANISOU 3443 O THR A 445 7222 8696 7436 -364 142 -481 O
ATOM 3444 CB THR A 445 -17.777 7.366 -28.256 1.00 62.78 C
ANISOU 3444 CB THR A 445 7355 8927 7572 -344 73 -394 C
ATOM 3445 OG1 THR A 445 -18.099 5.988 -28.487 1.00 77.31 O
ANISOU 3445 OG1 THR A 445 9201 10748 9426 -327 41 -346 O
ATOM 3446 CG2 THR A 445 -18.903 8.022 -27.469 1.00 51.46 C
ANISOU 3446 CG2 THR A 445 5913 7511 6128 -354 90 -397 C
ATOM 3447 N ILE A 446 -15.922 9.761 -28.949 1.00 64.43 N
ANISOU 3447 N ILE A 446 7560 9126 7792 -371 126 -486 N
ATOM 3448 CA ILE A 446 -15.491 11.090 -28.529 1.00 58.63 C
ANISOU 3448 CA ILE A 446 6814 8401 7060 -398 147 -533 C
ATOM 3449 C ILE A 446 -15.137 11.955 -29.733 1.00 66.00 C
ANISOU 3449 C ILE A 446 7764 9283 8029 -400 177 -546 C
ATOM 3450 O ILE A 446 -15.666 13.060 -29.897 1.00 68.73 O
ANISOU 3450 O ILE A 446 8124 9600 8391 -411 200 -571 O
ATOM 3451 CB ILE A 446 -14.309 10.974 -27.548 1.00 66.29 C
ANISOU 3451 CB ILE A 446 7746 9428 8011 -415 129 -549 C
ATOM 3452 CG1 ILE A 446 -14.734 10.198 -26.299 1.00 58.39 C
ANISOU 3452 CG1 ILE A 446 6734 8485 6969 -409 104 -532 C
ATOM 3453 CG2 ILE A 446 -13.786 12.351 -27.175 1.00 71.98 C
ANISOU 3453 CG2 ILE A 446 8455 10151 8743 -448 142 -604 C
ATOM 3454 CD1 ILE A 446 -13.624 10.003 -25.292 1.00 56.52 C
ANISOU 3454 CD1 ILE A 446 6460 8309 6704 -422 78 -543 C
ATOM 3455 N VAL A 447 -14.233 11.473 -30.588 1.00 71.63 N
ANISOU 3455 N VAL A 447 8476 9986 8756 -385 180 -527 N
ATOM 3456 CA VAL A 447 -13.820 12.263 -31.744 1.00 67.51 C
ANISOU 3456 CA VAL A 447 7968 9420 8264 -382 215 -530 C
ATOM 3457 C VAL A 447 -14.920 12.285 -32.799 1.00 66.11 C
ANISOU 3457 C VAL A 447 7838 9193 8088 -357 223 -512 C
ATOM 3458 O VAL A 447 -15.151 13.309 -33.453 1.00 66.60 O
ANISOU 3458 O VAL A 447 7918 9217 8169 -360 252 -520 O
ATOM 3459 CB VAL A 447 -12.495 11.724 -32.315 1.00 64.38 C
ANISOU 3459 CB VAL A 447 7552 9033 7876 -368 223 -510 C
ATOM 3460 CG1 VAL A 447 -12.074 12.526 -33.540 1.00 62.01 C
ANISOU 3460 CG1 VAL A 447 7265 8691 7604 -360 267 -503 C
ATOM 3461 CG2 VAL A 447 -11.409 11.756 -31.252 1.00 65.15 C
ANISOU 3461 CG2 VAL A 447 7594 9181 7977 -396 208 -525 C
ATOM 3462 N GLY A 448 -15.623 11.164 -32.973 1.00 63.57 N
ANISOU 3462 N GLY A 448 7537 8868 7748 -332 193 -487 N
ATOM 3463 CA GLY A 448 -16.649 11.073 -33.997 1.00 58.12 C
ANISOU 3463 CA GLY A 448 6890 8132 7060 -307 187 -471 C
ATOM 3464 C GLY A 448 -17.820 12.011 -33.794 1.00 64.63 C
ANISOU 3464 C GLY A 448 7721 8939 7896 -320 196 -481 C
ATOM 3465 O GLY A 448 -18.535 12.311 -34.756 1.00 66.80 O
ANISOU 3465 O GLY A 448 8029 9173 8178 -302 198 -470 O
ATOM 3466 N THR A 449 -18.032 12.489 -32.569 1.00 64.96 N
ANISOU 3466 N THR A 449 7734 9011 7937 -346 200 -502 N
ATOM 3467 CA THR A 449 -19.158 13.364 -32.272 1.00 62.94 C
ANISOU 3467 CA THR A 449 7482 8740 7691 -352 214 -513 C
ATOM 3468 C THR A 449 -18.813 14.845 -32.371 1.00 65.86 C
ANISOU 3468 C THR A 449 7854 9086 8082 -367 252 -546 C
ATOM 3469 O THR A 449 -19.727 15.675 -32.399 1.00 63.72 O
ANISOU 3469 O THR A 449 7594 8789 7827 -364 268 -554 O
ATOM 3470 CB THR A 449 -19.709 13.070 -30.870 1.00 56.58 C
ANISOU 3470 CB THR A 449 6651 7981 6868 -362 203 -517 C
ATOM 3471 OG1 THR A 449 -21.021 13.632 -30.743 1.00 55.87 O
ANISOU 3471 OG1 THR A 449 6564 7874 6789 -355 214 -514 O
ATOM 3472 CG2 THR A 449 -18.808 13.666 -29.800 1.00 58.52 C
ANISOU 3472 CG2 THR A 449 6872 8264 7098 -387 215 -559 C
ATOM 3473 N LEU A 450 -17.523 15.198 -32.431 1.00 61.07 N
ANISOU 3473 N LEU A 450 7234 8484 7485 -384 267 -563 N
ATOM 3474 CA LEU A 450 -17.159 16.613 -32.421 1.00 64.26 C
ANISOU 3474 CA LEU A 450 7635 8859 7919 -407 300 -595 C
ATOM 3475 C LEU A 450 -17.553 17.324 -33.711 1.00 63.99 C
ANISOU 3475 C LEU A 450 7634 8768 7913 -389 328 -574 C
ATOM 3476 O LEU A 450 -18.149 18.413 -33.630 1.00 60.04 O
ANISOU 3476 O LEU A 450 7143 8234 7436 -394 349 -591 O
ATOM 3477 CB LEU A 450 -15.667 16.766 -32.108 1.00 65.16 C
ANISOU 3477 CB LEU A 450 7717 8994 8045 -435 303 -613 C
ATOM 3478 CG LEU A 450 -15.247 16.311 -30.709 1.00 63.67 C
ANISOU 3478 CG LEU A 450 7496 8865 7829 -456 273 -640 C
ATOM 3479 CD1 LEU A 450 -13.742 16.415 -30.541 1.00 59.75 C
ANISOU 3479 CD1 LEU A 450 6962 8388 7352 -482 269 -652 C
ATOM 3480 CD2 LEU A 450 -15.964 17.124 -29.643 1.00 50.43 C
ANISOU 3480 CD2 LEU A 450 5824 7194 6144 -470 273 -685 C
ATOM 3481 N PRO A 451 -17.262 16.802 -34.910 1.00 59.46 N
ANISOU 3481 N PRO A 451 7081 8179 7333 -363 331 -538 N
ATOM 3482 CA PRO A 451 -17.767 17.477 -36.116 1.00 62.16 C
ANISOU 3482 CA PRO A 451 7458 8470 7690 -340 354 -514 C
ATOM 3483 C PRO A 451 -19.280 17.437 -36.230 1.00 64.68 C
ANISOU 3483 C PRO A 451 7799 8773 8003 -319 334 -503 C
ATOM 3484 O PRO A 451 -19.875 18.393 -36.741 1.00 59.30 O
ANISOU 3484 O PRO A 451 7136 8052 7344 -309 355 -496 O
ATOM 3485 CB PRO A 451 -17.089 16.710 -37.262 1.00 60.18 C
ANISOU 3485 CB PRO A 451 7227 8219 7417 -310 356 -480 C
ATOM 3486 CG PRO A 451 -15.892 16.081 -36.635 1.00 53.85 C
ANISOU 3486 CG PRO A 451 6390 7460 6612 -327 352 -490 C
ATOM 3487 CD PRO A 451 -16.345 15.703 -35.262 1.00 56.86 C
ANISOU 3487 CD PRO A 451 6745 7875 6983 -350 318 -518 C
ATOM 3488 N PHE A 452 -19.919 16.359 -35.769 1.00 51.33 N
ANISOU 3488 N PHE A 452 6103 7112 6290 -312 294 -497 N
ATOM 3489 CA PHE A 452 -21.378 16.311 -35.744 1.00 56.11 C
ANISOU 3489 CA PHE A 452 6715 7705 6899 -297 274 -483 C
ATOM 3490 C PHE A 452 -21.943 17.418 -34.862 1.00 63.79 C
ANISOU 3490 C PHE A 452 7670 8673 7895 -311 301 -509 C
ATOM 3491 O PHE A 452 -22.905 18.099 -35.236 1.00 63.91 O
ANISOU 3491 O PHE A 452 7696 8656 7931 -294 310 -497 O
ATOM 3492 CB PHE A 452 -21.846 14.937 -35.255 1.00 55.87 C
ANISOU 3492 CB PHE A 452 6672 7708 6850 -294 228 -468 C
ATOM 3493 CG PHE A 452 -23.341 14.811 -35.111 1.00 49.29 C
ANISOU 3493 CG PHE A 452 5830 6867 6029 -284 206 -447 C
ATOM 3494 CD1 PHE A 452 -23.981 15.211 -33.946 1.00 51.17 C
ANISOU 3494 CD1 PHE A 452 6038 7128 6277 -296 222 -458 C
ATOM 3495 CD2 PHE A 452 -24.104 14.274 -36.133 1.00 64.31 C
ANISOU 3495 CD2 PHE A 452 7757 8743 7936 -262 168 -415 C
ATOM 3496 CE1 PHE A 452 -25.353 15.095 -33.813 1.00 48.78 C
ANISOU 3496 CE1 PHE A 452 5720 6822 5994 -284 208 -431 C
ATOM 3497 CE2 PHE A 452 -25.477 14.151 -36.004 1.00 70.19 C
ANISOU 3497 CE2 PHE A 452 8484 9481 8703 -256 144 -391 C
ATOM 3498 CZ PHE A 452 -26.101 14.562 -34.841 1.00 59.37 C
ANISOU 3498 CZ PHE A 452 7074 8134 7348 -267 167 -395 C
ATOM 3499 N THR A 453 -21.354 17.608 -33.680 1.00 58.54 N
ANISOU 3499 N THR A 453 6979 8039 7224 -338 312 -545 N
ATOM 3500 CA THR A 453 -21.872 18.593 -32.736 1.00 54.82 C
ANISOU 3500 CA THR A 453 6498 7566 6766 -346 336 -579 C
ATOM 3501 C THR A 453 -21.640 20.013 -33.237 1.00 58.11 C
ANISOU 3501 C THR A 453 6931 7927 7221 -350 373 -597 C
ATOM 3502 O THR A 453 -22.551 20.849 -33.208 1.00 64.04 O
ANISOU 3502 O THR A 453 7691 8648 7995 -335 393 -601 O
ATOM 3503 CB THR A 453 -21.223 18.392 -31.365 1.00 57.60 C
ANISOU 3503 CB THR A 453 6825 7968 7092 -371 331 -618 C
ATOM 3504 OG1 THR A 453 -21.583 17.104 -30.849 1.00 58.12 O
ANISOU 3504 OG1 THR A 453 6874 8083 7125 -363 300 -592 O
ATOM 3505 CG2 THR A 453 -21.674 19.472 -30.392 1.00 55.23 C
ANISOU 3505 CG2 THR A 453 6524 7663 6797 -375 356 -664 C
ATOM 3506 N TYR A 454 -20.424 20.303 -33.703 1.00 51.10 N
ANISOU 3506 N TYR A 454 6045 7023 6346 -369 385 -603 N
ATOM 3507 CA TYR A 454 -20.110 21.652 -34.162 1.00 62.12 C
ANISOU 3507 CA TYR A 454 7454 8362 7788 -379 423 -614 C
ATOM 3508 C TYR A 454 -20.928 22.030 -35.390 1.00 66.79 C
ANISOU 3508 C TYR A 454 8074 8906 8396 -344 436 -569 C
ATOM 3509 O TYR A 454 -21.458 23.144 -35.469 1.00 68.84 O
ANISOU 3509 O TYR A 454 8346 9119 8692 -338 462 -576 O
ATOM 3510 CB TYR A 454 -18.615 21.772 -34.453 1.00 58.33 C
ANISOU 3510 CB TYR A 454 6960 7879 7324 -408 434 -616 C
ATOM 3511 CG TYR A 454 -18.260 22.915 -35.376 1.00 64.03 C
ANISOU 3511 CG TYR A 454 7695 8537 8097 -411 474 -599 C
ATOM 3512 CD1 TYR A 454 -18.393 24.235 -34.964 1.00 59.42 C
ANISOU 3512 CD1 TYR A 454 7114 7903 7561 -431 498 -633 C
ATOM 3513 CD2 TYR A 454 -17.788 22.673 -36.660 1.00 64.69 C
ANISOU 3513 CD2 TYR A 454 7792 8608 8179 -392 491 -546 C
ATOM 3514 CE1 TYR A 454 -18.069 25.282 -35.807 1.00 67.16 C
ANISOU 3514 CE1 TYR A 454 8105 8818 8595 -435 536 -609 C
ATOM 3515 CE2 TYR A 454 -17.461 23.713 -37.508 1.00 69.62 C
ANISOU 3515 CE2 TYR A 454 8428 9176 8849 -393 533 -520 C
ATOM 3516 CZ TYR A 454 -17.603 25.015 -37.077 1.00 73.02 C
ANISOU 3516 CZ TYR A 454 8856 9553 9334 -417 555 -548 C
ATOM 3517 OH TYR A 454 -17.277 26.053 -37.920 1.00 72.93 O
ANISOU 3517 OH TYR A 454 8855 9480 9376 -419 599 -515 O
ATOM 3518 N MET A 455 -21.047 21.116 -36.357 1.00 65.18 N
ANISOU 3518 N MET A 455 7886 8714 8165 -319 415 -525 N
ATOM 3519 CA MET A 455 -21.780 21.431 -37.580 1.00 67.83 C
ANISOU 3519 CA MET A 455 8253 9011 8507 -283 420 -482 C
ATOM 3520 C MET A 455 -23.266 21.626 -37.303 1.00 60.34 C
ANISOU 3520 C MET A 455 7303 8054 7568 -262 406 -476 C
ATOM 3521 O MET A 455 -23.895 22.525 -37.875 1.00 55.59 O
ANISOU 3521 O MET A 455 6718 7408 6994 -241 425 -457 O
ATOM 3522 CB MET A 455 -21.554 20.335 -38.622 1.00 66.76 C
ANISOU 3522 CB MET A 455 8140 8892 8332 -258 393 -445 C
ATOM 3523 CG MET A 455 -22.406 20.475 -39.873 1.00 52.66 C
ANISOU 3523 CG MET A 455 6392 7077 6539 -216 382 -401 C
ATOM 3524 SD MET A 455 -23.863 19.415 -39.826 1.00 69.30 S
ANISOU 3524 SD MET A 455 8500 9205 8626 -195 316 -387 S
ATOM 3525 CE MET A 455 -25.056 20.438 -40.682 1.00 51.11 C
ANISOU 3525 CE MET A 455 6216 6855 6347 -160 319 -352 C
ATOM 3526 N LEU A 456 -23.846 20.799 -36.429 1.00 58.83 N
ANISOU 3526 N LEU A 456 7089 7905 7358 -265 377 -487 N
ATOM 3527 CA LEU A 456 -25.251 20.968 -36.072 1.00 64.44 C
ANISOU 3527 CA LEU A 456 7788 8614 8084 -245 370 -478 C
ATOM 3528 C LEU A 456 -25.484 22.317 -35.406 1.00 66.07 C
ANISOU 3528 C LEU A 456 7990 8790 8325 -246 415 -511 C
ATOM 3529 O LEU A 456 -26.410 23.053 -35.770 1.00 64.49 O
ANISOU 3529 O LEU A 456 7795 8554 8154 -219 428 -492 O
ATOM 3530 CB LEU A 456 -25.706 19.828 -35.157 1.00 60.18 C
ANISOU 3530 CB LEU A 456 7218 8127 7520 -252 338 -478 C
ATOM 3531 CG LEU A 456 -27.175 19.788 -34.711 1.00 52.03 C
ANISOU 3531 CG LEU A 456 6160 7104 6504 -231 332 -457 C
ATOM 3532 CD1 LEU A 456 -27.622 18.350 -34.523 1.00 52.54 C
ANISOU 3532 CD1 LEU A 456 6203 7208 6552 -234 284 -427 C
ATOM 3533 CD2 LEU A 456 -27.416 20.577 -33.427 1.00 49.97 C
ANISOU 3533 CD2 LEU A 456 5880 6855 6250 -233 374 -496 C
ATOM 3534 N GLU A 457 -24.652 22.658 -34.420 1.00 65.27 N
ANISOU 3534 N GLU A 457 7879 8701 8220 -277 434 -562 N
ATOM 3535 CA GLU A 457 -24.849 23.907 -33.696 1.00 67.98 C
ANISOU 3535 CA GLU A 457 8224 9012 8594 -278 472 -606 C
ATOM 3536 C GLU A 457 -24.559 25.117 -34.573 1.00 70.34 C
ANISOU 3536 C GLU A 457 8548 9238 8940 -275 503 -598 C
ATOM 3537 O GLU A 457 -25.211 26.157 -34.422 1.00 70.82 O
ANISOU 3537 O GLU A 457 8617 9254 9038 -257 532 -610 O
ATOM 3538 CB GLU A 457 -23.975 23.929 -32.440 1.00 64.13 C
ANISOU 3538 CB GLU A 457 7724 8556 8086 -312 474 -668 C
ATOM 3539 CG GLU A 457 -24.278 25.071 -31.476 1.00 63.68 C
ANISOU 3539 CG GLU A 457 7674 8473 8046 -309 505 -725 C
ATOM 3540 CD GLU A 457 -25.520 24.832 -30.628 1.00 71.47 C
ANISOU 3540 CD GLU A 457 8649 9497 9010 -275 512 -727 C
ATOM 3541 OE1 GLU A 457 -26.533 24.324 -31.156 1.00 68.36 O
ANISOU 3541 OE1 GLU A 457 8242 9111 8619 -245 505 -671 O
ATOM 3542 OE2 GLU A 457 -25.480 25.153 -29.421 1.00 71.15 O
ANISOU 3542 OE2 GLU A 457 8609 9478 8946 -276 525 -783 O
ATOM 3543 N LYS A 458 -23.597 25.005 -35.492 1.00 66.48 N
ANISOU 3543 N LYS A 458 8070 8736 8455 -290 502 -574 N
ATOM 3544 CA LYS A 458 -23.331 26.114 -36.402 1.00 67.92 C
ANISOU 3544 CA LYS A 458 8275 8849 8684 -286 536 -553 C
ATOM 3545 C LYS A 458 -24.511 26.353 -37.334 1.00 62.19 C
ANISOU 3545 C LYS A 458 7567 8095 7968 -238 536 -500 C
ATOM 3546 O LYS A 458 -24.824 27.502 -37.665 1.00 63.16 O
ANISOU 3546 O LYS A 458 7704 8156 8137 -223 568 -490 O
ATOM 3547 CB LYS A 458 -22.057 25.854 -37.206 1.00 60.67 C
ANISOU 3547 CB LYS A 458 7361 7931 7761 -306 541 -528 C
ATOM 3548 CG LYS A 458 -21.737 26.969 -38.186 1.00 65.40 C
ANISOU 3548 CG LYS A 458 7979 8461 8408 -301 582 -494 C
ATOM 3549 CD LYS A 458 -20.261 27.026 -38.519 1.00 74.83 C
ANISOU 3549 CD LYS A 458 9163 9651 9618 -335 602 -486 C
ATOM 3550 CE LYS A 458 -19.904 28.370 -39.133 1.00 80.51 C
ANISOU 3550 CE LYS A 458 9892 10292 10404 -342 650 -460 C
ATOM 3551 NZ LYS A 458 -20.289 29.500 -38.238 1.00 78.18 N
ANISOU 3551 NZ LYS A 458 9596 9942 10166 -361 662 -512 N
ATOM 3552 N TRP A 459 -25.181 25.281 -37.762 1.00 57.35 N
ANISOU 3552 N TRP A 459 6953 7523 7316 -214 496 -464 N
ATOM 3553 CA TRP A 459 -26.361 25.441 -38.604 1.00 61.58 C
ANISOU 3553 CA TRP A 459 7500 8038 7860 -170 484 -414 C
ATOM 3554 C TRP A 459 -27.459 26.202 -37.872 1.00 69.78 C
ANISOU 3554 C TRP A 459 8521 9055 8935 -150 503 -430 C
ATOM 3555 O TRP A 459 -28.106 27.081 -38.452 1.00 65.18 O
ANISOU 3555 O TRP A 459 7951 8425 8389 -118 520 -400 O
ATOM 3556 CB TRP A 459 -26.867 24.075 -39.067 1.00 56.88 C
ANISOU 3556 CB TRP A 459 6902 7490 7220 -154 427 -383 C
ATOM 3557 CG TRP A 459 -28.069 24.158 -39.959 1.00 64.29 C
ANISOU 3557 CG TRP A 459 7850 8411 8168 -112 401 -332 C
ATOM 3558 CD1 TRP A 459 -28.074 24.271 -41.320 1.00 63.82 C
ANISOU 3558 CD1 TRP A 459 7825 8328 8093 -84 388 -286 C
ATOM 3559 CD2 TRP A 459 -29.442 24.139 -39.553 1.00 62.79 C
ANISOU 3559 CD2 TRP A 459 7629 8228 8001 -90 383 -319 C
ATOM 3560 NE1 TRP A 459 -29.366 24.322 -41.785 1.00 64.43 N
ANISOU 3560 NE1 TRP A 459 7897 8399 8184 -48 355 -248 N
ATOM 3561 CE2 TRP A 459 -30.225 24.243 -40.720 1.00 63.03 C
ANISOU 3561 CE2 TRP A 459 7675 8238 8034 -53 352 -265 C
ATOM 3562 CE3 TRP A 459 -30.086 24.044 -38.316 1.00 61.25 C
ANISOU 3562 CE3 TRP A 459 7393 8058 7822 -96 391 -343 C
ATOM 3563 CZ2 TRP A 459 -31.617 24.254 -40.687 1.00 61.54 C
ANISOU 3563 CZ2 TRP A 459 7457 8052 7875 -25 326 -235 C
ATOM 3564 CZ3 TRP A 459 -31.468 24.055 -38.284 1.00 62.01 C
ANISOU 3564 CZ3 TRP A 459 7459 8157 7945 -66 374 -310 C
ATOM 3565 CH2 TRP A 459 -32.219 24.159 -39.462 1.00 64.55 C
ANISOU 3565 CH2 TRP A 459 7791 8457 8279 -32 340 -256 C
ATOM 3566 N ARG A 460 -27.678 25.887 -36.592 1.00 72.34 N
ANISOU 3566 N ARG A 460 8819 9417 9250 -163 503 -473 N
ATOM 3567 CA ARG A 460 -28.704 26.588 -35.827 1.00 62.85 C
ANISOU 3567 CA ARG A 460 7602 8202 8078 -137 529 -489 C
ATOM 3568 C ARG A 460 -28.287 28.023 -35.529 1.00 69.59 C
ANISOU 3568 C ARG A 460 8476 8990 8975 -141 578 -531 C
ATOM 3569 O ARG A 460 -29.131 28.927 -35.507 1.00 65.51 O
ANISOU 3569 O ARG A 460 7962 8430 8499 -106 606 -526 O
ATOM 3570 CB ARG A 460 -29.008 25.833 -34.534 1.00 62.03 C
ANISOU 3570 CB ARG A 460 7467 8161 7942 -145 520 -520 C
ATOM 3571 CG ARG A 460 -29.632 24.466 -34.757 1.00 63.01 C
ANISOU 3571 CG ARG A 460 7565 8339 8038 -139 472 -474 C
ATOM 3572 CD ARG A 460 -30.381 23.979 -33.525 1.00 54.84 C
ANISOU 3572 CD ARG A 460 6491 7355 6989 -132 478 -483 C
ATOM 3573 NE ARG A 460 -29.492 23.702 -32.404 1.00 64.88 N
ANISOU 3573 NE ARG A 460 7764 8667 8222 -162 488 -537 N
ATOM 3574 CZ ARG A 460 -29.882 23.164 -31.256 1.00 63.09 C
ANISOU 3574 CZ ARG A 460 7508 8494 7967 -159 494 -547 C
ATOM 3575 NH1 ARG A 460 -31.145 22.834 -31.042 1.00 60.15 N
ANISOU 3575 NH1 ARG A 460 7101 8146 7608 -129 496 -505 N
ATOM 3576 NH2 ARG A 460 -28.982 22.950 -30.301 1.00 57.97 N
ANISOU 3576 NH2 ARG A 460 6865 7882 7277 -185 498 -596 N
ATOM 3577 N TRP A 461 -26.992 28.253 -35.293 1.00 63.84 N
ANISOU 3577 N TRP A 461 7761 8251 8247 -184 588 -572 N
ATOM 3578 CA TRP A 461 -26.507 29.617 -35.113 1.00 60.16 C
ANISOU 3578 CA TRP A 461 7314 7710 7832 -197 627 -610 C
ATOM 3579 C TRP A 461 -26.781 30.465 -36.348 1.00 74.42 C
ANISOU 3579 C TRP A 461 9143 9447 9688 -170 648 -553 C
ATOM 3580 O TRP A 461 -27.184 31.627 -36.235 1.00 81.37 O
ANISOU 3580 O TRP A 461 10036 10260 10620 -150 682 -566 O
ATOM 3581 CB TRP A 461 -25.012 29.610 -34.793 1.00 63.55 C
ANISOU 3581 CB TRP A 461 7745 8142 8260 -254 625 -652 C
ATOM 3582 CG TRP A 461 -24.685 29.181 -33.395 1.00 70.02 C
ANISOU 3582 CG TRP A 461 8549 9014 9042 -279 610 -721 C
ATOM 3583 CD1 TRP A 461 -25.548 29.084 -32.342 1.00 65.75 C
ANISOU 3583 CD1 TRP A 461 8001 8505 8474 -254 613 -756 C
ATOM 3584 CD2 TRP A 461 -23.400 28.789 -32.898 1.00 70.45 C
ANISOU 3584 CD2 TRP A 461 8592 9099 9077 -330 590 -759 C
ATOM 3585 NE1 TRP A 461 -24.879 28.656 -31.220 1.00 65.49 N
ANISOU 3585 NE1 TRP A 461 7959 8523 8400 -285 596 -814 N
ATOM 3586 CE2 TRP A 461 -23.559 28.468 -31.535 1.00 71.13 C
ANISOU 3586 CE2 TRP A 461 8670 9237 9120 -333 578 -818 C
ATOM 3587 CE3 TRP A 461 -22.130 28.677 -33.474 1.00 61.39 C
ANISOU 3587 CE3 TRP A 461 7438 7943 7943 -370 584 -745 C
ATOM 3588 CZ2 TRP A 461 -22.496 28.043 -30.740 1.00 69.56 C
ANISOU 3588 CZ2 TRP A 461 8458 9082 8892 -376 552 -864 C
ATOM 3589 CZ3 TRP A 461 -21.076 28.256 -32.682 1.00 60.58 C
ANISOU 3589 CZ3 TRP A 461 7316 7882 7819 -414 560 -790 C
ATOM 3590 CH2 TRP A 461 -21.266 27.943 -31.331 1.00 64.35 C
ANISOU 3590 CH2 TRP A 461 7787 8411 8253 -417 541 -850 C
ATOM 3591 N MET A 462 -26.577 29.897 -37.539 1.00 71.59 N
ANISOU 3591 N MET A 462 8791 9102 9309 -164 629 -490 N
ATOM 3592 CA MET A 462 -26.798 30.658 -38.764 1.00 66.07 C
ANISOU 3592 CA MET A 462 8115 8343 8645 -135 648 -428 C
ATOM 3593 C MET A 462 -28.283 30.819 -39.068 1.00 68.98 C
ANISOU 3593 C MET A 462 8480 8705 9023 -78 639 -389 C
ATOM 3594 O MET A 462 -28.688 31.835 -39.645 1.00 72.05 O
ANISOU 3594 O MET A 462 8885 9030 9460 -48 666 -355 O
ATOM 3595 CB MET A 462 -26.081 29.987 -39.934 1.00 62.12 C
ANISOU 3595 CB MET A 462 7630 7866 8108 -140 631 -375 C
ATOM 3596 CG MET A 462 -24.573 29.895 -39.755 1.00 73.93 C
ANISOU 3596 CG MET A 462 9122 9366 9604 -192 646 -402 C
ATOM 3597 SD MET A 462 -23.792 28.819 -40.972 1.00 66.81 S
ANISOU 3597 SD MET A 462 8233 8511 8642 -187 628 -346 S
ATOM 3598 CE MET A 462 -24.266 29.633 -42.494 1.00 62.97 C
ANISOU 3598 CE MET A 462 7785 7970 8172 -137 652 -261 C
ATOM 3599 N VAL A 463 -29.105 29.838 -38.692 1.00 69.62 N
ANISOU 3599 N VAL A 463 8536 8850 9068 -64 602 -387 N
ATOM 3600 CA VAL A 463 -30.547 29.964 -38.881 1.00 60.46 C
ANISOU 3600 CA VAL A 463 7359 7687 7926 -12 592 -348 C
ATOM 3601 C VAL A 463 -31.103 31.072 -37.994 1.00 67.32 C
ANISOU 3601 C VAL A 463 8221 8511 8846 9 639 -385 C
ATOM 3602 O VAL A 463 -31.886 31.917 -38.443 1.00 80.59 O
ANISOU 3602 O VAL A 463 9906 10143 10573 54 658 -350 O
ATOM 3603 CB VAL A 463 -31.245 28.619 -38.610 1.00 57.51 C
ANISOU 3603 CB VAL A 463 6951 7390 7509 -9 541 -336 C
ATOM 3604 CG1 VAL A 463 -32.742 28.816 -38.442 1.00 57.41 C
ANISOU 3604 CG1 VAL A 463 6905 7379 7529 38 538 -305 C
ATOM 3605 CG2 VAL A 463 -30.963 27.642 -39.739 1.00 63.19 C
ANISOU 3605 CG2 VAL A 463 7686 8137 8185 -14 489 -291 C
ATOM 3606 N PHE A 464 -30.701 31.087 -36.721 1.00 71.07 N
ANISOU 3606 N PHE A 464 8688 9002 9312 -17 659 -458 N
ATOM 3607 CA PHE A 464 -31.157 32.136 -35.816 1.00 74.93 C
ANISOU 3607 CA PHE A 464 9180 9447 9843 7 705 -506 C
ATOM 3608 C PHE A 464 -30.607 33.495 -36.232 1.00 76.97 C
ANISOU 3608 C PHE A 464 9475 9607 10162 4 742 -516 C
ATOM 3609 O PHE A 464 -31.320 34.504 -36.175 1.00 77.23 O
ANISOU 3609 O PHE A 464 9517 9581 10248 47 777 -514 O
ATOM 3610 CB PHE A 464 -30.752 31.802 -34.380 1.00 66.68 C
ANISOU 3610 CB PHE A 464 8128 8447 8762 -21 712 -586 C
ATOM 3611 CG PHE A 464 -31.327 30.508 -33.874 1.00 68.36 C
ANISOU 3611 CG PHE A 464 8301 8751 8920 -16 682 -572 C
ATOM 3612 CD1 PHE A 464 -32.548 30.047 -34.340 1.00 68.64 C
ANISOU 3612 CD1 PHE A 464 8305 8813 8963 24 666 -505 C
ATOM 3613 CD2 PHE A 464 -30.646 29.749 -32.935 1.00 69.78 C
ANISOU 3613 CD2 PHE A 464 8475 8992 9048 -54 669 -620 C
ATOM 3614 CE1 PHE A 464 -33.078 28.856 -33.879 1.00 68.83 C
ANISOU 3614 CE1 PHE A 464 8288 8914 8948 24 638 -485 C
ATOM 3615 CE2 PHE A 464 -31.171 28.557 -32.470 1.00 64.97 C
ANISOU 3615 CE2 PHE A 464 7830 8462 8394 -50 644 -598 C
ATOM 3616 CZ PHE A 464 -32.389 28.111 -32.942 1.00 64.86 C
ANISOU 3616 CZ PHE A 464 7782 8468 8395 -13 630 -530 C
ATOM 3617 N LYS A 465 -29.345 33.538 -36.668 1.00 71.09 N
ANISOU 3617 N LYS A 465 8750 8843 9418 -45 738 -521 N
ATOM 3618 CA LYS A 465 -28.740 34.782 -37.125 1.00 74.44 C
ANISOU 3618 CA LYS A 465 9204 9170 9908 -56 773 -519 C
ATOM 3619 C LYS A 465 -29.335 35.275 -38.439 1.00 82.94 C
ANISOU 3619 C LYS A 465 10292 10202 11018 -11 782 -430 C
ATOM 3620 O LYS A 465 -29.118 36.436 -38.801 1.00 81.17 O
ANISOU 3620 O LYS A 465 10093 9889 10860 -6 818 -418 O
ATOM 3621 CB LYS A 465 -27.226 34.599 -37.267 1.00 68.94 C
ANISOU 3621 CB LYS A 465 8514 8474 9206 -121 767 -536 C
ATOM 3622 CG LYS A 465 -26.421 35.885 -37.174 1.00 81.44 C
ANISOU 3622 CG LYS A 465 10118 9958 10866 -153 803 -567 C
ATOM 3623 CD LYS A 465 -24.946 35.594 -36.932 1.00 92.32 C
ANISOU 3623 CD LYS A 465 11487 11351 12238 -224 791 -601 C
ATOM 3624 CE LYS A 465 -24.739 34.833 -35.628 1.00 88.35 C
ANISOU 3624 CE LYS A 465 10968 10921 11680 -250 761 -682 C
ATOM 3625 NZ LYS A 465 -23.297 34.638 -35.307 1.00 79.51 N
ANISOU 3625 NZ LYS A 465 9835 9812 10562 -319 746 -719 N
ATOM 3626 N GLY A 466 -30.080 34.433 -39.151 1.00 86.25 N
ANISOU 3626 N GLY A 466 10698 10678 11395 22 747 -367 N
ATOM 3627 CA GLY A 466 -30.703 34.836 -40.396 1.00 70.63 C
ANISOU 3627 CA GLY A 466 8731 8667 9437 69 745 -281 C
ATOM 3628 C GLY A 466 -29.844 34.667 -41.626 1.00 72.57 C
ANISOU 3628 C GLY A 466 9002 8909 9661 53 738 -223 C
ATOM 3629 O GLY A 466 -30.148 35.267 -42.663 1.00 74.35 O
ANISOU 3629 O GLY A 466 9248 9092 9909 91 748 -152 O
ATOM 3630 N GLU A 467 -28.784 33.870 -41.548 1.00 76.14 N
ANISOU 3630 N GLU A 467 9454 9406 10068 4 724 -247 N
ATOM 3631 CA GLU A 467 -27.865 33.668 -42.658 1.00 69.18 C
ANISOU 3631 CA GLU A 467 8596 8527 9161 -8 726 -195 C
ATOM 3632 C GLU A 467 -28.274 32.519 -43.572 1.00 66.19 C
ANISOU 3632 C GLU A 467 8224 8219 8707 22 673 -144 C
ATOM 3633 O GLU A 467 -27.621 32.303 -44.596 1.00 58.08 O
ANISOU 3633 O GLU A 467 7223 7200 7646 25 675 -96 O
ATOM 3634 CB GLU A 467 -26.449 33.431 -42.121 1.00 74.99 C
ANISOU 3634 CB GLU A 467 9325 9274 9894 -72 740 -245 C
ATOM 3635 CG GLU A 467 -25.913 34.577 -41.270 1.00 77.25 C
ANISOU 3635 CG GLU A 467 9608 9485 10258 -109 782 -300 C
ATOM 3636 CD GLU A 467 -24.591 34.247 -40.602 1.00 84.37 C
ANISOU 3636 CD GLU A 467 10493 10407 11156 -175 782 -356 C
ATOM 3637 OE1 GLU A 467 -24.208 33.059 -40.598 1.00 93.18 O
ANISOU 3637 OE1 GLU A 467 11597 11602 12206 -189 751 -359 O
ATOM 3638 OE2 GLU A 467 -23.936 35.175 -40.081 1.00 97.34 O
ANISOU 3638 OE2 GLU A 467 12135 11985 12866 -214 810 -396 O
ATOM 3639 N ILE A 468 -29.322 31.777 -43.232 1.00 69.65 N
ANISOU 3639 N ILE A 468 8640 8706 9118 43 627 -153 N
ATOM 3640 CA ILE A 468 -29.812 30.699 -44.088 1.00 62.71 C
ANISOU 3640 CA ILE A 468 7767 7884 8174 69 566 -109 C
ATOM 3641 C ILE A 468 -31.294 30.909 -44.351 1.00 68.64 C
ANISOU 3641 C ILE A 468 8504 8631 8945 121 537 -69 C
ATOM 3642 O ILE A 468 -32.110 30.817 -43.417 1.00 74.30 O
ANISOU 3642 O ILE A 468 9182 9362 9688 124 530 -99 O
ATOM 3643 CB ILE A 468 -29.550 29.321 -43.459 1.00 67.03 C
ANISOU 3643 CB ILE A 468 8294 8504 8670 35 525 -154 C
ATOM 3644 CG1 ILE A 468 -28.050 29.113 -43.227 1.00 65.17 C
ANISOU 3644 CG1 ILE A 468 8068 8276 8418 -13 553 -189 C
ATOM 3645 CG2 ILE A 468 -30.103 28.220 -44.353 1.00 59.61 C
ANISOU 3645 CG2 ILE A 468 7365 7612 7670 61 455 -115 C
ATOM 3646 CD1 ILE A 468 -27.704 27.786 -42.582 1.00 65.78 C
ANISOU 3646 CD1 ILE A 468 8125 8420 8446 -44 515 -231 C
ATOM 3647 N PRO A 469 -31.698 31.192 -45.586 1.00 75.25 N
ANISOU 3647 N PRO A 469 9369 9453 9771 166 519 1 N
ATOM 3648 CA PRO A 469 -33.118 31.400 -45.877 1.00 71.40 C
ANISOU 3648 CA PRO A 469 8860 8962 9306 217 485 45 C
ATOM 3649 C PRO A 469 -33.919 30.114 -45.720 1.00 72.46 C
ANISOU 3649 C PRO A 469 8962 9164 9404 216 408 38 C
ATOM 3650 O PRO A 469 -33.385 29.004 -45.757 1.00 72.60 O
ANISOU 3650 O PRO A 469 8988 9230 9366 186 372 15 O
ATOM 3651 CB PRO A 469 -33.125 31.880 -47.332 1.00 69.97 C
ANISOU 3651 CB PRO A 469 8724 8756 9104 261 478 123 C
ATOM 3652 CG PRO A 469 -31.721 32.334 -47.603 1.00 64.15 C
ANISOU 3652 CG PRO A 469 8026 7988 8361 234 538 121 C
ATOM 3653 CD PRO A 469 -30.852 31.449 -46.764 1.00 81.23 C
ANISOU 3653 CD PRO A 469 10175 10192 10497 176 537 50 C
ATOM 3654 N LYS A 470 -35.234 30.289 -45.554 1.00 72.48 N
ANISOU 3654 N LYS A 470 8924 9168 9447 250 383 64 N
ATOM 3655 CA LYS A 470 -36.118 29.149 -45.325 1.00 69.72 C
ANISOU 3655 CA LYS A 470 8531 8877 9084 247 312 64 C
ATOM 3656 C LYS A 470 -36.103 28.184 -46.504 1.00 73.95 C
ANISOU 3656 C LYS A 470 9099 9448 9553 253 229 97 C
ATOM 3657 O LYS A 470 -36.109 26.962 -46.314 1.00 67.36 O
ANISOU 3657 O LYS A 470 8251 8660 8684 224 174 74 O
ATOM 3658 CB LYS A 470 -37.540 29.636 -45.053 1.00 64.38 C
ANISOU 3658 CB LYS A 470 7799 8191 8472 289 305 99 C
ATOM 3659 CG LYS A 470 -37.765 30.147 -43.642 1.00 64.44 C
ANISOU 3659 CG LYS A 470 7764 8186 8534 282 372 54 C
ATOM 3660 CD LYS A 470 -39.114 30.840 -43.517 1.00 73.17 C
ANISOU 3660 CD LYS A 470 8820 9272 9707 338 380 97 C
ATOM 3661 CE LYS A 470 -40.242 29.952 -44.014 1.00 75.58 C
ANISOU 3661 CE LYS A 470 9078 9627 10014 353 292 150 C
ATOM 3662 NZ LYS A 470 -41.575 30.596 -43.850 1.00 73.15 N
ANISOU 3662 NZ LYS A 470 8709 9306 9779 408 300 197 N
ATOM 3663 N ASP A 471 -36.083 28.710 -47.729 1.00 87.60 N
ANISOU 3663 N ASP A 471 10872 11153 11258 293 217 150 N
ATOM 3664 CA ASP A 471 -36.074 27.855 -48.911 1.00 85.03 C
ANISOU 3664 CA ASP A 471 10590 10861 10858 308 137 177 C
ATOM 3665 C ASP A 471 -34.734 27.168 -49.140 1.00 80.07 C
ANISOU 3665 C ASP A 471 10012 10252 10158 277 149 141 C
ATOM 3666 O ASP A 471 -34.584 26.468 -50.148 1.00 76.99 O
ANISOU 3666 O ASP A 471 9668 9887 9696 295 90 157 O
ATOM 3667 CB ASP A 471 -36.462 28.668 -50.149 1.00 83.20 C
ANISOU 3667 CB ASP A 471 10394 10603 10614 368 125 250 C
ATOM 3668 CG ASP A 471 -35.470 29.773 -50.458 1.00 86.33 C
ANISOU 3668 CG ASP A 471 10838 10952 11014 378 215 267 C
ATOM 3669 OD1 ASP A 471 -34.763 30.218 -49.531 1.00 92.41 O
ANISOU 3669 OD1 ASP A 471 11593 11694 11824 341 291 224 O
ATOM 3670 OD2 ASP A 471 -35.401 30.201 -51.629 1.00 92.39 O
ANISOU 3670 OD2 ASP A 471 11654 11707 11742 422 208 327 O
ATOM 3671 N GLN A 472 -33.761 27.348 -48.241 1.00 75.74 N
ANISOU 3671 N GLN A 472 9456 9693 9628 235 221 93 N
ATOM 3672 CA GLN A 472 -32.459 26.700 -48.355 1.00 76.66 C
ANISOU 3672 CA GLN A 472 9611 9830 9687 206 237 61 C
ATOM 3673 C GLN A 472 -32.018 26.074 -47.036 1.00 77.86 C
ANISOU 3673 C GLN A 472 9723 10005 9856 151 253 -5 C
ATOM 3674 O GLN A 472 -30.815 25.908 -46.809 1.00 78.59 O
ANISOU 3674 O GLN A 472 9832 10102 9927 121 293 -36 O
ATOM 3675 CB GLN A 472 -31.401 27.691 -48.847 1.00 81.59 C
ANISOU 3675 CB GLN A 472 10277 10416 10310 213 315 83 C
ATOM 3676 CG GLN A 472 -31.606 28.163 -50.277 1.00 91.05 C
ANISOU 3676 CG GLN A 472 11526 11600 11469 271 303 154 C
ATOM 3677 CD GLN A 472 -30.534 29.133 -50.727 1.00 98.66 C
ANISOU 3677 CD GLN A 472 12524 12524 12438 276 388 186 C
ATOM 3678 OE1 GLN A 472 -29.748 29.628 -49.919 1.00 98.02 O
ANISOU 3678 OE1 GLN A 472 12421 12415 12406 234 456 153 O
ATOM 3679 NE2 GLN A 472 -30.494 29.409 -52.025 1.00117.72 N
ANISOU 3679 NE2 GLN A 472 14992 14937 14801 327 385 252 N
ATOM 3680 N TRP A 473 -32.966 25.726 -46.162 1.00 73.63 N
ANISOU 3680 N TRP A 473 9132 9486 9359 139 224 -22 N
ATOM 3681 CA TRP A 473 -32.614 25.116 -44.884 1.00 66.55 C
ANISOU 3681 CA TRP A 473 8198 8616 8473 92 239 -78 C
ATOM 3682 C TRP A 473 -31.982 23.744 -45.085 1.00 70.29 C
ANISOU 3682 C TRP A 473 8691 9130 8885 68 192 -100 C
ATOM 3683 O TRP A 473 -30.867 23.484 -44.618 1.00 63.12 O
ANISOU 3683 O TRP A 473 7792 8233 7959 36 226 -138 O
ATOM 3684 CB TRP A 473 -33.851 25.013 -43.989 1.00 66.68 C
ANISOU 3684 CB TRP A 473 8149 8645 8540 93 221 -78 C
ATOM 3685 CG TRP A 473 -34.082 26.217 -43.131 1.00 68.73 C
ANISOU 3685 CG TRP A 473 8384 8872 8859 100 294 -92 C
ATOM 3686 CD1 TRP A 473 -33.441 27.418 -43.213 1.00 67.55 C
ANISOU 3686 CD1 TRP A 473 8263 8673 8731 107 360 -98 C
ATOM 3687 CD2 TRP A 473 -35.014 26.333 -42.048 1.00 60.80 C
ANISOU 3687 CD2 TRP A 473 7320 7878 7902 104 309 -102 C
ATOM 3688 NE1 TRP A 473 -33.921 28.278 -42.254 1.00 66.17 N
ANISOU 3688 NE1 TRP A 473 8057 8473 8613 116 411 -119 N
ATOM 3689 CE2 TRP A 473 -34.886 27.635 -41.525 1.00 66.20 C
ANISOU 3689 CE2 TRP A 473 8007 8516 8628 118 384 -122 C
ATOM 3690 CE3 TRP A 473 -35.945 25.463 -41.472 1.00 52.97 C
ANISOU 3690 CE3 TRP A 473 6272 6930 6923 100 269 -93 C
ATOM 3691 CZ2 TRP A 473 -35.654 28.088 -40.454 1.00 68.71 C
ANISOU 3691 CZ2 TRP A 473 8281 8834 8992 133 422 -138 C
ATOM 3692 CZ3 TRP A 473 -36.707 25.916 -40.409 1.00 62.70 C
ANISOU 3692 CZ3 TRP A 473 7454 8166 8204 113 311 -100 C
ATOM 3693 CH2 TRP A 473 -36.556 27.216 -39.911 1.00 67.49 C
ANISOU 3693 CH2 TRP A 473 8071 8730 8843 133 388 -126 C
ATOM 3694 N MET A 474 -32.686 22.849 -45.780 1.00 72.07 N
ANISOU 3694 N MET A 474 8924 9376 9084 84 108 -77 N
ATOM 3695 CA MET A 474 -32.175 21.495 -45.965 1.00 68.21 C
ANISOU 3695 CA MET A 474 8456 8917 8542 66 57 -101 C
ATOM 3696 C MET A 474 -31.033 21.455 -46.971 1.00 75.41 C
ANISOU 3696 C MET A 474 9438 9826 9387 83 74 -100 C
ATOM 3697 O MET A 474 -30.179 20.563 -46.900 1.00 74.10 O
ANISOU 3697 O MET A 474 9292 9681 9182 65 68 -130 O
ATOM 3698 CB MET A 474 -33.304 20.561 -46.397 1.00 59.66 C
ANISOU 3698 CB MET A 474 7361 7849 7458 75 -44 -81 C
ATOM 3699 CG MET A 474 -34.443 20.470 -45.393 1.00 73.13 C
ANISOU 3699 CG MET A 474 8988 9565 9235 57 -58 -73 C
ATOM 3700 SD MET A 474 -33.865 20.140 -43.715 1.00 79.46 S
ANISOU 3700 SD MET A 474 9742 10390 10059 8 2 -120 S
ATOM 3701 CE MET A 474 -32.939 18.631 -43.969 1.00 77.43 C
ANISOU 3701 CE MET A 474 9524 10154 9742 -18 -47 -150 C
ATOM 3702 N LYS A 475 -31.000 22.401 -47.911 1.00 76.92 N
ANISOU 3702 N LYS A 475 9667 9992 9567 122 99 -60 N
ATOM 3703 CA LYS A 475 -29.880 22.471 -48.842 1.00 75.45 C
ANISOU 3703 CA LYS A 475 9545 9806 9319 143 131 -50 C
ATOM 3704 C LYS A 475 -28.588 22.824 -48.116 1.00 78.79 C
ANISOU 3704 C LYS A 475 9955 10224 9760 107 216 -79 C
ATOM 3705 O LYS A 475 -27.547 22.201 -48.351 1.00 79.15 O
ANISOU 3705 O LYS A 475 10027 10288 9758 102 228 -95 O
ATOM 3706 CB LYS A 475 -30.176 23.488 -49.944 1.00 81.40 C
ANISOU 3706 CB LYS A 475 10336 10532 10060 194 145 8 C
ATOM 3707 CG LYS A 475 -29.083 23.611 -50.992 1.00 91.78 C
ANISOU 3707 CG LYS A 475 11717 11849 11306 224 185 32 C
ATOM 3708 CD LYS A 475 -29.387 24.734 -51.969 1.00 94.55 C
ANISOU 3708 CD LYS A 475 12100 12172 11651 274 210 99 C
ATOM 3709 CE LYS A 475 -28.269 24.911 -52.981 1.00103.55 C
ANISOU 3709 CE LYS A 475 13303 13317 12725 306 263 132 C
ATOM 3710 NZ LYS A 475 -28.519 26.077 -53.872 1.00126.64 N
ANISOU 3710 NZ LYS A 475 16257 16213 15649 354 296 206 N
ATOM 3711 N LYS A 476 -28.640 23.816 -47.222 1.00 73.57 N
ANISOU 3711 N LYS A 476 9251 9535 9166 83 272 -87 N
ATOM 3712 CA LYS A 476 -27.458 24.182 -46.449 1.00 66.95 C
ANISOU 3712 CA LYS A 476 8395 8690 8352 43 342 -120 C
ATOM 3713 C LYS A 476 -27.111 23.121 -45.415 1.00 66.29 C
ANISOU 3713 C LYS A 476 8280 8645 8262 2 321 -173 C
ATOM 3714 O LYS A 476 -25.933 22.939 -45.091 1.00 66.24 O
ANISOU 3714 O LYS A 476 8272 8651 8247 -25 356 -197 O
ATOM 3715 CB LYS A 476 -27.677 25.532 -45.765 1.00 63.22 C
ANISOU 3715 CB LYS A 476 7893 8172 7955 31 398 -122 C
ATOM 3716 CG LYS A 476 -26.689 26.613 -46.172 1.00 71.38 C
ANISOU 3716 CG LYS A 476 8947 9164 9011 28 472 -100 C
ATOM 3717 CD LYS A 476 -25.286 26.307 -45.676 1.00 66.72 C
ANISOU 3717 CD LYS A 476 8346 8590 8416 -16 507 -136 C
ATOM 3718 CE LYS A 476 -24.325 27.432 -46.026 1.00 75.19 C
ANISOU 3718 CE LYS A 476 9428 9615 9527 -25 580 -109 C
ATOM 3719 NZ LYS A 476 -22.957 27.178 -45.496 1.00 85.10 N
ANISOU 3719 NZ LYS A 476 10661 10886 10789 -71 612 -142 N
ATOM 3720 N TRP A 477 -28.118 22.417 -44.890 1.00 67.19 N
ANISOU 3720 N TRP A 477 8364 8780 8384 -3 264 -185 N
ATOM 3721 CA TRP A 477 -27.867 21.416 -43.858 1.00 65.42 C
ANISOU 3721 CA TRP A 477 8109 8593 8157 -41 245 -227 C
ATOM 3722 C TRP A 477 -26.983 20.290 -44.378 1.00 66.02 C
ANISOU 3722 C TRP A 477 8217 8694 8174 -40 220 -236 C
ATOM 3723 O TRP A 477 -26.057 19.847 -43.688 1.00 68.14 O
ANISOU 3723 O TRP A 477 8470 8983 8436 -70 241 -267 O
ATOM 3724 CB TRP A 477 -29.194 20.864 -43.334 1.00 62.55 C
ANISOU 3724 CB TRP A 477 7706 8244 7816 -42 190 -223 C
ATOM 3725 CG TRP A 477 -29.053 19.685 -42.412 1.00 66.48 C
ANISOU 3725 CG TRP A 477 8174 8780 8307 -75 162 -253 C
ATOM 3726 CD1 TRP A 477 -29.180 18.367 -42.744 1.00 64.81 C
ANISOU 3726 CD1 TRP A 477 7972 8586 8065 -76 96 -250 C
ATOM 3727 CD2 TRP A 477 -28.765 19.718 -41.008 1.00 65.60 C
ANISOU 3727 CD2 TRP A 477 8019 8688 8217 -110 199 -287 C
ATOM 3728 NE1 TRP A 477 -28.987 17.578 -41.636 1.00 63.73 N
ANISOU 3728 NE1 TRP A 477 7799 8479 7936 -110 92 -274 N
ATOM 3729 CE2 TRP A 477 -28.730 18.383 -40.557 1.00 68.77 C
ANISOU 3729 CE2 TRP A 477 8404 9123 8600 -129 155 -296 C
ATOM 3730 CE3 TRP A 477 -28.532 20.746 -40.089 1.00 63.09 C
ANISOU 3730 CE3 TRP A 477 7679 8362 7930 -124 261 -313 C
ATOM 3731 CZ2 TRP A 477 -28.473 18.050 -39.229 1.00 63.55 C
ANISOU 3731 CZ2 TRP A 477 7704 8494 7946 -160 174 -323 C
ATOM 3732 CZ3 TRP A 477 -28.276 20.413 -38.771 1.00 61.70 C
ANISOU 3732 CZ3 TRP A 477 7468 8218 7756 -154 276 -348 C
ATOM 3733 CH2 TRP A 477 -28.249 19.076 -38.354 1.00 59.03 C
ANISOU 3733 CH2 TRP A 477 7113 7920 7395 -171 234 -349 C
ATOM 3734 N TRP A 478 -27.241 19.820 -45.597 1.00 66.15 N
ANISOU 3734 N TRP A 478 8281 8709 8144 -2 174 -210 N
ATOM 3735 CA TRP A 478 -26.473 18.710 -46.140 1.00 60.63 C
ANISOU 3735 CA TRP A 478 7621 8032 7386 8 148 -222 C
ATOM 3736 C TRP A 478 -25.196 19.149 -46.842 1.00 62.81 C
ANISOU 3736 C TRP A 478 7934 8303 7626 26 211 -210 C
ATOM 3737 O TRP A 478 -24.268 18.341 -46.962 1.00 59.84 O
ANISOU 3737 O TRP A 478 7576 7949 7213 28 215 -227 O
ATOM 3738 CB TRP A 478 -27.343 17.884 -47.090 1.00 61.84 C
ANISOU 3738 CB TRP A 478 7813 8185 7499 41 60 -208 C
ATOM 3739 CG TRP A 478 -28.334 17.049 -46.345 1.00 68.20 C
ANISOU 3739 CG TRP A 478 8576 8999 8340 14 -7 -222 C
ATOM 3740 CD1 TRP A 478 -29.689 17.208 -46.316 1.00 67.14 C
ANISOU 3740 CD1 TRP A 478 8412 8855 8243 17 -57 -200 C
ATOM 3741 CD2 TRP A 478 -28.041 15.940 -45.487 1.00 63.50 C
ANISOU 3741 CD2 TRP A 478 7953 8423 7751 -19 -28 -252 C
ATOM 3742 NE1 TRP A 478 -30.259 16.255 -45.506 1.00 55.76 N
ANISOU 3742 NE1 TRP A 478 6926 7427 6834 -15 -105 -212 N
ATOM 3743 CE2 TRP A 478 -29.268 15.465 -44.985 1.00 58.13 C
ANISOU 3743 CE2 TRP A 478 7230 7744 7114 -38 -88 -244 C
ATOM 3744 CE3 TRP A 478 -26.861 15.297 -45.102 1.00 58.31 C
ANISOU 3744 CE3 TRP A 478 7301 7783 7070 -34 -1 -280 C
ATOM 3745 CZ2 TRP A 478 -29.348 14.378 -44.118 1.00 58.72 C
ANISOU 3745 CZ2 TRP A 478 7269 7833 7208 -71 -120 -260 C
ATOM 3746 CZ3 TRP A 478 -26.942 14.220 -44.241 1.00 57.75 C
ANISOU 3746 CZ3 TRP A 478 7198 7728 7015 -64 -36 -299 C
ATOM 3747 CH2 TRP A 478 -28.176 13.771 -43.758 1.00 57.19 C
ANISOU 3747 CH2 TRP A 478 7088 7655 6988 -83 -94 -287 C
ATOM 3748 N GLU A 479 -25.118 20.400 -47.299 1.00 63.77 N
ANISOU 3748 N GLU A 479 8066 8399 7766 42 264 -177 N
ATOM 3749 CA GLU A 479 -23.838 20.919 -47.769 1.00 63.11 C
ANISOU 3749 CA GLU A 479 8002 8310 7667 49 337 -160 C
ATOM 3750 C GLU A 479 -22.833 20.987 -46.627 1.00 70.07 C
ANISOU 3750 C GLU A 479 8833 9201 8591 -3 384 -194 C
ATOM 3751 O GLU A 479 -21.640 20.725 -46.820 1.00 64.36 O
ANISOU 3751 O GLU A 479 8114 8493 7847 -4 422 -194 O
ATOM 3752 CB GLU A 479 -24.021 22.295 -48.410 1.00 60.15 C
ANISOU 3752 CB GLU A 479 7641 7897 7315 72 385 -111 C
ATOM 3753 CG GLU A 479 -24.701 22.265 -49.771 1.00 80.12 C
ANISOU 3753 CG GLU A 479 10231 10424 9785 133 347 -66 C
ATOM 3754 CD GLU A 479 -24.853 23.646 -50.381 1.00 87.31 C
ANISOU 3754 CD GLU A 479 11156 11297 10721 158 398 -10 C
ATOM 3755 OE1 GLU A 479 -24.277 24.608 -49.830 1.00 88.28 O
ANISOU 3755 OE1 GLU A 479 11245 11390 10908 126 468 -5 O
ATOM 3756 OE2 GLU A 479 -25.552 23.769 -51.409 1.00 87.52 O
ANISOU 3756 OE2 GLU A 479 11227 11321 10705 209 365 31 O
ATOM 3757 N MET A 480 -23.304 21.324 -45.423 1.00 66.76 N
ANISOU 3757 N MET A 480 8363 8774 8227 -44 381 -225 N
ATOM 3758 CA MET A 480 -22.432 21.360 -44.254 1.00 63.13 C
ANISOU 3758 CA MET A 480 7858 8327 7802 -93 413 -264 C
ATOM 3759 C MET A 480 -22.140 19.964 -43.718 1.00 65.73 C
ANISOU 3759 C MET A 480 8175 8701 8100 -106 371 -295 C
ATOM 3760 O MET A 480 -21.068 19.738 -43.146 1.00 67.40 O
ANISOU 3760 O MET A 480 8361 8932 8317 -134 396 -316 O
ATOM 3761 CB MET A 480 -23.058 22.228 -43.161 1.00 56.89 C
ANISOU 3761 CB MET A 480 7028 7516 7073 -124 425 -288 C
ATOM 3762 CG MET A 480 -23.237 23.688 -43.552 1.00 58.45 C
ANISOU 3762 CG MET A 480 7234 7659 7314 -115 473 -262 C
ATOM 3763 SD MET A 480 -24.277 24.599 -42.392 1.00 61.82 S
ANISOU 3763 SD MET A 480 7627 8059 7804 -132 478 -293 S
ATOM 3764 CE MET A 480 -23.340 24.419 -40.877 1.00 57.87 C
ANISOU 3764 CE MET A 480 7084 7584 7321 -190 493 -360 C
ATOM 3765 N LYS A 481 -23.073 19.023 -43.883 1.00 60.28 N
ANISOU 3765 N LYS A 481 7498 8024 7382 -88 305 -295 N
ATOM 3766 CA LYS A 481 -22.792 17.639 -43.514 1.00 56.75 C
ANISOU 3766 CA LYS A 481 7046 7609 6906 -96 264 -318 C
ATOM 3767 C LYS A 481 -21.693 17.051 -44.389 1.00 68.09 C
ANISOU 3767 C LYS A 481 8520 9056 8293 -68 278 -310 C
ATOM 3768 O LYS A 481 -20.779 16.387 -43.887 1.00 71.42 O
ANISOU 3768 O LYS A 481 8923 9503 8709 -83 286 -329 O
ATOM 3769 CB LYS A 481 -24.064 16.798 -43.616 1.00 62.36 C
ANISOU 3769 CB LYS A 481 7764 8321 7608 -84 187 -314 C
ATOM 3770 CG LYS A 481 -25.000 16.918 -42.425 1.00 57.83 C
ANISOU 3770 CG LYS A 481 7138 7754 7083 -116 172 -325 C
ATOM 3771 CD LYS A 481 -24.520 16.063 -41.266 1.00 63.05 C
ANISOU 3771 CD LYS A 481 7761 8448 7746 -149 166 -352 C
ATOM 3772 CE LYS A 481 -25.547 16.029 -40.148 1.00 72.53 C
ANISOU 3772 CE LYS A 481 8913 9661 8983 -172 150 -355 C
ATOM 3773 NZ LYS A 481 -25.140 15.103 -39.059 1.00 60.57 N
ANISOU 3773 NZ LYS A 481 7367 8182 7466 -200 140 -373 N
ATOM 3774 N ARG A 482 -21.762 17.289 -45.701 1.00 65.00 N
ANISOU 3774 N ARG A 482 8184 8650 7864 -22 282 -279 N
ATOM 3775 CA ARG A 482 -20.728 16.793 -46.603 1.00 70.89 C
ANISOU 3775 CA ARG A 482 8971 9409 8556 16 306 -268 C
ATOM 3776 C ARG A 482 -19.388 17.465 -46.333 1.00 68.97 C
ANISOU 3776 C ARG A 482 8694 9172 8339 -4 388 -259 C
ATOM 3777 O ARG A 482 -18.349 16.797 -46.297 1.00 73.10 O
ANISOU 3777 O ARG A 482 9212 9719 8844 1 407 -267 O
ATOM 3778 CB ARG A 482 -21.150 17.014 -48.058 1.00 65.00 C
ANISOU 3778 CB ARG A 482 8293 8648 7755 75 296 -234 C
ATOM 3779 CG ARG A 482 -22.400 16.259 -48.485 1.00 61.64 C
ANISOU 3779 CG ARG A 482 7905 8216 7300 97 203 -243 C
ATOM 3780 CD ARG A 482 -23.063 16.941 -49.674 1.00 66.31 C
ANISOU 3780 CD ARG A 482 8548 8790 7856 144 194 -205 C
ATOM 3781 NE ARG A 482 -24.271 16.255 -50.117 1.00 66.07 N
ANISOU 3781 NE ARG A 482 8549 8754 7802 163 95 -213 N
ATOM 3782 CZ ARG A 482 -24.349 15.501 -51.205 1.00 72.27 C
ANISOU 3782 CZ ARG A 482 9406 9542 8509 214 44 -218 C
ATOM 3783 NH1 ARG A 482 -23.303 15.314 -51.993 1.00 71.58 N
ANISOU 3783 NH1 ARG A 482 9373 9470 8356 260 89 -213 N
ATOM 3784 NH2 ARG A 482 -25.507 14.924 -51.513 1.00 67.86 N
ANISOU 3784 NH2 ARG A 482 8868 8973 7941 222 -56 -228 N
ATOM 3785 N GLU A 483 -19.391 18.783 -46.128 1.00 59.34 N
ANISOU 3785 N GLU A 483 7450 7928 7170 -27 436 -243 N
ATOM 3786 CA GLU A 483 -18.138 19.524 -46.042 1.00 69.25 C
ANISOU 3786 CA GLU A 483 8674 9179 8458 -48 511 -227 C
ATOM 3787 C GLU A 483 -17.490 19.380 -44.669 1.00 76.48 C
ANISOU 3787 C GLU A 483 9525 10113 9420 -105 514 -268 C
ATOM 3788 O GLU A 483 -16.305 19.047 -44.567 1.00 77.65 O
ANISOU 3788 O GLU A 483 9650 10285 9570 -112 544 -267 O
ATOM 3789 CB GLU A 483 -18.381 20.998 -46.371 1.00 68.99 C
ANISOU 3789 CB GLU A 483 8641 9103 8468 -52 557 -193 C
ATOM 3790 CG GLU A 483 -17.140 21.867 -46.252 1.00 83.03 C
ANISOU 3790 CG GLU A 483 10381 10867 10298 -82 633 -173 C
ATOM 3791 CD GLU A 483 -17.406 23.317 -46.602 1.00 99.46 C
ANISOU 3791 CD GLU A 483 12466 12895 12430 -86 677 -136 C
ATOM 3792 OE1 GLU A 483 -18.481 23.606 -47.169 1.00 99.10 O
ANISOU 3792 OE1 GLU A 483 12460 12829 12365 -52 655 -115 O
ATOM 3793 OE2 GLU A 483 -16.540 24.168 -46.308 1.00117.44 O
ANISOU 3793 OE2 GLU A 483 14704 15148 14772 -125 731 -125 O
ATOM 3794 N ILE A 484 -18.251 19.626 -43.607 1.00 72.65 N
ANISOU 3794 N ILE A 484 9011 9622 8972 -142 484 -302 N
ATOM 3795 CA ILE A 484 -17.713 19.637 -42.248 1.00 68.06 C
ANISOU 3795 CA ILE A 484 8372 9058 8428 -196 485 -342 C
ATOM 3796 C ILE A 484 -17.654 18.236 -41.653 1.00 65.50 C
ANISOU 3796 C ILE A 484 8038 8778 8071 -197 436 -368 C
ATOM 3797 O ILE A 484 -16.622 17.821 -41.120 1.00 54.43 O
ANISOU 3797 O ILE A 484 6602 7405 6674 -217 446 -381 O
ATOM 3798 CB ILE A 484 -18.551 20.583 -41.362 1.00 64.65 C
ANISOU 3798 CB ILE A 484 7920 8601 8043 -227 482 -368 C
ATOM 3799 CG1 ILE A 484 -18.622 21.981 -41.978 1.00 55.14 C
ANISOU 3799 CG1 ILE A 484 6728 7343 6878 -223 530 -340 C
ATOM 3800 CG2 ILE A 484 -17.985 20.638 -39.947 1.00 60.91 C
ANISOU 3800 CG2 ILE A 484 7396 8149 7599 -278 480 -415 C
ATOM 3801 CD1 ILE A 484 -19.471 22.953 -41.185 1.00 52.53 C
ANISOU 3801 CD1 ILE A 484 6384 6979 6595 -245 530 -367 C
ATOM 3802 N VAL A 485 -18.753 17.485 -41.727 1.00 60.03 N
ANISOU 3802 N VAL A 485 7370 8090 7350 -177 382 -370 N
ATOM 3803 CA VAL A 485 -18.800 16.170 -41.097 1.00 67.13 C
ANISOU 3803 CA VAL A 485 8257 9022 8227 -181 334 -390 C
ATOM 3804 C VAL A 485 -18.303 15.058 -42.013 1.00 68.25 C
ANISOU 3804 C VAL A 485 8437 9174 8321 -139 318 -376 C
ATOM 3805 O VAL A 485 -17.934 13.982 -41.521 1.00 68.88 O
ANISOU 3805 O VAL A 485 8504 9279 8389 -142 292 -390 O
ATOM 3806 CB VAL A 485 -20.227 15.846 -40.615 1.00 59.16 C
ANISOU 3806 CB VAL A 485 7245 8009 7222 -186 282 -397 C
ATOM 3807 CG1 VAL A 485 -20.202 14.747 -39.556 1.00 61.40 C
ANISOU 3807 CG1 VAL A 485 7498 8328 7502 -207 246 -415 C
ATOM 3808 CG2 VAL A 485 -20.904 17.091 -40.072 1.00 54.75 C
ANISOU 3808 CG2 VAL A 485 6666 7432 6705 -207 305 -404 C
ATOM 3809 N GLY A 486 -18.265 15.287 -43.321 1.00 62.65 N
ANISOU 3809 N GLY A 486 7778 8445 7582 -96 336 -350 N
ATOM 3810 CA GLY A 486 -17.910 14.222 -44.243 1.00 57.64 C
ANISOU 3810 CA GLY A 486 7191 7817 6892 -47 318 -343 C
ATOM 3811 C GLY A 486 -18.969 13.145 -44.329 1.00 60.10 C
ANISOU 3811 C GLY A 486 7533 8121 7180 -33 237 -357 C
ATOM 3812 O GLY A 486 -18.636 11.956 -44.415 1.00 62.84 O
ANISOU 3812 O GLY A 486 7899 8477 7500 -13 207 -369 O
ATOM 3813 N VAL A 487 -20.242 13.535 -44.299 1.00 60.34 N
ANISOU 3813 N VAL A 487 7567 8132 7227 -43 200 -353 N
ATOM 3814 CA VAL A 487 -21.368 12.610 -44.309 1.00 63.02 C
ANISOU 3814 CA VAL A 487 7922 8460 7561 -39 119 -361 C
ATOM 3815 C VAL A 487 -22.355 13.073 -45.372 1.00 60.21 C
ANISOU 3815 C VAL A 487 7612 8078 7186 -8 89 -342 C
ATOM 3816 O VAL A 487 -22.688 14.261 -45.440 1.00 63.97 O
ANISOU 3816 O VAL A 487 8077 8546 7685 -13 123 -324 O
ATOM 3817 CB VAL A 487 -22.050 12.531 -42.928 1.00 61.79 C
ANISOU 3817 CB VAL A 487 7705 8316 7458 -89 98 -370 C
ATOM 3818 CG1 VAL A 487 -23.315 11.698 -43.003 1.00 57.53 C
ANISOU 3818 CG1 VAL A 487 7174 7760 6926 -89 17 -367 C
ATOM 3819 CG2 VAL A 487 -21.092 11.959 -41.891 1.00 53.86 C
ANISOU 3819 CG2 VAL A 487 6660 7341 6462 -115 117 -387 C
ATOM 3820 N VAL A 488 -22.818 12.141 -46.200 1.00 62.34 N
ANISOU 3820 N VAL A 488 7936 8335 7417 25 22 -348 N
ATOM 3821 CA VAL A 488 -23.718 12.439 -47.308 1.00 71.14 C
ANISOU 3821 CA VAL A 488 9100 9428 8502 60 -20 -332 C
ATOM 3822 C VAL A 488 -25.065 11.781 -47.041 1.00 64.68 C
ANISOU 3822 C VAL A 488 8266 8593 7715 40 -113 -337 C
ATOM 3823 O VAL A 488 -25.132 10.689 -46.465 1.00 58.22 O
ANISOU 3823 O VAL A 488 7431 7774 6914 18 -156 -356 O
ATOM 3824 CB VAL A 488 -23.119 11.971 -48.651 1.00 63.22 C
ANISOU 3824 CB VAL A 488 8182 8422 7417 124 -25 -336 C
ATOM 3825 CG1 VAL A 488 -22.830 10.478 -48.620 1.00 57.81 C
ANISOU 3825 CG1 VAL A 488 7522 7733 6710 134 -78 -370 C
ATOM 3826 CG2 VAL A 488 -24.038 12.327 -49.810 1.00 59.60 C
ANISOU 3826 CG2 VAL A 488 7778 7946 6919 164 -73 -319 C
ATOM 3827 N GLU A 489 -26.139 12.456 -47.446 1.00 61.60 N
ANISOU 3827 N GLU A 489 7877 8190 7340 46 -142 -314 N
ATOM 3828 CA GLU A 489 -27.466 11.889 -47.273 1.00 60.18 C
ANISOU 3828 CA GLU A 489 7674 7995 7198 27 -232 -311 C
ATOM 3829 C GLU A 489 -27.702 10.789 -48.307 1.00 64.01 C
ANISOU 3829 C GLU A 489 8227 8459 7633 59 -323 -330 C
ATOM 3830 O GLU A 489 -27.287 10.920 -49.463 1.00 68.91 O
ANISOU 3830 O GLU A 489 8923 9078 8183 111 -321 -334 O
ATOM 3831 CB GLU A 489 -28.544 12.971 -47.393 1.00 57.53 C
ANISOU 3831 CB GLU A 489 7310 7651 6896 27 -235 -278 C
ATOM 3832 CG GLU A 489 -28.765 13.538 -48.793 1.00 61.01 C
ANISOU 3832 CG GLU A 489 7817 8081 7283 80 -253 -259 C
ATOM 3833 CD GLU A 489 -27.783 14.637 -49.160 1.00 75.74 C
ANISOU 3833 CD GLU A 489 9707 9954 9116 106 -155 -243 C
ATOM 3834 OE1 GLU A 489 -26.726 14.744 -48.503 1.00 72.00 O
ANISOU 3834 OE1 GLU A 489 9212 9493 8651 86 -82 -256 O
ATOM 3835 OE2 GLU A 489 -28.073 15.400 -50.107 1.00 72.31 O
ANISOU 3835 OE2 GLU A 489 9310 9512 8652 145 -153 -213 O
ATOM 3836 N PRO A 490 -28.337 9.680 -47.917 1.00 65.51 N
ANISOU 3836 N PRO A 490 8398 8633 7860 31 -403 -343 N
ATOM 3837 CA PRO A 490 -28.626 8.622 -48.895 1.00 65.87 C
ANISOU 3837 CA PRO A 490 8513 8649 7865 58 -502 -368 C
ATOM 3838 C PRO A 490 -29.814 8.923 -49.790 1.00 69.73 C
ANISOU 3838 C PRO A 490 9023 9121 8349 75 -583 -353 C
ATOM 3839 O PRO A 490 -29.921 8.322 -50.868 1.00 70.26 O
ANISOU 3839 O PRO A 490 9168 9168 8358 113 -659 -378 O
ATOM 3840 CB PRO A 490 -28.895 7.396 -48.014 1.00 58.79 C
ANISOU 3840 CB PRO A 490 7575 7735 7028 13 -554 -380 C
ATOM 3841 CG PRO A 490 -29.412 7.971 -46.740 1.00 60.53 C
ANISOU 3841 CG PRO A 490 7697 7977 7327 -38 -511 -346 C
ATOM 3842 CD PRO A 490 -28.686 9.277 -46.543 1.00 63.67 C
ANISOU 3842 CD PRO A 490 8084 8406 7703 -26 -402 -336 C
ATOM 3843 N VAL A 491 -30.701 9.826 -49.386 1.00 76.39 N
ANISOU 3843 N VAL A 491 9803 9973 9249 53 -573 -315 N
ATOM 3844 CA VAL A 491 -31.876 10.187 -50.175 1.00 62.08 C
ANISOU 3844 CA VAL A 491 7998 8149 7441 69 -650 -292 C
ATOM 3845 C VAL A 491 -31.937 11.706 -50.276 1.00 70.21 C
ANISOU 3845 C VAL A 491 9010 9197 8468 89 -573 -254 C
ATOM 3846 O VAL A 491 -31.781 12.398 -49.259 1.00 79.50 O
ANISOU 3846 O VAL A 491 10122 10387 9696 61 -490 -237 O
ATOM 3847 CB VAL A 491 -33.161 9.615 -49.553 1.00 59.26 C
ANISOU 3847 CB VAL A 491 7565 7774 7176 19 -734 -275 C
ATOM 3848 CG1 VAL A 491 -34.392 10.175 -50.248 1.00 64.45 C
ANISOU 3848 CG1 VAL A 491 8212 8425 7851 33 -805 -243 C
ATOM 3849 CG2 VAL A 491 -33.154 8.095 -49.619 1.00 63.43 C
ANISOU 3849 CG2 VAL A 491 8119 8271 7710 0 -824 -311 C
ATOM 3850 N PRO A 492 -32.146 12.269 -51.466 1.00 72.98 N
ANISOU 3850 N PRO A 492 9420 9546 8761 140 -596 -240 N
ATOM 3851 CA PRO A 492 -32.265 13.728 -51.576 1.00 76.79 C
ANISOU 3851 CA PRO A 492 9886 10039 9251 160 -525 -196 C
ATOM 3852 C PRO A 492 -33.485 14.238 -50.823 1.00 70.64 C
ANISOU 3852 C PRO A 492 9015 9257 8568 126 -541 -161 C
ATOM 3853 O PRO A 492 -34.570 13.655 -50.889 1.00 71.67 O
ANISOU 3853 O PRO A 492 9116 9377 8738 111 -640 -154 O
ATOM 3854 CB PRO A 492 -32.391 13.962 -53.086 1.00 68.82 C
ANISOU 3854 CB PRO A 492 8965 9030 8156 224 -572 -185 C
ATOM 3855 CG PRO A 492 -32.887 12.662 -53.632 1.00 77.15 C
ANISOU 3855 CG PRO A 492 10059 10069 9184 226 -701 -221 C
ATOM 3856 CD PRO A 492 -32.263 11.604 -52.775 1.00 79.65 C
ANISOU 3856 CD PRO A 492 10358 10380 9527 185 -690 -262 C
ATOM 3857 N HIS A 493 -33.295 15.337 -50.096 1.00 66.22 N
ANISOU 3857 N HIS A 493 8408 8704 8050 117 -442 -139 N
ATOM 3858 CA HIS A 493 -34.330 15.919 -49.250 1.00 70.02 C
ANISOU 3858 CA HIS A 493 8800 9184 8621 92 -433 -108 C
ATOM 3859 C HIS A 493 -34.566 17.364 -49.661 1.00 68.67 C
ANISOU 3859 C HIS A 493 8631 9005 8454 128 -381 -68 C
ATOM 3860 O HIS A 493 -33.637 18.179 -49.639 1.00 54.67 O
ANISOU 3860 O HIS A 493 6884 7231 6659 141 -288 -69 O
ATOM 3861 CB HIS A 493 -33.939 15.840 -47.773 1.00 73.83 C
ANISOU 3861 CB HIS A 493 9219 9679 9156 45 -362 -126 C
ATOM 3862 CG HIS A 493 -34.043 14.463 -47.195 1.00 70.09 C
ANISOU 3862 CG HIS A 493 8720 9209 8702 5 -418 -149 C
ATOM 3863 ND1 HIS A 493 -33.702 14.177 -45.891 1.00 69.37 N
ANISOU 3863 ND1 HIS A 493 8577 9134 8648 -35 -367 -163 N
ATOM 3864 CD2 HIS A 493 -34.454 13.295 -47.742 1.00 73.54 C
ANISOU 3864 CD2 HIS A 493 9179 9634 9128 0 -523 -159 C
ATOM 3865 CE1 HIS A 493 -33.896 12.891 -45.660 1.00 74.25 C
ANISOU 3865 CE1 HIS A 493 9182 9748 9280 -63 -433 -174 C
ATOM 3866 NE2 HIS A 493 -34.352 12.333 -46.767 1.00 61.63 N
ANISOU 3866 NE2 HIS A 493 7629 8130 7658 -44 -530 -174 N
ATOM 3867 N ASP A 494 -35.806 17.679 -50.026 1.00 67.47 N
ANISOU 3867 N ASP A 494 8449 8847 8338 145 -442 -29 N
ATOM 3868 CA ASP A 494 -36.183 19.041 -50.376 1.00 70.96 C
ANISOU 3868 CA ASP A 494 8887 9279 8796 183 -399 16 C
ATOM 3869 C ASP A 494 -36.515 19.817 -49.102 1.00 69.09 C
ANISOU 3869 C ASP A 494 8568 9038 8647 159 -320 26 C
ATOM 3870 O ASP A 494 -36.217 19.384 -47.985 1.00 74.89 O
ANISOU 3870 O ASP A 494 9261 9782 9411 116 -284 -5 O
ATOM 3871 CB ASP A 494 -37.343 19.030 -51.370 1.00 79.03 C
ANISOU 3871 CB ASP A 494 9914 10298 9815 216 -504 55 C
ATOM 3872 CG ASP A 494 -38.462 18.100 -50.948 1.00 83.85 C
ANISOU 3872 CG ASP A 494 10456 10914 10490 181 -601 57 C
ATOM 3873 OD1 ASP A 494 -39.018 18.297 -49.848 1.00 78.65 O
ANISOU 3873 OD1 ASP A 494 9710 10258 9917 152 -565 70 O
ATOM 3874 OD2 ASP A 494 -38.789 17.172 -51.718 1.00 95.63 O
ANISOU 3874 OD2 ASP A 494 11982 12406 11948 184 -713 46 O
ATOM 3875 N GLU A 495 -37.148 20.979 -49.253 1.00 73.36 N
ANISOU 3875 N GLU A 495 9086 9562 9225 191 -291 69 N
ATOM 3876 CA GLU A 495 -37.438 21.849 -48.121 1.00 68.72 C
ANISOU 3876 CA GLU A 495 8432 8966 8714 180 -209 75 C
ATOM 3877 C GLU A 495 -38.728 21.485 -47.397 1.00 70.58 C
ANISOU 3877 C GLU A 495 8577 9214 9026 165 -252 95 C
ATOM 3878 O GLU A 495 -39.188 22.264 -46.555 1.00 64.11 O
ANISOU 3878 O GLU A 495 7702 8388 8270 170 -189 107 O
ATOM 3879 CB GLU A 495 -37.492 23.309 -48.577 1.00 69.86 C
ANISOU 3879 CB GLU A 495 8595 9079 8871 226 -150 113 C
ATOM 3880 CG GLU A 495 -36.174 23.825 -49.132 1.00 76.89 C
ANISOU 3880 CG GLU A 495 9561 9952 9700 237 -86 102 C
ATOM 3881 CD GLU A 495 -35.027 23.690 -48.146 1.00 76.69 C
ANISOU 3881 CD GLU A 495 9533 9930 9674 192 -11 48 C
ATOM 3882 OE1 GLU A 495 -35.256 23.856 -46.929 1.00 73.01 O
ANISOU 3882 OE1 GLU A 495 9009 9464 9265 165 29 25 O
ATOM 3883 OE2 GLU A 495 -33.894 23.412 -48.590 1.00 84.31 O
ANISOU 3883 OE2 GLU A 495 10554 10900 10579 187 9 29 O
ATOM 3884 N THR A 496 -39.328 20.339 -47.706 1.00 73.90 N
ANISOU 3884 N THR A 496 8982 9650 9446 148 -356 100 N
ATOM 3885 CA THR A 496 -40.404 19.804 -46.884 1.00 75.23 C
ANISOU 3885 CA THR A 496 9056 9834 9693 121 -390 119 C
ATOM 3886 C THR A 496 -39.883 18.978 -45.718 1.00 77.70 C
ANISOU 3886 C THR A 496 9342 10165 10015 71 -356 80 C
ATOM 3887 O THR A 496 -40.648 18.685 -44.794 1.00 82.78 O
ANISOU 3887 O THR A 496 9903 10824 10725 49 -352 99 O
ATOM 3888 CB THR A 496 -41.355 18.945 -47.727 1.00 73.60 C
ANISOU 3888 CB THR A 496 8836 9630 9499 120 -527 146 C
ATOM 3889 OG1 THR A 496 -40.668 17.772 -48.178 1.00 78.26 O
ANISOU 3889 OG1 THR A 496 9488 10222 10027 95 -590 104 O
ATOM 3890 CG2 THR A 496 -41.856 19.728 -48.930 1.00 91.82 C
ANISOU 3890 CG2 THR A 496 11175 11926 11788 174 -570 187 C
ATOM 3891 N TYR A 497 -38.608 18.600 -45.741 1.00 70.89 N
ANISOU 3891 N TYR A 497 8545 9304 9087 54 -328 32 N
ATOM 3892 CA TYR A 497 -38.005 17.855 -44.650 1.00 72.95 C
ANISOU 3892 CA TYR A 497 8786 9583 9349 11 -293 -4 C
ATOM 3893 C TYR A 497 -37.556 18.798 -43.536 1.00 80.57 C
ANISOU 3893 C TYR A 497 9727 10554 10331 9 -177 -21 C
ATOM 3894 O TYR A 497 -37.557 20.027 -43.678 1.00 69.48 O
ANISOU 3894 O TYR A 497 8333 9131 8934 40 -120 -12 O
ATOM 3895 CB TYR A 497 -36.814 17.039 -45.150 1.00 70.74 C
ANISOU 3895 CB TYR A 497 8582 9303 8995 -2 -315 -46 C
ATOM 3896 CG TYR A 497 -37.185 15.841 -45.990 1.00 77.83 C
ANISOU 3896 CG TYR A 497 9504 10193 9875 -8 -433 -45 C
ATOM 3897 CD1 TYR A 497 -37.457 15.976 -47.343 1.00 79.76 C
ANISOU 3897 CD1 TYR A 497 9803 10423 10080 29 -501 -32 C
ATOM 3898 CD2 TYR A 497 -37.252 14.572 -45.431 1.00 79.82 C
ANISOU 3898 CD2 TYR A 497 9728 10452 10149 -50 -478 -58 C
ATOM 3899 CE1 TYR A 497 -37.791 14.881 -48.115 1.00 79.45 C
ANISOU 3899 CE1 TYR A 497 9793 10374 10022 24 -617 -41 C
ATOM 3900 CE2 TYR A 497 -37.585 13.472 -46.194 1.00 66.60 C
ANISOU 3900 CE2 TYR A 497 8079 8760 8465 -58 -592 -63 C
ATOM 3901 CZ TYR A 497 -37.853 13.632 -47.536 1.00 69.66 C
ANISOU 3901 CZ TYR A 497 8524 9132 8810 -21 -663 -58 C
ATOM 3902 OH TYR A 497 -38.186 12.539 -48.300 1.00 88.01 O
ANISOU 3902 OH TYR A 497 10881 11437 11122 -28 -784 -72 O
ATOM 3903 N CYS A 498 -37.168 18.195 -42.409 1.00 76.43 N
ANISOU 3903 N CYS A 498 9174 10054 9813 -27 -145 -46 N
ATOM 3904 CA CYS A 498 -36.546 18.938 -41.321 1.00 74.37 C
ANISOU 3904 CA CYS A 498 8904 9802 9552 -32 -44 -77 C
ATOM 3905 C CYS A 498 -35.632 18.011 -40.530 1.00 72.88 C
ANISOU 3905 C CYS A 498 8720 9639 9332 -72 -32 -114 C
ATOM 3906 O CYS A 498 -35.869 17.751 -39.348 1.00 76.13 O
ANISOU 3906 O CYS A 498 9080 10078 9767 -90 -2 -116 O
ATOM 3907 CB CYS A 498 -37.614 19.556 -40.407 1.00 77.14 C
ANISOU 3907 CB CYS A 498 9181 10163 9967 -19 -1 -51 C
ATOM 3908 SG CYS A 498 -36.992 20.898 -39.366 1.00 66.21 S
ANISOU 3908 SG CYS A 498 7804 8772 8581 -6 119 -94 S
ATOM 3909 N ASP A 499 -34.581 17.514 -41.176 1.00 77.97 N
ANISOU 3909 N ASP A 499 9426 10277 9921 -80 -53 -141 N
ATOM 3910 CA ASP A 499 -33.740 16.493 -40.556 1.00 81.51 C
ANISOU 3910 CA ASP A 499 9880 10749 10343 -114 -55 -170 C
ATOM 3911 C ASP A 499 -33.072 16.934 -39.258 1.00 76.17 C
ANISOU 3911 C ASP A 499 9183 10096 9663 -131 27 -202 C
ATOM 3912 O ASP A 499 -32.944 16.088 -38.356 1.00 69.49 O
ANISOU 3912 O ASP A 499 8306 9279 8816 -157 24 -208 O
ATOM 3913 CB ASP A 499 -32.691 15.997 -41.563 1.00 74.40 C
ANISOU 3913 CB ASP A 499 9052 9836 9382 -109 -83 -193 C
ATOM 3914 CG ASP A 499 -33.316 15.414 -42.814 1.00 68.38 C
ANISOU 3914 CG ASP A 499 8319 9052 8610 -90 -175 -171 C
ATOM 3915 OD1 ASP A 499 -34.482 14.971 -42.755 1.00 61.89 O
ANISOU 3915 OD1 ASP A 499 7452 8229 7834 -97 -234 -140 O
ATOM 3916 OD2 ASP A 499 -32.636 15.406 -43.862 1.00 70.26 O
ANISOU 3916 OD2 ASP A 499 8625 9277 8794 -68 -188 -183 O
ATOM 3917 N PRO A 500 -32.618 18.183 -39.085 1.00 75.70 N
ANISOU 3917 N PRO A 500 9138 10024 9600 -118 96 -224 N
ATOM 3918 CA PRO A 500 -32.095 18.566 -37.761 1.00 65.45 C
ANISOU 3918 CA PRO A 500 7819 8749 8300 -136 162 -260 C
ATOM 3919 C PRO A 500 -33.096 18.353 -36.637 1.00 67.43 C
ANISOU 3919 C PRO A 500 8006 9030 8583 -138 174 -242 C
ATOM 3920 O PRO A 500 -32.720 17.855 -35.568 1.00 68.36 O
ANISOU 3920 O PRO A 500 8105 9185 8685 -159 193 -261 O
ATOM 3921 CB PRO A 500 -31.730 20.051 -37.939 1.00 56.54 C
ANISOU 3921 CB PRO A 500 6717 7587 7180 -118 223 -280 C
ATOM 3922 CG PRO A 500 -32.373 20.477 -39.223 1.00 61.59 C
ANISOU 3922 CG PRO A 500 7376 8190 7835 -86 193 -240 C
ATOM 3923 CD PRO A 500 -32.389 19.252 -40.070 1.00 74.69 C
ANISOU 3923 CD PRO A 500 9054 9859 9467 -90 117 -220 C
ATOM 3924 N ALA A 501 -34.369 18.688 -36.858 1.00 68.82 N
ANISOU 3924 N ALA A 501 8148 9196 8806 -113 162 -202 N
ATOM 3925 CA ALA A 501 -35.394 18.474 -35.844 1.00 67.29 C
ANISOU 3925 CA ALA A 501 7886 9034 8648 -109 179 -174 C
ATOM 3926 C ALA A 501 -35.652 16.999 -35.562 1.00 68.83 C
ANISOU 3926 C ALA A 501 8047 9258 8848 -138 125 -144 C
ATOM 3927 O ALA A 501 -36.298 16.684 -34.557 1.00 60.71 O
ANISOU 3927 O ALA A 501 6962 8265 7842 -141 147 -120 O
ATOM 3928 CB ALA A 501 -36.700 19.154 -36.260 1.00 55.39 C
ANISOU 3928 CB ALA A 501 6343 7507 7196 -73 176 -130 C
ATOM 3929 N SER A 502 -35.170 16.089 -36.413 1.00 67.66 N
ANISOU 3929 N SER A 502 7932 9095 8679 -158 57 -144 N
ATOM 3930 CA SER A 502 -35.304 14.665 -36.127 1.00 59.95 C
ANISOU 3930 CA SER A 502 6930 8137 7712 -188 6 -121 C
ATOM 3931 C SER A 502 -34.423 14.218 -34.968 1.00 69.35 C
ANISOU 3931 C SER A 502 8118 9366 8866 -209 47 -147 C
ATOM 3932 O SER A 502 -34.536 13.064 -34.539 1.00 69.77 O
ANISOU 3932 O SER A 502 8144 9435 8928 -233 15 -122 O
ATOM 3933 CB SER A 502 -34.978 13.837 -37.370 1.00 62.53 C
ANISOU 3933 CB SER A 502 7304 8432 8023 -197 -78 -123 C
ATOM 3934 OG SER A 502 -33.619 13.985 -37.742 1.00 69.37 O
ANISOU 3934 OG SER A 502 8236 9290 8829 -195 -59 -171 O
ATOM 3935 N LEU A 503 -33.548 15.086 -34.467 1.00 66.71 N
ANISOU 3935 N LEU A 503 7812 9042 8492 -202 112 -195 N
ATOM 3936 CA LEU A 503 -32.782 14.813 -33.263 1.00 58.49 C
ANISOU 3936 CA LEU A 503 6766 8044 7415 -219 152 -221 C
ATOM 3937 C LEU A 503 -33.507 15.393 -32.055 1.00 74.38 C
ANISOU 3937 C LEU A 503 8731 10091 9438 -202 214 -213 C
ATOM 3938 O LEU A 503 -34.208 16.403 -32.156 1.00 69.03 O
ANISOU 3938 O LEU A 503 8044 9398 8787 -175 246 -210 O
ATOM 3939 CB LEU A 503 -31.371 15.398 -33.368 1.00 61.05 C
ANISOU 3939 CB LEU A 503 7143 8361 7692 -224 181 -281 C
ATOM 3940 CG LEU A 503 -30.428 15.120 -32.193 1.00 55.75 C
ANISOU 3940 CG LEU A 503 6469 7734 6978 -242 211 -313 C
ATOM 3941 CD1 LEU A 503 -30.259 13.624 -31.981 1.00 50.72 C
ANISOU 3941 CD1 LEU A 503 5818 7121 6334 -262 165 -283 C
ATOM 3942 CD2 LEU A 503 -29.081 15.791 -32.399 1.00 59.62 C
ANISOU 3942 CD2 LEU A 503 7004 8212 7436 -250 234 -368 C
ATOM 3943 N PHE A 504 -33.334 14.735 -30.906 1.00 75.86 N
ANISOU 3943 N PHE A 504 8893 10327 9602 -215 232 -206 N
ATOM 3944 CA PHE A 504 -34.061 15.123 -29.700 1.00 66.35 C
ANISOU 3944 CA PHE A 504 7644 9165 8399 -194 293 -192 C
ATOM 3945 C PHE A 504 -33.780 16.572 -29.317 1.00 69.43 C
ANISOU 3945 C PHE A 504 8064 9550 8765 -168 357 -252 C
ATOM 3946 O PHE A 504 -34.707 17.350 -29.069 1.00 71.21 O
ANISOU 3946 O PHE A 504 8265 9774 9017 -134 399 -240 O
ATOM 3947 CB PHE A 504 -33.702 14.178 -28.552 1.00 63.37 C
ANISOU 3947 CB PHE A 504 7248 8845 7986 -210 302 -178 C
ATOM 3948 CG PHE A 504 -34.162 14.657 -27.202 1.00 68.06 C
ANISOU 3948 CG PHE A 504 7814 9492 8555 -182 375 -178 C
ATOM 3949 CD1 PHE A 504 -35.455 14.417 -26.769 1.00 57.96 C
ANISOU 3949 CD1 PHE A 504 6469 8236 7316 -163 398 -110 C
ATOM 3950 CD2 PHE A 504 -33.295 15.339 -26.362 1.00 67.22 C
ANISOU 3950 CD2 PHE A 504 7743 9413 8383 -173 419 -245 C
ATOM 3951 CE1 PHE A 504 -35.877 14.856 -25.528 1.00 53.88 C
ANISOU 3951 CE1 PHE A 504 5930 7773 6768 -128 472 -108 C
ATOM 3952 CE2 PHE A 504 -33.712 15.781 -25.122 1.00 63.12 C
ANISOU 3952 CE2 PHE A 504 7208 8945 7829 -141 484 -251 C
ATOM 3953 CZ PHE A 504 -35.003 15.539 -24.704 1.00 58.23 C
ANISOU 3953 CZ PHE A 504 6529 8353 7244 -115 515 -182 C
ATOM 3954 N HIS A 505 -32.501 16.954 -29.268 1.00 66.13 N
ANISOU 3954 N HIS A 505 7697 9127 8303 -182 364 -315 N
ATOM 3955 CA HIS A 505 -32.136 18.263 -28.734 1.00 70.71 C
ANISOU 3955 CA HIS A 505 8305 9700 8861 -165 421 -378 C
ATOM 3956 C HIS A 505 -32.658 19.405 -29.598 1.00 70.38 C
ANISOU 3956 C HIS A 505 8277 9599 8864 -140 436 -382 C
ATOM 3957 O HIS A 505 -32.914 20.500 -29.083 1.00 60.18 O
ANISOU 3957 O HIS A 505 6993 8298 7574 -112 489 -417 O
ATOM 3958 CB HIS A 505 -30.617 18.364 -28.589 1.00 66.07 C
ANISOU 3958 CB HIS A 505 7761 9114 8228 -194 414 -439 C
ATOM 3959 CG HIS A 505 -30.026 17.322 -27.691 1.00 66.28 C
ANISOU 3959 CG HIS A 505 7775 9200 8207 -214 400 -436 C
ATOM 3960 ND1 HIS A 505 -30.052 15.977 -27.992 1.00 65.71 N
ANISOU 3960 ND1 HIS A 505 7683 9142 8141 -232 353 -384 N
ATOM 3961 CD2 HIS A 505 -29.392 17.428 -26.499 1.00 60.48 C
ANISOU 3961 CD2 HIS A 505 7048 8513 7419 -217 424 -479 C
ATOM 3962 CE1 HIS A 505 -29.460 15.299 -27.025 1.00 67.29 C
ANISOU 3962 CE1 HIS A 505 7876 9395 8295 -244 352 -389 C
ATOM 3963 NE2 HIS A 505 -29.049 16.156 -26.108 1.00 66.66 N
ANISOU 3963 NE2 HIS A 505 7812 9340 8175 -236 393 -446 N
ATOM 3964 N VAL A 506 -32.825 19.176 -30.900 1.00 67.48 N
ANISOU 3964 N VAL A 506 7917 9192 8531 -145 389 -349 N
ATOM 3965 CA VAL A 506 -33.286 20.242 -31.782 1.00 67.76 C
ANISOU 3965 CA VAL A 506 7968 9173 8607 -119 399 -346 C
ATOM 3966 C VAL A 506 -34.794 20.429 -31.666 1.00 67.74 C
ANISOU 3966 C VAL A 506 7914 9174 8651 -83 413 -295 C
ATOM 3967 O VAL A 506 -35.286 21.562 -31.609 1.00 65.29 O
ANISOU 3967 O VAL A 506 7605 8837 8366 -47 458 -306 O
ATOM 3968 CB VAL A 506 -32.856 19.953 -33.231 1.00 62.48 C
ANISOU 3968 CB VAL A 506 7331 8464 7944 -133 344 -329 C
ATOM 3969 CG1 VAL A 506 -33.303 21.075 -34.154 1.00 54.29 C
ANISOU 3969 CG1 VAL A 506 6312 7372 6943 -102 356 -319 C
ATOM 3970 CG2 VAL A 506 -31.348 19.761 -33.307 1.00 56.06 C
ANISOU 3970 CG2 VAL A 506 6560 7651 7088 -164 339 -373 C
ATOM 3971 N SER A 507 -35.552 19.332 -31.624 1.00 67.35 N
ANISOU 3971 N SER A 507 7814 9154 8621 -90 376 -236 N
ATOM 3972 CA SER A 507 -37.002 19.424 -31.508 1.00 68.50 C
ANISOU 3972 CA SER A 507 7898 9308 8820 -59 387 -178 C
ATOM 3973 C SER A 507 -37.477 19.611 -30.073 1.00 71.92 C
ANISOU 3973 C SER A 507 8293 9791 9241 -34 458 -179 C
ATOM 3974 O SER A 507 -38.679 19.802 -29.859 1.00 72.81 O
ANISOU 3974 O SER A 507 8349 9914 9400 0 483 -130 O
ATOM 3975 CB SER A 507 -37.661 18.180 -32.109 1.00 64.40 C
ANISOU 3975 CB SER A 507 7336 8795 8339 -81 311 -110 C
ATOM 3976 OG SER A 507 -37.180 16.996 -31.498 1.00 66.35 O
ANISOU 3976 OG SER A 507 7574 9079 8557 -116 292 -105 O
ATOM 3977 N ASN A 508 -36.576 19.560 -29.091 1.00 66.92 N
ANISOU 3977 N ASN A 508 7688 9191 8546 -46 491 -231 N
ATOM 3978 CA ASN A 508 -36.933 19.785 -27.696 1.00 66.73 C
ANISOU 3978 CA ASN A 508 7642 9220 8493 -16 561 -240 C
ATOM 3979 C ASN A 508 -36.263 21.026 -27.118 1.00 61.92 C
ANISOU 3979 C ASN A 508 7089 8596 7842 6 617 -328 C
ATOM 3980 O ASN A 508 -36.325 21.241 -25.901 1.00 63.29 O
ANISOU 3980 O ASN A 508 7262 8815 7972 31 672 -354 O
ATOM 3981 CB ASN A 508 -36.593 18.553 -26.851 1.00 63.69 C
ANISOU 3981 CB ASN A 508 7237 8897 8066 -43 550 -219 C
ATOM 3982 CG ASN A 508 -37.529 17.388 -27.121 1.00 67.97 C
ANISOU 3982 CG ASN A 508 7710 9455 8662 -57 510 -125 C
ATOM 3983 OD1 ASN A 508 -38.482 17.158 -26.377 1.00 65.73 O
ANISOU 3983 OD1 ASN A 508 7366 9213 8396 -32 550 -70 O
ATOM 3984 ND2 ASN A 508 -37.267 16.655 -28.197 1.00 67.57 N
ANISOU 3984 ND2 ASN A 508 7667 9368 8638 -95 431 -105 N
ATOM 3985 N ASP A 509 -35.616 21.838 -27.958 1.00 56.55 N
ANISOU 3985 N ASP A 509 6458 7853 7174 -4 602 -372 N
ATOM 3986 CA ASP A 509 -35.104 23.159 -27.592 1.00 57.65 C
ANISOU 3986 CA ASP A 509 6648 7958 7297 15 649 -451 C
ATOM 3987 C ASP A 509 -34.039 23.054 -26.495 1.00 66.86 C
ANISOU 3987 C ASP A 509 7849 9165 8390 -6 662 -520 C
ATOM 3988 O ASP A 509 -34.213 23.495 -25.356 1.00 73.76 O
ANISOU 3988 O ASP A 509 8730 10070 9226 26 714 -559 O
ATOM 3989 CB ASP A 509 -36.257 24.083 -27.178 1.00 54.03 C
ANISOU 3989 CB ASP A 509 6169 7490 6870 79 714 -445 C
ATOM 3990 CG ASP A 509 -35.812 25.516 -26.965 1.00 62.55 C
ANISOU 3990 CG ASP A 509 7305 8514 7946 101 757 -526 C
ATOM 3991 OD1 ASP A 509 -35.091 26.054 -27.830 1.00 66.79 O
ANISOU 3991 OD1 ASP A 509 7883 8989 8506 76 731 -552 O
ATOM 3992 OD2 ASP A 509 -36.198 26.108 -25.936 1.00 68.23 O
ANISOU 3992 OD2 ASP A 509 8030 9251 8643 146 818 -564 O
ATOM 3993 N TYR A 510 -32.915 22.454 -26.883 1.00 62.93 N
ANISOU 3993 N TYR A 510 7372 8667 7870 -57 612 -534 N
ATOM 3994 CA TYR A 510 -31.740 22.338 -26.032 1.00 64.84 C
ANISOU 3994 CA TYR A 510 7645 8941 8049 -85 609 -597 C
ATOM 3995 C TYR A 510 -30.508 22.744 -26.824 1.00 66.30 C
ANISOU 3995 C TYR A 510 7871 9074 8246 -125 578 -638 C
ATOM 3996 O TYR A 510 -30.337 22.329 -27.974 1.00 71.99 O
ANISOU 3996 O TYR A 510 8589 9766 8998 -145 540 -598 O
ATOM 3997 CB TYR A 510 -31.560 20.908 -25.496 1.00 74.23 C
ANISOU 3997 CB TYR A 510 8805 10203 9197 -106 580 -557 C
ATOM 3998 CG TYR A 510 -32.500 20.534 -24.371 1.00 66.17 C
ANISOU 3998 CG TYR A 510 7748 9248 8148 -70 621 -525 C
ATOM 3999 CD1 TYR A 510 -32.332 21.059 -23.096 1.00 65.56 C
ANISOU 3999 CD1 TYR A 510 7692 9210 8007 -44 667 -582 C
ATOM 4000 CD2 TYR A 510 -33.544 19.642 -24.579 1.00 65.91 C
ANISOU 4000 CD2 TYR A 510 7657 9236 8149 -60 614 -435 C
ATOM 4001 CE1 TYR A 510 -33.185 20.717 -22.064 1.00 68.39 C
ANISOU 4001 CE1 TYR A 510 8019 9634 8332 -3 713 -548 C
ATOM 4002 CE2 TYR A 510 -34.401 19.293 -23.553 1.00 73.63 C
ANISOU 4002 CE2 TYR A 510 8594 10276 9105 -26 659 -395 C
ATOM 4003 CZ TYR A 510 -34.218 19.833 -22.298 1.00 75.11 C
ANISOU 4003 CZ TYR A 510 8807 10508 9224 5 713 -449 C
ATOM 4004 OH TYR A 510 -35.071 19.487 -21.275 1.00 78.21 O
ANISOU 4004 OH TYR A 510 9160 10968 9588 46 766 -404 O
ATOM 4005 N SER A 511 -29.655 23.560 -26.208 1.00 72.08 N
ANISOU 4005 N SER A 511 8641 9794 8953 -136 594 -718 N
ATOM 4006 CA SER A 511 -28.388 23.919 -26.826 1.00 60.88 C
ANISOU 4006 CA SER A 511 7251 8331 7548 -179 567 -754 C
ATOM 4007 C SER A 511 -27.497 22.688 -26.936 1.00 64.31 C
ANISOU 4007 C SER A 511 7672 8810 7951 -219 519 -732 C
ATOM 4008 O SER A 511 -27.522 21.797 -26.083 1.00 67.23 O
ANISOU 4008 O SER A 511 8023 9249 8272 -219 510 -722 O
ATOM 4009 CB SER A 511 -27.683 25.010 -26.021 1.00 59.03 C
ANISOU 4009 CB SER A 511 7055 8075 7300 -187 587 -847 C
ATOM 4010 OG SER A 511 -27.146 24.488 -24.819 1.00 66.73 O
ANISOU 4010 OG SER A 511 8029 9120 8206 -199 575 -885 O
ATOM 4011 N PHE A 512 -26.700 22.642 -28.006 1.00 61.10 N
ANISOU 4011 N PHE A 512 7277 8365 7572 -248 493 -721 N
ATOM 4012 CA PHE A 512 -25.928 21.451 -28.323 1.00 56.18 C
ANISOU 4012 CA PHE A 512 6642 7776 6928 -277 450 -692 C
ATOM 4013 C PHE A 512 -24.423 21.635 -28.198 1.00 58.18 C
ANISOU 4013 C PHE A 512 6907 8027 7170 -317 436 -738 C
ATOM 4014 O PHE A 512 -23.711 20.638 -28.046 1.00 63.65 O
ANISOU 4014 O PHE A 512 7587 8764 7834 -337 405 -725 O
ATOM 4015 CB PHE A 512 -26.259 20.974 -29.745 1.00 57.86 C
ANISOU 4015 CB PHE A 512 6853 7956 7174 -271 428 -629 C
ATOM 4016 CG PHE A 512 -26.102 19.494 -29.940 1.00 52.54 C
ANISOU 4016 CG PHE A 512 6161 7323 6477 -282 385 -585 C
ATOM 4017 CD1 PHE A 512 -26.934 18.603 -29.281 1.00 50.08 C
ANISOU 4017 CD1 PHE A 512 5821 7059 6149 -270 376 -550 C
ATOM 4018 CD2 PHE A 512 -25.134 18.993 -30.793 1.00 49.74 C
ANISOU 4018 CD2 PHE A 512 5820 6957 6122 -301 358 -574 C
ATOM 4019 CE1 PHE A 512 -26.796 17.241 -29.461 1.00 55.45 C
ANISOU 4019 CE1 PHE A 512 6486 7766 6816 -280 335 -509 C
ATOM 4020 CE2 PHE A 512 -24.990 17.632 -30.977 1.00 54.05 C
ANISOU 4020 CE2 PHE A 512 6355 7533 6649 -306 319 -538 C
ATOM 4021 CZ PHE A 512 -25.823 16.754 -30.311 1.00 57.61 C
ANISOU 4021 CZ PHE A 512 6779 8024 7088 -298 304 -506 C
ATOM 4022 N ILE A 513 -23.922 22.873 -28.243 1.00 51.30 N
ANISOU 4022 N ILE A 513 6058 7105 6328 -330 456 -789 N
ATOM 4023 CA ILE A 513 -22.484 23.108 -28.162 1.00 57.40 C
ANISOU 4023 CA ILE A 513 6835 7872 7105 -373 439 -829 C
ATOM 4024 C ILE A 513 -21.900 22.703 -26.818 1.00 68.57 C
ANISOU 4024 C ILE A 513 8238 9352 8462 -390 418 -875 C
ATOM 4025 O ILE A 513 -20.672 22.638 -26.679 1.00 65.87 O
ANISOU 4025 O ILE A 513 7888 9020 8119 -427 393 -900 O
ATOM 4026 CB ILE A 513 -22.162 24.590 -28.453 1.00 56.63 C
ANISOU 4026 CB ILE A 513 6760 7695 7062 -386 465 -873 C
ATOM 4027 CG1 ILE A 513 -20.718 24.743 -28.942 1.00 56.09 C
ANISOU 4027 CG1 ILE A 513 6684 7605 7023 -433 449 -881 C
ATOM 4028 CG2 ILE A 513 -22.401 25.445 -27.217 1.00 55.56 C
ANISOU 4028 CG2 ILE A 513 6642 7558 6911 -380 479 -949 C
ATOM 4029 CD1 ILE A 513 -20.424 23.994 -30.223 1.00 61.82 C
ANISOU 4029 CD1 ILE A 513 7401 8329 7760 -431 443 -810 C
ATOM 4030 N ARG A 514 -22.748 22.420 -25.823 1.00 70.45 N
ANISOU 4030 N ARG A 514 8475 9639 8654 -360 428 -882 N
ATOM 4031 CA ARG A 514 -22.249 21.998 -24.519 1.00 62.04 C
ANISOU 4031 CA ARG A 514 7404 8644 7523 -369 407 -919 C
ATOM 4032 C ARG A 514 -21.457 20.700 -24.615 1.00 62.93 C
ANISOU 4032 C ARG A 514 7491 8809 7612 -390 367 -878 C
ATOM 4033 O ARG A 514 -20.531 20.481 -23.828 1.00 62.97 O
ANISOU 4033 O ARG A 514 7488 8858 7579 -412 339 -912 O
ATOM 4034 CB ARG A 514 -23.412 21.843 -23.538 1.00 63.33 C
ANISOU 4034 CB ARG A 514 7570 8855 7638 -324 434 -916 C
ATOM 4035 CG ARG A 514 -24.250 20.590 -23.748 1.00 58.36 C
ANISOU 4035 CG ARG A 514 6909 8267 6997 -302 433 -831 C
ATOM 4036 CD ARG A 514 -25.728 20.867 -23.552 1.00 63.28 C
ANISOU 4036 CD ARG A 514 7529 8889 7627 -255 478 -806 C
ATOM 4037 NE ARG A 514 -26.032 21.346 -22.210 1.00 81.43 N
ANISOU 4037 NE ARG A 514 9843 11230 9867 -226 508 -856 N
ATOM 4038 CZ ARG A 514 -27.210 21.831 -21.841 1.00 93.34 C
ANISOU 4038 CZ ARG A 514 11352 12738 11374 -178 558 -852 C
ATOM 4039 NH1 ARG A 514 -28.215 21.930 -22.696 1.00 73.71 N
ANISOU 4039 NH1 ARG A 514 8847 10211 8948 -157 578 -798 N
ATOM 4040 NH2 ARG A 514 -27.383 22.230 -20.584 1.00 95.51 N
ANISOU 4040 NH2 ARG A 514 11648 13058 11585 -147 586 -903 N
ATOM 4041 N TYR A 515 -21.796 19.836 -25.574 1.00 62.12 N
ANISOU 4041 N TYR A 515 7373 8699 7531 -382 361 -807 N
ATOM 4042 CA TYR A 515 -21.084 18.576 -25.737 1.00 56.47 C
ANISOU 4042 CA TYR A 515 6636 8023 6798 -396 325 -768 C
ATOM 4043 C TYR A 515 -19.734 18.756 -26.413 1.00 58.95 C
ANISOU 4043 C TYR A 515 6946 8310 7141 -430 308 -781 C
ATOM 4044 O TYR A 515 -18.861 17.894 -26.265 1.00 53.63 O
ANISOU 4044 O TYR A 515 6253 7676 6448 -443 279 -767 O
ATOM 4045 CB TYR A 515 -21.939 17.588 -26.531 1.00 50.25 C
ANISOU 4045 CB TYR A 515 5839 7229 6024 -374 320 -693 C
ATOM 4046 CG TYR A 515 -23.302 17.362 -25.922 1.00 61.05 C
ANISOU 4046 CG TYR A 515 7199 8624 7376 -344 338 -667 C
ATOM 4047 CD1 TYR A 515 -23.467 16.514 -24.835 1.00 57.59 C
ANISOU 4047 CD1 TYR A 515 6740 8253 6887 -336 331 -648 C
ATOM 4048 CD2 TYR A 515 -24.424 18.005 -26.428 1.00 62.37 C
ANISOU 4048 CD2 TYR A 515 7371 8747 7578 -320 366 -653 C
ATOM 4049 CE1 TYR A 515 -24.711 16.310 -24.271 1.00 63.22 C
ANISOU 4049 CE1 TYR A 515 7439 8992 7589 -307 355 -615 C
ATOM 4050 CE2 TYR A 515 -25.673 17.806 -25.871 1.00 65.14 C
ANISOU 4050 CE2 TYR A 515 7705 9124 7920 -291 387 -623 C
ATOM 4051 CZ TYR A 515 -25.810 16.958 -24.793 1.00 58.61 C
ANISOU 4051 CZ TYR A 515 6857 8366 7046 -285 384 -602 C
ATOM 4052 OH TYR A 515 -27.051 16.758 -24.238 1.00 56.00 O
ANISOU 4052 OH TYR A 515 6503 8064 6711 -254 412 -563 O
ATOM 4053 N TYR A 516 -19.545 19.853 -27.148 1.00 63.10 N
ANISOU 4053 N TYR A 516 7487 8770 7718 -441 330 -803 N
ATOM 4054 CA TYR A 516 -18.238 20.153 -27.717 1.00 58.90 C
ANISOU 4054 CA TYR A 516 6946 8214 7221 -474 322 -813 C
ATOM 4055 C TYR A 516 -17.298 20.712 -26.656 1.00 57.17 C
ANISOU 4055 C TYR A 516 6716 8016 6991 -508 302 -880 C
ATOM 4056 O TYR A 516 -16.157 20.258 -26.525 1.00 60.16 O
ANISOU 4056 O TYR A 516 7067 8424 7367 -534 274 -880 O
ATOM 4057 CB TYR A 516 -18.384 21.138 -28.879 1.00 53.54 C
ANISOU 4057 CB TYR A 516 6286 7455 6602 -473 354 -804 C
ATOM 4058 CG TYR A 516 -17.081 21.456 -29.581 1.00 61.06 C
ANISOU 4058 CG TYR A 516 7224 8379 7598 -505 356 -800 C
ATOM 4059 CD1 TYR A 516 -16.296 22.531 -29.182 1.00 58.56 C
ANISOU 4059 CD1 TYR A 516 6900 8032 7319 -544 358 -852 C
ATOM 4060 CD2 TYR A 516 -16.637 20.680 -30.644 1.00 55.98 C
ANISOU 4060 CD2 TYR A 516 6573 7737 6959 -495 356 -744 C
ATOM 4061 CE1 TYR A 516 -15.104 22.823 -29.820 1.00 64.34 C
ANISOU 4061 CE1 TYR A 516 7608 8738 8099 -575 363 -839 C
ATOM 4062 CE2 TYR A 516 -15.448 20.964 -31.288 1.00 60.55 C
ANISOU 4062 CE2 TYR A 516 7134 8295 7577 -518 367 -733 C
ATOM 4063 CZ TYR A 516 -14.686 22.036 -30.873 1.00 65.81 C
ANISOU 4063 CZ TYR A 516 7784 8933 8288 -560 372 -776 C
ATOM 4064 OH TYR A 516 -13.501 22.322 -31.512 1.00 64.98 O
ANISOU 4064 OH TYR A 516 7652 8807 8232 -586 386 -756 O
ATOM 4065 N THR A 517 -17.767 21.698 -25.887 1.00 58.30 N
ANISOU 4065 N THR A 517 6881 8143 7129 -508 314 -938 N
ATOM 4066 CA THR A 517 -16.924 22.303 -24.860 1.00 65.33 C
ANISOU 4066 CA THR A 517 7768 9047 8007 -541 287 -1012 C
ATOM 4067 C THR A 517 -16.623 21.316 -23.739 1.00 65.42 C
ANISOU 4067 C THR A 517 7763 9151 7943 -537 249 -1017 C
ATOM 4068 O THR A 517 -15.501 21.282 -23.222 1.00 56.72 O
ANISOU 4068 O THR A 517 6639 8078 6833 -570 210 -1049 O
ATOM 4069 CB THR A 517 -17.595 23.559 -24.302 1.00 65.18 C
ANISOU 4069 CB THR A 517 7786 8986 7994 -532 309 -1079 C
ATOM 4070 OG1 THR A 517 -18.891 23.224 -23.790 1.00 72.24 O
ANISOU 4070 OG1 THR A 517 8697 9914 8836 -482 333 -1066 O
ATOM 4071 CG2 THR A 517 -17.742 24.614 -25.387 1.00 56.39 C
ANISOU 4071 CG2 THR A 517 6686 7775 6963 -539 344 -1073 C
ATOM 4072 N ARG A 518 -17.613 20.506 -23.353 1.00 66.85 N
ANISOU 4072 N ARG A 518 7950 9380 8071 -497 260 -981 N
ATOM 4073 CA ARG A 518 -17.403 19.520 -22.297 1.00 61.67 C
ANISOU 4073 CA ARG A 518 7279 8812 7341 -488 229 -973 C
ATOM 4074 C ARG A 518 -16.329 18.513 -22.684 1.00 68.46 C
ANISOU 4074 C ARG A 518 8102 9700 8210 -508 195 -930 C
ATOM 4075 O ARG A 518 -15.527 18.093 -21.842 1.00 69.25 O
ANISOU 4075 O ARG A 518 8184 9860 8269 -521 155 -946 O
ATOM 4076 CB ARG A 518 -18.714 18.801 -21.988 1.00 67.47 C
ANISOU 4076 CB ARG A 518 8019 9582 8033 -442 255 -924 C
ATOM 4077 CG ARG A 518 -18.579 17.645 -21.017 1.00 79.55 C
ANISOU 4077 CG ARG A 518 9532 11201 9493 -430 229 -895 C
ATOM 4078 CD ARG A 518 -19.395 16.449 -21.472 1.00 84.79 C
ANISOU 4078 CD ARG A 518 10179 11877 10160 -404 241 -806 C
ATOM 4079 NE ARG A 518 -18.707 15.666 -22.491 1.00 74.86 N
ANISOU 4079 NE ARG A 518 8902 10597 8946 -421 217 -761 N
ATOM 4080 CZ ARG A 518 -19.218 14.591 -23.076 1.00 77.72 C
ANISOU 4080 CZ ARG A 518 9253 10955 9324 -406 216 -690 C
ATOM 4081 NH1 ARG A 518 -20.431 14.154 -22.780 1.00 84.86 N
ANISOU 4081 NH1 ARG A 518 10155 11874 10213 -379 235 -648 N
ATOM 4082 NH2 ARG A 518 -18.494 13.940 -23.982 1.00 81.15 N
ANISOU 4082 NH2 ARG A 518 9676 11367 9790 -416 195 -660 N
ATOM 4083 N THR A 519 -16.302 18.110 -23.956 1.00 71.18 N
ANISOU 4083 N THR A 519 8437 10004 8604 -506 208 -874 N
ATOM 4084 CA THR A 519 -15.313 17.136 -24.403 1.00 66.73 C
ANISOU 4084 CA THR A 519 7842 9462 8050 -516 183 -832 C
ATOM 4085 C THR A 519 -13.899 17.688 -24.279 1.00 69.92 C
ANISOU 4085 C THR A 519 8219 9865 8482 -558 158 -872 C
ATOM 4086 O THR A 519 -12.989 16.990 -23.817 1.00 72.96 O
ANISOU 4086 O THR A 519 8572 10303 8847 -567 121 -862 O
ATOM 4087 CB THR A 519 -15.604 16.718 -25.843 1.00 56.19 C
ANISOU 4087 CB THR A 519 6513 8079 6759 -500 206 -774 C
ATOM 4088 OG1 THR A 519 -16.871 16.050 -25.897 1.00 52.02 O
ANISOU 4088 OG1 THR A 519 6001 7557 6208 -466 216 -734 O
ATOM 4089 CG2 THR A 519 -14.522 15.786 -26.357 1.00 62.15 C
ANISOU 4089 CG2 THR A 519 7239 8851 7524 -503 186 -736 C
ATOM 4090 N LEU A 520 -13.694 18.944 -24.676 1.00 62.37 N
ANISOU 4090 N LEU A 520 7272 8847 7579 -584 175 -912 N
ATOM 4091 CA LEU A 520 -12.373 19.543 -24.526 1.00 68.70 C
ANISOU 4091 CA LEU A 520 8042 9642 8420 -630 148 -950 C
ATOM 4092 C LEU A 520 -12.056 19.837 -23.065 1.00 71.86 C
ANISOU 4092 C LEU A 520 8441 10092 8772 -649 102 -1018 C
ATOM 4093 O LEU A 520 -10.886 19.793 -22.668 1.00 76.57 O
ANISOU 4093 O LEU A 520 8998 10717 9378 -682 58 -1036 O
ATOM 4094 CB LEU A 520 -12.269 20.814 -25.372 1.00 73.07 C
ANISOU 4094 CB LEU A 520 8604 10106 9052 -655 181 -968 C
ATOM 4095 CG LEU A 520 -11.869 20.643 -26.844 1.00 68.09 C
ANISOU 4095 CG LEU A 520 7958 9434 8479 -652 215 -903 C
ATOM 4096 CD1 LEU A 520 -12.915 19.872 -27.638 1.00 61.16 C
ANISOU 4096 CD1 LEU A 520 7109 8552 7576 -602 245 -845 C
ATOM 4097 CD2 LEU A 520 -11.599 21.991 -27.492 1.00 62.70 C
ANISOU 4097 CD2 LEU A 520 7278 8669 7877 -683 244 -921 C
ATOM 4098 N TYR A 521 -13.077 20.123 -22.251 1.00 73.00 N
ANISOU 4098 N TYR A 521 8626 10250 8861 -624 110 -1055 N
ATOM 4099 CA TYR A 521 -12.848 20.380 -20.832 1.00 64.78 C
ANISOU 4099 CA TYR A 521 7594 9262 7756 -632 66 -1124 C
ATOM 4100 C TYR A 521 -12.349 19.134 -20.111 1.00 73.00 C
ANISOU 4100 C TYR A 521 8607 10397 8733 -621 25 -1090 C
ATOM 4101 O TYR A 521 -11.422 19.213 -19.297 1.00 72.16 O
ANISOU 4101 O TYR A 521 8480 10334 8602 -647 -31 -1132 O
ATOM 4102 CB TYR A 521 -14.132 20.878 -20.164 1.00 66.51 C
ANISOU 4102 CB TYR A 521 7867 9480 7924 -596 96 -1162 C
ATOM 4103 CG TYR A 521 -14.565 22.278 -20.541 1.00 70.04 C
ANISOU 4103 CG TYR A 521 8347 9838 8426 -605 128 -1216 C
ATOM 4104 CD1 TYR A 521 -13.676 23.176 -21.118 1.00 65.39 C
ANISOU 4104 CD1 TYR A 521 7744 9179 7922 -655 116 -1246 C
ATOM 4105 CD2 TYR A 521 -15.868 22.700 -20.311 1.00 66.07 C
ANISOU 4105 CD2 TYR A 521 7888 9319 7897 -562 173 -1230 C
ATOM 4106 CE1 TYR A 521 -14.080 24.457 -21.459 1.00 60.80 C
ANISOU 4106 CE1 TYR A 521 7194 8509 7397 -663 145 -1290 C
ATOM 4107 CE2 TYR A 521 -16.280 23.972 -20.647 1.00 61.22 C
ANISOU 4107 CE2 TYR A 521 7305 8619 7336 -565 203 -1277 C
ATOM 4108 CZ TYR A 521 -15.383 24.848 -21.221 1.00 64.25 C
ANISOU 4108 CZ TYR A 521 7679 8930 7804 -616 188 -1307 C
ATOM 4109 OH TYR A 521 -15.795 26.117 -21.556 1.00 64.01 O
ANISOU 4109 OH TYR A 521 7681 8807 7832 -619 218 -1349 O
ATOM 4110 N GLN A 522 -12.955 17.976 -20.391 1.00 73.65 N
ANISOU 4110 N GLN A 522 8686 10510 8788 -583 47 -1014 N
ATOM 4111 CA GLN A 522 -12.660 16.783 -19.605 1.00 72.78 C
ANISOU 4111 CA GLN A 522 8555 10487 8612 -565 12 -978 C
ATOM 4112 C GLN A 522 -11.221 16.319 -19.792 1.00 68.77 C
ANISOU 4112 C GLN A 522 7995 10001 8136 -594 -32 -960 C
ATOM 4113 O GLN A 522 -10.611 15.810 -18.846 1.00 71.41 O
ANISOU 4113 O GLN A 522 8309 10407 8417 -594 -81 -964 O
ATOM 4114 CB GLN A 522 -13.642 15.661 -19.956 1.00 67.83 C
ANISOU 4114 CB GLN A 522 7933 9871 7966 -522 45 -896 C
ATOM 4115 CG GLN A 522 -13.487 15.086 -21.353 1.00 67.21 C
ANISOU 4115 CG GLN A 522 7838 9744 7956 -521 64 -835 C
ATOM 4116 CD GLN A 522 -14.594 14.114 -21.712 1.00 77.29 C
ANISOU 4116 CD GLN A 522 9127 11019 9222 -484 90 -766 C
ATOM 4117 OE1 GLN A 522 -15.778 14.425 -21.574 1.00 76.31 O
ANISOU 4117 OE1 GLN A 522 9029 10882 9084 -464 121 -768 O
ATOM 4118 NE2 GLN A 522 -14.214 12.927 -22.172 1.00 69.88 N
ANISOU 4118 NE2 GLN A 522 8166 10090 8294 -472 76 -705 N
ATOM 4119 N PHE A 523 -10.655 16.494 -20.987 1.00 67.33 N
ANISOU 4119 N PHE A 523 7788 9760 8036 -614 -15 -937 N
ATOM 4120 CA PHE A 523 -9.267 16.100 -21.189 1.00 71.57 C
ANISOU 4120 CA PHE A 523 8267 10317 8608 -638 -50 -917 C
ATOM 4121 C PHE A 523 -8.302 17.159 -20.675 1.00 69.57 C
ANISOU 4121 C PHE A 523 7990 10059 8384 -690 -94 -988 C
ATOM 4122 O PHE A 523 -7.171 16.828 -20.302 1.00 71.44 O
ANISOU 4122 O PHE A 523 8176 10341 8627 -710 -143 -984 O
ATOM 4123 CB PHE A 523 -9.015 15.794 -22.664 1.00 63.82 C
ANISOU 4123 CB PHE A 523 7268 9282 7698 -632 -9 -858 C
ATOM 4124 CG PHE A 523 -9.765 14.591 -23.158 1.00 60.49 C
ANISOU 4124 CG PHE A 523 6865 8866 7250 -584 16 -790 C
ATOM 4125 CD1 PHE A 523 -9.330 13.313 -22.847 1.00 52.33 C
ANISOU 4125 CD1 PHE A 523 5806 7889 6188 -561 -10 -742 C
ATOM 4126 CD2 PHE A 523 -10.913 14.735 -23.917 1.00 70.06 C
ANISOU 4126 CD2 PHE A 523 8121 10027 8474 -562 62 -774 C
ATOM 4127 CE1 PHE A 523 -10.024 12.204 -23.291 1.00 57.52 C
ANISOU 4127 CE1 PHE A 523 6482 8543 6829 -520 8 -682 C
ATOM 4128 CE2 PHE A 523 -11.611 13.629 -24.365 1.00 66.49 C
ANISOU 4128 CE2 PHE A 523 7684 9575 8004 -523 76 -715 C
ATOM 4129 CZ PHE A 523 -11.164 12.362 -24.052 1.00 67.31 C
ANISOU 4129 CZ PHE A 523 7764 9728 8082 -504 48 -670 C
ATOM 4130 N GLN A 524 -8.724 18.424 -20.641 1.00 64.76 N
ANISOU 4130 N GLN A 524 7415 9394 7797 -713 -80 -1053 N
ATOM 4131 CA GLN A 524 -7.968 19.427 -19.901 1.00 75.91 C
ANISOU 4131 CA GLN A 524 8816 10802 9225 -762 -133 -1134 C
ATOM 4132 C GLN A 524 -7.934 19.083 -18.417 1.00 73.47 C
ANISOU 4132 C GLN A 524 8520 10582 8816 -750 -193 -1176 C
ATOM 4133 O GLN A 524 -6.878 19.147 -17.775 1.00 66.37 O
ANISOU 4133 O GLN A 524 7581 9722 7914 -783 -262 -1207 O
ATOM 4134 CB GLN A 524 -8.573 20.815 -20.117 1.00 66.49 C
ANISOU 4134 CB GLN A 524 7667 9524 8072 -780 -104 -1197 C
ATOM 4135 CG GLN A 524 -8.370 21.388 -21.506 1.00 64.97 C
ANISOU 4135 CG GLN A 524 7458 9243 7986 -802 -55 -1164 C
ATOM 4136 CD GLN A 524 -8.928 22.791 -21.636 1.00 69.52 C
ANISOU 4136 CD GLN A 524 8078 9732 8606 -821 -30 -1225 C
ATOM 4137 OE1 GLN A 524 -10.030 22.989 -22.148 1.00 78.75 O
ANISOU 4137 OE1 GLN A 524 9291 10860 9771 -786 26 -1209 O
ATOM 4138 NE2 GLN A 524 -8.167 23.775 -21.170 1.00 69.34 N
ANISOU 4138 NE2 GLN A 524 8042 9677 8628 -875 -76 -1296 N
ATOM 4139 N PHE A 525 -9.089 18.711 -17.857 1.00 70.83 N
ANISOU 4139 N PHE A 525 8235 10281 8394 -700 -168 -1172 N
ATOM 4140 CA PHE A 525 -9.144 18.288 -16.461 1.00 72.05 C
ANISOU 4140 CA PHE A 525 8407 10527 8440 -678 -215 -1198 C
ATOM 4141 C PHE A 525 -8.262 17.070 -16.225 1.00 70.32 C
ANISOU 4141 C PHE A 525 8134 10385 8201 -672 -258 -1135 C
ATOM 4142 O PHE A 525 -7.439 17.053 -15.302 1.00 69.09 O
ANISOU 4142 O PHE A 525 7958 10289 8004 -689 -330 -1170 O
ATOM 4143 CB PHE A 525 -10.586 17.973 -16.055 1.00 73.84 C
ANISOU 4143 CB PHE A 525 8688 10777 8589 -620 -164 -1181 C
ATOM 4144 CG PHE A 525 -11.480 19.177 -15.966 1.00 66.20 C
ANISOU 4144 CG PHE A 525 7778 9753 7622 -615 -127 -1251 C
ATOM 4145 CD1 PHE A 525 -10.960 20.458 -16.014 1.00 64.80 C
ANISOU 4145 CD1 PHE A 525 7610 9514 7498 -660 -152 -1337 C
ATOM 4146 CD2 PHE A 525 -12.849 19.020 -15.821 1.00 65.87 C
ANISOU 4146 CD2 PHE A 525 7778 9717 7532 -563 -68 -1229 C
ATOM 4147 CE1 PHE A 525 -11.790 21.559 -15.928 1.00 70.32 C
ANISOU 4147 CE1 PHE A 525 8364 10153 8200 -651 -117 -1402 C
ATOM 4148 CE2 PHE A 525 -13.684 20.115 -15.735 1.00 60.41 C
ANISOU 4148 CE2 PHE A 525 7137 8974 6844 -551 -31 -1291 C
ATOM 4149 CZ PHE A 525 -13.154 21.387 -15.788 1.00 69.39 C
ANISOU 4149 CZ PHE A 525 8288 10045 8030 -593 -55 -1379 C
ATOM 4150 N GLN A 526 -8.425 16.037 -17.054 1.00 70.29 N
ANISOU 4150 N GLN A 526 8107 10376 8223 -646 -220 -1044 N
ATOM 4151 CA GLN A 526 -7.696 14.792 -16.840 1.00 69.36 C
ANISOU 4151 CA GLN A 526 7943 10325 8085 -631 -254 -978 C
ATOM 4152 C GLN A 526 -6.193 14.997 -16.976 1.00 77.25 C
ANISOU 4152 C GLN A 526 8876 11329 9145 -675 -308 -990 C
ATOM 4153 O GLN A 526 -5.417 14.497 -16.154 1.00 75.19 O
ANISOU 4153 O GLN A 526 8581 11142 8844 -676 -371 -985 O
ATOM 4154 CB GLN A 526 -8.189 13.722 -17.815 1.00 68.12 C
ANISOU 4154 CB GLN A 526 7782 10145 7956 -595 -201 -886 C
ATOM 4155 CG GLN A 526 -7.530 12.357 -17.645 1.00 77.37 C
ANISOU 4155 CG GLN A 526 8912 11376 9112 -570 -229 -813 C
ATOM 4156 CD GLN A 526 -7.995 11.616 -16.400 1.00 85.03 C
ANISOU 4156 CD GLN A 526 9901 12429 9979 -535 -253 -792 C
ATOM 4157 OE1 GLN A 526 -8.786 12.131 -15.608 1.00 77.48 O
ANISOU 4157 OE1 GLN A 526 8989 11494 8956 -526 -248 -835 O
ATOM 4158 NE2 GLN A 526 -7.505 10.394 -16.227 1.00 92.13 N
ANISOU 4158 NE2 GLN A 526 10766 13375 10863 -509 -276 -722 N
ATOM 4159 N GLU A 527 -5.762 15.740 -17.998 1.00 74.69 N
ANISOU 4159 N GLU A 527 8529 10928 8921 -713 -284 -1002 N
ATOM 4160 CA GLU A 527 -4.333 15.972 -18.182 1.00 75.52 C
ANISOU 4160 CA GLU A 527 8562 11035 9098 -758 -330 -1005 C
ATOM 4161 C GLU A 527 -3.741 16.736 -17.004 1.00 77.71 C
ANISOU 4161 C GLU A 527 8830 11348 9346 -799 -413 -1090 C
ATOM 4162 O GLU A 527 -2.599 16.484 -16.601 1.00 76.12 O
ANISOU 4162 O GLU A 527 8567 11197 9160 -822 -479 -1085 O
ATOM 4163 CB GLU A 527 -4.083 16.727 -19.486 1.00 62.17 C
ANISOU 4163 CB GLU A 527 6852 9252 7519 -789 -279 -998 C
ATOM 4164 CG GLU A 527 -2.623 16.767 -19.903 1.00 67.78 C
ANISOU 4164 CG GLU A 527 7474 9962 8316 -827 -307 -974 C
ATOM 4165 CD GLU A 527 -2.368 17.739 -21.037 1.00 84.30 C
ANISOU 4165 CD GLU A 527 9550 11964 10517 -864 -258 -974 C
ATOM 4166 OE1 GLU A 527 -2.686 18.936 -20.877 1.00 88.04 O
ANISOU 4166 OE1 GLU A 527 10055 12383 11014 -902 -262 -1042 O
ATOM 4167 OE2 GLU A 527 -1.858 17.305 -22.092 1.00 77.35 O
ANISOU 4167 OE2 GLU A 527 8627 11065 9696 -852 -214 -904 O
ATOM 4168 N ALA A 528 -4.506 17.668 -16.433 1.00 77.56 N
ANISOU 4168 N ALA A 528 8877 11308 9286 -806 -414 -1171 N
ATOM 4169 CA ALA A 528 -4.007 18.445 -15.304 1.00 73.69 C
ANISOU 4169 CA ALA A 528 8391 10846 8761 -842 -498 -1264 C
ATOM 4170 C ALA A 528 -3.967 17.606 -14.032 1.00 81.13 C
ANISOU 4170 C ALA A 528 9343 11901 9581 -806 -556 -1261 C
ATOM 4171 O ALA A 528 -2.982 17.639 -13.285 1.00 80.26 O
ANISOU 4171 O ALA A 528 9194 11844 9456 -833 -644 -1292 O
ATOM 4172 CB ALA A 528 -4.870 19.691 -15.103 1.00 59.61 C
ANISOU 4172 CB ALA A 528 6682 8999 6968 -853 -477 -1355 C
ATOM 4173 N LEU A 529 -5.033 16.845 -13.769 1.00 78.13 N
ANISOU 4173 N LEU A 529 9012 11559 9114 -743 -508 -1219 N
ATOM 4174 CA LEU A 529 -5.079 16.034 -12.557 1.00 69.60 C
ANISOU 4174 CA LEU A 529 7946 10587 7913 -703 -554 -1205 C
ATOM 4175 C LEU A 529 -4.069 14.894 -12.611 1.00 77.17 C
ANISOU 4175 C LEU A 529 8830 11604 8888 -697 -593 -1124 C
ATOM 4176 O LEU A 529 -3.488 14.523 -11.584 1.00 77.75 O
ANISOU 4176 O LEU A 529 8887 11764 8889 -690 -668 -1130 O
ATOM 4177 CB LEU A 529 -6.493 15.492 -12.341 1.00 67.25 C
ANISOU 4177 CB LEU A 529 7711 10308 7533 -639 -484 -1166 C
ATOM 4178 CG LEU A 529 -7.593 16.534 -12.128 1.00 65.92 C
ANISOU 4178 CG LEU A 529 7618 10096 7332 -630 -441 -1241 C
ATOM 4179 CD1 LEU A 529 -8.939 15.863 -11.898 1.00 62.97 C
ANISOU 4179 CD1 LEU A 529 7289 9751 6884 -566 -372 -1186 C
ATOM 4180 CD2 LEU A 529 -7.247 17.461 -10.974 1.00 60.49 C
ANISOU 4180 CD2 LEU A 529 6966 9442 6577 -648 -513 -1354 C
ATOM 4181 N CYS A 530 -3.847 14.324 -13.799 1.00 79.93 N
ANISOU 4181 N CYS A 530 9134 11907 9326 -695 -544 -1046 N
ATOM 4182 CA CYS A 530 -2.869 13.248 -13.922 1.00 80.96 C
ANISOU 4182 CA CYS A 530 9193 12086 9481 -684 -575 -968 C
ATOM 4183 C CYS A 530 -1.448 13.756 -13.724 1.00 82.93 C
ANISOU 4183 C CYS A 530 9371 12352 9788 -738 -656 -1004 C
ATOM 4184 O CYS A 530 -0.596 13.021 -13.213 1.00 80.75 O
ANISOU 4184 O CYS A 530 9041 12149 9493 -728 -716 -966 O
ATOM 4185 CB CYS A 530 -3.012 12.561 -15.280 1.00 71.38 C
ANISOU 4185 CB CYS A 530 7959 10814 8347 -663 -498 -885 C
ATOM 4186 SG CYS A 530 -4.564 11.659 -15.457 1.00 82.57 S
ANISOU 4186 SG CYS A 530 9446 12224 9703 -600 -422 -825 S
ATOM 4187 N GLN A 531 -1.172 15.001 -14.118 1.00 84.12 N
ANISOU 4187 N GLN A 531 9514 12433 10015 -796 -661 -1074 N
ATOM 4188 CA GLN A 531 0.128 15.589 -13.818 1.00 73.77 C
ANISOU 4188 CA GLN A 531 8133 11135 8762 -856 -747 -1116 C
ATOM 4189 C GLN A 531 0.291 15.807 -12.320 1.00 78.02 C
ANISOU 4189 C GLN A 531 8696 11754 9195 -861 -847 -1188 C
ATOM 4190 O GLN A 531 1.374 15.578 -11.766 1.00 76.82 O
ANISOU 4190 O GLN A 531 8478 11663 9047 -881 -936 -1185 O
ATOM 4191 CB GLN A 531 0.303 16.905 -14.575 1.00 71.57 C
ANISOU 4191 CB GLN A 531 7846 10755 8594 -920 -727 -1171 C
ATOM 4192 CG GLN A 531 1.686 17.515 -14.420 1.00 74.29 C
ANISOU 4192 CG GLN A 531 8102 11098 9025 -990 -812 -1203 C
ATOM 4193 CD GLN A 531 1.696 19.015 -14.636 1.00 79.10 C
ANISOU 4193 CD GLN A 531 8727 11615 9712 -1058 -820 -1291 C
ATOM 4194 OE1 GLN A 531 1.965 19.783 -13.712 1.00 97.76 O
ANISOU 4194 OE1 GLN A 531 11104 13988 12052 -1100 -908 -1385 O
ATOM 4195 NE2 GLN A 531 1.409 19.441 -15.860 1.00100.55 N
ANISOU 4195 NE2 GLN A 531 11444 14239 12521 -1069 -730 -1260 N
ATOM 4196 N ALA A 532 -0.777 16.246 -11.647 1.00 79.90 N
ANISOU 4196 N ALA A 532 9028 11995 9336 -839 -835 -1252 N
ATOM 4197 CA ALA A 532 -0.735 16.373 -10.195 1.00 76.56 C
ANISOU 4197 CA ALA A 532 8642 11657 8790 -828 -922 -1318 C
ATOM 4198 C ALA A 532 -0.563 15.017 -9.524 1.00 70.64 C
ANISOU 4198 C ALA A 532 7874 11018 7949 -772 -949 -1237 C
ATOM 4199 O ALA A 532 0.088 14.921 -8.477 1.00 81.60 O
ANISOU 4199 O ALA A 532 9248 12489 9267 -774 -1048 -1266 O
ATOM 4200 CB ALA A 532 -2.006 17.061 -9.691 1.00 74.46 C
ANISOU 4200 CB ALA A 532 8485 11372 8435 -803 -884 -1394 C
ATOM 4201 N ALA A 533 -1.133 13.963 -10.109 1.00 74.16 N
ANISOU 4201 N ALA A 533 8320 11462 8394 -721 -868 -1135 N
ATOM 4202 CA ALA A 533 -0.963 12.609 -9.597 1.00 74.57 C
ANISOU 4202 CA ALA A 533 8350 11605 8377 -666 -885 -1045 C
ATOM 4203 C ALA A 533 0.384 12.002 -9.963 1.00 78.79 C
ANISOU 4203 C ALA A 533 8781 12161 8995 -683 -933 -983 C
ATOM 4204 O ALA A 533 0.621 10.832 -9.641 1.00 81.25 O
ANISOU 4204 O ALA A 533 9066 12540 9266 -637 -946 -900 O
ATOM 4205 CB ALA A 533 -2.090 11.709 -10.109 1.00 72.44 C
ANISOU 4205 CB ALA A 533 8119 11315 8089 -609 -783 -960 C
ATOM 4206 N LYS A 534 1.256 12.761 -10.631 1.00 75.23 N
ANISOU 4206 N LYS A 534 8269 11653 8663 -746 -954 -1017 N
ATOM 4207 CA LYS A 534 2.588 12.297 -11.021 1.00 75.67 C
ANISOU 4207 CA LYS A 534 8215 11727 8810 -764 -996 -959 C
ATOM 4208 C LYS A 534 2.509 11.064 -11.920 1.00 87.74 C
ANISOU 4208 C LYS A 534 9716 13242 10379 -711 -916 -843 C
ATOM 4209 O LYS A 534 3.334 10.152 -11.830 1.00 88.91 O
ANISOU 4209 O LYS A 534 9796 13442 10542 -686 -949 -771 O
ATOM 4210 CB LYS A 534 3.459 12.021 -9.793 1.00 74.93 C
ANISOU 4210 CB LYS A 534 8081 11740 8648 -764 -1117 -970 C
ATOM 4211 CG LYS A 534 3.571 13.196 -8.836 1.00 93.73 C
ANISOU 4211 CG LYS A 534 10496 14138 10979 -813 -1209 -1094 C
ATOM 4212 CD LYS A 534 4.245 12.783 -7.538 1.00109.46 C
ANISOU 4212 CD LYS A 534 12467 16250 12875 -798 -1330 -1099 C
ATOM 4213 CE LYS A 534 4.270 13.927 -6.538 1.00110.98 C
ANISOU 4213 CE LYS A 534 12709 16459 12999 -840 -1425 -1233 C
ATOM 4214 NZ LYS A 534 5.049 15.089 -7.048 1.00126.95 N
ANISOU 4214 NZ LYS A 534 14674 18403 15157 -931 -1469 -1304 N
ATOM 4215 N HIS A 535 1.508 11.036 -12.797 1.00 86.18 N
ANISOU 4215 N HIS A 535 9572 12970 10200 -692 -815 -825 N
ATOM 4216 CA HIS A 535 1.343 9.909 -13.704 1.00 86.08 C
ANISOU 4216 CA HIS A 535 9547 12933 10226 -642 -741 -726 C
ATOM 4217 C HIS A 535 2.420 9.922 -14.780 1.00 90.85 C
ANISOU 4217 C HIS A 535 10063 13495 10959 -663 -724 -689 C
ATOM 4218 O HIS A 535 2.735 10.966 -15.357 1.00 95.88 O
ANISOU 4218 O HIS A 535 10679 14074 11676 -717 -714 -736 O
ATOM 4219 CB HIS A 535 -0.039 9.941 -14.355 1.00 79.22 C
ANISOU 4219 CB HIS A 535 8760 11996 9344 -619 -647 -724 C
ATOM 4220 CG HIS A 535 -0.201 8.953 -15.467 1.00 83.04 C
ANISOU 4220 CG HIS A 535 9235 12436 9881 -577 -574 -637 C
ATOM 4221 ND1 HIS A 535 -0.223 7.591 -15.255 1.00 94.64 N
ANISOU 4221 ND1 HIS A 535 10698 13947 11315 -520 -573 -555 N
ATOM 4222 CD2 HIS A 535 -0.337 9.128 -16.803 1.00 78.75 C
ANISOU 4222 CD2 HIS A 535 8692 11808 9421 -581 -502 -622 C
ATOM 4223 CE1 HIS A 535 -0.371 6.970 -16.412 1.00 86.05 C
ANISOU 4223 CE1 HIS A 535 9608 12797 10288 -492 -507 -500 C
ATOM 4224 NE2 HIS A 535 -0.444 7.880 -17.367 1.00 76.15 N
ANISOU 4224 NE2 HIS A 535 8360 11471 9102 -526 -462 -539 N
ATOM 4225 N GLU A 536 2.982 8.748 -15.052 1.00 98.24 N
ANISOU 4225 N GLU A 536 10949 14460 11917 -618 -717 -600 N
ATOM 4226 CA GLU A 536 3.992 8.574 -16.084 1.00103.36 C
ANISOU 4226 CA GLU A 536 11514 15076 12680 -620 -688 -551 C
ATOM 4227 C GLU A 536 3.436 7.709 -17.206 1.00 99.14 C
ANISOU 4227 C GLU A 536 11012 14485 12170 -564 -592 -484 C
ATOM 4228 O GLU A 536 2.756 6.709 -16.953 1.00102.58 O
ANISOU 4228 O GLU A 536 11496 14938 12541 -511 -576 -442 O
ATOM 4229 CB GLU A 536 5.262 7.935 -15.513 1.00112.02 C
ANISOU 4229 CB GLU A 536 12516 16253 13793 -609 -764 -504 C
ATOM 4230 CG GLU A 536 5.902 8.716 -14.373 1.00129.48 C
ANISOU 4230 CG GLU A 536 14690 18527 15979 -664 -876 -569 C
ATOM 4231 CD GLU A 536 6.548 10.009 -14.833 1.00156.73 C
ANISOU 4231 CD GLU A 536 18088 21929 19533 -742 -889 -627 C
ATOM 4232 OE1 GLU A 536 6.793 10.158 -16.049 1.00169.13 O
ANISOU 4232 OE1 GLU A 536 19626 23432 21204 -747 -813 -595 O
ATOM 4233 OE2 GLU A 536 6.813 10.878 -13.975 1.00153.86 O
ANISOU 4233 OE2 GLU A 536 17718 21592 19149 -797 -976 -704 O
ATOM 4234 N GLY A 537 3.724 8.100 -18.444 1.00 89.25 N
ANISOU 4234 N GLY A 537 9736 13164 11010 -577 -528 -476 N
ATOM 4235 CA GLY A 537 3.295 7.345 -19.596 1.00 75.25 C
ANISOU 4235 CA GLY A 537 7994 11335 9261 -523 -441 -420 C
ATOM 4236 C GLY A 537 2.187 8.032 -20.367 1.00 79.66 C
ANISOU 4236 C GLY A 537 8632 11813 9821 -538 -374 -459 C
ATOM 4237 O GLY A 537 1.904 9.219 -20.174 1.00 80.67 O
ANISOU 4237 O GLY A 537 8779 11919 9952 -592 -384 -526 O
ATOM 4238 N PRO A 538 1.542 7.291 -21.268 1.00 78.32 N
ANISOU 4238 N PRO A 538 8512 11596 9650 -487 -306 -417 N
ATOM 4239 CA PRO A 538 0.451 7.872 -22.058 1.00 64.11 C
ANISOU 4239 CA PRO A 538 6786 9722 7850 -495 -245 -447 C
ATOM 4240 C PRO A 538 -0.695 8.339 -21.173 1.00 63.60 C
ANISOU 4240 C PRO A 538 6788 9666 7710 -516 -269 -500 C
ATOM 4241 O PRO A 538 -0.995 7.742 -20.137 1.00 79.43 O
ANISOU 4241 O PRO A 538 8807 11726 9644 -499 -311 -492 O
ATOM 4242 CB PRO A 538 0.019 6.718 -22.970 1.00 73.52 C
ANISOU 4242 CB PRO A 538 8016 10876 9041 -429 -191 -388 C
ATOM 4243 CG PRO A 538 1.211 5.817 -23.033 1.00 65.10 C
ANISOU 4243 CG PRO A 538 6878 9847 8008 -392 -204 -330 C
ATOM 4244 CD PRO A 538 1.856 5.914 -21.684 1.00 74.68 C
ANISOU 4244 CD PRO A 538 8037 11142 9197 -419 -286 -342 C
ATOM 4245 N LEU A 539 -1.342 9.422 -21.609 1.00 66.06 N
ANISOU 4245 N LEU A 539 7141 9921 8037 -550 -235 -550 N
ATOM 4246 CA LEU A 539 -2.394 10.038 -20.808 1.00 67.02 C
ANISOU 4246 CA LEU A 539 7322 10046 8095 -570 -250 -607 C
ATOM 4247 C LEU A 539 -3.595 9.115 -20.630 1.00 64.42 C
ANISOU 4247 C LEU A 539 7056 9721 7700 -523 -230 -574 C
ATOM 4248 O LEU A 539 -4.286 9.190 -19.607 1.00 76.04 O
ANISOU 4248 O LEU A 539 8562 11231 9100 -523 -255 -598 O
ATOM 4249 CB LEU A 539 -2.825 11.357 -21.451 1.00 60.11 C
ANISOU 4249 CB LEU A 539 6477 9101 7263 -609 -212 -660 C
ATOM 4250 CG LEU A 539 -3.903 12.181 -20.747 1.00 68.07 C
ANISOU 4250 CG LEU A 539 7547 10100 8216 -627 -218 -725 C
ATOM 4251 CD1 LEU A 539 -3.484 12.507 -19.323 1.00 72.29 C
ANISOU 4251 CD1 LEU A 539 8065 10703 8697 -653 -294 -776 C
ATOM 4252 CD2 LEU A 539 -4.193 13.452 -21.530 1.00 62.56 C
ANISOU 4252 CD2 LEU A 539 6870 9322 7576 -662 -176 -768 C
ATOM 4253 N HIS A 540 -3.856 8.236 -21.598 1.00 65.19 N
ANISOU 4253 N HIS A 540 7169 9780 7822 -481 -186 -518 N
ATOM 4254 CA HIS A 540 -5.044 7.393 -21.546 1.00 72.05 C
ANISOU 4254 CA HIS A 540 8093 10638 8645 -443 -167 -485 C
ATOM 4255 C HIS A 540 -4.933 6.252 -20.542 1.00 73.88 C
ANISOU 4255 C HIS A 540 8312 10936 8824 -412 -209 -438 C
ATOM 4256 O HIS A 540 -5.947 5.607 -20.252 1.00 74.48 O
ANISOU 4256 O HIS A 540 8428 11010 8858 -388 -199 -409 O
ATOM 4257 CB HIS A 540 -5.352 6.824 -22.934 1.00 63.03 C
ANISOU 4257 CB HIS A 540 6976 9426 7547 -411 -115 -446 C
ATOM 4258 CG HIS A 540 -4.432 5.721 -23.356 1.00 69.12 C
ANISOU 4258 CG HIS A 540 7710 10204 8347 -371 -118 -390 C
ATOM 4259 ND1 HIS A 540 -3.232 5.955 -23.993 1.00 70.88 N
ANISOU 4259 ND1 HIS A 540 7882 10424 8627 -373 -106 -385 N
ATOM 4260 CD2 HIS A 540 -4.541 4.376 -23.242 1.00 66.81 C
ANISOU 4260 CD2 HIS A 540 7426 9921 8039 -325 -128 -334 C
ATOM 4261 CE1 HIS A 540 -2.640 4.801 -24.248 1.00 78.38 C
ANISOU 4261 CE1 HIS A 540 8809 11382 9590 -326 -107 -331 C
ATOM 4262 NE2 HIS A 540 -3.414 3.828 -23.803 1.00 75.09 N
ANISOU 4262 NE2 HIS A 540 8430 10970 9132 -297 -123 -301 N
ATOM 4263 N LYS A 541 -3.743 5.986 -20.008 1.00 69.76 N
ANISOU 4263 N LYS A 541 7730 10471 8306 -413 -254 -424 N
ATOM 4264 CA LYS A 541 -3.543 4.931 -19.025 1.00 71.05 C
ANISOU 4264 CA LYS A 541 7877 10701 8419 -381 -297 -375 C
ATOM 4265 C LYS A 541 -3.524 5.462 -17.598 1.00 79.79 C
ANISOU 4265 C LYS A 541 8980 11885 9450 -404 -352 -414 C
ATOM 4266 O LYS A 541 -3.140 4.731 -16.679 1.00 80.53 O
ANISOU 4266 O LYS A 541 9052 12049 9498 -382 -398 -376 O
ATOM 4267 CB LYS A 541 -2.242 4.180 -19.315 1.00 67.01 C
ANISOU 4267 CB LYS A 541 7299 10208 7954 -357 -316 -326 C
ATOM 4268 CG LYS A 541 -2.096 3.718 -20.753 1.00 69.67 C
ANISOU 4268 CG LYS A 541 7639 10471 8360 -328 -260 -295 C
ATOM 4269 CD LYS A 541 -0.743 3.066 -20.992 1.00 71.23 C
ANISOU 4269 CD LYS A 541 7767 10692 8606 -299 -273 -250 C
ATOM 4270 CE LYS A 541 -0.614 1.755 -20.235 1.00 77.44 C
ANISOU 4270 CE LYS A 541 8542 11522 9358 -252 -309 -186 C
ATOM 4271 NZ LYS A 541 0.708 1.111 -20.470 1.00 78.58 N
ANISOU 4271 NZ LYS A 541 8615 11689 9553 -217 -320 -139 N
ATOM 4272 N CYS A 542 -3.940 6.708 -17.391 1.00 76.60 N
ANISOU 4272 N CYS A 542 8604 11471 9031 -445 -350 -489 N
ATOM 4273 CA CYS A 542 -3.766 7.367 -16.106 1.00 74.58 C
ANISOU 4273 CA CYS A 542 8347 11285 8706 -469 -408 -543 C
ATOM 4274 C CYS A 542 -4.861 6.987 -15.118 1.00 80.07 C
ANISOU 4274 C CYS A 542 9096 12025 9302 -439 -405 -530 C
ATOM 4275 O CYS A 542 -6.023 6.799 -15.489 1.00 72.57 O
ANISOU 4275 O CYS A 542 8193 11032 8347 -422 -350 -510 O
ATOM 4276 CB CYS A 542 -3.748 8.882 -16.288 1.00 82.38 C
ANISOU 4276 CB CYS A 542 9345 12235 9721 -522 -406 -634 C
ATOM 4277 SG CYS A 542 -4.142 9.794 -14.783 1.00 83.64 S
ANISOU 4277 SG CYS A 542 9546 12456 9778 -541 -457 -718 S
ATOM 4278 N ASP A 543 -4.474 6.891 -13.847 1.00 86.16 N
ANISOU 4278 N ASP A 543 9858 12886 9995 -433 -466 -537 N
ATOM 4279 CA ASP A 543 -5.399 6.664 -12.743 1.00 72.76 C
ANISOU 4279 CA ASP A 543 8210 11246 8190 -404 -466 -528 C
ATOM 4280 C ASP A 543 -5.015 7.617 -11.622 1.00 68.74 C
ANISOU 4280 C ASP A 543 7710 10804 7606 -427 -529 -611 C
ATOM 4281 O ASP A 543 -3.892 7.551 -11.112 1.00 78.69 O
ANISOU 4281 O ASP A 543 8922 12119 8856 -437 -602 -617 O
ATOM 4282 CB ASP A 543 -5.346 5.210 -12.264 1.00 77.81 C
ANISOU 4282 CB ASP A 543 8834 11938 8793 -354 -478 -426 C
ATOM 4283 CG ASP A 543 -6.332 4.925 -11.150 1.00 79.40 C
ANISOU 4283 CG ASP A 543 9083 12201 8885 -320 -468 -402 C
ATOM 4284 OD1 ASP A 543 -7.303 5.695 -10.998 1.00 77.12 O
ANISOU 4284 OD1 ASP A 543 8844 11897 8561 -327 -430 -451 O
ATOM 4285 OD2 ASP A 543 -6.130 3.930 -10.421 1.00 78.81 O
ANISOU 4285 OD2 ASP A 543 8995 12191 8760 -283 -494 -328 O
ATOM 4286 N ILE A 544 -5.936 8.502 -11.244 1.00 73.58 N
ANISOU 4286 N ILE A 544 8382 11409 8167 -433 -504 -676 N
ATOM 4287 CA ILE A 544 -5.638 9.536 -10.257 1.00 74.28 C
ANISOU 4287 CA ILE A 544 8492 11545 8186 -455 -562 -772 C
ATOM 4288 C ILE A 544 -5.947 9.027 -8.855 1.00 79.53 C
ANISOU 4288 C ILE A 544 9188 12317 8713 -408 -590 -750 C
ATOM 4289 O ILE A 544 -5.923 9.796 -7.888 1.00 86.39 O
ANISOU 4289 O ILE A 544 10093 13237 9496 -412 -634 -829 O
ATOM 4290 CB ILE A 544 -6.418 10.830 -10.549 1.00 74.68 C
ANISOU 4290 CB ILE A 544 8595 11530 8251 -480 -520 -861 C
ATOM 4291 CG1 ILE A 544 -7.907 10.637 -10.252 1.00 76.10 C
ANISOU 4291 CG1 ILE A 544 8837 11714 8363 -434 -448 -836 C
ATOM 4292 CG2 ILE A 544 -6.211 11.261 -11.992 1.00 75.76 C
ANISOU 4292 CG2 ILE A 544 8704 11562 8521 -519 -481 -867 C
ATOM 4293 CD1 ILE A 544 -8.707 11.921 -10.288 1.00 58.80 C
ANISOU 4293 CD1 ILE A 544 6701 9473 6166 -447 -412 -926 C
ATOM 4294 N SER A 545 -6.237 7.734 -8.736 1.00 72.53 N
ANISOU 4294 N SER A 545 8292 11463 7804 -363 -567 -642 N
ATOM 4295 CA SER A 545 -6.535 7.151 -7.435 1.00 76.92 C
ANISOU 4295 CA SER A 545 8873 12122 8229 -314 -587 -602 C
ATOM 4296 C SER A 545 -5.351 7.314 -6.488 1.00 93.18 C
ANISOU 4296 C SER A 545 10908 14270 10226 -321 -692 -640 C
ATOM 4297 O SER A 545 -4.189 7.320 -6.904 1.00 90.44 O
ANISOU 4297 O SER A 545 10499 13910 9953 -354 -747 -648 O
ATOM 4298 CB SER A 545 -6.893 5.673 -7.585 1.00 73.70 C
ANISOU 4298 CB SER A 545 8447 11722 7833 -270 -549 -469 C
ATOM 4299 OG SER A 545 -8.041 5.509 -8.400 1.00 79.89 O
ANISOU 4299 OG SER A 545 9255 12427 8672 -264 -461 -436 O
ATOM 4300 N ASN A 546 -5.666 7.466 -5.200 1.00 83.48 N
ANISOU 4300 N ASN A 546 9728 13133 8856 -287 -718 -663 N
ATOM 4301 CA ASN A 546 -4.716 7.639 -4.102 1.00 76.73 C
ANISOU 4301 CA ASN A 546 8865 12377 7911 -285 -824 -704 C
ATOM 4302 C ASN A 546 -3.940 8.947 -4.174 1.00 80.05 C
ANISOU 4302 C ASN A 546 9279 12770 8366 -348 -894 -836 C
ATOM 4303 O ASN A 546 -2.993 9.137 -3.401 1.00 88.08 O
ANISOU 4303 O ASN A 546 10277 13858 9332 -359 -997 -877 O
ATOM 4304 CB ASN A 546 -3.723 6.473 -4.013 1.00 83.18 C
ANISOU 4304 CB ASN A 546 9612 13244 8748 -269 -878 -606 C
ATOM 4305 CG ASN A 546 -4.390 5.171 -3.629 1.00 92.01 C
ANISOU 4305 CG ASN A 546 10742 14406 9810 -204 -828 -477 C
ATOM 4306 OD1 ASN A 546 -5.396 5.163 -2.919 1.00101.37 O
ANISOU 4306 OD1 ASN A 546 11990 15634 10892 -163 -783 -465 O
ATOM 4307 ND2 ASN A 546 -3.835 4.060 -4.096 1.00 98.21 N
ANISOU 4307 ND2 ASN A 546 11466 15180 10668 -191 -833 -376 N
ATOM 4308 N SER A 547 -4.313 9.862 -5.066 1.00 81.09 N
ANISOU 4308 N SER A 547 9424 12800 8588 -390 -846 -902 N
ATOM 4309 CA SER A 547 -3.619 11.139 -5.220 1.00 83.53 C
ANISOU 4309 CA SER A 547 9724 13065 8948 -454 -907 -1022 C
ATOM 4310 C SER A 547 -4.469 12.230 -4.579 1.00 86.98 C
ANISOU 4310 C SER A 547 10252 13500 9296 -447 -892 -1130 C
ATOM 4311 O SER A 547 -5.448 12.696 -5.168 1.00 82.97 O
ANISOU 4311 O SER A 547 9784 12917 8824 -445 -805 -1148 O
ATOM 4312 CB SER A 547 -3.351 11.439 -6.690 1.00 87.30 C
ANISOU 4312 CB SER A 547 10151 13426 9592 -506 -864 -1017 C
ATOM 4313 OG SER A 547 -2.838 12.751 -6.852 1.00 77.37 O
ANISOU 4313 OG SER A 547 8891 12116 8390 -569 -910 -1131 O
ATOM 4314 N THR A 548 -4.088 12.640 -3.368 1.00 91.39 N
ANISOU 4314 N THR A 548 10844 14141 9737 -439 -980 -1204 N
ATOM 4315 CA THR A 548 -4.796 13.729 -2.705 1.00 86.01 C
ANISOU 4315 CA THR A 548 10255 13459 8967 -427 -974 -1320 C
ATOM 4316 C THR A 548 -4.465 15.076 -3.335 1.00 83.02 C
ANISOU 4316 C THR A 548 9875 12974 8696 -500 -996 -1437 C
ATOM 4317 O THR A 548 -5.272 16.010 -3.257 1.00 81.60 O
ANISOU 4317 O THR A 548 9767 12746 8492 -494 -953 -1520 O
ATOM 4318 CB THR A 548 -4.465 13.745 -1.211 1.00 79.66 C
ANISOU 4318 CB THR A 548 9495 12777 7994 -392 -1066 -1369 C
ATOM 4319 OG1 THR A 548 -3.048 13.865 -1.032 1.00 81.59 O
ANISOU 4319 OG1 THR A 548 9678 13048 8276 -444 -1194 -1404 O
ATOM 4320 CG2 THR A 548 -4.948 12.463 -0.547 1.00 68.45 C
ANISOU 4320 CG2 THR A 548 8085 11461 6460 -312 -1028 -1247 C
ATOM 4321 N GLU A 549 -3.294 15.193 -3.967 1.00 90.57 N
ANISOU 4321 N GLU A 549 10749 13889 9776 -567 -1059 -1439 N
ATOM 4322 CA GLU A 549 -2.926 16.444 -4.623 1.00 87.30 C
ANISOU 4322 CA GLU A 549 10323 13368 9479 -641 -1078 -1536 C
ATOM 4323 C GLU A 549 -3.839 16.731 -5.809 1.00 88.29 C
ANISOU 4323 C GLU A 549 10463 13382 9702 -644 -956 -1511 C
ATOM 4324 O GLU A 549 -4.250 17.878 -6.020 1.00 88.29 O
ANISOU 4324 O GLU A 549 10509 13302 9736 -670 -936 -1602 O
ATOM 4325 CB GLU A 549 -1.464 16.396 -5.071 1.00 85.99 C
ANISOU 4325 CB GLU A 549 10053 13189 9431 -708 -1163 -1522 C
ATOM 4326 CG GLU A 549 -0.499 15.873 -4.016 1.00 97.42 C
ANISOU 4326 CG GLU A 549 11467 14754 10796 -701 -1284 -1517 C
ATOM 4327 CD GLU A 549 -0.373 14.360 -4.036 1.00116.79 C
ANISOU 4327 CD GLU A 549 13872 17283 13222 -648 -1260 -1374 C
ATOM 4328 OE1 GLU A 549 -0.220 13.789 -5.137 1.00111.21 O
ANISOU 4328 OE1 GLU A 549 13100 16522 12632 -656 -1197 -1285 O
ATOM 4329 OE2 GLU A 549 -0.438 13.741 -2.952 1.00110.54 O
ANISOU 4329 OE2 GLU A 549 13108 16601 12289 -594 -1302 -1352 O
ATOM 4330 N ALA A 550 -4.165 15.703 -6.596 1.00 81.32 N
ANISOU 4330 N ALA A 550 9542 12490 8865 -618 -878 -1388 N
ATOM 4331 CA ALA A 550 -5.103 15.890 -7.696 1.00 75.03 C
ANISOU 4331 CA ALA A 550 8763 11597 8149 -614 -767 -1360 C
ATOM 4332 C ALA A 550 -6.507 16.168 -7.177 1.00 84.29 C
ANISOU 4332 C ALA A 550 10027 12778 9222 -559 -699 -1388 C
ATOM 4333 O ALA A 550 -7.238 16.984 -7.751 1.00 79.19 O
ANISOU 4333 O ALA A 550 9416 12046 8625 -568 -637 -1430 O
ATOM 4334 CB ALA A 550 -5.097 14.664 -8.608 1.00 74.33 C
ANISOU 4334 CB ALA A 550 8616 11499 8125 -596 -712 -1227 C
ATOM 4335 N GLY A 551 -6.901 15.501 -6.090 1.00 86.88 N
ANISOU 4335 N GLY A 551 10391 13211 9410 -499 -706 -1359 N
ATOM 4336 CA GLY A 551 -8.212 15.754 -5.516 1.00 77.78 C
ANISOU 4336 CA GLY A 551 9320 12077 8156 -440 -637 -1380 C
ATOM 4337 C GLY A 551 -8.338 17.155 -4.951 1.00 81.87 C
ANISOU 4337 C GLY A 551 9907 12568 8631 -452 -667 -1526 C
ATOM 4338 O GLY A 551 -9.404 17.773 -5.031 1.00 76.85 O
ANISOU 4338 O GLY A 551 9329 11888 7982 -425 -592 -1562 O
ATOM 4339 N GLN A 552 -7.255 17.677 -4.372 1.00 85.66 N
ANISOU 4339 N GLN A 552 10381 13073 9093 -492 -780 -1613 N
ATOM 4340 CA GLN A 552 -7.279 19.045 -3.868 1.00 91.42 C
ANISOU 4340 CA GLN A 552 11177 13764 9793 -511 -821 -1762 C
ATOM 4341 C GLN A 552 -7.394 20.048 -5.009 1.00 91.67 C
ANISOU 4341 C GLN A 552 11199 13653 9978 -567 -780 -1808 C
ATOM 4342 O GLN A 552 -8.113 21.048 -4.894 1.00 96.05 O
ANISOU 4342 O GLN A 552 11825 14151 10519 -554 -745 -1895 O
ATOM 4343 CB GLN A 552 -6.026 19.321 -3.036 1.00 93.08 C
ANISOU 4343 CB GLN A 552 11375 14029 9961 -549 -964 -1842 C
ATOM 4344 CG GLN A 552 -5.966 20.722 -2.448 1.00 91.13 C
ANISOU 4344 CG GLN A 552 11202 13741 9683 -571 -1023 -2007 C
ATOM 4345 CD GLN A 552 -7.052 20.968 -1.419 1.00 94.34 C
ANISOU 4345 CD GLN A 552 11720 14204 9920 -486 -980 -2063 C
ATOM 4346 OE1 GLN A 552 -7.001 20.441 -0.308 1.00 99.85 O
ANISOU 4346 OE1 GLN A 552 12452 15023 10462 -432 -1022 -2059 O
ATOM 4347 NE2 GLN A 552 -8.044 21.772 -1.786 1.00 90.92 N
ANISOU 4347 NE2 GLN A 552 11344 13686 9516 -468 -892 -2110 N
ATOM 4348 N LYS A 553 -6.700 19.793 -6.121 1.00 85.95 N
ANISOU 4348 N LYS A 553 10390 12870 9399 -624 -782 -1746 N
ATOM 4349 CA LYS A 553 -6.745 20.716 -7.249 1.00 72.64 C
ANISOU 4349 CA LYS A 553 8690 11051 7858 -677 -742 -1777 C
ATOM 4350 C LYS A 553 -8.115 20.721 -7.912 1.00 83.05 C
ANISOU 4350 C LYS A 553 10047 12316 9193 -632 -616 -1732 C
ATOM 4351 O LYS A 553 -8.562 21.766 -8.399 1.00 86.16 O
ANISOU 4351 O LYS A 553 10473 12611 9651 -649 -579 -1792 O
ATOM 4352 CB LYS A 553 -5.661 20.356 -8.263 1.00 83.69 C
ANISOU 4352 CB LYS A 553 9987 12412 9398 -739 -767 -1710 C
ATOM 4353 CG LYS A 553 -4.999 21.560 -8.913 1.00 89.85 C
ANISOU 4353 CG LYS A 553 10743 13082 10314 -819 -798 -1783 C
ATOM 4354 CD LYS A 553 -3.844 21.138 -9.808 1.00 92.61 C
ANISOU 4354 CD LYS A 553 10985 13412 10792 -874 -823 -1709 C
ATOM 4355 CE LYS A 553 -2.970 22.328 -10.177 1.00106.79 C
ANISOU 4355 CE LYS A 553 12745 15116 12713 -960 -878 -1785 C
ATOM 4356 NZ LYS A 553 -3.734 23.396 -10.879 1.00102.76 N
ANISOU 4356 NZ LYS A 553 12284 14486 12275 -973 -806 -1828 N
ATOM 4357 N LEU A 554 -8.794 19.572 -7.940 1.00 83.74 N
ANISOU 4357 N LEU A 554 10127 12463 9228 -575 -554 -1623 N
ATOM 4358 CA LEU A 554 -10.142 19.526 -8.497 1.00 72.89 C
ANISOU 4358 CA LEU A 554 8784 11045 7865 -531 -442 -1577 C
ATOM 4359 C LEU A 554 -11.149 20.168 -7.552 1.00 80.79 C
ANISOU 4359 C LEU A 554 9873 12069 8753 -475 -409 -1651 C
ATOM 4360 O LEU A 554 -12.060 20.878 -7.996 1.00 73.81 O
ANISOU 4360 O LEU A 554 9026 11112 7906 -460 -338 -1677 O
ATOM 4361 CB LEU A 554 -10.538 18.081 -8.799 1.00 68.70 C
ANISOU 4361 CB LEU A 554 8215 10566 7321 -493 -392 -1439 C
ATOM 4362 CG LEU A 554 -11.936 17.872 -9.386 1.00 70.09 C
ANISOU 4362 CG LEU A 554 8412 10705 7515 -450 -284 -1377 C
ATOM 4363 CD1 LEU A 554 -12.033 18.472 -10.781 1.00 71.15 C
ANISOU 4363 CD1 LEU A 554 8526 10718 7790 -491 -244 -1376 C
ATOM 4364 CD2 LEU A 554 -12.298 16.396 -9.405 1.00 59.82 C
ANISOU 4364 CD2 LEU A 554 7079 9466 6184 -411 -252 -1248 C
ATOM 4365 N PHE A 555 -11.000 19.935 -6.245 1.00 83.90 N
ANISOU 4365 N PHE A 555 10305 12569 9006 -438 -459 -1685 N
ATOM 4366 CA PHE A 555 -11.945 20.489 -5.281 1.00 69.07 C
ANISOU 4366 CA PHE A 555 8515 10725 7005 -373 -423 -1754 C
ATOM 4367 C PHE A 555 -11.892 22.011 -5.246 1.00 79.23 C
ANISOU 4367 C PHE A 555 9857 11922 8324 -400 -446 -1898 C
ATOM 4368 O PHE A 555 -12.895 22.655 -4.918 1.00 82.51 O
ANISOU 4368 O PHE A 555 10342 12319 8689 -349 -384 -1950 O
ATOM 4369 CB PHE A 555 -11.677 19.914 -3.889 1.00 74.88 C
ANISOU 4369 CB PHE A 555 9280 11597 7575 -326 -478 -1760 C
ATOM 4370 CG PHE A 555 -12.640 20.395 -2.841 1.00 79.51 C
ANISOU 4370 CG PHE A 555 9960 12232 8017 -248 -435 -1823 C
ATOM 4371 CD1 PHE A 555 -13.879 19.793 -2.693 1.00 68.39 C
ANISOU 4371 CD1 PHE A 555 8568 10867 6550 -173 -327 -1734 C
ATOM 4372 CD2 PHE A 555 -12.310 21.451 -2.008 1.00 73.25 C
ANISOU 4372 CD2 PHE A 555 9240 11440 7151 -247 -502 -1972 C
ATOM 4373 CE1 PHE A 555 -14.769 20.235 -1.736 1.00 67.60 C
ANISOU 4373 CE1 PHE A 555 8551 10816 6318 -94 -277 -1787 C
ATOM 4374 CE2 PHE A 555 -13.196 21.897 -1.049 1.00 70.27 C
ANISOU 4374 CE2 PHE A 555 8955 11109 6634 -166 -457 -2034 C
ATOM 4375 CZ PHE A 555 -14.427 21.287 -0.912 1.00 74.93 C
ANISOU 4375 CZ PHE A 555 9557 11748 7164 -87 -340 -1939 C
ATOM 4376 N ASN A 556 -10.742 22.603 -5.583 1.00 84.88 N
ANISOU 4376 N ASN A 556 10540 12579 9132 -480 -534 -1962 N
ATOM 4377 CA ASN A 556 -10.633 24.058 -5.612 1.00 85.23 C
ANISOU 4377 CA ASN A 556 10633 12524 9228 -516 -561 -2096 C
ATOM 4378 C ASN A 556 -11.530 24.685 -6.671 1.00 78.55 C
ANISOU 4378 C ASN A 556 9796 11561 8490 -514 -461 -2082 C
ATOM 4379 O ASN A 556 -11.806 25.887 -6.599 1.00 82.88 O
ANISOU 4379 O ASN A 556 10402 12027 9061 -518 -457 -2188 O
ATOM 4380 CB ASN A 556 -9.181 24.475 -5.845 1.00 90.44 C
ANISOU 4380 CB ASN A 556 11239 13141 9983 -610 -674 -2148 C
ATOM 4381 CG ASN A 556 -8.282 24.139 -4.670 1.00102.76 C
ANISOU 4381 CG ASN A 556 12802 14809 11432 -613 -792 -2193 C
ATOM 4382 OD1 ASN A 556 -8.743 24.020 -3.535 1.00 84.55 O
ANISOU 4382 OD1 ASN A 556 10568 12592 8967 -546 -799 -2234 O
ATOM 4383 ND2 ASN A 556 -6.991 23.986 -4.939 1.00119.43 N
ANISOU 4383 ND2 ASN A 556 14834 16917 13626 -688 -883 -2183 N
ATOM 4384 N MET A 557 -11.984 23.904 -7.649 1.00 76.28 N
ANISOU 4384 N MET A 557 9454 11261 8269 -506 -384 -1955 N
ATOM 4385 CA MET A 557 -12.941 24.369 -8.644 1.00 75.91 C
ANISOU 4385 CA MET A 557 9415 11117 8312 -495 -288 -1927 C
ATOM 4386 C MET A 557 -14.362 23.917 -8.352 1.00 77.12 C
ANISOU 4386 C MET A 557 9603 11317 8380 -407 -190 -1872 C
ATOM 4387 O MET A 557 -15.307 24.661 -8.635 1.00 83.90 O
ANISOU 4387 O MET A 557 10502 12109 9267 -377 -120 -1899 O
ATOM 4388 CB MET A 557 -12.528 23.883 -10.039 1.00 69.84 C
ANISOU 4388 CB MET A 557 8564 10292 7681 -546 -269 -1827 C
ATOM 4389 CG MET A 557 -13.491 24.242 -11.166 1.00 64.09 C
ANISOU 4389 CG MET A 557 7837 9470 7045 -534 -174 -1783 C
ATOM 4390 SD MET A 557 -14.762 22.993 -11.463 1.00 84.84 S
ANISOU 4390 SD MET A 557 10450 12156 9631 -463 -80 -1647 S
ATOM 4391 CE MET A 557 -13.751 21.565 -11.848 1.00 70.45 C
ANISOU 4391 CE MET A 557 8545 10394 7829 -497 -126 -1543 C
ATOM 4392 N LEU A 558 -14.532 22.717 -7.790 1.00 74.49 N
ANISOU 4392 N LEU A 558 9254 11098 7953 -366 -182 -1790 N
ATOM 4393 CA LEU A 558 -15.871 22.208 -7.513 1.00 74.42 C
ANISOU 4393 CA LEU A 558 9267 11137 7872 -286 -88 -1722 C
ATOM 4394 C LEU A 558 -16.606 23.094 -6.515 1.00 76.87 C
ANISOU 4394 C LEU A 558 9665 11464 8078 -223 -58 -1821 C
ATOM 4395 O LEU A 558 -17.798 23.378 -6.686 1.00 74.41 O
ANISOU 4395 O LEU A 558 9377 11124 7770 -170 34 -1803 O
ATOM 4396 CB LEU A 558 -15.791 20.773 -6.993 1.00 70.82 C
ANISOU 4396 CB LEU A 558 8777 10800 7333 -257 -95 -1617 C
ATOM 4397 CG LEU A 558 -15.093 19.723 -7.860 1.00 71.62 C
ANISOU 4397 CG LEU A 558 8795 10897 7520 -305 -121 -1513 C
ATOM 4398 CD1 LEU A 558 -15.102 18.372 -7.162 1.00 63.33 C
ANISOU 4398 CD1 LEU A 558 7722 9963 6375 -267 -126 -1417 C
ATOM 4399 CD2 LEU A 558 -15.740 19.625 -9.231 1.00 69.84 C
ANISOU 4399 CD2 LEU A 558 8533 10581 7421 -319 -51 -1441 C
ATOM 4400 N ARG A 559 -15.910 23.549 -5.470 1.00 73.75 N
ANISOU 4400 N ARG A 559 9319 11112 7589 -224 -138 -1929 N
ATOM 4401 CA ARG A 559 -16.550 24.363 -4.443 1.00 76.32 C
ANISOU 4401 CA ARG A 559 9739 11460 7800 -156 -114 -2032 C
ATOM 4402 C ARG A 559 -16.934 25.748 -4.946 1.00 81.62 C
ANISOU 4402 C ARG A 559 10453 12000 8558 -166 -85 -2129 C
ATOM 4403 O ARG A 559 -17.727 26.431 -4.289 1.00 81.93 O
ANISOU 4403 O ARG A 559 10570 12041 8520 -97 -37 -2202 O
ATOM 4404 CB ARG A 559 -15.635 24.499 -3.225 1.00 76.05 C
ANISOU 4404 CB ARG A 559 9751 11504 7641 -157 -220 -2131 C
ATOM 4405 CG ARG A 559 -14.326 25.214 -3.511 1.00 78.86 C
ANISOU 4405 CG ARG A 559 10092 11785 8086 -252 -336 -2226 C
ATOM 4406 CD ARG A 559 -13.712 25.765 -2.236 1.00 83.31 C
ANISOU 4406 CD ARG A 559 10729 12401 8522 -241 -435 -2363 C
ATOM 4407 NE ARG A 559 -14.575 26.761 -1.611 1.00103.70 N
ANISOU 4407 NE ARG A 559 13416 14958 11028 -173 -388 -2474 N
ATOM 4408 CZ ARG A 559 -14.542 28.058 -1.886 1.00100.90 C
ANISOU 4408 CZ ARG A 559 13105 14479 10752 -203 -404 -2594 C
ATOM 4409 NH1 ARG A 559 -13.690 28.557 -2.766 1.00103.22 N
ANISOU 4409 NH1 ARG A 559 13348 14664 11206 -302 -464 -2616 N
ATOM 4410 NH2 ARG A 559 -15.387 28.875 -1.262 1.00106.64 N
ANISOU 4410 NH2 ARG A 559 13931 15189 11397 -127 -354 -2689 N
ATOM 4411 N LEU A 560 -16.391 26.179 -6.086 1.00 74.44 N
ANISOU 4411 N LEU A 560 9497 10978 7807 -245 -109 -2129 N
ATOM 4412 CA LEU A 560 -16.708 27.509 -6.595 1.00 70.11 C
ANISOU 4412 CA LEU A 560 8988 10299 7350 -258 -83 -2214 C
ATOM 4413 C LEU A 560 -18.154 27.593 -7.066 1.00 65.87 C
ANISOU 4413 C LEU A 560 8461 9731 6836 -191 41 -2154 C
ATOM 4414 O LEU A 560 -18.815 28.621 -6.876 1.00 66.57 O
ANISOU 4414 O LEU A 560 8614 9759 6923 -150 84 -2235 O
ATOM 4415 CB LEU A 560 -15.756 27.882 -7.730 1.00 68.82 C
ANISOU 4415 CB LEU A 560 8766 10029 7352 -358 -134 -2211 C
ATOM 4416 CG LEU A 560 -14.286 28.095 -7.372 1.00 73.93 C
ANISOU 4416 CG LEU A 560 9400 10679 8012 -435 -261 -2286 C
ATOM 4417 CD1 LEU A 560 -13.474 28.415 -8.617 1.00 70.82 C
ANISOU 4417 CD1 LEU A 560 8937 10178 7792 -527 -288 -2258 C
ATOM 4418 CD2 LEU A 560 -14.136 29.201 -6.337 1.00 70.25 C
ANISOU 4418 CD2 LEU A 560 9025 10191 7476 -422 -318 -2450 C
ATOM 4419 N GLY A 561 -18.662 26.526 -7.673 1.00 75.05 N
ANISOU 4419 N GLY A 561 9558 10933 8024 -179 98 -2012 N
ATOM 4420 CA GLY A 561 -20.003 26.580 -8.231 1.00 74.43 C
ANISOU 4420 CA GLY A 561 9475 10821 7985 -125 208 -1946 C
ATOM 4421 C GLY A 561 -20.057 27.570 -9.378 1.00 73.23 C
ANISOU 4421 C GLY A 561 9317 10525 7982 -166 223 -1971 C
ATOM 4422 O GLY A 561 -19.230 27.538 -10.297 1.00 63.00 O
ANISOU 4422 O GLY A 561 7972 9170 6793 -243 178 -1947 O
ATOM 4423 N LYS A 562 -21.044 28.462 -9.331 1.00 74.73 N
ANISOU 4423 N LYS A 562 9556 10659 8179 -109 293 -2016 N
ATOM 4424 CA LYS A 562 -21.164 29.558 -10.283 1.00 79.50 C
ANISOU 4424 CA LYS A 562 10167 11123 8915 -137 311 -2051 C
ATOM 4425 C LYS A 562 -20.704 30.888 -9.702 1.00 80.76 C
ANISOU 4425 C LYS A 562 10405 11210 9070 -146 266 -2209 C
ATOM 4426 O LYS A 562 -20.967 31.937 -10.298 1.00 89.23 O
ANISOU 4426 O LYS A 562 11500 12163 10241 -152 291 -2250 O
ATOM 4427 CB LYS A 562 -22.608 29.685 -10.768 1.00 72.71 C
ANISOU 4427 CB LYS A 562 9303 10236 8089 -68 419 -1985 C
ATOM 4428 CG LYS A 562 -22.907 28.940 -12.050 1.00 73.32 C
ANISOU 4428 CG LYS A 562 9300 10294 8265 -96 448 -1848 C
ATOM 4429 CD LYS A 562 -24.319 29.228 -12.530 1.00100.05 C
ANISOU 4429 CD LYS A 562 12682 13643 11692 -31 544 -1795 C
ATOM 4430 CE LYS A 562 -24.542 30.720 -12.727 1.00101.56 C
ANISOU 4430 CE LYS A 562 12927 13714 11948 -18 565 -1889 C
ATOM 4431 NZ LYS A 562 -25.923 31.024 -13.195 1.00113.03 N
ANISOU 4431 NZ LYS A 562 14371 15130 13444 50 658 -1834 N
ATOM 4432 N SER A 563 -20.027 30.870 -8.553 1.00 71.59 N
ANISOU 4432 N SER A 563 9287 10115 7798 -146 196 -2298 N
ATOM 4433 CA SER A 563 -19.672 32.117 -7.886 1.00 77.87 C
ANISOU 4433 CA SER A 563 10166 10844 8576 -148 148 -2458 C
ATOM 4434 C SER A 563 -18.586 32.878 -8.633 1.00 79.87 C
ANISOU 4434 C SER A 563 10399 10975 8972 -251 72 -2509 C
ATOM 4435 O SER A 563 -18.512 34.107 -8.528 1.00 79.55 O
ANISOU 4435 O SER A 563 10419 10829 8979 -259 54 -2623 O
ATOM 4436 CB SER A 563 -19.229 31.836 -6.452 1.00 79.85 C
ANISOU 4436 CB SER A 563 10471 11208 8662 -119 86 -2539 C
ATOM 4437 OG SER A 563 -18.172 30.892 -6.420 1.00 76.17 O
ANISOU 4437 OG SER A 563 9944 10816 8182 -184 3 -2488 O
ATOM 4438 N GLU A 564 -17.746 32.180 -9.385 1.00 83.71 N
ANISOU 4438 N GLU A 564 10801 11471 9533 -329 29 -2424 N
ATOM 4439 CA GLU A 564 -16.643 32.773 -10.118 1.00 80.42 C
ANISOU 4439 CA GLU A 564 10350 10952 9254 -430 -40 -2452 C
ATOM 4440 C GLU A 564 -16.819 32.546 -11.614 1.00 80.89 C
ANISOU 4440 C GLU A 564 10338 10949 9449 -461 16 -2328 C
ATOM 4441 O GLU A 564 -17.556 31.644 -12.031 1.00 91.89 O
ANISOU 4441 O GLU A 564 11694 12400 10820 -419 83 -2214 O
ATOM 4442 CB GLU A 564 -15.302 32.180 -9.657 1.00 78.81 C
ANISOU 4442 CB GLU A 564 10107 10820 9018 -497 -151 -2466 C
ATOM 4443 CG GLU A 564 -14.998 32.401 -8.182 1.00 71.35 C
ANISOU 4443 CG GLU A 564 9234 9941 7935 -472 -224 -2592 C
ATOM 4444 CD GLU A 564 -14.662 33.846 -7.855 1.00 81.05 C
ANISOU 4444 CD GLU A 564 10532 11053 9211 -501 -280 -2748 C
ATOM 4445 OE1 GLU A 564 -14.452 34.644 -8.792 1.00 88.91 O
ANISOU 4445 OE1 GLU A 564 11506 11915 10361 -557 -272 -2751 O
ATOM 4446 OE2 GLU A 564 -14.602 34.185 -6.654 1.00 95.44 O
ANISOU 4446 OE2 GLU A 564 12433 12916 10914 -467 -331 -2868 O
ATOM 4447 N PRO A 565 -16.178 33.362 -12.451 1.00 79.60 N
ANISOU 4447 N PRO A 565 10154 10664 9428 -534 -9 -2346 N
ATOM 4448 CA PRO A 565 -16.230 33.121 -13.898 1.00 77.67 C
ANISOU 4448 CA PRO A 565 9841 10365 9304 -564 39 -2226 C
ATOM 4449 C PRO A 565 -15.673 31.750 -14.251 1.00 70.77 C
ANISOU 4449 C PRO A 565 8890 9590 8412 -591 20 -2116 C
ATOM 4450 O PRO A 565 -14.740 31.252 -13.617 1.00 74.05 O
ANISOU 4450 O PRO A 565 9284 10076 8777 -626 -57 -2140 O
ATOM 4451 CB PRO A 565 -15.361 34.243 -14.476 1.00 75.69 C
ANISOU 4451 CB PRO A 565 9584 9980 9195 -646 -4 -2278 C
ATOM 4452 CG PRO A 565 -15.419 35.327 -13.451 1.00 81.74 C
ANISOU 4452 CG PRO A 565 10435 10696 9927 -632 -41 -2431 C
ATOM 4453 CD PRO A 565 -15.497 34.627 -12.126 1.00 66.85 C
ANISOU 4453 CD PRO A 565 8583 8945 7872 -584 -76 -2478 C
ATOM 4454 N TRP A 566 -16.265 31.137 -15.281 1.00 70.43 N
ANISOU 4454 N TRP A 566 8803 9547 8408 -571 87 -1996 N
ATOM 4455 CA TRP A 566 -15.829 29.806 -15.693 1.00 72.51 C
ANISOU 4455 CA TRP A 566 8998 9895 8658 -588 76 -1890 C
ATOM 4456 C TRP A 566 -14.383 29.812 -16.170 1.00 71.27 C
ANISOU 4456 C TRP A 566 8785 9711 8584 -676 9 -1884 C
ATOM 4457 O TRP A 566 -13.694 28.790 -16.077 1.00 69.95 O
ANISOU 4457 O TRP A 566 8568 9626 8385 -695 -30 -1834 O
ATOM 4458 CB TRP A 566 -16.751 29.259 -16.786 1.00 82.70 C
ANISOU 4458 CB TRP A 566 10262 11176 9986 -553 155 -1773 C
ATOM 4459 CG TRP A 566 -16.616 29.947 -18.115 1.00 76.57 C
ANISOU 4459 CG TRP A 566 9465 10285 9343 -589 183 -1738 C
ATOM 4460 CD1 TRP A 566 -17.351 31.004 -18.571 1.00 75.74 C
ANISOU 4460 CD1 TRP A 566 9396 10080 9301 -567 233 -1759 C
ATOM 4461 CD2 TRP A 566 -15.696 29.617 -19.164 1.00 75.64 C
ANISOU 4461 CD2 TRP A 566 9286 10143 9310 -647 166 -1669 C
ATOM 4462 NE1 TRP A 566 -16.942 31.354 -19.836 1.00 71.77 N
ANISOU 4462 NE1 TRP A 566 8861 9495 8915 -610 246 -1705 N
ATOM 4463 CE2 TRP A 566 -15.927 30.518 -20.222 1.00 71.73 C
ANISOU 4463 CE2 TRP A 566 8797 9536 8923 -658 208 -1650 C
ATOM 4464 CE3 TRP A 566 -14.698 28.649 -19.309 1.00 69.62 C
ANISOU 4464 CE3 TRP A 566 8466 9445 8542 -685 122 -1619 C
ATOM 4465 CZ2 TRP A 566 -15.197 30.480 -21.407 1.00 70.15 C
ANISOU 4465 CZ2 TRP A 566 8547 9289 8817 -705 211 -1582 C
ATOM 4466 CZ3 TRP A 566 -13.974 28.613 -20.485 1.00 59.62 C
ANISOU 4466 CZ3 TRP A 566 7150 8131 7372 -730 127 -1555 C
ATOM 4467 CH2 TRP A 566 -14.227 29.522 -21.519 1.00 74.59 C
ANISOU 4467 CH2 TRP A 566 9055 9919 9368 -740 173 -1536 C
ATOM 4468 N THR A 567 -13.907 30.949 -16.684 1.00 72.57 N
ANISOU 4468 N THR A 567 8953 9760 8862 -727 -3 -1929 N
ATOM 4469 CA THR A 567 -12.507 31.053 -17.076 1.00 76.18 C
ANISOU 4469 CA THR A 567 9350 10188 9407 -813 -66 -1925 C
ATOM 4470 C THR A 567 -11.587 30.939 -15.866 1.00 77.17 C
ANISOU 4470 C THR A 567 9476 10379 9467 -845 -164 -2009 C
ATOM 4471 O THR A 567 -10.510 30.337 -15.950 1.00 73.07 O
ANISOU 4471 O THR A 567 8890 9905 8968 -894 -219 -1974 O
ATOM 4472 CB THR A 567 -12.269 32.371 -17.815 1.00 75.91 C
ANISOU 4472 CB THR A 567 9322 10010 9511 -861 -54 -1955 C
ATOM 4473 OG1 THR A 567 -12.671 33.467 -16.985 1.00 80.65 O
ANISOU 4473 OG1 THR A 567 9998 10552 10094 -846 -70 -2078 O
ATOM 4474 CG2 THR A 567 -13.069 32.407 -19.110 1.00 69.40 C
ANISOU 4474 CG2 THR A 567 8489 9128 8750 -830 38 -1858 C
ATOM 4475 N LEU A 568 -11.999 31.505 -14.729 1.00 74.62 N
ANISOU 4475 N LEU A 568 9226 10063 9063 -814 -190 -2121 N
ATOM 4476 CA LEU A 568 -11.219 31.377 -13.503 1.00 80.11 C
ANISOU 4476 CA LEU A 568 9932 10829 9676 -835 -289 -2206 C
ATOM 4477 C LEU A 568 -11.352 29.983 -12.901 1.00 78.42 C
ANISOU 4477 C LEU A 568 9701 10765 9330 -787 -293 -2146 C
ATOM 4478 O LEU A 568 -10.365 29.420 -12.412 1.00 79.29 O
ANISOU 4478 O LEU A 568 9770 10947 9409 -822 -373 -2148 O
ATOM 4479 CB LEU A 568 -11.654 32.438 -12.491 1.00 80.36 C
ANISOU 4479 CB LEU A 568 10059 10821 9653 -808 -312 -2350 C
ATOM 4480 CG LEU A 568 -11.037 32.340 -11.093 1.00 71.87 C
ANISOU 4480 CG LEU A 568 9015 9828 8464 -813 -415 -2451 C
ATOM 4481 CD1 LEU A 568 -9.521 32.466 -11.157 1.00 72.00 C
ANISOU 4481 CD1 LEU A 568 8964 9826 8565 -914 -523 -2473 C
ATOM 4482 CD2 LEU A 568 -11.628 33.392 -10.167 1.00 75.81 C
ANISOU 4482 CD2 LEU A 568 9622 10283 8900 -772 -424 -2594 C
ATOM 4483 N ALA A 569 -12.562 29.417 -12.919 1.00 72.34 N
ANISOU 4483 N ALA A 569 8958 10041 8487 -708 -210 -2088 N
ATOM 4484 CA ALA A 569 -12.752 28.059 -12.420 1.00 64.09 C
ANISOU 4484 CA ALA A 569 7893 9129 7328 -663 -206 -2016 C
ATOM 4485 C ALA A 569 -11.918 27.063 -13.214 1.00 75.50 C
ANISOU 4485 C ALA A 569 9249 10606 8833 -706 -224 -1910 C
ATOM 4486 O ALA A 569 -11.330 26.137 -12.641 1.00 79.84 O
ANISOU 4486 O ALA A 569 9768 11254 9314 -707 -274 -1883 O
ATOM 4487 CB ALA A 569 -14.231 27.682 -12.472 1.00 62.28 C
ANISOU 4487 CB ALA A 569 7697 8926 7039 -578 -107 -1961 C
ATOM 4488 N LEU A 570 -11.855 27.237 -14.535 1.00 76.61 N
ANISOU 4488 N LEU A 570 9349 10663 9097 -737 -180 -1846 N
ATOM 4489 CA LEU A 570 -11.011 26.376 -15.352 1.00 70.30 C
ANISOU 4489 CA LEU A 570 8469 9885 8358 -775 -193 -1751 C
ATOM 4490 C LEU A 570 -9.537 26.574 -15.024 1.00 75.03 C
ANISOU 4490 C LEU A 570 9021 10490 8996 -846 -288 -1795 C
ATOM 4491 O LEU A 570 -8.761 25.611 -15.051 1.00 80.44 O
ANISOU 4491 O LEU A 570 9645 11245 9672 -861 -323 -1735 O
ATOM 4492 CB LEU A 570 -11.276 26.645 -16.834 1.00 67.72 C
ANISOU 4492 CB LEU A 570 8118 9465 8148 -787 -124 -1681 C
ATOM 4493 CG LEU A 570 -10.441 25.864 -17.850 1.00 70.30 C
ANISOU 4493 CG LEU A 570 8367 9799 8544 -819 -123 -1583 C
ATOM 4494 CD1 LEU A 570 -10.644 24.370 -17.682 1.00 58.14 C
ANISOU 4494 CD1 LEU A 570 6805 8363 6922 -775 -116 -1503 C
ATOM 4495 CD2 LEU A 570 -10.783 26.299 -19.266 1.00 76.87 C
ANISOU 4495 CD2 LEU A 570 9192 10536 9480 -824 -53 -1526 C
ATOM 4496 N GLU A 571 -9.137 27.807 -14.696 1.00 75.88 N
ANISOU 4496 N GLU A 571 9154 10525 9152 -892 -334 -1899 N
ATOM 4497 CA GLU A 571 -7.743 28.081 -14.373 1.00 79.76 C
ANISOU 4497 CA GLU A 571 9596 11016 9693 -967 -433 -1946 C
ATOM 4498 C GLU A 571 -7.312 27.420 -13.070 1.00 78.02 C
ANISOU 4498 C GLU A 571 9381 10916 9348 -952 -517 -1985 C
ATOM 4499 O GLU A 571 -6.123 27.134 -12.900 1.00 85.93 O
ANISOU 4499 O GLU A 571 10317 11954 10379 -1004 -596 -1979 O
ATOM 4500 CB GLU A 571 -7.511 29.591 -14.293 1.00 75.99 C
ANISOU 4500 CB GLU A 571 9152 10422 9300 -1019 -466 -2054 C
ATOM 4501 CG GLU A 571 -6.050 29.992 -14.392 1.00 81.02 C
ANISOU 4501 CG GLU A 571 9716 11024 10044 -1114 -554 -2076 C
ATOM 4502 CD GLU A 571 -5.838 31.485 -14.235 1.00 82.70 C
ANISOU 4502 CD GLU A 571 9964 11114 10344 -1170 -595 -2188 C
ATOM 4503 OE1 GLU A 571 -6.558 32.108 -13.428 1.00 75.75 O
ANISOU 4503 OE1 GLU A 571 9176 10216 9390 -1133 -603 -2292 O
ATOM 4504 OE2 GLU A 571 -4.951 32.034 -14.923 1.00 85.78 O
ANISOU 4504 OE2 GLU A 571 10290 11424 10879 -1248 -616 -2171 O
ATOM 4505 N ASN A 572 -8.247 27.171 -12.148 1.00 72.63 N
ANISOU 4505 N ASN A 572 8770 10299 8526 -881 -499 -2019 N
ATOM 4506 CA ASN A 572 -7.896 26.504 -10.900 1.00 73.79 C
ANISOU 4506 CA ASN A 572 8927 10568 8541 -858 -573 -2047 C
ATOM 4507 C ASN A 572 -7.498 25.049 -11.109 1.00 80.92 C
ANISOU 4507 C ASN A 572 9760 11568 9419 -844 -572 -1926 C
ATOM 4508 O ASN A 572 -6.808 24.482 -10.256 1.00 81.73 O
ANISOU 4508 O ASN A 572 9843 11764 9447 -846 -651 -1935 O
ATOM 4509 CB ASN A 572 -9.060 26.568 -9.911 1.00 76.98 C
ANISOU 4509 CB ASN A 572 9427 11023 8800 -776 -539 -2100 C
ATOM 4510 CG ASN A 572 -9.290 27.958 -9.364 1.00 80.23 C
ANISOU 4510 CG ASN A 572 9918 11358 9206 -782 -564 -2242 C
ATOM 4511 OD1 ASN A 572 -8.888 28.953 -9.967 1.00 80.82 O
ANISOU 4511 OD1 ASN A 572 9982 11317 9408 -843 -579 -2288 O
ATOM 4512 ND2 ASN A 572 -9.945 28.035 -8.212 1.00 72.80 N
ANISOU 4512 ND2 ASN A 572 9059 10481 8119 -715 -567 -2312 N
ATOM 4513 N VAL A 573 -7.915 24.433 -12.212 1.00 81.44 N
ANISOU 4513 N VAL A 573 9790 11611 9543 -828 -488 -1816 N
ATOM 4514 CA VAL A 573 -7.610 23.029 -12.457 1.00 75.55 C
ANISOU 4514 CA VAL A 573 8984 10945 8776 -809 -482 -1703 C
ATOM 4515 C VAL A 573 -6.431 22.911 -13.412 1.00 81.65 C
ANISOU 4515 C VAL A 573 9666 11679 9676 -872 -505 -1651 C
ATOM 4516 O VAL A 573 -5.427 22.260 -13.101 1.00 90.83 O
ANISOU 4516 O VAL A 573 10770 12908 10832 -892 -571 -1624 O
ATOM 4517 CB VAL A 573 -8.832 22.279 -13.017 1.00 69.10 C
ANISOU 4517 CB VAL A 573 8186 10135 7932 -745 -380 -1612 C
ATOM 4518 CG1 VAL A 573 -8.565 20.781 -13.036 1.00 71.64 C
ANISOU 4518 CG1 VAL A 573 8459 10545 8215 -719 -383 -1506 C
ATOM 4519 CG2 VAL A 573 -10.072 22.604 -12.212 1.00 68.41 C
ANISOU 4519 CG2 VAL A 573 8184 10069 7742 -684 -341 -1661 C
ATOM 4520 N VAL A 574 -6.545 23.550 -14.577 1.00 75.60 N
ANISOU 4520 N VAL A 574 8889 10809 9028 -900 -449 -1633 N
ATOM 4521 CA VAL A 574 -5.590 23.348 -15.663 1.00 75.30 C
ANISOU 4521 CA VAL A 574 8767 10734 9109 -945 -444 -1563 C
ATOM 4522 C VAL A 574 -4.542 24.450 -15.751 1.00 78.18 C
ANISOU 4522 C VAL A 574 9092 11029 9581 -1027 -503 -1626 C
ATOM 4523 O VAL A 574 -3.520 24.262 -16.431 1.00 79.84 O
ANISOU 4523 O VAL A 574 9221 11229 9888 -1070 -515 -1571 O
ATOM 4524 CB VAL A 574 -6.320 23.214 -17.017 1.00 77.03 C
ANISOU 4524 CB VAL A 574 8990 10888 9389 -920 -340 -1483 C
ATOM 4525 CG1 VAL A 574 -7.454 22.206 -16.903 1.00 66.71 C
ANISOU 4525 CG1 VAL A 574 7723 9639 7985 -845 -287 -1427 C
ATOM 4526 CG2 VAL A 574 -6.847 24.565 -17.474 1.00 68.75 C
ANISOU 4526 CG2 VAL A 574 7985 9727 8410 -941 -302 -1538 C
ATOM 4527 N GLY A 575 -4.752 25.584 -15.089 1.00 75.30 N
ANISOU 4527 N GLY A 575 8783 10617 9210 -1050 -540 -1738 N
ATOM 4528 CA GLY A 575 -3.820 26.689 -15.156 1.00 65.76 C
ANISOU 4528 CA GLY A 575 7542 9330 8113 -1132 -600 -1803 C
ATOM 4529 C GLY A 575 -4.025 27.632 -16.321 1.00 81.56 C
ANISOU 4529 C GLY A 575 9541 11201 10245 -1163 -531 -1786 C
ATOM 4530 O GLY A 575 -3.326 28.650 -16.400 1.00 78.11 O
ANISOU 4530 O GLY A 575 9080 10684 9914 -1235 -575 -1840 O
ATOM 4531 N ALA A 576 -4.950 27.328 -17.227 1.00 86.05 N
ANISOU 4531 N ALA A 576 10134 11746 10814 -1112 -428 -1712 N
ATOM 4532 CA ALA A 576 -5.263 28.179 -18.364 1.00 79.28 C
ANISOU 4532 CA ALA A 576 9282 10771 10068 -1130 -356 -1688 C
ATOM 4533 C ALA A 576 -6.665 28.754 -18.210 1.00 76.03 C
ANISOU 4533 C ALA A 576 8968 10315 9607 -1078 -301 -1735 C
ATOM 4534 O ALA A 576 -7.535 28.152 -17.574 1.00 73.53 O
ANISOU 4534 O ALA A 576 8701 10068 9168 -1013 -287 -1743 O
ATOM 4535 CB ALA A 576 -5.158 27.405 -19.682 1.00 90.73 C
ANISOU 4535 CB ALA A 576 10680 12225 11569 -1112 -281 -1558 C
ATOM 4536 N LYS A 577 -6.880 29.925 -18.806 1.00 76.75 N
ANISOU 4536 N LYS A 577 9080 10285 9795 -1104 -268 -1760 N
ATOM 4537 CA LYS A 577 -8.151 30.626 -18.684 1.00 78.14 C
ANISOU 4537 CA LYS A 577 9343 10404 9940 -1056 -217 -1810 C
ATOM 4538 C LYS A 577 -9.153 30.270 -19.775 1.00 82.74 C
ANISOU 4538 C LYS A 577 9939 10969 10529 -1000 -114 -1713 C
ATOM 4539 O LYS A 577 -10.312 30.687 -19.684 1.00 77.09 O
ANISOU 4539 O LYS A 577 9290 10222 9780 -949 -66 -1740 O
ATOM 4540 CB LYS A 577 -7.926 32.142 -18.698 1.00 73.82 C
ANISOU 4540 CB LYS A 577 8821 9728 9498 -1110 -237 -1893 C
ATOM 4541 CG LYS A 577 -7.112 32.677 -17.535 1.00 75.39 C
ANISOU 4541 CG LYS A 577 9026 9929 9690 -1164 -347 -2012 C
ATOM 4542 CD LYS A 577 -6.899 34.175 -17.681 1.00 78.97 C
ANISOU 4542 CD LYS A 577 9502 10238 10266 -1221 -364 -2088 C
ATOM 4543 CE LYS A 577 -6.077 34.741 -16.537 1.00 81.96 C
ANISOU 4543 CE LYS A 577 9888 10609 10642 -1280 -485 -2214 C
ATOM 4544 NZ LYS A 577 -5.847 36.203 -16.704 1.00 88.01 N
ANISOU 4544 NZ LYS A 577 10676 11222 11543 -1341 -506 -2289 N
ATOM 4545 N ASN A 578 -8.751 29.522 -20.799 1.00 79.09 N
ANISOU 4545 N ASN A 578 9416 10526 10107 -1005 -81 -1605 N
ATOM 4546 CA ASN A 578 -9.620 29.269 -21.937 1.00 84.37 C
ANISOU 4546 CA ASN A 578 10098 11168 10791 -958 8 -1517 C
ATOM 4547 C ASN A 578 -9.628 27.786 -22.282 1.00 84.95 C
ANISOU 4547 C ASN A 578 10137 11338 10803 -920 24 -1426 C
ATOM 4548 O ASN A 578 -8.762 27.017 -21.856 1.00 89.54 O
ANISOU 4548 O ASN A 578 10671 11993 11356 -939 -26 -1415 O
ATOM 4549 CB ASN A 578 -9.189 30.088 -23.164 1.00 95.18 C
ANISOU 4549 CB ASN A 578 11438 12432 12294 -998 47 -1472 C
ATOM 4550 CG ASN A 578 -10.319 30.292 -24.156 1.00102.01 C
ANISOU 4550 CG ASN A 578 12343 13244 13172 -947 132 -1415 C
ATOM 4551 OD1 ASN A 578 -11.343 29.609 -24.100 1.00 89.75 O
ANISOU 4551 OD1 ASN A 578 10824 11742 11536 -883 161 -1390 O
ATOM 4552 ND2 ASN A 578 -10.136 31.234 -25.074 1.00110.62 N
ANISOU 4552 ND2 ASN A 578 13427 14232 14372 -975 168 -1388 N
ATOM 4553 N MET A 579 -10.636 27.400 -23.061 1.00 70.01 N
ANISOU 4553 N MET A 579 8269 9438 8892 -866 91 -1360 N
ATOM 4554 CA MET A 579 -10.733 26.038 -23.562 1.00 73.92 C
ANISOU 4554 CA MET A 579 8739 10005 9342 -830 110 -1272 C
ATOM 4555 C MET A 579 -9.553 25.727 -24.476 1.00 83.04 C
ANISOU 4555 C MET A 579 9829 11155 10570 -865 111 -1206 C
ATOM 4556 O MET A 579 -9.123 26.568 -25.269 1.00 91.72 O
ANISOU 4556 O MET A 579 10911 12175 11763 -899 136 -1192 O
ATOM 4557 CB MET A 579 -12.056 25.858 -24.309 1.00 82.90 C
ANISOU 4557 CB MET A 579 9916 11120 10461 -771 176 -1220 C
ATOM 4558 CG MET A 579 -12.229 24.521 -25.002 1.00 75.56 C
ANISOU 4558 CG MET A 579 8966 10244 9497 -735 196 -1130 C
ATOM 4559 SD MET A 579 -13.823 24.398 -25.840 1.00 77.94 S
ANISOU 4559 SD MET A 579 9314 10514 9784 -673 259 -1078 S
ATOM 4560 CE MET A 579 -13.805 25.894 -26.825 1.00 66.22 C
ANISOU 4560 CE MET A 579 7844 8911 8404 -695 301 -1082 C
ATOM 4561 N ASN A 580 -9.025 24.511 -24.356 1.00 78.58 N
ANISOU 4561 N ASN A 580 9224 10672 9960 -854 88 -1162 N
ATOM 4562 CA ASN A 580 -7.846 24.103 -25.106 1.00 72.24 C
ANISOU 4562 CA ASN A 580 8354 9876 9216 -879 89 -1101 C
ATOM 4563 C ASN A 580 -8.060 22.709 -25.675 1.00 67.06 C
ANISOU 4563 C ASN A 580 7692 9278 8511 -827 114 -1020 C
ATOM 4564 O ASN A 580 -8.551 21.814 -24.980 1.00 72.17 O
ANISOU 4564 O ASN A 580 8356 9992 9073 -792 92 -1022 O
ATOM 4565 CB ASN A 580 -6.592 24.128 -24.221 1.00 80.31 C
ANISOU 4565 CB ASN A 580 9320 10940 10254 -931 15 -1142 C
ATOM 4566 CG ASN A 580 -5.314 23.948 -25.014 1.00 75.77 C
ANISOU 4566 CG ASN A 580 8666 10361 9763 -963 22 -1080 C
ATOM 4567 OD1 ASN A 580 -5.293 24.133 -26.230 1.00 85.72 O
ANISOU 4567 OD1 ASN A 580 9919 11569 11082 -956 85 -1018 O
ATOM 4568 ND2 ASN A 580 -4.237 23.587 -24.326 1.00 92.85 N
ANISOU 4568 ND2 ASN A 580 10768 12581 11929 -995 -42 -1092 N
ATOM 4569 N VAL A 581 -7.683 22.530 -26.945 1.00 67.38 N
ANISOU 4569 N VAL A 581 7708 9289 8604 -819 161 -949 N
ATOM 4570 CA VAL A 581 -7.858 21.246 -27.619 1.00 70.75 C
ANISOU 4570 CA VAL A 581 8135 9757 8989 -767 185 -876 C
ATOM 4571 C VAL A 581 -6.611 20.375 -27.558 1.00 71.52 C
ANISOU 4571 C VAL A 581 8167 9913 9094 -774 159 -841 C
ATOM 4572 O VAL A 581 -6.668 19.196 -27.944 1.00 65.96 O
ANISOU 4572 O VAL A 581 7463 9249 8350 -729 170 -788 O
ATOM 4573 CB VAL A 581 -8.273 21.466 -29.089 1.00 73.61 C
ANISOU 4573 CB VAL A 581 8522 10058 9387 -740 253 -819 C
ATOM 4574 CG1 VAL A 581 -7.058 21.781 -29.953 1.00 64.11 C
ANISOU 4574 CG1 VAL A 581 7265 8829 8264 -766 281 -774 C
ATOM 4575 CG2 VAL A 581 -9.037 20.265 -29.623 1.00 65.19 C
ANISOU 4575 CG2 VAL A 581 7488 9022 8257 -678 270 -769 C
ATOM 4576 N ARG A 582 -5.488 20.910 -27.081 1.00 65.73 N
ANISOU 4576 N ARG A 582 7377 9185 8415 -828 123 -868 N
ATOM 4577 CA ARG A 582 -4.260 20.120 -27.033 1.00 66.60 C
ANISOU 4577 CA ARG A 582 7414 9351 8540 -834 98 -829 C
ATOM 4578 C ARG A 582 -4.356 18.897 -26.124 1.00 67.14 C
ANISOU 4578 C ARG A 582 7483 9506 8522 -802 51 -830 C
ATOM 4579 O ARG A 582 -3.868 17.829 -26.532 1.00 64.33 O
ANISOU 4579 O ARG A 582 7096 9188 8156 -768 61 -770 O
ATOM 4580 CB ARG A 582 -3.084 21.017 -26.623 1.00 63.56 C
ANISOU 4580 CB ARG A 582 6960 8951 8237 -905 59 -861 C
ATOM 4581 CG ARG A 582 -1.740 20.316 -26.665 1.00 77.02 C
ANISOU 4581 CG ARG A 582 8577 10711 9976 -913 38 -813 C
ATOM 4582 CD ARG A 582 -0.693 21.077 -25.871 1.00 83.96 C
ANISOU 4582 CD ARG A 582 9389 11593 10921 -988 -29 -860 C
ATOM 4583 NE ARG A 582 -1.178 21.423 -24.540 1.00 87.52 N
ANISOU 4583 NE ARG A 582 9880 12062 11311 -1009 -102 -951 N
ATOM 4584 CZ ARG A 582 -1.230 20.580 -23.518 1.00 86.72 C
ANISOU 4584 CZ ARG A 582 9784 12044 11121 -986 -160 -972 C
ATOM 4585 NH1 ARG A 582 -0.838 19.322 -23.639 1.00 89.49 N
ANISOU 4585 NH1 ARG A 582 10100 12461 11439 -944 -158 -908 N
ATOM 4586 NH2 ARG A 582 -1.691 21.008 -22.347 1.00 85.32 N
ANISOU 4586 NH2 ARG A 582 9650 11882 10885 -1002 -218 -1057 N
ATOM 4587 N PRO A 583 -4.933 18.964 -24.916 1.00 73.71 N
ANISOU 4587 N PRO A 583 8348 10371 9288 -806 3 -890 N
ATOM 4588 CA PRO A 583 -5.069 17.731 -24.119 1.00 70.30 C
ANISOU 4588 CA PRO A 583 7918 10022 8772 -769 -34 -875 C
ATOM 4589 C PRO A 583 -5.895 16.657 -24.804 1.00 69.92 C
ANISOU 4589 C PRO A 583 7907 9977 8683 -707 10 -814 C
ATOM 4590 O PRO A 583 -5.595 15.466 -24.650 1.00 67.49 O
ANISOU 4590 O PRO A 583 7579 9723 8342 -676 -6 -771 O
ATOM 4591 CB PRO A 583 -5.738 18.221 -22.828 1.00 58.12 C
ANISOU 4591 CB PRO A 583 6418 8501 7164 -780 -77 -952 C
ATOM 4592 CG PRO A 583 -5.357 19.650 -22.731 1.00 64.63 C
ANISOU 4592 CG PRO A 583 7235 9269 8053 -838 -91 -1017 C
ATOM 4593 CD PRO A 583 -5.336 20.152 -24.140 1.00 71.20 C
ANISOU 4593 CD PRO A 583 8062 10020 8970 -844 -24 -975 C
ATOM 4594 N LEU A 584 -6.935 17.043 -25.548 1.00 68.81 N
ANISOU 4594 N LEU A 584 7820 9777 8546 -689 61 -810 N
ATOM 4595 CA LEU A 584 -7.700 16.066 -26.317 1.00 58.18 C
ANISOU 4595 CA LEU A 584 6508 8426 7172 -635 96 -753 C
ATOM 4596 C LEU A 584 -6.821 15.369 -27.348 1.00 67.42 C
ANISOU 4596 C LEU A 584 7644 9594 8379 -615 120 -692 C
ATOM 4597 O LEU A 584 -6.895 14.145 -27.515 1.00 67.74 O
ANISOU 4597 O LEU A 584 7689 9664 8387 -573 118 -648 O
ATOM 4598 CB LEU A 584 -8.885 16.753 -26.997 1.00 70.05 C
ANISOU 4598 CB LEU A 584 8069 9865 8684 -624 142 -761 C
ATOM 4599 CG LEU A 584 -9.633 15.965 -28.074 1.00 64.61 C
ANISOU 4599 CG LEU A 584 7415 9152 7981 -574 177 -705 C
ATOM 4600 CD1 LEU A 584 -10.443 14.834 -27.465 1.00 56.94 C
ANISOU 4600 CD1 LEU A 584 6464 8224 6945 -541 154 -688 C
ATOM 4601 CD2 LEU A 584 -10.523 16.891 -28.885 1.00 60.64 C
ANISOU 4601 CD2 LEU A 584 6956 8580 7505 -571 220 -710 C
ATOM 4602 N LEU A 585 -5.978 16.132 -28.048 1.00 62.36 N
ANISOU 4602 N LEU A 585 6968 8918 7809 -642 146 -685 N
ATOM 4603 CA LEU A 585 -5.076 15.531 -29.023 1.00 62.89 C
ANISOU 4603 CA LEU A 585 6999 8987 7910 -617 178 -624 C
ATOM 4604 C LEU A 585 -3.980 14.720 -28.345 1.00 68.60 C
ANISOU 4604 C LEU A 585 7657 9778 8631 -618 135 -609 C
ATOM 4605 O LEU A 585 -3.526 13.711 -28.896 1.00 74.02 O
ANISOU 4605 O LEU A 585 8328 10483 9314 -574 152 -557 O
ATOM 4606 CB LEU A 585 -4.465 16.616 -29.909 1.00 67.87 C
ANISOU 4606 CB LEU A 585 7604 9564 8621 -646 223 -613 C
ATOM 4607 CG LEU A 585 -5.456 17.544 -30.613 1.00 67.84 C
ANISOU 4607 CG LEU A 585 7659 9488 8628 -646 267 -623 C
ATOM 4608 CD1 LEU A 585 -4.724 18.523 -31.521 1.00 57.51 C
ANISOU 4608 CD1 LEU A 585 6318 8129 7402 -672 316 -597 C
ATOM 4609 CD2 LEU A 585 -6.488 16.743 -31.395 1.00 63.75 C
ANISOU 4609 CD2 LEU A 585 7207 8960 8056 -584 294 -591 C
ATOM 4610 N ASN A 586 -3.539 15.148 -27.159 1.00 65.98 N
ANISOU 4610 N ASN A 586 7289 9481 8300 -664 78 -654 N
ATOM 4611 CA ASN A 586 -2.562 14.370 -26.407 1.00 64.13 C
ANISOU 4611 CA ASN A 586 6993 9317 8056 -663 27 -639 C
ATOM 4612 C ASN A 586 -3.127 13.014 -26.005 1.00 64.07 C
ANISOU 4612 C ASN A 586 7016 9354 7972 -609 9 -613 C
ATOM 4613 O ASN A 586 -2.384 12.029 -25.927 1.00 71.06 O
ANISOU 4613 O ASN A 586 7860 10284 8855 -582 -6 -570 O
ATOM 4614 CB ASN A 586 -2.116 15.156 -25.172 1.00 65.97 C
ANISOU 4614 CB ASN A 586 7192 9580 8294 -722 -41 -702 C
ATOM 4615 CG ASN A 586 -1.071 14.421 -24.354 1.00 70.64 C
ANISOU 4615 CG ASN A 586 7716 10249 8877 -723 -102 -686 C
ATOM 4616 OD1 ASN A 586 -0.302 13.618 -24.881 1.00 75.73 O
ANISOU 4616 OD1 ASN A 586 8312 10914 9548 -693 -85 -625 O
ATOM 4617 ND2 ASN A 586 -1.040 14.694 -23.054 1.00 69.40 N
ANISOU 4617 ND2 ASN A 586 7555 10136 8677 -754 -174 -741 N
ATOM 4618 N TYR A 587 -4.437 12.942 -25.761 1.00 60.78 N
ANISOU 4618 N TYR A 587 6670 8925 7499 -593 14 -632 N
ATOM 4619 CA TYR A 587 -5.052 11.682 -25.358 1.00 60.80 C
ANISOU 4619 CA TYR A 587 6701 8963 7437 -548 -2 -602 C
ATOM 4620 C TYR A 587 -5.062 10.677 -26.503 1.00 64.61 C
ANISOU 4620 C TYR A 587 7196 9419 7932 -495 37 -542 C
ATOM 4621 O TYR A 587 -4.823 9.483 -26.289 1.00 75.61 O
ANISOU 4621 O TYR A 587 8578 10846 9303 -459 19 -503 O
ATOM 4622 CB TYR A 587 -6.473 11.940 -24.855 1.00 61.56 C
ANISOU 4622 CB TYR A 587 6861 9049 7481 -546 -2 -634 C
ATOM 4623 CG TYR A 587 -7.175 10.725 -24.285 1.00 67.55 C
ANISOU 4623 CG TYR A 587 7644 9846 8178 -507 -20 -600 C
ATOM 4624 CD1 TYR A 587 -7.885 9.858 -25.107 1.00 65.24 C
ANISOU 4624 CD1 TYR A 587 7387 9519 7884 -466 9 -554 C
ATOM 4625 CD2 TYR A 587 -7.145 10.457 -22.923 1.00 63.05 C
ANISOU 4625 CD2 TYR A 587 7063 9344 7551 -511 -67 -612 C
ATOM 4626 CE1 TYR A 587 -8.533 8.752 -24.590 1.00 68.12 C
ANISOU 4626 CE1 TYR A 587 7769 9909 8204 -436 -8 -519 C
ATOM 4627 CE2 TYR A 587 -7.794 9.356 -22.397 1.00 67.54 C
ANISOU 4627 CE2 TYR A 587 7651 9945 8068 -476 -78 -572 C
ATOM 4628 CZ TYR A 587 -8.485 8.506 -23.235 1.00 74.27 C
ANISOU 4628 CZ TYR A 587 8533 10755 8931 -441 -48 -523 C
ATOM 4629 OH TYR A 587 -9.130 7.406 -22.716 1.00 70.99 O
ANISOU 4629 OH TYR A 587 8132 10364 8476 -411 -61 -478 O
ATOM 4630 N PHE A 588 -5.333 11.139 -27.722 1.00 71.65 N
ANISOU 4630 N PHE A 588 8117 10250 8858 -488 90 -535 N
ATOM 4631 CA PHE A 588 -5.500 10.266 -28.876 1.00 67.61 C
ANISOU 4631 CA PHE A 588 7635 9708 8347 -434 127 -489 C
ATOM 4632 C PHE A 588 -4.260 10.188 -29.757 1.00 73.21 C
ANISOU 4632 C PHE A 588 8298 10412 9105 -417 162 -454 C
ATOM 4633 O PHE A 588 -4.343 9.661 -30.871 1.00 72.30 O
ANISOU 4633 O PHE A 588 8215 10266 8991 -369 202 -423 O
ATOM 4634 CB PHE A 588 -6.692 10.727 -29.718 1.00 60.17 C
ANISOU 4634 CB PHE A 588 6761 8704 7398 -425 162 -498 C
ATOM 4635 CG PHE A 588 -8.023 10.497 -29.066 1.00 61.69 C
ANISOU 4635 CG PHE A 588 6998 8898 7543 -424 138 -514 C
ATOM 4636 CD1 PHE A 588 -8.601 9.238 -29.071 1.00 66.25 C
ANISOU 4636 CD1 PHE A 588 7604 9480 8089 -385 122 -483 C
ATOM 4637 CD2 PHE A 588 -8.706 11.540 -28.463 1.00 57.83 C
ANISOU 4637 CD2 PHE A 588 6523 8401 7047 -460 134 -558 C
ATOM 4638 CE1 PHE A 588 -9.830 9.019 -28.478 1.00 58.98 C
ANISOU 4638 CE1 PHE A 588 6716 8561 7134 -385 103 -488 C
ATOM 4639 CE2 PHE A 588 -9.936 11.329 -27.868 1.00 67.13 C
ANISOU 4639 CE2 PHE A 588 7738 9585 8184 -454 119 -567 C
ATOM 4640 CZ PHE A 588 -10.499 10.066 -27.876 1.00 62.28 C
ANISOU 4640 CZ PHE A 588 7143 8979 7542 -418 105 -528 C
ATOM 4641 N GLU A 589 -3.118 10.696 -29.295 1.00 65.03 N
ANISOU 4641 N GLU A 589 7190 9409 8111 -453 148 -460 N
ATOM 4642 CA GLU A 589 -1.921 10.670 -30.131 1.00 60.89 C
ANISOU 4642 CA GLU A 589 6611 8883 7641 -437 188 -419 C
ATOM 4643 C GLU A 589 -1.446 9.260 -30.475 1.00 70.48 C
ANISOU 4643 C GLU A 589 7818 10120 8841 -370 195 -370 C
ATOM 4644 O GLU A 589 -1.045 9.048 -31.633 1.00 79.36 O
ANISOU 4644 O GLU A 589 8946 11220 9986 -327 252 -334 O
ATOM 4645 CB GLU A 589 -0.796 11.476 -29.467 1.00 62.62 C
ANISOU 4645 CB GLU A 589 6742 9133 7917 -495 161 -432 C
ATOM 4646 CG GLU A 589 0.479 11.525 -30.300 1.00 77.39 C
ANISOU 4646 CG GLU A 589 8542 11005 9856 -482 207 -382 C
ATOM 4647 CD GLU A 589 1.428 12.626 -29.870 1.00 89.78 C
ANISOU 4647 CD GLU A 589 10027 12583 11501 -553 188 -397 C
ATOM 4648 OE1 GLU A 589 1.102 13.357 -28.910 1.00 86.02 O
ANISOU 4648 OE1 GLU A 589 9555 12109 11019 -611 134 -454 O
ATOM 4649 OE2 GLU A 589 2.499 12.763 -30.497 1.00 76.37 O
ANISOU 4649 OE2 GLU A 589 8259 10887 9870 -550 228 -351 O
ATOM 4650 N PRO A 590 -1.446 8.276 -29.566 1.00 69.70 N
ANISOU 4650 N PRO A 590 7710 10065 8707 -354 144 -363 N
ATOM 4651 CA PRO A 590 -1.063 6.916 -29.986 1.00 75.73 C
ANISOU 4651 CA PRO A 590 8475 10837 9461 -284 155 -316 C
ATOM 4652 C PRO A 590 -1.938 6.355 -31.093 1.00 72.50 C
ANISOU 4652 C PRO A 590 8151 10370 9024 -232 193 -307 C
ATOM 4653 O PRO A 590 -1.453 5.564 -31.912 1.00 70.05 O
ANISOU 4653 O PRO A 590 7847 10048 8720 -170 226 -273 O
ATOM 4654 CB PRO A 590 -1.195 6.101 -28.692 1.00 70.66 C
ANISOU 4654 CB PRO A 590 7821 10244 8781 -285 88 -314 C
ATOM 4655 CG PRO A 590 -0.989 7.089 -27.611 1.00 73.86 C
ANISOU 4655 CG PRO A 590 8183 10690 9191 -353 44 -352 C
ATOM 4656 CD PRO A 590 -1.622 8.356 -28.103 1.00 71.25 C
ANISOU 4656 CD PRO A 590 7888 10310 8873 -393 75 -393 C
ATOM 4657 N LEU A 591 -3.215 6.738 -31.144 1.00 70.15 N
ANISOU 4657 N LEU A 591 7921 10037 8696 -250 188 -338 N
ATOM 4658 CA LEU A 591 -4.077 6.297 -32.235 1.00 67.34 C
ANISOU 4658 CA LEU A 591 7645 9625 8316 -206 216 -332 C
ATOM 4659 C LEU A 591 -3.848 7.122 -33.495 1.00 72.95 C
ANISOU 4659 C LEU A 591 8370 10299 9048 -196 279 -329 C
ATOM 4660 O LEU A 591 -3.870 6.581 -34.606 1.00 74.67 O
ANISOU 4660 O LEU A 591 8633 10486 9253 -139 314 -311 O
ATOM 4661 CB LEU A 591 -5.545 6.373 -31.812 1.00 62.22 C
ANISOU 4661 CB LEU A 591 7054 8954 7632 -228 184 -359 C
ATOM 4662 CG LEU A 591 -6.563 5.992 -32.891 1.00 67.28 C
ANISOU 4662 CG LEU A 591 7776 9536 8251 -191 200 -358 C
ATOM 4663 CD1 LEU A 591 -6.455 4.515 -33.244 1.00 65.34 C
ANISOU 4663 CD1 LEU A 591 7557 9277 7992 -130 187 -331 C
ATOM 4664 CD2 LEU A 591 -7.974 6.343 -32.457 1.00 62.88 C
ANISOU 4664 CD2 LEU A 591 7259 8961 7673 -223 174 -381 C
ATOM 4665 N PHE A 592 -3.623 8.430 -33.339 1.00 73.66 N
ANISOU 4665 N PHE A 592 8425 10391 9171 -251 294 -347 N
ATOM 4666 CA PHE A 592 -3.433 9.297 -34.498 1.00 63.79 C
ANISOU 4666 CA PHE A 592 7186 9105 7946 -246 357 -336 C
ATOM 4667 C PHE A 592 -2.211 8.881 -35.308 1.00 69.36 C
ANISOU 4667 C PHE A 592 7854 9823 8676 -197 409 -290 C
ATOM 4668 O PHE A 592 -2.248 8.880 -36.544 1.00 70.23 O
ANISOU 4668 O PHE A 592 8007 9903 8775 -149 464 -269 O
ATOM 4669 CB PHE A 592 -3.311 10.753 -34.048 1.00 57.73 C
ANISOU 4669 CB PHE A 592 6379 8333 7222 -318 359 -360 C
ATOM 4670 CG PHE A 592 -3.115 11.723 -35.178 1.00 58.93 C
ANISOU 4670 CG PHE A 592 6538 8445 7407 -318 426 -341 C
ATOM 4671 CD1 PHE A 592 -4.048 11.817 -36.197 1.00 67.71 C
ANISOU 4671 CD1 PHE A 592 7730 9511 8486 -284 457 -338 C
ATOM 4672 CD2 PHE A 592 -2.005 12.550 -35.215 1.00 62.68 C
ANISOU 4672 CD2 PHE A 592 6937 8928 7950 -354 455 -322 C
ATOM 4673 CE1 PHE A 592 -3.873 12.711 -37.237 1.00 62.78 C
ANISOU 4673 CE1 PHE A 592 7114 8852 7887 -279 520 -313 C
ATOM 4674 CE2 PHE A 592 -1.825 13.447 -36.251 1.00 63.53 C
ANISOU 4674 CE2 PHE A 592 7048 8997 8092 -354 521 -295 C
ATOM 4675 CZ PHE A 592 -2.761 13.527 -37.263 1.00 63.92 C
ANISOU 4675 CZ PHE A 592 7183 9004 8100 -314 556 -289 C
ATOM 4676 N THR A 593 -1.119 8.520 -34.630 1.00 68.27 N
ANISOU 4676 N THR A 593 7636 9734 8570 -202 392 -272 N
ATOM 4677 CA THR A 593 0.051 8.026 -35.347 1.00 72.58 C
ANISOU 4677 CA THR A 593 8139 10297 9141 -148 443 -224 C
ATOM 4678 C THR A 593 -0.217 6.668 -35.982 1.00 74.17 C
ANISOU 4678 C THR A 593 8405 10483 9293 -62 452 -210 C
ATOM 4679 O THR A 593 0.313 6.373 -37.059 1.00 81.81 O
ANISOU 4679 O THR A 593 9385 11442 10259 2 515 -178 O
ATOM 4680 CB THR A 593 1.255 7.943 -34.409 1.00 54.16 C
ANISOU 4680 CB THR A 593 5698 8022 6859 -175 415 -206 C
ATOM 4681 OG1 THR A 593 0.934 7.108 -33.290 1.00 83.34 O
ANISOU 4681 OG1 THR A 593 9397 11747 10522 -179 342 -224 O
ATOM 4682 CG2 THR A 593 1.637 9.330 -33.912 1.00 57.72 C
ANISOU 4682 CG2 THR A 593 6083 8480 7368 -260 406 -222 C
ATOM 4683 N TRP A 594 -1.037 5.834 -35.338 1.00 63.73 N
ANISOU 4683 N TRP A 594 7127 9157 7930 -58 392 -233 N
ATOM 4684 CA TRP A 594 -1.380 4.542 -35.922 1.00 72.86 C
ANISOU 4684 CA TRP A 594 8352 10286 9046 18 391 -225 C
ATOM 4685 C TRP A 594 -2.335 4.704 -37.098 1.00 79.71 C
ANISOU 4685 C TRP A 594 9316 11097 9874 47 419 -242 C
ATOM 4686 O TRP A 594 -2.252 3.956 -38.079 1.00 77.65 O
ANISOU 4686 O TRP A 594 9108 10810 9585 122 448 -232 O
ATOM 4687 CB TRP A 594 -1.985 3.630 -34.854 1.00 71.76 C
ANISOU 4687 CB TRP A 594 8225 10155 8886 8 318 -237 C
ATOM 4688 CG TRP A 594 -2.377 2.279 -35.369 1.00 70.41 C
ANISOU 4688 CG TRP A 594 8123 9945 8683 78 307 -231 C
ATOM 4689 CD1 TRP A 594 -1.591 1.165 -35.432 1.00 78.51 C
ANISOU 4689 CD1 TRP A 594 9134 10980 9718 141 312 -203 C
ATOM 4690 CD2 TRP A 594 -3.654 1.898 -35.894 1.00 69.98 C
ANISOU 4690 CD2 TRP A 594 8163 9834 8592 93 286 -255 C
ATOM 4691 NE1 TRP A 594 -2.299 0.115 -35.964 1.00 75.33 N
ANISOU 4691 NE1 TRP A 594 8815 10522 9284 193 294 -213 N
ATOM 4692 CE2 TRP A 594 -3.569 0.539 -36.256 1.00 66.66 C
ANISOU 4692 CE2 TRP A 594 7784 9384 8159 162 275 -244 C
ATOM 4693 CE3 TRP A 594 -4.861 2.575 -36.093 1.00 73.55 C
ANISOU 4693 CE3 TRP A 594 8667 10254 9024 54 273 -284 C
ATOM 4694 CZ2 TRP A 594 -4.645 -0.156 -36.803 1.00 63.10 C
ANISOU 4694 CZ2 TRP A 594 7424 8872 7679 188 246 -265 C
ATOM 4695 CZ3 TRP A 594 -5.928 1.883 -36.637 1.00 70.41 C
ANISOU 4695 CZ3 TRP A 594 8353 9802 8596 81 245 -299 C
ATOM 4696 CH2 TRP A 594 -5.812 0.533 -36.988 1.00 65.65 C
ANISOU 4696 CH2 TRP A 594 7791 9170 7985 145 229 -291 C
ATOM 4697 N LEU A 595 -3.249 5.675 -37.018 1.00 76.42 N
ANISOU 4697 N LEU A 595 8926 10660 9452 -7 408 -268 N
ATOM 4698 CA LEU A 595 -4.185 5.903 -38.115 1.00 69.18 C
ANISOU 4698 CA LEU A 595 8095 9692 8497 18 427 -281 C
ATOM 4699 C LEU A 595 -3.468 6.422 -39.355 1.00 76.66 C
ANISOU 4699 C LEU A 595 9047 10633 9447 60 508 -254 C
ATOM 4700 O LEU A 595 -3.788 6.015 -40.479 1.00 85.67 O
ANISOU 4700 O LEU A 595 10264 11743 10544 123 532 -253 O
ATOM 4701 CB LEU A 595 -5.278 6.880 -37.684 1.00 62.61 C
ANISOU 4701 CB LEU A 595 7280 8843 7665 -47 400 -311 C
ATOM 4702 CG LEU A 595 -6.334 6.356 -36.709 1.00 72.60 C
ANISOU 4702 CG LEU A 595 8567 10106 8914 -76 329 -335 C
ATOM 4703 CD1 LEU A 595 -7.277 7.475 -36.296 1.00 64.96 C
ANISOU 4703 CD1 LEU A 595 7605 9126 7951 -136 316 -361 C
ATOM 4704 CD2 LEU A 595 -7.105 5.204 -37.330 1.00 69.70 C
ANISOU 4704 CD2 LEU A 595 8277 9699 8508 -23 303 -338 C
ATOM 4705 N LYS A 596 -2.500 7.324 -39.174 1.00 73.26 N
ANISOU 4705 N LYS A 596 8535 10233 9069 25 548 -230 N
ATOM 4706 CA LYS A 596 -1.764 7.855 -40.317 1.00 72.58 C
ANISOU 4706 CA LYS A 596 8441 10144 8992 63 633 -192 C
ATOM 4707 C LYS A 596 -0.978 6.759 -41.025 1.00 78.76 C
ANISOU 4707 C LYS A 596 9234 10938 9751 156 673 -164 C
ATOM 4708 O LYS A 596 -0.854 6.769 -42.256 1.00 81.02 O
ANISOU 4708 O LYS A 596 9571 11210 10004 220 737 -144 O
ATOM 4709 CB LYS A 596 -0.834 8.982 -39.867 1.00 71.47 C
ANISOU 4709 CB LYS A 596 8198 10030 8927 0 663 -168 C
ATOM 4710 CG LYS A 596 -1.556 10.259 -39.467 1.00 67.57 C
ANISOU 4710 CG LYS A 596 7706 9512 8457 -80 642 -195 C
ATOM 4711 CD LYS A 596 -0.578 11.375 -39.132 1.00 70.82 C
ANISOU 4711 CD LYS A 596 8020 9939 8952 -142 671 -172 C
ATOM 4712 CE LYS A 596 0.231 11.053 -37.886 1.00 71.65 C
ANISOU 4712 CE LYS A 596 8034 10091 9099 -181 620 -179 C
ATOM 4713 NZ LYS A 596 1.074 12.207 -37.463 1.00 75.43 N
ANISOU 4713 NZ LYS A 596 8418 10578 9664 -254 630 -167 N
ATOM 4714 N ASP A 597 -0.442 5.801 -40.265 1.00 82.67 N
ANISOU 4714 N ASP A 597 9688 11462 10261 169 639 -162 N
ATOM 4715 CA ASP A 597 0.274 4.690 -40.881 1.00 82.81 C
ANISOU 4715 CA ASP A 597 9720 11487 10259 263 675 -138 C
ATOM 4716 C ASP A 597 -0.677 3.758 -41.621 1.00 83.43 C
ANISOU 4716 C ASP A 597 9920 11516 10264 328 653 -170 C
ATOM 4717 O ASP A 597 -0.303 3.178 -42.646 1.00 91.23 O
ANISOU 4717 O ASP A 597 10955 12493 11215 417 703 -159 O
ATOM 4718 CB ASP A 597 1.065 3.923 -39.818 1.00 84.36 C
ANISOU 4718 CB ASP A 597 9835 11723 10494 259 638 -125 C
ATOM 4719 CG ASP A 597 1.802 2.719 -40.386 1.00 97.03 C
ANISOU 4719 CG ASP A 597 11453 13330 12083 362 674 -101 C
ATOM 4720 OD1 ASP A 597 1.152 1.688 -40.663 1.00101.31 O
ANISOU 4720 OD1 ASP A 597 12083 13833 12576 414 643 -128 O
ATOM 4721 OD2 ASP A 597 3.035 2.806 -40.561 1.00 93.96 O
ANISOU 4721 OD2 ASP A 597 10984 12981 11736 391 733 -55 O
ATOM 4722 N GLN A 598 -1.905 3.601 -41.123 1.00 82.64 N
ANISOU 4722 N GLN A 598 9871 11385 10143 286 578 -211 N
ATOM 4723 CA GLN A 598 -2.863 2.728 -41.791 1.00 75.78 C
ANISOU 4723 CA GLN A 598 9114 10465 9215 338 545 -243 C
ATOM 4724 C GLN A 598 -3.382 3.342 -43.083 1.00 81.32 C
ANISOU 4724 C GLN A 598 9893 11137 9868 368 585 -250 C
ATOM 4725 O GLN A 598 -3.746 2.612 -44.011 1.00 93.19 O
ANISOU 4725 O GLN A 598 11489 12605 11315 439 582 -269 O
ATOM 4726 CB GLN A 598 -4.023 2.408 -40.852 1.00 74.25 C
ANISOU 4726 CB GLN A 598 8940 10249 9023 280 455 -274 C
ATOM 4727 CG GLN A 598 -3.669 1.414 -39.766 1.00 78.23 C
ANISOU 4727 CG GLN A 598 9398 10771 9555 276 409 -266 C
ATOM 4728 CD GLN A 598 -3.406 0.029 -40.319 1.00 81.77 C
ANISOU 4728 CD GLN A 598 9900 11188 9981 363 406 -268 C
ATOM 4729 OE1 GLN A 598 -4.186 -0.490 -41.119 1.00 70.59 O
ANISOU 4729 OE1 GLN A 598 8580 9719 8524 403 386 -296 O
ATOM 4730 NE2 GLN A 598 -2.299 -0.575 -39.903 1.00 83.58 N
ANISOU 4730 NE2 GLN A 598 10068 11449 10239 396 423 -239 N
ATOM 4731 N ASN A 599 -3.421 4.671 -43.166 1.00 82.80 N
ANISOU 4731 N ASN A 599 10048 11336 10075 317 619 -235 N
ATOM 4732 CA ASN A 599 -3.945 5.368 -44.332 1.00 83.36 C
ANISOU 4732 CA ASN A 599 10188 11382 10101 341 656 -234 C
ATOM 4733 C ASN A 599 -2.856 5.762 -45.325 1.00 92.90 C
ANISOU 4733 C ASN A 599 11381 12615 11303 400 758 -187 C
ATOM 4734 O ASN A 599 -3.084 6.645 -46.160 1.00 91.43 O
ANISOU 4734 O ASN A 599 11226 12420 11094 407 804 -170 O
ATOM 4735 CB ASN A 599 -4.731 6.606 -43.891 1.00 77.93 C
ANISOU 4735 CB ASN A 599 9482 10687 9442 255 635 -242 C
ATOM 4736 CG ASN A 599 -5.852 6.272 -42.925 1.00 71.49 C
ANISOU 4736 CG ASN A 599 8680 9852 8632 201 543 -282 C
ATOM 4737 OD1 ASN A 599 -6.426 5.184 -42.975 1.00 78.28 O
ANISOU 4737 OD1 ASN A 599 9596 10687 9459 232 491 -306 O
ATOM 4738 ND2 ASN A 599 -6.169 7.208 -42.039 1.00 61.87 N
ANISOU 4738 ND2 ASN A 599 7409 8642 7455 119 525 -288 N
ATOM 4739 N LYS A 600 -1.682 5.128 -45.256 1.00 96.16 N
ANISOU 4739 N LYS A 600 11743 13060 11735 447 798 -161 N
ATOM 4740 CA LYS A 600 -0.603 5.475 -46.175 1.00 98.20 C
ANISOU 4740 CA LYS A 600 11976 13345 11991 508 904 -108 C
ATOM 4741 C LYS A 600 -0.941 5.094 -47.611 1.00109.67 C
ANISOU 4741 C LYS A 600 13547 14774 13349 608 942 -115 C
ATOM 4742 O LYS A 600 -0.488 5.758 -48.550 1.00104.19 O
ANISOU 4742 O LYS A 600 12858 14095 12635 648 1030 -72 O
ATOM 4743 CB LYS A 600 0.701 4.806 -45.736 1.00 92.30 C
ANISOU 4743 CB LYS A 600 11142 12638 11289 540 936 -77 C
ATOM 4744 CG LYS A 600 0.633 3.289 -45.645 1.00102.35 C
ANISOU 4744 CG LYS A 600 12467 13894 12525 608 892 -109 C
ATOM 4745 CD LYS A 600 1.927 2.714 -45.087 1.00 97.69 C
ANISOU 4745 CD LYS A 600 11779 13347 11991 633 920 -72 C
ATOM 4746 CE LYS A 600 1.809 1.219 -44.833 1.00101.38 C
ANISOU 4746 CE LYS A 600 12294 13791 12435 692 868 -104 C
ATOM 4747 NZ LYS A 600 0.785 0.905 -43.797 1.00 98.03 N
ANISOU 4747 NZ LYS A 600 11887 13339 12020 618 758 -148 N
ATOM 4748 N ASN A 601 -1.730 4.037 -47.804 1.00124.55 N
ANISOU 4748 N ASN A 601 15529 16621 15175 650 876 -169 N
ATOM 4749 CA ASN A 601 -2.186 3.624 -49.125 1.00128.59 C
ANISOU 4749 CA ASN A 601 16166 17105 15589 743 891 -190 C
ATOM 4750 C ASN A 601 -3.687 3.843 -49.297 1.00126.31 C
ANISOU 4750 C ASN A 601 15961 16770 15259 705 810 -236 C
ATOM 4751 O ASN A 601 -4.351 3.106 -50.029 1.00129.50 O
ANISOU 4751 O ASN A 601 16476 17137 15590 765 769 -278 O
ATOM 4752 CB ASN A 601 -1.819 2.164 -49.386 1.00129.08 C
ANISOU 4752 CB ASN A 601 16281 17152 15613 836 882 -218 C
ATOM 4753 CG ASN A 601 -2.156 1.256 -48.218 1.00145.00 C
ANISOU 4753 CG ASN A 601 18273 19145 17675 790 787 -253 C
ATOM 4754 OD1 ASN A 601 -3.027 1.565 -47.404 1.00144.23 O
ANISOU 4754 OD1 ASN A 601 18157 19032 17611 699 713 -272 O
ATOM 4755 ND2 ASN A 601 -1.460 0.129 -48.127 1.00134.95 N
ANISOU 4755 ND2 ASN A 601 16998 17870 16405 856 794 -257 N
ATOM 4756 N SER A 602 -4.230 4.854 -48.623 1.00 98.04 N
ANISOU 4756 N SER A 602 12329 13190 11730 606 783 -229 N
ATOM 4757 CA SER A 602 -5.636 5.208 -48.726 1.00 84.92 C
ANISOU 4757 CA SER A 602 10732 11491 10044 566 712 -262 C
ATOM 4758 C SER A 602 -5.763 6.711 -48.923 1.00 82.92 C
ANISOU 4758 C SER A 602 10446 11249 9811 518 759 -225 C
ATOM 4759 O SER A 602 -4.839 7.477 -48.635 1.00 88.88 O
ANISOU 4759 O SER A 602 11113 12036 10622 489 827 -179 O
ATOM 4760 CB SER A 602 -6.424 4.771 -47.482 1.00 93.06 C
ANISOU 4760 CB SER A 602 11735 12502 11122 490 614 -299 C
ATOM 4761 OG SER A 602 -6.328 3.373 -47.280 1.00106.59 O
ANISOU 4761 OG SER A 602 13478 14199 12824 531 569 -328 O
ATOM 4762 N PHE A 603 -6.924 7.127 -49.420 1.00 76.90 N
ANISOU 4762 N PHE A 603 9754 10456 9009 510 718 -243 N
ATOM 4763 CA PHE A 603 -7.201 8.537 -49.662 1.00 70.32 C
ANISOU 4763 CA PHE A 603 8902 9623 8193 470 756 -208 C
ATOM 4764 C PHE A 603 -7.773 9.165 -48.397 1.00 78.40 C
ANISOU 4764 C PHE A 603 9857 10637 9296 363 704 -223 C
ATOM 4765 O PHE A 603 -8.800 8.712 -47.881 1.00 75.99 O
ANISOU 4765 O PHE A 603 9576 10307 8989 332 618 -266 O
ATOM 4766 CB PHE A 603 -8.167 8.706 -50.834 1.00 70.28 C
ANISOU 4766 CB PHE A 603 9006 9592 8105 519 737 -217 C
ATOM 4767 CG PHE A 603 -8.425 10.137 -51.204 1.00 68.83 C
ANISOU 4767 CG PHE A 603 8810 9406 7935 489 782 -173 C
ATOM 4768 CD1 PHE A 603 -7.521 10.837 -51.986 1.00 69.97 C
ANISOU 4768 CD1 PHE A 603 8943 9575 8069 530 888 -111 C
ATOM 4769 CD2 PHE A 603 -9.571 10.784 -50.770 1.00 69.70 C
ANISOU 4769 CD2 PHE A 603 8920 9488 8074 424 721 -190 C
ATOM 4770 CE1 PHE A 603 -7.753 12.155 -52.327 1.00 73.47 C
ANISOU 4770 CE1 PHE A 603 9374 10009 8532 503 930 -64 C
ATOM 4771 CE2 PHE A 603 -9.808 12.103 -51.108 1.00 70.31 C
ANISOU 4771 CE2 PHE A 603 8988 9557 8170 401 763 -148 C
ATOM 4772 CZ PHE A 603 -8.897 12.789 -51.886 1.00 70.66 C
ANISOU 4772 CZ PHE A 603 9022 9621 8205 439 865 -86 C
ATOM 4773 N VAL A 604 -7.106 10.202 -47.900 1.00 77.34 N
ANISOU 4773 N VAL A 604 9635 10521 9230 308 757 -188 N
ATOM 4774 CA VAL A 604 -7.539 10.932 -46.713 1.00 62.73 C
ANISOU 4774 CA VAL A 604 7720 8662 7451 211 718 -203 C
ATOM 4775 C VAL A 604 -8.244 12.203 -47.166 1.00 65.32 C
ANISOU 4775 C VAL A 604 8070 8964 7785 187 735 -185 C
ATOM 4776 O VAL A 604 -7.713 12.960 -47.989 1.00 82.47 O
ANISOU 4776 O VAL A 604 10242 11138 9955 212 812 -136 O
ATOM 4777 CB VAL A 604 -6.353 11.252 -45.787 1.00 68.67 C
ANISOU 4777 CB VAL A 604 8362 9447 8282 162 752 -184 C
ATOM 4778 CG1 VAL A 604 -6.838 11.938 -44.521 1.00 67.18 C
ANISOU 4778 CG1 VAL A 604 8119 9250 8155 68 703 -212 C
ATOM 4779 CG2 VAL A 604 -5.589 9.980 -45.453 1.00 67.69 C
ANISOU 4779 CG2 VAL A 604 8217 9351 8150 198 741 -192 C
ATOM 4780 N GLY A 605 -9.430 12.441 -46.626 1.00 68.34 N
ANISOU 4780 N GLY A 605 8468 9320 8176 141 669 -219 N
ATOM 4781 CA GLY A 605 -10.309 13.494 -47.092 1.00 71.85 C
ANISOU 4781 CA GLY A 605 8946 9735 8620 128 672 -206 C
ATOM 4782 C GLY A 605 -11.534 12.910 -47.773 1.00 73.03 C
ANISOU 4782 C GLY A 605 9186 9862 8699 172 610 -229 C
ATOM 4783 O GLY A 605 -11.710 11.694 -47.870 1.00 72.48 O
ANISOU 4783 O GLY A 605 9157 9796 8587 207 562 -258 O
ATOM 4784 N TRP A 606 -12.391 13.807 -48.253 1.00 73.52 N
ANISOU 4784 N TRP A 606 9280 9898 8755 168 608 -214 N
ATOM 4785 CA TRP A 606 -13.620 13.369 -48.895 1.00 82.20 C
ANISOU 4785 CA TRP A 606 10460 10977 9796 203 541 -234 C
ATOM 4786 C TRP A 606 -14.056 14.380 -49.943 1.00 85.19 C
ANISOU 4786 C TRP A 606 10884 11338 10146 233 573 -193 C
ATOM 4787 O TRP A 606 -13.819 15.584 -49.810 1.00 82.58 O
ANISOU 4787 O TRP A 606 10512 10998 9866 200 628 -159 O
ATOM 4788 CB TRP A 606 -14.744 13.155 -47.873 1.00 73.46 C
ANISOU 4788 CB TRP A 606 9331 9853 8726 147 459 -273 C
ATOM 4789 CG TRP A 606 -14.973 14.328 -46.974 1.00 74.15 C
ANISOU 4789 CG TRP A 606 9354 9931 8887 78 476 -268 C
ATOM 4790 CD1 TRP A 606 -15.678 15.460 -47.265 1.00 76.81 C
ANISOU 4790 CD1 TRP A 606 9701 10243 9242 68 488 -248 C
ATOM 4791 CD2 TRP A 606 -14.504 14.482 -45.630 1.00 76.44 C
ANISOU 4791 CD2 TRP A 606 9566 10235 9241 15 482 -287 C
ATOM 4792 NE1 TRP A 606 -15.672 16.311 -46.186 1.00 76.36 N
ANISOU 4792 NE1 TRP A 606 9578 10177 9257 2 503 -257 N
ATOM 4793 CE2 TRP A 606 -14.958 15.733 -45.170 1.00 75.04 C
ANISOU 4793 CE2 TRP A 606 9358 10036 9116 -31 497 -283 C
ATOM 4794 CE3 TRP A 606 -13.742 13.683 -44.772 1.00 68.93 C
ANISOU 4794 CE3 TRP A 606 8571 9314 8307 -4 473 -308 C
ATOM 4795 CZ2 TRP A 606 -14.675 16.204 -43.890 1.00 69.82 C
ANISOU 4795 CZ2 TRP A 606 8629 9383 8517 -95 501 -306 C
ATOM 4796 CZ3 TRP A 606 -13.463 14.152 -43.503 1.00 68.66 C
ANISOU 4796 CZ3 TRP A 606 8464 9290 8331 -68 476 -324 C
ATOM 4797 CH2 TRP A 606 -13.928 15.401 -43.074 1.00 67.24 C
ANISOU 4797 CH2 TRP A 606 8261 9089 8197 -113 488 -327 C
ATOM 4798 N SER A 607 -14.697 13.867 -50.989 1.00 82.41 N
ANISOU 4798 N SER A 607 10620 10979 9713 296 534 -198 N
ATOM 4799 CA SER A 607 -15.311 14.693 -52.016 1.00 81.64 C
ANISOU 4799 CA SER A 607 10576 10867 9575 331 545 -161 C
ATOM 4800 C SER A 607 -16.788 14.877 -51.692 1.00 76.50 C
ANISOU 4800 C SER A 607 9933 10189 8946 298 460 -184 C
ATOM 4801 O SER A 607 -17.494 13.903 -51.412 1.00 74.16 O
ANISOU 4801 O SER A 607 9654 9886 8637 293 374 -228 O
ATOM 4802 CB SER A 607 -15.143 14.054 -53.394 1.00 71.29 C
ANISOU 4802 CB SER A 607 9362 9571 8155 426 549 -154 C
ATOM 4803 OG SER A 607 -15.886 14.758 -54.371 1.00 92.95 O
ANISOU 4803 OG SER A 607 12164 12302 10850 463 543 -121 O
ATOM 4804 N THR A 608 -17.251 16.124 -51.733 1.00 75.74 N
ANISOU 4804 N THR A 608 9819 10073 8886 276 485 -149 N
ATOM 4805 CA THR A 608 -18.611 16.444 -51.326 1.00 74.99 C
ANISOU 4805 CA THR A 608 9715 9952 8824 242 416 -163 C
ATOM 4806 C THR A 608 -19.639 16.255 -52.434 1.00 82.09 C
ANISOU 4806 C THR A 608 10694 10843 9653 298 353 -155 C
ATOM 4807 O THR A 608 -20.841 16.301 -52.150 1.00 81.82 O
ANISOU 4807 O THR A 608 10653 10791 9644 276 282 -169 O
ATOM 4808 CB THR A 608 -18.685 17.887 -50.814 1.00 71.09 C
ANISOU 4808 CB THR A 608 9166 9436 8408 196 468 -133 C
ATOM 4809 OG1 THR A 608 -18.367 18.791 -51.878 1.00 84.09 O
ANISOU 4809 OG1 THR A 608 10846 11074 10028 238 532 -73 O
ATOM 4810 CG2 THR A 608 -17.704 18.095 -49.671 1.00 80.50 C
ANISOU 4810 CG2 THR A 608 10280 10635 9673 136 517 -148 C
ATOM 4811 N ASP A 609 -19.212 16.042 -53.679 1.00 86.48 N
ANISOU 4811 N ASP A 609 11324 11414 10119 372 375 -133 N
ATOM 4812 CA ASP A 609 -20.160 15.900 -54.776 1.00 89.69 C
ANISOU 4812 CA ASP A 609 11812 11815 10449 428 309 -127 C
ATOM 4813 C ASP A 609 -20.675 14.477 -54.945 1.00 88.16 C
ANISOU 4813 C ASP A 609 11669 11622 10206 449 206 -186 C
ATOM 4814 O ASP A 609 -21.729 14.287 -55.563 1.00 96.26 O
ANISOU 4814 O ASP A 609 12745 12636 11191 474 120 -194 O
ATOM 4815 CB ASP A 609 -19.533 16.374 -56.092 1.00 94.55 C
ANISOU 4815 CB ASP A 609 12495 12450 10981 506 379 -74 C
ATOM 4816 CG ASP A 609 -18.443 15.447 -56.592 1.00 93.02 C
ANISOU 4816 CG ASP A 609 12345 12285 10714 561 415 -89 C
ATOM 4817 OD1 ASP A 609 -17.672 14.929 -55.758 1.00104.77 O
ANISOU 4817 OD1 ASP A 609 13780 13779 12248 526 441 -116 O
ATOM 4818 OD2 ASP A 609 -18.360 15.237 -57.822 1.00 82.81 O
ANISOU 4818 OD2 ASP A 609 11142 11009 9314 644 419 -74 O
ATOM 4819 N TRP A 610 -19.970 13.481 -54.417 1.00 77.24 N
ANISOU 4819 N TRP A 610 10271 10247 8828 438 207 -226 N
ATOM 4820 CA TRP A 610 -20.445 12.108 -54.507 1.00 77.10 C
ANISOU 4820 CA TRP A 610 10299 10219 8777 453 107 -283 C
ATOM 4821 C TRP A 610 -21.612 11.884 -53.552 1.00 81.60 C
ANISOU 4821 C TRP A 610 10814 10765 9425 384 20 -306 C
ATOM 4822 O TRP A 610 -21.641 12.423 -52.442 1.00 81.22 O
ANISOU 4822 O TRP A 610 10681 10716 9462 319 51 -296 O
ATOM 4823 CB TRP A 610 -19.318 11.124 -54.190 1.00 74.45 C
ANISOU 4823 CB TRP A 610 9961 9896 8431 465 140 -312 C
ATOM 4824 CG TRP A 610 -19.756 9.685 -54.209 1.00 70.75 C
ANISOU 4824 CG TRP A 610 9537 9406 7940 476 39 -372 C
ATOM 4825 CD1 TRP A 610 -19.716 8.831 -55.272 1.00 70.07 C
ANISOU 4825 CD1 TRP A 610 9552 9314 7759 551 -5 -404 C
ATOM 4826 CD2 TRP A 610 -20.305 8.937 -53.115 1.00 70.96 C
ANISOU 4826 CD2 TRP A 610 9511 9411 8041 412 -32 -405 C
ATOM 4827 NE1 TRP A 610 -20.203 7.599 -54.908 1.00 71.21 N
ANISOU 4827 NE1 TRP A 610 9709 9426 7922 533 -102 -458 N
ATOM 4828 CE2 TRP A 610 -20.573 7.638 -53.590 1.00 62.65 C
ANISOU 4828 CE2 TRP A 610 8528 8333 6943 447 -118 -454 C
ATOM 4829 CE3 TRP A 610 -20.597 9.241 -51.781 1.00 76.82 C
ANISOU 4829 CE3 TRP A 610 10155 10152 8880 331 -29 -397 C
ATOM 4830 CZ2 TRP A 610 -21.116 6.643 -52.779 1.00 61.70 C
ANISOU 4830 CZ2 TRP A 610 8378 8183 6882 399 -199 -488 C
ATOM 4831 CZ3 TRP A 610 -21.137 8.251 -50.977 1.00 77.04 C
ANISOU 4831 CZ3 TRP A 610 10155 10158 8957 289 -104 -428 C
ATOM 4832 CH2 TRP A 610 -21.390 6.969 -51.479 1.00 71.13 C
ANISOU 4832 CH2 TRP A 610 9473 9382 8172 321 -188 -470 C
ATOM 4833 N SER A 611 -22.575 11.078 -53.992 1.00 72.57 N
ANISOU 4833 N SER A 611 9720 9601 8252 398 -90 -338 N
ATOM 4834 CA SER A 611 -23.719 10.702 -53.176 1.00 75.53 C
ANISOU 4834 CA SER A 611 10045 9953 8701 338 -178 -356 C
ATOM 4835 C SER A 611 -24.132 9.292 -53.560 1.00 78.07 C
ANISOU 4835 C SER A 611 10424 10250 8989 356 -286 -406 C
ATOM 4836 O SER A 611 -23.969 8.897 -54.720 1.00 74.97 O
ANISOU 4836 O SER A 611 10126 9856 8505 424 -314 -425 O
ATOM 4837 CB SER A 611 -24.895 11.672 -53.363 1.00 73.87 C
ANISOU 4837 CB SER A 611 9816 9734 8517 325 -210 -322 C
ATOM 4838 OG SER A 611 -25.377 11.643 -54.694 1.00 80.35 O
ANISOU 4838 OG SER A 611 10724 10552 9255 386 -268 -319 O
ATOM 4839 N PRO A 612 -24.662 8.507 -52.616 1.00 82.08 N
ANISOU 4839 N PRO A 612 10880 10737 9570 300 -347 -429 N
ATOM 4840 CA PRO A 612 -25.076 7.135 -52.949 1.00 84.02 C
ANISOU 4840 CA PRO A 612 11178 10948 9798 311 -456 -476 C
ATOM 4841 C PRO A 612 -26.278 7.063 -53.877 1.00 78.61 C
ANISOU 4841 C PRO A 612 10544 10240 9083 329 -567 -484 C
ATOM 4842 O PRO A 612 -26.611 5.963 -54.339 1.00 89.57 O
ANISOU 4842 O PRO A 612 11990 11594 10449 345 -666 -529 O
ATOM 4843 CB PRO A 612 -25.394 6.520 -51.579 1.00 83.24 C
ANISOU 4843 CB PRO A 612 10992 10834 9799 236 -480 -480 C
ATOM 4844 CG PRO A 612 -25.710 7.683 -50.708 1.00 71.44 C
ANISOU 4844 CG PRO A 612 9408 9364 8370 188 -421 -436 C
ATOM 4845 CD PRO A 612 -24.848 8.812 -51.187 1.00 73.77 C
ANISOU 4845 CD PRO A 612 9722 9691 8616 225 -317 -411 C
ATOM 4846 N TYR A 613 -26.938 8.185 -54.163 1.00 77.37 N
ANISOU 4846 N TYR A 613 10370 10098 8931 329 -560 -443 N
ATOM 4847 CA TYR A 613 -28.041 8.224 -55.114 1.00 83.82 C
ANISOU 4847 CA TYR A 613 11234 10899 9714 353 -665 -445 C
ATOM 4848 C TYR A 613 -27.672 8.953 -56.400 1.00 91.56 C
ANISOU 4848 C TYR A 613 12301 11905 10584 433 -629 -428 C
ATOM 4849 O TYR A 613 -28.555 9.231 -57.219 1.00 93.02 O
ANISOU 4849 O TYR A 613 12523 12086 10733 458 -706 -418 O
ATOM 4850 CB TYR A 613 -29.273 8.872 -54.474 1.00 78.76 C
ANISOU 4850 CB TYR A 613 10503 10255 9169 295 -700 -405 C
ATOM 4851 CG TYR A 613 -29.063 10.302 -54.019 1.00 89.43 C
ANISOU 4851 CG TYR A 613 11795 11634 10551 285 -588 -351 C
ATOM 4852 CD1 TYR A 613 -29.283 11.367 -54.884 1.00 88.96 C
ANISOU 4852 CD1 TYR A 613 11769 11589 10445 329 -568 -313 C
ATOM 4853 CD2 TYR A 613 -28.655 10.586 -52.722 1.00 84.64 C
ANISOU 4853 CD2 TYR A 613 11102 11037 10020 232 -507 -339 C
ATOM 4854 CE1 TYR A 613 -29.095 12.673 -54.472 1.00 89.72 C
ANISOU 4854 CE1 TYR A 613 11812 11700 10576 319 -468 -265 C
ATOM 4855 CE2 TYR A 613 -28.466 11.889 -52.302 1.00 79.78 C
ANISOU 4855 CE2 TYR A 613 10437 10439 9435 221 -412 -299 C
ATOM 4856 CZ TYR A 613 -28.687 12.928 -53.180 1.00 82.74 C
ANISOU 4856 CZ TYR A 613 10846 10821 9772 264 -392 -262 C
ATOM 4857 OH TYR A 613 -28.499 14.226 -52.765 1.00 83.82 O
ANISOU 4857 OH TYR A 613 10936 10964 9947 252 -299 -222 O
ATOM 4858 N ALA A 614 -26.395 9.267 -56.596 1.00 91.27 N
ANISOU 4858 N ALA A 614 12292 11894 10491 474 -515 -418 N
ATOM 4859 CA ALA A 614 -25.944 9.985 -57.784 1.00 89.17 C
ANISOU 4859 CA ALA A 614 12104 11656 10120 552 -463 -391 C
ATOM 4860 C ALA A 614 -26.161 9.160 -59.049 1.00100.12 C
ANISOU 4860 C ALA A 614 13614 13035 11394 624 -557 -436 C
ATOM 4861 O ALA A 614 -26.521 9.697 -60.097 1.00108.39 O
ANISOU 4861 O ALA A 614 14725 14098 12360 680 -579 -414 O
ATOM 4862 CB ALA A 614 -24.476 10.367 -57.646 1.00 75.45 C
ANISOU 4862 CB ALA A 614 10360 9947 8360 575 -319 -369 C
TER 4863 ALA A 614
ATOM 4864 N ASN B 334 -36.714 17.002 47.557 1.00121.28 N
ANISOU 4864 N ASN B 334 16299 15975 13805 3188 1165 1656 N
ATOM 4865 CA ASN B 334 -37.388 17.532 46.378 1.00128.94 C
ANISOU 4865 CA ASN B 334 17160 16955 14878 2975 1192 1522 C
ATOM 4866 C ASN B 334 -36.472 17.475 45.160 1.00140.30 C
ANISOU 4866 C ASN B 334 18570 18332 16407 3013 1115 1289 C
ATOM 4867 O ASN B 334 -35.410 18.096 45.142 1.00146.44 O
ANISOU 4867 O ASN B 334 19270 19253 17116 3169 1052 1141 O
ATOM 4868 CB ASN B 334 -37.850 18.970 46.626 1.00126.22 C
ANISOU 4868 CB ASN B 334 16638 16884 14437 2909 1228 1477 C
ATOM 4869 CG ASN B 334 -39.290 19.199 46.210 1.00136.51 C
ANISOU 4869 CG ASN B 334 17886 18164 15818 2649 1308 1529 C
ATOM 4870 OD1 ASN B 334 -40.068 18.253 46.080 1.00140.36 O
ANISOU 4870 OD1 ASN B 334 18479 18448 16402 2523 1355 1652 O
ATOM 4871 ND2 ASN B 334 -39.653 20.459 46.001 1.00141.04 N
ANISOU 4871 ND2 ASN B 334 18289 18941 16358 2567 1321 1434 N
ATOM 4872 N LEU B 335 -36.887 16.724 44.143 1.00129.34 N
ANISOU 4872 N LEU B 335 17242 16730 15172 2866 1122 1251 N
ATOM 4873 CA LEU B 335 -36.111 16.580 42.920 1.00112.07 C
ANISOU 4873 CA LEU B 335 15037 14468 13076 2877 1061 1029 C
ATOM 4874 C LEU B 335 -36.499 17.665 41.924 1.00107.41 C
ANISOU 4874 C LEU B 335 14293 14020 12499 2709 1068 866 C
ATOM 4875 O LEU B 335 -37.682 17.969 41.748 1.00107.39 O
ANISOU 4875 O LEU B 335 14247 14030 12525 2511 1123 933 O
ATOM 4876 CB LEU B 335 -36.320 15.195 42.299 1.00106.61 C
ANISOU 4876 CB LEU B 335 14492 13472 12542 2806 1062 1058 C
ATOM 4877 CG LEU B 335 -35.705 13.979 43.003 1.00109.40 C
ANISOU 4877 CG LEU B 335 15011 13638 12920 2986 1032 1177 C
ATOM 4878 CD1 LEU B 335 -36.511 13.555 44.227 1.00117.67 C
ANISOU 4878 CD1 LEU B 335 16154 14644 13913 2973 1092 1455 C
ATOM 4879 CD2 LEU B 335 -35.560 12.820 42.029 1.00106.33 C
ANISOU 4879 CD2 LEU B 335 14727 12971 12705 2936 1010 1100 C
ATOM 4880 N CYS B 336 -35.494 18.250 41.278 1.00109.85 N
ANISOU 4880 N CYS B 336 14519 14432 12788 2790 1010 651 N
ATOM 4881 CA CYS B 336 -35.749 19.334 40.339 1.00111.87 C
ANISOU 4881 CA CYS B 336 14634 14830 13044 2643 1008 494 C
ATOM 4882 C CYS B 336 -36.455 18.798 39.095 1.00102.86 C
ANISOU 4882 C CYS B 336 13531 13512 12040 2425 1020 440 C
ATOM 4883 O CYS B 336 -36.092 17.734 38.582 1.00100.43 O
ANISOU 4883 O CYS B 336 13333 13000 11827 2442 1002 398 O
ATOM 4884 CB CYS B 336 -34.443 20.025 39.945 1.00109.44 C
ANISOU 4884 CB CYS B 336 14237 14665 12681 2782 949 278 C
ATOM 4885 SG CYS B 336 -33.553 20.810 41.317 1.00145.63 S
ANISOU 4885 SG CYS B 336 18750 19484 17100 3034 925 305 S
ATOM 4886 N PRO B 337 -37.460 19.509 38.580 1.00 94.73 N
ANISOU 4886 N PRO B 337 12412 12553 11027 2219 1045 435 N
ATOM 4887 CA PRO B 337 -38.254 18.980 37.456 1.00 99.33 C
ANISOU 4887 CA PRO B 337 13034 12970 11737 2000 1053 400 C
ATOM 4888 C PRO B 337 -37.522 19.061 36.118 1.00110.86 C
ANISOU 4888 C PRO B 337 14475 14411 13235 1967 1002 166 C
ATOM 4889 O PRO B 337 -37.953 19.741 35.184 1.00105.34 O
ANISOU 4889 O PRO B 337 13695 13779 12549 1801 989 65 O
ATOM 4890 CB PRO B 337 -39.503 19.870 37.491 1.00102.06 C
ANISOU 4890 CB PRO B 337 13272 13434 12073 1818 1088 473 C
ATOM 4891 CG PRO B 337 -39.008 21.170 38.021 1.00 89.08 C
ANISOU 4891 CG PRO B 337 11495 12050 10301 1927 1073 425 C
ATOM 4892 CD PRO B 337 -37.953 20.821 39.039 1.00 96.62 C
ANISOU 4892 CD PRO B 337 12508 13027 11175 2178 1064 464 C
ATOM 4893 N PHE B 338 -36.400 18.344 36.013 1.00109.40 N
ANISOU 4893 N PHE B 338 14368 14131 13069 2124 972 75 N
ATOM 4894 CA PHE B 338 -35.676 18.310 34.745 1.00 96.48 C
ANISOU 4894 CA PHE B 338 12722 12465 11473 2091 934 -155 C
ATOM 4895 C PHE B 338 -36.409 17.481 33.699 1.00 98.02 C
ANISOU 4895 C PHE B 338 12994 12455 11795 1890 943 -182 C
ATOM 4896 O PHE B 338 -36.207 17.687 32.497 1.00 98.41 O
ANISOU 4896 O PHE B 338 13015 12511 11867 1782 920 -363 O
ATOM 4897 CB PHE B 338 -34.265 17.765 34.955 1.00105.13 C
ANISOU 4897 CB PHE B 338 13868 13516 12563 2322 901 -255 C
ATOM 4898 CG PHE B 338 -33.295 18.782 35.478 1.00107.06 C
ANISOU 4898 CG PHE B 338 14004 13991 12684 2495 876 -333 C
ATOM 4899 CD1 PHE B 338 -33.295 20.076 34.988 1.00 99.11 C
ANISOU 4899 CD1 PHE B 338 12860 13192 11604 2412 869 -445 C
ATOM 4900 CD2 PHE B 338 -32.386 18.445 36.467 1.00109.41 C
ANISOU 4900 CD2 PHE B 338 14336 14295 12942 2740 853 -293 C
ATOM 4901 CE1 PHE B 338 -32.401 21.013 35.469 1.00 94.31 C
ANISOU 4901 CE1 PHE B 338 12150 12792 10890 2567 848 -523 C
ATOM 4902 CE2 PHE B 338 -31.492 19.378 36.953 1.00101.79 C
ANISOU 4902 CE2 PHE B 338 13266 13544 11866 2898 827 -372 C
ATOM 4903 CZ PHE B 338 -31.500 20.664 36.454 1.00 95.42 C
ANISOU 4903 CZ PHE B 338 12321 12942 10992 2809 828 -490 C
ATOM 4904 N HIS B 339 -37.253 16.542 34.133 1.00104.17 N
ANISOU 4904 N HIS B 339 13872 13052 12655 1832 978 -7 N
ATOM 4905 CA HIS B 339 -38.025 15.744 33.186 1.00107.74 C
ANISOU 4905 CA HIS B 339 14395 13307 13236 1632 988 -28 C
ATOM 4906 C HIS B 339 -38.993 16.609 32.389 1.00116.79 C
ANISOU 4906 C HIS B 339 15442 14556 14377 1400 985 -67 C
ATOM 4907 O HIS B 339 -39.256 16.328 31.214 1.00112.51 O
ANISOU 4907 O HIS B 339 14920 13924 13905 1241 967 -185 O
ATOM 4908 CB HIS B 339 -38.778 14.640 33.929 1.00107.88 C
ANISOU 4908 CB HIS B 339 14531 13119 13340 1616 1032 184 C
ATOM 4909 CG HIS B 339 -39.481 13.670 33.029 1.00126.05 C
ANISOU 4909 CG HIS B 339 16914 15191 15786 1431 1042 162 C
ATOM 4910 ND1 HIS B 339 -40.663 13.973 32.387 1.00150.11 N
ANISOU 4910 ND1 HIS B 339 19912 18244 18877 1190 1054 174 N
ATOM 4911 CD2 HIS B 339 -39.176 12.400 32.675 1.00114.63 C
ANISOU 4911 CD2 HIS B 339 15595 13501 14458 1453 1038 126 C
ATOM 4912 CE1 HIS B 339 -41.050 12.934 31.669 1.00131.31 C
ANISOU 4912 CE1 HIS B 339 17625 15638 16630 1068 1058 142 C
ATOM 4913 NE2 HIS B 339 -40.166 11.966 31.826 1.00126.94 N
ANISOU 4913 NE2 HIS B 339 17179 14927 16124 1223 1051 112 N
ATOM 4914 N GLU B 340 -39.525 17.667 33.005 1.00112.23 N
ANISOU 4914 N GLU B 340 14757 14168 13717 1380 998 26 N
ATOM 4915 CA GLU B 340 -40.456 18.544 32.303 1.00104.74 C
ANISOU 4915 CA GLU B 340 13708 13321 12770 1169 985 -4 C
ATOM 4916 C GLU B 340 -39.767 19.325 31.191 1.00100.09 C
ANISOU 4916 C GLU B 340 13048 12852 12128 1135 932 -223 C
ATOM 4917 O GLU B 340 -40.406 19.674 30.193 1.00113.23 O
ANISOU 4917 O GLU B 340 14675 14526 13823 938 905 -291 O
ATOM 4918 CB GLU B 340 -41.116 19.507 33.290 1.00103.96 C
ANISOU 4918 CB GLU B 340 13504 13397 12601 1175 1012 140 C
ATOM 4919 CG GLU B 340 -41.775 18.830 34.481 1.00101.72 C
ANISOU 4919 CG GLU B 340 13283 13020 12345 1210 1075 362 C
ATOM 4920 CD GLU B 340 -42.383 19.826 35.451 1.00104.67 C
ANISOU 4920 CD GLU B 340 13545 13584 12643 1217 1108 484 C
ATOM 4921 OE1 GLU B 340 -42.402 21.034 35.133 1.00103.43 O
ANISOU 4921 OE1 GLU B 340 13256 13612 12429 1178 1077 398 O
ATOM 4922 OE2 GLU B 340 -42.840 19.401 36.533 1.00106.26 O
ANISOU 4922 OE2 GLU B 340 13789 13744 12840 1259 1167 665 O
ATOM 4923 N VAL B 341 -38.472 19.601 31.340 1.00 96.52 N
ANISOU 4923 N VAL B 341 12581 12493 11600 1320 915 -336 N
ATOM 4924 CA VAL B 341 -37.761 20.416 30.361 1.00 92.66 C
ANISOU 4924 CA VAL B 341 12021 12136 11051 1291 874 -543 C
ATOM 4925 C VAL B 341 -37.251 19.559 29.210 1.00 87.76 C
ANISOU 4925 C VAL B 341 11488 11362 10495 1239 859 -711 C
ATOM 4926 O VAL B 341 -37.450 19.887 28.035 1.00 89.35 O
ANISOU 4926 O VAL B 341 11667 11585 10697 1071 832 -837 O
ATOM 4927 CB VAL B 341 -36.613 21.183 31.043 1.00 84.74 C
ANISOU 4927 CB VAL B 341 10945 11316 9937 1505 867 -599 C
ATOM 4928 CG1 VAL B 341 -35.824 21.984 30.018 1.00 91.19 C
ANISOU 4928 CG1 VAL B 341 11693 12261 10695 1473 833 -817 C
ATOM 4929 CG2 VAL B 341 -37.155 22.091 32.137 1.00 75.82 C
ANISOU 4929 CG2 VAL B 341 9721 10347 8739 1544 883 -446 C
ATOM 4930 N PHE B 342 -36.590 18.447 29.527 1.00 80.67 N
ANISOU 4930 N PHE B 342 10691 10306 9652 1381 873 -717 N
ATOM 4931 CA PHE B 342 -35.955 17.647 28.487 1.00 87.22 C
ANISOU 4931 CA PHE B 342 11596 10999 10545 1357 862 -900 C
ATOM 4932 C PHE B 342 -36.960 16.774 27.746 1.00 92.30 C
ANISOU 4932 C PHE B 342 12323 11444 11304 1153 868 -874 C
ATOM 4933 O PHE B 342 -36.874 16.632 26.521 1.00 93.13 O
ANISOU 4933 O PHE B 342 12445 11508 11432 1021 850 -1041 O
ATOM 4934 CB PHE B 342 -34.844 16.792 29.095 1.00 82.73 C
ANISOU 4934 CB PHE B 342 11098 10330 10006 1594 868 -926 C
ATOM 4935 CG PHE B 342 -33.635 17.582 29.493 1.00 81.42 C
ANISOU 4935 CG PHE B 342 10848 10352 9736 1786 853 -1024 C
ATOM 4936 CD1 PHE B 342 -33.649 18.368 30.633 1.00 90.68 C
ANISOU 4936 CD1 PHE B 342 11949 11687 10819 1902 855 -894 C
ATOM 4937 CD2 PHE B 342 -32.487 17.549 28.720 1.00 82.80 C
ANISOU 4937 CD2 PHE B 342 11011 10546 9903 1845 840 -1256 C
ATOM 4938 CE1 PHE B 342 -32.541 19.103 30.998 1.00 87.53 C
ANISOU 4938 CE1 PHE B 342 11468 11463 10328 2075 839 -991 C
ATOM 4939 CE2 PHE B 342 -31.375 18.281 29.080 1.00 94.47 C
ANISOU 4939 CE2 PHE B 342 12404 12198 11292 2017 828 -1354 C
ATOM 4940 CZ PHE B 342 -31.402 19.058 30.222 1.00 93.03 C
ANISOU 4940 CZ PHE B 342 12150 12173 11023 2133 825 -1220 C
ATOM 4941 N ASN B 343 -37.919 16.189 28.460 1.00 89.98 N
ANISOU 4941 N ASN B 343 12081 11028 11081 1117 894 -672 N
ATOM 4942 CA ASN B 343 -38.884 15.270 27.862 1.00 85.10 C
ANISOU 4942 CA ASN B 343 11544 10204 10587 932 903 -638 C
ATOM 4943 C ASN B 343 -40.197 15.956 27.511 1.00 77.53 C
ANISOU 4943 C ASN B 343 10513 9320 9626 707 894 -566 C
ATOM 4944 O ASN B 343 -41.265 15.348 27.601 1.00 84.00 O
ANISOU 4944 O ASN B 343 11376 9999 10541 580 914 -444 O
ATOM 4945 CB ASN B 343 -39.127 14.087 28.791 1.00 96.48 C
ANISOU 4945 CB ASN B 343 13094 11438 12124 1019 941 -467 C
ATOM 4946 CG ASN B 343 -37.897 13.215 28.953 1.00112.65 C
ANISOU 4946 CG ASN B 343 15228 13365 14207 1222 938 -551 C
ATOM 4947 OD1 ASN B 343 -37.682 12.615 30.008 1.00126.32 O
ANISOU 4947 OD1 ASN B 343 17025 15007 15963 1380 956 -410 O
ATOM 4948 ND2 ASN B 343 -37.078 13.149 27.912 1.00101.73 N
ANISOU 4948 ND2 ASN B 343 13845 11979 12828 1218 913 -783 N
ATOM 4949 N ALA B 344 -40.147 17.221 27.103 1.00 75.76 N
ANISOU 4949 N ALA B 344 10176 9309 9300 653 861 -642 N
ATOM 4950 CA ALA B 344 -41.357 17.918 26.689 1.00 80.86 C
ANISOU 4950 CA ALA B 344 10747 10026 9950 442 837 -588 C
ATOM 4951 C ALA B 344 -41.848 17.379 25.350 1.00 87.81 C
ANISOU 4951 C ALA B 344 11680 10779 10904 231 806 -702 C
ATOM 4952 O ALA B 344 -41.053 17.022 24.475 1.00 85.57 O
ANISOU 4952 O ALA B 344 11447 10451 10613 234 790 -883 O
ATOM 4953 CB ALA B 344 -41.103 19.422 26.592 1.00 77.72 C
ANISOU 4953 CB ALA B 344 10218 9882 9428 449 803 -643 C
ATOM 4954 N THR B 345 -43.173 17.313 25.197 1.00 85.35 N
ANISOU 4954 N THR B 345 11352 10411 10666 45 798 -600 N
ATOM 4955 CA THR B 345 -43.755 16.829 23.948 1.00 76.61 C
ANISOU 4955 CA THR B 345 10289 9189 9629 -168 761 -699 C
ATOM 4956 C THR B 345 -43.372 17.733 22.784 1.00 85.16 C
ANISOU 4956 C THR B 345 11320 10424 10615 -261 697 -878 C
ATOM 4957 O THR B 345 -42.915 17.261 21.736 1.00 80.92 O
ANISOU 4957 O THR B 345 10847 9817 10080 -325 678 -1048 O
ATOM 4958 CB THR B 345 -45.277 16.739 24.077 1.00 77.01 C
ANISOU 4958 CB THR B 345 10310 9178 9774 -346 758 -551 C
ATOM 4959 OG1 THR B 345 -45.619 15.787 25.091 1.00 94.29 O
ANISOU 4959 OG1 THR B 345 12563 11206 12055 -276 826 -390 O
ATOM 4960 CG2 THR B 345 -45.900 16.314 22.757 1.00 77.74 C
ANISOU 4960 CG2 THR B 345 10439 9166 9932 -573 708 -661 C
ATOM 4961 N ARG B 346 -43.550 19.038 22.953 1.00 88.46 N
ANISOU 4961 N ARG B 346 11621 11046 10942 -271 666 -842 N
ATOM 4962 CA ARG B 346 -43.203 20.020 21.940 1.00 86.24 C
ANISOU 4962 CA ARG B 346 11287 10922 10559 -356 604 -989 C
ATOM 4963 C ARG B 346 -42.284 21.064 22.557 1.00 85.12 C
ANISOU 4963 C ARG B 346 11065 10978 10300 -183 614 -1002 C
ATOM 4964 O ARG B 346 -42.486 21.482 23.701 1.00 85.11 O
ANISOU 4964 O ARG B 346 10999 11046 10292 -74 642 -858 O
ATOM 4965 CB ARG B 346 -44.460 20.689 21.366 1.00 86.90 C
ANISOU 4965 CB ARG B 346 11301 11058 10660 -576 536 -938 C
ATOM 4966 CG ARG B 346 -44.222 21.565 20.145 1.00 83.58 C
ANISOU 4966 CG ARG B 346 10849 10767 10140 -700 460 -1086 C
ATOM 4967 CD ARG B 346 -45.497 22.295 19.748 1.00 86.97 C
ANISOU 4967 CD ARG B 346 11199 11253 10594 -894 383 -1010 C
ATOM 4968 NE ARG B 346 -46.627 21.385 19.594 1.00 78.53 N
ANISOU 4968 NE ARG B 346 10171 10011 9657 -1035 377 -941 N
ATOM 4969 CZ ARG B 346 -47.014 20.857 18.440 1.00 80.20 C
ANISOU 4969 CZ ARG B 346 10446 10127 9900 -1216 326 -1038 C
ATOM 4970 NH1 ARG B 346 -46.384 21.128 17.310 1.00 73.81 N
ANISOU 4970 NH1 ARG B 346 9673 9378 8991 -1284 279 -1207 N
ATOM 4971 NH2 ARG B 346 -48.063 20.040 18.421 1.00 80.24 N
ANISOU 4971 NH2 ARG B 346 10477 9974 10035 -1335 325 -966 N
ATOM 4972 N PHE B 347 -41.268 21.464 21.803 1.00 81.97 N
ANISOU 4972 N PHE B 347 10667 10669 9808 -161 596 -1180 N
ATOM 4973 CA PHE B 347 -40.362 22.527 22.207 1.00 69.21 C
ANISOU 4973 CA PHE B 347 8969 9248 8078 -21 599 -1220 C
ATOM 4974 C PHE B 347 -40.812 23.853 21.605 1.00 75.14 C
ANISOU 4974 C PHE B 347 9626 10168 8757 -162 534 -1235 C
ATOM 4975 O PHE B 347 -41.695 23.911 20.746 1.00 80.94 O
ANISOU 4975 O PHE B 347 10367 10868 9518 -367 478 -1237 O
ATOM 4976 CB PHE B 347 -38.926 22.203 21.786 1.00 71.04 C
ANISOU 4976 CB PHE B 347 9252 9483 8256 94 626 -1411 C
ATOM 4977 CG PHE B 347 -38.165 21.396 22.797 1.00 76.44 C
ANISOU 4977 CG PHE B 347 9980 10083 8979 322 684 -1380 C
ATOM 4978 CD1 PHE B 347 -38.731 20.272 23.375 1.00 80.95 C
ANISOU 4978 CD1 PHE B 347 10627 10465 9664 345 714 -1256 C
ATOM 4979 CD2 PHE B 347 -36.879 21.758 23.167 1.00 74.84 C
ANISOU 4979 CD2 PHE B 347 9744 9989 8702 512 706 -1474 C
ATOM 4980 CE1 PHE B 347 -38.035 19.527 24.308 1.00 78.16 C
ANISOU 4980 CE1 PHE B 347 10323 10029 9345 556 758 -1216 C
ATOM 4981 CE2 PHE B 347 -36.176 21.016 24.097 1.00 74.07 C
ANISOU 4981 CE2 PHE B 347 9687 9814 8642 727 747 -1444 C
ATOM 4982 CZ PHE B 347 -36.754 19.900 24.668 1.00 78.92 C
ANISOU 4982 CZ PHE B 347 10385 10236 9366 751 770 -1310 C
ATOM 4983 N ALA B 348 -40.196 24.930 22.075 1.00 73.71 N
ANISOU 4983 N ALA B 348 9353 10166 8485 -49 535 -1243 N
ATOM 4984 CA ALA B 348 -40.529 26.265 21.606 1.00 72.83 C
ANISOU 4984 CA ALA B 348 9148 10217 8307 -161 472 -1250 C
ATOM 4985 C ALA B 348 -39.678 26.634 20.398 1.00 78.92 C
ANISOU 4985 C ALA B 348 9946 11059 8981 -232 446 -1445 C
ATOM 4986 O ALA B 348 -38.582 26.105 20.200 1.00 78.92 O
ANISOU 4986 O ALA B 348 10004 11032 8949 -136 490 -1581 O
ATOM 4987 CB ALA B 348 -40.326 27.296 22.717 1.00 77.58 C
ANISOU 4987 CB ALA B 348 9634 10979 8865 -13 487 -1164 C
ATOM 4988 N SER B 349 -40.203 27.541 19.580 1.00 77.40 N
ANISOU 4988 N SER B 349 9710 10953 8743 -404 372 -1458 N
ATOM 4989 CA SER B 349 -39.404 28.107 18.506 1.00 78.32 C
ANISOU 4989 CA SER B 349 9842 11167 8748 -475 348 -1626 C
ATOM 4990 C SER B 349 -38.276 28.946 19.094 1.00 77.92 C
ANISOU 4990 C SER B 349 9718 11273 8615 -300 387 -1679 C
ATOM 4991 O SER B 349 -38.412 29.547 20.162 1.00 73.03 O
ANISOU 4991 O SER B 349 9007 10731 8009 -181 397 -1566 O
ATOM 4992 CB SER B 349 -40.273 28.954 17.577 1.00 78.09 C
ANISOU 4992 CB SER B 349 9785 11199 8688 -696 251 -1604 C
ATOM 4993 OG SER B 349 -41.270 28.165 16.948 1.00 70.78 O
ANISOU 4993 OG SER B 349 8927 10132 7834 -863 209 -1575 O
ATOM 4994 N VAL B 350 -37.143 28.972 18.389 1.00 85.69 N
ANISOU 4994 N VAL B 350 10738 12305 9513 -288 413 -1861 N
ATOM 4995 CA VAL B 350 -35.954 29.622 18.935 1.00 74.98 C
ANISOU 4995 CA VAL B 350 9316 11085 8088 -112 459 -1933 C
ATOM 4996 C VAL B 350 -36.176 31.120 19.108 1.00 76.65 C
ANISOU 4996 C VAL B 350 9415 11465 8244 -142 412 -1872 C
ATOM 4997 O VAL B 350 -35.602 31.738 20.013 1.00 78.95 O
ANISOU 4997 O VAL B 350 9621 11863 8513 22 442 -1854 O
ATOM 4998 CB VAL B 350 -34.729 29.317 18.050 1.00 75.91 C
ANISOU 4998 CB VAL B 350 9493 11216 8133 -113 500 -2155 C
ATOM 4999 CG1 VAL B 350 -34.929 29.863 16.647 1.00 80.56 C
ANISOU 4999 CG1 VAL B 350 10115 11858 8637 -345 448 -2243 C
ATOM 5000 CG2 VAL B 350 -33.457 29.872 18.680 1.00 75.54 C
ANISOU 5000 CG2 VAL B 350 9373 11298 8030 82 553 -2238 C
ATOM 5001 N TYR B 351 -37.017 31.727 18.265 1.00 76.40 N
ANISOU 5001 N TYR B 351 9379 11457 8192 -348 334 -1837 N
ATOM 5002 CA TYR B 351 -37.307 33.148 18.430 1.00 84.15 C
ANISOU 5002 CA TYR B 351 10253 12582 9137 -380 281 -1769 C
ATOM 5003 C TYR B 351 -38.108 33.396 19.702 1.00 77.41 C
ANISOU 5003 C TYR B 351 9308 11733 8371 -281 276 -1590 C
ATOM 5004 O TYR B 351 -37.918 34.416 20.374 1.00 82.19 O
ANISOU 5004 O TYR B 351 9807 12465 8956 -192 275 -1551 O
ATOM 5005 CB TYR B 351 -38.049 33.686 17.203 1.00 76.64 C
ANISOU 5005 CB TYR B 351 9326 11642 8150 -624 186 -1768 C
ATOM 5006 CG TYR B 351 -39.557 33.598 17.290 1.00 77.56 C
ANISOU 5006 CG TYR B 351 9426 11680 8365 -740 112 -1608 C
ATOM 5007 CD1 TYR B 351 -40.226 32.432 16.945 1.00 80.30 C
ANISOU 5007 CD1 TYR B 351 9860 11871 8780 -827 106 -1590 C
ATOM 5008 CD2 TYR B 351 -40.313 34.686 17.712 1.00 73.62 C
ANISOU 5008 CD2 TYR B 351 8816 11260 7898 -762 49 -1484 C
ATOM 5009 CE1 TYR B 351 -41.604 32.349 17.024 1.00 74.73 C
ANISOU 5009 CE1 TYR B 351 9129 11094 8170 -935 41 -1451 C
ATOM 5010 CE2 TYR B 351 -41.689 34.612 17.795 1.00 73.12 C
ANISOU 5010 CE2 TYR B 351 8724 11126 7933 -866 -17 -1348 C
ATOM 5011 CZ TYR B 351 -42.330 33.442 17.449 1.00 73.12 C
ANISOU 5011 CZ TYR B 351 8809 10975 7997 -954 -20 -1332 C
ATOM 5012 OH TYR B 351 -43.701 33.367 17.529 1.00 70.03 O
ANISOU 5012 OH TYR B 351 8382 10515 7711 -1060 -84 -1204 O
ATOM 5013 N ALA B 352 -39.005 32.474 20.048 1.00 78.30 N
ANISOU 5013 N ALA B 352 9460 11710 8582 -301 279 -1484 N
ATOM 5014 CA ALA B 352 -39.756 32.555 21.293 1.00 71.44 C
ANISOU 5014 CA ALA B 352 8514 10836 7794 -208 292 -1317 C
ATOM 5015 C ALA B 352 -39.283 31.463 22.242 1.00 77.64 C
ANISOU 5015 C ALA B 352 9347 11535 8618 -25 379 -1297 C
ATOM 5016 O ALA B 352 -40.079 30.635 22.695 1.00 81.61 O
ANISOU 5016 O ALA B 352 9883 11914 9209 -33 395 -1186 O
ATOM 5017 CB ALA B 352 -41.258 32.431 21.032 1.00 71.85 C
ANISOU 5017 CB ALA B 352 8559 10803 7937 -380 228 -1194 C
ATOM 5018 N TRP B 353 -37.982 31.450 22.530 1.00 81.41 N
ANISOU 5018 N TRP B 353 9828 12072 9030 139 432 -1405 N
ATOM 5019 CA TRP B 353 -37.401 30.403 23.358 1.00 75.17 C
ANISOU 5019 CA TRP B 353 9092 11199 8271 322 503 -1399 C
ATOM 5020 C TRP B 353 -38.009 30.419 24.755 1.00 84.56 C
ANISOU 5020 C TRP B 353 10223 12393 9512 438 528 -1223 C
ATOM 5021 O TRP B 353 -38.288 31.479 25.321 1.00 85.11 O
ANISOU 5021 O TRP B 353 10182 12593 9562 463 512 -1157 O
ATOM 5022 CB TRP B 353 -35.883 30.574 23.434 1.00 72.78 C
ANISOU 5022 CB TRP B 353 8780 10984 7889 480 544 -1553 C
ATOM 5023 CG TRP B 353 -35.446 31.967 23.777 1.00 87.45 C
ANISOU 5023 CG TRP B 353 10517 13035 9675 539 532 -1573 C
ATOM 5024 CD1 TRP B 353 -35.321 33.022 22.920 1.00 86.58 C
ANISOU 5024 CD1 TRP B 353 10362 13035 9501 415 490 -1652 C
ATOM 5025 CD2 TRP B 353 -35.068 32.455 25.070 1.00 97.40 C
ANISOU 5025 CD2 TRP B 353 11689 14399 10921 735 561 -1514 C
ATOM 5026 NE1 TRP B 353 -34.894 34.137 23.600 1.00 83.22 N
ANISOU 5026 NE1 TRP B 353 9821 12768 9032 521 493 -1647 N
ATOM 5027 CE2 TRP B 353 -34.730 33.815 24.921 1.00 89.02 C
ANISOU 5027 CE2 TRP B 353 10524 13505 9794 718 536 -1569 C
ATOM 5028 CE3 TRP B 353 -34.985 31.874 26.340 1.00 91.95 C
ANISOU 5028 CE3 TRP B 353 11000 13676 10263 920 604 -1420 C
ATOM 5029 CZ2 TRP B 353 -34.315 34.603 25.993 1.00 92.63 C
ANISOU 5029 CZ2 TRP B 353 10875 14098 10223 881 554 -1542 C
ATOM 5030 CZ3 TRP B 353 -34.572 32.658 27.402 1.00 85.80 C
ANISOU 5030 CZ3 TRP B 353 10119 13039 9443 1080 620 -1390 C
ATOM 5031 CH2 TRP B 353 -34.243 34.007 27.222 1.00 87.56 C
ANISOU 5031 CH2 TRP B 353 10234 13428 9606 1060 596 -1456 C
ATOM 5032 N ASN B 354 -38.217 29.227 25.306 1.00 92.15 N
ANISOU 5032 N ASN B 354 11262 13210 10541 504 570 -1148 N
ATOM 5033 CA ASN B 354 -38.880 29.053 26.590 1.00 85.09 C
ANISOU 5033 CA ASN B 354 10336 12298 9696 593 603 -972 C
ATOM 5034 C ASN B 354 -37.849 28.954 27.706 1.00 85.76 C
ANISOU 5034 C ASN B 354 10410 12443 9734 841 654 -975 C
ATOM 5035 O ASN B 354 -36.770 28.384 27.520 1.00 85.87 O
ANISOU 5035 O ASN B 354 10485 12419 9722 946 674 -1091 O
ATOM 5036 CB ASN B 354 -39.759 27.801 26.575 1.00 78.94 C
ANISOU 5036 CB ASN B 354 9654 11320 9019 512 620 -874 C
ATOM 5037 CG ASN B 354 -40.664 27.710 27.785 1.00104.95 C
ANISOU 5037 CG ASN B 354 12911 14601 12366 555 654 -681 C
ATOM 5038 OD1 ASN B 354 -41.801 28.183 27.759 1.00132.37 O
ANISOU 5038 OD1 ASN B 354 16318 18091 15884 421 628 -590 O
ATOM 5039 ND2 ASN B 354 -40.167 27.099 28.855 1.00108.88 N
ANISOU 5039 ND2 ASN B 354 13447 15066 12856 741 711 -619 N
ATOM 5040 N ARG B 355 -38.189 29.512 28.866 1.00 97.51 N
ANISOU 5040 N ARG B 355 11814 14026 11211 934 672 -852 N
ATOM 5041 CA ARG B 355 -37.332 29.469 30.044 1.00 90.63 C
ANISOU 5041 CA ARG B 355 10926 13222 10288 1168 714 -833 C
ATOM 5042 C ARG B 355 -38.121 28.909 31.217 1.00 80.38 C
ANISOU 5042 C ARG B 355 9648 11861 9032 1223 756 -642 C
ATOM 5043 O ARG B 355 -39.249 29.342 31.475 1.00 73.36 O
ANISOU 5043 O ARG B 355 8697 10996 8179 1117 755 -527 O
ATOM 5044 CB ARG B 355 -36.784 30.859 30.389 1.00 83.80 C
ANISOU 5044 CB ARG B 355 9929 12571 9340 1246 700 -892 C
ATOM 5045 CG ARG B 355 -36.283 30.987 31.820 1.00 83.05 C
ANISOU 5045 CG ARG B 355 9791 12568 9196 1467 738 -828 C
ATOM 5046 CD ARG B 355 -35.450 32.242 32.018 1.00 78.19 C
ANISOU 5046 CD ARG B 355 9057 12153 8499 1560 723 -932 C
ATOM 5047 NE ARG B 355 -34.123 32.110 31.429 1.00 79.53 N
ANISOU 5047 NE ARG B 355 9255 12338 8626 1638 718 -1112 N
ATOM 5048 CZ ARG B 355 -33.165 33.022 31.527 1.00 79.74 C
ANISOU 5048 CZ ARG B 355 9192 12521 8584 1732 712 -1231 C
ATOM 5049 NH1 ARG B 355 -33.355 34.156 32.181 1.00 86.91 N
ANISOU 5049 NH1 ARG B 355 9979 13585 9457 1766 706 -1194 N
ATOM 5050 NH2 ARG B 355 -31.987 32.789 30.955 1.00 79.39 N
ANISOU 5050 NH2 ARG B 355 9177 12476 8511 1794 714 -1398 N
ATOM 5051 N LYS B 356 -37.528 27.948 31.921 1.00 82.52 N
ANISOU 5051 N LYS B 356 10004 12050 9301 1385 793 -608 N
ATOM 5052 CA LYS B 356 -38.130 27.334 33.100 1.00 81.74 C
ANISOU 5052 CA LYS B 356 9941 11889 9227 1454 840 -424 C
ATOM 5053 C LYS B 356 -37.187 27.560 34.274 1.00 92.52 C
ANISOU 5053 C LYS B 356 11278 13370 10504 1694 859 -413 C
ATOM 5054 O LYS B 356 -36.092 26.989 34.315 1.00 91.55 O
ANISOU 5054 O LYS B 356 11218 13207 10359 1841 855 -494 O
ATOM 5055 CB LYS B 356 -38.388 25.844 32.873 1.00 79.53 C
ANISOU 5055 CB LYS B 356 9809 11376 9033 1417 860 -371 C
ATOM 5056 CG LYS B 356 -39.508 25.252 33.724 1.00 84.72 C
ANISOU 5056 CG LYS B 356 10504 11940 9746 1378 906 -164 C
ATOM 5057 CD LYS B 356 -39.056 24.947 35.144 1.00 95.84 C
ANISOU 5057 CD LYS B 356 11941 13378 11097 1588 948 -52 C
ATOM 5058 CE LYS B 356 -40.208 24.432 35.991 1.00 97.94 C
ANISOU 5058 CE LYS B 356 12241 13564 11407 1532 1004 156 C
ATOM 5059 NZ LYS B 356 -41.300 25.438 36.110 1.00102.99 N
ANISOU 5059 NZ LYS B 356 12753 14325 12052 1396 1014 215 N
ATOM 5060 N ARG B 357 -37.609 28.391 35.223 1.00 90.34 N
ANISOU 5060 N ARG B 357 10905 13239 10182 1734 877 -320 N
ATOM 5061 CA ARG B 357 -36.796 28.678 36.396 1.00 81.30 C
ANISOU 5061 CA ARG B 357 9726 12220 8945 1956 893 -304 C
ATOM 5062 C ARG B 357 -36.842 27.502 37.363 1.00 84.75 C
ANISOU 5062 C ARG B 357 10280 12535 9387 2070 932 -157 C
ATOM 5063 O ARG B 357 -37.916 26.966 37.655 1.00 87.95 O
ANISOU 5063 O ARG B 357 10731 12838 9846 1971 969 -4 O
ATOM 5064 CB ARG B 357 -37.279 29.953 37.085 1.00 83.15 C
ANISOU 5064 CB ARG B 357 9816 12649 9129 1952 902 -258 C
ATOM 5065 CG ARG B 357 -36.511 30.290 38.349 1.00 91.64 C
ANISOU 5065 CG ARG B 357 10850 13866 10101 2174 918 -240 C
ATOM 5066 CD ARG B 357 -37.014 31.571 38.983 1.00 97.73 C
ANISOU 5066 CD ARG B 357 11473 14829 10831 2160 930 -210 C
ATOM 5067 NE ARG B 357 -36.387 31.808 40.277 1.00102.88 N
ANISOU 5067 NE ARG B 357 12095 15614 11381 2366 949 -179 N
ATOM 5068 CZ ARG B 357 -36.604 32.876 41.031 1.00 97.56 C
ANISOU 5068 CZ ARG B 357 11295 15121 10653 2401 963 -166 C
ATOM 5069 NH1 ARG B 357 -37.427 33.838 40.646 1.00 92.12 N
ANISOU 5069 NH1 ARG B 357 10492 14500 10010 2251 959 -179 N
ATOM 5070 NH2 ARG B 357 -35.980 32.983 42.200 1.00103.73 N
ANISOU 5070 NH2 ARG B 357 12062 16017 11334 2594 977 -141 N
ATOM 5071 N ILE B 358 -35.674 27.105 37.860 1.00 86.39 N
ANISOU 5071 N ILE B 358 10533 12751 9540 2276 922 -202 N
ATOM 5072 CA ILE B 358 -35.528 25.963 38.753 1.00 88.19 C
ANISOU 5072 CA ILE B 358 10884 12857 9766 2408 945 -71 C
ATOM 5073 C ILE B 358 -35.050 26.474 40.103 1.00 98.28 C
ANISOU 5073 C ILE B 358 12109 14302 10929 2601 952 -12 C
ATOM 5074 O ILE B 358 -34.042 27.187 40.182 1.00 99.44 O
ANISOU 5074 O ILE B 358 12177 14598 11007 2729 919 -144 O
ATOM 5075 CB ILE B 358 -34.551 24.928 38.173 1.00 84.93 C
ANISOU 5075 CB ILE B 358 10581 12288 9400 2493 915 -173 C
ATOM 5076 CG1 ILE B 358 -34.962 24.569 36.745 1.00 86.72 C
ANISOU 5076 CG1 ILE B 358 10845 12377 9729 2293 905 -263 C
ATOM 5077 CG2 ILE B 358 -34.505 23.689 39.044 1.00 85.69 C
ANISOU 5077 CG2 ILE B 358 10816 12232 9512 2614 932 -21 C
ATOM 5078 CD1 ILE B 358 -33.814 24.131 35.875 1.00 93.65 C
ANISOU 5078 CD1 ILE B 358 11763 13187 10632 2356 870 -454 C
ATOM 5079 N SER B 359 -35.768 26.111 41.163 1.00 95.38 N
ANISOU 5079 N SER B 359 11787 13916 10538 2619 998 182 N
ATOM 5080 CA SER B 359 -35.472 26.649 42.480 1.00 93.37 C
ANISOU 5080 CA SER B 359 11480 13833 10162 2781 1010 249 C
ATOM 5081 C SER B 359 -35.979 25.702 43.557 1.00108.04 C
ANISOU 5081 C SER B 359 13458 15594 11999 2829 1056 466 C
ATOM 5082 O SER B 359 -36.981 25.004 43.373 1.00110.46 O
ANISOU 5082 O SER B 359 13838 15745 12385 2682 1099 586 O
ATOM 5083 CB SER B 359 -36.098 28.036 42.666 1.00 99.35 C
ANISOU 5083 CB SER B 359 12075 14792 10880 2695 1031 233 C
ATOM 5084 OG SER B 359 -37.493 27.995 42.424 1.00109.19 O
ANISOU 5084 OG SER B 359 13314 15970 12203 2487 1076 338 O
ATOM 5085 N ASN B 360 -35.265 25.693 44.685 1.00108.79 N
ANISOU 5085 N ASN B 360 13570 15783 11981 3036 1045 514 N
ATOM 5086 CA ASN B 360 -35.668 24.971 45.891 1.00103.69 C
ANISOU 5086 CA ASN B 360 13030 15089 11278 3101 1088 728 C
ATOM 5087 C ASN B 360 -35.871 23.480 45.609 1.00104.44 C
ANISOU 5087 C ASN B 360 13302 14911 11470 3066 1094 831 C
ATOM 5088 O ASN B 360 -36.965 22.934 45.758 1.00108.00 O
ANISOU 5088 O ASN B 360 13818 15247 11971 2926 1157 987 O
ATOM 5089 CB ASN B 360 -36.927 25.602 46.497 1.00101.18 C
ANISOU 5089 CB ASN B 360 12638 14878 10928 2967 1166 851 C
ATOM 5090 CG ASN B 360 -36.745 27.073 46.806 1.00106.55 C
ANISOU 5090 CG ASN B 360 13141 15820 11523 3004 1160 746 C
ATOM 5091 OD1 ASN B 360 -37.094 27.936 46.002 1.00 99.41 O
ANISOU 5091 OD1 ASN B 360 12115 14979 10675 2874 1154 633 O
ATOM 5092 ND2 ASN B 360 -36.183 27.365 47.973 1.00117.12 N
ANISOU 5092 ND2 ASN B 360 14466 17309 12724 3183 1156 784 N
ATOM 5093 N CYS B 361 -34.785 22.825 45.205 1.00 96.23 N
ANISOU 5093 N CYS B 361 12335 13766 10463 3197 1030 736 N
ATOM 5094 CA CYS B 361 -34.832 21.405 44.888 1.00106.20 C
ANISOU 5094 CA CYS B 361 13763 14760 11828 3183 1026 810 C
ATOM 5095 C CYS B 361 -33.414 20.856 44.826 1.00109.66 C
ANISOU 5095 C CYS B 361 14259 15138 12267 3398 946 705 C
ATOM 5096 O CYS B 361 -32.436 21.602 44.714 1.00108.08 O
ANISOU 5096 O CYS B 361 13959 15094 12012 3518 896 539 O
ATOM 5097 CB CYS B 361 -35.566 21.149 43.564 1.00124.42 C
ANISOU 5097 CB CYS B 361 16073 16920 14280 2954 1045 744 C
ATOM 5098 SG CYS B 361 -34.910 22.069 42.156 1.00 99.32 S
ANISOU 5098 SG CYS B 361 12760 13840 11138 2900 994 459 S
ATOM 5099 N VAL B 362 -33.325 19.533 44.901 1.00112.11 N
ANISOU 5099 N VAL B 362 14730 15217 12650 3443 935 802 N
ATOM 5100 CA VAL B 362 -32.075 18.815 44.685 1.00110.67 C
ANISOU 5100 CA VAL B 362 14615 14925 12509 3627 859 699 C
ATOM 5101 C VAL B 362 -32.007 18.416 43.219 1.00120.56 C
ANISOU 5101 C VAL B 362 15875 16023 13910 3502 850 533 C
ATOM 5102 O VAL B 362 -32.935 17.791 42.692 1.00124.60 O
ANISOU 5102 O VAL B 362 16457 16362 14523 3322 894 604 O
ATOM 5103 CB VAL B 362 -31.973 17.582 45.601 1.00106.05 C
ANISOU 5103 CB VAL B 362 14205 14163 11926 3756 843 898 C
ATOM 5104 CG1 VAL B 362 -30.770 16.739 45.215 1.00108.53 C
ANISOU 5104 CG1 VAL B 362 14589 14325 12321 3927 761 781 C
ATOM 5105 CG2 VAL B 362 -31.898 18.016 47.051 1.00 90.73 C
ANISOU 5105 CG2 VAL B 362 12258 12396 9817 3895 843 1046 C
ATOM 5106 N ALA B 363 -30.909 18.771 42.559 1.00131.35 N
ANISOU 5106 N ALA B 363 17167 17454 15288 3594 796 307 N
ATOM 5107 CA ALA B 363 -30.742 18.548 41.127 1.00130.82 C
ANISOU 5107 CA ALA B 363 17089 17278 15339 3476 790 118 C
ATOM 5108 C ALA B 363 -29.873 17.315 40.908 1.00133.85 C
ANISOU 5108 C ALA B 363 17588 17447 15822 3614 741 64 C
ATOM 5109 O ALA B 363 -28.676 17.331 41.210 1.00132.02 O
ANISOU 5109 O ALA B 363 17333 17269 15559 3826 682 -35 O
ATOM 5110 CB ALA B 363 -30.128 19.778 40.462 1.00123.08 C
ANISOU 5110 CB ALA B 363 15948 16510 14308 3465 773 -107 C
ATOM 5111 N ASP B 364 -30.476 16.253 40.374 1.00117.82 N
ANISOU 5111 N ASP B 364 15676 15171 13919 3494 764 121 N
ATOM 5112 CA ASP B 364 -29.748 15.044 39.996 1.00116.87 C
ANISOU 5112 CA ASP B 364 15663 14821 13921 3597 722 53 C
ATOM 5113 C ASP B 364 -29.185 15.269 38.598 1.00123.14 C
ANISOU 5113 C ASP B 364 16384 15620 14784 3525 712 -223 C
ATOM 5114 O ASP B 364 -29.784 14.886 37.593 1.00127.42 O
ANISOU 5114 O ASP B 364 16959 16032 15424 3334 744 -277 O
ATOM 5115 CB ASP B 364 -30.665 13.827 40.055 1.00106.61 C
ANISOU 5115 CB ASP B 364 14521 13256 12732 3493 755 234 C
ATOM 5116 CG ASP B 364 -29.902 12.509 40.021 1.00116.58 C
ANISOU 5116 CG ASP B 364 15911 14271 14115 3643 704 214 C
ATOM 5117 OD1 ASP B 364 -28.686 12.517 39.731 1.00112.63 O
ANISOU 5117 OD1 ASP B 364 15368 13796 13632 3804 646 26 O
ATOM 5118 OD2 ASP B 364 -30.522 11.458 40.293 1.00121.91 O
ANISOU 5118 OD2 ASP B 364 16726 14720 14873 3600 722 386 O
ATOM 5119 N TYR B 365 -28.016 15.914 38.533 1.00121.13 N
ANISOU 5119 N TYR B 365 16174 14601 15251 949 -368 -2082 N
ATOM 5120 CA TYR B 365 -27.412 16.210 37.238 1.00117.66 C
ANISOU 5120 CA TYR B 365 15566 14403 14736 1127 -399 -1972 C
ATOM 5121 C TYR B 365 -27.021 14.940 36.497 1.00126.09 C
ANISOU 5121 C TYR B 365 16977 15415 15517 1381 -328 -2009 C
ATOM 5122 O TYR B 365 -26.976 14.936 35.263 1.00135.42 O
ANISOU 5122 O TYR B 365 18117 16713 16624 1462 -346 -1988 O
ATOM 5123 CB TYR B 365 -26.192 17.114 37.415 1.00108.75 C
ANISOU 5123 CB TYR B 365 14098 13557 13665 1300 -438 -1766 C
ATOM 5124 CG TYR B 365 -26.530 18.507 37.886 1.00114.91 C
ANISOU 5124 CG TYR B 365 14485 14441 14734 1061 -521 -1711 C
ATOM 5125 CD1 TYR B 365 -26.910 19.492 36.986 1.00104.71 C
ANISOU 5125 CD1 TYR B 365 12883 13314 13590 929 -599 -1671 C
ATOM 5126 CD2 TYR B 365 -26.473 18.837 39.231 1.00114.35 C
ANISOU 5126 CD2 TYR B 365 14356 14303 14788 968 -523 -1700 C
ATOM 5127 CE1 TYR B 365 -27.222 20.770 37.414 1.00108.07 C
ANISOU 5127 CE1 TYR B 365 12947 13834 14280 710 -676 -1620 C
ATOM 5128 CE2 TYR B 365 -26.778 20.110 39.672 1.00107.81 C
ANISOU 5128 CE2 TYR B 365 13169 13570 14224 751 -601 -1650 C
ATOM 5129 CZ TYR B 365 -27.155 21.073 38.760 1.00101.48 C
ANISOU 5129 CZ TYR B 365 12062 12931 13566 621 -677 -1611 C
ATOM 5130 OH TYR B 365 -27.464 22.342 39.193 1.00 81.98 O
ANISOU 5130 OH TYR B 365 9235 10555 11359 404 -755 -1562 O
ATOM 5131 N SER B 366 -26.740 13.857 37.225 1.00128.96 N
ANISOU 5131 N SER B 366 17680 15601 15717 1509 -248 -2065 N
ATOM 5132 CA SER B 366 -26.391 12.602 36.571 1.00129.90 C
ANISOU 5132 CA SER B 366 18144 15653 15561 1748 -178 -2107 C
ATOM 5133 C SER B 366 -27.547 12.096 35.724 1.00140.95 C
ANISOU 5133 C SER B 366 19733 16891 16928 1589 -176 -2270 C
ATOM 5134 O SER B 366 -27.338 11.569 34.627 1.00152.23 O
ANISOU 5134 O SER B 366 21277 18374 18189 1751 -160 -2270 O
ATOM 5135 CB SER B 366 -25.988 11.563 37.617 1.00115.85 C
ANISOU 5135 CB SER B 366 16694 13691 13633 1881 -94 -2149 C
ATOM 5136 OG SER B 366 -24.829 11.976 38.323 1.00123.59 O
ANISOU 5136 OG SER B 366 17507 14830 14621 2059 -94 -1993 O
ATOM 5137 N VAL B 367 -28.776 12.269 36.218 1.00135.15 N
ANISOU 5137 N VAL B 367 19029 15962 16360 1269 -193 -2407 N
ATOM 5138 CA VAL B 367 -29.987 11.881 35.503 1.00135.19 C
ANISOU 5138 CA VAL B 367 19195 15802 16368 1078 -198 -2569 C
ATOM 5139 C VAL B 367 -30.030 12.500 34.113 1.00144.52 C
ANISOU 5139 C VAL B 367 20147 17189 17575 1088 -259 -2513 C
ATOM 5140 O VAL B 367 -30.500 11.866 33.158 1.00150.10 O
ANISOU 5140 O VAL B 367 21042 17823 18164 1102 -246 -2604 O
ATOM 5141 CB VAL B 367 -31.212 12.275 36.354 1.00133.67 C
ANISOU 5141 CB VAL B 367 18975 15414 16398 716 -221 -2692 C
ATOM 5142 CG1 VAL B 367 -32.369 12.762 35.477 1.00136.32 C
ANISOU 5142 CG1 VAL B 367 19197 15730 16868 460 -280 -2782 C
ATOM 5143 CG2 VAL B 367 -31.635 11.111 37.254 1.00132.32 C
ANISOU 5143 CG2 VAL B 367 19211 14938 16127 686 -140 -2835 C
ATOM 5144 N LEU B 368 -29.544 13.736 33.972 1.00140.60 N
ANISOU 5144 N LEU B 368 19241 16950 17230 1083 -328 -2363 N
ATOM 5145 CA LEU B 368 -29.395 14.338 32.653 1.00143.28 C
ANISOU 5145 CA LEU B 368 19347 17512 17579 1135 -384 -2285 C
ATOM 5146 C LEU B 368 -28.528 13.446 31.775 1.00158.31 C
ANISOU 5146 C LEU B 368 21449 19493 19207 1470 -334 -2238 C
ATOM 5147 O LEU B 368 -29.053 12.655 30.986 1.00160.30 O
ANISOU 5147 O LEU B 368 21949 19629 19329 1479 -309 -2350 O
ATOM 5148 CB LEU B 368 -28.786 15.737 32.755 1.00129.01 C
ANISOU 5148 CB LEU B 368 17081 15981 15957 1126 -456 -2111 C
ATOM 5149 CG LEU B 368 -29.567 16.733 33.614 1.00125.63 C
ANISOU 5149 CG LEU B 368 16418 15504 15811 802 -512 -2141 C
ATOM 5150 CD1 LEU B 368 -28.961 18.122 33.508 1.00111.73 C
ANISOU 5150 CD1 LEU B 368 14194 14034 14223 806 -589 -1965 C
ATOM 5151 CD2 LEU B 368 -31.033 16.746 33.212 1.00114.06 C
ANISOU 5151 CD2 LEU B 368 15016 13867 14452 497 -539 -2308 C
ATOM 5152 N TYR B 369 -27.203 13.537 31.942 1.00156.05 N
ANISOU 5152 N TYR B 369 21067 19395 18830 1747 -318 -2075 N
ATOM 5153 CA TYR B 369 -26.266 12.768 31.125 1.00158.07 C
ANISOU 5153 CA TYR B 369 21481 19750 18827 2083 -272 -2010 C
ATOM 5154 C TYR B 369 -26.634 11.286 31.008 1.00165.67 C
ANISOU 5154 C TYR B 369 22916 20462 19570 2155 -194 -2164 C
ATOM 5155 O TYR B 369 -26.237 10.638 30.034 1.00165.13 O
ANISOU 5155 O TYR B 369 22995 20447 19300 2369 -167 -2153 O
ATOM 5156 CB TYR B 369 -24.845 12.924 31.702 1.00148.62 C
ANISOU 5156 CB TYR B 369 20176 18726 17569 2350 -252 -1836 C
ATOM 5157 CG TYR B 369 -23.785 12.067 31.033 1.00166.26 C
ANISOU 5157 CG TYR B 369 22592 21051 19527 2714 -197 -1764 C
ATOM 5158 CD1 TYR B 369 -23.187 12.459 29.838 1.00168.00 C
ANISOU 5158 CD1 TYR B 369 22622 21519 19690 2883 -228 -1646 C
ATOM 5159 CD2 TYR B 369 -23.375 10.869 31.606 1.00170.31 C
ANISOU 5159 CD2 TYR B 369 23469 21404 19839 2889 -113 -1813 C
ATOM 5160 CE1 TYR B 369 -22.219 11.671 29.231 1.00170.15 C
ANISOU 5160 CE1 TYR B 369 23064 21875 19710 3217 -177 -1580 C
ATOM 5161 CE2 TYR B 369 -22.412 10.080 31.007 1.00167.94 C
ANISOU 5161 CE2 TYR B 369 23339 21184 19288 3220 -62 -1749 C
ATOM 5162 CZ TYR B 369 -21.837 10.483 29.822 1.00170.19 C
ANISOU 5162 CZ TYR B 369 23431 21714 19518 3383 -94 -1632 C
ATOM 5163 OH TYR B 369 -20.877 9.689 29.233 1.00159.58 O
ANISOU 5163 OH TYR B 369 22261 20451 17924 3715 -42 -1568 O
ATOM 5164 N ASN B 370 -27.417 10.737 31.941 1.00186.71 N
ANISOU 5164 N ASN B 370 25820 22852 22268 1977 -158 -2309 N
ATOM 5165 CA ASN B 370 -27.691 9.302 31.910 1.00180.31 C
ANISOU 5165 CA ASN B 370 25463 21803 21245 2060 -80 -2448 C
ATOM 5166 C ASN B 370 -28.829 8.899 30.968 1.00179.01 C
ANISOU 5166 C ASN B 370 25455 21501 21061 1903 -91 -2603 C
ATOM 5167 O ASN B 370 -28.937 7.708 30.650 1.00183.74 O
ANISOU 5167 O ASN B 370 26413 21943 21456 2017 -32 -2701 O
ATOM 5168 CB ASN B 370 -28.000 8.783 33.324 1.00172.48 C
ANISOU 5168 CB ASN B 370 24689 20566 20279 1957 -29 -2539 C
ATOM 5169 CG ASN B 370 -26.764 8.729 34.223 1.00171.45 C
ANISOU 5169 CG ASN B 370 24537 20527 20082 2184 7 -2407 C
ATOM 5170 OD1 ASN B 370 -25.640 8.545 33.756 1.00171.55 O
ANISOU 5170 OD1 ASN B 370 24530 20716 19936 2482 25 -2283 O
ATOM 5171 ND2 ASN B 370 -26.978 8.886 35.526 1.00168.34 N
ANISOU 5171 ND2 ASN B 370 24148 20008 19808 2044 18 -2436 N
ATOM 5172 N PHE B 371 -29.659 9.836 30.495 1.00172.41 N
ANISOU 5172 N PHE B 371 24363 20720 20425 1654 -166 -2626 N
ATOM 5173 CA PHE B 371 -30.917 9.508 29.818 1.00172.62 C
ANISOU 5173 CA PHE B 371 24537 20578 20472 1447 -179 -2793 C
ATOM 5174 C PHE B 371 -30.908 9.793 28.322 1.00176.48 C
ANISOU 5174 C PHE B 371 24896 21242 20917 1516 -224 -2756 C
ATOM 5175 O PHE B 371 -31.276 8.916 27.531 1.00182.85 O
ANISOU 5175 O PHE B 371 25968 21941 21567 1571 -197 -2858 O
ATOM 5176 CB PHE B 371 -32.080 10.260 30.489 1.00174.68 C
ANISOU 5176 CB PHE B 371 24650 20717 21002 1070 -226 -2882 C
ATOM 5177 CG PHE B 371 -32.510 9.668 31.800 1.00169.33 C
ANISOU 5177 CG PHE B 371 24215 19776 20347 952 -173 -2990 C
ATOM 5178 CD1 PHE B 371 -32.138 8.381 32.143 1.00165.02 C
ANISOU 5178 CD1 PHE B 371 24051 19070 19578 1142 -88 -3044 C
ATOM 5179 CD2 PHE B 371 -33.291 10.394 32.687 1.00158.18 C
ANISOU 5179 CD2 PHE B 371 22649 18276 19177 652 -208 -3036 C
ATOM 5180 CE1 PHE B 371 -32.530 7.828 33.351 1.00156.52 C
ANISOU 5180 CE1 PHE B 371 23199 17750 18520 1036 -37 -3141 C
ATOM 5181 CE2 PHE B 371 -33.686 9.848 33.893 1.00150.01 C
ANISOU 5181 CE2 PHE B 371 21838 16999 18160 546 -158 -3133 C
ATOM 5182 CZ PHE B 371 -33.304 8.560 34.226 1.00145.02 C
ANISOU 5182 CZ PHE B 371 21588 16209 17305 739 -72 -3186 C
ATOM 5183 N ALA B 372 -30.552 11.005 27.905 1.00167.46 N
ANISOU 5183 N ALA B 372 23352 20361 19914 1502 -293 -2618 N
ATOM 5184 CA ALA B 372 -30.612 10.981 26.449 1.00163.07 C
ANISOU 5184 CA ALA B 372 22765 19924 19270 1585 -320 -2612 C
ATOM 5185 C ALA B 372 -29.209 10.957 25.859 1.00168.20 C
ANISOU 5185 C ALA B 372 23329 20827 19752 1940 -305 -2437 C
ATOM 5186 O ALA B 372 -28.247 11.390 26.514 1.00174.19 O
ANISOU 5186 O ALA B 372 23922 21728 20537 2070 -302 -2296 O
ATOM 5187 CB ALA B 372 -31.357 12.198 25.900 1.00145.28 C
ANISOU 5187 CB ALA B 372 20165 17786 17251 1332 -410 -2604 C
ATOM 5188 N PRO B 373 -29.052 10.451 24.630 1.00167.42 N
ANISOU 5188 N PRO B 373 23343 20789 19479 2108 -297 -2443 N
ATOM 5189 CA PRO B 373 -27.761 10.586 23.940 1.00162.40 C
ANISOU 5189 CA PRO B 373 22576 20423 18706 2431 -293 -2268 C
ATOM 5190 C PRO B 373 -27.503 12.024 23.509 1.00164.03 C
ANISOU 5190 C PRO B 373 22315 20909 19100 2374 -374 -2121 C
ATOM 5191 O PRO B 373 -27.845 12.407 22.384 1.00160.43 O
ANISOU 5191 O PRO B 373 21730 20559 18666 2336 -420 -2120 O
ATOM 5192 CB PRO B 373 -27.902 9.649 22.733 1.00148.80 C
ANISOU 5192 CB PRO B 373 21117 18656 16765 2575 -267 -2343 C
ATOM 5193 CG PRO B 373 -29.110 8.793 23.027 1.00147.28 C
ANISOU 5193 CG PRO B 373 21261 18138 16560 2370 -238 -2560 C
ATOM 5194 CD PRO B 373 -30.012 9.642 23.860 1.00149.64 C
ANISOU 5194 CD PRO B 373 21371 18352 17134 2025 -285 -2614 C
ATOM 5195 N PHE B 374 -26.915 12.824 24.401 1.00161.63 N
ANISOU 5195 N PHE B 374 21756 20722 18933 2365 -393 -1998 N
ATOM 5196 CA PHE B 374 -26.660 14.241 24.148 1.00150.66 C
ANISOU 5196 CA PHE B 374 19910 19592 17742 2298 -471 -1855 C
ATOM 5197 C PHE B 374 -25.512 14.396 23.161 1.00152.44 C
ANISOU 5197 C PHE B 374 19995 20094 17831 2606 -474 -1689 C
ATOM 5198 O PHE B 374 -24.344 14.219 23.519 1.00146.28 O
ANISOU 5198 O PHE B 374 19213 19424 16943 2862 -438 -1564 O
ATOM 5199 CB PHE B 374 -26.350 14.964 25.453 1.00149.49 C
ANISOU 5199 CB PHE B 374 19559 19472 17770 2208 -486 -1779 C
ATOM 5200 CG PHE B 374 -27.440 14.853 26.461 1.00165.06 C
ANISOU 5200 CG PHE B 374 21655 21181 19880 1908 -483 -1934 C
ATOM 5201 CD1 PHE B 374 -28.654 15.482 26.254 1.00162.74 C
ANISOU 5201 CD1 PHE B 374 21229 20819 19783 1587 -542 -2031 C
ATOM 5202 CD2 PHE B 374 -27.268 14.100 27.603 1.00180.42 C
ANISOU 5202 CD2 PHE B 374 23854 22941 21754 1948 -420 -1985 C
ATOM 5203 CE1 PHE B 374 -29.667 15.382 27.181 1.00170.62 C
ANISOU 5203 CE1 PHE B 374 22341 21575 20911 1310 -538 -2173 C
ATOM 5204 CE2 PHE B 374 -28.278 13.991 28.524 1.00186.29 C
ANISOU 5204 CE2 PHE B 374 24715 23442 22625 1674 -415 -2127 C
ATOM 5205 CZ PHE B 374 -29.480 14.632 28.318 1.00183.72 C
ANISOU 5205 CZ PHE B 374 24253 23052 22499 1354 -474 -2221 C
ATOM 5206 N PHE B 375 -25.850 14.751 21.921 1.00162.62 N
ANISOU 5206 N PHE B 375 21160 21497 19129 2580 -518 -1686 N
ATOM 5207 CA PHE B 375 -24.841 14.930 20.883 1.00159.69 C
ANISOU 5207 CA PHE B 375 20648 21391 18634 2861 -524 -1532 C
ATOM 5208 C PHE B 375 -23.842 16.010 21.268 1.00154.57 C
ANISOU 5208 C PHE B 375 19620 21003 18109 2949 -558 -1330 C
ATOM 5209 O PHE B 375 -22.646 15.894 20.977 1.00147.40 O
ANISOU 5209 O PHE B 375 18670 20276 17061 3250 -533 -1185 O
ATOM 5210 CB PHE B 375 -25.516 15.274 19.554 1.00139.71 C
ANISOU 5210 CB PHE B 375 18016 18933 16134 2768 -574 -1571 C
ATOM 5211 CG PHE B 375 -26.381 14.175 19.007 1.00148.64 C
ANISOU 5211 CG PHE B 375 19522 19835 17120 2723 -541 -1758 C
ATOM 5212 CD1 PHE B 375 -25.988 13.463 17.889 1.00144.41 C
ANISOU 5212 CD1 PHE B 375 19155 19357 16357 2964 -512 -1750 C
ATOM 5213 CD2 PHE B 375 -27.590 13.858 19.606 1.00150.29 C
ANISOU 5213 CD2 PHE B 375 19912 19769 17421 2441 -538 -1941 C
ATOM 5214 CE1 PHE B 375 -26.783 12.455 17.378 1.00135.82 C
ANISOU 5214 CE1 PHE B 375 18410 18058 15136 2924 -484 -1922 C
ATOM 5215 CE2 PHE B 375 -28.387 12.851 19.102 1.00152.57 C
ANISOU 5215 CE2 PHE B 375 20544 19846 17581 2399 -509 -2112 C
ATOM 5216 CZ PHE B 375 -27.984 12.149 17.986 1.00147.93 C
ANISOU 5216 CZ PHE B 375 20121 19318 16767 2641 -483 -2104 C
ATOM 5217 N ALA B 376 -24.314 17.064 21.923 1.00138.43 N
ANISOU 5217 N ALA B 376 17294 18977 16325 2692 -616 -1316 N
ATOM 5218 CA ALA B 376 -23.467 18.147 22.399 1.00122.17 C
ANISOU 5218 CA ALA B 376 14864 17147 14410 2741 -655 -1134 C
ATOM 5219 C ALA B 376 -23.702 18.352 23.888 1.00115.78 C
ANISOU 5219 C ALA B 376 14046 16196 13749 2566 -653 -1170 C
ATOM 5220 O ALA B 376 -24.851 18.400 24.339 1.00110.99 O
ANISOU 5220 O ALA B 376 13504 15392 13275 2274 -670 -1316 O
ATOM 5221 CB ALA B 376 -23.745 19.443 21.633 1.00 98.03 C
ANISOU 5221 CB ALA B 376 11399 14300 11547 2601 -742 -1055 C
ATOM 5222 N PHE B 377 -22.606 18.462 24.652 1.00114.40 N
ANISOU 5222 N PHE B 377 13795 16122 13551 2750 -631 -1038 N
ATOM 5223 CA PHE B 377 -22.670 18.728 26.091 1.00104.17 C
ANISOU 5223 CA PHE B 377 12462 14723 12396 2614 -630 -1049 C
ATOM 5224 C PHE B 377 -21.403 19.510 26.454 1.00 99.63 C
ANISOU 5224 C PHE B 377 11580 14400 11873 2796 -651 -839 C
ATOM 5225 O PHE B 377 -20.427 18.973 26.983 1.00114.62 O
ANISOU 5225 O PHE B 377 13603 16314 13634 3034 -598 -769 O
ATOM 5226 CB PHE B 377 -22.792 17.448 26.917 1.00104.09 C
ANISOU 5226 CB PHE B 377 12879 14442 12228 2661 -549 -1175 C
ATOM 5227 CG PHE B 377 -23.453 17.650 28.257 1.00117.87 C
ANISOU 5227 CG PHE B 377 14640 15999 14144 2406 -554 -1262 C
ATOM 5228 CD1 PHE B 377 -22.834 18.389 29.253 1.00124.03 C
ANISOU 5228 CD1 PHE B 377 15186 16879 15060 2408 -576 -1146 C
ATOM 5229 CD2 PHE B 377 -24.694 17.092 28.521 1.00129.15 C
ANISOU 5229 CD2 PHE B 377 16321 17151 15598 2168 -538 -1459 C
ATOM 5230 CE1 PHE B 377 -23.443 18.574 30.486 1.00119.67 C
ANISOU 5230 CE1 PHE B 377 14651 16155 14664 2177 -581 -1226 C
ATOM 5231 CE2 PHE B 377 -25.308 17.271 29.750 1.00132.23 C
ANISOU 5231 CE2 PHE B 377 16729 17368 16145 1935 -541 -1538 C
ATOM 5232 CZ PHE B 377 -24.682 18.013 30.734 1.00119.65 C
ANISOU 5232 CZ PHE B 377 14901 15878 14684 1940 -562 -1421 C
ATOM 5233 N LYS B 378 -21.428 20.806 26.161 1.00101.64 N
ANISOU 5233 N LYS B 378 11426 14858 12335 2680 -730 -738 N
ATOM 5234 CA LYS B 378 -20.296 21.695 26.390 1.00102.95 C
ANISOU 5234 CA LYS B 378 11254 15283 12578 2830 -761 -533 C
ATOM 5235 C LYS B 378 -20.647 22.662 27.513 1.00 98.69 C
ANISOU 5235 C LYS B 378 10470 14725 12304 2582 -814 -523 C
ATOM 5236 O LYS B 378 -21.610 23.427 27.398 1.00 98.40 O
ANISOU 5236 O LYS B 378 10250 14668 12468 2297 -875 -581 O
ATOM 5237 CB LYS B 378 -19.940 22.459 25.115 1.00101.93 C
ANISOU 5237 CB LYS B 378 10828 15426 12475 2916 -812 -407 C
ATOM 5238 CG LYS B 378 -19.693 21.573 23.903 1.00115.56 C
ANISOU 5238 CG LYS B 378 12780 17177 13952 3141 -767 -423 C
ATOM 5239 CD LYS B 378 -19.632 22.397 22.625 1.00108.79 C
ANISOU 5239 CD LYS B 378 11625 16558 13151 3159 -825 -327 C
ATOM 5240 CE LYS B 378 -19.413 21.519 21.401 1.00107.83 C
ANISOU 5240 CE LYS B 378 11729 16461 12781 3380 -782 -346 C
ATOM 5241 NZ LYS B 378 -18.078 20.858 21.412 1.00 99.66 N
ANISOU 5241 NZ LYS B 378 10819 15522 11527 3746 -720 -230 N
ATOM 5242 N CYS B 379 -19.869 22.626 28.590 1.00106.68 N
ANISOU 5242 N CYS B 379 11479 15740 13314 2691 -790 -449 N
ATOM 5243 CA CYS B 379 -20.067 23.514 29.726 1.00114.41 C
ANISOU 5243 CA CYS B 379 12230 16710 14532 2488 -837 -427 C
ATOM 5244 C CYS B 379 -19.022 24.622 29.709 1.00115.99 C
ANISOU 5244 C CYS B 379 12021 17206 14843 2612 -889 -214 C
ATOM 5245 O CYS B 379 -17.864 24.394 29.344 1.00109.62 O
ANISOU 5245 O CYS B 379 11202 16562 13887 2916 -861 -82 O
ATOM 5246 CB CYS B 379 -19.993 22.741 31.044 1.00107.27 C
ANISOU 5246 CB CYS B 379 11604 15589 13567 2500 -777 -501 C
ATOM 5247 SG CYS B 379 -21.330 21.542 31.298 1.00129.43 S
ANISOU 5247 SG CYS B 379 14869 18022 16285 2305 -720 -759 S
ATOM 5248 N TYR B 380 -19.438 25.822 30.101 1.00114.83 N
ANISOU 5248 N TYR B 380 11539 17130 14962 2375 -966 -182 N
ATOM 5249 CA TYR B 380 -18.574 26.994 30.115 1.00117.63 C
ANISOU 5249 CA TYR B 380 11476 17761 15459 2450 -1026 13 C
ATOM 5250 C TYR B 380 -18.506 27.541 31.532 1.00122.52 C
ANISOU 5250 C TYR B 380 11966 18332 16253 2325 -1050 34 C
ATOM 5251 O TYR B 380 -19.542 27.818 32.146 1.00124.65 O
ANISOU 5251 O TYR B 380 12235 18442 16685 2029 -1076 -84 O
ATOM 5252 CB TYR B 380 -19.088 28.072 29.152 1.00124.87 C
ANISOU 5252 CB TYR B 380 12058 18842 16546 2288 -1105 51 C
ATOM 5253 CG TYR B 380 -19.283 27.590 27.730 1.00125.33 C
ANISOU 5253 CG TYR B 380 12233 18939 16447 2381 -1088 19 C
ATOM 5254 CD1 TYR B 380 -20.457 26.953 27.347 1.00125.76 C
ANISOU 5254 CD1 TYR B 380 12547 18781 16456 2206 -1069 -167 C
ATOM 5255 CD2 TYR B 380 -18.298 27.779 26.768 1.00122.31 C
ANISOU 5255 CD2 TYR B 380 11700 18806 15965 2644 -1090 176 C
ATOM 5256 CE1 TYR B 380 -20.642 26.512 26.051 1.00114.02 C
ANISOU 5256 CE1 TYR B 380 11169 17328 14826 2292 -1055 -199 C
ATOM 5257 CE2 TYR B 380 -18.476 27.342 25.467 1.00113.87 C
ANISOU 5257 CE2 TYR B 380 10739 17774 14752 2732 -1074 147 C
ATOM 5258 CZ TYR B 380 -19.650 26.709 25.115 1.00109.50 C
ANISOU 5258 CZ TYR B 380 10446 17006 14154 2556 -1058 -42 C
ATOM 5259 OH TYR B 380 -19.834 26.271 23.824 1.00108.49 O
ANISOU 5259 OH TYR B 380 10427 16912 13882 2643 -1044 -74 O
ATOM 5260 N GLY B 381 -17.287 27.689 32.052 1.00117.52 N
ANISOU 5260 N GLY B 381 16153 13709 14791 1102 -1630 -3609 N
ATOM 5261 CA GLY B 381 -17.078 28.190 33.391 1.00122.43 C
ANISOU 5261 CA GLY B 381 16864 14551 15104 1272 -1348 -3749 C
ATOM 5262 C GLY B 381 -17.288 27.184 34.502 1.00123.39 C
ANISOU 5262 C GLY B 381 17014 14727 15141 1474 -1430 -3910 C
ATOM 5263 O GLY B 381 -16.846 27.430 35.631 1.00119.75 O
ANISOU 5263 O GLY B 381 16642 14514 14343 1595 -1168 -3958 O
ATOM 5264 N VAL B 382 -17.952 26.063 34.227 1.00124.90 N
ANISOU 5264 N VAL B 382 17129 14677 15651 1496 -1791 -3954 N
ATOM 5265 CA VAL B 382 -18.162 25.009 35.208 1.00112.47 C
ANISOU 5265 CA VAL B 382 15396 13262 14076 1490 -1705 -3569 C
ATOM 5266 C VAL B 382 -17.602 23.708 34.642 1.00115.41 C
ANISOU 5266 C VAL B 382 15827 13427 14595 1281 -2120 -3502 C
ATOM 5267 O VAL B 382 -17.192 23.631 33.484 1.00124.03 O
ANISOU 5267 O VAL B 382 17039 14272 15816 1140 -2430 -3674 O
ATOM 5268 CB VAL B 382 -19.646 24.848 35.592 1.00104.59 C
ANISOU 5268 CB VAL B 382 14006 12317 13415 1525 -1506 -3066 C
ATOM 5269 CG1 VAL B 382 -20.190 26.146 36.173 1.00102.29 C
ANISOU 5269 CG1 VAL B 382 13664 12237 12964 1752 -1084 -3140 C
ATOM 5270 CG2 VAL B 382 -20.466 24.412 34.387 1.00112.65 C
ANISOU 5270 CG2 VAL B 382 14833 13003 14967 1338 -1829 -2854 C
ATOM 5271 N SER B 383 -17.590 22.677 35.485 1.00114.74 N
ANISOU 5271 N SER B 383 15638 13471 14487 1257 -2089 -3192 N
ATOM 5272 CA SER B 383 -17.071 21.374 35.096 1.00120.09 C
ANISOU 5272 CA SER B 383 16361 13972 15294 1071 -2464 -3098 C
ATOM 5273 C SER B 383 -18.198 20.355 35.094 1.00120.49 C
ANISOU 5273 C SER B 383 16061 13918 15803 956 -2569 -2550 C
ATOM 5274 O SER B 383 -18.890 20.207 36.112 1.00126.96 O
ANISOU 5274 O SER B 383 16647 14958 16633 1046 -2278 -2193 O
ATOM 5275 CB SER B 383 -15.952 20.933 36.040 1.00127.03 C
ANISOU 5275 CB SER B 383 17439 15068 15757 1120 -2391 -3214 C
ATOM 5276 OG SER B 383 -14.842 21.812 35.959 1.00127.74 O
ANISOU 5276 OG SER B 383 17828 15244 15463 1186 -2302 -3652 O
ATOM 5277 N PRO B 384 -18.426 19.643 33.987 1.00128.05 N
ANISOU 5277 N PRO B 384 16967 14542 17146 762 -2979 -2459 N
ATOM 5278 CA PRO B 384 -19.493 18.631 33.984 1.00128.52 C
ANISOU 5278 CA PRO B 384 16686 14481 17664 641 -3109 -1923 C
ATOM 5279 C PRO B 384 -19.180 17.427 34.853 1.00138.58 C
ANISOU 5279 C PRO B 384 17901 15872 18881 595 -3139 -1643 C
ATOM 5280 O PRO B 384 -20.109 16.809 35.388 1.00133.89 O
ANISOU 5280 O PRO B 384 16988 15329 18553 570 -3059 -1152 O
ATOM 5281 CB PRO B 384 -19.606 18.247 32.502 1.00136.33 C
ANISOU 5281 CB PRO B 384 17711 15068 19021 452 -3579 -1992 C
ATOM 5282 CG PRO B 384 -18.257 18.549 31.936 1.00138.72 C
ANISOU 5282 CG PRO B 384 18407 15307 18994 451 -3746 -2526 C
ATOM 5283 CD PRO B 384 -17.762 19.759 32.677 1.00134.64 C
ANISOU 5283 CD PRO B 384 18045 15091 18022 654 -3342 -2833 C
ATOM 5284 N THR B 385 -17.903 17.075 35.012 1.00148.43 N
ANISOU 5284 N THR B 385 19436 17162 19797 583 -3251 -1930 N
ATOM 5285 CA THR B 385 -17.548 15.951 35.872 1.00150.41 C
ANISOU 5285 CA THR B 385 19642 17533 19973 543 -3273 -1678 C
ATOM 5286 C THR B 385 -17.868 16.248 37.332 1.00141.32 C
ANISOU 5286 C THR B 385 18349 16769 18576 720 -2803 -1457 C
ATOM 5287 O THR B 385 -18.399 15.389 38.045 1.00139.79 O
ANISOU 5287 O THR B 385 17910 16668 18538 691 -2748 -1004 O
ATOM 5288 CB THR B 385 -16.067 15.609 35.707 1.00157.95 C
ANISOU 5288 CB THR B 385 20951 18457 20608 504 -3481 -2063 C
ATOM 5289 OG1 THR B 385 -15.273 16.757 36.028 1.00149.21 O
ANISOU 5289 OG1 THR B 385 20104 17553 19036 666 -3224 -2501 O
ATOM 5290 CG2 THR B 385 -15.775 15.179 34.278 1.00140.44 C
ANISOU 5290 CG2 THR B 385 18863 15856 18643 335 -3958 -2242 C
ATOM 5291 N LYS B 386 -17.551 17.457 37.794 1.00135.53 N
ANISOU 5291 N LYS B 386 17770 16266 17459 909 -2466 -1767 N
ATOM 5292 CA LYS B 386 -17.866 17.864 39.159 1.00133.40 C
ANISOU 5292 CA LYS B 386 17391 16370 16924 1106 -2003 -1595 C
ATOM 5293 C LYS B 386 -19.062 18.809 39.185 1.00132.96 C
ANISOU 5293 C LYS B 386 17110 16379 17031 1227 -1715 -1448 C
ATOM 5294 O LYS B 386 -18.970 19.924 39.711 1.00124.94 O
ANISOU 5294 O LYS B 386 16196 15584 15691 1425 -1374 -1675 O
ATOM 5295 CB LYS B 386 -16.646 18.523 39.813 1.00123.18 C
ANISOU 5295 CB LYS B 386 16436 15313 15054 1252 -1812 -2033 C
ATOM 5296 CG LYS B 386 -15.420 17.630 39.862 1.00122.49 C
ANISOU 5296 CG LYS B 386 16574 15186 14781 1147 -2070 -2181 C
ATOM 5297 CD LYS B 386 -14.241 18.332 40.509 1.00122.77 C
ANISOU 5297 CD LYS B 386 16935 15453 14261 1291 -1883 -2606 C
ATOM 5298 CE LYS B 386 -13.035 17.411 40.572 1.00123.44 C
ANISOU 5298 CE LYS B 386 17228 15499 14175 1185 -2138 -2730 C
ATOM 5299 NZ LYS B 386 -11.857 18.041 41.230 1.00113.74 N
ANISOU 5299 NZ LYS B 386 16311 14491 12413 1316 -1973 -3125 N
ATOM 5300 N LEU B 387 -20.189 18.373 38.623 1.00135.16 N
ANISOU 5300 N LEU B 387 17081 16458 17816 1112 -1856 -1066 N
ATOM 5301 CA LEU B 387 -21.378 19.213 38.542 1.00132.26 C
ANISOU 5301 CA LEU B 387 16478 16118 17658 1210 -1615 -900 C
ATOM 5302 C LEU B 387 -22.071 19.360 39.890 1.00130.16 C
ANISOU 5302 C LEU B 387 15978 16207 17268 1400 -1154 -544 C
ATOM 5303 O LEU B 387 -21.975 20.407 40.540 1.00132.61 O
ANISOU 5303 O LEU B 387 16389 16771 17226 1618 -782 -750 O
ATOM 5304 CB LEU B 387 -22.365 18.647 37.517 1.00127.46 C
ANISOU 5304 CB LEU B 387 15606 15176 17647 1018 -1931 -582 C
ATOM 5305 CG LEU B 387 -22.323 19.227 36.104 1.00131.27 C
ANISOU 5305 CG LEU B 387 16224 15344 18310 923 -2211 -913 C
ATOM 5306 CD1 LEU B 387 -23.241 18.444 35.179 1.00131.50 C
ANISOU 5306 CD1 LEU B 387 15997 15040 18928 718 -2566 -559 C
ATOM 5307 CD2 LEU B 387 -22.695 20.703 36.111 1.00106.45 C
ANISOU 5307 CD2 LEU B 387 13101 12317 15027 1104 -1886 -1135 C
ATOM 5308 N ASN B 388 -22.768 18.308 40.319 1.00122.66 N
ANISOU 5308 N ASN B 388 14720 15277 16608 1323 -1180 -4 N
ATOM 5309 CA ASN B 388 -23.596 18.357 41.517 1.00122.13 C
ANISOU 5309 CA ASN B 388 14375 15530 16501 1494 -755 416 C
ATOM 5310 C ASN B 388 -22.771 18.365 42.800 1.00132.34 C
ANISOU 5310 C ASN B 388 15845 17182 17256 1660 -469 308 C
ATOM 5311 O ASN B 388 -23.073 17.625 43.741 1.00122.59 O
ANISOU 5311 O ASN B 388 14410 16147 16022 1693 -319 725 O
ATOM 5312 CB ASN B 388 -24.576 17.179 41.526 1.00119.86 C
ANISOU 5312 CB ASN B 388 13689 15133 16717 1344 -902 1047 C
ATOM 5313 CG ASN B 388 -23.934 15.878 41.084 1.00114.80 C
ANISOU 5313 CG ASN B 388 13123 14262 16235 1106 -1359 1095 C
ATOM 5314 OD1 ASN B 388 -22.716 15.714 41.162 1.00111.41 O
ANISOU 5314 OD1 ASN B 388 13014 13856 15459 1090 -1474 736 O
ATOM 5315 ND2 ASN B 388 -24.754 14.943 40.616 1.00100.29 N
ANISOU 5315 ND2 ASN B 388 10985 12192 14929 922 -1628 1544 N
ATOM 5316 N ASP B 389 -21.733 19.204 42.852 1.00140.70 N
ANISOU 5316 N ASP B 389 17275 18326 17858 1766 -396 -240 N
ATOM 5317 CA ASP B 389 -20.952 19.406 44.063 1.00138.63 C
ANISOU 5317 CA ASP B 389 17208 18410 17054 1947 -106 -393 C
ATOM 5318 C ASP B 389 -21.038 20.820 44.616 1.00140.40 C
ANISOU 5318 C ASP B 389 17547 18879 16918 2217 311 -661 C
ATOM 5319 O ASP B 389 -20.690 21.026 45.783 1.00144.74 O
ANISOU 5319 O ASP B 389 18190 19758 17048 2406 623 -687 O
ATOM 5320 CB ASP B 389 -19.471 19.066 43.823 1.00131.42 C
ANISOU 5320 CB ASP B 389 16665 17413 15857 1843 -389 -810 C
ATOM 5321 CG ASP B 389 -19.255 17.612 43.443 1.00131.90 C
ANISOU 5321 CG ASP B 389 16644 17265 16207 1600 -783 -561 C
ATOM 5322 OD1 ASP B 389 -20.120 16.770 43.765 1.00140.37 O
ANISOU 5322 OD1 ASP B 389 17385 18353 17594 1542 -772 -29 O
ATOM 5323 OD2 ASP B 389 -18.212 17.313 42.824 1.00136.06 O
ANISOU 5323 OD2 ASP B 389 17439 17612 16647 1471 -1107 -894 O
ATOM 5324 N LEU B 390 -21.481 21.791 43.824 1.00139.35 N
ANISOU 5324 N LEU B 390 17418 18597 16932 2245 318 -862 N
ATOM 5325 CA LEU B 390 -21.651 23.165 44.269 1.00149.80 C
ANISOU 5325 CA LEU B 390 18835 20123 17960 2500 698 -1109 C
ATOM 5326 C LEU B 390 -23.130 23.526 44.295 1.00141.23 C
ANISOU 5326 C LEU B 390 17385 19068 17208 2592 940 -721 C
ATOM 5327 O LEU B 390 -23.998 22.749 43.888 1.00135.44 O
ANISOU 5327 O LEU B 390 16333 18179 16949 2443 790 -280 O
ATOM 5328 CB LEU B 390 -20.882 24.133 43.363 1.00153.10 C
ANISOU 5328 CB LEU B 390 19578 20356 18238 2478 532 -1700 C
ATOM 5329 CG LEU B 390 -19.371 23.913 43.296 1.00154.39 C
ANISOU 5329 CG LEU B 390 20116 20489 18057 2403 304 -2119 C
ATOM 5330 CD1 LEU B 390 -18.734 24.847 42.279 1.00149.01 C
ANISOU 5330 CD1 LEU B 390 19707 19598 17313 2366 122 -2648 C
ATOM 5331 CD2 LEU B 390 -18.745 24.102 44.670 1.00138.06 C
ANISOU 5331 CD2 LEU B 390 18213 18783 15460 2606 616 -2212 C
ATOM 5332 N CYS B 391 -23.408 24.732 44.775 1.00117.49 N
ANISOU 5332 N CYS B 391 14429 16259 13952 2842 1312 -892 N
ATOM 5333 CA CYS B 391 -24.765 25.236 44.913 1.00102.86 C
ANISOU 5333 CA CYS B 391 12254 14478 12350 2977 1603 -563 C
ATOM 5334 C CYS B 391 -24.951 26.485 44.060 1.00108.51 C
ANISOU 5334 C CYS B 391 13070 15028 13132 3023 1601 -925 C
ATOM 5335 O CYS B 391 -23.990 27.105 43.599 1.00121.03 O
ANISOU 5335 O CYS B 391 14994 16517 14475 3006 1458 -1449 O
ATOM 5336 CB CYS B 391 -25.084 25.545 46.378 1.00116.31 C
ANISOU 5336 CB CYS B 391 13888 16601 13702 3274 2103 -378 C
ATOM 5337 SG CYS B 391 -25.248 24.100 47.445 1.00127.14 S
ANISOU 5337 SG CYS B 391 15028 18197 15082 3247 2178 193 S
ATOM 5338 N PHE B 392 -26.214 26.855 43.855 1.00106.34 N
ANISOU 5338 N PHE B 392 12484 14723 13199 3081 1762 -624 N
ATOM 5339 CA PHE B 392 -26.549 28.031 43.066 1.00106.34 C
ANISOU 5339 CA PHE B 392 12530 14569 13307 3130 1781 -906 C
ATOM 5340 C PHE B 392 -27.793 28.688 43.644 1.00102.77 C
ANISOU 5340 C PHE B 392 11792 14310 12946 3363 2210 -602 C
ATOM 5341 O PHE B 392 -28.635 28.027 44.258 1.00106.26 O
ANISOU 5341 O PHE B 392 11908 14894 13572 3401 2382 -71 O
ATOM 5342 CB PHE B 392 -26.780 27.682 41.591 1.00105.54 C
ANISOU 5342 CB PHE B 392 12344 14055 13700 2846 1334 -892 C
ATOM 5343 CG PHE B 392 -25.599 27.034 40.931 1.00100.14 C
ANISOU 5343 CG PHE B 392 11934 13164 12949 2621 902 -1186 C
ATOM 5344 CD1 PHE B 392 -24.484 27.782 40.591 1.00 91.92 C
ANISOU 5344 CD1 PHE B 392 11280 12077 11567 2643 809 -1770 C
ATOM 5345 CD2 PHE B 392 -25.602 25.678 40.651 1.00 97.49 C
ANISOU 5345 CD2 PHE B 392 11465 12678 12898 2393 587 -871 C
ATOM 5346 CE1 PHE B 392 -23.393 27.189 39.988 1.00 87.72 C
ANISOU 5346 CE1 PHE B 392 10994 11364 10971 2449 425 -2029 C
ATOM 5347 CE2 PHE B 392 -24.515 25.080 40.047 1.00 95.65 C
ANISOU 5347 CE2 PHE B 392 11488 12257 12599 2201 196 -1143 C
ATOM 5348 CZ PHE B 392 -23.410 25.837 39.714 1.00 93.73 C
ANISOU 5348 CZ PHE B 392 11625 11980 12007 2233 121 -1720 C
ATOM 5349 N THR B 393 -27.897 30.002 43.440 1.00 97.82 N
ANISOU 5349 N THR B 393 11286 13686 12194 3524 2382 -939 N
ATOM 5350 CA THR B 393 -29.085 30.724 43.880 1.00110.83 C
ANISOU 5350 CA THR B 393 12674 15491 13945 3753 2782 -686 C
ATOM 5351 C THR B 393 -30.301 30.320 43.056 1.00107.82 C
ANISOU 5351 C THR B 393 11895 14877 14195 3589 2637 -239 C
ATOM 5352 O THR B 393 -31.350 29.968 43.607 1.00106.15 O
ANISOU 5352 O THR B 393 11327 14809 14197 3673 2875 283 O
ATOM 5353 CB THR B 393 -28.847 32.232 43.787 1.00120.65 C
ANISOU 5353 CB THR B 393 14163 16765 14916 3951 2963 -1184 C
ATOM 5354 OG1 THR B 393 -27.642 32.570 44.485 1.00128.22 O
ANISOU 5354 OG1 THR B 393 15508 17907 15303 4077 3042 -1616 O
ATOM 5355 CG2 THR B 393 -30.012 32.993 44.402 1.00111.28 C
ANISOU 5355 CG2 THR B 393 12731 15782 13769 4229 3418 -937 C
ATOM 5356 N ASN B 394 -30.175 30.362 41.732 1.00112.15 N
ANISOU 5356 N ASN B 394 14462 15026 13121 27 -867 -213 N
ATOM 5357 CA ASN B 394 -31.226 29.922 40.827 1.00102.97 C
ANISOU 5357 CA ASN B 394 13477 13604 12044 -62 -728 -316 C
ATOM 5358 C ASN B 394 -30.590 29.256 39.618 1.00 96.20 C
ANISOU 5358 C ASN B 394 12566 12794 11194 -7 -574 -300 C
ATOM 5359 O ASN B 394 -29.439 29.531 39.271 1.00103.26 O
ANISOU 5359 O ASN B 394 13268 13926 12039 6 -626 -231 O
ATOM 5360 CB ASN B 394 -32.119 31.086 40.371 1.00106.43 C
ANISOU 5360 CB ASN B 394 13949 13951 12537 -366 -880 -432 C
ATOM 5361 CG ASN B 394 -33.001 31.616 41.483 1.00110.19 C
ANISOU 5361 CG ASN B 394 14525 14319 13022 -424 -999 -468 C
ATOM 5362 OD1 ASN B 394 -34.041 31.036 41.795 1.00107.01 O
ANISOU 5362 OD1 ASN B 394 14316 13678 12666 -378 -894 -520 O
ATOM 5363 ND2 ASN B 394 -32.594 32.729 42.082 1.00 99.56 N
ANISOU 5363 ND2 ASN B 394 13046 13146 11636 -527 -1217 -445 N
ATOM 5364 N VAL B 395 -31.351 28.369 38.982 1.00 98.49 N
ANISOU 5364 N VAL B 395 13024 12852 11544 26 -381 -368 N
ATOM 5365 CA VAL B 395 -30.931 27.698 37.758 1.00 96.89 C
ANISOU 5365 CA VAL B 395 12800 12656 11357 65 -222 -375 C
ATOM 5366 C VAL B 395 -32.027 27.883 36.720 1.00 90.40 C
ANISOU 5366 C VAL B 395 12104 11629 10614 -140 -189 -518 C
ATOM 5367 O VAL B 395 -33.197 27.590 36.988 1.00 91.42 O
ANISOU 5367 O VAL B 395 12416 11517 10802 -165 -131 -602 O
ATOM 5368 CB VAL B 395 -30.645 26.201 37.988 1.00 92.78 C
ANISOU 5368 CB VAL B 395 12359 12065 10828 357 19 -310 C
ATOM 5369 CG1 VAL B 395 -30.278 25.525 36.676 1.00 82.22 C
ANISOU 5369 CG1 VAL B 395 11009 10722 9510 385 185 -330 C
ATOM 5370 CG2 VAL B 395 -29.532 26.024 39.011 1.00 81.11 C
ANISOU 5370 CG2 VAL B 395 10751 10806 9261 572 -17 -163 C
ATOM 5371 N TYR B 396 -31.652 28.375 35.543 1.00 85.11 N
ANISOU 5371 N TYR B 396 11332 11059 9945 -285 -226 -547 N
ATOM 5372 CA TYR B 396 -32.591 28.625 34.459 1.00 88.46 C
ANISOU 5372 CA TYR B 396 11854 11324 10432 -481 -207 -681 C
ATOM 5373 C TYR B 396 -32.336 27.637 33.330 1.00 88.28 C
ANISOU 5373 C TYR B 396 11858 11262 10422 -390 -1 -702 C
ATOM 5374 O TYR B 396 -31.186 27.425 32.933 1.00 93.72 O
ANISOU 5374 O TYR B 396 12405 12141 11063 -295 38 -615 O
ATOM 5375 CB TYR B 396 -32.470 30.061 33.947 1.00 81.65 C
ANISOU 5375 CB TYR B 396 10868 10597 9560 -736 -417 -707 C
ATOM 5376 CG TYR B 396 -32.721 31.106 35.010 1.00 90.48 C
ANISOU 5376 CG TYR B 396 11957 11756 10668 -842 -627 -695 C
ATOM 5377 CD1 TYR B 396 -34.015 31.455 35.377 1.00 99.12 C
ANISOU 5377 CD1 TYR B 396 13205 12645 11812 -964 -682 -792 C
ATOM 5378 CD2 TYR B 396 -31.665 31.746 35.645 1.00 92.60 C
ANISOU 5378 CD2 TYR B 396 12040 12268 10876 -822 -770 -591 C
ATOM 5379 CE1 TYR B 396 -34.250 32.410 36.348 1.00 94.82 C
ANISOU 5379 CE1 TYR B 396 12636 12134 11257 -1060 -871 -783 C
ATOM 5380 CE2 TYR B 396 -31.890 32.702 36.617 1.00106.29 C
ANISOU 5380 CE2 TYR B 396 13746 14039 12599 -920 -962 -587 C
ATOM 5381 CZ TYR B 396 -33.184 33.030 36.965 1.00106.49 C
ANISOU 5381 CZ TYR B 396 13931 13855 12674 -1037 -1011 -682 C
ATOM 5382 OH TYR B 396 -33.411 33.982 37.933 1.00108.39 O
ANISOU 5382 OH TYR B 396 14148 14132 12904 -1133 -1200 -680 O
ATOM 5383 N ALA B 397 -33.408 27.037 32.821 1.00 90.05 N
ANISOU 5383 N ALA B 397 12260 11241 10713 -418 131 -822 N
ATOM 5384 CA ALA B 397 -33.337 26.064 31.737 1.00 89.44 C
ANISOU 5384 CA ALA B 397 12232 11094 10658 -342 335 -866 C
ATOM 5385 C ALA B 397 -34.036 26.649 30.516 1.00 87.80 C
ANISOU 5385 C ALA B 397 12056 10820 10483 -571 291 -998 C
ATOM 5386 O ALA B 397 -35.269 26.735 30.481 1.00 85.46 O
ANISOU 5386 O ALA B 397 11906 10317 10246 -683 288 -1120 O
ATOM 5387 CB ALA B 397 -33.968 24.737 32.152 1.00 85.35 C
ANISOU 5387 CB ALA B 397 11896 10341 10192 -161 551 -901 C
ATOM 5388 N ASP B 398 -33.250 27.053 29.523 1.00 89.92 N
ANISOU 5388 N ASP B 398 12186 11266 10711 -635 258 -972 N
ATOM 5389 CA ASP B 398 -33.769 27.604 28.278 1.00 89.71 C
ANISOU 5389 CA ASP B 398 12176 11208 10702 -835 222 -1082 C
ATOM 5390 C ASP B 398 -33.794 26.513 27.216 1.00 89.54 C
ANISOU 5390 C ASP B 398 12222 11102 10698 -741 437 -1146 C
ATOM 5391 O ASP B 398 -32.789 25.830 26.999 1.00 87.33 O
ANISOU 5391 O ASP B 398 11864 10935 10381 -575 552 -1060 O
ATOM 5392 CB ASP B 398 -32.920 28.786 27.808 1.00 78.82 C
ANISOU 5392 CB ASP B 398 10606 10074 9269 -974 53 -1015 C
ATOM 5393 CG ASP B 398 -32.813 29.878 28.854 1.00 90.87 C
ANISOU 5393 CG ASP B 398 12051 11695 10779 -1067 -160 -954 C
ATOM 5394 OD1 ASP B 398 -33.735 29.995 29.689 1.00 83.41 O
ANISOU 5394 OD1 ASP B 398 11224 10596 9871 -1101 -210 -1004 O
ATOM 5395 OD2 ASP B 398 -31.809 30.621 28.843 1.00 96.03 O
ANISOU 5395 OD2 ASP B 398 12524 12576 11387 -1108 -276 -860 O
ATOM 5396 N SER B 399 -34.941 26.354 26.555 1.00 88.39 N
ANISOU 5396 N SER B 399 12220 10760 10605 -845 490 -1299 N
ATOM 5397 CA SER B 399 -35.139 25.296 25.575 1.00 86.17 C
ANISOU 5397 CA SER B 399 12023 10368 10348 -766 696 -1387 C
ATOM 5398 C SER B 399 -35.762 25.860 24.307 1.00 88.82 C
ANISOU 5398 C SER B 399 12380 10679 10687 -963 649 -1516 C
ATOM 5399 O SER B 399 -36.609 26.756 24.365 1.00 99.00 O
ANISOU 5399 O SER B 399 13709 11911 11996 -1147 504 -1588 O
ATOM 5400 CB SER B 399 -36.026 24.178 26.142 1.00 92.47 C
ANISOU 5400 CB SER B 399 13007 10906 11221 -648 863 -1464 C
ATOM 5401 OG SER B 399 -37.261 24.693 26.606 1.00104.24 O
ANISOU 5401 OG SER B 399 14609 12234 12765 -793 766 -1562 O
ATOM 5402 N PHE B 400 -35.339 25.328 23.166 1.00 84.97 N
ANISOU 5402 N PHE B 400 11869 10239 10179 -915 774 -1543 N
ATOM 5403 CA PHE B 400 -35.844 25.727 21.853 1.00 81.24 C
ANISOU 5403 CA PHE B 400 11414 9756 9698 -1071 754 -1664 C
ATOM 5404 C PHE B 400 -35.401 24.670 20.844 1.00 78.15 C
ANISOU 5404 C PHE B 400 11032 9367 9293 -941 957 -1697 C
ATOM 5405 O PHE B 400 -34.857 23.624 21.218 1.00 78.97 O
ANISOU 5405 O PHE B 400 11149 9450 9407 -740 1115 -1638 O
ATOM 5406 CB PHE B 400 -35.362 27.129 21.472 1.00 81.55 C
ANISOU 5406 CB PHE B 400 11307 10002 9678 -1240 554 -1600 C
ATOM 5407 CG PHE B 400 -33.886 27.335 21.658 1.00 83.47 C
ANISOU 5407 CG PHE B 400 11367 10488 9861 -1152 524 -1427 C
ATOM 5408 CD1 PHE B 400 -32.986 26.924 20.688 1.00 73.80 C
ANISOU 5408 CD1 PHE B 400 10056 9394 8590 -1072 630 -1387 C
ATOM 5409 CD2 PHE B 400 -33.399 27.946 22.802 1.00 84.30 C
ANISOU 5409 CD2 PHE B 400 11381 10696 9955 -1150 388 -1308 C
ATOM 5410 CE1 PHE B 400 -31.628 27.114 20.857 1.00 78.00 C
ANISOU 5410 CE1 PHE B 400 10413 10154 9071 -991 603 -1230 C
ATOM 5411 CE2 PHE B 400 -32.042 28.139 22.977 1.00 89.51 C
ANISOU 5411 CE2 PHE B 400 11864 11586 10562 -1070 357 -1156 C
ATOM 5412 CZ PHE B 400 -31.156 27.722 22.003 1.00 89.29 C
ANISOU 5412 CZ PHE B 400 11748 11685 10491 -992 466 -1116 C
ATOM 5413 N VAL B 401 -35.628 24.944 19.560 1.00 84.89 N
ANISOU 5413 N VAL B 401 11883 10249 10122 -1050 956 -1790 N
ATOM 5414 CA VAL B 401 -35.278 24.021 18.485 1.00 87.13 C
ANISOU 5414 CA VAL B 401 12179 10538 10389 -946 1139 -1839 C
ATOM 5415 C VAL B 401 -34.635 24.806 17.351 1.00 83.31 C
ANISOU 5415 C VAL B 401 11566 10260 9827 -1043 1062 -1806 C
ATOM 5416 O VAL B 401 -35.158 25.843 16.930 1.00 74.77 O
ANISOU 5416 O VAL B 401 10474 9206 8729 -1231 913 -1857 O
ATOM 5417 CB VAL B 401 -36.506 23.239 17.974 1.00 86.46 C
ANISOU 5417 CB VAL B 401 12272 10213 10368 -962 1268 -2040 C
ATOM 5418 CG1 VAL B 401 -36.277 22.735 16.556 1.00 75.24 C
ANISOU 5418 CG1 VAL B 401 10846 8833 8911 -934 1393 -2118 C
ATOM 5419 CG2 VAL B 401 -36.808 22.075 18.898 1.00 77.33 C
ANISOU 5419 CG2 VAL B 401 11232 8865 9286 -799 1426 -2053 C
ATOM 5420 N ILE B 402 -33.496 24.310 16.861 1.00 84.43 N
ANISOU 5420 N ILE B 402 11610 10548 9921 -909 1168 -1716 N
ATOM 5421 CA ILE B 402 -32.804 24.865 15.704 1.00 80.66 C
ANISOU 5421 CA ILE B 402 11014 10263 9371 -970 1134 -1682 C
ATOM 5422 C ILE B 402 -32.322 23.708 14.839 1.00 80.43 C
ANISOU 5422 C ILE B 402 11002 10235 9323 -809 1348 -1711 C
ATOM 5423 O ILE B 402 -32.440 22.537 15.204 1.00 85.34 O
ANISOU 5423 O ILE B 402 11715 10720 9990 -652 1513 -1743 O
ATOM 5424 CB ILE B 402 -31.618 25.768 16.105 1.00 82.05 C
ANISOU 5424 CB ILE B 402 10997 10681 9496 -988 1000 -1496 C
ATOM 5425 CG1 ILE B 402 -30.695 25.032 17.078 1.00 73.39 C
ANISOU 5425 CG1 ILE B 402 9842 9637 8406 -785 1081 -1362 C
ATOM 5426 CG2 ILE B 402 -32.112 27.071 16.710 1.00 76.46 C
ANISOU 5426 CG2 ILE B 402 10266 9986 8800 -1179 778 -1483 C
ATOM 5427 CD1 ILE B 402 -29.516 25.855 17.536 1.00 70.70 C
ANISOU 5427 CD1 ILE B 402 9305 9537 8020 -794 952 -1188 C
ATOM 5428 N ARG B 403 -31.773 24.048 13.676 1.00 90.50 N
ANISOU 5428 N ARG B 403 12190 11664 10532 -849 1349 -1698 N
ATOM 5429 CA ARG B 403 -31.201 23.033 12.805 1.00 97.27 C
ANISOU 5429 CA ARG B 403 13047 12550 11362 -698 1543 -1714 C
ATOM 5430 C ARG B 403 -29.792 22.668 13.269 1.00 99.38 C
ANISOU 5430 C ARG B 403 13179 12981 11601 -526 1603 -1531 C
ATOM 5431 O ARG B 403 -29.208 23.309 14.147 1.00102.73 O
ANISOU 5431 O ARG B 403 13493 13523 12019 -539 1480 -1393 O
ATOM 5432 CB ARG B 403 -31.189 23.509 11.353 1.00 85.32 C
ANISOU 5432 CB ARG B 403 11499 11137 9782 -798 1528 -1776 C
ATOM 5433 CG ARG B 403 -30.811 24.964 11.189 1.00 98.99 C
ANISOU 5433 CG ARG B 403 13096 13054 11463 -962 1330 -1681 C
ATOM 5434 CD ARG B 403 -30.732 25.372 9.728 1.00 99.16 C
ANISOU 5434 CD ARG B 403 13085 13180 11413 -1039 1334 -1729 C
ATOM 5435 NE ARG B 403 -29.542 24.839 9.076 1.00104.01 N
ANISOU 5435 NE ARG B 403 13598 13948 11974 -898 1463 -1640 N
ATOM 5436 CZ ARG B 403 -29.053 25.292 7.930 1.00110.93 C
ANISOU 5436 CZ ARG B 403 14394 14978 12776 -940 1461 -1617 C
ATOM 5437 NH1 ARG B 403 -29.624 26.294 7.283 1.00117.63 N
ANISOU 5437 NH1 ARG B 403 15249 15853 13591 -1116 1339 -1672 N
ATOM 5438 NH2 ARG B 403 -27.959 24.729 7.424 1.00119.08 N
ANISOU 5438 NH2 ARG B 403 15337 16142 13765 -798 1588 -1532 N
ATOM 5439 N GLY B 404 -29.244 21.617 12.654 1.00 85.82 N
ANISOU 5439 N GLY B 404 11468 11273 9866 -362 1796 -1535 N
ATOM 5440 CA GLY B 404 -27.990 21.057 13.136 1.00 88.93 C
ANISOU 5440 CA GLY B 404 11755 11794 10241 -169 1884 -1374 C
ATOM 5441 C GLY B 404 -26.818 22.012 13.021 1.00 91.49 C
ANISOU 5441 C GLY B 404 11871 12391 10499 -211 1760 -1211 C
ATOM 5442 O GLY B 404 -26.023 22.146 13.955 1.00 89.43 O
ANISOU 5442 O GLY B 404 11502 12242 10234 -134 1711 -1065 O
ATOM 5443 N ASN B 405 -26.691 22.688 11.878 1.00101.34 N
ANISOU 5443 N ASN B 405 13059 13752 11694 -331 1710 -1235 N
ATOM 5444 CA ASN B 405 -25.549 23.567 11.655 1.00 99.38 C
ANISOU 5444 CA ASN B 405 12610 13761 11388 -372 1613 -1084 C
ATOM 5445 C ASN B 405 -25.584 24.824 12.513 1.00 94.95 C
ANISOU 5445 C ASN B 405 11965 13272 10840 -527 1390 -1009 C
ATOM 5446 O ASN B 405 -24.605 25.578 12.513 1.00 93.97 O
ANISOU 5446 O ASN B 405 11664 13360 10680 -562 1302 -877 O
ATOM 5447 CB ASN B 405 -25.463 23.960 10.179 1.00105.50 C
ANISOU 5447 CB ASN B 405 13354 14627 12102 -459 1627 -1131 C
ATOM 5448 CG ASN B 405 -25.171 22.778 9.279 1.00137.99 C
ANISOU 5448 CG ASN B 405 17519 18719 16193 -296 1845 -1181 C
ATOM 5449 OD1 ASN B 405 -25.652 22.711 8.147 1.00147.87 O
ANISOU 5449 OD1 ASN B 405 18838 19932 17413 -349 1896 -1298 O
ATOM 5450 ND2 ASN B 405 -24.386 21.832 9.782 1.00145.47 N
ANISOU 5450 ND2 ASN B 405 18432 19690 17149 -92 1976 -1095 N
ATOM 5451 N GLU B 406 -26.673 25.069 13.238 1.00 90.23 N
ANISOU 5451 N GLU B 406 11484 12505 10295 -620 1302 -1093 N
ATOM 5452 CA GLU B 406 -26.803 26.255 14.072 1.00 87.94 C
ANISOU 5452 CA GLU B 406 11128 12265 10020 -771 1091 -1036 C
ATOM 5453 C GLU B 406 -26.533 25.981 15.544 1.00 86.22 C
ANISOU 5453 C GLU B 406 10890 12033 9837 -665 1063 -949 C
ATOM 5454 O GLU B 406 -26.562 26.918 16.347 1.00 87.65 O
ANISOU 5454 O GLU B 406 11009 12264 10030 -774 889 -896 O
ATOM 5455 CB GLU B 406 -28.199 26.864 13.904 1.00 90.97 C
ANISOU 5455 CB GLU B 406 11646 12485 10432 -959 990 -1181 C
ATOM 5456 CG GLU B 406 -28.450 27.433 12.518 1.00 91.53 C
ANISOU 5456 CG GLU B 406 11717 12604 10459 -1091 972 -1252 C
ATOM 5457 CD GLU B 406 -29.856 27.970 12.351 1.00 80.40 C
ANISOU 5457 CD GLU B 406 10443 11030 9074 -1262 879 -1400 C
ATOM 5458 OE1 GLU B 406 -30.743 27.566 13.131 1.00 89.16 O
ANISOU 5458 OE1 GLU B 406 11681 11954 10243 -1251 882 -1481 O
ATOM 5459 OE2 GLU B 406 -30.074 28.795 11.440 1.00 86.29 O
ANISOU 5459 OE2 GLU B 406 11168 11838 9780 -1404 806 -1434 O
ATOM 5460 N VAL B 407 -26.270 24.725 15.917 1.00 94.38 N
ANISOU 5460 N VAL B 407 11975 13000 10885 -451 1232 -933 N
ATOM 5461 CA VAL B 407 -25.937 24.412 17.304 1.00 82.60 C
ANISOU 5461 CA VAL B 407 10461 11509 9415 -326 1217 -838 C
ATOM 5462 C VAL B 407 -24.639 25.096 17.709 1.00 81.27 C
ANISOU 5462 C VAL B 407 10072 11604 9204 -312 1109 -668 C
ATOM 5463 O VAL B 407 -24.453 25.455 18.879 1.00 85.09 O
ANISOU 5463 O VAL B 407 10501 12130 9698 -301 998 -593 O
ATOM 5464 CB VAL B 407 -25.863 22.883 17.500 1.00 76.30 C
ANISOU 5464 CB VAL B 407 9763 10590 8637 -87 1441 -850 C
ATOM 5465 CG1 VAL B 407 -25.535 22.538 18.945 1.00 78.80 C
ANISOU 5465 CG1 VAL B 407 10063 10908 8971 57 1432 -747 C
ATOM 5466 CG2 VAL B 407 -27.172 22.232 17.081 1.00 77.28 C
ANISOU 5466 CG2 VAL B 407 10099 10449 8813 -115 1548 -1031 C
ATOM 5467 N SER B 408 -23.730 25.306 16.753 1.00 80.92 N
ANISOU 5467 N SER B 408 9894 11741 9111 -314 1136 -609 N
ATOM 5468 CA SER B 408 -22.482 26.000 17.045 1.00 80.69 C
ANISOU 5468 CA SER B 408 9643 11969 9046 -315 1035 -455 C
ATOM 5469 C SER B 408 -22.709 27.450 17.452 1.00 82.93 C
ANISOU 5469 C SER B 408 9852 12316 9342 -537 804 -442 C
ATOM 5470 O SER B 408 -21.838 28.044 18.097 1.00 84.38 O
ANISOU 5470 O SER B 408 9866 12681 9512 -542 695 -325 O
ATOM 5471 CB SER B 408 -21.551 25.939 15.833 1.00 88.65 C
ANISOU 5471 CB SER B 408 10534 13144 10005 -284 1123 -406 C
ATOM 5472 OG SER B 408 -22.130 26.580 14.710 1.00 91.97 O
ANISOU 5472 OG SER B 408 10998 13532 10416 -463 1087 -497 O
ATOM 5473 N GLN B 409 -23.853 28.035 17.090 1.00 84.98 N
ANISOU 5473 N GLN B 409 10231 12432 9625 -720 729 -562 N
ATOM 5474 CA GLN B 409 -24.154 29.405 17.483 1.00 89.64 C
ANISOU 5474 CA GLN B 409 10766 13062 10230 -933 515 -556 C
ATOM 5475 C GLN B 409 -24.567 29.522 18.943 1.00 83.73 C
ANISOU 5475 C GLN B 409 10059 12236 9518 -924 413 -546 C
ATOM 5476 O GLN B 409 -24.500 30.621 19.505 1.00 85.77 O
ANISOU 5476 O GLN B 409 10230 12572 9786 -1065 232 -508 O
ATOM 5477 CB GLN B 409 -25.257 29.984 16.595 1.00 83.56 C
ANISOU 5477 CB GLN B 409 10113 12166 9468 -1122 472 -686 C
ATOM 5478 CG GLN B 409 -24.915 30.019 15.119 1.00 85.09 C
ANISOU 5478 CG GLN B 409 10269 12443 9618 -1150 554 -699 C
ATOM 5479 CD GLN B 409 -25.901 30.846 14.320 1.00 95.81 C
ANISOU 5479 CD GLN B 409 11711 13718 10975 -1354 474 -807 C
ATOM 5480 OE1 GLN B 409 -26.512 31.778 14.842 1.00 91.99 O
ANISOU 5480 OE1 GLN B 409 11246 13187 10518 -1512 315 -829 O
ATOM 5481 NE2 GLN B 409 -26.064 30.506 13.047 1.00111.65 N
ANISOU 5481 NE2 GLN B 409 13769 15708 12946 -1346 585 -875 N
ATOM 5482 N ILE B 410 -24.995 28.426 19.568 1.00 73.48 N
ANISOU 5482 N ILE B 410 8892 10784 8243 -762 527 -581 N
ATOM 5483 CA ILE B 410 -25.368 28.446 20.977 1.00 84.70 C
ANISOU 5483 CA ILE B 410 10358 12129 9693 -730 446 -566 C
ATOM 5484 C ILE B 410 -24.095 28.362 21.810 1.00 87.02 C
ANISOU 5484 C ILE B 410 10478 12628 9956 -588 421 -413 C
ATOM 5485 O ILE B 410 -23.814 27.339 22.444 1.00 78.43 O
ANISOU 5485 O ILE B 410 9423 11513 8865 -375 537 -369 O
ATOM 5486 CB ILE B 410 -26.344 27.305 21.319 1.00 88.61 C
ANISOU 5486 CB ILE B 410 11066 12373 10229 -611 587 -662 C
ATOM 5487 CG1 ILE B 410 -27.422 27.191 20.240 1.00 83.76 C
ANISOU 5487 CG1 ILE B 410 10603 11583 9638 -721 650 -817 C
ATOM 5488 CG2 ILE B 410 -26.994 27.547 22.674 1.00 83.80 C
ANISOU 5488 CG2 ILE B 410 10527 11659 9654 -629 480 -668 C
ATOM 5489 CD1 ILE B 410 -28.265 28.439 20.080 1.00 80.90 C
ANISOU 5489 CD1 ILE B 410 10267 11180 9292 -972 470 -891 C
ATOM 5490 N ALA B 411 -23.316 29.440 21.802 1.00 87.94 N
ANISOU 5490 N ALA B 411 10407 12954 10052 -703 273 -333 N
ATOM 5491 CA ALA B 411 -22.038 29.498 22.495 1.00 90.02 C
ANISOU 5491 CA ALA B 411 10478 13444 10284 -590 232 -193 C
ATOM 5492 C ALA B 411 -21.652 30.960 22.656 1.00 98.87 C
ANISOU 5492 C ALA B 411 11434 14726 11405 -792 22 -151 C
ATOM 5493 O ALA B 411 -22.116 31.814 21.889 1.00 94.70 O
ANISOU 5493 O ALA B 411 10920 14169 10892 -996 -49 -210 O
ATOM 5494 CB ALA B 411 -20.952 28.729 21.725 1.00 87.63 C
ANISOU 5494 CB ALA B 411 10074 13279 9941 -427 392 -119 C
ATOM 5495 N PRO B 412 -20.823 31.286 23.647 1.00100.52 N
ANISOU 5495 N PRO B 412 11488 15106 11600 -742 -81 -53 N
ATOM 5496 CA PRO B 412 -20.427 32.686 23.841 1.00101.56 C
ANISOU 5496 CA PRO B 412 11456 15392 11740 -938 -280 -18 C
ATOM 5497 C PRO B 412 -19.668 33.231 22.638 1.00100.77 C
ANISOU 5497 C PRO B 412 11210 15448 11628 -1037 -266 20 C
ATOM 5498 O PRO B 412 -18.863 32.533 22.017 1.00 92.95 O
ANISOU 5498 O PRO B 412 10151 14558 10608 -899 -128 76 O
ATOM 5499 CB PRO B 412 -19.538 32.633 25.089 1.00 93.94 C
ANISOU 5499 CB PRO B 412 10345 14595 10752 -809 -352 81 C
ATOM 5500 CG PRO B 412 -19.971 31.399 25.808 1.00105.23 C
ANISOU 5500 CG PRO B 412 11928 15881 12172 -589 -232 71 C
ATOM 5501 CD PRO B 412 -20.333 30.419 24.733 1.00 94.82 C
ANISOU 5501 CD PRO B 412 10746 14426 10855 -507 -28 20 C
ATOM 5502 N GLY B 413 -19.939 34.491 22.314 1.00 96.82 N
ANISOU 5502 N GLY B 413 10668 14966 11154 -1277 -407 -10 N
ATOM 5503 CA GLY B 413 -19.232 35.176 21.246 1.00 99.33 C
ANISOU 5503 CA GLY B 413 10841 15434 11466 -1392 -410 32 C
ATOM 5504 C GLY B 413 -19.432 34.597 19.862 1.00100.35 C
ANISOU 5504 C GLY B 413 11058 15496 11575 -1362 -245 -7 C
ATOM 5505 O GLY B 413 -18.485 34.569 19.066 1.00 96.56 O
ANISOU 5505 O GLY B 413 10443 15174 11070 -1331 -174 62 O
ATOM 5506 N GLN B 414 -20.640 34.139 19.550 1.00103.27 N
ANISOU 5506 N GLN B 414 11647 15637 11952 -1371 -182 -119 N
ATOM 5507 CA GLN B 414 -20.955 33.587 18.242 1.00 92.97 C
ANISOU 5507 CA GLN B 414 10443 14256 10627 -1347 -30 -176 C
ATOM 5508 C GLN B 414 -21.852 34.544 17.468 1.00 96.60 C
ANISOU 5508 C GLN B 414 10982 14622 11100 -1574 -109 -261 C
ATOM 5509 O GLN B 414 -22.591 35.341 18.054 1.00100.08 O
ANISOU 5509 O GLN B 414 11474 14979 11574 -1722 -254 -306 O
ATOM 5510 CB GLN B 414 -21.641 32.222 18.367 1.00 95.81 C
ANISOU 5510 CB GLN B 414 10994 14425 10986 -1171 124 -251 C
ATOM 5511 CG GLN B 414 -20.760 31.134 18.955 1.00 99.55 C
ANISOU 5511 CG GLN B 414 11406 14979 11438 -921 238 -165 C
ATOM 5512 CD GLN B 414 -19.617 30.746 18.038 1.00 94.72 C
ANISOU 5512 CD GLN B 414 10661 14543 10787 -820 361 -86 C
ATOM 5513 OE1 GLN B 414 -19.708 30.886 16.818 1.00 98.26 O
ANISOU 5513 OE1 GLN B 414 11126 14988 11218 -892 421 -123 O
ATOM 5514 NE2 GLN B 414 -18.529 30.257 18.622 1.00106.93 N
ANISOU 5514 NE2 GLN B 414 12072 16245 12313 -647 400 25 N
ATOM 5515 N THR B 415 -21.776 34.460 16.144 1.00 92.48 N
ANISOU 5515 N THR B 415 10470 14120 10549 -1594 -10 -280 N
ATOM 5516 CA THR B 415 -22.600 35.256 15.249 1.00 89.18 C
ANISOU 5516 CA THR B 415 10133 13621 10130 -1783 -59 -360 C
ATOM 5517 C THR B 415 -23.489 34.339 14.417 1.00 95.86 C
ANISOU 5517 C THR B 415 11171 14295 10955 -1715 84 -479 C
ATOM 5518 O THR B 415 -23.338 33.115 14.418 1.00 94.64 O
ANISOU 5518 O THR B 415 11071 14098 10789 -1525 234 -492 O
ATOM 5519 CB THR B 415 -21.741 36.139 14.334 1.00 82.26 C
ANISOU 5519 CB THR B 415 9090 12933 9233 -1889 -81 -278 C
ATOM 5520 OG1 THR B 415 -20.881 35.313 13.538 1.00102.69 O
ANISOU 5520 OG1 THR B 415 11614 15626 11777 -1734 84 -227 O
ATOM 5521 CG2 THR B 415 -20.894 37.096 15.160 1.00 81.88 C
ANISOU 5521 CG2 THR B 415 8846 13049 9214 -1973 -227 -172 C
ATOM 5522 N GLY B 416 -24.422 34.949 13.700 1.00 91.77 N
ANISOU 5522 N GLY B 416 10755 13679 10434 -1870 39 -570 N
ATOM 5523 CA GLY B 416 -25.393 34.226 12.903 1.00 95.70 C
ANISOU 5523 CA GLY B 416 11437 14010 10915 -1834 152 -704 C
ATOM 5524 C GLY B 416 -26.812 34.627 13.251 1.00 92.08 C
ANISOU 5524 C GLY B 416 11142 13355 10490 -1964 53 -826 C
ATOM 5525 O GLY B 416 -27.070 35.381 14.188 1.00 97.31 O
ANISOU 5525 O GLY B 416 11787 13997 11191 -2068 -96 -807 O
ATOM 5526 N ASN B 417 -27.746 34.090 12.461 1.00 88.45 N
ANISOU 5526 N ASN B 417 10841 12751 10016 -1954 141 -958 N
ATOM 5527 CA ASN B 417 -29.153 34.446 12.631 1.00 79.85 C
ANISOU 5527 CA ASN B 417 9910 11474 8954 -2078 58 -1087 C
ATOM 5528 C ASN B 417 -29.664 34.065 14.015 1.00 86.18 C
ANISOU 5528 C ASN B 417 10788 12140 9815 -2034 17 -1113 C
ATOM 5529 O ASN B 417 -30.426 34.819 14.632 1.00 92.26 O
ANISOU 5529 O ASN B 417 11610 12826 10620 -2167 -122 -1149 O
ATOM 5530 CB ASN B 417 -30.000 33.782 11.546 1.00 94.15 C
ANISOU 5530 CB ASN B 417 11871 13164 10739 -2052 175 -1233 C
ATOM 5531 CG ASN B 417 -29.795 34.408 10.182 1.00 96.78 C
ANISOU 5531 CG ASN B 417 12155 13610 11008 -2136 180 -1227 C
ATOM 5532 OD1 ASN B 417 -29.423 35.577 10.072 1.00 90.42 O
ANISOU 5532 OD1 ASN B 417 11243 12922 10191 -2268 63 -1143 O
ATOM 5533 ND2 ASN B 417 -30.041 33.633 9.132 1.00 97.52 N
ANISOU 5533 ND2 ASN B 417 12327 13665 11060 -2056 319 -1318 N
ATOM 5534 N ILE B 418 -29.255 32.902 14.523 1.00 89.66 N
ANISOU 5534 N ILE B 418 11241 12558 10269 -1842 141 -1091 N
ATOM 5535 CA ILE B 418 -29.717 32.469 15.839 1.00 89.73 C
ANISOU 5535 CA ILE B 418 11327 12436 10330 -1780 118 -1108 C
ATOM 5536 C ILE B 418 -29.066 33.304 16.934 1.00 84.97 C
ANISOU 5536 C ILE B 418 10588 11956 9741 -1829 -35 -985 C
ATOM 5537 O ILE B 418 -29.742 33.807 17.839 1.00 85.46 O
ANISOU 5537 O ILE B 418 10703 11926 9840 -1915 -158 -1013 O
ATOM 5538 CB ILE B 418 -29.444 30.968 16.038 1.00 86.60 C
ANISOU 5538 CB ILE B 418 10986 11979 9941 -1551 308 -1114 C
ATOM 5539 CG1 ILE B 418 -30.190 30.149 14.985 1.00 82.78 C
ANISOU 5539 CG1 ILE B 418 10647 11356 9450 -1514 456 -1256 C
ATOM 5540 CG2 ILE B 418 -29.847 30.534 17.439 1.00 84.39 C
ANISOU 5540 CG2 ILE B 418 10780 11574 9712 -1475 290 -1115 C
ATOM 5541 CD1 ILE B 418 -31.686 30.359 14.998 1.00 70.09 C
ANISOU 5541 CD1 ILE B 418 9207 9542 7881 -1639 402 -1411 C
ATOM 5542 N ALA B 419 -27.744 33.472 16.863 1.00 83.90 N
ANISOU 5542 N ALA B 419 10269 12033 9575 -1776 -32 -852 N
ATOM 5543 CA ALA B 419 -27.030 34.166 17.928 1.00 83.69 C
ANISOU 5543 CA ALA B 419 10099 12138 9562 -1804 -168 -739 C
ATOM 5544 C ALA B 419 -27.346 35.657 17.951 1.00 90.12 C
ANISOU 5544 C ALA B 419 10867 12985 10391 -2039 -357 -739 C
ATOM 5545 O ALA B 419 -27.271 36.286 19.012 1.00 92.06 O
ANISOU 5545 O ALA B 419 11057 13258 10662 -2097 -495 -696 O
ATOM 5546 CB ALA B 419 -25.525 33.944 17.780 1.00 83.07 C
ANISOU 5546 CB ALA B 419 9828 12284 9449 -1688 -110 -604 C
ATOM 5547 N ASP B 420 -27.703 36.238 16.806 1.00 92.19 N
ANISOU 5547 N ASP B 420 11151 13242 10633 -2170 -364 -786 N
ATOM 5548 CA ASP B 420 -27.952 37.672 16.730 1.00 93.72 C
ANISOU 5548 CA ASP B 420 11300 13472 10840 -2390 -529 -778 C
ATOM 5549 C ASP B 420 -29.422 38.043 16.844 1.00 88.07 C
ANISOU 5549 C ASP B 420 10760 12553 10150 -2514 -605 -905 C
ATOM 5550 O ASP B 420 -29.739 39.098 17.402 1.00 92.36 O
ANISOU 5550 O ASP B 420 11284 13087 10721 -2667 -762 -897 O
ATOM 5551 CB ASP B 420 -27.405 38.240 15.415 1.00 86.07 C
ANISOU 5551 CB ASP B 420 10237 12635 9830 -2467 -501 -738 C
ATOM 5552 CG ASP B 420 -25.919 37.998 15.247 1.00 89.72 C
ANISOU 5552 CG ASP B 420 10510 13310 10269 -2361 -434 -608 C
ATOM 5553 OD1 ASP B 420 -25.201 37.956 16.268 1.00 96.04 O
ANISOU 5553 OD1 ASP B 420 11201 14200 11090 -2300 -482 -528 O
ATOM 5554 OD2 ASP B 420 -25.469 37.842 14.093 1.00 92.86 O
ANISOU 5554 OD2 ASP B 420 10868 13790 10625 -2335 -333 -589 O
ATOM 5555 N TYR B 421 -30.331 37.211 16.332 1.00 82.23 N
ANISOU 5555 N TYR B 421 10187 11652 9405 -2456 -496 -1024 N
ATOM 5556 CA TYR B 421 -31.737 37.579 16.253 1.00 88.38 C
ANISOU 5556 CA TYR B 421 11126 12249 10204 -2580 -560 -1152 C
ATOM 5557 C TYR B 421 -32.664 36.710 17.090 1.00 85.07 C
ANISOU 5557 C TYR B 421 10866 11629 9828 -2496 -520 -1247 C
ATOM 5558 O TYR B 421 -33.816 37.104 17.303 1.00 85.29 O
ANISOU 5558 O TYR B 421 11014 11508 9884 -2605 -598 -1343 O
ATOM 5559 CB TYR B 421 -32.216 37.546 14.791 1.00 87.47 C
ANISOU 5559 CB TYR B 421 11081 12107 10047 -2623 -486 -1237 C
ATOM 5560 CG TYR B 421 -31.465 38.479 13.864 1.00 91.68 C
ANISOU 5560 CG TYR B 421 11479 12818 10536 -2720 -522 -1152 C
ATOM 5561 CD1 TYR B 421 -30.840 39.622 14.349 1.00 85.30 C
ANISOU 5561 CD1 TYR B 421 10532 12134 9745 -2836 -660 -1043 C
ATOM 5562 CD2 TYR B 421 -31.384 38.217 12.501 1.00 78.15 C
ANISOU 5562 CD2 TYR B 421 9778 11147 8767 -2694 -415 -1184 C
ATOM 5563 CE1 TYR B 421 -30.153 40.475 13.505 1.00 86.83 C
ANISOU 5563 CE1 TYR B 421 10603 12483 9907 -2927 -683 -964 C
ATOM 5564 CE2 TYR B 421 -30.700 39.066 11.649 1.00 76.13 C
ANISOU 5564 CE2 TYR B 421 9403 11051 8471 -2777 -439 -1101 C
ATOM 5565 CZ TYR B 421 -30.087 40.193 12.157 1.00 83.23 C
ANISOU 5565 CZ TYR B 421 10165 12064 9393 -2894 -570 -989 C
ATOM 5566 OH TYR B 421 -29.405 41.041 11.314 1.00 84.69 O
ANISOU 5566 OH TYR B 421 10232 12401 9547 -2980 -584 -904 O
ATOM 5567 N ASN B 422 -32.210 35.554 17.575 1.00 85.27 N
ANISOU 5567 N ASN B 422 10593 11084 10720 -1311 247 -1048 N
ATOM 5568 CA ASN B 422 -33.090 34.623 18.276 1.00 85.88 C
ANISOU 5568 CA ASN B 422 10727 11138 10767 -1182 234 -971 C
ATOM 5569 C ASN B 422 -32.649 34.372 19.712 1.00 81.63 C
ANISOU 5569 C ASN B 422 10220 10636 10160 -1110 141 -995 C
ATOM 5570 O ASN B 422 -33.425 34.627 20.638 1.00 82.11 O
ANISOU 5570 O ASN B 422 10408 10641 10148 -1053 151 -952 O
ATOM 5571 CB ASN B 422 -33.177 33.306 17.496 1.00 80.53 C
ANISOU 5571 CB ASN B 422 9959 10482 10155 -1127 251 -934 C
ATOM 5572 CG ASN B 422 -33.848 33.474 16.147 1.00 79.49 C
ANISOU 5572 CG ASN B 422 9824 10310 10067 -1171 333 -905 C
ATOM 5573 OD1 ASN B 422 -35.053 33.268 16.012 1.00 76.42 O
ANISOU 5573 OD1 ASN B 422 9493 9861 9683 -1124 378 -840 O
ATOM 5574 ND2 ASN B 422 -33.069 33.856 15.141 1.00 78.75 N
ANISOU 5574 ND2 ASN B 422 9663 10253 10005 -1257 355 -956 N
ATOM 5575 N TYR B 423 -31.433 33.875 19.930 1.00 89.02 N
ANISOU 5575 N TYR B 423 11047 11665 11112 -1098 50 -1062 N
ATOM 5576 CA TYR B 423 -30.963 33.535 21.269 1.00 87.54 C
ANISOU 5576 CA TYR B 423 10889 11525 10846 -1004 -60 -1086 C
ATOM 5577 C TYR B 423 -29.477 33.842 21.359 1.00 80.21 C
ANISOU 5577 C TYR B 423 9830 10702 9944 -1065 -167 -1212 C
ATOM 5578 O TYR B 423 -28.674 33.238 20.642 1.00 71.26 O
ANISOU 5578 O TYR B 423 8546 9634 8895 -1078 -181 -1243 O
ATOM 5579 CB TYR B 423 -31.234 32.061 21.587 1.00 82.77 C
ANISOU 5579 CB TYR B 423 10286 10924 10237 -855 -66 -1006 C
ATOM 5580 CG TYR B 423 -30.934 31.673 23.015 1.00 82.48 C
ANISOU 5580 CG TYR B 423 10324 10923 10093 -726 -165 -1005 C
ATOM 5581 CD1 TYR B 423 -31.826 31.970 24.037 1.00 87.61 C
ANISOU 5581 CD1 TYR B 423 11149 11502 10636 -661 -138 -949 C
ATOM 5582 CD2 TYR B 423 -29.764 31.002 23.341 1.00 85.64 C
ANISOU 5582 CD2 TYR B 423 10624 11426 10491 -658 -284 -1059 C
ATOM 5583 CE1 TYR B 423 -31.557 31.615 25.345 1.00 89.54 C
ANISOU 5583 CE1 TYR B 423 11486 11777 10759 -529 -224 -944 C
ATOM 5584 CE2 TYR B 423 -29.487 30.642 24.645 1.00 88.11 C
ANISOU 5584 CE2 TYR B 423 11018 11775 10686 -519 -386 -1056 C
ATOM 5585 CZ TYR B 423 -30.386 30.951 25.643 1.00 90.38 C
ANISOU 5585 CZ TYR B 423 11499 11989 10853 -454 -354 -997 C
ATOM 5586 OH TYR B 423 -30.113 30.594 26.944 1.00 92.85 O
ANISOU 5586 OH TYR B 423 11917 12337 11026 -304 -452 -990 O
ATOM 5587 N LYS B 424 -29.114 34.771 22.241 1.00 86.10 N
ANISOU 5587 N LYS B 424 10627 11462 10624 -1102 -242 -1291 N
ATOM 5588 CA LYS B 424 -27.739 35.228 22.389 1.00 86.66 C
ANISOU 5588 CA LYS B 424 10564 11628 10733 -1180 -350 -1432 C
ATOM 5589 C LYS B 424 -27.221 34.868 23.774 1.00 94.11 C
ANISOU 5589 C LYS B 424 11534 12649 11574 -1058 -514 -1481 C
ATOM 5590 O LYS B 424 -27.890 35.131 24.779 1.00 95.80 O
ANISOU 5590 O LYS B 424 11919 12817 11662 -987 -533 -1450 O
ATOM 5591 CB LYS B 424 -27.635 36.740 22.167 1.00 82.05 C
ANISOU 5591 CB LYS B 424 10008 10994 10173 -1349 -306 -1514 C
ATOM 5592 CG LYS B 424 -26.239 37.305 22.378 1.00 74.26 C
ANISOU 5592 CG LYS B 424 8876 10096 9245 -1451 -412 -1678 C
ATOM 5593 CD LYS B 424 -25.219 36.610 21.490 1.00 83.66 C
ANISOU 5593 CD LYS B 424 9847 11376 10565 -1477 -417 -1716 C
ATOM 5594 CE LYS B 424 -23.825 37.178 21.695 1.00 86.46 C
ANISOU 5594 CE LYS B 424 10029 11820 11002 -1585 -517 -1890 C
ATOM 5595 NZ LYS B 424 -22.809 36.457 20.880 1.00 97.33 N
ANISOU 5595 NZ LYS B 424 11181 13289 12512 -1597 -514 -1927 N
ATOM 5596 N LEU B 425 -26.031 34.273 23.821 1.00 97.74 N
ANISOU 5596 N LEU B 425 11826 13228 12082 -1023 -630 -1557 N
ATOM 5597 CA LEU B 425 -25.329 33.961 25.058 1.00 87.92 C
ANISOU 5597 CA LEU B 425 10579 12082 10745 -902 -813 -1625 C
ATOM 5598 C LEU B 425 -24.251 35.001 25.333 1.00 98.30 C
ANISOU 5598 C LEU B 425 11782 13472 12098 -1029 -930 -1808 C
ATOM 5599 O LEU B 425 -23.541 35.418 24.411 1.00105.63 O
ANISOU 5599 O LEU B 425 12537 14425 13173 -1179 -890 -1888 O
ATOM 5600 CB LEU B 425 -24.686 32.575 24.988 1.00 90.11 C
ANISOU 5600 CB LEU B 425 10734 12448 11053 -758 -881 -1596 C
ATOM 5601 CG LEU B 425 -25.630 31.373 25.043 1.00 95.40 C
ANISOU 5601 CG LEU B 425 11526 13050 11671 -600 -798 -1429 C
ATOM 5602 CD1 LEU B 425 -24.848 30.073 24.935 1.00 86.82 C
ANISOU 5602 CD1 LEU B 425 10312 12048 10629 -466 -865 -1416 C
ATOM 5603 CD2 LEU B 425 -26.450 31.401 26.322 1.00 91.64 C
ANISOU 5603 CD2 LEU B 425 11281 12520 11020 -475 -822 -1362 C
ATOM 5604 N PRO B 426 -24.106 35.435 26.583 1.00106.21 N
ANISOU 5604 N PRO B 426 12879 14505 12970 -974 -1070 -1882 N
ATOM 5605 CA PRO B 426 -23.098 36.450 26.904 1.00104.13 C
ANISOU 5605 CA PRO B 426 12506 14310 12750 -1104 -1194 -2078 C
ATOM 5606 C PRO B 426 -21.687 35.894 26.775 1.00117.26 C
ANISOU 5606 C PRO B 426 13908 16128 14518 -1085 -1338 -2192 C
ATOM 5607 O PRO B 426 -21.461 34.687 26.675 1.00123.90 O
ANISOU 5607 O PRO B 426 14682 17033 15363 -937 -1371 -2120 O
ATOM 5608 CB PRO B 426 -23.421 36.824 28.352 1.00101.97 C
ANISOU 5608 CB PRO B 426 12430 14034 12280 -1004 -1318 -2114 C
ATOM 5609 CG PRO B 426 -24.081 35.607 28.907 1.00 99.40 C
ANISOU 5609 CG PRO B 426 12244 13705 11819 -772 -1320 -1955 C
ATOM 5610 CD PRO B 426 -24.869 35.016 27.771 1.00100.73 C
ANISOU 5610 CD PRO B 426 12406 13784 12084 -791 -1116 -1796 C
ATOM 5611 N ASP B 427 -20.720 36.815 26.783 1.00111.31 N
ANISOU 5611 N ASP B 427 13002 15429 13861 -1242 -1419 -2378 N
ATOM 5612 CA ASP B 427 -19.321 36.419 26.660 1.00113.97 C
ANISOU 5612 CA ASP B 427 13059 15919 14324 -1243 -1557 -2511 C
ATOM 5613 C ASP B 427 -18.821 35.713 27.915 1.00112.31 C
ANISOU 5613 C ASP B 427 12851 15844 13976 -1027 -1806 -2560 C
ATOM 5614 O ASP B 427 -17.979 34.812 27.823 1.00103.15 O
ANISOU 5614 O ASP B 427 11507 14807 12878 -920 -1906 -2582 O
ATOM 5615 CB ASP B 427 -18.455 37.641 26.354 1.00114.91 C
ANISOU 5615 CB ASP B 427 13008 16050 14602 -1484 -1565 -2708 C
ATOM 5616 CG ASP B 427 -18.788 38.271 25.013 1.00105.34 C
ANISOU 5616 CG ASP B 427 11780 14712 13534 -1685 -1312 -2656 C
ATOM 5617 OD1 ASP B 427 -19.581 37.675 24.254 1.00102.31 O
ANISOU 5617 OD1 ASP B 427 11481 14256 13136 -1631 -1153 -2482 O
ATOM 5618 OD2 ASP B 427 -18.258 39.364 24.720 1.00 97.36 O
ANISOU 5618 OD2 ASP B 427 10675 13669 12648 -1894 -1270 -2793 O
ATOM 5619 N ASP B 428 -19.321 36.100 29.087 1.00124.16 N
ANISOU 5619 N ASP B 428 14567 17324 15284 -947 -1906 -2574 N
ATOM 5620 CA ASP B 428 -18.941 35.483 30.357 1.00124.86 C
ANISOU 5620 CA ASP B 428 14708 17532 15201 -720 -2144 -2611 C
ATOM 5621 C ASP B 428 -19.954 34.437 30.803 1.00127.44 C
ANISOU 5621 C ASP B 428 15276 17799 15347 -488 -2083 -2395 C
ATOM 5622 O ASP B 428 -20.315 34.365 31.982 1.00134.05 O
ANISOU 5622 O ASP B 428 16321 18642 15969 -329 -2189 -2376 O
ATOM 5623 CB ASP B 428 -18.765 36.551 31.432 1.00128.63 C
ANISOU 5623 CB ASP B 428 15278 18032 15564 -766 -2305 -2780 C
ATOM 5624 CG ASP B 428 -20.016 37.386 31.638 1.00123.27 C
ANISOU 5624 CG ASP B 428 14879 17183 14774 -837 -2150 -2703 C
ATOM 5625 OD1 ASP B 428 -20.837 37.472 30.701 1.00109.99 O
ANISOU 5625 OD1 ASP B 428 13250 15370 13172 -931 -1912 -2567 O
ATOM 5626 OD2 ASP B 428 -20.176 37.958 32.737 1.00132.30 O
ANISOU 5626 OD2 ASP B 428 16192 18328 15749 -792 -2270 -2784 O
ATOM 5627 N PHE B 429 -20.424 33.609 29.874 1.00120.13 N
ANISOU 5627 N PHE B 429 14330 16810 14505 -464 -1906 -2234 N
ATOM 5628 CA PHE B 429 -21.460 32.633 30.184 1.00120.94 C
ANISOU 5628 CA PHE B 429 14651 16829 14470 -274 -1812 -2028 C
ATOM 5629 C PHE B 429 -20.922 31.556 31.118 1.00121.09 C
ANISOU 5629 C PHE B 429 14691 16959 14358 -8 -1994 -2008 C
ATOM 5630 O PHE B 429 -19.877 30.955 30.855 1.00121.32 O
ANISOU 5630 O PHE B 429 14502 17110 14483 46 -2105 -2070 O
ATOM 5631 CB PHE B 429 -21.988 32.008 28.893 1.00110.65 C
ANISOU 5631 CB PHE B 429 13293 15438 13310 -327 -1594 -1890 C
ATOM 5632 CG PHE B 429 -22.961 30.884 29.111 1.00104.06 C
ANISOU 5632 CG PHE B 429 12642 14518 12376 -144 -1492 -1691 C
ATOM 5633 CD1 PHE B 429 -24.223 31.133 29.623 1.00102.92 C
ANISOU 5633 CD1 PHE B 429 12754 14248 12104 -114 -1382 -1583 C
ATOM 5634 CD2 PHE B 429 -22.619 29.582 28.784 1.00 97.98 C
ANISOU 5634 CD2 PHE B 429 11787 13785 11656 -5 -1491 -1615 C
ATOM 5635 CE1 PHE B 429 -25.122 30.103 29.818 1.00102.25 C
ANISOU 5635 CE1 PHE B 429 12827 14074 11951 42 -1270 -1406 C
ATOM 5636 CE2 PHE B 429 -23.516 28.547 28.976 1.00 97.91 C
ANISOU 5636 CE2 PHE B 429 11948 13681 11573 152 -1381 -1438 C
ATOM 5637 CZ PHE B 429 -24.769 28.808 29.494 1.00100.22 C
ANISOU 5637 CZ PHE B 429 12486 13846 11747 170 -1268 -1334 C
ATOM 5638 N THR B 430 -21.633 31.320 32.216 1.00124.17 N
ANISOU 5638 N THR B 430 15348 17304 14526 166 -2019 -1919 N
ATOM 5639 CA THR B 430 -21.301 30.258 33.163 1.00122.90 C
ANISOU 5639 CA THR B 430 15270 17221 14204 448 -2165 -1864 C
ATOM 5640 C THR B 430 -22.470 29.274 33.171 1.00120.95 C
ANISOU 5640 C THR B 430 15239 16831 13884 586 -1966 -1629 C
ATOM 5641 O THR B 430 -23.496 29.512 33.816 1.00119.23 O
ANISOU 5641 O THR B 430 15280 16506 13517 629 -1872 -1539 O
ATOM 5642 CB THR B 430 -20.991 30.823 34.559 1.00124.24 C
ANISOU 5642 CB THR B 430 15578 17473 14156 554 -2386 -1979 C
ATOM 5643 OG1 THR B 430 -21.035 29.771 35.533 1.00128.56 O
ANISOU 5643 OG1 THR B 430 16299 18049 14497 856 -2473 -1870 O
ATOM 5644 CG2 THR B 430 -21.971 31.935 34.943 1.00125.42 C
ANISOU 5644 CG2 THR B 430 15945 17502 14207 437 -2284 -1982 C
ATOM 5645 N GLY B 431 -22.316 28.178 32.435 1.00109.37 N
ANISOU 5645 N GLY B 431 13663 15358 12536 647 -1889 -1535 N
ATOM 5646 CA GLY B 431 -23.373 27.188 32.342 1.00108.12 C
ANISOU 5646 CA GLY B 431 13680 15056 12345 758 -1692 -1326 C
ATOM 5647 C GLY B 431 -23.007 26.103 31.348 1.00112.14 C
ANISOU 5647 C GLY B 431 14017 15569 13023 784 -1623 -1268 C
ATOM 5648 O GLY B 431 -21.844 25.964 30.959 1.00111.07 O
ANISOU 5648 O GLY B 431 13647 15564 12992 777 -1753 -1378 O
ATOM 5649 N CYS B 432 -24.020 25.338 30.941 1.00106.06 N
ANISOU 5649 N CYS B 432 13361 14650 12286 812 -1412 -1102 N
ATOM 5650 CA CYS B 432 -23.844 24.234 30.009 1.00107.14 C
ANISOU 5650 CA CYS B 432 13374 14761 12573 842 -1320 -1035 C
ATOM 5651 C CYS B 432 -24.851 24.356 28.873 1.00114.49 C
ANISOU 5651 C CYS B 432 14295 15557 13649 657 -1092 -972 C
ATOM 5652 O CYS B 432 -25.993 24.774 29.086 1.00108.70 O
ANISOU 5652 O CYS B 432 13731 14708 12863 603 -967 -901 O
ATOM 5653 CB CYS B 432 -24.009 22.884 30.718 1.00100.63 C
ANISOU 5653 CB CYS B 432 12711 13885 11640 1109 -1303 -890 C
ATOM 5654 SG CYS B 432 -22.861 22.620 32.093 1.00123.84 S
ANISOU 5654 SG CYS B 432 15690 16985 14378 1377 -1584 -947 S
ATOM 5655 N VAL B 433 -24.418 23.998 27.666 1.00114.08 N
ANISOU 5655 N VAL B 433 14043 15525 13778 568 -1042 -1004 N
ATOM 5656 CA VAL B 433 -25.274 23.962 26.486 1.00 97.94 C
ANISOU 5656 CA VAL B 433 11976 13366 11869 415 -844 -951 C
ATOM 5657 C VAL B 433 -25.467 22.506 26.094 1.00 93.16 C
ANISOU 5657 C VAL B 433 11382 12687 11328 537 -744 -844 C
ATOM 5658 O VAL B 433 -24.488 21.772 25.910 1.00 94.48 O
ANISOU 5658 O VAL B 433 11422 12932 11544 635 -821 -874 O
ATOM 5659 CB VAL B 433 -24.677 24.769 25.322 1.00 96.03 C
ANISOU 5659 CB VAL B 433 11517 13192 11777 204 -845 -1076 C
ATOM 5660 CG1 VAL B 433 -25.478 24.524 24.051 1.00 79.75 C
ANISOU 5660 CG1 VAL B 433 9436 11024 9842 86 -656 -1018 C
ATOM 5661 CG2 VAL B 433 -24.655 26.245 25.665 1.00 93.65 C
ANISOU 5661 CG2 VAL B 433 11230 12928 11426 64 -907 -1174 C
ATOM 5662 N ILE B 434 -26.721 22.086 25.970 1.00 93.43 N
ANISOU 5662 N ILE B 434 11562 12566 11370 532 -572 -725 N
ATOM 5663 CA ILE B 434 -27.053 20.691 25.719 1.00 95.43 C
ANISOU 5663 CA ILE B 434 11859 12719 11682 647 -460 -619 C
ATOM 5664 C ILE B 434 -27.932 20.620 24.480 1.00 93.61 C
ANISOU 5664 C ILE B 434 11584 12385 11599 486 -292 -602 C
ATOM 5665 O ILE B 434 -28.912 21.364 24.367 1.00 92.03 O
ANISOU 5665 O ILE B 434 11452 12120 11398 365 -210 -587 O
ATOM 5666 CB ILE B 434 -27.763 20.050 26.926 1.00 99.31 C
ANISOU 5666 CB ILE B 434 12590 13104 12038 827 -405 -484 C
ATOM 5667 CG1 ILE B 434 -27.137 20.519 28.239 1.00 95.47 C
ANISOU 5667 CG1 ILE B 434 12192 12722 11362 960 -579 -511 C
ATOM 5668 CG2 ILE B 434 -27.662 18.553 26.852 1.00103.34 C
ANISOU 5668 CG2 ILE B 434 13132 13539 12595 986 -336 -394 C
ATOM 5669 CD1 ILE B 434 -27.777 19.897 29.461 1.00102.07 C
ANISOU 5669 CD1 ILE B 434 13288 13455 12040 1157 -519 -372 C
ATOM 5670 N ALA B 435 -27.588 19.728 23.554 1.00100.22 N
ANISOU 5670 N ALA B 435 12310 13210 12561 493 -244 -609 N
ATOM 5671 CA ALA B 435 -28.340 19.616 22.313 1.00 95.59 C
ANISOU 5671 CA ALA B 435 11674 12538 12108 349 -105 -610 C
ATOM 5672 C ALA B 435 -28.373 18.167 21.858 1.00 94.78 C
ANISOU 5672 C ALA B 435 11567 12350 12096 443 -17 -559 C
ATOM 5673 O ALA B 435 -27.413 17.419 22.065 1.00102.52 O
ANISOU 5673 O ALA B 435 12498 13381 13072 581 -84 -563 O
ATOM 5674 CB ALA B 435 -27.739 20.499 21.216 1.00 84.88 C
ANISOU 5674 CB ALA B 435 10140 11283 10827 180 -144 -730 C
ATOM 5675 N TRP B 436 -29.481 17.780 21.230 1.00 93.44 N
ANISOU 5675 N TRP B 436 11443 12047 12013 368 129 -518 N
ATOM 5676 CA TRP B 436 -29.610 16.435 20.697 1.00 92.73 C
ANISOU 5676 CA TRP B 436 11350 11856 12026 431 226 -484 C
ATOM 5677 C TRP B 436 -30.529 16.455 19.483 1.00 94.86 C
ANISOU 5677 C TRP B 436 11578 12048 12417 272 336 -517 C
ATOM 5678 O TRP B 436 -31.420 17.300 19.372 1.00 87.08 O
ANISOU 5678 O TRP B 436 10622 11040 11425 153 368 -519 O
ATOM 5679 CB TRP B 436 -30.128 15.458 21.760 1.00102.09 C
ANISOU 5679 CB TRP B 436 12711 12909 13168 594 303 -358 C
ATOM 5680 CG TRP B 436 -31.545 15.693 22.189 1.00 90.08 C
ANISOU 5680 CG TRP B 436 11326 11260 11641 538 423 -285 C
ATOM 5681 CD1 TRP B 436 -32.661 15.107 21.672 1.00 92.51 C
ANISOU 5681 CD1 TRP B 436 11663 11416 12071 470 578 -254 C
ATOM 5682 CD2 TRP B 436 -31.998 16.566 23.234 1.00 77.69 C
ANISOU 5682 CD2 TRP B 436 9873 9701 9944 548 403 -240 C
ATOM 5683 NE1 TRP B 436 -33.781 15.561 22.324 1.00 84.56 N
ANISOU 5683 NE1 TRP B 436 10770 10327 11032 436 660 -191 N
ATOM 5684 CE2 TRP B 436 -33.402 16.458 23.287 1.00 79.50 C
ANISOU 5684 CE2 TRP B 436 10193 9780 10232 487 561 -177 C
ATOM 5685 CE3 TRP B 436 -31.353 17.429 24.126 1.00 85.23 C
ANISOU 5685 CE3 TRP B 436 10862 10776 10745 602 266 -258 C
ATOM 5686 CZ2 TRP B 436 -34.173 17.180 24.196 1.00 88.52 C
ANISOU 5686 CZ2 TRP B 436 11462 10888 11282 485 599 -121 C
ATOM 5687 CZ3 TRP B 436 -32.123 18.146 25.029 1.00 92.98 C
ANISOU 5687 CZ3 TRP B 436 11984 11721 11624 599 296 -207 C
ATOM 5688 CH2 TRP B 436 -33.517 18.016 25.056 1.00 88.48 C
ANISOU 5688 CH2 TRP B 436 11506 10998 11112 544 468 -135 C
ATOM 5689 N ASN B 437 -30.291 15.511 18.574 1.00 98.58 N
ANISOU 5689 N ASN B 437 11981 12481 12995 280 386 -548 N
ATOM 5690 CA ASN B 437 -31.063 15.412 17.341 1.00 89.60 C
ANISOU 5690 CA ASN B 437 10798 11278 11966 144 472 -597 C
ATOM 5691 C ASN B 437 -32.462 14.884 17.631 1.00 88.28 C
ANISOU 5691 C ASN B 437 10746 10942 11855 134 597 -527 C
ATOM 5692 O ASN B 437 -32.628 13.866 18.311 1.00 85.39 O
ANISOU 5692 O ASN B 437 10473 10465 11507 252 667 -449 O
ATOM 5693 CB ASN B 437 -30.346 14.498 16.342 1.00 94.42 C
ANISOU 5693 CB ASN B 437 11316 11893 12666 170 490 -659 C
ATOM 5694 CG ASN B 437 -31.069 14.396 15.005 1.00 91.09 C
ANISOU 5694 CG ASN B 437 10853 11418 12341 37 562 -726 C
ATOM 5695 OD1 ASN B 437 -32.096 13.725 14.889 1.00 97.12 O
ANISOU 5695 OD1 ASN B 437 11679 12042 13180 20 655 -703 O
ATOM 5696 ND2 ASN B 437 -30.517 15.039 13.983 1.00 84.30 N
ANISOU 5696 ND2 ASN B 437 9887 10665 11479 -53 520 -816 N
ATOM 5697 N SER B 438 -33.466 15.577 17.104 1.00 83.90 N
ANISOU 5697 N SER B 438 10181 10365 11334 -6 631 -554 N
ATOM 5698 CA SER B 438 -34.871 15.236 17.281 1.00 87.28 C
ANISOU 5698 CA SER B 438 10682 10644 11836 -42 747 -507 C
ATOM 5699 C SER B 438 -35.562 15.099 15.932 1.00 88.98 C
ANISOU 5699 C SER B 438 10816 10822 12169 -168 784 -592 C
ATOM 5700 O SER B 438 -36.667 15.606 15.722 1.00 89.58 O
ANISOU 5700 O SER B 438 10893 10861 12284 -260 818 -600 O
ATOM 5701 CB SER B 438 -35.578 16.280 18.139 1.00 97.71 C
ANISOU 5701 CB SER B 438 12076 11971 13078 -70 747 -453 C
ATOM 5702 OG SER B 438 -35.474 17.561 17.543 1.00 83.86 O
ANISOU 5702 OG SER B 438 10252 10334 11278 -182 665 -520 O
ATOM 5703 N ASN B 439 -34.901 14.422 14.992 1.00 95.03 N
ANISOU 5703 N ASN B 439 11513 11607 12989 -163 772 -663 N
ATOM 5704 CA ASN B 439 -35.493 14.228 13.675 1.00 89.46 C
ANISOU 5704 CA ASN B 439 10742 10872 12377 -269 795 -756 C
ATOM 5705 C ASN B 439 -36.706 13.311 13.744 1.00 85.38 C
ANISOU 5705 C ASN B 439 10264 10182 11994 -287 906 -742 C
ATOM 5706 O ASN B 439 -37.642 13.462 12.951 1.00 89.93 O
ANISOU 5706 O ASN B 439 10797 10729 12644 -391 917 -808 O
ATOM 5707 CB ASN B 439 -34.452 13.665 12.708 1.00 88.10 C
ANISOU 5707 CB ASN B 439 10500 10752 12222 -247 767 -835 C
ATOM 5708 CG ASN B 439 -34.855 13.831 11.257 1.00 85.89 C
ANISOU 5708 CG ASN B 439 10158 10493 11984 -357 757 -944 C
ATOM 5709 OD1 ASN B 439 -35.491 14.819 10.887 1.00 80.72 O
ANISOU 5709 OD1 ASN B 439 9489 9883 11296 -449 722 -966 O
ATOM 5710 ND2 ASN B 439 -34.490 12.863 10.425 1.00 85.47 N
ANISOU 5710 ND2 ASN B 439 10078 10402 11996 -337 786 -1014 N
ATOM 5711 N LYS B 440 -36.715 12.369 14.689 1.00 88.56 N
ANISOU 5711 N LYS B 440 10750 10467 12432 -185 992 -658 N
ATOM 5712 CA LYS B 440 -37.848 11.462 14.825 1.00 94.05 C
ANISOU 5712 CA LYS B 440 11484 10979 13273 -209 1123 -642 C
ATOM 5713 C LYS B 440 -39.066 12.139 15.439 1.00 92.29 C
ANISOU 5713 C LYS B 440 11288 10710 13066 -269 1172 -592 C
ATOM 5714 O LYS B 440 -40.175 11.607 15.323 1.00 94.29 O
ANISOU 5714 O LYS B 440 11533 10828 13465 -331 1274 -608 O
ATOM 5715 CB LYS B 440 -37.454 10.250 15.672 1.00 93.28 C
ANISOU 5715 CB LYS B 440 11486 10753 13202 -71 1221 -555 C
ATOM 5716 CG LYS B 440 -36.346 9.399 15.076 1.00110.46 C
ANISOU 5716 CG LYS B 440 13634 12944 15389 3 1195 -603 C
ATOM 5717 CD LYS B 440 -36.003 8.230 15.986 1.00112.27 C
ANISOU 5717 CD LYS B 440 13980 13038 15638 158 1296 -503 C
ATOM 5718 CE LYS B 440 -34.918 7.353 15.382 1.00118.90 C
ANISOU 5718 CE LYS B 440 14791 13886 16500 243 1277 -552 C
ATOM 5719 NZ LYS B 440 -34.562 6.216 16.276 1.00129.38 N
ANISOU 5719 NZ LYS B 440 16244 15077 17839 414 1374 -445 N
ATOM 5720 N LEU B 441 -38.890 13.290 16.081 1.00 93.48 N
ANISOU 5720 N LEU B 441 11468 10968 13083 -256 1108 -540 N
ATOM 5721 CA LEU B 441 -39.971 13.970 16.787 1.00 90.32 C
ANISOU 5721 CA LEU B 441 11108 10525 12683 -293 1164 -482 C
ATOM 5722 C LEU B 441 -40.455 15.233 16.097 1.00 89.32 C
ANISOU 5722 C LEU B 441 10904 10505 12530 -404 1079 -547 C
ATOM 5723 O LEU B 441 -41.658 15.503 16.091 1.00 89.78 O
ANISOU 5723 O LEU B 441 10940 10503 12671 -471 1136 -550 O
ATOM 5724 CB LEU B 441 -39.529 14.324 18.213 1.00 89.77 C
ANISOU 5724 CB LEU B 441 11164 10474 12471 -178 1171 -364 C
ATOM 5725 CG LEU B 441 -39.139 13.172 19.141 1.00 84.54 C
ANISOU 5725 CG LEU B 441 10618 9699 11804 -35 1263 -269 C
ATOM 5726 CD1 LEU B 441 -38.655 13.709 20.478 1.00 79.55 C
ANISOU 5726 CD1 LEU B 441 10112 9118 10994 85 1233 -167 C
ATOM 5727 CD2 LEU B 441 -40.308 12.221 19.335 1.00 80.95 C
ANISOU 5727 CD2 LEU B 441 10202 9039 11516 -58 1448 -231 C
ATOM 5728 N ASP B 442 -39.551 16.018 15.512 1.00 93.69 N
ANISOU 5728 N ASP B 442 11413 11211 12976 -423 954 -599 N
ATOM 5729 CA ASP B 442 -39.884 17.340 14.998 1.00 96.44 C
ANISOU 5729 CA ASP B 442 11717 11657 13268 -508 879 -640 C
ATOM 5730 C ASP B 442 -39.838 17.412 13.475 1.00 91.12 C
ANISOU 5730 C ASP B 442 10949 11043 12630 -588 815 -754 C
ATOM 5731 O ASP B 442 -39.828 18.511 12.911 1.00 83.19 O
ANISOU 5731 O ASP B 442 9919 10136 11555 -644 743 -788 O
ATOM 5732 CB ASP B 442 -38.953 18.383 15.616 1.00 89.77 C
ANISOU 5732 CB ASP B 442 10915 10931 12262 -474 800 -604 C
ATOM 5733 CG ASP B 442 -39.082 18.450 17.129 1.00 87.69 C
ANISOU 5733 CG ASP B 442 10764 10619 11936 -390 850 -498 C
ATOM 5734 OD1 ASP B 442 -40.220 18.326 17.633 1.00 91.89 O
ANISOU 5734 OD1 ASP B 442 11338 11044 12531 -396 949 -449 O
ATOM 5735 OD2 ASP B 442 -38.050 18.619 17.814 1.00 91.64 O
ANISOU 5735 OD2 ASP B 442 11308 11186 12323 -315 792 -469 O
ATOM 5736 N SER B 443 -39.820 16.268 12.796 1.00 89.28 N
ANISOU 5736 N SER B 443 10677 10747 12499 -589 844 -813 N
ATOM 5737 CA SER B 443 -39.875 16.224 11.343 1.00 79.03 C
ANISOU 5737 CA SER B 443 9305 9493 11230 -655 788 -928 C
ATOM 5738 C SER B 443 -41.083 15.420 10.886 1.00 84.81 C
ANISOU 5738 C SER B 443 9994 10107 12123 -706 840 -989 C
ATOM 5739 O SER B 443 -41.509 14.470 11.549 1.00 98.84 O
ANISOU 5739 O SER B 443 11794 11750 14012 -681 940 -952 O
ATOM 5740 CB SER B 443 -38.603 15.615 10.745 1.00 83.24 C
ANISOU 5740 CB SER B 443 9822 10074 11732 -615 762 -975 C
ATOM 5741 OG SER B 443 -37.472 16.421 11.015 1.00 96.40 O
ANISOU 5741 OG SER B 443 11498 11862 13268 -584 704 -943 O
ATOM 5742 N LYS B 444 -41.631 15.823 9.742 1.00 81.99 N
ANISOU 5742 N LYS B 444 9577 9799 11777 -775 772 -1085 N
ATOM 5743 CA LYS B 444 -42.710 15.099 9.088 1.00 87.69 C
ANISOU 5743 CA LYS B 444 10235 10433 12651 -831 787 -1179 C
ATOM 5744 C LYS B 444 -42.497 15.163 7.582 1.00 83.17 C
ANISOU 5744 C LYS B 444 9624 9942 12034 -864 689 -1306 C
ATOM 5745 O LYS B 444 -41.810 16.048 7.071 1.00 78.57 O
ANISOU 5745 O LYS B 444 9062 9485 11305 -856 618 -1307 O
ATOM 5746 CB LYS B 444 -44.088 15.656 9.467 1.00 84.80 C
ANISOU 5746 CB LYS B 444 9830 10030 12362 -876 804 -1161 C
ATOM 5747 CG LYS B 444 -44.220 17.159 9.317 1.00 77.08 C
ANISOU 5747 CG LYS B 444 8858 9175 11254 -885 722 -1135 C
ATOM 5748 CD LYS B 444 -45.573 17.659 9.812 1.00 74.73 C
ANISOU 5748 CD LYS B 444 8520 8832 11043 -912 754 -1108 C
ATOM 5749 CE LYS B 444 -46.716 17.142 8.948 1.00 90.22 C
ANISOU 5749 CE LYS B 444 10370 10748 13161 -971 723 -1231 C
ATOM 5750 NZ LYS B 444 -48.050 17.569 9.468 1.00 83.58 N
ANISOU 5750 NZ LYS B 444 9465 9860 12431 -994 765 -1208 N
ATOM 5751 N VAL B 445 -43.116 14.209 6.882 1.00 75.64 N
ANISOU 5751 N VAL B 445 8619 8909 11211 -902 692 -1418 N
ATOM 5752 CA VAL B 445 -42.854 13.988 5.460 1.00 78.47 C
ANISOU 5752 CA VAL B 445 8960 9326 11528 -919 609 -1551 C
ATOM 5753 C VAL B 445 -43.188 15.231 4.645 1.00 97.08 C
ANISOU 5753 C VAL B 445 11308 11815 13764 -938 495 -1585 C
ATOM 5754 O VAL B 445 -42.407 15.659 3.788 1.00100.84 O
ANISOU 5754 O VAL B 445 11823 12393 14100 -919 439 -1617 O
ATOM 5755 CB VAL B 445 -43.639 12.757 4.970 1.00 68.51 C
ANISOU 5755 CB VAL B 445 7645 7942 10446 -965 630 -1676 C
ATOM 5756 CG1 VAL B 445 -43.535 12.606 3.461 1.00 83.07 C
ANISOU 5756 CG1 VAL B 445 9478 9852 12234 -981 528 -1830 C
ATOM 5757 CG2 VAL B 445 -43.142 11.493 5.674 1.00 69.13 C
ANISOU 5757 CG2 VAL B 445 7757 7880 10629 -933 756 -1638 C
ATOM 5758 N SER B 446 -44.348 15.835 4.903 1.00 95.45 N
ANISOU 5758 N SER B 446 11055 11602 13609 -969 469 -1573 N
ATOM 5759 CA SER B 446 -44.759 17.014 4.152 1.00106.13 C
ANISOU 5759 CA SER B 446 12406 13070 14849 -972 361 -1599 C
ATOM 5760 C SER B 446 -44.033 18.277 4.595 1.00 98.58 C
ANISOU 5760 C SER B 446 11522 12204 13729 -941 364 -1481 C
ATOM 5761 O SER B 446 -44.006 19.257 3.842 1.00113.50 O
ANISOU 5761 O SER B 446 13443 14192 15490 -932 289 -1494 O
ATOM 5762 CB SER B 446 -46.273 17.213 4.275 1.00124.49 C
ANISOU 5762 CB SER B 446 14642 15357 17300 -1006 331 -1633 C
ATOM 5763 OG SER B 446 -46.634 17.547 5.604 1.00 92.09 O
ANISOU 5763 OG SER B 446 10537 11198 13256 -1004 422 -1511 O
ATOM 5764 N GLY B 447 -43.427 18.271 5.779 1.00 85.86 N
ANISOU 5764 N GLY B 447 9946 10559 12116 -922 449 -1370 N
ATOM 5765 CA GLY B 447 -42.741 19.442 6.284 1.00 86.31 C
ANISOU 5765 CA GLY B 447 10065 10695 12034 -903 449 -1272 C
ATOM 5766 C GLY B 447 -43.332 19.952 7.581 1.00 82.02 C
ANISOU 5766 C GLY B 447 9532 10105 11526 -898 502 -1170 C
ATOM 5767 O GLY B 447 -44.515 20.303 7.636 1.00 85.32 O
ANISOU 5767 O GLY B 447 9913 10499 12008 -914 491 -1176 O
ATOM 5768 N ASN B 448 -42.521 19.988 8.638 1.00 76.22 N
ANISOU 5768 N ASN B 448 8849 9363 10750 -867 557 -1081 N
ATOM 5769 CA ASN B 448 -42.962 20.462 9.949 1.00 82.84 C
ANISOU 5769 CA ASN B 448 9722 10158 11595 -850 613 -981 C
ATOM 5770 C ASN B 448 -42.664 21.952 10.048 1.00 82.26 C
ANISOU 5770 C ASN B 448 9699 10174 11380 -855 570 -938 C
ATOM 5771 O ASN B 448 -41.539 22.354 10.353 1.00 82.17 O
ANISOU 5771 O ASN B 448 9734 10221 11268 -842 559 -906 O
ATOM 5772 CB ASN B 448 -42.277 19.687 11.069 1.00 84.69 C
ANISOU 5772 CB ASN B 448 10000 10334 11845 -799 686 -912 C
ATOM 5773 CG ASN B 448 -42.771 20.096 12.445 1.00 80.11 C
ANISOU 5773 CG ASN B 448 9476 9701 11261 -770 754 -810 C
ATOM 5774 OD1 ASN B 448 -43.883 20.602 12.592 1.00 81.53 O
ANISOU 5774 OD1 ASN B 448 9640 9850 11488 -794 775 -798 O
ATOM 5775 ND2 ASN B 448 -41.943 19.880 13.462 1.00 82.15 N
ANISOU 5775 ND2 ASN B 448 9804 9952 11458 -709 785 -738 N
ATOM 5776 N TYR B 449 -43.681 22.777 9.795 1.00 79.76 N
ANISOU 5776 N TYR B 449 9372 9866 11068 -873 546 -941 N
ATOM 5777 CA TYR B 449 -43.551 24.227 9.868 1.00 80.09 C
ANISOU 5777 CA TYR B 449 9472 9972 10987 -877 517 -899 C
ATOM 5778 C TYR B 449 -43.956 24.781 11.229 1.00 83.15 C
ANISOU 5778 C TYR B 449 9909 10312 11370 -856 578 -809 C
ATOM 5779 O TYR B 449 -44.408 25.931 11.320 1.00 75.32 O
ANISOU 5779 O TYR B 449 8954 9340 10324 -857 567 -780 O
ATOM 5780 CB TYR B 449 -44.364 24.881 8.750 1.00 78.49 C
ANISOU 5780 CB TYR B 449 9245 9808 10770 -888 451 -950 C
ATOM 5781 CG TYR B 449 -43.913 24.468 7.365 1.00 81.62 C
ANISOU 5781 CG TYR B 449 9620 10258 11133 -898 388 -1040 C
ATOM 5782 CD1 TYR B 449 -44.415 23.322 6.764 1.00 80.06 C
ANISOU 5782 CD1 TYR B 449 9348 10026 11046 -903 367 -1124 C
ATOM 5783 CD2 TYR B 449 -42.978 25.218 6.665 1.00 84.89 C
ANISOU 5783 CD2 TYR B 449 10095 10752 11409 -905 359 -1044 C
ATOM 5784 CE1 TYR B 449 -44.002 22.936 5.502 1.00 86.25 C
ANISOU 5784 CE1 TYR B 449 10127 10858 11786 -906 310 -1213 C
ATOM 5785 CE2 TYR B 449 -42.559 24.841 5.402 1.00 85.41 C
ANISOU 5785 CE2 TYR B 449 10157 10864 11431 -906 318 -1122 C
ATOM 5786 CZ TYR B 449 -43.074 23.700 4.825 1.00 84.18 C
ANISOU 5786 CZ TYR B 449 9936 10678 11371 -902 288 -1208 C
ATOM 5787 OH TYR B 449 -42.658 23.323 3.569 1.00 70.71 O
ANISOU 5787 OH TYR B 449 8241 9017 9609 -896 247 -1292 O
ATOM 5788 N ASN B 450 -43.798 23.990 12.293 1.00 79.85 N
ANISOU 5788 N ASN B 450 9509 9829 11002 -827 647 -762 N
ATOM 5789 CA ASN B 450 -44.169 24.437 13.630 1.00 78.56 C
ANISOU 5789 CA ASN B 450 9412 9617 10820 -796 714 -676 C
ATOM 5790 C ASN B 450 -43.096 25.313 14.265 1.00 82.07 C
ANISOU 5790 C ASN B 450 9945 10124 11115 -783 686 -637 C
ATOM 5791 O ASN B 450 -43.421 26.205 15.058 1.00 78.59 O
ANISOU 5791 O ASN B 450 9573 9671 10618 -770 712 -586 O
ATOM 5792 CB ASN B 450 -44.456 23.226 14.523 1.00 78.10 C
ANISOU 5792 CB ASN B 450 9357 9455 10863 -758 811 -634 C
ATOM 5793 CG ASN B 450 -44.572 23.595 15.990 1.00 74.65 C
ANISOU 5793 CG ASN B 450 9021 8972 10371 -707 887 -539 C
ATOM 5794 OD1 ASN B 450 -45.606 24.086 16.438 1.00 76.46 O
ANISOU 5794 OD1 ASN B 450 9260 9153 10638 -704 948 -504 O
ATOM 5795 ND2 ASN B 450 -43.507 23.354 16.747 1.00 75.96 N
ANISOU 5795 ND2 ASN B 450 9262 9155 10443 -658 881 -500 N
ATOM 5796 N TYR B 451 -41.829 25.087 13.932 1.00 79.39 N
ANISOU 5796 N TYR B 451 9601 9850 10716 -788 635 -668 N
ATOM 5797 CA TYR B 451 -40.718 25.806 14.539 1.00 79.31 C
ANISOU 5797 CA TYR B 451 9648 9900 10584 -783 601 -650 C
ATOM 5798 C TYR B 451 -40.286 26.956 13.640 1.00 77.55 C
ANISOU 5798 C TYR B 451 9423 9754 10286 -845 548 -693 C
ATOM 5799 O TYR B 451 -40.135 26.782 12.427 1.00 72.30 O
ANISOU 5799 O TYR B 451 8707 9125 9641 -875 521 -747 O
ATOM 5800 CB TYR B 451 -39.545 24.862 14.802 1.00 71.41 C
ANISOU 5800 CB TYR B 451 8630 8926 9576 -744 582 -660 C
ATOM 5801 CG TYR B 451 -39.878 23.775 15.794 1.00 80.96 C
ANISOU 5801 CG TYR B 451 9872 10049 10839 -669 646 -602 C
ATOM 5802 CD1 TYR B 451 -39.841 24.023 17.158 1.00 84.00 C
ANISOU 5802 CD1 TYR B 451 10351 10410 11154 -610 670 -534 C
ATOM 5803 CD2 TYR B 451 -40.245 22.505 15.368 1.00 85.16 C
ANISOU 5803 CD2 TYR B 451 10355 10515 11488 -654 690 -617 C
ATOM 5804 CE1 TYR B 451 -40.149 23.036 18.072 1.00 81.27 C
ANISOU 5804 CE1 TYR B 451 10058 9976 10845 -530 746 -470 C
ATOM 5805 CE2 TYR B 451 -40.556 21.510 16.276 1.00 84.71 C
ANISOU 5805 CE2 TYR B 451 10341 10360 11485 -586 771 -557 C
ATOM 5806 CZ TYR B 451 -40.506 21.782 17.628 1.00 81.96 C
ANISOU 5806 CZ TYR B 451 10096 9989 11058 -520 803 -477 C
ATOM 5807 OH TYR B 451 -40.814 20.799 18.541 1.00 83.18 O
ANISOU 5807 OH TYR B 451 10315 10037 11252 -440 900 -405 O
ATOM 5808 N LEU B 452 -40.085 28.126 14.240 1.00 78.32 N
ANISOU 5808 N LEU B 452 9591 9870 10298 -860 541 -669 N
ATOM 5809 CA LEU B 452 -39.747 29.339 13.514 1.00 79.14 C
ANISOU 5809 CA LEU B 452 9714 10022 10332 -920 514 -697 C
ATOM 5810 C LEU B 452 -38.430 29.911 14.023 1.00 82.93 C
ANISOU 5810 C LEU B 452 10217 10557 10735 -949 484 -716 C
ATOM 5811 O LEU B 452 -37.887 29.488 15.048 1.00 82.86 O
ANISOU 5811 O LEU B 452 10218 10556 10711 -911 468 -705 O
ATOM 5812 CB LEU B 452 -40.857 30.391 13.648 1.00 80.01 C
ANISOU 5812 CB LEU B 452 9888 10088 10425 -921 542 -661 C
ATOM 5813 CG LEU B 452 -42.295 29.945 13.377 1.00 75.43 C
ANISOU 5813 CG LEU B 452 9273 9451 9935 -886 570 -644 C
ATOM 5814 CD1 LEU B 452 -43.250 31.114 13.555 1.00 68.89 C
ANISOU 5814 CD1 LEU B 452 8504 8588 9082 -877 596 -609 C
ATOM 5815 CD2 LEU B 452 -42.427 29.347 11.987 1.00 82.16 C
ANISOU 5815 CD2 LEU B 452 10047 10332 10836 -900 534 -700 C
ATOM 5816 N TYR B 453 -37.920 30.891 13.279 1.00 77.18 N
ANISOU 5816 N TYR B 453 9498 9868 9960 -1015 476 -749 N
ATOM 5817 CA TYR B 453 -36.737 31.640 13.674 1.00 78.29 C
ANISOU 5817 CA TYR B 453 9649 10053 10044 -1067 454 -782 C
ATOM 5818 C TYR B 453 -36.827 33.029 13.061 1.00 78.20 C
ANISOU 5818 C TYR B 453 9698 10028 9985 -1136 485 -789 C
ATOM 5819 O TYR B 453 -37.507 33.241 12.053 1.00 78.15 O
ANISOU 5819 O TYR B 453 9708 10003 9982 -1137 511 -776 O
ATOM 5820 CB TYR B 453 -35.443 30.939 13.242 1.00 71.23 C
ANISOU 5820 CB TYR B 453 8657 9231 9176 -1082 427 -837 C
ATOM 5821 CG TYR B 453 -35.269 30.830 11.744 1.00 82.71 C
ANISOU 5821 CG TYR B 453 10068 10709 10649 -1118 454 -868 C
ATOM 5822 CD1 TYR B 453 -35.824 29.771 11.039 1.00 86.86 C
ANISOU 5822 CD1 TYR B 453 10557 11223 11225 -1073 459 -867 C
ATOM 5823 CD2 TYR B 453 -34.546 31.783 11.037 1.00 84.03 C
ANISOU 5823 CD2 TYR B 453 10239 10904 10783 -1198 482 -902 C
ATOM 5824 CE1 TYR B 453 -35.668 29.665 9.671 1.00 83.30 C
ANISOU 5824 CE1 TYR B 453 10082 10794 10772 -1096 479 -902 C
ATOM 5825 CE2 TYR B 453 -34.385 31.686 9.668 1.00 81.24 C
ANISOU 5825 CE2 TYR B 453 9869 10570 10430 -1219 520 -924 C
ATOM 5826 CZ TYR B 453 -34.948 30.624 8.991 1.00 94.49 C
ANISOU 5826 CZ TYR B 453 11518 12244 12140 -1163 511 -925 C
ATOM 5827 OH TYR B 453 -34.794 30.518 7.629 1.00 98.77 O
ANISOU 5827 OH TYR B 453 12058 12806 12663 -1174 543 -954 O
ATOM 5828 N ARG B 454 -36.133 33.978 13.680 1.00 78.81 N
ANISOU 5828 N ARG B 454 9814 10114 10018 -1189 479 -812 N
ATOM 5829 CA ARG B 454 -36.140 35.359 13.217 1.00 75.36 C
ANISOU 5829 CA ARG B 454 9450 9645 9538 -1259 523 -817 C
ATOM 5830 C ARG B 454 -35.048 35.541 12.170 1.00 77.17 C
ANISOU 5830 C ARG B 454 9622 9920 9779 -1336 548 -868 C
ATOM 5831 O ARG B 454 -33.873 35.269 12.437 1.00 79.57 O
ANISOU 5831 O ARG B 454 9844 10281 10107 -1374 520 -924 O
ATOM 5832 CB ARG B 454 -35.942 36.324 14.384 1.00 76.47 C
ANISOU 5832 CB ARG B 454 9666 9756 9633 -1290 515 -830 C
ATOM 5833 CG ARG B 454 -36.091 37.785 13.998 1.00 73.63 C
ANISOU 5833 CG ARG B 454 9404 9337 9236 -1357 576 -828 C
ATOM 5834 CD ARG B 454 -36.234 38.671 15.221 1.00 78.55 C
ANISOU 5834 CD ARG B 454 10123 9910 9812 -1368 571 -836 C
ATOM 5835 NE ARG B 454 -37.386 38.291 16.030 1.00 86.11 N
ANISOU 5835 NE ARG B 454 11133 10830 10754 -1268 567 -776 N
ATOM 5836 CZ ARG B 454 -38.627 38.702 15.805 1.00 81.16 C
ANISOU 5836 CZ ARG B 454 10579 10138 10122 -1220 618 -714 C
ATOM 5837 NH1 ARG B 454 -38.914 39.511 14.799 1.00 80.47 N
ANISOU 5837 NH1 ARG B 454 10535 10014 10027 -1248 668 -697 N
ATOM 5838 NH2 ARG B 454 -39.603 38.288 16.607 1.00 79.49 N
ANISOU 5838 NH2 ARG B 454 10397 9894 9913 -1134 626 -666 N
ATOM 5839 N LEU B 455 -35.439 35.999 10.982 1.00 79.79 N
ANISOU 5839 N LEU B 455 9998 10227 10090 -1350 602 -848 N
ATOM 5840 CA LEU B 455 -34.493 36.193 9.891 1.00 81.70 C
ANISOU 5840 CA LEU B 455 10208 10501 10334 -1416 653 -884 C
ATOM 5841 C LEU B 455 -33.975 37.622 9.805 1.00 80.01 C
ANISOU 5841 C LEU B 455 10067 10242 10091 -1512 724 -897 C
ATOM 5842 O LEU B 455 -32.819 37.829 9.420 1.00 89.56 O
ANISOU 5842 O LEU B 455 11221 11480 11328 -1594 768 -949 O
ATOM 5843 CB LEU B 455 -35.137 35.796 8.558 1.00 86.69 C
ANISOU 5843 CB LEU B 455 10860 11132 10944 -1366 676 -858 C
ATOM 5844 CG LEU B 455 -34.265 35.878 7.303 1.00 77.24 C
ANISOU 5844 CG LEU B 455 9651 9965 9733 -1412 744 -887 C
ATOM 5845 CD1 LEU B 455 -33.013 35.027 7.459 1.00 86.89 C
ANISOU 5845 CD1 LEU B 455 10738 11258 11020 -1444 732 -950 C
ATOM 5846 CD2 LEU B 455 -35.048 35.461 6.067 1.00 73.17 C
ANISOU 5846 CD2 LEU B 455 9177 9451 9173 -1342 746 -864 C
ATOM 5847 N PHE B 456 -34.795 38.608 10.163 1.00 71.11 N
ANISOU 5847 N PHE B 456 9060 9040 8920 -1505 745 -855 N
ATOM 5848 CA PHE B 456 -34.404 40.008 10.097 1.00 85.36 C
ANISOU 5848 CA PHE B 456 10954 10777 10700 -1594 825 -864 C
ATOM 5849 C PHE B 456 -34.710 40.700 11.417 1.00 76.39 C
ANISOU 5849 C PHE B 456 9882 9591 9551 -1605 797 -870 C
ATOM 5850 O PHE B 456 -35.673 40.359 12.109 1.00 82.10 O
ANISOU 5850 O PHE B 456 10632 10303 10259 -1519 747 -831 O
ATOM 5851 CB PHE B 456 -35.122 40.743 8.955 1.00 85.54 C
ANISOU 5851 CB PHE B 456 11103 10736 10662 -1567 905 -800 C
ATOM 5852 CG PHE B 456 -34.999 40.062 7.623 1.00 88.87 C
ANISOU 5852 CG PHE B 456 11491 11205 11069 -1533 926 -791 C
ATOM 5853 CD1 PHE B 456 -33.765 39.928 7.008 1.00 92.42 C
ANISOU 5853 CD1 PHE B 456 11877 11691 11546 -1612 987 -839 C
ATOM 5854 CD2 PHE B 456 -36.121 39.567 6.977 1.00 85.20 C
ANISOU 5854 CD2 PHE B 456 11057 10748 10565 -1423 886 -743 C
ATOM 5855 CE1 PHE B 456 -33.649 39.304 5.781 1.00 84.75 C
ANISOU 5855 CE1 PHE B 456 10892 10761 10550 -1575 1015 -833 C
ATOM 5856 CE2 PHE B 456 -36.012 38.944 5.748 1.00 78.68 C
ANISOU 5856 CE2 PHE B 456 10215 9968 9713 -1388 897 -746 C
ATOM 5857 CZ PHE B 456 -34.775 38.814 5.149 1.00 86.04 C
ANISOU 5857 CZ PHE B 456 11102 10932 10658 -1461 966 -788 C
ATOM 5858 N ARG B 457 -33.879 41.685 11.755 1.00 75.86 N
ANISOU 5858 N ARG B 457 9840 9487 9495 -1715 840 -925 N
ATOM 5859 CA ARG B 457 -34.068 42.486 12.956 1.00 83.00 C
ANISOU 5859 CA ARG B 457 10823 10334 10378 -1737 820 -948 C
ATOM 5860 C ARG B 457 -33.224 43.747 12.828 1.00 89.25 C
ANISOU 5860 C ARG B 457 11662 11059 11190 -1875 904 -1006 C
ATOM 5861 O ARG B 457 -32.190 43.748 12.156 1.00 88.27 O
ANISOU 5861 O ARG B 457 11457 10964 11119 -1965 952 -1054 O
ATOM 5862 CB ARG B 457 -33.690 41.706 14.222 1.00 86.67 C
ANISOU 5862 CB ARG B 457 11201 10872 10856 -1710 705 -1001 C
ATOM 5863 CG ARG B 457 -34.264 42.286 15.506 1.00 88.63 C
ANISOU 5863 CG ARG B 457 11556 11065 11053 -1682 675 -1003 C
ATOM 5864 CD ARG B 457 -33.918 41.423 16.710 1.00 81.52 C
ANISOU 5864 CD ARG B 457 10590 10242 10143 -1631 560 -1044 C
ATOM 5865 NE ARG B 457 -34.572 41.898 17.923 1.00 77.16 N
ANISOU 5865 NE ARG B 457 10160 9635 9523 -1583 540 -1037 N
ATOM 5866 CZ ARG B 457 -34.067 42.814 18.739 1.00 84.25 C
ANISOU 5866 CZ ARG B 457 11118 10501 10391 -1652 520 -1118 C
ATOM 5867 NH1 ARG B 457 -32.895 43.379 18.502 1.00 84.41 N
ANISOU 5867 NH1 ARG B 457 11075 10538 10460 -1783 515 -1218 N
ATOM 5868 NH2 ARG B 457 -34.754 43.170 19.820 1.00 82.00 N
ANISOU 5868 NH2 ARG B 457 10959 10165 10032 -1591 509 -1105 N
ATOM 5869 N LYS B 458 -33.682 44.822 13.477 1.00 85.47 N
ANISOU 5869 N LYS B 458 11316 10483 10676 -1893 935 -1004 N
ATOM 5870 CA LYS B 458 -32.973 46.095 13.377 1.00 88.81 C
ANISOU 5870 CA LYS B 458 11802 10816 11125 -2031 1029 -1062 C
ATOM 5871 C LYS B 458 -31.598 46.037 14.031 1.00 87.27 C
ANISOU 5871 C LYS B 458 11473 10681 11004 -2154 973 -1197 C
ATOM 5872 O LYS B 458 -30.658 46.677 13.547 1.00 88.80 O
ANISOU 5872 O LYS B 458 11636 10839 11265 -2289 1059 -1258 O
ATOM 5873 CB LYS B 458 -33.799 47.219 14.005 1.00 83.10 C
ANISOU 5873 CB LYS B 458 11258 9968 10349 -2015 1070 -1036 C
ATOM 5874 CG LYS B 458 -35.056 47.595 13.237 1.00 73.67 C
ANISOU 5874 CG LYS B 458 10202 8696 9094 -1908 1147 -911 C
ATOM 5875 CD LYS B 458 -35.483 49.017 13.578 1.00 76.74 C
ANISOU 5875 CD LYS B 458 10773 8933 9452 -1934 1237 -901 C
ATOM 5876 CE LYS B 458 -36.972 49.108 13.869 1.00 75.42 C
ANISOU 5876 CE LYS B 458 10712 8723 9220 -1780 1226 -808 C
ATOM 5877 NZ LYS B 458 -37.805 48.732 12.695 1.00101.31 N
ANISOU 5877 NZ LYS B 458 14002 12021 12471 -1665 1247 -700 N
ATOM 5878 N SER B 459 -31.457 45.288 15.122 1.00 86.41 N
ANISOU 5878 N SER B 459 11285 10661 10887 -2104 833 -1246 N
ATOM 5879 CA SER B 459 -30.187 45.202 15.827 1.00 84.40 C
ANISOU 5879 CA SER B 459 10897 10478 10694 -2198 749 -1382 C
ATOM 5880 C SER B 459 -30.037 43.806 16.412 1.00 84.92 C
ANISOU 5880 C SER B 459 10839 10679 10747 -2091 606 -1387 C
ATOM 5881 O SER B 459 -30.976 43.007 16.421 1.00 91.47 O
ANISOU 5881 O SER B 459 11704 11527 11523 -1957 580 -1291 O
ATOM 5882 CB SER B 459 -30.084 46.267 16.925 1.00 92.14 C
ANISOU 5882 CB SER B 459 11971 11387 11653 -2268 723 -1470 C
ATOM 5883 OG SER B 459 -31.083 46.080 17.913 1.00 92.59 O
ANISOU 5883 OG SER B 459 12138 11432 11609 -2142 653 -1422 O
ATOM 5884 N LYS B 460 -28.834 43.519 16.901 1.00 82.26 N
ANISOU 5884 N LYS B 460 10352 10433 10469 -2150 514 -1505 N
ATOM 5885 CA LYS B 460 -28.572 42.236 17.531 1.00 87.31 C
ANISOU 5885 CA LYS B 460 10882 11198 11094 -2040 374 -1515 C
ATOM 5886 C LYS B 460 -29.251 42.161 18.896 1.00 87.97 C
ANISOU 5886 C LYS B 460 11079 11275 11071 -1937 274 -1504 C
ATOM 5887 O LYS B 460 -29.574 43.175 19.520 1.00 91.43 O
ANISOU 5887 O LYS B 460 11646 11632 11461 -1977 287 -1536 O
ATOM 5888 CB LYS B 460 -27.068 42.006 17.683 1.00 92.67 C
ANISOU 5888 CB LYS B 460 11362 11982 11867 -2120 294 -1650 C
ATOM 5889 CG LYS B 460 -26.316 41.885 16.368 1.00 85.74 C
ANISOU 5889 CG LYS B 460 10352 11124 11101 -2207 400 -1660 C
ATOM 5890 CD LYS B 460 -24.835 41.642 16.606 1.00 91.76 C
ANISOU 5890 CD LYS B 460 10897 11997 11972 -2280 319 -1801 C
ATOM 5891 CE LYS B 460 -24.084 41.472 15.295 1.00104.84 C
ANISOU 5891 CE LYS B 460 12420 13672 13744 -2359 445 -1808 C
ATOM 5892 NZ LYS B 460 -22.624 41.272 15.512 1.00116.11 N
ANISOU 5892 NZ LYS B 460 13611 15206 15299 -2433 375 -1952 N
ATOM 5893 N LEU B 461 -29.466 40.933 19.357 1.00 82.97 N
ANISOU 5893 N LEU B 461 10408 10719 10398 -1798 186 -1457 N
ATOM 5894 CA LEU B 461 -30.093 40.713 20.651 1.00 80.79 C
ANISOU 5894 CA LEU B 461 10245 10439 10012 -1682 106 -1434 C
ATOM 5895 C LEU B 461 -29.077 40.842 21.776 1.00 93.92 C
ANISOU 5895 C LEU B 461 11859 12179 11648 -1697 -42 -1568 C
ATOM 5896 O LEU B 461 -27.928 40.407 21.651 1.00 99.20 O
ANISOU 5896 O LEU B 461 12356 12949 12386 -1729 -122 -1652 O
ATOM 5897 CB LEU B 461 -30.743 39.331 20.709 1.00 76.45 C
ANISOU 5897 CB LEU B 461 9687 9926 9434 -1526 88 -1326 C
ATOM 5898 CG LEU B 461 -32.153 39.173 20.144 1.00 84.69 C
ANISOU 5898 CG LEU B 461 10829 10884 10466 -1465 201 -1193 C
ATOM 5899 CD1 LEU B 461 -32.651 37.763 20.396 1.00 80.65 C
ANISOU 5899 CD1 LEU B 461 10296 10406 9940 -1323 174 -1111 C
ATOM 5900 CD2 LEU B 461 -33.095 40.188 20.765 1.00 79.06 C
ANISOU 5900 CD2 LEU B 461 10293 10068 9679 -1460 252 -1167 C
ATOM 5901 N LYS B 462 -29.509 41.449 22.878 1.00 98.04 N
ANISOU 5901 N LYS B 462 12530 12654 12066 -1666 -81 -1592 N
ATOM 5902 CA LYS B 462 -28.738 41.413 24.104 1.00 91.57 C
ANISOU 5902 CA LYS B 462 11696 11914 11181 -1635 -246 -1709 C
ATOM 5903 C LYS B 462 -28.688 39.980 24.630 1.00 91.82 C
ANISOU 5903 C LYS B 462 11687 12044 11157 -1461 -344 -1651 C
ATOM 5904 O LYS B 462 -29.523 39.148 24.267 1.00 92.95 O
ANISOU 5904 O LYS B 462 11863 12160 11292 -1363 -268 -1514 O
ATOM 5905 CB LYS B 462 -29.358 42.340 25.146 1.00101.40 C
ANISOU 5905 CB LYS B 462 13144 13076 12307 -1622 -250 -1736 C
ATOM 5906 CG LYS B 462 -29.410 43.802 24.733 1.00100.61 C
ANISOU 5906 CG LYS B 462 13108 12862 12259 -1787 -150 -1797 C
ATOM 5907 CD LYS B 462 -30.494 44.548 25.495 1.00111.33 C
ANISOU 5907 CD LYS B 462 14698 14103 13498 -1737 -93 -1758 C
ATOM 5908 CE LYS B 462 -30.344 44.370 26.997 1.00114.67 C
ANISOU 5908 CE LYS B 462 15212 14580 13777 -1634 -240 -1827 C
ATOM 5909 NZ LYS B 462 -31.479 44.982 27.742 1.00116.74 N
ANISOU 5909 NZ LYS B 462 15711 14727 13916 -1564 -165 -1775 N
ATOM 5910 N PRO B 463 -27.704 39.660 25.469 1.00 90.15 N
ANISOU 5910 N PRO B 463 11401 11945 10909 -1417 -515 -1758 N
ATOM 5911 CA PRO B 463 -27.656 38.314 26.057 1.00 92.15 C
ANISOU 5911 CA PRO B 463 11642 12281 11092 -1230 -607 -1695 C
ATOM 5912 C PRO B 463 -28.937 37.994 26.816 1.00 89.97 C
ANISOU 5912 C PRO B 463 11584 11925 10676 -1084 -550 -1564 C
ATOM 5913 O PRO B 463 -29.429 38.801 27.609 1.00 95.09 O
ANISOU 5913 O PRO B 463 12398 12511 11220 -1082 -546 -1586 O
ATOM 5914 CB PRO B 463 -26.442 38.381 26.989 1.00 88.06 C
ANISOU 5914 CB PRO B 463 11043 11884 10531 -1211 -814 -1853 C
ATOM 5915 CG PRO B 463 -25.564 39.411 26.367 1.00 83.57 C
ANISOU 5915 CG PRO B 463 10330 11324 10098 -1420 -812 -2000 C
ATOM 5916 CD PRO B 463 -26.495 40.441 25.786 1.00 78.00 C
ANISOU 5916 CD PRO B 463 9756 10468 9415 -1539 -631 -1946 C
ATOM 5917 N PHE B 464 -29.483 36.808 26.546 1.00 92.14 N
ANISOU 5917 N PHE B 464 11857 12194 10959 -966 -492 -1431 N
ATOM 5918 CA PHE B 464 -30.710 36.305 27.162 1.00 87.85 C
ANISOU 5918 CA PHE B 464 11494 11571 10316 -826 -412 -1294 C
ATOM 5919 C PHE B 464 -31.924 37.178 26.858 1.00 84.93 C
ANISOU 5919 C PHE B 464 11248 11071 9952 -892 -257 -1233 C
ATOM 5920 O PHE B 464 -32.907 37.158 27.606 1.00 92.54 O
ANISOU 5920 O PHE B 464 12380 11960 10819 -796 -193 -1153 O
ATOM 5921 CB PHE B 464 -30.550 36.138 28.679 1.00 79.95 C
ANISOU 5921 CB PHE B 464 10631 10607 9139 -683 -528 -1318 C
ATOM 5922 CG PHE B 464 -29.556 35.085 29.069 1.00 79.59 C
ANISOU 5922 CG PHE B 464 10490 10683 9066 -564 -676 -1345 C
ATOM 5923 CD1 PHE B 464 -29.790 33.752 28.776 1.00 89.97 C
ANISOU 5923 CD1 PHE B 464 11771 11998 10418 -449 -626 -1226 C
ATOM 5924 CD2 PHE B 464 -28.392 35.425 29.737 1.00 78.87 C
ANISOU 5924 CD2 PHE B 464 10344 10705 8919 -562 -869 -1494 C
ATOM 5925 CE1 PHE B 464 -28.879 32.777 29.136 1.00 94.08 C
ANISOU 5925 CE1 PHE B 464 12213 12622 10911 -324 -758 -1244 C
ATOM 5926 CE2 PHE B 464 -27.477 34.455 30.102 1.00 85.24 C
ANISOU 5926 CE2 PHE B 464 11058 11630 9699 -434 -1016 -1518 C
ATOM 5927 CZ PHE B 464 -27.720 33.130 29.800 1.00 87.99 C
ANISOU 5927 CZ PHE B 464 11383 11972 10077 -309 -956 -1387 C
ATOM 5928 N GLU B 465 -31.884 37.942 25.771 1.00 84.21 N
ANISOU 5928 N GLU B 465 11080 10946 9971 -1043 -187 -1263 N
ATOM 5929 CA GLU B 465 -33.031 38.732 25.353 1.00 80.08 C
ANISOU 5929 CA GLU B 465 10664 10302 9462 -1091 -42 -1198 C
ATOM 5930 C GLU B 465 -33.933 37.904 24.445 1.00 78.46 C
ANISOU 5930 C GLU B 465 10418 10059 9336 -1047 69 -1070 C
ATOM 5931 O GLU B 465 -33.468 37.051 23.685 1.00 85.71 O
ANISOU 5931 O GLU B 465 11195 11035 10335 -1050 52 -1060 O
ATOM 5932 CB GLU B 465 -32.581 40.005 24.632 1.00 71.99 C
ANISOU 5932 CB GLU B 465 9602 9247 8506 -1264 -13 -1287 C
ATOM 5933 CG GLU B 465 -33.700 40.998 24.347 1.00 78.31 C
ANISOU 5933 CG GLU B 465 10537 9918 9300 -1300 122 -1230 C
ATOM 5934 CD GLU B 465 -33.217 42.223 23.593 1.00 87.70 C
ANISOU 5934 CD GLU B 465 11702 11062 10557 -1465 167 -1308 C
ATOM 5935 OE1 GLU B 465 -32.005 42.309 23.307 1.00 81.92 O
ANISOU 5935 OE1 GLU B 465 10840 10399 9887 -1564 99 -1413 O
ATOM 5936 OE2 GLU B 465 -34.051 43.099 23.283 1.00 99.11 O
ANISOU 5936 OE2 GLU B 465 13259 12398 12001 -1493 278 -1263 O
ATOM 5937 N ARG B 466 -35.236 38.157 24.540 1.00 70.43 N
ANISOU 5937 N ARG B 466 9521 8942 8298 -1004 181 -980 N
ATOM 5938 CA ARG B 466 -36.234 37.475 23.728 1.00 80.96 C
ANISOU 5938 CA ARG B 466 10817 10232 9712 -966 283 -871 C
ATOM 5939 C ARG B 466 -37.039 38.507 22.954 1.00 81.68 C
ANISOU 5939 C ARG B 466 10950 10240 9845 -1037 384 -847 C
ATOM 5940 O ARG B 466 -37.455 39.526 23.516 1.00 79.99 O
ANISOU 5940 O ARG B 466 10864 9960 9570 -1047 420 -859 O
ATOM 5941 CB ARG B 466 -37.164 36.620 24.594 1.00 86.11 C
ANISOU 5941 CB ARG B 466 11558 10842 10319 -824 333 -774 C
ATOM 5942 CG ARG B 466 -38.157 35.789 23.796 1.00 85.62 C
ANISOU 5942 CG ARG B 466 11433 10737 10360 -790 430 -679 C
ATOM 5943 CD ARG B 466 -39.222 35.158 24.685 1.00 89.76 C
ANISOU 5943 CD ARG B 466 12056 11191 10857 -669 516 -584 C
ATOM 5944 NE ARG B 466 -38.658 34.264 25.690 1.00 98.52 N
ANISOU 5944 NE ARG B 466 13208 12337 11887 -568 462 -573 N
ATOM 5945 CZ ARG B 466 -38.510 34.573 26.972 1.00106.77 C
ANISOU 5945 CZ ARG B 466 14398 13376 12792 -496 435 -582 C
ATOM 5946 NH1 ARG B 466 -38.879 35.752 27.446 1.00107.85 N
ANISOU 5946 NH1 ARG B 466 14654 13468 12858 -521 463 -609 N
ATOM 5947 NH2 ARG B 466 -37.981 33.676 27.798 1.00100.47 N
ANISOU 5947 NH2 ARG B 466 13641 12617 11916 -386 379 -565 N
ATOM 5948 N ASP B 467 -37.254 38.244 21.666 1.00 76.77 N
ANISOU 5948 N ASP B 467 10230 9621 9319 -1076 426 -816 N
ATOM 5949 CA ASP B 467 -38.046 39.114 20.802 1.00 78.29 C
ANISOU 5949 CA ASP B 467 10458 9743 9547 -1121 514 -783 C
ATOM 5950 C ASP B 467 -39.079 38.255 20.086 1.00 79.07 C
ANISOU 5950 C ASP B 467 10499 9825 9718 -1056 568 -698 C
ATOM 5951 O ASP B 467 -38.728 37.449 19.218 1.00 87.95 O
ANISOU 5951 O ASP B 467 11509 11003 10906 -1069 544 -701 O
ATOM 5952 CB ASP B 467 -37.161 39.858 19.801 1.00 88.39 C
ANISOU 5952 CB ASP B 467 11683 11040 10860 -1246 508 -848 C
ATOM 5953 CG ASP B 467 -37.915 40.933 19.037 1.00 90.18 C
ANISOU 5953 CG ASP B 467 11986 11182 11096 -1279 599 -812 C
ATOM 5954 OD1 ASP B 467 -39.118 41.134 19.310 1.00 87.46 O
ANISOU 5954 OD1 ASP B 467 11724 10771 10737 -1204 655 -745 O
ATOM 5955 OD2 ASP B 467 -37.302 41.581 18.162 1.00 89.89 O
ANISOU 5955 OD2 ASP B 467 11928 11141 11083 -1374 621 -849 O
ATOM 5956 N ILE B 468 -40.348 38.423 20.452 1.00 74.16 N
ANISOU 5956 N ILE B 468 9954 9130 9095 -986 641 -631 N
ATOM 5957 CA ILE B 468 -41.447 37.684 19.848 1.00 82.53 C
ANISOU 5957 CA ILE B 468 10951 10168 10239 -928 691 -562 C
ATOM 5958 C ILE B 468 -42.324 38.582 18.986 1.00 76.07 C
ANISOU 5958 C ILE B 468 10155 9298 9449 -938 745 -536 C
ATOM 5959 O ILE B 468 -43.431 38.183 18.607 1.00 70.26 O
ANISOU 5959 O ILE B 468 9377 8537 8783 -881 786 -486 O
ATOM 5960 CB ILE B 468 -42.289 36.965 20.915 1.00 84.00 C
ANISOU 5960 CB ILE B 468 11176 10311 10428 -828 743 -502 C
ATOM 5961 CG1 ILE B 468 -43.016 37.985 21.794 1.00 65.74 C
ANISOU 5961 CG1 ILE B 468 9004 7920 8053 -791 813 -478 C
ATOM 5962 CG2 ILE B 468 -41.412 36.058 21.763 1.00 62.69 C
ANISOU 5962 CG2 ILE B 468 8475 7660 7684 -796 688 -519 C
ATOM 5963 CD1 ILE B 468 -44.021 37.368 22.738 1.00 69.51 C
ANISOU 5963 CD1 ILE B 468 9526 8340 8544 -690 900 -408 C
ATOM 5964 N SER B 469 -41.859 39.787 18.668 1.00 72.91 N
ANISOU 5964 N SER B 469 9821 8880 9002 -1006 748 -571 N
ATOM 5965 CA SER B 469 -42.660 40.722 17.894 1.00 82.91 C
ANISOU 5965 CA SER B 469 11135 10090 10279 -998 801 -537 C
ATOM 5966 C SER B 469 -42.831 40.236 16.458 1.00 87.57 C
ANISOU 5966 C SER B 469 11624 10721 10927 -999 781 -525 C
ATOM 5967 O SER B 469 -41.944 39.603 15.879 1.00 72.36 O
ANISOU 5967 O SER B 469 9615 8862 9016 -1049 733 -563 O
ATOM 5968 CB SER B 469 -42.019 42.110 17.903 1.00 74.87 C
ANISOU 5968 CB SER B 469 10225 9026 9196 -1075 822 -578 C
ATOM 5969 OG SER B 469 -40.728 42.079 17.321 1.00 98.71 O
ANISOU 5969 OG SER B 469 13190 12101 12216 -1175 779 -640 O
ATOM 5970 N THR B 470 -43.995 40.539 15.886 1.00 86.00 N
ANISOU 5970 N THR B 470 11432 10485 10758 -935 814 -477 N
ATOM 5971 CA THR B 470 -44.327 40.169 14.516 1.00 87.97 C
ANISOU 5971 CA THR B 470 11604 10773 11048 -917 784 -469 C
ATOM 5972 C THR B 470 -44.417 41.391 13.607 1.00 91.25 C
ANISOU 5972 C THR B 470 12109 11151 11409 -920 811 -452 C
ATOM 5973 O THR B 470 -45.215 41.418 12.668 1.00 94.33 O
ANISOU 5973 O THR B 470 12478 11547 11816 -856 797 -425 O
ATOM 5974 CB THR B 470 -45.635 39.380 14.474 1.00 86.00 C
ANISOU 5974 CB THR B 470 11267 10523 10887 -828 782 -437 C
ATOM 5975 OG1 THR B 470 -46.704 40.199 14.964 1.00 98.74 O
ANISOU 5975 OG1 THR B 470 12947 12065 12503 -760 840 -392 O
ATOM 5976 CG2 THR B 470 -45.529 38.131 15.334 1.00 83.99 C
ANISOU 5976 CG2 THR B 470 10937 10287 10688 -824 777 -445 C
ATOM 5977 N GLU B 471 -43.604 42.408 13.880 1.00 80.12 N
ANISOU 5977 N GLU B 471 10807 9700 9936 -992 849 -472 N
ATOM 5978 CA GLU B 471 -43.624 43.627 13.084 1.00 82.09 C
ANISOU 5978 CA GLU B 471 11167 9892 10132 -998 898 -448 C
ATOM 5979 C GLU B 471 -42.957 43.386 11.735 1.00 89.06 C
ANISOU 5979 C GLU B 471 12014 10827 10999 -1036 880 -462 C
ATOM 5980 O GLU B 471 -41.881 42.786 11.660 1.00 86.53 O
ANISOU 5980 O GLU B 471 11622 10564 10690 -1117 857 -514 O
ATOM 5981 CB GLU B 471 -42.917 44.755 13.834 1.00 75.35 C
ANISOU 5981 CB GLU B 471 10436 8963 9230 -1078 956 -476 C
ATOM 5982 CG GLU B 471 -42.971 46.104 13.140 1.00 92.23 C
ANISOU 5982 CG GLU B 471 12714 11011 11317 -1085 1032 -446 C
ATOM 5983 CD GLU B 471 -42.053 47.123 13.785 1.00100.86 C
ANISOU 5983 CD GLU B 471 13913 12029 12381 -1197 1091 -497 C
ATOM 5984 OE1 GLU B 471 -41.127 46.711 14.515 1.00 85.21 O
ANISOU 5984 OE1 GLU B 471 11871 10091 10414 -1284 1051 -570 O
ATOM 5985 OE2 GLU B 471 -42.257 48.335 13.561 1.00124.17 O
ANISOU 5985 OE2 GLU B 471 17008 14874 15296 -1195 1173 -469 O
ATOM 5986 N ILE B 472 -43.602 43.856 10.665 1.00 83.79 N
ANISOU 5986 N ILE B 472 11399 10140 10298 -967 892 -416 N
ATOM 5987 CA ILE B 472 -43.053 43.686 9.324 1.00 82.48 C
ANISOU 5987 CA ILE B 472 11227 10016 10094 -984 887 -422 C
ATOM 5988 C ILE B 472 -41.748 44.458 9.210 1.00 83.68 C
ANISOU 5988 C ILE B 472 11459 10128 10208 -1106 966 -448 C
ATOM 5989 O ILE B 472 -41.694 45.665 9.475 1.00 76.12 O
ANISOU 5989 O ILE B 472 10632 9074 9216 -1132 1044 -428 O
ATOM 5990 CB ILE B 472 -44.070 44.139 8.265 1.00 87.25 C
ANISOU 5990 CB ILE B 472 11899 10604 10649 -863 878 -364 C
ATOM 5991 CG1 ILE B 472 -45.330 43.272 8.324 1.00 86.67 C
ANISOU 5991 CG1 ILE B 472 11709 10582 10641 -755 790 -359 C
ATOM 5992 CG2 ILE B 472 -43.452 44.089 6.874 1.00 92.19 C
ANISOU 5992 CG2 ILE B 472 12558 11264 11206 -874 887 -365 C
ATOM 5993 CD1 ILE B 472 -45.088 41.815 8.001 1.00 83.57 C
ANISOU 5993 CD1 ILE B 472 11164 10286 10303 -776 713 -413 C
ATOM 5994 N TYR B 473 -40.685 43.760 8.814 1.00 80.96 N
ANISOU 5994 N TYR B 473 11030 9852 9881 -1185 954 -499 N
ATOM 5995 CA TYR B 473 -39.367 44.377 8.719 1.00 83.74 C
ANISOU 5995 CA TYR B 473 11419 10174 10224 -1314 1033 -538 C
ATOM 5996 C TYR B 473 -39.310 45.304 7.511 1.00 88.81 C
ANISOU 5996 C TYR B 473 12199 10753 10794 -1306 1129 -488 C
ATOM 5997 O TYR B 473 -39.569 44.881 6.380 1.00 95.69 O
ANISOU 5997 O TYR B 473 13070 11666 11620 -1236 1114 -460 O
ATOM 5998 CB TYR B 473 -38.281 43.308 8.623 1.00 68.97 C
ANISOU 5998 CB TYR B 473 9403 8400 8403 -1386 996 -605 C
ATOM 5999 CG TYR B 473 -36.882 43.878 8.534 1.00 68.12 C
ANISOU 5999 CG TYR B 473 9299 8272 8312 -1526 1077 -658 C
ATOM 6000 CD1 TYR B 473 -36.223 44.328 9.670 1.00 84.93 C
ANISOU 6000 CD1 TYR B 473 11412 10374 10482 -1621 1078 -718 C
ATOM 6001 CD2 TYR B 473 -36.222 43.971 7.316 1.00 84.07 C
ANISOU 6001 CD2 TYR B 473 11336 10297 10310 -1563 1156 -655 C
ATOM 6002 CE1 TYR B 473 -34.946 44.854 9.596 1.00 87.60 C
ANISOU 6002 CE1 TYR B 473 11731 10695 10859 -1759 1149 -783 C
ATOM 6003 CE2 TYR B 473 -34.945 44.494 7.232 1.00 83.75 C
ANISOU 6003 CE2 TYR B 473 11284 10232 10307 -1700 1248 -708 C
ATOM 6004 CZ TYR B 473 -34.312 44.933 8.375 1.00 80.53 C
ANISOU 6004 CZ TYR B 473 10838 9800 9960 -1803 1241 -776 C
ATOM 6005 OH TYR B 473 -33.043 45.454 8.294 1.00 90.84 O
ANISOU 6005 OH TYR B 473 12109 11082 11324 -1948 1329 -844 O
ATOM 6006 N GLN B 474 -38.964 46.566 7.751 1.00 84.84 N
ANISOU 6006 N GLN B 474 11822 10140 10273 -1373 1232 -480 N
ATOM 6007 CA GLN B 474 -38.845 47.563 6.690 1.00 85.70 C
ANISOU 6007 CA GLN B 474 12090 10162 10311 -1369 1352 -424 C
ATOM 6008 C GLN B 474 -37.400 47.575 6.208 1.00 94.98 C
ANISOU 6008 C GLN B 474 13231 11342 11514 -1511 1441 -476 C
ATOM 6009 O GLN B 474 -36.510 48.099 6.882 1.00 96.35 O
ANISOU 6009 O GLN B 474 13392 11468 11750 -1649 1500 -538 O
ATOM 6010 CB GLN B 474 -39.284 48.935 7.191 1.00 89.67 C
ANISOU 6010 CB GLN B 474 12758 10522 10790 -1364 1433 -385 C
ATOM 6011 CG GLN B 474 -39.144 50.045 6.163 1.00 99.22 C
ANISOU 6011 CG GLN B 474 14156 11617 11926 -1357 1578 -318 C
ATOM 6012 CD GLN B 474 -39.632 51.381 6.683 1.00 97.79 C
ANISOU 6012 CD GLN B 474 14147 11283 11725 -1341 1662 -278 C
ATOM 6013 OE1 GLN B 474 -40.290 51.454 7.721 1.00103.17 O
ANISOU 6013 OE1 GLN B 474 14811 11954 12435 -1305 1602 -290 O
ATOM 6014 NE2 GLN B 474 -39.311 52.448 5.962 1.00 93.92 N
ANISOU 6014 NE2 GLN B 474 13834 10664 11186 -1365 1816 -226 N
ATOM 6015 N ALA B 475 -37.164 46.990 5.033 1.00 94.18 N
ANISOU 6015 N ALA B 475 13110 11302 11371 -1476 1453 -459 N
ATOM 6016 CA ALA B 475 -35.823 46.928 4.467 1.00 92.04 C
ANISOU 6016 CA ALA B 475 12799 11041 11130 -1599 1554 -504 C
ATOM 6017 C ALA B 475 -35.473 48.160 3.645 1.00 94.56 C
ANISOU 6017 C ALA B 475 13305 11230 11393 -1638 1739 -448 C
ATOM 6018 O ALA B 475 -34.287 48.476 3.493 1.00104.84 O
ANISOU 6018 O ALA B 475 14585 12497 12753 -1780 1862 -494 O
ATOM 6019 CB ALA B 475 -35.673 45.677 3.599 1.00 86.46 C
ANISOU 6019 CB ALA B 475 11992 10456 10404 -1544 1496 -516 C
ATOM 6020 N GLY B 476 -36.468 48.857 3.116 1.00 92.27 N
ANISOU 6020 N GLY B 476 13196 10864 10998 -1511 1767 -351 N
ATOM 6021 CA GLY B 476 -36.267 50.044 2.313 1.00 98.74 C
ANISOU 6021 CA GLY B 476 14227 11545 11746 -1519 1949 -279 C
ATOM 6022 C GLY B 476 -36.450 51.321 3.104 1.00100.03 C
ANISOU 6022 C GLY B 476 14513 11557 11938 -1569 2029 -264 C
ATOM 6023 O GLY B 476 -36.191 51.378 4.312 1.00101.26 O
ANISOU 6023 O GLY B 476 14572 11709 12194 -1670 1983 -343 O
ATOM 6024 N ASN B 477 -36.904 52.366 2.411 1.00 97.84 N
ANISOU 6024 N ASN B 477 14464 11148 11561 -1488 2150 -162 N
ATOM 6025 CA ASN B 477 -37.111 53.677 3.013 1.00 98.04 C
ANISOU 6025 CA ASN B 477 14644 11003 11603 -1523 2252 -137 C
ATOM 6026 C ASN B 477 -38.575 54.097 2.994 1.00101.06 C
ANISOU 6026 C ASN B 477 15160 11348 11889 -1318 2184 -40 C
ATOM 6027 O ASN B 477 -38.877 55.272 3.233 1.00101.35 O
ANISOU 6027 O ASN B 477 15373 11226 11909 -1304 2289 8 O
ATOM 6028 CB ASN B 477 -36.258 54.728 2.301 1.00103.10 C
ANISOU 6028 CB ASN B 477 15458 11481 12233 -1624 2496 -100 C
ATOM 6029 CG ASN B 477 -34.833 54.266 2.081 1.00105.96 C
ANISOU 6029 CG ASN B 477 15679 11889 12690 -1808 2577 -188 C
ATOM 6030 OD1 ASN B 477 -34.304 54.350 0.973 1.00109.96 O
ANISOU 6030 OD1 ASN B 477 16269 12365 13146 -1815 2721 -140 O
ATOM 6031 ND2 ASN B 477 -34.205 53.763 3.138 1.00103.44 N
ANISOU 6031 ND2 ASN B 477 15147 11647 12508 -1949 2486 -316 N
ATOM 6032 N LYS B 478 -39.487 53.173 2.710 1.00105.29 N
ANISOU 6032 N LYS B 478 15612 12022 12371 -1158 2016 -16 N
ATOM 6033 CA LYS B 478 -40.912 53.451 2.697 1.00108.45 C
ANISOU 6033 CA LYS B 478 16095 12410 12699 -957 1931 62 C
ATOM 6034 C LYS B 478 -41.620 52.612 3.754 1.00108.38 C
ANISOU 6034 C LYS B 478 15894 12513 12773 -927 1753 2 C
ATOM 6035 O LYS B 478 -41.217 51.476 4.024 1.00116.89 O
ANISOU 6035 O LYS B 478 16777 13719 13915 -996 1656 -76 O
ATOM 6036 CB LYS B 478 -41.521 53.162 1.318 1.00103.66 C
ANISOU 6036 CB LYS B 478 15570 11864 11952 -771 1886 144 C
ATOM 6037 CG LYS B 478 -40.965 54.034 0.203 1.00115.08 C
ANISOU 6037 CG LYS B 478 17248 13190 13287 -762 2075 227 C
ATOM 6038 CD LYS B 478 -41.604 53.699 -1.136 1.00133.04 C
ANISOU 6038 CD LYS B 478 19613 15538 15398 -556 2008 303 C
ATOM 6039 CE LYS B 478 -41.085 54.612 -2.238 1.00140.23 C
ANISOU 6039 CE LYS B 478 20788 16315 16178 -528 2214 402 C
ATOM 6040 NZ LYS B 478 -41.688 54.284 -3.559 1.00122.66 N
ANISOU 6040 NZ LYS B 478 18670 14168 13768 -312 2140 473 N
ATOM 6041 N PRO B 479 -42.674 53.144 4.370 1.00102.89 N
ANISOU 6041 N PRO B 479 15253 11763 12078 -820 1720 40 N
ATOM 6042 CA PRO B 479 -43.379 52.389 5.411 1.00102.64 C
ANISOU 6042 CA PRO B 479 15050 11821 12127 -790 1578 -9 C
ATOM 6043 C PRO B 479 -44.105 51.180 4.842 1.00110.91 C
ANISOU 6043 C PRO B 479 15951 13026 13163 -669 1420 -10 C
ATOM 6044 O PRO B 479 -44.558 51.175 3.695 1.00117.25 O
ANISOU 6044 O PRO B 479 16821 13857 13873 -538 1393 48 O
ATOM 6045 CB PRO B 479 -44.368 53.412 5.979 1.00104.54 C
ANISOU 6045 CB PRO B 479 15418 11946 12356 -684 1615 48 C
ATOM 6046 CG PRO B 479 -44.591 54.371 4.857 1.00100.31 C
ANISOU 6046 CG PRO B 479 15097 11310 11706 -573 1710 150 C
ATOM 6047 CD PRO B 479 -43.273 54.471 4.145 1.00 99.98 C
ANISOU 6047 CD PRO B 479 15113 11238 11637 -715 1824 136 C
ATOM 6048 N CYS B 480 -44.221 50.148 5.675 1.00109.39 N
ANISOU 6048 N CYS B 480 15566 12933 13065 -709 1314 -79 N
ATOM 6049 CA CYS B 480 -44.805 48.879 5.263 1.00111.25 C
ANISOU 6049 CA CYS B 480 15639 13311 13320 -628 1169 -102 C
ATOM 6050 C CYS B 480 -46.303 48.790 5.522 1.00116.78 C
ANISOU 6050 C CYS B 480 16291 14032 14047 -467 1078 -71 C
ATOM 6051 O CYS B 480 -46.953 47.888 4.981 1.00112.02 O
ANISOU 6051 O CYS B 480 15571 13534 13456 -378 958 -86 O
ATOM 6052 CB CYS B 480 -44.097 47.723 5.974 1.00114.35 C
ANISOU 6052 CB CYS B 480 15847 13792 13808 -756 1116 -191 C
ATOM 6053 SG CYS B 480 -42.338 47.617 5.592 1.00129.75 S
ANISOU 6053 SG CYS B 480 17800 15749 15751 -935 1202 -243 S
ATOM 6054 N ASN B 481 -46.858 49.685 6.337 1.00117.90 N
ANISOU 6054 N ASN B 481 16513 14076 14208 -430 1134 -36 N
ATOM 6055 CA ASN B 481 -48.283 49.753 6.650 1.00118.39 C
ANISOU 6055 CA ASN B 481 16533 14143 14307 -274 1073 -3 C
ATOM 6056 C ASN B 481 -48.815 48.480 7.299 1.00116.47 C
ANISOU 6056 C ASN B 481 16068 14005 14180 -277 969 -61 C
ATOM 6057 O ASN B 481 -50.036 48.292 7.371 1.00117.47 O
ANISOU 6057 O ASN B 481 16114 14160 14358 -148 904 -45 O
ATOM 6058 CB ASN B 481 -49.116 50.088 5.404 1.00127.01 C
ANISOU 6058 CB ASN B 481 17694 15252 15312 -91 1019 62 C
ATOM 6059 CG ASN B 481 -48.723 51.413 4.779 1.00130.91 C
ANISOU 6059 CG ASN B 481 18435 15621 15685 -61 1141 139 C
ATOM 6060 OD1 ASN B 481 -48.272 52.328 5.468 1.00136.58 O
ANISOU 6060 OD1 ASN B 481 19275 16211 16407 -140 1269 154 O
ATOM 6061 ND2 ASN B 481 -48.891 51.521 3.466 1.00125.91 N
ANISOU 6061 ND2 ASN B 481 17886 15017 14939 57 1105 186 N
ATOM 6062 N GLY B 482 -47.937 47.600 7.773 1.00109.38 N
ANISOU 6062 N GLY B 482 15068 13160 13332 -417 957 -127 N
ATOM 6063 CA GLY B 482 -48.357 46.400 8.463 1.00102.34 C
ANISOU 6063 CA GLY B 482 13989 12347 12550 -427 883 -175 C
ATOM 6064 C GLY B 482 -48.552 45.176 7.597 1.00 95.79 C
ANISOU 6064 C GLY B 482 13012 11634 11749 -398 770 -214 C
ATOM 6065 O GLY B 482 -49.021 44.151 8.105 1.00 97.38 O
ANISOU 6065 O GLY B 482 13056 11889 12054 -398 716 -252 O
ATOM 6066 N VAL B 483 -48.211 45.244 6.312 1.00 93.33 N
ANISOU 6066 N VAL B 483 12756 11356 11348 -372 742 -208 N
ATOM 6067 CA VAL B 483 -48.345 44.108 5.411 1.00 97.10 C
ANISOU 6067 CA VAL B 483 13112 11942 11838 -344 632 -256 C
ATOM 6068 C VAL B 483 -47.042 43.941 4.642 1.00104.14 C
ANISOU 6068 C VAL B 483 14063 12857 12647 -435 664 -277 C
ATOM 6069 O VAL B 483 -46.272 44.892 4.471 1.00103.42 O
ANISOU 6069 O VAL B 483 14124 12696 12476 -483 767 -240 O
ATOM 6070 CB VAL B 483 -49.545 44.273 4.447 1.00 82.75 C
ANISOU 6070 CB VAL B 483 11295 10162 9985 -172 536 -235 C
ATOM 6071 CG1 VAL B 483 -49.209 45.244 3.323 1.00 96.26 C
ANISOU 6071 CG1 VAL B 483 13202 11840 11532 -106 570 -177 C
ATOM 6072 CG2 VAL B 483 -49.991 42.923 3.897 1.00 83.87 C
ANISOU 6072 CG2 VAL B 483 11259 10416 10193 -146 402 -312 C
ATOM 6073 N ALA B 484 -46.790 42.715 4.191 1.00 93.47 N
ANISOU 6073 N ALA B 484 12588 11598 11329 -463 589 -341 N
ATOM 6074 CA ALA B 484 -45.576 42.412 3.450 1.00 86.21 C
ANISOU 6074 CA ALA B 484 11703 10708 10344 -543 622 -369 C
ATOM 6075 C ALA B 484 -45.665 42.945 2.026 1.00 94.93 C
ANISOU 6075 C ALA B 484 12946 11820 11304 -447 618 -333 C
ATOM 6076 O ALA B 484 -46.737 42.978 1.417 1.00 94.58 O
ANISOU 6076 O ALA B 484 12906 11807 11225 -306 525 -321 O
ATOM 6077 CB ALA B 484 -45.321 40.905 3.432 1.00 84.17 C
ANISOU 6077 CB ALA B 484 11276 10538 10166 -590 548 -449 C
ATOM 6078 N GLY B 485 -44.518 43.364 1.497 1.00 96.47 N
ANISOU 6078 N GLY B 485 13254 11986 11416 -519 723 -318 N
ATOM 6079 CA GLY B 485 -44.449 43.892 0.149 1.00 87.73 C
ANISOU 6079 CA GLY B 485 12309 10873 10154 -432 750 -274 C
ATOM 6080 C GLY B 485 -43.027 44.111 -0.321 1.00 87.23 C
ANISOU 6080 C GLY B 485 12331 10779 10032 -544 888 -272 C
ATOM 6081 O GLY B 485 -42.111 43.403 0.109 1.00 96.95 O
ANISOU 6081 O GLY B 485 13446 12044 11348 -673 912 -333 O
ATOM 6082 N PHE B 486 -42.826 45.087 -1.203 1.00 87.79 N
ANISOU 6082 N PHE B 486 12606 10784 9965 -491 988 -200 N
ATOM 6083 CA PHE B 486 -41.488 45.395 -1.693 1.00 90.11 C
ANISOU 6083 CA PHE B 486 12991 11033 10213 -600 1150 -192 C
ATOM 6084 C PHE B 486 -40.655 46.000 -0.569 1.00 98.19 C
ANISOU 6084 C PHE B 486 13990 11970 11348 -770 1271 -200 C
ATOM 6085 O PHE B 486 -41.040 47.015 0.021 1.00 94.79 O
ANISOU 6085 O PHE B 486 13649 11442 10926 -762 1319 -150 O
ATOM 6086 CB PHE B 486 -41.568 46.347 -2.884 1.00 79.43 C
ANISOU 6086 CB PHE B 486 11885 9613 8681 -490 1245 -100 C
ATOM 6087 CG PHE B 486 -40.230 46.707 -3.462 1.00 89.91 C
ANISOU 6087 CG PHE B 486 13317 10882 9963 -599 1440 -84 C
ATOM 6088 CD1 PHE B 486 -39.506 45.782 -4.195 1.00 92.58 C
ANISOU 6088 CD1 PHE B 486 13599 11303 10274 -631 1449 -139 C
ATOM 6089 CD2 PHE B 486 -39.699 47.972 -3.277 1.00 94.32 C
ANISOU 6089 CD2 PHE B 486 14028 11294 10514 -673 1628 -18 C
ATOM 6090 CE1 PHE B 486 -38.275 46.110 -4.729 1.00 90.12 C
ANISOU 6090 CE1 PHE B 486 13372 10936 9934 -732 1646 -125 C
ATOM 6091 CE2 PHE B 486 -38.468 48.307 -3.810 1.00100.22 C
ANISOU 6091 CE2 PHE B 486 1 |
