*** VIRAL PROTEIN 17-DEC-21 7WBQ ***
Job options:
ID = 220221231311117641
JOBID = VIRAL PROTEIN 17-DEC-21 7WBQ
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 17-DEC-21 7WBQ
TITLE CRYSTAL STRUCTURE OF THE RECEPTOR BINDING DOMAIN OF SARS-COV-2 DELTA
TITLE 2 VARIANT SPIKE GLYCOPROTEIN IN COMPLEX WITH ITS RECEPTOR HUMAN ACE2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ACE-RELATED CARBOXYPEPTIDASE,ANGIOTENSIN-CONVERTING ENZYME
COMPND 5 HOMOLOG;
COMPND 6 EC: 3.4.17.23,3.4.17.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SPIKE PROTEIN S1;
COMPND 10 CHAIN: B, D;
COMPND 11 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;
SOURCE 6 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266783;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 10 2;
SOURCE 11 ORGANISM_TAXID: 2697049;
SOURCE 12 GENE: S, 2;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS COMPLEX, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.QI,P.HAN
REVDAT 1 19-JAN-22 7WBQ 0
JRNL AUTH P.HAN,L.LI,S.LIU,Q.WANG,D.ZHANG,Z.XU,P.HAN,X.LI,Q.PENG,C.SU,
JRNL AUTH 2 B.HUANG,D.LI,R.ZHANG,M.TIAN,L.FU,Y.GAO,X.ZHAO,K.LIU,J.QI,
JRNL AUTH 3 G.F.GAO,P.WANG
JRNL TITL RECEPTOR BINDING AND COMPLEX STRUCTURES OF HUMAN ACE2 TO
JRNL TITL 2 SPIKE RBD FROM OMICRON AND DELTA SARS-COV-2.
JRNL REF CELL(CAMBRIDGE,MASS.) 2022
JRNL REFN ISSN 0092-8674
JRNL DOI 10.1016/J.CELL.2022.01.001
REMARK 2
REMARK 2 RESOLUTION. 3.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19RC3_4028
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) : 3.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 38490
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 1986
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 44.7000 - 8.0400 0.98 2652 144 0.1793 0.1924
REMARK 3 2 8.0400 - 6.3900 1.00 2661 144 0.1897 0.1875
REMARK 3 3 6.3900 - 5.5800 1.00 2636 144 0.1879 0.2281
REMARK 3 4 5.5800 - 5.0700 1.00 2658 145 0.1742 0.2119
REMARK 3 5 5.0700 - 4.7100 1.00 2633 143 0.1548 0.1777
REMARK 3 6 4.7100 - 4.4300 1.00 2622 143 0.1571 0.2286
REMARK 3 7 4.4300 - 4.2100 1.00 2654 146 0.1779 0.2000
REMARK 3 8 4.2100 - 4.0300 1.00 2625 142 0.1875 0.2142
REMARK 3 9 4.0300 - 3.8700 1.00 2637 144 0.2043 0.2488
REMARK 3 10 3.8700 - 3.7400 1.00 2618 143 0.2254 0.2816
REMARK 3 11 3.7400 - 3.6200 1.00 2618 143 0.2616 0.3103
REMARK 3 12 3.6200 - 3.5200 0.99 2591 139 0.2993 0.3117
REMARK 3 13 3.5200 - 3.4300 0.99 2598 141 0.3336 0.3821
REMARK 3 14 3.4300 - 3.3400 0.87 2301 125 0.3704 0.4375
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.513
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.685
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 106.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 120.4
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 : 0.003 13398
REMARK 3 ANGLE : 0.629 18212
REMARK 3 CHIRALITY : 0.044 1949
REMARK 3 PLANARITY : 0.005 2344
REMARK 3 DIHEDRAL : 7.845 1842
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 19:109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.286 42.262 56.751
REMARK 3 T TENSOR
REMARK 3 T11: 1.1115 T22: 0.9350
REMARK 3 T33: 0.9274 T12: 0.0232
REMARK 3 T13: -0.1068 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 3.2298 L22: 5.5823
REMARK 3 L33: 0.6298 L12: 1.4314
REMARK 3 L13: 1.1993 L23: 0.7815
REMARK 3 S TENSOR
REMARK 3 S11: -0.2206 S12: 0.3407 S13: 0.0891
REMARK 3 S21: 0.2815 S22: 0.2974 S23: 0.7008
REMARK 3 S31: -0.2329 S32: -0.0843 S33: -0.0759
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 110:172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.422 22.263 53.820
REMARK 3 T TENSOR
REMARK 3 T11: 0.8842 T22: 1.0343
REMARK 3 T33: 0.7364 T12: -0.0419
REMARK 3 T13: 0.0960 T23: -0.0739
REMARK 3 L TENSOR
REMARK 3 L11: 6.4297 L22: 7.0029
REMARK 3 L33: 4.9589 L12: 2.1396
REMARK 3 L13: 1.8657 L23: 3.3679
REMARK 3 S TENSOR
REMARK 3 S11: 0.7008 S12: -0.8434 S13: -0.0164
REMARK 3 S21: 1.6527 S22: -0.7792 S23: 0.8224
REMARK 3 S31: 0.7774 S32: -1.1545 S33: -0.0283
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 173:318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.269 19.812 40.094
REMARK 3 T TENSOR
REMARK 3 T11: 0.7104 T22: 0.7357
REMARK 3 T33: 0.6079 T12: 0.0632
REMARK 3 T13: -0.0194 T23: -0.1531
REMARK 3 L TENSOR
REMARK 3 L11: 3.6913 L22: 2.4967
REMARK 3 L33: 2.9613 L12: 0.9263
REMARK 3 L13: 1.2951 L23: 0.4498
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: 0.4935 S13: -0.3995
REMARK 3 S21: 0.0480 S22: 0.0595 S23: -0.1496
REMARK 3 S31: 0.1103 S32: 0.2387 S33: -0.0923
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 319:431 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.639 15.655 52.665
REMARK 3 T TENSOR
REMARK 3 T11: 0.8177 T22: 0.9081
REMARK 3 T33: 0.9715 T12: 0.2038
REMARK 3 T13: -0.2557 T23: -0.1246
REMARK 3 L TENSOR
REMARK 3 L11: 2.4601 L22: 7.0193
REMARK 3 L33: 4.4013 L12: 1.6947
REMARK 3 L13: 0.3409 L23: 0.8298
REMARK 3 S TENSOR
REMARK 3 S11: 0.3045 S12: 0.3888 S13: -0.8611
REMARK 3 S21: 0.4413 S22: -0.0868 S23: -0.1776
REMARK 3 S31: 0.8091 S32: 0.4611 S33: -0.2085
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 432:614 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.910 20.165 35.113
REMARK 3 T TENSOR
REMARK 3 T11: 0.7011 T22: 0.7572
REMARK 3 T33: 0.6277 T12: 0.0144
REMARK 3 T13: -0.0360 T23: -0.0974
REMARK 3 L TENSOR
REMARK 3 L11: 4.8780 L22: 2.5642
REMARK 3 L33: 2.9305 L12: 0.5608
REMARK 3 L13: 0.8973 L23: 0.8582
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.7597 S13: -0.7915
REMARK 3 S21: -0.1939 S22: 0.0555 S23: 0.0041
REMARK 3 S31: 0.0778 S32: 0.2933 S33: -0.0390
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 333:364 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.049 36.759 76.079
REMARK 3 T TENSOR
REMARK 3 T11: 1.0288 T22: 1.0909
REMARK 3 T33: 1.0388 T12: 0.2107
REMARK 3 T13: -0.2914 T23: -0.3108
REMARK 3 L TENSOR
REMARK 3 L11: 8.8422 L22: 5.8925
REMARK 3 L33: 7.4497 L12: -0.8609
REMARK 3 L13: 3.7721 L23: -0.9731
REMARK 3 S TENSOR
REMARK 3 S11: -0.3487 S12: -0.4128 S13: 0.4052
REMARK 3 S21: 0.0943 S22: 0.2501 S23: -0.9081
REMARK 3 S31: 0.2346 S32: 0.7996 S33: 0.0310
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 365:375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.434 23.334 69.430
REMARK 3 T TENSOR
REMARK 3 T11: 1.6265 T22: 1.4678
REMARK 3 T33: 2.0125 T12: 0.1044
REMARK 3 T13: -0.3750 T23: 0.1781
REMARK 3 L TENSOR
REMARK 3 L11: 2.0114 L22: 2.6284
REMARK 3 L33: 7.0126 L12: -4.4471
REMARK 3 L13: 6.2724 L23: -0.1541
REMARK 3 S TENSOR
REMARK 3 S11: 0.3089 S12: -0.5814 S13: -2.9442
REMARK 3 S21: -0.0320 S22: 0.1923 S23: -0.4442
REMARK 3 S31: 1.6579 S32: 0.6744 S33: -0.2658
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 376:459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.022 36.786 64.059
REMARK 3 T TENSOR
REMARK 3 T11: 0.9098 T22: 1.0360
REMARK 3 T33: 0.8463 T12: -0.0304
REMARK 3 T13: -0.1247 T23: -0.1705
REMARK 3 L TENSOR
REMARK 3 L11: 6.4489 L22: 3.9260
REMARK 3 L33: 4.5644 L12: -2.4776
REMARK 3 L13: -0.9680 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1140 S12: 0.4596 S13: -0.4191
REMARK 3 S21: -0.3032 S22: 0.2709 S23: -0.8762
REMARK 3 S31: 0.0443 S32: 0.8418 S33: -0.3240
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN B AND RESID 460:479 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.114 54.679 61.306
REMARK 3 T TENSOR
REMARK 3 T11: 0.9446 T22: 1.0813
REMARK 3 T33: 1.2044 T12: -0.1508
REMARK 3 T13: -0.1071 T23: 0.2742
REMARK 3 L TENSOR
REMARK 3 L11: 5.9465 L22: 3.8369
REMARK 3 L33: 3.4346 L12: -1.9320
REMARK 3 L13: 2.4941 L23: -0.1750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.4498 S13: 1.8739
REMARK 3 S21: -0.8956 S22: 0.2912 S23: 0.1043
REMARK 3 S31: -0.4110 S32: 0.0323 S33: 0.0304
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND RESID 480:527 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.158 41.084 66.304
REMARK 3 T TENSOR
REMARK 3 T11: 0.9160 T22: 0.9704
REMARK 3 T33: 0.5927 T12: 0.0649
REMARK 3 T13: -0.0736 T23: -0.1392
REMARK 3 L TENSOR
REMARK 3 L11: 4.3866 L22: 5.3425
REMARK 3 L33: 1.7689 L12: -1.9352
REMARK 3 L13: 1.7300 L23: -1.2730
REMARK 3 S TENSOR
REMARK 3 S11: -0.2710 S12: -0.1749 S13: 0.1587
REMARK 3 S21: -0.0596 S22: 0.6193 S23: -0.3343
REMARK 3 S31: -0.0282 S32: 0.3287 S33: -0.3041
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 19:82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.667 46.324 15.522
REMARK 3 T TENSOR
REMARK 3 T11: 1.2441 T22: 1.5891
REMARK 3 T33: 0.9146 T12: 0.0087
REMARK 3 T13: -0.0540 T23: 0.2559
REMARK 3 L TENSOR
REMARK 3 L11: 1.9539 L22: 5.7730
REMARK 3 L33: 2.5994 L12: -2.0897
REMARK 3 L13: 0.0728 L23: 4.7566
REMARK 3 S TENSOR
REMARK 3 S11: -0.1219 S12: -1.1887 S13: -0.1169
REMARK 3 S21: 1.7106 S22: 0.5007 S23: 0.1673
REMARK 3 S31: 1.2347 S32: 0.2583 S33: -0.3452
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN C AND RESID 83:129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.582 58.116 18.862
REMARK 3 T TENSOR
REMARK 3 T11: 1.4137 T22: 1.9771
REMARK 3 T33: 1.0702 T12: 0.3108
REMARK 3 T13: -0.2086 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 4.0935 L22: 1.0536
REMARK 3 L33: 1.7338 L12: 0.5573
REMARK 3 L13: 0.2155 L23: -1.4611
REMARK 3 S TENSOR
REMARK 3 S11: 0.0632 S12: -1.4050 S13: 0.8610
REMARK 3 S21: 0.3842 S22: 0.1096 S23: 0.4018
REMARK 3 S31: 0.2905 S32: -0.3324 S33: -0.1277
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 130:193 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.212 54.551 -1.841
REMARK 3 T TENSOR
REMARK 3 T11: 1.4034 T22: 1.3173
REMARK 3 T33: 1.4568 T12: -0.0065
REMARK 3 T13: -0.2779 T23: 0.5560
REMARK 3 L TENSOR
REMARK 3 L11: 3.6252 L22: 1.7831
REMARK 3 L33: 5.6293 L12: -0.6478
REMARK 3 L13: 1.0956 L23: 0.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.2943 S12: -0.6386 S13: -0.9248
REMARK 3 S21: 0.0374 S22: 0.5625 S23: 0.7818
REMARK 3 S31: 0.6936 S32: -1.2831 S33: -0.7626
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN C AND RESID 194:293 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.868 69.737 -7.905
REMARK 3 T TENSOR
REMARK 3 T11: 0.7738 T22: 0.8742
REMARK 3 T33: 0.8352 T12: 0.0430
REMARK 3 T13: -0.0715 T23: 0.1383
REMARK 3 L TENSOR
REMARK 3 L11: 3.5120 L22: 1.7577
REMARK 3 L33: 3.9612 L12: -1.1729
REMARK 3 L13: 0.9315 L23: -0.9744
REMARK 3 S TENSOR
REMARK 3 S11: -0.2714 S12: -0.6574 S13: 0.2638
REMARK 3 S21: 0.5510 S22: 0.5690 S23: 0.1032
REMARK 3 S31: -0.0067 S32: -0.8210 S33: -0.3130
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN C AND RESID 294:352 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.660 45.665 -12.428
REMARK 3 T TENSOR
REMARK 3 T11: 0.7213 T22: 0.9790
REMARK 3 T33: 0.8407 T12: 0.0491
REMARK 3 T13: -0.0746 T23: 0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 5.1417 L22: 5.5305
REMARK 3 L33: 7.0612 L12: -0.3599
REMARK 3 L13: 1.2449 L23: 0.0399
REMARK 3 S TENSOR
REMARK 3 S11: 0.5848 S12: -0.7933 S13: -0.6361
REMARK 3 S21: 0.0230 S22: -0.1045 S23: -0.0847
REMARK 3 S31: 0.7123 S32: -0.2884 S33: -0.4497
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN C AND RESID 353:431 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.190 56.075 -10.659
REMARK 3 T TENSOR
REMARK 3 T11: 0.7318 T22: 0.7888
REMARK 3 T33: 0.6699 T12: -0.0007
REMARK 3 T13: -0.1994 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 4.4372 L22: 2.7486
REMARK 3 L33: 1.9154 L12: -0.5039
REMARK 3 L13: -1.1664 L23: 1.3625
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: -0.3679 S13: 0.1129
REMARK 3 S21: 0.0648 S22: 0.3257 S23: 0.0706
REMARK 3 S31: 0.1165 S32: -0.3990 S33: -0.2956
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN C AND RESID 432:558 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.003 67.788 -5.675
REMARK 3 T TENSOR
REMARK 3 T11: 0.9004 T22: 0.8873
REMARK 3 T33: 0.8187 T12: 0.1136
REMARK 3 T13: -0.1194 T23: 0.1404
REMARK 3 L TENSOR
REMARK 3 L11: 5.3170 L22: 2.8234
REMARK 3 L33: 2.8326 L12: -0.3971
REMARK 3 L13: 0.0834 L23: -0.0249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0657 S12: -0.7950 S13: 0.0916
REMARK 3 S21: 0.3852 S22: 0.4418 S23: 0.2725
REMARK 3 S31: -0.1605 S32: -0.5159 S33: -0.4323
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN C AND RESID 559:614 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.250 74.932 -10.553
REMARK 3 T TENSOR
REMARK 3 T11: 0.7600 T22: 0.7639
REMARK 3 T33: 0.7444 T12: 0.0832
REMARK 3 T13: -0.0526 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 6.4571 L22: 3.3705
REMARK 3 L33: 4.5335 L12: -1.5936
REMARK 3 L13: 3.0715 L23: -1.3171
REMARK 3 S TENSOR
REMARK 3 S11: -0.5603 S12: -0.9473 S13: 0.9689
REMARK 3 S21: 0.4807 S22: 0.3316 S23: -0.1096
REMARK 3 S31: -0.4319 S32: -0.5432 S33: 0.3000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN D AND RESID 333:364 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.872 32.226 14.481
REMARK 3 T TENSOR
REMARK 3 T11: 1.0207 T22: 1.4445
REMARK 3 T33: 1.1117 T12: 0.1780
REMARK 3 T13: -0.1471 T23: 0.2324
REMARK 3 L TENSOR
REMARK 3 L11: 5.6816 L22: 4.7538
REMARK 3 L33: 5.6159 L12: -0.1084
REMARK 3 L13: -0.5832 L23: 0.7152
REMARK 3 S TENSOR
REMARK 3 S11: 0.3755 S12: -0.2510 S13: -0.7369
REMARK 3 S21: 0.0553 S22: -0.0654 S23: -0.8837
REMARK 3 S31: 0.8709 S32: 0.4574 S33: -0.0701
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ( CHAIN D AND RESID 365:459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.183 43.290 11.663
REMARK 3 T TENSOR
REMARK 3 T11: 1.1147 T22: 1.2142
REMARK 3 T33: 0.8965 T12: 0.0682
REMARK 3 T13: -0.2377 T23: 0.1974
REMARK 3 L TENSOR
REMARK 3 L11: 5.7510 L22: 2.8481
REMARK 3 L33: 3.6011 L12: 0.5402
REMARK 3 L13: 0.2310 L23: 0.3572
REMARK 3 S TENSOR
REMARK 3 S11: -0.1506 S12: -0.8037 S13: -0.1422
REMARK 3 S21: -0.2967 S22: 0.0622 S23: -0.0575
REMARK 3 S31: -0.0468 S32: 0.3602 S33: 0.1093
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: ( CHAIN D AND RESID 460:506 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.072 45.930 24.573
REMARK 3 T TENSOR
REMARK 3 T11: 1.0867 T22: 1.7286
REMARK 3 T33: 0.8196 T12: 0.0609
REMARK 3 T13: -0.1052 T23: 0.1203
REMARK 3 L TENSOR
REMARK 3 L11: 3.9807 L22: 2.5986
REMARK 3 L33: 0.8808 L12: -1.7405
REMARK 3 L13: -0.6005 L23: -0.7172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0456 S12: -1.6814 S13: -0.0998
REMARK 3 S21: 0.7981 S22: 0.2411 S23: 0.0144
REMARK 3 S31: -0.4535 S32: -0.0648 S33: -0.1152
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: ( CHAIN D AND RESID 507:526 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.691 39.423 14.213
REMARK 3 T TENSOR
REMARK 3 T11: 1.0414 T22: 1.5413
REMARK 3 T33: 0.8785 T12: -0.0571
REMARK 3 T13: -0.0948 T23: 0.0969
REMARK 3 L TENSOR
REMARK 3 L11: 7.3274 L22: 6.8793
REMARK 3 L33: 5.7762 L12: 0.9957
REMARK 3 L13: 2.3779 L23: 1.1683
REMARK 3 S TENSOR
REMARK 3 S11: 0.1666 S12: 0.3049 S13: -0.7815
REMARK 3 S21: 0.2397 S22: 0.2748 S23: -0.7816
REMARK 3 S31: -0.4012 S32: 1.1683 S33: -0.5381
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 7WBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1300026403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38716
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.340
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.16200
REMARK 200 R SYM (I) : 0.16200
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.30700
REMARK 200 R SYM FOR SHELL (I) : 1.30700
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6LZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5,10%W/V PEG 5000
REMARK 280 MME,12% V/V 1-PROPANOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 71.82700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ARG B 319
REMARK 465 VAL B 320
REMARK 465 GLN B 321
REMARK 465 PRO B 322
REMARK 465 THR B 323
REMARK 465 GLU B 324
REMARK 465 SER B 325
REMARK 465 ILE B 326
REMARK 465 VAL B 327
REMARK 465 ARG B 328
REMARK 465 PHE B 329
REMARK 465 PRO B 330
REMARK 465 ASN B 331
REMARK 465 ILE B 332
REMARK 465 LYS B 528
REMARK 465 LYS B 529
REMARK 465 SER B 530
REMARK 465 THR B 531
REMARK 465 ASN B 532
REMARK 465 LEU B 533
REMARK 465 VAL B 534
REMARK 465 LYS B 535
REMARK 465 ASN B 536
REMARK 465 LYS B 537
REMARK 465 CYS B 538
REMARK 465 VAL B 539
REMARK 465 ASN B 540
REMARK 465 PHE B 541
REMARK 465 ARG D 319
REMARK 465 VAL D 320
REMARK 465 GLN D 321
REMARK 465 PRO D 322
REMARK 465 THR D 323
REMARK 465 GLU D 324
REMARK 465 SER D 325
REMARK 465 ILE D 326
REMARK 465 VAL D 327
REMARK 465 ARG D 328
REMARK 465 PHE D 329
REMARK 465 PRO D 330
REMARK 465 ASN D 331
REMARK 465 ILE D 332
REMARK 465 PRO D 527
REMARK 465 LYS D 528
REMARK 465 LYS D 529
REMARK 465 SER D 530
REMARK 465 THR D 531
REMARK 465 ASN D 532
REMARK 465 LEU D 533
REMARK 465 VAL D 534
REMARK 465 LYS D 535
REMARK 465 ASN D 536
REMARK 465 LYS D 537
REMARK 465 CYS D 538
REMARK 465 VAL D 539
REMARK 465 ASN D 540
REMARK 465 PHE D 541
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 ARG C 161 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP C 198 N ASP C 201 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 53 77.66 -151.11
REMARK 500 ASN A 137 83.17 -151.94
REMARK 500 LEU A 156 45.09 -141.06
REMARK 500 ARG A 273 -73.29 -83.53
REMARK 500 ASN A 338 -127.56 57.65
REMARK 500 MET A 360 117.39 -160.09
REMARK 500 GLN A 472 19.14 -140.64
REMARK 500 ASP A 494 -168.35 -73.65
REMARK 500 CYS A 498 58.13 -147.74
REMARK 500 SER A 547 79.98 -152.81
REMARK 500 ALA B 352 51.07 -107.80
REMARK 500 PHE B 377 84.19 -155.43
REMARK 500 ASN B 422 -51.88 -135.24
REMARK 500 ASP B 428 37.40 -98.07
REMARK 500 SER B 477 20.12 -146.76
REMARK 500 ALA B 522 72.22 58.55
REMARK 500 ASN C 53 100.70 -162.94
REMARK 500 ASP C 136 -4.94 85.37
REMARK 500 ASN C 194 39.35 -82.99
REMARK 500 ASN C 338 -128.24 52.65
REMARK 500 GLN C 340 109.28 -48.70
REMARK 500 MET C 360 118.34 -166.62
REMARK 500 GLU C 495 47.93 -79.03
REMARK 500 CYS C 498 53.87 -144.28
REMARK 500 ASN C 601 60.44 -107.36
REMARK 500 ALA D 352 70.21 -107.06
REMARK 500 ASN D 370 42.46 -109.12
REMARK 500 PHE D 377 79.48 -154.69
REMARK 500 ASN D 422 -50.40 -133.60
REMARK 500 ASP D 428 47.07 -95.07
REMARK 500 CYS D 525 -74.76 -106.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374 NE2
REMARK 620 2 HIS A 378 NE2 110.3
REMARK 620 3 GLU A 402 OE2 89.4 98.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 374 NE2
REMARK 620 2 HIS C 378 NE2 94.4
REMARK 620 3 GLU C 402 OE2 91.9 106.2
REMARK 620 N 1 2
DBREF 7WBQ A 19 614 UNP Q9BYF1 ACE2_HUMAN 19 614
DBREF 7WBQ B 319 541 UNP P0DTC2 SPIKE_SARS2 319 541
DBREF 7WBQ C 19 614 UNP Q9BYF1 ACE2_HUMAN 19 614
DBREF 7WBQ D 319 541 UNP P0DTC2 SPIKE_SARS2 319 541
SEQADV 7WBQ ARG B 452 UNP P0DTC2 LEU 452 VARIANT
SEQADV 7WBQ LYS B 478 UNP P0DTC2 THR 478 ENGINEERED MUTATION
SEQADV 7WBQ ARG D 452 UNP P0DTC2 LEU 452 VARIANT
SEQADV 7WBQ LYS D 478 UNP P0DTC2 THR 478 ENGINEERED MUTATION
SEQRES 1 A 596 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS
SEQRES 2 A 596 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER
SEQRES 3 A 596 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU
SEQRES 4 A 596 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER
SEQRES 5 A 596 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR
SEQRES 6 A 596 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN
SEQRES 7 A 596 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER
SEQRES 8 A 596 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR
SEQRES 9 A 596 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO
SEQRES 10 A 596 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU
SEQRES 11 A 596 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG
SEQRES 12 A 596 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS
SEQRES 13 A 596 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS
SEQRES 14 A 596 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY
SEQRES 15 A 596 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP
SEQRES 16 A 596 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL
SEQRES 17 A 596 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS
SEQRES 18 A 596 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR
SEQRES 19 A 596 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS
SEQRES 20 A 596 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU
SEQRES 21 A 596 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE
SEQRES 22 A 596 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA
SEQRES 23 A 596 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER
SEQRES 24 A 596 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN
SEQRES 25 A 596 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL
SEQRES 26 A 596 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE
SEQRES 27 A 596 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE
SEQRES 28 A 596 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP
SEQRES 29 A 596 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY
SEQRES 30 A 596 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET
SEQRES 31 A 596 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE
SEQRES 32 A 596 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR
SEQRES 33 A 596 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL
SEQRES 34 A 596 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG
SEQRES 35 A 596 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP
SEQRES 36 A 596 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY
SEQRES 37 A 596 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP
SEQRES 38 A 596 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE
SEQRES 39 A 596 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE
SEQRES 40 A 596 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO
SEQRES 41 A 596 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY
SEQRES 42 A 596 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU
SEQRES 43 A 596 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS
SEQRES 44 A 596 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO
SEQRES 45 A 596 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE
SEQRES 46 A 596 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA
SEQRES 1 B 223 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN
SEQRES 2 B 223 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA
SEQRES 3 B 223 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG
SEQRES 4 B 223 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN
SEQRES 5 B 223 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER
SEQRES 6 B 223 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR
SEQRES 7 B 223 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN
SEQRES 8 B 223 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN
SEQRES 9 B 223 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA
SEQRES 10 B 223 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN
SEQRES 11 B 223 TYR ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU
SEQRES 12 B 223 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN
SEQRES 13 B 223 ALA GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN
SEQRES 14 B 223 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR
SEQRES 15 B 223 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU
SEQRES 16 B 223 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY
SEQRES 17 B 223 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL
SEQRES 18 B 223 ASN PHE
SEQRES 1 C 596 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS
SEQRES 2 C 596 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER
SEQRES 3 C 596 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU
SEQRES 4 C 596 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER
SEQRES 5 C 596 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR
SEQRES 6 C 596 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN
SEQRES 7 C 596 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER
SEQRES 8 C 596 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR
SEQRES 9 C 596 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO
SEQRES 10 C 596 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU
SEQRES 11 C 596 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG
SEQRES 12 C 596 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS
SEQRES 13 C 596 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS
SEQRES 14 C 596 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY
SEQRES 15 C 596 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP
SEQRES 16 C 596 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL
SEQRES 17 C 596 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS
SEQRES 18 C 596 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR
SEQRES 19 C 596 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS
SEQRES 20 C 596 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU
SEQRES 21 C 596 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE
SEQRES 22 C 596 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA
SEQRES 23 C 596 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER
SEQRES 24 C 596 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN
SEQRES 25 C 596 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL
SEQRES 26 C 596 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE
SEQRES 27 C 596 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE
SEQRES 28 C 596 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP
SEQRES 29 C 596 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY
SEQRES 30 C 596 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET
SEQRES 31 C 596 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE
SEQRES 32 C 596 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR
SEQRES 33 C 596 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL
SEQRES 34 C 596 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG
SEQRES 35 C 596 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP
SEQRES 36 C 596 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY
SEQRES 37 C 596 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP
SEQRES 38 C 596 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE
SEQRES 39 C 596 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE
SEQRES 40 C 596 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO
SEQRES 41 C 596 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY
SEQRES 42 C 596 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU
SEQRES 43 C 596 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS
SEQRES 44 C 596 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO
SEQRES 45 C 596 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE
SEQRES 46 C 596 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA
SEQRES 1 D 223 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN
SEQRES 2 D 223 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA
SEQRES 3 D 223 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG
SEQRES 4 D 223 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN
SEQRES 5 D 223 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER
SEQRES 6 D 223 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR
SEQRES 7 D 223 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN
SEQRES 8 D 223 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN
SEQRES 9 D 223 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA
SEQRES 10 D 223 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN
SEQRES 11 D 223 TYR ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU
SEQRES 12 D 223 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN
SEQRES 13 D 223 ALA GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN
SEQRES 14 D 223 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR
SEQRES 15 D 223 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU
SEQRES 16 D 223 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY
SEQRES 17 D 223 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL
SEQRES 18 D 223 ASN PHE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET FUL F 2 10
HET NAG G 1 14
HET NAG G 2 14
HET NAG A 701 14
HET ZN A 702 1
HET NAG A 703 14
HET NAG A 704 14
HET NAG A 705 14
HET NAG C 701 14
HET ZN C 702 1
HET NAG C 703 14
HET NAG C 704 14
HET NAG C 705 14
HET NAG C 706 14
HET NAG D 601 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM ZN ZINC ION
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
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
FORMUL 5 NAG 15(C8 H15 N O6)
FORMUL 6 FUL C6 H12 O5
FORMUL 9 ZN 2(ZN 2+)
HELIX 1 AA1 THR A 20 ASN A 53 1 34
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 101 1 12
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 GLY A 205 1 8
HELIX 12 AB3 ASP A 206 GLU A 208 5 3
HELIX 13 AB4 GLY A 220 ASN A 250 1 31
HELIX 14 AB5 HIS A 265 LEU A 267 5 3
HELIX 15 AB6 TRP A 275 ASN A 277 5 3
HELIX 16 AB7 LEU A 278 VAL A 283 1 6
HELIX 17 AB8 VAL A 293 GLN A 300 1 8
HELIX 18 AB9 ASP A 303 SER A 317 1 15
HELIX 19 AC1 THR A 324 SER A 331 1 8
HELIX 20 AC2 THR A 365 TYR A 385 1 21
HELIX 21 AC3 PRO A 389 ARG A 393 5 5
HELIX 22 AC4 GLY A 399 THR A 414 1 16
HELIX 23 AC5 THR A 414 ILE A 421 1 8
HELIX 24 AC6 ASP A 431 GLY A 466 1 36
HELIX 25 AC7 PRO A 469 ASP A 471 5 3
HELIX 26 AC8 GLN A 472 ILE A 484 1 13
HELIX 27 AC9 CYS A 498 SER A 502 5 5
HELIX 28 AD1 LEU A 503 ASN A 508 1 6
HELIX 29 AD2 ILE A 513 ALA A 533 1 21
HELIX 30 AD3 PRO A 538 CYS A 542 5 5
HELIX 31 AD4 SER A 547 ARG A 559 1 13
HELIX 32 AD5 PRO A 565 GLY A 575 1 11
HELIX 33 AD6 VAL A 581 LYS A 596 1 16
HELIX 34 AD7 PRO B 337 ASN B 343 1 7
HELIX 35 AD8 SER B 349 TRP B 353 5 5
HELIX 36 AD9 ASP B 364 ASN B 370 1 7
HELIX 37 AE1 LYS B 386 LEU B 390 5 5
HELIX 38 AE2 ASP 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 TYR B 505 5 4
HELIX 42 AE6 THR C 20 ASN C 53 1 34
HELIX 43 AE7 THR C 55 GLN C 81 1 27
HELIX 44 AE8 MET C 82 TYR C 83 5 2
HELIX 45 AE9 PRO C 84 ILE C 88 5 5
HELIX 46 AF1 ASN C 90 GLN C 102 1 13
HELIX 47 AF2 ASN C 103 LEU C 108 5 6
HELIX 48 AF3 SER C 109 GLY C 130 1 22
HELIX 49 AF4 PRO C 146 SER C 155 1 10
HELIX 50 AF5 ASP C 157 ASN C 194 1 38
HELIX 51 AF6 ASP C 198 ARG C 204 1 7
HELIX 52 AF7 GLY C 205 GLU C 208 5 4
HELIX 53 AF8 SER C 218 TYR C 252 1 35
HELIX 54 AF9 HIS C 265 LEU C 267 5 3
HELIX 55 AG1 TRP C 275 ASN C 277 5 3
HELIX 56 AG2 LEU C 278 VAL C 283 1 6
HELIX 57 AG3 VAL C 293 GLN C 300 1 8
HELIX 58 AG4 ASP C 303 VAL C 318 1 16
HELIX 59 AG5 THR C 324 SER C 331 1 8
HELIX 60 AG6 THR C 365 TYR C 385 1 21
HELIX 61 AG7 PRO C 389 ARG C 393 5 5
HELIX 62 AG8 GLY C 399 ALA C 413 1 15
HELIX 63 AG9 THR C 414 ILE C 421 1 8
HELIX 64 AH1 ASP C 431 GLY C 466 1 36
HELIX 65 AH2 PRO C 469 ASP C 471 5 3
HELIX 66 AH3 GLN C 472 ILE C 484 1 13
HELIX 67 AH4 CYS C 498 SER C 502 5 5
HELIX 68 AH5 LEU C 503 ASN C 508 1 6
HELIX 69 AH6 ILE C 513 ALA C 533 1 21
HELIX 70 AH7 PRO C 538 CYS C 542 5 5
HELIX 71 AH8 SER C 547 ARG C 559 1 13
HELIX 72 AH9 PRO C 565 GLY C 575 1 11
HELIX 73 AI1 VAL C 581 ASN C 599 1 19
HELIX 74 AI2 LYS C 600 SER C 602 5 3
HELIX 75 AI3 PRO D 337 ASN D 343 1 7
HELIX 76 AI4 ASP D 364 ASN D 370 1 7
HELIX 77 AI5 ASP D 405 ILE D 410 5 6
HELIX 78 AI6 GLY D 416 ASN D 422 1 7
HELIX 79 AI7 SER D 438 SER D 443 1 6
HELIX 80 AI8 GLY D 502 TYR D 505 5 4
SHEET 1 AA1 2 LYS A 131 ASN A 134 0
SHEET 2 AA1 2 ASN A 137 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 TYR B 508 N ILE B 402
SHEET 4 AA4 5 GLY B 431 ASN B 437 -1 N TRP B 436 O ARG B 509
SHEET 5 AA4 5 THR B 376 TYR B 380 -1 N TYR B 380 O GLY B 431
SHEET 1 AA5 2 ARG B 452 ARG B 454 0
SHEET 2 AA5 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453
SHEET 1 AA6 2 TYR B 473 GLN B 474 0
SHEET 2 AA6 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473
SHEET 1 AA7 2 VAL C 132 CYS C 133 0
SHEET 2 AA7 2 CYS C 141 LEU C 142 -1 O LEU C 142 N VAL C 132
SHEET 1 AA8 2 LEU C 262 PRO C 263 0
SHEET 2 AA8 2 VAL C 487 VAL C 488 1 O VAL C 488 N LEU C 262
SHEET 1 AA9 2 THR C 347 GLY C 352 0
SHEET 2 AA9 2 ASP C 355 LEU C 359 -1 O ARG C 357 N TRP C 349
SHEET 1 AB1 5 ASN D 354 ILE D 358 0
SHEET 2 AB1 5 ASN D 394 ARG D 403 -1 O VAL D 395 N ILE D 358
SHEET 3 AB1 5 PRO D 507 GLU D 516 -1 O TYR D 508 N ILE D 402
SHEET 4 AB1 5 GLY D 431 ASN D 437 -1 N ILE D 434 O VAL D 511
SHEET 5 AB1 5 THR D 376 TYR D 380 -1 N TYR D 380 O GLY D 431
SHEET 1 AB2 2 ARG D 452 ARG D 454 0
SHEET 2 AB2 2 LEU D 492 SER D 494 -1 O GLN D 493 N TYR D 453
SHEET 1 AB3 2 TYR D 473 GLN D 474 0
SHEET 2 AB3 2 CYS D 488 TYR D 489 -1 O TYR D 489 N TYR D 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
SSBOND 8 CYS C 133 CYS C 141 1555 1555 2.03
SSBOND 9 CYS C 344 CYS C 361 1555 1555 2.03
SSBOND 10 CYS C 530 CYS C 542 1555 1555 2.03
SSBOND 11 CYS D 336 CYS D 361 1555 1555 2.03
SSBOND 12 CYS D 379 CYS D 432 1555 1555 2.03
SSBOND 13 CYS D 391 CYS D 525 1555 1555 2.03
SSBOND 14 CYS D 480 CYS D 488 1555 1555 2.03
LINK ND2 ASN A 53 C1 NAG A 703 1555 1555 1.43
LINK ND2 ASN A 90 C1 NAG E 1 1555 1555 1.46
LINK ND2 ASN A 103 C1 NAG A 705 1555 1555 1.44
LINK ND2 ASN A 322 C1 NAG A 701 1555 1555 1.45
LINK ND2 ASN A 546 C1 NAG A 704 1555 1555 1.46
LINK ND2 ASN B 343 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN C 53 C1 NAG C 701 1555 1555 1.44
LINK ND2 ASN C 90 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN C 103 C1 NAG C 704 1555 1555 1.44
LINK ND2 ASN C 322 C1 NAG C 706 1555 1555 1.45
LINK ND2 ASN C 432 C1 NAG C 705 1555 1555 1.44
LINK ND2 ASN C 546 C1 NAG C 703 1555 1555 1.45
LINK ND2 ASN D 343 C1 NAG D 601 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46
LINK O6 NAG F 1 C1 FUL F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK NE2 HIS A 374 ZN ZN A 702 1555 1555 2.09
LINK NE2 HIS A 378 ZN ZN A 702 1555 1555 2.09
LINK OE2 GLU A 402 ZN ZN A 702 1555 1555 2.09
LINK NE2 HIS C 374 ZN ZN C 702 1555 1555 2.10
LINK NE2 HIS C 378 ZN ZN C 702 1555 1555 2.11
LINK OE2 GLU C 402 ZN ZN C 702 1555 1555 2.09
CISPEP 1 GLU A 145 PRO A 146 0 4.50
CISPEP 2 GLU C 145 PRO C 146 0 5.86
CRYST1 89.773 143.654 106.414 90.00 95.29 90.00 P 1 21 1 4
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 0.011139 0.000000 0.001031 0.00000
SCALE2 0.000000 0.006961 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009437 0.00000
ATOM 1 N SER A 19 33.472 58.470 46.809 1.00122.89 N
ANISOU 1 N SER A 19 17410 15709 13572 -2992 -1788 1564 N
ATOM 2 CA SER A 19 32.316 59.068 47.466 1.00108.72 C
ANISOU 2 CA SER A 19 15699 13692 11916 -2734 -2103 1758 C
ATOM 3 C SER A 19 31.047 58.879 46.640 1.00135.72 C
ANISOU 3 C SER A 19 19249 17241 15076 -2826 -2230 1962 C
ATOM 4 O SER A 19 30.042 59.546 46.879 1.00144.07 O
ANISOU 4 O SER A 19 20371 18117 16252 -2696 -2506 2180 O
ATOM 5 CB SER A 19 32.555 60.559 47.723 1.00110.34 C
ANISOU 5 CB SER A 19 15941 13641 12341 -2759 -2317 2006 C
ATOM 6 OG SER A 19 33.092 61.201 46.578 1.00119.60 O
ANISOU 6 OG SER A 19 17184 14930 13327 -3164 -2269 2230 O
ATOM 7 N THR A 20 31.099 57.970 45.668 1.00133.28 N
ANISOU 7 N THR A 20 18971 17231 14440 -3053 -2038 1873 N
ATOM 8 CA THR A 20 29.941 57.717 44.826 1.00117.15 C
ANISOU 8 CA THR A 20 17063 15314 12136 -3161 -2182 2051 C
ATOM 9 C THR A 20 28.799 57.131 45.651 1.00123.85 C
ANISOU 9 C THR A 20 17849 16042 13167 -2794 -2312 1966 C
ATOM 10 O THR A 20 29.000 56.564 46.729 1.00121.05 O
ANISOU 10 O THR A 20 17366 15597 13029 -2502 -2206 1709 O
ATOM 11 CB THR A 20 30.291 56.760 43.684 1.00117.08 C
ANISOU 11 CB THR A 20 17103 15652 11728 -3468 -1925 1910 C
ATOM 12 OG1 THR A 20 30.134 55.406 44.126 1.00125.01 O
ANISOU 12 OG1 THR A 20 17977 16745 12776 -3250 -1769 1573 O
ATOM 13 CG2 THR A 20 31.725 56.972 43.233 1.00123.17 C
ANISOU 13 CG2 THR A 20 17842 16546 12411 -3756 -1634 1811 C
ATOM 14 N ILE A 21 27.581 57.282 45.126 1.00127.55 N
ANISOU 14 N ILE A 21 18415 16495 13555 -2825 -2556 2194 N
ATOM 15 CA ILE A 21 26.415 56.709 45.791 1.00117.16 C
ANISOU 15 CA ILE A 21 17022 15070 12423 -2511 -2658 2122 C
ATOM 16 C ILE A 21 26.523 55.190 45.838 1.00115.44 C
ANISOU 16 C ILE A 21 16722 15058 12081 -2444 -2409 1801 C
ATOM 17 O ILE A 21 26.087 54.552 46.805 1.00122.72 O
ANISOU 17 O ILE A 21 17537 15881 13210 -2138 -2365 1627 O
ATOM 18 CB ILE A 21 25.122 57.168 45.095 1.00114.54 C
ANISOU 18 CB ILE A 21 16783 14665 12070 -2590 -2992 2432 C
ATOM 19 CG1 ILE A 21 25.148 58.682 44.872 1.00119.03 C
ANISOU 19 CG1 ILE A 21 17440 15032 12751 -2718 -3260 2768 C
ATOM 20 CG2 ILE A 21 23.912 56.766 45.916 1.00119.72 C
ANISOU 20 CG2 ILE A 21 17318 15147 13023 -2245 -3088 2362 C
ATOM 21 CD1 ILE A 21 25.044 59.491 46.148 1.00126.01 C
ANISOU 21 CD1 ILE A 21 18211 15591 14076 -2398 -3343 2751 C
ATOM 22 N GLU A 22 27.106 54.587 44.798 1.00107.27 N
ANISOU 22 N GLU A 22 15741 14307 10710 -2739 -2236 1712 N
ATOM 23 CA GLU A 22 27.385 53.154 44.824 1.00115.30 C
ANISOU 23 CA GLU A 22 16655 15508 11646 -2689 -1987 1370 C
ATOM 24 C GLU A 22 28.276 52.788 46.004 1.00113.32 C
ANISOU 24 C GLU A 22 16244 15149 11662 -2451 -1802 1093 C
ATOM 25 O GLU A 22 27.926 51.929 46.822 1.00108.83 O
ANISOU 25 O GLU A 22 15577 14515 11258 -2185 -1767 909 O
ATOM 26 CB GLU A 22 28.048 52.712 43.520 1.00117.71 C
ANISOU 26 CB GLU A 22 17041 16123 11561 -3071 -1791 1283 C
ATOM 27 CG GLU A 22 28.584 51.290 43.605 1.00119.06 C
ANISOU 27 CG GLU A 22 17062 16456 11719 -3019 -1505 877 C
ATOM 28 CD GLU A 22 29.108 50.765 42.287 1.00126.92 C
ANISOU 28 CD GLU A 22 18134 17765 12325 -3393 -1286 742 C
ATOM 29 OE1 GLU A 22 28.360 50.796 41.288 1.00129.84 O
ANISOU 29 OE1 GLU A 22 18689 18268 12374 -3604 -1423 914 O
ATOM 30 OE2 GLU A 22 30.270 50.308 42.255 1.00126.67 O1-
ANISOU 30 OE2 GLU A 22 17975 17835 12318 -3479 -978 448 O1-
ATOM 31 N GLU A 23 29.452 53.423 46.092 1.00117.86 N
ANISOU 31 N GLU A 23 16798 15694 12289 -2561 -1696 1068 N
ATOM 32 CA GLU A 23 30.396 53.122 47.166 1.00109.42 C
ANISOU 32 CA GLU A 23 15584 14499 11490 -2361 -1567 810 C
ATOM 33 C GLU A 23 29.745 53.247 48.535 1.00105.13 C
ANISOU 33 C GLU A 23 15032 13692 11223 -1986 -1729 824 C
ATOM 34 O GLU A 23 29.951 52.396 49.408 1.00108.46 O
ANISOU 34 O GLU A 23 15368 14050 11792 -1772 -1656 588 O
ATOM 35 CB GLU A 23 31.608 54.051 47.077 1.00107.48 C
ANISOU 35 CB GLU A 23 15320 14201 11316 -2530 -1499 847 C
ATOM 36 CG GLU A 23 32.405 53.939 45.796 1.00121.40 C
ANISOU 36 CG GLU A 23 17087 16224 12815 -2925 -1264 799 C
ATOM 37 CD GLU A 23 33.466 55.013 45.693 1.00127.47 C
ANISOU 37 CD GLU A 23 17841 16914 13678 -3108 -1212 896 C
ATOM 38 OE1 GLU A 23 33.606 55.803 46.651 1.00119.10 O
ANISOU 38 OE1 GLU A 23 16760 15588 12907 -2906 -1383 981 O
ATOM 39 OE2 GLU A 23 34.145 55.081 44.648 1.00141.67 O1-
ANISOU 39 OE2 GLU A 23 19657 18914 15258 -3465 -992 884 O1-
ATOM 40 N GLN A 24 28.960 54.309 48.742 1.00 94.70 N
ANISOU 40 N GLN A 24 13803 12201 9978 -1914 -1950 1094 N
ATOM 41 CA GLN A 24 28.206 54.449 49.984 1.00 98.24 C
ANISOU 41 CA GLN A 24 14253 12408 10666 -1577 -2068 1093 C
ATOM 42 C GLN A 24 27.326 53.232 50.234 1.00 99.25 C
ANISOU 42 C GLN A 24 14339 12597 10775 -1417 -2011 963 C
ATOM 43 O GLN A 24 27.267 52.719 51.357 1.00101.13 O
ANISOU 43 O GLN A 24 14552 12712 11161 -1169 -1963 802 O
ATOM 44 CB GLN A 24 27.348 55.713 49.936 1.00 91.87 C
ANISOU 44 CB GLN A 24 13521 11425 9961 -1556 -2307 1389 C
ATOM 45 CG GLN A 24 28.120 57.016 49.927 1.00 96.48 C
ANISOU 45 CG GLN A 24 14144 11877 10637 -1662 -2403 1533 C
ATOM 46 CD GLN A 24 27.246 58.182 49.520 1.00103.48 C
ANISOU 46 CD GLN A 24 15095 12620 11603 -1716 -2668 1855 C
ATOM 47 OE1 GLN A 24 26.023 58.127 49.649 1.00105.72 O
ANISOU 47 OE1 GLN A 24 15369 12818 11980 -1577 -2791 1930 O
ATOM 48 NE2 GLN A 24 27.865 59.237 49.004 1.00117.78 N
ANISOU 48 NE2 GLN A 24 16956 14386 13408 -1930 -2767 2049 N
ATOM 49 N ALA A 25 26.636 52.757 49.192 1.00 91.43 N
ANISOU 49 N ALA A 25 13355 11788 9597 -1572 -2029 1038 N
ATOM 50 CA ALA A 25 25.745 51.611 49.342 1.00 93.47 C
ANISOU 50 CA ALA A 25 13557 12096 9861 -1438 -1992 930 C
ATOM 51 C ALA A 25 26.525 50.326 49.592 1.00 89.06 C
ANISOU 51 C ALA A 25 12910 11652 9277 -1407 -1788 620 C
ATOM 52 O ALA A 25 26.094 49.483 50.386 1.00 96.48 O
ANISOU 52 O ALA A 25 13800 12520 10337 -1195 -1747 493 O
ATOM 53 CB ALA A 25 24.859 51.469 48.104 1.00 95.41 C
ANISOU 53 CB ALA A 25 13839 12492 9921 -1629 -2107 1088 C
ATOM 54 N LYS A 26 27.657 50.146 48.903 1.00 86.24 N
ANISOU 54 N LYS A 26 12522 11460 8785 -1628 -1654 494 N
ATOM 55 CA LYS A 26 28.581 49.067 49.243 1.00 86.40 C
ANISOU 55 CA LYS A 26 12422 11530 8878 -1588 -1480 178 C
ATOM 56 C LYS A 26 28.877 49.064 50.738 1.00103.22 C
ANISOU 56 C LYS A 26 14540 13411 11267 -1307 -1519 92 C
ATOM 57 O LYS A 26 28.691 48.055 51.426 1.00103.93 O
ANISOU 57 O LYS A 26 14584 13447 11458 -1136 -1493 -63 O
ATOM 58 CB LYS A 26 29.883 49.215 48.450 1.00 88.98 C
ANISOU 58 CB LYS A 26 12695 12003 9110 -1856 -1319 58 C
ATOM 59 CG LYS A 26 29.808 48.856 46.978 1.00 92.25 C
ANISOU 59 CG LYS A 26 13131 12704 9215 -2165 -1207 40 C
ATOM 60 CD LYS A 26 31.211 48.801 46.390 1.00 95.26 C
ANISOU 60 CD LYS A 26 13421 13217 9558 -2408 -966 -166 C
ATOM 61 CE LYS A 26 31.273 47.941 45.141 1.00116.49 C
ANISOU 61 CE LYS A 26 16094 16197 11971 -2670 -773 -346 C
ATOM 62 NZ LYS A 26 32.680 47.613 44.778 1.00120.82 N
ANISOU 62 NZ LYS A 26 16484 16844 12580 -2854 -478 -653 N
ATOM 63 N THR A 27 29.339 50.207 51.250 1.00111.02 N
ANISOU 63 N THR A 27 15590 14236 12355 -1272 -1599 200 N
ATOM 64 CA THR A 27 29.593 50.352 52.680 1.00 93.67 C
ANISOU 64 CA THR A 27 13435 11789 10364 -1020 -1668 134 C
ATOM 65 C THR A 27 28.326 50.104 53.491 1.00 97.86 C
ANISOU 65 C THR A 27 14045 12206 10932 -788 -1725 201 C
ATOM 66 O THR A 27 28.342 49.350 54.471 1.00 91.21 O
ANISOU 66 O THR A 27 13223 11259 10174 -611 -1707 64 O
ATOM 67 CB THR A 27 30.149 51.746 52.966 1.00 88.58 C
ANISOU 67 CB THR A 27 12856 10990 9811 -1037 -1768 260 C
ATOM 68 OG1 THR A 27 31.467 51.858 52.416 1.00 89.91 O
ANISOU 68 OG1 THR A 27 12927 11231 10005 -1237 -1685 156 O
ATOM 69 CG2 THR A 27 30.206 51.999 54.459 1.00 93.21 C
ANISOU 69 CG2 THR A 27 13537 11309 10569 -774 -1869 208 C
ATOM 70 N PHE A 28 27.218 50.743 53.100 1.00102.03 N
ANISOU 70 N PHE A 28 14616 12735 11417 -796 -1797 416 N
ATOM 71 CA PHE A 28 25.933 50.475 53.740 1.00102.25 C
ANISOU 71 CA PHE A 28 14674 12662 11516 -599 -1810 466 C
ATOM 72 C PHE A 28 25.644 48.982 53.785 1.00 97.15 C
ANISOU 72 C PHE A 28 13958 12116 10838 -555 -1707 311 C
ATOM 73 O PHE A 28 25.361 48.419 54.848 1.00 97.95 O
ANISOU 73 O PHE A 28 14102 12094 11021 -368 -1662 227 O
ATOM 74 CB PHE A 28 24.810 51.204 52.998 1.00102.36 C
ANISOU 74 CB PHE A 28 14681 12683 11529 -662 -1920 701 C
ATOM 75 CG PHE A 28 23.439 50.652 53.286 1.00 99.68 C
ANISOU 75 CG PHE A 28 14299 12292 11281 -516 -1904 727 C
ATOM 76 CD1 PHE A 28 22.750 51.035 54.423 1.00 98.02 C
ANISOU 76 CD1 PHE A 28 14130 11863 11251 -292 -1882 735 C
ATOM 77 CD2 PHE A 28 22.845 49.742 52.423 1.00 96.24 C
ANISOU 77 CD2 PHE A 28 13781 12023 10763 -612 -1896 725 C
ATOM 78 CE1 PHE A 28 21.494 50.524 54.694 1.00 91.46 C
ANISOU 78 CE1 PHE A 28 13236 10977 10539 -171 -1828 747 C
ATOM 79 CE2 PHE A 28 21.592 49.226 52.692 1.00 93.19 C
ANISOU 79 CE2 PHE A 28 13329 11570 10507 -482 -1883 748 C
ATOM 80 CZ PHE A 28 20.915 49.619 53.827 1.00 92.80 C
ANISOU 80 CZ PHE A 28 13300 11300 10661 -264 -1837 762 C
ATOM 81 N LEU A 29 25.713 48.326 52.625 1.00 94.20 N
ANISOU 81 N LEU A 29 13493 11962 10336 -741 -1670 271 N
ATOM 82 CA LEU A 29 25.452 46.894 52.553 1.00 96.08 C
ANISOU 82 CA LEU A 29 13646 12294 10569 -714 -1590 113 C
ATOM 83 C LEU A 29 26.450 46.100 53.381 1.00 88.60 C
ANISOU 83 C LEU A 29 12675 11275 9714 -627 -1529 -112 C
ATOM 84 O LEU A 29 26.106 45.044 53.925 1.00 78.96 O
ANISOU 84 O LEU A 29 11427 10012 8563 -511 -1498 -209 O
ATOM 85 CB LEU A 29 25.492 46.439 51.096 1.00 93.85 C
ANISOU 85 CB LEU A 29 13286 12261 10112 -953 -1564 80 C
ATOM 86 CG LEU A 29 24.181 46.506 50.316 1.00 82.52 C
ANISOU 86 CG LEU A 29 11854 10892 8607 -1010 -1662 255 C
ATOM 87 CD1 LEU A 29 24.324 45.714 49.042 1.00 94.72 C
ANISOU 87 CD1 LEU A 29 13347 12684 9956 -1232 -1623 146 C
ATOM 88 CD2 LEU A 29 23.022 45.977 51.145 1.00 82.15 C
ANISOU 88 CD2 LEU A 29 11772 10701 8742 -784 -1673 282 C
ATOM 89 N ASP A 30 27.688 46.588 53.485 1.00 99.73 N
ANISOU 89 N ASP A 30 14088 12650 11153 -688 -1533 -189 N
ATOM 90 CA ASP A 30 28.705 45.882 54.258 1.00 99.79 C
ANISOU 90 CA ASP A 30 14061 12552 11302 -612 -1530 -402 C
ATOM 91 C ASP A 30 28.323 45.816 55.731 1.00 89.62 C
ANISOU 91 C ASP A 30 12923 11032 10098 -377 -1602 -369 C
ATOM 92 O ASP A 30 28.417 44.758 56.364 1.00 83.25 O
ANISOU 92 O ASP A 30 12112 10152 9367 -287 -1613 -491 O
ATOM 93 CB ASP A 30 30.059 46.567 54.078 1.00 95.42 C
ANISOU 93 CB ASP A 30 13467 11977 10813 -726 -1538 -475 C
ATOM 94 CG ASP A 30 31.219 45.617 54.261 1.00104.63 C
ANISOU 94 CG ASP A 30 14493 13106 12157 -740 -1518 -748 C
ATOM 95 OD1 ASP A 30 30.971 44.414 54.484 1.00102.51 O
ANISOU 95 OD1 ASP A 30 14168 12835 11948 -668 -1513 -872 O
ATOM 96 OD2 ASP A 30 32.379 46.074 54.181 1.00107.37 O1-
ANISOU 96 OD2 ASP A 30 14768 13405 12624 -825 -1519 -839 O1-
ATOM 97 N LYS A 31 27.886 46.946 56.291 1.00 87.91 N
ANISOU 97 N LYS A 31 12850 10689 9863 -287 -1652 -208 N
ATOM 98 CA LYS A 31 27.401 46.965 57.668 1.00 94.24 C
ANISOU 98 CA LYS A 31 13828 11284 10693 -84 -1678 -183 C
ATOM 99 C LYS A 31 26.183 46.065 57.834 1.00 91.75 C
ANISOU 99 C LYS A 31 13505 10999 10356 -8 -1587 -151 C
ATOM 100 O LYS A 31 26.081 45.313 58.810 1.00103.99 O
ANISOU 100 O LYS A 31 15156 12434 11921 102 -1576 -210 O
ATOM 101 CB LYS A 31 27.075 48.403 58.079 1.00 99.90 C
ANISOU 101 CB LYS A 31 14672 11874 11410 -18 -1721 -42 C
ATOM 102 CG LYS A 31 26.084 48.532 59.230 1.00100.10 C
ANISOU 102 CG LYS A 31 14866 11737 11430 167 -1670 4 C
ATOM 103 CD LYS A 31 26.698 48.204 60.580 1.00 83.73 C
ANISOU 103 CD LYS A 31 12997 9482 9336 280 -1721 -110 C
ATOM 104 CE LYS A 31 25.763 48.627 61.705 1.00105.25 C
ANISOU 104 CE LYS A 31 15929 12048 12013 434 -1635 -69 C
ATOM 105 NZ LYS A 31 26.331 48.359 63.055 1.00130.84 N
ANISOU 105 NZ LYS A 31 19436 15107 15168 521 -1701 -165 N
ATOM 106 N PHE A 32 25.247 46.129 56.881 1.00 86.46 N
ANISOU 106 N PHE A 32 12724 10469 9658 -78 -1538 -46 N
ATOM 107 CA PHE A 32 24.020 45.341 56.971 1.00 92.74 C
ANISOU 107 CA PHE A 32 13478 11278 10482 -11 -1457 -8 C
ATOM 108 C PHE A 32 24.315 43.853 57.111 1.00 95.81 C
ANISOU 108 C PHE A 32 13808 11701 10895 -12 -1433 -157 C
ATOM 109 O PHE A 32 23.745 43.177 57.973 1.00102.84 O
ANISOU 109 O PHE A 32 14766 12486 11823 98 -1378 -156 O
ATOM 110 CB PHE A 32 23.139 45.599 55.744 1.00 98.33 C
ANISOU 110 CB PHE A 32 14054 12128 11180 -116 -1472 113 C
ATOM 111 CG PHE A 32 21.998 44.625 55.600 1.00 89.03 C
ANISOU 111 CG PHE A 32 12779 10982 10069 -79 -1414 126 C
ATOM 112 CD1 PHE A 32 20.782 44.857 56.226 1.00 90.58 C
ANISOU 112 CD1 PHE A 32 12990 11041 10386 52 -1347 228 C
ATOM 113 CD2 PHE A 32 22.138 43.481 54.830 1.00 86.74 C
ANISOU 113 CD2 PHE A 32 12363 10846 9750 -179 -1416 18 C
ATOM 114 CE1 PHE A 32 19.737 43.956 56.095 1.00 91.35 C
ANISOU 114 CE1 PHE A 32 12972 11149 10587 80 -1290 240 C
ATOM 115 CE2 PHE A 32 21.100 42.581 54.694 1.00 89.01 C
ANISOU 115 CE2 PHE A 32 12550 11145 10125 -146 -1382 28 C
ATOM 116 CZ PHE A 32 19.897 42.818 55.326 1.00 89.32 C
ANISOU 116 CZ PHE A 32 12599 11042 10298 -18 -1323 150 C
ATOM 117 N ASN A 33 25.207 43.326 56.266 1.00 93.45 N
ANISOU 117 N ASN A 33 13378 11540 10589 -146 -1465 -292 N
ATOM 118 CA ASN A 33 25.432 41.882 56.217 1.00 96.57 C
ANISOU 118 CA ASN A 33 13668 11967 11058 -158 -1458 -452 C
ATOM 119 C ASN A 33 25.876 41.335 57.570 1.00 98.89 C
ANISOU 119 C ASN A 33 14091 12051 11431 -31 -1512 -511 C
ATOM 120 O ASN A 33 25.346 40.324 58.046 1.00100.86 O
ANISOU 120 O ASN A 33 14348 12239 11735 31 -1497 -519 O
ATOM 121 CB ASN A 33 26.465 41.546 55.142 1.00 96.33 C
ANISOU 121 CB ASN A 33 13470 12097 11032 -327 -1460 -633 C
ATOM 122 CG ASN A 33 25.989 41.895 53.750 1.00 90.42 C
ANISOU 122 CG ASN A 33 12636 11572 10148 -490 -1413 -576 C
ATOM 123 OD1 ASN A 33 24.822 41.693 53.415 1.00118.96 O
ANISOU 123 OD1 ASN A 33 16232 15237 13729 -478 -1408 -469 O
ATOM 124 ND2 ASN A 33 26.893 42.411 52.926 1.00 92.40 N
ANISOU 124 ND2 ASN A 33 12838 11947 10321 -658 -1386 -644 N
ATOM 125 N HIS A 34 26.851 41.991 58.204 1.00 93.93 N
ANISOU 125 N HIS A 34 13581 11297 10812 -2 -1598 -542 N
ATOM 126 CA HIS A 34 27.395 41.469 59.454 1.00102.71 C
ANISOU 126 CA HIS A 34 14846 12193 11984 94 -1710 -597 C
ATOM 127 C HIS A 34 26.362 41.513 60.575 1.00 94.33 C
ANISOU 127 C HIS A 34 14019 11001 10821 219 -1649 -454 C
ATOM 128 O HIS A 34 26.225 40.546 61.335 1.00 95.80 O
ANISOU 128 O HIS A 34 14299 11074 11028 264 -1682 -463 O
ATOM 129 CB HIS A 34 28.655 42.242 59.840 1.00103.85 C
ANISOU 129 CB HIS A 34 15064 12217 12176 91 -1847 -662 C
ATOM 130 CG HIS A 34 29.774 42.092 58.857 1.00119.43 C
ANISOU 130 CG HIS A 34 16794 14290 14292 -42 -1874 -835 C
ATOM 131 ND1 HIS A 34 29.990 42.987 57.832 1.00128.03 N
ANISOU 131 ND1 HIS A 34 17771 15542 15331 -164 -1789 -817 N
ATOM 132 CD2 HIS A 34 30.728 41.139 58.731 1.00116.70 C
ANISOU 132 CD2 HIS A 34 16287 13898 14156 -85 -1961 -1038 C
ATOM 133 CE1 HIS A 34 31.036 42.599 57.124 1.00126.21 C
ANISOU 133 CE1 HIS A 34 17331 15377 15246 -285 -1783 -1011 C
ATOM 134 NE2 HIS A 34 31.502 41.480 57.649 1.00123.77 N
ANISOU 134 NE2 HIS A 34 16969 14938 15122 -231 -1886 -1164 N
ATOM 135 N GLU A 35 25.622 42.619 60.693 1.00 84.37 N
ANISOU 135 N GLU A 35 12850 9742 9464 264 -1551 -325 N
ATOM 136 CA GLU A 35 24.551 42.675 61.683 1.00 87.78 C
ANISOU 136 CA GLU A 35 13472 10063 9817 369 -1426 -221 C
ATOM 137 C GLU A 35 23.422 41.703 61.355 1.00 86.01 C
ANISOU 137 C GLU A 35 13116 9916 9649 362 -1294 -175 C
ATOM 138 O GLU A 35 22.809 41.139 62.269 1.00 88.74 O
ANISOU 138 O GLU A 35 13602 10153 9960 419 -1201 -130 O
ATOM 139 CB GLU A 35 24.005 44.102 61.793 1.00 83.70 C
ANISOU 139 CB GLU A 35 13030 9517 9256 422 -1346 -129 C
ATOM 140 CG GLU A 35 22.954 44.273 62.883 1.00 90.52 C
ANISOU 140 CG GLU A 35 14088 10250 10055 527 -1172 -66 C
ATOM 141 CD GLU A 35 23.329 45.324 63.904 1.00119.41 C
ANISOU 141 CD GLU A 35 18017 13745 13609 602 -1197 -86 C
ATOM 142 OE1 GLU A 35 24.281 46.088 63.647 1.00129.94 O
ANISOU 142 OE1 GLU A 35 19348 15067 14958 580 -1359 -120 O
ATOM 143 OE2 GLU A 35 22.670 45.386 64.965 1.00135.92 O1-
ANISOU 143 OE2 GLU A 35 20326 15716 15602 674 -1042 -76 O1-
ATOM 144 N ALA A 36 23.143 41.484 60.067 1.00 94.25 N
ANISOU 144 N ALA A 36 13901 11138 10769 280 -1286 -184 N
ATOM 145 CA ALA A 36 22.013 40.643 59.683 1.00 86.20 C
ANISOU 145 CA ALA A 36 12738 10181 9833 274 -1186 -140 C
ATOM 146 C ALA A 36 22.242 39.181 60.049 1.00100.26 C
ANISOU 146 C ALA A 36 14506 11913 11676 267 -1224 -217 C
ATOM 147 O ALA A 36 21.313 38.501 60.498 1.00103.59 O
ANISOU 147 O ALA A 36 14939 12274 12148 304 -1119 -150 O
ATOM 148 CB ALA A 36 21.741 40.773 58.184 1.00 87.57 C
ANISOU 148 CB ALA A 36 12675 10551 10046 170 -1216 -140 C
ATOM 149 N GLU A 37 23.466 38.679 59.856 1.00111.49 N
ANISOU 149 N GLU A 37 15885 13341 13134 214 -1377 -359 N
ATOM 150 CA GLU A 37 23.734 37.261 60.084 1.00105.48 C
ANISOU 150 CA GLU A 37 15070 12514 12493 201 -1458 -445 C
ATOM 151 C GLU A 37 23.436 36.860 61.524 1.00 95.37 C
ANISOU 151 C GLU A 37 14051 11024 11162 274 -1448 -342 C
ATOM 152 O GLU A 37 22.803 35.827 61.773 1.00 95.78 O
ANISOU 152 O GLU A 37 14078 11024 11289 273 -1411 -300 O
ATOM 153 CB GLU A 37 25.184 36.929 59.731 1.00 95.66 C
ANISOU 153 CB GLU A 37 13725 11268 11353 142 -1632 -638 C
ATOM 154 CG GLU A 37 25.395 36.541 58.282 1.00 91.60 C
ANISOU 154 CG GLU A 37 12916 10959 10929 33 -1615 -795 C
ATOM 155 CD GLU A 37 26.811 36.082 58.007 1.00111.45 C
ANISOU 155 CD GLU A 37 15295 13444 13605 -27 -1744 -1027 C
ATOM 156 OE1 GLU A 37 27.699 36.945 57.845 1.00122.15 O
ANISOU 156 OE1 GLU A 37 16660 14817 14933 -64 -1767 -1082 O
ATOM 157 OE2 GLU A 37 27.034 34.854 57.953 1.00111.33 O1-
ANISOU 157 OE2 GLU A 37 15144 13372 13786 -37 -1825 -1163 O1-
ATOM 158 N ASP A 38 23.889 37.665 62.488 1.00 86.51 N
ANISOU 158 N ASP A 38 13199 9772 9898 323 -1484 -300 N
ATOM 159 CA ASP A 38 23.649 37.342 63.892 1.00106.30 C
ANISOU 159 CA ASP A 38 16020 12083 12286 364 -1473 -202 C
ATOM 160 C ASP A 38 22.161 37.372 64.218 1.00 98.00 C
ANISOU 160 C ASP A 38 15017 11044 11174 393 -1194 -67 C
ATOM 161 O ASP A 38 21.633 36.449 64.851 1.00 99.91 O
ANISOU 161 O ASP A 38 15354 11194 11415 376 -1133 8 O
ATOM 162 CB ASP A 38 24.414 38.309 64.795 1.00 98.80 C
ANISOU 162 CB ASP A 38 15368 11000 11173 403 -1573 -202 C
ATOM 163 CG ASP A 38 24.104 38.097 66.261 1.00102.48 C
ANISOU 163 CG ASP A 38 16224 11277 11438 423 -1542 -98 C
ATOM 164 OD1 ASP A 38 24.283 36.958 66.745 1.00104.67 O
ANISOU 164 OD1 ASP A 38 16586 11437 11746 381 -1668 -69 O
ATOM 165 OD2 ASP A 38 23.668 39.060 66.926 1.00104.12 O1-
ANISOU 165 OD2 ASP A 38 16660 11444 11455 468 -1389 -49 O1-
ATOM 166 N LEU A 39 21.465 38.433 63.795 1.00 84.19 N
ANISOU 166 N LEU A 39 13191 9390 9408 428 -1026 -32 N
ATOM 167 CA LEU A 39 20.040 38.550 64.090 1.00 85.25 C
ANISOU 167 CA LEU A 39 13324 9510 9556 462 -750 70 C
ATOM 168 C LEU A 39 19.244 37.421 63.448 1.00 93.87 C
ANISOU 168 C LEU A 39 14160 10667 10841 422 -696 97 C
ATOM 169 O LEU A 39 18.285 36.914 64.043 1.00 89.79 O
ANISOU 169 O LEU A 39 13689 10073 10356 425 -502 181 O
ATOM 170 CB LEU A 39 19.517 39.908 63.624 1.00 85.43 C
ANISOU 170 CB LEU A 39 13256 9596 9606 509 -642 87 C
ATOM 171 CG LEU A 39 19.740 41.056 64.610 1.00 95.16 C
ANISOU 171 CG LEU A 39 14777 10710 10668 572 -579 82 C
ATOM 172 CD1 LEU A 39 20.065 42.342 63.873 1.00104.45 C
ANISOU 172 CD1 LEU A 39 15844 11953 11889 592 -669 60 C
ATOM 173 CD2 LEU A 39 18.527 41.239 65.512 1.00 96.89 C
ANISOU 173 CD2 LEU A 39 15122 10829 10865 619 -263 133 C
ATOM 174 N PHE A 40 19.624 37.017 62.232 1.00 82.86 N
ANISOU 174 N PHE A 40 12496 9410 9577 373 -854 15 N
ATOM 175 CA PHE A 40 18.988 35.863 61.606 1.00 86.93 C
ANISOU 175 CA PHE A 40 12774 9974 10281 332 -849 12 C
ATOM 176 C PHE A 40 19.247 34.590 62.401 1.00 91.14 C
ANISOU 176 C PHE A 40 13419 10371 10841 308 -909 23 C
ATOM 177 O PHE A 40 18.343 33.764 62.577 1.00 93.52 O
ANISOU 177 O PHE A 40 13651 10620 11262 294 -800 98 O
ATOM 178 CB PHE A 40 19.482 35.698 60.167 1.00 92.75 C
ANISOU 178 CB PHE A 40 13247 10890 11106 268 -1011 -113 C
ATOM 179 CG PHE A 40 18.820 34.570 59.428 1.00 94.33 C
ANISOU 179 CG PHE A 40 13199 11144 11497 224 -1027 -143 C
ATOM 180 CD1 PHE A 40 17.443 34.428 59.447 1.00 86.56 C
ANISOU 180 CD1 PHE A 40 12120 10128 10642 248 -876 -29 C
ATOM 181 CD2 PHE A 40 19.575 33.640 58.732 1.00 91.80 C
ANISOU 181 CD2 PHE A 40 12726 10889 11265 160 -1192 -305 C
ATOM 182 CE1 PHE A 40 16.831 33.386 58.779 1.00 88.29 C
ANISOU 182 CE1 PHE A 40 12108 10378 11061 209 -916 -58 C
ATOM 183 CE2 PHE A 40 18.968 32.595 58.061 1.00 86.71 C
ANISOU 183 CE2 PHE A 40 11859 10283 10804 122 -1221 -353 C
ATOM 184 CZ PHE A 40 17.595 32.469 58.085 1.00 90.60 C
ANISOU 184 CZ PHE A 40 12271 10741 11410 147 -1096 -220 C
ATOM 185 N TYR A 41 20.479 34.412 62.887 1.00100.83 N
ANISOU 185 N TYR A 41 14808 11514 11988 296 -1106 -43 N
ATOM 186 CA TYR A 41 20.806 33.230 63.679 1.00101.62 C
ANISOU 186 CA TYR A 41 15038 11446 12128 263 -1228 -14 C
ATOM 187 C TYR A 41 19.906 33.117 64.903 1.00104.75 C
ANISOU 187 C TYR A 41 15709 11705 12388 262 -1021 165 C
ATOM 188 O TYR A 41 19.317 32.060 65.157 1.00119.87 O
ANISOU 188 O TYR A 41 17595 13542 14409 218 -978 247 O
ATOM 189 CB TYR A 41 22.275 33.269 64.102 1.00 87.56 C
ANISOU 189 CB TYR A 41 13412 9557 10301 257 -1502 -103 C
ATOM 190 CG TYR A 41 22.850 31.904 64.399 1.00 88.02 C
ANISOU 190 CG TYR A 41 13458 9456 10530 212 -1744 -133 C
ATOM 191 CD1 TYR A 41 22.654 31.304 65.637 1.00 94.36 C
ANISOU 191 CD1 TYR A 41 14565 10050 11236 182 -1784 26 C
ATOM 192 CD2 TYR A 41 23.593 31.220 63.449 1.00 87.42 C
ANISOU 192 CD2 TYR A 41 13072 9424 10718 187 -1934 -326 C
ATOM 193 CE1 TYR A 41 23.175 30.055 65.916 1.00 89.71 C
ANISOU 193 CE1 TYR A 41 13968 9283 10834 133 -2051 22 C
ATOM 194 CE2 TYR A 41 24.122 29.974 63.719 1.00 93.26 C
ANISOU 194 CE2 TYR A 41 13770 9985 11678 153 -2178 -369 C
ATOM 195 CZ TYR A 41 23.910 29.396 64.953 1.00 96.07 C
ANISOU 195 CZ TYR A 41 14426 10116 11959 129 -2259 -182 C
ATOM 196 OH TYR A 41 24.437 28.153 65.216 1.00 90.55 O
ANISOU 196 OH TYR A 41 13685 9209 11510 88 -2547 -204 O
ATOM 197 N GLN A 42 19.797 34.201 65.679 1.00 89.70 N
ANISOU 197 N GLN A 42 14074 9761 10246 300 -878 219 N
ATOM 198 CA GLN A 42 18.957 34.189 66.873 1.00103.01 C
ANISOU 198 CA GLN A 42 16051 11328 11761 281 -624 360 C
ATOM 199 C GLN A 42 17.534 33.754 66.552 1.00107.82 C
ANISOU 199 C GLN A 42 16431 11979 12555 269 -342 433 C
ATOM 200 O GLN A 42 16.921 32.994 67.312 1.00109.62 O
ANISOU 200 O GLN A 42 16794 12097 12760 205 -193 551 O
ATOM 201 CB GLN A 42 18.958 35.573 67.525 1.00106.83 C
ANISOU 201 CB GLN A 42 16792 11795 12002 334 -475 350 C
ATOM 202 CG GLN A 42 20.336 36.068 67.925 1.00 94.49 C
ANISOU 202 CG GLN A 42 15470 10163 10270 347 -762 281 C
ATOM 203 CD GLN A 42 20.893 35.330 69.128 1.00108.38 C
ANISOU 203 CD GLN A 42 17620 11724 11835 275 -926 360 C
ATOM 204 OE1 GLN A 42 20.166 34.631 69.835 1.00113.27 O
ANISOU 204 OE1 GLN A 42 18408 12263 12367 206 -759 486 O
ATOM 205 NE2 GLN A 42 22.192 35.475 69.360 1.00112.56 N
ANISOU 205 NE2 GLN A 42 18298 12160 12311 278 -1269 297 N
ATOM 206 N SER A 43 16.993 34.220 65.426 1.00101.31 N
ANISOU 206 N SER A 43 15264 11300 11928 316 -282 374 N
ATOM 207 CA SER A 43 15.668 33.777 65.005 1.00106.76 C
ANISOU 207 CA SER A 43 15689 12011 12862 308 -75 432 C
ATOM 208 C SER A 43 15.680 32.305 64.611 1.00105.06 C
ANISOU 208 C SER A 43 15299 11775 12845 245 -228 442 C
ATOM 209 O SER A 43 14.834 31.526 65.066 1.00111.95 O
ANISOU 209 O SER A 43 16159 12552 13824 198 -62 548 O
ATOM 210 CB SER A 43 15.171 34.641 63.847 1.00107.57 C
ANISOU 210 CB SER A 43 15488 12252 13131 363 -59 374 C
ATOM 211 OG SER A 43 14.077 34.021 63.196 1.00113.61 O
ANISOU 211 OG SER A 43 15943 13032 14190 348 20 408 O
ATOM 212 N SER A 44 16.637 31.907 63.768 1.00 92.58 N
ANISOU 212 N SER A 44 13571 10272 11333 236 -533 320 N
ATOM 213 CA SER A 44 16.710 30.521 63.309 1.00 95.66 C
ANISOU 213 CA SER A 44 13763 10634 11948 184 -702 287 C
ATOM 214 C SER A 44 16.851 29.553 64.477 1.00104.77 C
ANISOU 214 C SER A 44 15163 11585 13058 123 -731 408 C
ATOM 215 O SER A 44 16.118 28.562 64.569 1.00109.48 O
ANISOU 215 O SER A 44 15656 12102 13841 74 -670 493 O
ATOM 216 CB SER A 44 17.875 30.356 62.331 1.00 92.38 C
ANISOU 216 CB SER A 44 13184 10323 11593 180 -996 92 C
ATOM 217 OG SER A 44 17.802 31.305 61.281 1.00103.60 O
ANISOU 217 OG SER A 44 14437 11933 12994 205 -972 6 O
ATOM 218 N LEU A 45 17.790 29.830 65.385 1.00116.10 N
ANISOU 218 N LEU A 45 16938 12920 14253 114 -846 429 N
ATOM 219 CA LEU A 45 18.025 28.939 66.517 1.00108.10 C
ANISOU 219 CA LEU A 45 16215 11695 13162 33 -937 566 C
ATOM 220 C LEU A 45 16.785 28.819 67.399 1.00108.73 C
ANISOU 220 C LEU A 45 16468 11697 13146 -26 -581 761 C
ATOM 221 O LEU A 45 16.388 27.712 67.784 1.00112.31 O
ANISOU 221 O LEU A 45 16943 12022 13710 -114 -583 888 O
ATOM 222 CB LEU A 45 19.221 29.438 67.327 1.00 92.45 C
ANISOU 222 CB LEU A 45 14595 9613 10920 34 -1147 555 C
ATOM 223 CG LEU A 45 19.701 28.507 68.438 1.00113.18 C
ANISOU 223 CG LEU A 45 17551 11992 13460 -64 -1363 696 C
ATOM 224 CD1 LEU A 45 19.918 27.098 67.900 1.00109.61 C
ANISOU 224 CD1 LEU A 45 16822 11453 13371 -104 -1624 666 C
ATOM 225 CD2 LEU A 45 20.962 29.054 69.095 1.00136.95 C
ANISOU 225 CD2 LEU A 45 20882 14893 16259 -55 -1643 659 C
ATOM 226 N ALA A 46 16.156 29.951 67.726 1.00 96.46 N
ANISOU 226 N ALA A 46 15028 10210 11413 14 -260 778 N
ATOM 227 CA ALA A 46 14.942 29.921 68.538 1.00 99.87 C
ANISOU 227 CA ALA A 46 15594 10573 11780 -48 147 924 C
ATOM 228 C ALA A 46 13.808 29.208 67.809 1.00112.64 C
ANISOU 228 C ALA A 46 16805 12216 13776 -58 293 953 C
ATOM 229 O ALA A 46 13.166 28.309 68.364 1.00115.78 O
ANISOU 229 O ALA A 46 17254 12493 14245 -160 438 1098 O
ATOM 230 CB ALA A 46 14.529 31.343 68.920 1.00 99.46 C
ANISOU 230 CB ALA A 46 15682 10580 11529 14 457 879 C
ATOM 231 N SER A 47 13.544 29.602 66.559 1.00115.35 N
ANISOU 231 N SER A 47 16755 12706 14368 33 243 825 N
ATOM 232 CA SER A 47 12.557 28.899 65.748 1.00109.57 C
ANISOU 232 CA SER A 47 15623 11988 14020 26 298 833 C
ATOM 233 C SER A 47 12.920 27.434 65.551 1.00107.26 C
ANISOU 233 C SER A 47 15236 11613 13906 -44 31 858 C
ATOM 234 O SER A 47 12.032 26.615 65.290 1.00116.78 O
ANISOU 234 O SER A 47 16202 12761 15408 -84 109 918 O
ATOM 235 CB SER A 47 12.396 29.588 64.392 1.00108.92 C
ANISOU 235 CB SER A 47 15193 12074 14119 119 199 690 C
ATOM 236 OG SER A 47 12.094 30.964 64.556 1.00111.11 O
ANISOU 236 OG SER A 47 15543 12401 14275 185 403 671 O
ATOM 237 N TRP A 48 14.201 27.086 65.671 1.00 97.65 N
ANISOU 237 N TRP A 48 14179 10364 12558 -57 -297 805 N
ATOM 238 CA TRP A 48 14.577 25.680 65.655 1.00 97.35 C
ANISOU 238 CA TRP A 48 14077 10197 12715 -126 -561 831 C
ATOM 239 C TRP A 48 14.227 24.998 66.972 1.00106.73 C
ANISOU 239 C TRP A 48 15582 11176 13794 -250 -435 1069 C
ATOM 240 O TRP A 48 13.973 23.789 66.990 1.00110.60 O
ANISOU 240 O TRP A 48 15962 11535 14525 -326 -538 1153 O
ATOM 241 CB TRP A 48 16.072 25.534 65.350 1.00 97.66 C
ANISOU 241 CB TRP A 48 14148 10238 12720 -99 -960 676 C
ATOM 242 CG TRP A 48 16.660 24.265 65.863 1.00 94.46 C
ANISOU 242 CG TRP A 48 13836 9618 12437 -180 -1245 742 C
ATOM 243 CD1 TRP A 48 17.136 24.020 67.120 1.00101.76 C
ANISOU 243 CD1 TRP A 48 15172 10344 13148 -262 -1342 912 C
ATOM 244 CD2 TRP A 48 16.798 23.042 65.136 1.00 93.59 C
ANISOU 244 CD2 TRP A 48 13405 9446 12709 -196 -1496 644 C
ATOM 245 NE1 TRP A 48 17.572 22.721 67.213 1.00 96.54 N
ANISOU 245 NE1 TRP A 48 14456 9486 12737 -328 -1662 945 N
ATOM 246 CE2 TRP A 48 17.378 22.101 66.006 1.00 93.91 C
ANISOU 246 CE2 TRP A 48 13660 9233 12789 -282 -1752 768 C
ATOM 247 CE3 TRP A 48 16.495 22.655 63.828 1.00 94.83 C
ANISOU 247 CE3 TRP A 48 13127 9727 13176 -153 -1549 456 C
ATOM 248 CZ2 TRP A 48 17.657 20.797 65.611 1.00 99.96 C
ANISOU 248 CZ2 TRP A 48 14185 9854 13940 -312 -2051 702 C
ATOM 249 CZ3 TRP A 48 16.774 21.361 63.437 1.00 96.08 C
ANISOU 249 CZ3 TRP A 48 13062 9760 13684 -185 -1822 369 C
ATOM 250 CH2 TRP A 48 17.350 20.447 64.325 1.00 98.81 C
ANISOU 250 CH2 TRP A 48 13595 9842 14108 -257 -2068 488 C
ATOM 251 N ASN A 49 14.201 25.751 68.075 1.00114.65 N
ANISOU 251 N ASN A 49 16992 12142 14427 -285 -213 1178 N
ATOM 252 CA ASN A 49 13.830 25.167 69.361 1.00112.54 C
ANISOU 252 CA ASN A 49 17087 11690 13983 -437 -53 1416 C
ATOM 253 C ASN A 49 12.353 24.797 69.394 1.00118.01 C
ANISOU 253 C ASN A 49 17584 12359 14894 -499 348 1529 C
ATOM 254 O ASN A 49 11.996 23.679 69.786 1.00124.46 O
ANISOU 254 O ASN A 49 18426 13021 15842 -627 342 1697 O
ATOM 255 CB ASN A 49 14.171 26.123 70.504 1.00122.47 C
ANISOU 255 CB ASN A 49 18855 12927 14751 -470 101 1472 C
ATOM 256 CG ASN A 49 15.644 26.107 70.857 1.00111.02 C
ANISOU 256 CG ASN A 49 17697 11393 13095 -470 -346 1443 C
ATOM 257 OD1 ASN A 49 16.462 25.553 70.125 1.00105.24 O
ANISOU 257 OD1 ASN A 49 16731 10644 12613 -421 -746 1336 O
ATOM 258 ND2 ASN A 49 15.987 26.706 71.991 1.00103.72 N
ANISOU 258 ND2 ASN A 49 17279 10398 11730 -531 -283 1523 N
ATOM 259 N TYR A 50 11.475 25.723 68.994 1.00120.34 N
ANISOU 259 N TYR A 50 17671 12784 15268 -416 687 1442 N
ATOM 260 CA TYR A 50 10.049 25.411 68.971 1.00125.41 C
ANISOU 260 CA TYR A 50 18068 13383 16199 -465 1064 1526 C
ATOM 261 C TYR A 50 9.762 24.209 68.081 1.00129.07 C
ANISOU 261 C TYR A 50 18123 13798 17118 -474 831 1528 C
ATOM 262 O TYR A 50 8.931 23.359 68.422 1.00137.02 O
ANISOU 262 O TYR A 50 19055 14673 18334 -587 1011 1680 O
ATOM 263 CB TYR A 50 9.232 26.612 68.495 1.00125.45 C
ANISOU 263 CB TYR A 50 17836 13511 16320 -349 1369 1399 C
ATOM 264 CG TYR A 50 7.820 26.212 68.129 1.00137.39 C
ANISOU 264 CG TYR A 50 18952 14967 18283 -370 1647 1440 C
ATOM 265 CD1 TYR A 50 6.925 25.797 69.104 1.00138.71 C
ANISOU 265 CD1 TYR A 50 19241 14995 18469 -513 2071 1600 C
ATOM 266 CD2 TYR A 50 7.393 26.211 66.807 1.00143.74 C
ANISOU 266 CD2 TYR A 50 19270 15845 19499 -265 1476 1321 C
ATOM 267 CE1 TYR A 50 5.639 25.410 68.776 1.00140.14 C
ANISOU 267 CE1 TYR A 50 19027 15101 19120 -536 2326 1633 C
ATOM 268 CE2 TYR A 50 6.105 25.828 66.471 1.00147.03 C
ANISOU 268 CE2 TYR A 50 19313 16180 20372 -284 1685 1357 C
ATOM 269 CZ TYR A 50 5.233 25.429 67.463 1.00143.06 C
ANISOU 269 CZ TYR A 50 18898 15527 19933 -413 2114 1510 C
ATOM 270 OH TYR A 50 3.951 25.045 67.146 1.00149.67 O
ANISOU 270 OH TYR A 50 19332 16260 21276 -435 2331 1541 O
ATOM 271 N ASN A 51 10.445 24.117 66.939 1.00112.34 N
ANISOU 271 N ASN A 51 15742 11784 15160 -368 442 1350 N
ATOM 272 CA ASN A 51 10.194 23.013 66.020 1.00115.71 C
ANISOU 272 CA ASN A 51 15777 12173 16016 -370 209 1306 C
ATOM 273 C ASN A 51 10.702 21.693 66.580 1.00113.72 C
ANISOU 273 C ASN A 51 15672 11727 15810 -488 -30 1437 C
ATOM 274 O ASN A 51 10.170 20.627 66.244 1.00116.40 O
ANISOU 274 O ASN A 51 15749 11959 16517 -539 -104 1483 O
ATOM 275 CB ASN A 51 10.843 23.302 64.666 1.00109.35 C
ANISOU 275 CB ASN A 51 14695 11541 15312 -247 -117 1056 C
ATOM 276 CG ASN A 51 9.997 24.215 63.796 1.00124.90 C
ANISOU 276 CG ASN A 51 16378 13656 17421 -156 47 958 C
ATOM 277 OD1 ASN A 51 9.284 25.085 64.297 1.00133.95 O
ANISOU 277 OD1 ASN A 51 17605 14806 18484 -143 390 1030 O
ATOM 278 ND2 ASN A 51 10.080 24.025 62.483 1.00124.63 N
ANISOU 278 ND2 ASN A 51 16016 13731 17606 -101 -211 786 N
ATOM 279 N THR A 52 11.723 21.736 67.427 1.00115.62 N
ANISOU 279 N THR A 52 16324 11897 15711 -537 -186 1501 N
ATOM 280 CA THR A 52 12.265 20.515 68.009 1.00112.87 C
ANISOU 280 CA THR A 52 16143 11328 15416 -658 -472 1645 C
ATOM 281 C THR A 52 11.723 20.237 69.395 1.00114.75 C
ANISOU 281 C THR A 52 16782 11396 15420 -840 -194 1948 C
ATOM 282 O THR A 52 11.849 19.113 69.882 1.00111.52 O
ANISOU 282 O THR A 52 16483 10775 15114 -975 -383 2128 O
ATOM 283 CB THR A 52 13.778 20.616 68.136 1.00103.16 C
ANISOU 283 CB THR A 52 15130 10069 13995 -621 -886 1548 C
ATOM 284 OG1 THR A 52 14.093 21.907 68.661 1.00103.90 O
ANISOU 284 OG1 THR A 52 15545 10274 13659 -581 -713 1530 O
ATOM 285 CG2 THR A 52 14.444 20.424 66.777 1.00110.19 C
ANISOU 285 CG2 THR A 52 15606 11069 15193 -493 -1218 1253 C
ATOM 286 N ASN A 53 11.147 21.246 70.038 1.00120.42 N
ANISOU 286 N ASN A 53 17732 12197 15825 -858 250 2002 N
ATOM 287 CA ASN A 53 10.773 21.142 71.436 1.00123.90 C
ANISOU 287 CA ASN A 53 18647 12503 15927 -1052 550 2261 C
ATOM 288 C ASN A 53 9.578 22.048 71.687 1.00125.91 C
ANISOU 288 C ASN A 53 18865 12862 16114 -1051 1164 2249 C
ATOM 289 O ASN A 53 9.730 23.148 72.222 1.00129.18 O
ANISOU 289 O ASN A 53 19573 13364 16147 -1023 1383 2192 O
ATOM 290 CB ASN A 53 11.985 21.501 72.292 1.00128.53 C
ANISOU 290 CB ASN A 53 19771 13036 16030 -1092 296 2305 C
ATOM 291 CG ASN A 53 11.724 21.445 73.781 1.00136.07 C
ANISOU 291 CG ASN A 53 21311 13858 16532 -1316 568 2569 C
ATOM 292 OD1 ASN A 53 10.980 20.600 74.279 1.00140.14 O
ANISOU 292 OD1 ASN A 53 21887 14236 17123 -1498 765 2794 O
ATOM 293 ND2 ASN A 53 12.370 22.350 74.507 1.00145.27 N
ANISOU 293 ND2 ASN A 53 22935 15058 17205 -1318 573 2543 N
ATOM 294 N ILE A 54 8.387 21.602 71.285 1.00129.79 N
ANISOU 294 N ILE A 54 18971 13325 17018 -1075 1434 2284 N
ATOM 295 CA ILE A 54 7.211 22.466 71.365 1.00129.88 C
ANISOU 295 CA ILE A 54 18836 13414 17100 -1050 1997 2229 C
ATOM 296 C ILE A 54 6.902 22.766 72.825 1.00130.70 C
ANISOU 296 C ILE A 54 19460 13448 16752 -1237 2463 2391 C
ATOM 297 O ILE A 54 6.657 21.853 73.623 1.00135.74 O
ANISOU 297 O ILE A 54 20336 13928 17311 -1453 2573 2632 O
ATOM 298 CB ILE A 54 6.016 21.815 70.656 1.00136.90 C
ANISOU 298 CB ILE A 54 19187 14244 18584 -1051 2146 2241 C
ATOM 299 CG1 ILE A 54 6.345 21.571 69.179 1.00134.12 C
ANISOU 299 CG1 ILE A 54 18365 13975 18619 -875 1675 2054 C
ATOM 300 CG2 ILE A 54 4.730 22.668 70.828 1.00138.72 C
ANISOU 300 CG2 ILE A 54 19240 14504 18965 -1038 2749 2187 C
ATOM 301 CD1 ILE A 54 5.276 20.831 68.423 1.00138.35 C
ANISOU 301 CD1 ILE A 54 18384 14433 19749 -876 1716 2059 C
ATOM 302 N THR A 55 6.936 24.048 73.180 1.00125.45 N
ANISOU 302 N THR A 55 18994 12898 15775 -1167 2731 2258 N
ATOM 303 CA THR A 55 6.593 24.538 74.505 1.00131.24 C
ANISOU 303 CA THR A 55 20214 13595 16055 -1329 3234 2341 C
ATOM 304 C THR A 55 5.922 25.885 74.318 1.00136.03 C
ANISOU 304 C THR A 55 20624 14320 16739 -1188 3654 2112 C
ATOM 305 O THR A 55 6.293 26.627 73.409 1.00139.07 O
ANISOU 305 O THR A 55 20742 14826 17272 -973 3397 1917 O
ATOM 306 CB THR A 55 7.824 24.724 75.403 1.00137.18 C
ANISOU 306 CB THR A 55 21618 14327 16177 -1406 2965 2411 C
ATOM 307 OG1 THR A 55 8.432 25.986 75.093 1.00128.45 O
ANISOU 307 OG1 THR A 55 20533 13365 14905 -1210 2854 2178 O
ATOM 308 CG2 THR A 55 8.844 23.609 75.209 1.00141.64 C
ANISOU 308 CG2 THR A 55 22263 14781 16772 -1447 2325 2553 C
ATOM 309 N GLU A 56 4.941 26.214 75.168 1.00152.55 N
ANISOU 309 N GLU A 56 22844 16369 18748 -1318 4302 2127 N
ATOM 310 CA GLU A 56 4.420 27.579 75.115 1.00151.71 C
ANISOU 310 CA GLU A 56 22599 16348 18695 -1182 4683 1884 C
ATOM 311 C GLU A 56 5.535 28.575 75.367 1.00149.34 C
ANISOU 311 C GLU A 56 22689 16147 17904 -1080 4438 1760 C
ATOM 312 O GLU A 56 5.475 29.711 74.885 1.00152.26 O
ANISOU 312 O GLU A 56 22850 16604 18398 -893 4473 1542 O
ATOM 313 CB GLU A 56 3.289 27.788 76.120 1.00152.03 C
ANISOU 313 CB GLU A 56 22767 16315 18683 -1355 5457 1886 C
ATOM 314 CG GLU A 56 2.113 28.564 75.553 1.00155.42 C
ANISOU 314 CG GLU A 56 22624 16742 19686 -1214 5859 1669 C
ATOM 315 CD GLU A 56 2.388 30.049 75.489 1.00159.27 C
ANISOU 315 CD GLU A 56 23154 17324 20038 -1029 5900 1410 C
ATOM 316 OE1 GLU A 56 3.115 30.548 76.372 1.00157.60 O
ANISOU 316 OE1 GLU A 56 23513 17156 19212 -1089 5942 1385 O
ATOM 317 OE2 GLU A 56 1.905 30.712 74.549 1.00157.23 O1-
ANISOU 317 OE2 GLU A 56 22371 17082 20289 -828 5849 1240 O1-
ATOM 318 N GLU A 57 6.559 28.166 76.119 1.00143.49 N
ANISOU 318 N GLU A 57 22513 15373 16634 -1206 4158 1904 N
ATOM 319 CA GLU A 57 7.703 29.039 76.336 1.00141.09 C
ANISOU 319 CA GLU A 57 22570 15139 15899 -1111 3856 1793 C
ATOM 320 C GLU A 57 8.374 29.379 75.015 1.00134.27 C
ANISOU 320 C GLU A 57 21288 14378 15350 -866 3336 1652 C
ATOM 321 O GLU A 57 8.625 30.550 74.713 1.00141.81 O
ANISOU 321 O GLU A 57 22183 15427 16273 -705 3317 1457 O
ATOM 322 CB GLU A 57 8.714 28.382 77.278 1.00157.48 C
ANISOU 322 CB GLU A 57 25282 17121 17434 -1294 3542 1995 C
ATOM 323 CG GLU A 57 9.999 29.188 77.390 1.00164.30 C
ANISOU 323 CG GLU A 57 26465 18030 17932 -1182 3126 1882 C
ATOM 324 CD GLU A 57 10.921 28.715 78.493 1.00169.60 C
ANISOU 324 CD GLU A 57 27827 18575 18036 -1375 2848 2069 C
ATOM 325 OE1 GLU A 57 10.460 28.031 79.430 1.00172.20 O
ANISOU 325 OE1 GLU A 57 28524 18800 18105 -1626 3115 2275 O
ATOM 326 OE2 GLU A 57 12.137 28.979 78.381 1.00155.39 O1-
ANISOU 326 OE2 GLU A 57 26193 16767 16081 -1285 2324 2022 O1-
ATOM 327 N ASN A 58 8.657 28.360 74.201 1.00128.39 N
ANISOU 327 N ASN A 58 20250 13614 14920 -847 2922 1741 N
ATOM 328 CA ASN A 58 9.379 28.604 72.960 1.00133.03 C
ANISOU 328 CA ASN A 58 20488 14307 15751 -649 2436 1601 C
ATOM 329 C ASN A 58 8.488 29.181 71.869 1.00133.71 C
ANISOU 329 C ASN A 58 19999 14485 16321 -493 2590 1448 C
ATOM 330 O ASN A 58 8.987 29.900 70.998 1.00128.60 O
ANISOU 330 O ASN A 58 19152 13952 15759 -332 2321 1298 O
ATOM 331 CB ASN A 58 10.054 27.323 72.474 1.00134.36 C
ANISOU 331 CB ASN A 58 20555 14415 16080 -687 1937 1709 C
ATOM 332 CG ASN A 58 11.064 26.777 73.470 1.00126.14 C
ANISOU 332 CG ASN A 58 20066 13250 14613 -829 1665 1863 C
ATOM 333 OD1 ASN A 58 11.485 27.473 74.394 1.00132.52 O
ANISOU 333 OD1 ASN A 58 21349 14045 14956 -874 1754 1863 O
ATOM 334 ND2 ASN A 58 11.483 25.541 73.260 1.00119.17 N
ANISOU 334 ND2 ASN A 58 19117 12257 13904 -897 1291 1985 N
ATOM 335 N VAL A 59 7.185 28.887 71.887 1.00149.52 N
ANISOU 335 N VAL A 59 21729 16426 18658 -548 3001 1489 N
ATOM 336 CA VAL A 59 6.273 29.593 70.990 1.00146.69 C
ANISOU 336 CA VAL A 59 20860 16115 18760 -404 3159 1340 C
ATOM 337 C VAL A 59 6.444 31.095 71.160 1.00144.99 C
ANISOU 337 C VAL A 59 20765 15971 18355 -286 3295 1168 C
ATOM 338 O VAL A 59 6.407 31.859 70.188 1.00148.41 O
ANISOU 338 O VAL A 59 20870 16481 19040 -127 3122 1036 O
ATOM 339 CB VAL A 59 4.816 29.165 71.242 1.00149.67 C
ANISOU 339 CB VAL A 59 20974 16374 19521 -496 3654 1400 C
ATOM 340 CG1 VAL A 59 3.875 29.903 70.303 1.00151.40 C
ANISOU 340 CG1 VAL A 59 20645 16603 20277 -343 3756 1247 C
ATOM 341 CG2 VAL A 59 4.666 27.676 71.065 1.00150.36 C
ANISOU 341 CG2 VAL A 59 20937 16375 19819 -615 3492 1578 C
ATOM 342 N GLN A 60 6.651 31.538 72.401 1.00144.14 N
ANISOU 342 N GLN A 60 21150 15829 17786 -375 3588 1170 N
ATOM 343 CA GLN A 60 6.889 32.949 72.672 1.00147.81 C
ANISOU 343 CA GLN A 60 21774 16342 18044 -270 3706 995 C
ATOM 344 C GLN A 60 8.328 33.355 72.374 1.00144.56 C
ANISOU 344 C GLN A 60 21579 16021 17326 -182 3180 956 C
ATOM 345 O GLN A 60 8.567 34.491 71.951 1.00146.45 O
ANISOU 345 O GLN A 60 21722 16324 17600 -38 3094 806 O
ATOM 346 CB GLN A 60 6.535 33.267 74.127 1.00153.94 C
ANISOU 346 CB GLN A 60 23014 17046 18432 -411 4241 982 C
ATOM 347 CG GLN A 60 5.112 32.881 74.535 1.00162.57 C
ANISOU 347 CG GLN A 60 23910 18040 19820 -527 4845 1006 C
ATOM 348 CD GLN A 60 4.064 33.876 74.062 1.00163.43 C
ANISOU 348 CD GLN A 60 23542 18122 20431 -384 5176 799 C
ATOM 349 OE1 GLN A 60 4.049 34.280 72.899 1.00164.12 O
ANISOU 349 OE1 GLN A 60 23190 18250 20917 -207 4850 728 O
ATOM 350 NE2 GLN A 60 3.179 34.275 74.969 1.00156.00 N
ANISOU 350 NE2 GLN A 60 22691 17100 19482 -472 5825 696 N
ATOM 351 N ASN A 61 9.292 32.455 72.587 1.00145.53 N
ANISOU 351 N ASN A 61 21976 16131 17188 -269 2819 1087 N
ATOM 352 CA ASN A 61 10.676 32.768 72.240 1.00146.44 C
ANISOU 352 CA ASN A 61 22234 16311 17095 -186 2310 1036 C
ATOM 353 C ASN A 61 10.856 32.859 70.731 1.00144.43 C
ANISOU 353 C ASN A 61 21476 16169 17234 -44 1970 951 C
ATOM 354 O ASN A 61 11.539 33.762 70.235 1.00144.67 O
ANISOU 354 O ASN A 61 21475 16284 17212 70 1747 834 O
ATOM 355 CB ASN A 61 11.622 31.720 72.825 1.00141.48 C
ANISOU 355 CB ASN A 61 21978 15600 16177 -317 1986 1189 C
ATOM 356 CG ASN A 61 11.883 31.931 74.299 1.00154.19 C
ANISOU 356 CG ASN A 61 24219 17116 17250 -452 2168 1254 C
ATOM 357 OD1 ASN A 61 11.811 33.054 74.798 1.00151.63 O
ANISOU 357 OD1 ASN A 61 24099 16815 16698 -409 2406 1130 O
ATOM 358 ND2 ASN A 61 12.214 30.855 75.002 1.00161.32 N
ANISOU 358 ND2 ASN A 61 25453 17899 17940 -624 2029 1448 N
ATOM 359 N MET A 62 10.261 31.923 69.989 1.00135.98 N
ANISOU 359 N MET A 62 20027 15096 16544 -63 1923 1011 N
ATOM 360 CA MET A 62 10.305 31.974 68.530 1.00121.70 C
ANISOU 360 CA MET A 62 17757 13395 15087 48 1628 925 C
ATOM 361 C MET A 62 9.754 33.296 68.010 1.00118.64 C
ANISOU 361 C MET A 62 17144 13069 14865 171 1773 803 C
ATOM 362 O MET A 62 10.348 33.928 67.128 1.00120.97 O
ANISOU 362 O MET A 62 17307 13472 15184 262 1482 714 O
ATOM 363 CB MET A 62 9.518 30.795 67.957 1.00125.50 C
ANISOU 363 CB MET A 62 17886 13836 15964 -3 1624 1002 C
ATOM 364 CG MET A 62 9.513 30.686 66.447 1.00115.99 C
ANISOU 364 CG MET A 62 16238 12738 15097 82 1307 913 C
ATOM 365 SD MET A 62 8.408 29.362 65.925 1.00131.69 S
ANISOU 365 SD MET A 62 17826 14640 17569 19 1348 994 S
ATOM 366 CE MET A 62 8.692 29.330 64.158 1.00131.35 C
ANISOU 366 CE MET A 62 17378 14746 17784 106 903 856 C
ATOM 367 N ASN A 63 8.622 33.739 68.563 1.00126.74 N
ANISOU 367 N ASN A 63 18121 14012 16023 165 2228 795 N
ATOM 368 CA ASN A 63 7.982 34.956 68.075 1.00132.21 C
ANISOU 368 CA ASN A 63 18551 14715 16968 284 2355 678 C
ATOM 369 C ASN A 63 8.807 36.195 68.404 1.00129.97 C
ANISOU 369 C ASN A 63 18548 14475 16361 356 2286 577 C
ATOM 370 O ASN A 63 8.885 37.125 67.592 1.00132.16 O
ANISOU 370 O ASN A 63 18616 14804 16792 462 2112 499 O
ATOM 371 CB ASN A 63 6.574 35.077 68.659 1.00130.78 C
ANISOU 371 CB ASN A 63 18224 14402 17065 256 2886 665 C
ATOM 372 CG ASN A 63 5.639 33.993 68.156 1.00129.48 C
ANISOU 372 CG ASN A 63 17685 14176 17335 202 2934 753 C
ATOM 373 OD1 ASN A 63 5.743 33.549 67.013 1.00130.00 O
ANISOU 373 OD1 ASN A 63 17454 14303 17639 240 2560 774 O
ATOM 374 ND2 ASN A 63 4.722 33.556 69.013 1.00134.00 N
ANISOU 374 ND2 ASN A 63 18278 14625 18009 101 3406 798 N
ATOM 375 N ASN A 64 9.427 36.229 69.587 1.00126.07 N
ANISOU 375 N ASN A 64 18540 13945 15417 290 2397 587 N
ATOM 376 CA ASN A 64 10.202 37.404 69.978 1.00122.54 C
ANISOU 376 CA ASN A 64 18374 13515 14669 357 2329 482 C
ATOM 377 C ASN A 64 11.420 37.590 69.084 1.00121.48 C
ANISOU 377 C ASN A 64 18195 13492 14470 418 1810 467 C
ATOM 378 O ASN A 64 11.762 38.721 68.721 1.00124.41 O
ANISOU 378 O ASN A 64 18525 13900 14846 512 1697 376 O
ATOM 379 CB ASN A 64 10.624 37.298 71.444 1.00121.30 C
ANISOU 379 CB ASN A 64 18783 13285 14020 254 2516 502 C
ATOM 380 CG ASN A 64 9.452 37.414 72.396 1.00129.37 C
ANISOU 380 CG ASN A 64 19894 14209 15051 184 3110 469 C
ATOM 381 OD1 ASN A 64 8.438 38.031 72.073 1.00133.69 O
ANISOU 381 OD1 ASN A 64 20098 14724 15974 259 3393 369 O
ATOM 382 ND2 ASN A 64 9.589 36.830 73.581 1.00143.96 N
ANISOU 382 ND2 ASN A 64 22209 15995 16494 29 3301 548 N
ATOM 383 N ALA A 65 12.087 36.496 68.715 1.00117.96 N
ANISOU 383 N ALA A 65 17743 13090 13987 358 1502 547 N
ATOM 384 CA ALA A 65 13.224 36.608 67.810 1.00113.43 C
ANISOU 384 CA ALA A 65 17085 12622 13391 401 1055 505 C
ATOM 385 C ALA A 65 12.773 36.968 66.399 1.00123.27 C
ANISOU 385 C ALA A 65 17876 13972 14990 468 939 466 C
ATOM 386 O ALA A 65 13.421 37.775 65.722 1.00122.43 O
ANISOU 386 O ALA A 65 17709 13949 14860 520 714 403 O
ATOM 387 CB ALA A 65 14.023 35.307 67.808 1.00105.81 C
ANISOU 387 CB ALA A 65 16206 11650 12347 318 775 569 C
ATOM 388 N GLY A 66 11.665 36.386 65.939 1.00126.81 N
ANISOU 388 N GLY A 66 18011 14404 15768 453 1075 510 N
ATOM 389 CA GLY A 66 11.178 36.700 64.605 1.00115.11 C
ANISOU 389 CA GLY A 66 16125 12998 14612 500 925 486 C
ATOM 390 C GLY A 66 10.645 38.116 64.498 1.00118.35 C
ANISOU 390 C GLY A 66 16445 13374 15148 587 1048 438 C
ATOM 391 O GLY A 66 10.772 38.761 63.453 1.00123.16 O
ANISOU 391 O GLY A 66 16861 14060 15875 622 809 420 O
ATOM 392 N ASP A 67 10.040 38.619 65.577 1.00126.69 N
ANISOU 392 N ASP A 67 17647 14306 16184 611 1420 412 N
ATOM 393 CA ASP A 67 9.530 39.986 65.563 1.00134.03 C
ANISOU 393 CA ASP A 67 18480 15167 17278 702 1546 339 C
ATOM 394 C ASP A 67 10.666 41.001 65.514 1.00128.23 C
ANISOU 394 C ASP A 67 17960 14491 16268 745 1313 287 C
ATOM 395 O ASP A 67 10.544 42.046 64.865 1.00127.43 O
ANISOU 395 O ASP A 67 17689 14384 16344 810 1187 261 O
ATOM 396 CB ASP A 67 8.641 40.231 66.781 1.00134.64 C
ANISOU 396 CB ASP A 67 18666 15093 17399 707 2047 280 C
ATOM 397 CG ASP A 67 7.286 39.562 66.658 1.00147.26 C
ANISOU 397 CG ASP A 67 19930 16598 19424 681 2308 314 C
ATOM 398 OD1 ASP A 67 6.961 39.067 65.557 1.00151.80 O
ANISOU 398 OD1 ASP A 67 20166 17211 20299 680 2061 378 O
ATOM 399 OD2 ASP A 67 6.541 39.540 67.659 1.00148.83 O1-
ANISOU 399 OD2 ASP A 67 20207 16680 19661 652 2769 267 O1-
ATOM 400 N LYS A 68 11.777 40.712 66.195 1.00121.73 N
ANISOU 400 N LYS A 68 17508 13705 15039 704 1229 281 N
ATOM 401 CA LYS A 68 12.936 41.596 66.128 1.00124.34 C
ANISOU 401 CA LYS A 68 18026 14080 15136 738 981 232 C
ATOM 402 C LYS A 68 13.611 41.523 64.765 1.00113.98 C
ANISOU 402 C LYS A 68 16498 12912 13896 718 591 263 C
ATOM 403 O LYS A 68 14.186 42.515 64.302 1.00113.93 O
ANISOU 403 O LYS A 68 16487 12942 13860 748 406 238 O
ATOM 404 CB LYS A 68 13.929 41.236 67.232 1.00121.64 C
ANISOU 404 CB LYS A 68 18129 13708 14382 692 960 217 C
ATOM 405 CG LYS A 68 13.392 41.456 68.633 1.00128.70 C
ANISOU 405 CG LYS A 68 19328 14471 15102 686 1347 174 C
ATOM 406 CD LYS A 68 14.419 41.077 69.685 1.00129.32 C
ANISOU 406 CD LYS A 68 19888 14506 14740 620 1251 182 C
ATOM 407 CE LYS A 68 13.874 41.303 71.087 1.00123.96 C
ANISOU 407 CE LYS A 68 19570 13710 13820 583 1653 133 C
ATOM 408 NZ LYS A 68 14.851 40.911 72.140 1.00105.53 N
ANISOU 408 NZ LYS A 68 17755 11315 11026 498 1515 163 N
ATOM 409 N TRP A 69 13.551 40.361 64.114 1.00111.81 N
ANISOU 409 N TRP A 69 16053 12718 13713 655 474 311 N
ATOM 410 CA TRP A 69 14.116 40.208 62.780 1.00109.38 C
ANISOU 410 CA TRP A 69 15543 12560 13458 614 148 314 C
ATOM 411 C TRP A 69 13.190 40.780 61.714 1.00103.79 C
ANISOU 411 C TRP A 69 14509 11872 13053 631 97 352 C
ATOM 412 O TRP A 69 13.667 41.316 60.707 1.00 98.90 O
ANISOU 412 O TRP A 69 13800 11357 12419 600 -151 358 O
ATOM 413 CB TRP A 69 14.405 38.725 62.525 1.00108.08 C
ANISOU 413 CB TRP A 69 15324 12455 13286 540 41 318 C
ATOM 414 CG TRP A 69 14.687 38.343 61.105 1.00 94.51 C
ANISOU 414 CG TRP A 69 13357 10890 11664 482 -223 293 C
ATOM 415 CD1 TRP A 69 13.920 37.549 60.306 1.00 99.09 C
ANISOU 415 CD1 TRP A 69 13668 11509 12473 445 -263 312 C
ATOM 416 CD2 TRP A 69 15.842 38.695 60.332 1.00 93.02 C
ANISOU 416 CD2 TRP A 69 13180 10834 11332 437 -472 228 C
ATOM 417 NE1 TRP A 69 14.513 37.401 59.076 1.00 99.18 N
ANISOU 417 NE1 TRP A 69 13548 11679 12456 377 -520 254 N
ATOM 418 CE2 TRP A 69 15.695 38.094 59.066 1.00 93.69 C
ANISOU 418 CE2 TRP A 69 13016 11048 11532 364 -629 201 C
ATOM 419 CE3 TRP A 69 16.978 39.468 60.584 1.00 94.80 C
ANISOU 419 CE3 TRP A 69 13596 11073 11350 442 -567 182 C
ATOM 420 CZ2 TRP A 69 16.641 38.242 58.056 1.00 95.57 C
ANISOU 420 CZ2 TRP A 69 13210 11446 11659 283 -838 123 C
ATOM 421 CZ3 TRP A 69 17.917 39.614 59.579 1.00 95.34 C
ANISOU 421 CZ3 TRP A 69 13587 11286 11352 368 -780 116 C
ATOM 422 CH2 TRP A 69 17.743 39.004 58.330 1.00 93.30 C
ANISOU 422 CH2 TRP A 69 13094 11170 11184 283 -893 84 C
ATOM 423 N SER A 70 11.875 40.685 61.923 1.00115.03 N
ANISOU 423 N SER A 70 15759 13183 14762 667 321 383 N
ATOM 424 CA SER A 70 10.931 41.351 61.032 1.00121.42 C
ANISOU 424 CA SER A 70 16264 13954 15915 694 247 423 C
ATOM 425 C SER A 70 11.051 42.865 61.140 1.00118.43 C
ANISOU 425 C SER A 70 15942 13507 15547 759 226 407 C
ATOM 426 O SER A 70 10.947 43.578 60.135 1.00124.11 O
ANISOU 426 O SER A 70 16500 14250 16408 746 -18 460 O
ATOM 427 CB SER A 70 9.502 40.909 61.352 1.00137.59 C
ANISOU 427 CB SER A 70 18089 15857 18332 724 511 440 C
ATOM 428 OG SER A 70 9.244 39.601 60.871 1.00139.57 O
ANISOU 428 OG SER A 70 18192 16163 18675 658 438 474 O
ATOM 429 N ALA A 71 11.268 43.376 62.355 1.00113.59 N
ANISOU 429 N ALA A 71 15578 12800 14782 818 465 337 N
ATOM 430 CA ALA A 71 11.379 44.813 62.570 1.00117.31 C
ANISOU 430 CA ALA A 71 16109 13180 15285 889 459 297 C
ATOM 431 C ALA A 71 12.751 45.362 62.202 1.00106.43 C
ANISOU 431 C ALA A 71 14912 11913 13613 855 169 305 C
ATOM 432 O ALA A 71 12.881 46.572 61.992 1.00110.78 O
ANISOU 432 O ALA A 71 15449 12406 14238 892 59 308 O
ATOM 433 CB ALA A 71 11.061 45.154 64.026 1.00122.19 C
ANISOU 433 CB ALA A 71 16937 13650 15841 958 843 187 C
ATOM 434 N PHE A 72 13.774 44.509 62.132 1.00 96.63 N
ANISOU 434 N PHE A 72 13822 10811 12082 782 43 304 N
ATOM 435 CA PHE A 72 15.081 44.954 61.664 1.00101.01 C
ANISOU 435 CA PHE A 72 14492 11470 12417 734 -225 301 C
ATOM 436 C PHE A 72 15.099 45.098 60.148 1.00100.76 C
ANISOU 436 C PHE A 72 14225 11567 12492 649 -492 382 C
ATOM 437 O PHE A 72 15.696 46.040 59.616 1.00106.00 O
ANISOU 437 O PHE A 72 14907 12263 13104 616 -676 414 O
ATOM 438 CB PHE A 72 16.162 43.976 62.132 1.00103.85 C
ANISOU 438 CB PHE A 72 15063 11900 12495 686 -270 249 C
ATOM 439 CG PHE A 72 17.477 44.124 61.416 1.00 94.37 C
ANISOU 439 CG PHE A 72 13887 10824 11144 612 -543 230 C
ATOM 440 CD1 PHE A 72 18.335 45.168 61.720 1.00 96.65 C
ANISOU 440 CD1 PHE A 72 14339 11067 11315 633 -634 200 C
ATOM 441 CD2 PHE A 72 17.865 43.203 60.455 1.00 90.54 C
ANISOU 441 CD2 PHE A 72 13255 10493 10652 514 -690 221 C
ATOM 442 CE1 PHE A 72 19.547 45.299 61.069 1.00 97.36 C
ANISOU 442 CE1 PHE A 72 14428 11261 11303 552 -854 176 C
ATOM 443 CE2 PHE A 72 19.074 43.329 59.800 1.00 88.47 C
ANISOU 443 CE2 PHE A 72 12999 10345 10272 431 -888 175 C
ATOM 444 CZ PHE A 72 19.917 44.377 60.107 1.00 87.03 C
ANISOU 444 CZ PHE A 72 12963 10113 9990 447 -962 158 C
ATOM 445 N LEU A 73 14.439 44.178 59.441 1.00 88.59 N
ANISOU 445 N LEU A 73 12478 10094 11089 598 -521 419 N
ATOM 446 CA LEU A 73 14.402 44.250 57.985 1.00 84.86 C
ANISOU 446 CA LEU A 73 11821 9747 10674 495 -782 491 C
ATOM 447 C LEU A 73 13.547 45.418 57.510 1.00 94.63 C
ANISOU 447 C LEU A 73 12912 10871 12174 521 -877 592 C
ATOM 448 O LEU A 73 13.875 46.066 56.509 1.00 88.35 O
ANISOU 448 O LEU A 73 12086 10148 11333 428 -1128 674 O
ATOM 449 CB LEU A 73 13.887 42.930 57.412 1.00 85.73 C
ANISOU 449 CB LEU A 73 11764 9938 10870 438 -804 486 C
ATOM 450 CG LEU A 73 14.966 41.872 57.174 1.00 84.28 C
ANISOU 450 CG LEU A 73 11659 9917 10445 353 -875 394 C
ATOM 451 CD1 LEU A 73 14.358 40.584 56.646 1.00 85.51 C
ANISOU 451 CD1 LEU A 73 11635 10124 10730 309 -898 374 C
ATOM 452 CD2 LEU A 73 16.027 42.402 56.221 1.00 83.26 C
ANISOU 452 CD2 LEU A 73 11576 9948 10112 238 -1087 382 C
ATOM 453 N LYS A 74 12.448 45.703 58.214 1.00117.56 N
ANISOU 453 N LYS A 74 15718 13580 15368 636 -679 585 N
ATOM 454 CA LYS A 74 11.649 46.878 57.883 1.00116.00 C
ANISOU 454 CA LYS A 74 15360 13222 15494 680 -777 659 C
ATOM 455 C LYS A 74 12.418 48.163 58.159 1.00114.89 C
ANISOU 455 C LYS A 74 15385 13032 15236 704 -848 658 C
ATOM 456 O LYS A 74 12.244 49.157 57.445 1.00111.64 O
ANISOU 456 O LYS A 74 14880 12554 14984 675 -1085 763 O
ATOM 457 CB LYS A 74 10.335 46.856 58.667 1.00115.60 C
ANISOU 457 CB LYS A 74 15140 12955 15828 801 -496 605 C
ATOM 458 CG LYS A 74 9.277 47.821 58.150 1.00133.98 C
ANISOU 458 CG LYS A 74 17198 15082 18628 844 -638 675 C
ATOM 459 CD LYS A 74 8.102 47.927 59.113 1.00129.71 C
ANISOU 459 CD LYS A 74 16489 14303 18490 975 -284 567 C
ATOM 460 CE LYS A 74 7.505 49.326 59.106 1.00118.46 C
ANISOU 460 CE LYS A 74 14900 12633 17476 1061 -360 562 C
ATOM 461 NZ LYS A 74 6.478 49.506 60.171 1.00125.63 N
ANISOU 461 NZ LYS A 74 15659 13308 18766 1189 58 398 N
ATOM 462 N GLU A 75 13.273 48.156 59.185 1.00110.76 N
ANISOU 462 N GLU A 75 15116 12522 14445 750 -676 550 N
ATOM 463 CA GLU A 75 14.128 49.306 59.454 1.00108.10 C
ANISOU 463 CA GLU A 75 14949 12142 13984 768 -766 538 C
ATOM 464 C GLU A 75 15.201 49.455 58.383 1.00106.32 C
ANISOU 464 C GLU A 75 14766 12093 13539 622 -1062 627 C
ATOM 465 O GLU A 75 15.564 50.576 58.008 1.00100.88 O
ANISOU 465 O GLU A 75 14093 11357 12878 592 -1243 700 O
ATOM 466 CB GLU A 75 14.774 49.169 60.831 1.00117.12 C
ANISOU 466 CB GLU A 75 16372 13243 14885 844 -538 395 C
ATOM 467 CG GLU A 75 15.610 50.370 61.251 1.00134.19 C
ANISOU 467 CG GLU A 75 18713 15324 16949 879 -624 358 C
ATOM 468 CD GLU A 75 16.269 50.180 62.605 1.00141.74 C
ANISOU 468 CD GLU A 75 19982 16232 17640 940 -446 216 C
ATOM 469 OE1 GLU A 75 16.618 49.027 62.939 1.00124.76 O
ANISOU 469 OE1 GLU A 75 17947 14176 15279 903 -374 186 O
ATOM 470 OE2 GLU A 75 16.448 51.180 63.331 1.00135.53 O1-
ANISOU 470 OE2 GLU A 75 19338 15301 16858 1019 -405 136 O1-
ATOM 471 N GLN A 76 15.724 48.334 57.884 1.00105.89 N
ANISOU 471 N GLN A 76 14724 12235 13276 521 -1103 614 N
ATOM 472 CA GLN A 76 16.797 48.387 56.898 1.00101.55 C
ANISOU 472 CA GLN A 76 14214 11866 12502 364 -1319 657 C
ATOM 473 C GLN A 76 16.259 48.598 55.490 1.00108.96 C
ANISOU 473 C GLN A 76 14989 12879 13533 232 -1550 806 C
ATOM 474 O GLN A 76 16.933 49.221 54.662 1.00103.45 O
ANISOU 474 O GLN A 76 14336 12270 12701 94 -1740 890 O
ATOM 475 CB GLN A 76 17.627 47.106 56.959 1.00 95.64 C
ANISOU 475 CB GLN A 76 13534 11279 11524 309 -1260 543 C
ATOM 476 CG GLN A 76 18.429 46.943 58.241 1.00107.23 C
ANISOU 476 CG GLN A 76 15212 12674 12855 399 -1126 420 C
ATOM 477 CD GLN A 76 19.543 47.958 58.386 1.00114.56 C
ANISOU 477 CD GLN A 76 16280 13576 13671 378 -1232 409 C
ATOM 478 OE1 GLN A 76 20.435 48.042 57.544 1.00115.21 O
ANISOU 478 OE1 GLN A 76 16338 13792 13644 246 -1372 419 O
ATOM 479 NE2 GLN A 76 19.504 48.728 59.468 1.00110.02 N
ANISOU 479 NE2 GLN A 76 15854 12823 13126 501 -1152 376 N
ATOM 480 N SER A 77 15.060 48.080 55.203 1.00109.33 N
ANISOU 480 N SER A 77 14857 12880 13802 258 -1547 844 N
ATOM 481 CA SER A 77 14.417 48.348 53.922 1.00 99.79 C
ANISOU 481 CA SER A 77 13509 11694 12710 137 -1816 999 C
ATOM 482 C SER A 77 14.241 49.843 53.701 1.00107.35 C
ANISOU 482 C SER A 77 14462 12496 13831 133 -2006 1143 C
ATOM 483 O SER A 77 14.457 50.348 52.593 1.00113.49 O
ANISOU 483 O SER A 77 15262 13345 14515 -36 -2281 1294 O
ATOM 484 CB SER A 77 13.061 47.640 53.859 1.00111.35 C
ANISOU 484 CB SER A 77 14760 13065 14481 201 -1785 1006 C
ATOM 485 OG SER A 77 12.395 47.914 52.640 1.00141.25 O
ANISOU 485 OG SER A 77 18424 16843 18403 84 -2099 1162 O
ATOM 486 N THR A 78 13.855 50.568 54.754 1.00108.03 N
ANISOU 486 N THR A 78 14531 12358 14157 306 -1861 1094 N
ATOM 487 CA THR A 78 13.652 52.008 54.644 1.00110.24 C
ANISOU 487 CA THR A 78 14781 12446 14659 324 -2043 1208 C
ATOM 488 C THR A 78 14.953 52.723 54.296 1.00103.80 C
ANISOU 488 C THR A 78 14156 11735 13550 199 -2184 1272 C
ATOM 489 O THR A 78 14.998 53.538 53.367 1.00112.67 O
ANISOU 489 O THR A 78 15271 12836 14701 64 -2477 1459 O
ATOM 490 CB THR A 78 13.077 52.554 55.951 1.00102.06 C
ANISOU 490 CB THR A 78 13700 11158 13919 540 -1801 1079 C
ATOM 491 OG1 THR A 78 11.833 51.903 56.245 1.00104.77 O
ANISOU 491 OG1 THR A 78 13841 11395 14572 638 -1637 1018 O
ATOM 492 CG2 THR A 78 12.851 54.051 55.841 1.00103.47 C
ANISOU 492 CG2 THR A 78 13819 11108 14387 571 -2005 1174 C
ATOM 493 N LEU A 79 16.025 52.428 55.037 1.00108.49 N
ANISOU 493 N LEU A 79 14922 12425 13872 231 -1992 1128 N
ATOM 494 CA LEU A 79 17.310 53.076 54.789 1.00114.42 C
ANISOU 494 CA LEU A 79 15828 13256 14389 118 -2100 1166 C
ATOM 495 C LEU A 79 17.856 52.752 53.404 1.00110.37 C
ANISOU 495 C LEU A 79 15332 12980 13622 -133 -2278 1281 C
ATOM 496 O LEU A 79 18.507 53.600 52.783 1.00113.80 O
ANISOU 496 O LEU A 79 15838 13441 13960 -281 -2449 1409 O
ATOM 497 CB LEU A 79 18.319 52.658 55.860 1.00104.87 C
ANISOU 497 CB LEU A 79 14783 12087 12978 202 -1883 972 C
ATOM 498 CG LEU A 79 17.980 53.059 57.296 1.00 98.08 C
ANISOU 498 CG LEU A 79 13988 11006 12270 419 -1696 842 C
ATOM 499 CD1 LEU A 79 18.913 52.365 58.273 1.00106.75 C
ANISOU 499 CD1 LEU A 79 15277 12159 13125 472 -1525 668 C
ATOM 500 CD2 LEU A 79 18.028 54.573 57.469 1.00 94.11 C
ANISOU 500 CD2 LEU A 79 13502 10302 11954 462 -1829 904 C
ATOM 501 N ALA A 80 17.604 51.538 52.907 1.00 99.43 N
ANISOU 501 N ALA A 80 13891 11766 12121 -195 -2229 1231 N
ATOM 502 CA ALA A 80 18.154 51.128 51.617 1.00 99.10 C
ANISOU 502 CA ALA A 80 13887 11968 11797 -444 -2353 1289 C
ATOM 503 C ALA A 80 17.622 51.991 50.479 1.00108.01 C
ANISOU 503 C ALA A 80 15004 13062 12973 -611 -2665 1541 C
ATOM 504 O ALA A 80 18.357 52.308 49.536 1.00104.57 O
ANISOU 504 O ALA A 80 14679 12779 12275 -847 -2784 1640 O
ATOM 505 CB ALA A 80 17.837 49.655 51.358 1.00 94.36 C
ANISOU 505 CB ALA A 80 13214 11522 11115 -457 -2254 1165 C
ATOM 506 N GLN A 81 16.346 52.378 50.546 1.00116.65 N
ANISOU 506 N GLN A 81 15967 13943 14413 -507 -2804 1650 N
ATOM 507 CA GLN A 81 15.746 53.168 49.477 1.00120.35 C
ANISOU 507 CA GLN A 81 16420 14331 14975 -664 -3167 1909 C
ATOM 508 C GLN A 81 16.398 54.537 49.326 1.00115.83 C
ANISOU 508 C GLN A 81 15959 13670 14380 -759 -3327 2071 C
ATOM 509 O GLN A 81 16.257 55.163 48.270 1.00124.65 O
ANISOU 509 O GLN A 81 17139 14780 15444 -970 -3644 2314 O
ATOM 510 CB GLN A 81 14.243 53.320 49.725 1.00121.87 C
ANISOU 510 CB GLN A 81 16400 14255 15649 -500 -3285 1962 C
ATOM 511 CG GLN A 81 13.488 52.000 49.693 1.00119.36 C
ANISOU 511 CG GLN A 81 15954 14007 15392 -442 -3180 1845 C
ATOM 512 CD GLN A 81 12.055 52.132 50.163 1.00132.35 C
ANISOU 512 CD GLN A 81 17349 15359 17580 -252 -3214 1851 C
ATOM 513 OE1 GLN A 81 11.536 53.239 50.311 1.00146.78 O
ANISOU 513 OE1 GLN A 81 19086 16924 19759 -185 -3378 1960 O
ATOM 514 NE2 GLN A 81 11.407 51.000 50.410 1.00125.20 N
ANISOU 514 NE2 GLN A 81 16308 14478 16783 -164 -3051 1724 N
ATOM 515 N MET A 82 17.115 55.012 50.349 1.00107.87 N
ANISOU 515 N MET A 82 14995 12586 13406 -622 -3137 1953 N
ATOM 516 CA MET A 82 17.830 56.278 50.236 1.00110.29 C
ANISOU 516 CA MET A 82 15400 12805 13700 -714 -3281 2093 C
ATOM 517 C MET A 82 18.950 56.219 49.204 1.00109.60 C
ANISOU 517 C MET A 82 15476 12980 13186 -1020 -3326 2182 C
ATOM 518 O MET A 82 19.444 57.270 48.781 1.00110.25 O
ANISOU 518 O MET A 82 15646 13006 13238 -1172 -3501 2369 O
ATOM 519 CB MET A 82 18.394 56.685 51.599 1.00104.33 C
ANISOU 519 CB MET A 82 14666 11915 13060 -498 -3064 1911 C
ATOM 520 CG MET A 82 17.336 56.911 52.669 1.00115.72 C
ANISOU 520 CG MET A 82 15972 13086 14909 -216 -2978 1805 C
ATOM 521 SD MET A 82 17.921 57.952 54.021 1.00117.99 S
ANISOU 521 SD MET A 82 16331 13148 15354 -22 -2861 1667 S
ATOM 522 CE MET A 82 16.472 57.992 55.073 1.00123.59 C
ANISOU 522 CE MET A 82 16867 13582 16509 264 -2701 1516 C
ATOM 523 N TYR A 83 19.369 55.016 48.798 1.00104.49 N
ANISOU 523 N TYR A 83 14865 12610 12228 -1121 -3156 2043 N
ATOM 524 CA TYR A 83 20.346 54.838 47.733 1.00104.31 C
ANISOU 524 CA TYR A 83 14980 12854 11798 -1431 -3149 2086 C
ATOM 525 C TYR A 83 19.603 54.458 46.457 1.00117.62 C
ANISOU 525 C TYR A 83 16707 14660 13322 -1645 -3366 2240 C
ATOM 526 O TYR A 83 19.239 53.285 46.284 1.00117.91 O
ANISOU 526 O TYR A 83 16691 14834 13275 -1621 -3270 2090 O
ATOM 527 CB TYR A 83 21.371 53.761 48.104 1.00112.18 C
ANISOU 527 CB TYR A 83 15976 14061 12585 -1410 -2820 1792 C
ATOM 528 CG TYR A 83 22.025 53.950 49.459 1.00109.90 C
ANISOU 528 CG TYR A 83 15661 13636 12461 -1180 -2638 1620 C
ATOM 529 CD1 TYR A 83 23.185 54.704 49.593 1.00104.06 C
ANISOU 529 CD1 TYR A 83 14990 12881 11667 -1262 -2607 1628 C
ATOM 530 CD2 TYR A 83 21.495 53.358 50.599 1.00107.23 C
ANISOU 530 CD2 TYR A 83 15243 13179 12321 -898 -2502 1452 C
ATOM 531 CE1 TYR A 83 23.788 54.876 50.828 1.00100.23 C
ANISOU 531 CE1 TYR A 83 14500 12254 11329 -1057 -2486 1468 C
ATOM 532 CE2 TYR A 83 22.093 53.524 51.837 1.00109.34 C
ANISOU 532 CE2 TYR A 83 15537 13319 12689 -710 -2363 1301 C
ATOM 533 CZ TYR A 83 23.239 54.283 51.945 1.00107.56 C
ANISOU 533 CZ TYR A 83 15386 13071 12412 -785 -2374 1306 C
ATOM 534 OH TYR A 83 23.839 54.451 53.174 1.00114.42 O
ANISOU 534 OH TYR A 83 16299 13796 13380 -603 -2278 1153 O
ATOM 535 N PRO A 84 19.348 55.396 45.543 1.00110.82 N
ANISOU 535 N PRO A 84 15953 13739 12415 -1864 -3685 2541 N
ATOM 536 CA PRO A 84 18.500 55.090 44.380 1.00105.99 C
ANISOU 536 CA PRO A 84 15406 13193 11674 -2060 -3964 2709 C
ATOM 537 C PRO A 84 19.232 54.238 43.352 1.00114.51 C
ANISOU 537 C PRO A 84 16648 14634 12227 -2358 -3829 2619 C
ATOM 538 O PRO A 84 20.330 54.582 42.910 1.00115.68 O
ANISOU 538 O PRO A 84 16945 14944 12064 -2592 -3713 2642 O
ATOM 539 CB PRO A 84 18.155 56.475 43.824 1.00119.32 C
ANISOU 539 CB PRO A 84 17186 14671 13478 -2213 -4368 3076 C
ATOM 540 CG PRO A 84 19.307 57.330 44.236 1.00102.39 C
ANISOU 540 CG PRO A 84 15107 12512 11286 -2250 -4226 3089 C
ATOM 541 CD PRO A 84 19.747 56.814 45.580 1.00108.98 C
ANISOU 541 CD PRO A 84 15789 13333 12285 -1936 -3851 2758 C
ATOM 542 N LEU A 85 18.581 53.141 42.941 1.00106.17 N
ANISOU 542 N LEU A 85 15555 13692 11093 -2359 -3844 2509 N
ATOM 543 CA LEU A 85 19.208 52.126 42.093 1.00102.19 C
ANISOU 543 CA LEU A 85 15170 13528 10130 -2595 -3665 2333 C
ATOM 544 C LEU A 85 19.800 52.697 40.811 1.00117.14 C
ANISOU 544 C LEU A 85 17346 15603 11561 -3019 -3783 2531 C
ATOM 545 O LEU A 85 20.751 52.127 40.261 1.00112.35 O
ANISOU 545 O LEU A 85 16844 15287 10559 -3236 -3516 2349 O
ATOM 546 CB LEU A 85 18.187 51.046 41.732 1.00102.47 C
ANISOU 546 CB LEU A 85 15135 13599 10200 -2546 -3779 2247 C
ATOM 547 CG LEU A 85 17.665 50.123 42.830 1.00101.94 C
ANISOU 547 CG LEU A 85 14808 13426 10497 -2189 -3593 2008 C
ATOM 548 CD1 LEU A 85 16.875 48.981 42.213 1.00114.62 C
ANISOU 548 CD1 LEU A 85 16376 15124 12052 -2226 -3694 1913 C
ATOM 549 CD2 LEU A 85 18.814 49.587 43.664 1.00113.04 C
ANISOU 549 CD2 LEU A 85 16150 14950 11852 -2072 -3176 1715 C
ATOM 550 N GLN A 86 19.247 53.806 40.312 1.00138.85 N
ANISOU 550 N GLN A 86 20220 18176 14360 -3156 -4178 2898 N
ATOM 551 CA GLN A 86 19.671 54.347 39.022 1.00137.92 C
ANISOU 551 CA GLN A 86 20419 18218 13767 -3599 -4338 3138 C
ATOM 552 C GLN A 86 21.161 54.653 38.995 1.00136.45 C
ANISOU 552 C GLN A 86 20322 18222 13300 -3783 -3978 3048 C
ATOM 553 O GLN A 86 21.804 54.539 37.944 1.00144.49 O
ANISOU 553 O GLN A 86 21582 19507 13811 -4166 -3880 3067 O
ATOM 554 CB GLN A 86 18.874 55.613 38.716 1.00132.32 C
ANISOU 554 CB GLN A 86 19798 17213 13264 -3673 -4851 3570 C
ATOM 555 CG GLN A 86 17.397 55.370 38.499 1.00159.30 C
ANISOU 555 CG GLN A 86 23142 20431 16954 -3564 -5269 3691 C
ATOM 556 CD GLN A 86 16.632 56.655 38.271 1.00188.25 C
ANISOU 556 CD GLN A 86 26852 23751 20921 -3614 -5803 4104 C
ATOM 557 OE1 GLN A 86 17.056 57.728 38.703 1.00172.04 O
ANISOU 557 OE1 GLN A 86 24781 21533 19053 -3586 -5823 4251 O
ATOM 558 NE2 GLN A 86 15.493 56.555 37.596 1.00188.93 N
ANISOU 558 NE2 GLN A 86 26984 23701 21100 -3686 -6267 4291 N
ATOM 559 N GLU A 87 21.722 55.027 40.136 1.00138.50 N
ANISOU 559 N GLU A 87 20393 18344 13886 -3525 -3771 2937 N
ATOM 560 CA GLU A 87 23.099 55.476 40.234 1.00141.60 C
ANISOU 560 CA GLU A 87 20827 18841 14134 -3666 -3481 2876 C
ATOM 561 C GLU A 87 24.069 54.345 40.559 1.00142.27 C
ANISOU 561 C GLU A 87 20789 19159 14108 -3606 -3010 2448 C
ATOM 562 O GLU A 87 25.284 54.568 40.553 1.00146.45 O
ANISOU 562 O GLU A 87 21327 19794 14522 -3746 -2737 2349 O
ATOM 563 CB GLU A 87 23.167 56.586 41.285 1.00149.93 C
ANISOU 563 CB GLU A 87 21755 19580 15633 -3425 -3577 3001 C
ATOM 564 CG GLU A 87 22.387 57.826 40.838 1.00151.89 C
ANISOU 564 CG GLU A 87 22125 19585 16003 -3539 -4052 3435 C
ATOM 565 CD GLU A 87 22.258 58.890 41.911 1.00164.46 C
ANISOU 565 CD GLU A 87 23564 20826 18099 -3263 -4180 3528 C
ATOM 566 OE1 GLU A 87 22.577 58.604 43.082 1.00170.49 O
ANISOU 566 OE1 GLU A 87 24136 21522 19120 -2947 -3925 3255 O
ATOM 567 OE2 GLU A 87 21.812 60.010 41.581 1.00144.91 O1-
ANISOU 567 OE2 GLU A 87 21167 18126 15766 -3367 -4558 3874 O1-
ATOM 568 N ILE A 88 23.562 53.141 40.820 1.00137.39 N
ANISOU 568 N ILE A 88 20042 18603 13556 -3412 -2924 2194 N
ATOM 569 CA ILE A 88 24.390 51.963 41.059 1.00137.59 C
ANISOU 569 CA ILE A 88 19942 18828 13509 -3360 -2529 1785 C
ATOM 570 C ILE A 88 24.623 51.228 39.746 1.00120.96 C
ANISOU 570 C ILE A 88 17998 17044 10918 -3713 -2414 1671 C
ATOM 571 O ILE A 88 23.679 50.943 38.999 1.00121.11 O
ANISOU 571 O ILE A 88 18143 17111 10763 -3819 -2657 1786 O
ATOM 572 CB ILE A 88 23.752 51.030 42.107 1.00135.04 C
ANISOU 572 CB ILE A 88 19392 18381 13536 -2964 -2493 1569 C
ATOM 573 CG1 ILE A 88 23.638 51.700 43.487 1.00123.63 C
ANISOU 573 CG1 ILE A 88 17811 16638 12527 -2626 -2536 1624 C
ATOM 574 CG2 ILE A 88 24.509 49.712 42.193 1.00136.94 C
ANISOU 574 CG2 ILE A 88 19513 18818 13699 -2942 -2151 1163 C
ATOM 575 CD1 ILE A 88 22.487 52.631 43.667 1.00120.79 C
ANISOU 575 CD1 ILE A 88 17470 16020 12406 -2517 -2884 1935 C
ATOM 576 N GLN A 89 25.886 50.903 39.477 1.00128.84 N
ANISOU 576 N GLN A 89 18984 18250 11719 -3895 -2042 1421 N
ATOM 577 CA GLN A 89 26.306 50.251 38.243 1.00131.80 C
ANISOU 577 CA GLN A 89 19514 18948 11616 -4260 -1844 1254 C
ATOM 578 C GLN A 89 26.831 48.837 38.449 1.00135.39 C
ANISOU 578 C GLN A 89 19762 19551 12130 -4150 -1504 771 C
ATOM 579 O GLN A 89 26.567 47.966 37.619 1.00139.23 O
ANISOU 579 O GLN A 89 20330 20241 12330 -4310 -1457 603 O
ATOM 580 CB GLN A 89 27.369 51.108 37.548 1.00131.12 C
ANISOU 580 CB GLN A 89 19598 18996 11225 -4644 -1657 1361 C
ATOM 581 CG GLN A 89 26.890 52.529 37.269 1.00140.32 C
ANISOU 581 CG GLN A 89 20984 20002 12330 -4789 -2022 1863 C
ATOM 582 CD GLN A 89 27.975 53.427 36.708 1.00173.43 C
ANISOU 582 CD GLN A 89 25328 24294 16274 -5158 -1830 1993 C
ATOM 583 OE1 GLN A 89 29.142 53.042 36.636 1.00186.74 O
ANISOU 583 OE1 GLN A 89 26914 26149 17891 -5279 -1393 1690 O
ATOM 584 NE2 GLN A 89 27.594 54.637 36.313 1.00173.44 N
ANISOU 584 NE2 GLN A 89 25553 24169 16178 -5344 -2162 2448 N
ATOM 585 N ASN A 90 27.576 48.584 39.527 1.00144.42 N
ANISOU 585 N ASN A 90 20644 20580 13648 -3889 -1292 540 N
ATOM 586 CA ASN A 90 27.933 47.217 39.901 1.00138.99 C
ANISOU 586 CA ASN A 90 19728 19955 13126 -3723 -1055 108 C
ATOM 587 C ASN A 90 26.662 46.394 40.069 1.00132.78 C
ANISOU 587 C ASN A 90 18907 19109 12436 -3508 -1284 106 C
ATOM 588 O ASN A 90 25.833 46.683 40.939 1.00136.15 O
ANISOU 588 O ASN A 90 19275 19299 13158 -3220 -1522 297 O
ATOM 589 CB ASN A 90 28.762 47.222 41.194 1.00133.24 C
ANISOU 589 CB ASN A 90 18752 19033 12839 -3439 -915 -53 C
ATOM 590 CG ASN A 90 29.374 45.848 41.534 1.00136.02 C
ANISOU 590 CG ASN A 90 18860 19433 13389 -3312 -668 -510 C
ATOM 591 OD1 ASN A 90 28.745 44.816 41.320 1.00138.82 O
ANISOU 591 OD1 ASN A 90 19177 19856 13714 -3251 -702 -661 O
ATOM 592 ND2 ASN A 90 30.597 45.844 42.093 1.00131.42 N
ANISOU 592 ND2 ASN A 90 18096 18783 13055 -3266 -450 -726 N
ATOM 593 N LEU A 91 26.512 45.369 39.226 1.00117.15 N
ANISOU 593 N LEU A 91 16957 17340 10217 -3660 -1198 -128 N
ATOM 594 CA LEU A 91 25.263 44.617 39.173 1.00111.83 C
ANISOU 594 CA LEU A 91 16270 16621 9598 -3515 -1441 -110 C
ATOM 595 C LEU A 91 25.023 43.812 40.443 1.00110.46 C
ANISOU 595 C LEU A 91 15820 16249 9900 -3110 -1427 -275 C
ATOM 596 O LEU A 91 23.868 43.614 40.835 1.00103.15 O
ANISOU 596 O LEU A 91 14856 15171 9165 -2904 -1671 -133 O
ATOM 597 CB LEU A 91 25.260 43.689 37.957 1.00118.45 C
ANISOU 597 CB LEU A 91 17212 17732 10060 -3787 -1344 -359 C
ATOM 598 CG LEU A 91 25.298 44.316 36.561 1.00132.28 C
ANISOU 598 CG LEU A 91 19311 19706 11243 -4234 -1390 -193 C
ATOM 599 CD1 LEU A 91 25.343 43.230 35.496 1.00115.02 C
ANISOU 599 CD1 LEU A 91 17213 17787 8704 -4471 -1251 -524 C
ATOM 600 CD2 LEU A 91 24.103 45.231 36.342 1.00110.32 C
ANISOU 600 CD2 LEU A 91 16739 16780 8399 -4254 -1857 286 C
ATOM 601 N THR A 92 26.087 43.330 41.091 1.00118.07 N
ANISOU 601 N THR A 92 16590 17196 11076 -3002 -1154 -570 N
ATOM 602 CA THR A 92 25.901 42.544 42.303 1.00102.89 C
ANISOU 602 CA THR A 92 14444 15077 9574 -2646 -1162 -707 C
ATOM 603 C THR A 92 25.557 43.426 43.496 1.00108.47 C
ANISOU 603 C THR A 92 15145 15517 10553 -2387 -1310 -434 C
ATOM 604 O THR A 92 24.918 42.957 44.444 1.00109.84 O
ANISOU 604 O THR A 92 15213 15510 11011 -2106 -1396 -426 O
ATOM 605 CB THR A 92 27.145 41.695 42.591 1.00 99.95 C
ANISOU 605 CB THR A 92 13868 14742 9368 -2624 -876 -1112 C
ATOM 606 OG1 THR A 92 26.789 40.605 43.447 1.00116.65 O
ANISOU 606 OG1 THR A 92 15800 16707 11814 -2343 -923 -1268 O
ATOM 607 CG2 THR A 92 28.232 42.514 43.270 1.00110.47 C
ANISOU 607 CG2 THR A 92 15155 15964 10856 -2589 -761 -1091 C
ATOM 608 N VAL A 93 25.959 44.699 43.462 1.00109.79 N
ANISOU 608 N VAL A 93 15429 15652 10635 -2489 -1334 -216 N
ATOM 609 CA VAL A 93 25.476 45.654 44.452 1.00104.30 C
ANISOU 609 CA VAL A 93 14756 14705 10169 -2268 -1506 56 C
ATOM 610 C VAL A 93 24.001 45.951 44.221 1.00111.01 C
ANISOU 610 C VAL A 93 15687 15475 11018 -2221 -1785 331 C
ATOM 611 O VAL A 93 23.211 46.015 45.171 1.00107.46 O
ANISOU 611 O VAL A 93 15166 14810 10853 -1950 -1892 427 O
ATOM 612 CB VAL A 93 26.322 46.941 44.414 1.00 91.20 C
ANISOU 612 CB VAL A 93 13188 13019 8444 -2403 -1474 206 C
ATOM 613 CG1 VAL A 93 25.706 48.008 45.307 1.00 89.89 C
ANISOU 613 CG1 VAL A 93 13061 12591 8501 -2194 -1680 489 C
ATOM 614 CG2 VAL A 93 27.757 46.653 44.831 1.00 90.93 C
ANISOU 614 CG2 VAL A 93 13024 13000 8524 -2403 -1218 -75 C
ATOM 615 N LYS A 94 23.602 46.118 42.956 1.00118.38 N
ANISOU 615 N LYS A 94 16769 16568 11640 -2493 -1910 453 N
ATOM 616 CA LYS A 94 22.221 46.484 42.659 1.00107.39 C
ANISOU 616 CA LYS A 94 15448 15070 10286 -2469 -2233 732 C
ATOM 617 C LYS A 94 21.250 45.370 43.033 1.00105.16 C
ANISOU 617 C LYS A 94 15013 14716 10228 -2253 -2286 613 C
ATOM 618 O LYS A 94 20.140 45.647 43.497 1.00109.84 O
ANISOU 618 O LYS A 94 15548 15100 11086 -2071 -2486 798 O
ATOM 619 CB LYS A 94 22.067 46.849 41.181 1.00107.86 C
ANISOU 619 CB LYS A 94 15739 15312 9930 -2840 -2394 891 C
ATOM 620 CG LYS A 94 20.727 47.513 40.872 1.00112.82 C
ANISOU 620 CG LYS A 94 16452 15772 10643 -2835 -2804 1239 C
ATOM 621 CD LYS A 94 20.465 47.666 39.380 1.00123.11 C
ANISOU 621 CD LYS A 94 18017 17249 11509 -3211 -3021 1390 C
ATOM 622 CE LYS A 94 21.470 48.587 38.709 1.00132.70 C
ANISOU 622 CE LYS A 94 19458 18606 12355 -3543 -2937 1516 C
ATOM 623 NZ LYS A 94 20.944 49.083 37.404 1.00115.75 N
ANISOU 623 NZ LYS A 94 17618 16535 9826 -3896 -3268 1801 N
ATOM 624 N LEU A 95 21.642 44.107 42.835 1.00102.79 N
ANISOU 624 N LEU A 95 14628 14569 9860 -2274 -2105 298 N
ATOM 625 CA LEU A 95 20.771 42.993 43.202 1.00 95.01 C
ANISOU 625 CA LEU A 95 13486 13506 9107 -2078 -2152 183 C
ATOM 626 C LEU A 95 20.440 43.022 44.689 1.00 92.45 C
ANISOU 626 C LEU A 95 13015 12925 9185 -1739 -2107 220 C
ATOM 627 O LEU A 95 19.267 43.021 45.080 1.00 99.26 O
ANISOU 627 O LEU A 95 13808 13615 10291 -1577 -2256 364 O
ATOM 628 CB LEU A 95 21.419 41.659 42.828 1.00 91.48 C
ANISOU 628 CB LEU A 95 12955 13244 8560 -2150 -1952 -188 C
ATOM 629 CG LEU A 95 21.494 41.267 41.354 1.00 94.59 C
ANISOU 629 CG LEU A 95 13481 13897 8561 -2470 -1979 -301 C
ATOM 630 CD1 LEU A 95 22.085 39.874 41.217 1.00 94.55 C
ANISOU 630 CD1 LEU A 95 13332 14019 8574 -2475 -1763 -716 C
ATOM 631 CD2 LEU A 95 20.116 41.328 40.720 1.00103.75 C
ANISOU 631 CD2 LEU A 95 14726 15010 9683 -2515 -2318 -81 C
ATOM 632 N GLN A 96 21.472 43.041 45.536 1.00102.39 N
ANISOU 632 N GLN A 96 14232 14149 10524 -1639 -1900 83 N
ATOM 633 CA GLN A 96 21.252 43.061 46.979 1.00 93.61 C
ANISOU 633 CA GLN A 96 13036 12802 9729 -1344 -1848 107 C
ATOM 634 C GLN A 96 20.460 44.295 47.393 1.00 97.32 C
ANISOU 634 C GLN A 96 13563 13082 10331 -1248 -1998 400 C
ATOM 635 O GLN A 96 19.500 44.200 48.166 1.00101.97 O
ANISOU 635 O GLN A 96 14075 13486 11182 -1041 -2029 473 O
ATOM 636 CB GLN A 96 22.592 43.016 47.709 1.00106.27 C
ANISOU 636 CB GLN A 96 14625 14391 11362 -1293 -1660 -71 C
ATOM 637 CG GLN A 96 23.514 41.884 47.294 1.00107.38 C
ANISOU 637 CG GLN A 96 14674 14690 11435 -1394 -1511 -391 C
ATOM 638 CD GLN A 96 24.898 42.022 47.902 1.00112.29 C
ANISOU 638 CD GLN A 96 15267 15271 12126 -1372 -1369 -549 C
ATOM 639 OE1 GLN A 96 25.046 42.131 49.120 1.00 94.96 O
ANISOU 639 OE1 GLN A 96 13068 12878 10133 -1165 -1371 -526 O
ATOM 640 NE2 GLN A 96 25.921 42.021 47.053 1.00100.81 N
ANISOU 640 NE2 GLN A 96 13798 13996 10508 -1596 -1244 -716 N
ATOM 641 N LEU A 97 20.859 45.465 46.887 1.00 97.35 N
ANISOU 641 N LEU A 97 13691 13117 10178 -1404 -2080 563 N
ATOM 642 CA LEU A 97 20.129 46.698 47.166 1.00 98.65 C
ANISOU 642 CA LEU A 97 13898 13086 10499 -1330 -2256 838 C
ATOM 643 C LEU A 97 18.664 46.576 46.770 1.00112.50 C
ANISOU 643 C LEU A 97 15589 14750 12404 -1299 -2473 987 C
ATOM 644 O LEU A 97 17.766 46.966 47.525 1.00116.99 O
ANISOU 644 O LEU A 97 16073 15089 13291 -1097 -2528 1091 O
ATOM 645 CB LEU A 97 20.784 47.867 46.428 1.00 96.96 C
ANISOU 645 CB LEU A 97 13834 12940 10068 -1561 -2350 1004 C
ATOM 646 CG LEU A 97 21.374 48.994 47.274 1.00 94.52 C
ANISOU 646 CG LEU A 97 13560 12466 9885 -1462 -2317 1084 C
ATOM 647 CD1 LEU A 97 21.652 50.208 46.407 1.00103.66 C
ANISOU 647 CD1 LEU A 97 14858 13652 10877 -1704 -2486 1326 C
ATOM 648 CD2 LEU A 97 20.426 49.355 48.403 1.00101.37 C
ANISOU 648 CD2 LEU A 97 14349 13060 11109 -1171 -2365 1157 C
ATOM 649 N GLN A 98 18.406 46.029 45.581 1.00115.96 N
ANISOU 649 N GLN A 98 16065 15359 12634 -1504 -2597 981 N
ATOM 650 CA GLN A 98 17.035 45.901 45.101 1.00119.32 C
ANISOU 650 CA GLN A 98 16431 15686 13218 -1495 -2858 1124 C
ATOM 651 C GLN A 98 16.255 44.884 45.926 1.00121.55 C
ANISOU 651 C GLN A 98 16512 15848 13824 -1249 -2753 991 C
ATOM 652 O GLN A 98 15.068 45.087 46.209 1.00125.18 O
ANISOU 652 O GLN A 98 16851 16096 14617 -1115 -2891 1121 O
ATOM 653 CB GLN A 98 17.045 45.517 43.623 1.00119.61 C
ANISOU 653 CB GLN A 98 16599 15946 12901 -1796 -3025 1129 C
ATOM 654 CG GLN A 98 15.690 45.450 42.955 1.00117.18 C
ANISOU 654 CG GLN A 98 16262 15532 12730 -1832 -3373 1297 C
ATOM 655 CD GLN A 98 15.807 45.106 41.484 1.00132.45 C
ANISOU 655 CD GLN A 98 18390 17700 14236 -2160 -3548 1292 C
ATOM 656 OE1 GLN A 98 16.886 45.208 40.898 1.00127.19 O
ANISOU 656 OE1 GLN A 98 17903 17267 13156 -2391 -3408 1214 O
ATOM 657 NE2 GLN A 98 14.699 44.699 40.877 1.00150.09 N
ANISOU 657 NE2 GLN A 98 20593 19865 16570 -2192 -3848 1366 N
ATOM 658 N ALA A 99 16.907 43.790 46.328 1.00119.73 N
ANISOU 658 N ALA A 99 16230 15728 13532 -1194 -2510 733 N
ATOM 659 CA ALA A 99 16.248 42.783 47.153 1.00117.67 C
ANISOU 659 CA ALA A 99 15797 15349 13562 -981 -2398 620 C
ATOM 660 C ALA A 99 15.841 43.328 48.514 1.00100.88 C
ANISOU 660 C ALA A 99 13611 12978 11742 -735 -2280 698 C
ATOM 661 O ALA A 99 14.949 42.762 49.156 1.00102.21 O
ANISOU 661 O ALA A 99 13639 13000 12197 -573 -2217 682 O
ATOM 662 CB ALA A 99 17.160 41.569 47.336 1.00109.71 C
ANISOU 662 CB ALA A 99 14760 14486 12437 -984 -2190 339 C
ATOM 663 N LEU A 100 16.471 44.409 48.968 1.00 96.11 N
ANISOU 663 N LEU A 100 13114 12321 11083 -714 -2236 770 N
ATOM 664 CA LEU A 100 16.155 45.019 50.250 1.00102.92 C
ANISOU 664 CA LEU A 100 13954 12956 12196 -496 -2116 817 C
ATOM 665 C LEU A 100 15.245 46.234 50.119 1.00109.03 C
ANISOU 665 C LEU A 100 14691 13541 13195 -466 -2301 1035 C
ATOM 666 O LEU A 100 14.771 46.745 51.139 1.00111.96 O
ANISOU 666 O LEU A 100 15013 13701 13824 -281 -2194 1055 O
ATOM 667 CB LEU A 100 17.452 45.414 50.970 1.00106.75 C
ANISOU 667 CB LEU A 100 14574 13464 12521 -467 -1961 728 C
ATOM 668 CG LEU A 100 17.425 45.574 52.489 1.00 92.02 C
ANISOU 668 CG LEU A 100 12735 11408 10820 -243 -1770 676 C
ATOM 669 CD1 LEU A 100 17.131 44.236 53.148 1.00 92.61 C
ANISOU 669 CD1 LEU A 100 12745 11468 10976 -139 -1606 539 C
ATOM 670 CD2 LEU A 100 18.745 46.143 52.983 1.00 90.43 C
ANISOU 670 CD2 LEU A 100 12683 11222 10456 -250 -1710 614 C
ATOM 671 N GLN A 101 14.982 46.696 48.895 1.00126.82 N
ANISOU 671 N GLN A 101 16971 15851 15363 -653 -2583 1192 N
ATOM 672 CA GLN A 101 14.164 47.876 48.637 1.00123.76 C
ANISOU 672 CA GLN A 101 16545 15262 15216 -652 -2835 1419 C
ATOM 673 C GLN A 101 12.718 47.522 48.301 1.00123.87 C
ANISOU 673 C GLN A 101 16368 15127 15569 -605 -3018 1495 C
ATOM 674 O GLN A 101 12.055 48.261 47.565 1.00142.11 O
ANISOU 674 O GLN A 101 18655 17317 18022 -692 -3349 1697 O
ATOM 675 CB GLN A 101 14.776 48.701 47.505 1.00114.54 C
ANISOU 675 CB GLN A 101 15554 14215 13752 -911 -3082 1588 C
ATOM 676 CG GLN A 101 15.923 49.599 47.924 1.00119.31 C
ANISOU 676 CG GLN A 101 16296 14837 14200 -931 -2973 1595 C
ATOM 677 CD GLN A 101 16.351 50.540 46.816 1.00116.91 C
ANISOU 677 CD GLN A 101 16155 14605 13658 -1200 -3231 1811 C
ATOM 678 OE1 GLN A 101 15.743 50.575 45.745 1.00117.04 O
ANISOU 678 OE1 GLN A 101 16209 14648 13614 -1375 -3518 1972 O
ATOM 679 NE2 GLN A 101 17.411 51.301 47.062 1.00112.85 N
ANISOU 679 NE2 GLN A 101 15754 14117 13005 -1250 -3144 1825 N
ATOM 680 N GLN A 102 12.216 46.408 48.825 1.00126.61 N
ANISOU 680 N GLN A 102 16573 15457 16075 -476 -2832 1346 N
ATOM 681 CA GLN A 102 10.878 45.929 48.495 1.00138.70 C
ANISOU 681 CA GLN A 102 17895 16847 17956 -437 -2992 1394 C
ATOM 682 C GLN A 102 9.874 46.580 49.439 1.00144.23 C
ANISOU 682 C GLN A 102 18398 17229 19174 -222 -2911 1438 C
ATOM 683 O GLN A 102 9.827 46.251 50.630 1.00133.32 O
ANISOU 683 O GLN A 102 16958 15776 17921 -46 -2562 1302 O
ATOM 684 CB GLN A 102 10.814 44.407 48.583 1.00126.91 C
ANISOU 684 CB GLN A 102 16327 15476 16417 -414 -2828 1214 C
ATOM 685 CG GLN A 102 11.792 43.699 47.662 1.00136.69 C
ANISOU 685 CG GLN A 102 17731 17020 17186 -619 -2879 1115 C
ATOM 686 CD GLN A 102 11.485 43.921 46.192 1.00162.53 C
ANISOU 686 CD GLN A 102 21077 20370 20308 -848 -3268 1250 C
ATOM 687 OE1 GLN A 102 10.327 44.076 45.802 1.00156.11 O
ANISOU 687 OE1 GLN A 102 20132 19378 19805 -838 -3535 1383 O
ATOM 688 NE2 GLN A 102 12.526 43.937 45.367 1.00158.86 N
ANISOU 688 NE2 GLN A 102 20828 20162 19368 -1070 -3303 1212 N
ATOM 689 N ASN A 103 9.074 47.508 48.904 1.00150.70 N
ANISOU 689 N ASN A 103 19120 17843 20294 -249 -3235 1622 N
ATOM 690 CA ASN A 103 8.034 48.148 49.702 1.00141.04 C
ANISOU 690 CA ASN A 103 17659 16287 19642 -51 -3170 1638 C
ATOM 691 C ASN A 103 7.038 47.124 50.226 1.00137.42 C
ANISOU 691 C ASN A 103 16949 15719 19545 83 -2966 1516 C
ATOM 692 O ASN A 103 6.684 47.131 51.410 1.00136.39 O
ANISOU 692 O ASN A 103 16704 15443 19677 266 -2609 1396 O
ATOM 693 CB ASN A 103 7.310 49.206 48.874 1.00143.58 C
ANISOU 693 CB ASN A 103 17890 16384 20279 -123 -3632 1862 C
ATOM 694 CG ASN A 103 8.256 50.162 48.187 1.00155.75 C
ANISOU 694 CG ASN A 103 19696 18038 21443 -305 -3878 2025 C
ATOM 695 OD1 ASN A 103 9.469 50.119 48.392 1.00162.90 O
ANISOU 695 OD1 ASN A 103 20828 19177 21889 -362 -3673 1953 O
ATOM 696 ND2 ASN A 103 7.696 51.042 47.373 1.00165.43 N
ANISOU 696 ND2 ASN A 103 20887 19076 22894 -406 -4335 2254 N
ATOM 697 N GLY A 104 6.565 46.242 49.349 1.00124.14 N
ANISOU 697 N GLY A 104 15189 14101 17879 -19 -3184 1542 N
ATOM 698 CA GLY A 104 5.623 45.223 49.774 1.00115.56 C
ANISOU 698 CA GLY A 104 13849 12904 17156 91 -3011 1438 C
ATOM 699 C GLY A 104 4.281 45.831 50.124 1.00127.49 C
ANISOU 699 C GLY A 104 15032 14042 19368 230 -3055 1485 C
ATOM 700 O GLY A 104 3.834 46.813 49.519 1.00139.19 O
ANISOU 700 O GLY A 104 16442 15339 21104 193 -3426 1639 O
ATOM 701 N SER A 105 3.625 45.239 51.124 1.00122.95 N
ANISOU 701 N SER A 105 14247 13337 19132 384 -2670 1348 N
ATOM 702 CA SER A 105 2.347 45.758 51.598 1.00140.61 C
ANISOU 702 CA SER A 105 16131 15207 22086 527 -2609 1338 C
ATOM 703 C SER A 105 2.471 47.156 52.194 1.00147.82 C
ANISOU 703 C SER A 105 17065 15955 23146 622 -2526 1340 C
ATOM 704 O SER A 105 1.456 47.846 52.341 1.00141.70 O
ANISOU 704 O SER A 105 15989 14848 23005 720 -2589 1346 O
ATOM 705 CB SER A 105 1.750 44.800 52.631 1.00131.71 C
ANISOU 705 CB SER A 105 14817 14010 21215 644 -2124 1177 C
ATOM 706 OG SER A 105 0.517 45.284 53.131 1.00131.42 O
ANISOU 706 OG SER A 105 14414 13616 21902 775 -1997 1133 O
ATOM 707 N SER A 106 3.689 47.586 52.538 1.00150.85 N
ANISOU 707 N SER A 106 17776 16541 22999 598 -2397 1320 N
ATOM 708 CA SER A 106 3.880 48.907 53.131 1.00143.28 C
ANISOU 708 CA SER A 106 16854 15427 22160 689 -2323 1306 C
ATOM 709 C SER A 106 3.513 50.023 52.163 1.00150.34 C
ANISOU 709 C SER A 106 17651 16124 23349 625 -2852 1500 C
ATOM 710 O SER A 106 3.107 51.108 52.596 1.00158.03 O
ANISOU 710 O SER A 106 18482 16823 24737 734 -2848 1482 O
ATOM 711 CB SER A 106 5.328 49.069 53.594 1.00140.45 C
ANISOU 711 CB SER A 106 16873 15328 21163 657 -2136 1257 C
ATOM 712 OG SER A 106 5.757 47.937 54.331 1.00152.27 O
ANISOU 712 OG SER A 106 18494 17015 22348 682 -1748 1113 O
ATOM 713 N VAL A 107 3.640 49.781 50.857 1.00141.37 N
ANISOU 713 N VAL A 107 16600 15107 22007 439 -3320 1682 N
ATOM 714 CA VAL A 107 3.271 50.768 49.852 1.00130.60 C
ANISOU 714 CA VAL A 107 15185 13550 20887 340 -3885 1908 C
ATOM 715 C VAL A 107 1.807 51.172 49.949 1.00128.94 C
ANISOU 715 C VAL A 107 14545 12906 21543 470 -4036 1911 C
ATOM 716 O VAL A 107 1.395 52.157 49.327 1.00132.44 O
ANISOU 716 O VAL A 107 14896 13096 22329 426 -4502 2087 O
ATOM 717 CB VAL A 107 3.586 50.227 48.438 1.00132.76 C
ANISOU 717 CB VAL A 107 15655 14047 20739 92 -4329 2084 C
ATOM 718 CG1 VAL A 107 2.463 49.311 47.945 1.00128.77 C
ANISOU 718 CG1 VAL A 107 14890 13422 20614 88 -4515 2083 C
ATOM 719 CG2 VAL A 107 3.847 51.373 47.469 1.00141.79 C
ANISOU 719 CG2 VAL A 107 16960 15122 21791 -80 -4857 2346 C
ATOM 720 N LEU A 108 1.016 50.437 50.720 1.00129.73 N
ANISOU 720 N LEU A 108 14369 12895 22029 618 -3656 1723 N
ATOM 721 CA LEU A 108 -0.404 50.686 50.905 1.00139.68 C
ANISOU 721 CA LEU A 108 15166 13735 24171 750 -3713 1677 C
ATOM 722 C LEU A 108 -0.635 51.514 52.164 1.00138.94 C
ANISOU 722 C LEU A 108 14910 13415 24465 949 -3272 1481 C
ATOM 723 O LEU A 108 0.208 51.566 53.063 1.00143.96 O
ANISOU 723 O LEU A 108 15792 14246 24661 1000 -2829 1347 O
ATOM 724 CB LEU A 108 -1.159 49.360 51.006 1.00136.74 C
ANISOU 724 CB LEU A 108 14569 13369 24019 777 -3518 1575 C
ATOM 725 CG LEU A 108 -1.657 48.769 49.688 1.00132.16 C
ANISOU 725 CG LEU A 108 13920 12770 23525 629 -4088 1749 C
ATOM 726 CD1 LEU A 108 -2.526 47.551 49.946 1.00129.82 C
ANISOU 726 CD1 LEU A 108 13330 12407 23590 688 -3861 1623 C
ATOM 727 CD2 LEU A 108 -2.416 49.816 48.885 1.00139.28 C
ANISOU 727 CD2 LEU A 108 14615 13301 25004 600 -4710 1935 C
ATOM 728 N SER A 109 -1.792 52.169 52.217 1.00136.19 N
ANISOU 728 N SER A 109 14143 12636 24969 1058 -3410 1452 N
ATOM 729 CA SER A 109 -2.196 52.844 53.440 1.00137.02 C
ANISOU 729 CA SER A 109 14031 12495 25536 1254 -2931 1206 C
ATOM 730 C SER A 109 -2.264 51.839 54.584 1.00143.36 C
ANISOU 730 C SER A 109 14833 13451 26188 1336 -2205 959 C
ATOM 731 O SER A 109 -2.595 50.666 54.386 1.00141.75 O
ANISOU 731 O SER A 109 14560 13356 25942 1286 -2134 968 O
ATOM 732 CB SER A 109 -3.551 53.525 53.255 1.00149.58 C
ANISOU 732 CB SER A 109 15095 13570 28170 1355 -3188 1183 C
ATOM 733 OG SER A 109 -4.614 52.623 53.512 1.00147.01 O
ANISOU 733 OG SER A 109 14398 13100 28360 1418 -2933 1049 O
ATOM 734 N GLU A 110 -1.923 52.304 55.790 1.00168.01 N
ANISOU 734 N GLU A 110 21500 15278 27057 2011 -492 -3839 N
ATOM 735 CA GLU A 110 -1.960 51.425 56.957 1.00166.34 C
ANISOU 735 CA GLU A 110 21204 15703 26295 1978 -302 -4313 C
ATOM 736 C GLU A 110 -3.331 50.781 57.109 1.00157.71 C
ANISOU 736 C GLU A 110 19945 14972 25007 2303 -146 -4447 C
ATOM 737 O GLU A 110 -3.437 49.572 57.336 1.00147.90 O
ANISOU 737 O GLU A 110 18670 14355 23172 2237 -12 -4379 O
ATOM 738 CB GLU A 110 -1.589 52.197 58.222 1.00164.44 C
ANISOU 738 CB GLU A 110 20999 15269 26211 1888 -280 -5026 C
ATOM 739 CG GLU A 110 -0.175 52.741 58.247 1.00169.27 C
ANISOU 739 CG GLU A 110 21731 15601 26985 1518 -423 -4996 C
ATOM 740 CD GLU A 110 0.210 53.256 59.617 1.00190.07 C
ANISOU 740 CD GLU A 110 24395 18202 29622 1409 -412 -5753 C
ATOM 741 OE1 GLU A 110 -0.400 52.807 60.611 1.00189.35 O
ANISOU 741 OE1 GLU A 110 24272 18535 29136 1526 -259 -6232 O
ATOM 742 OE2 GLU A 110 1.112 54.115 59.701 1.00198.61 O1-
ANISOU 742 OE2 GLU A 110 25539 18843 31080 1175 -546 -5883 O1-
ATOM 743 N ASP A 111 -4.394 51.576 56.961 1.00143.23 N
ANISOU 743 N ASP A 111 17988 12720 23711 2654 -181 -4644 N
ATOM 744 CA ASP A 111 -5.750 51.045 57.071 1.00138.06 C
ANISOU 744 CA ASP A 111 17096 12392 22969 2965 -24 -4837 C
ATOM 745 C ASP A 111 -5.985 49.906 56.083 1.00138.41 C
ANISOU 745 C ASP A 111 17108 12851 22631 2965 -42 -4203 C
ATOM 746 O ASP A 111 -6.605 48.892 56.427 1.00128.73 O
ANISOU 746 O ASP A 111 15750 12196 20967 2989 167 -4320 O
ATOM 747 CB ASP A 111 -6.764 52.165 56.844 1.00129.80 C
ANISOU 747 CB ASP A 111 15880 10733 22706 3382 -157 -5099 C
ATOM 748 CG ASP A 111 -6.665 53.258 57.887 1.00160.50 C
ANISOU 748 CG ASP A 111 19761 14254 26969 3401 -112 -5813 C
ATOM 749 OD1 ASP A 111 -5.706 53.230 58.688 1.00165.67 O
ANISOU 749 OD1 ASP A 111 20575 15034 27339 3089 -20 -6089 O
ATOM 750 OD2 ASP A 111 -7.541 54.149 57.901 1.00169.27 O1-
ANISOU 750 OD2 ASP A 111 20717 15092 28505 3653 -192 -5982 O1-
ATOM 751 N LYS A 112 -5.494 50.056 54.851 1.00136.96 N
ANISOU 751 N LYS A 112 17059 12391 22588 2902 -276 -3541 N
ATOM 752 CA LYS A 112 -5.648 49.010 53.845 1.00122.69 C
ANISOU 752 CA LYS A 112 15233 10971 20411 2884 -305 -2962 C
ATOM 753 C LYS A 112 -4.701 47.842 54.099 1.00126.87 C
ANISOU 753 C LYS A 112 15842 12076 20286 2542 -172 -2834 C
ATOM 754 O LYS A 112 -5.125 46.681 54.097 1.00124.03 O
ANISOU 754 O LYS A 112 15390 12242 19494 2557 -55 -2763 O
ATOM 755 CB LYS A 112 -5.420 49.592 52.449 1.00124.18 C
ANISOU 755 CB LYS A 112 15579 10697 20907 2887 -587 -2320 C
ATOM 756 CG LYS A 112 -6.485 50.585 52.028 1.00126.59 C
ANISOU 756 CG LYS A 112 15820 10422 21857 3288 -830 -2339 C
ATOM 757 CD LYS A 112 -6.254 51.081 50.613 1.00129.01 C
ANISOU 757 CD LYS A 112 16374 10292 22353 3241 -1149 -1610 C
ATOM 758 CE LYS A 112 -7.447 51.881 50.117 1.00134.25 C
ANISOU 758 CE LYS A 112 16972 10414 23624 3704 -1490 -1572 C
ATOM 759 NZ LYS A 112 -7.267 52.330 48.709 1.00127.74 N
ANISOU 759 NZ LYS A 112 16470 9169 22897 3633 -1852 -790 N
ATOM 760 N SER A 113 -3.414 48.132 54.317 1.00138.74 N
ANISOU 760 N SER A 113 17501 13460 21754 2235 -214 -2823 N
ATOM 761 CA SER A 113 -2.461 47.075 54.641 1.00133.96 C
ANISOU 761 CA SER A 113 16936 13352 20609 1952 -156 -2775 C
ATOM 762 C SER A 113 -2.868 46.321 55.900 1.00116.02 C
ANISOU 762 C SER A 113 14635 11534 17912 1970 2 -3231 C
ATOM 763 O SER A 113 -2.490 45.157 56.076 1.00 99.25 O
ANISOU 763 O SER A 113 12543 9873 15294 1828 18 -3121 O
ATOM 764 CB SER A 113 -1.057 47.664 54.798 1.00135.99 C
ANISOU 764 CB SER A 113 17299 13369 21002 1639 -247 -2816 C
ATOM 765 OG SER A 113 -0.884 48.249 56.077 1.00132.61 O
ANISOU 765 OG SER A 113 16909 12819 20659 1604 -226 -3406 O
ATOM 766 N LYS A 114 -3.639 46.962 56.782 1.00111.68 N
ANISOU 766 N LYS A 114 14038 10850 17543 2126 118 -3754 N
ATOM 767 CA LYS A 114 -4.186 46.263 57.938 1.00117.85 C
ANISOU 767 CA LYS A 114 14816 12099 17864 2100 328 -4181 C
ATOM 768 C LYS A 114 -5.408 45.429 57.575 1.00114.74 C
ANISOU 768 C LYS A 114 14256 12036 17304 2273 484 -4050 C
ATOM 769 O LYS A 114 -5.668 44.411 58.225 1.00116.75 O
ANISOU 769 O LYS A 114 14557 12778 17025 2142 644 -4155 O
ATOM 770 CB LYS A 114 -4.532 47.261 59.046 1.00121.15 C
ANISOU 770 CB LYS A 114 15221 12306 18503 2159 451 -4877 C
ATOM 771 CG LYS A 114 -3.341 47.646 59.918 1.00134.00 C
ANISOU 771 CG LYS A 114 17046 13866 20001 1891 346 -5168 C
ATOM 772 CD LYS A 114 -3.495 49.037 60.521 1.00144.70 C
ANISOU 772 CD LYS A 114 18369 14749 21860 1987 371 -5756 C
ATOM 773 CE LYS A 114 -4.779 49.169 61.322 1.00137.29 C
ANISOU 773 CE LYS A 114 17285 13985 20892 2170 671 -6360 C
ATOM 774 NZ LYS A 114 -4.925 50.539 61.891 1.00121.19 N
ANISOU 774 NZ LYS A 114 15185 11458 19406 2294 685 -7004 N
ATOM 775 N ARG A 115 -6.168 45.831 56.550 1.00121.44 N
ANISOU 775 N ARG A 115 14928 12618 18597 2547 414 -3814 N
ATOM 776 CA ARG A 115 -7.282 44.999 56.103 1.00120.07 C
ANISOU 776 CA ARG A 115 14559 12768 18295 2702 521 -3679 C
ATOM 777 C ARG A 115 -6.793 43.794 55.312 1.00113.23 C
ANISOU 777 C ARG A 115 13775 12230 17018 2547 430 -3116 C
ATOM 778 O ARG A 115 -7.242 42.666 55.547 1.00107.48 O
ANISOU 778 O ARG A 115 13008 11953 15875 2470 572 -3108 O
ATOM 779 CB ARG A 115 -8.273 45.802 55.264 1.00112.69 C
ANISOU 779 CB ARG A 115 13396 11442 17981 3075 397 -3629 C
ATOM 780 CG ARG A 115 -9.428 44.929 54.799 1.00 98.85 C
ANISOU 780 CG ARG A 115 11391 10047 16120 3230 482 -3533 C
ATOM 781 CD ARG A 115 -10.563 44.896 55.806 1.00113.51 C
ANISOU 781 CD ARG A 115 12976 12143 18008 3327 804 -4196 C
ATOM 782 NE ARG A 115 -11.222 43.593 55.822 1.00124.49 N
ANISOU 782 NE ARG A 115 14240 14097 18962 3213 1010 -4134 N
ATOM 783 CZ ARG A 115 -12.373 43.316 55.226 1.00132.09 C
ANISOU 783 CZ ARG A 115 14865 15168 20154 3439 1016 -4133 C
ATOM 784 NH1 ARG A 115 -13.031 44.231 54.532 1.00133.20 N
ANISOU 784 NH1 ARG A 115 14759 14893 20957 3835 778 -4169 N
ATOM 785 NH2 ARG A 115 -12.879 42.091 55.331 1.00113.06 N
ANISOU 785 NH2 ARG A 115 12367 13270 17322 3261 1228 -4095 N
ATOM 786 N LEU A 116 -5.888 44.016 54.352 1.00107.97 N
ANISOU 786 N LEU A 116 13215 11334 16472 2479 209 -2663 N
ATOM 787 CA LEU A 116 -5.347 42.907 53.569 1.00 97.30 C
ANISOU 787 CA LEU A 116 11911 10295 14763 2333 136 -2203 C
ATOM 788 C LEU A 116 -4.815 41.806 54.475 1.00106.66 C
ANISOU 788 C LEU A 116 13203 11902 15420 2105 213 -2343 C
ATOM 789 O LEU A 116 -5.072 40.619 54.242 1.00 99.69 O
ANISOU 789 O LEU A 116 12295 11375 14207 2068 240 -2163 O
ATOM 790 CB LEU A 116 -4.248 43.419 52.634 1.00 92.10 C
ANISOU 790 CB LEU A 116 11360 9357 14278 2200 -42 -1823 C
ATOM 791 CG LEU A 116 -3.479 42.393 51.797 1.00 98.91 C
ANISOU 791 CG LEU A 116 12240 10527 14814 2021 -97 -1430 C
ATOM 792 CD1 LEU A 116 -4.421 41.581 50.921 1.00 89.60 C
ANISOU 792 CD1 LEU A 116 10947 9602 13495 2176 -99 -1160 C
ATOM 793 CD2 LEU A 116 -2.427 43.088 50.948 1.00105.80 C
ANISOU 793 CD2 LEU A 116 13195 11120 15884 1835 -193 -1140 C
ATOM 794 N ASN A 117 -4.099 42.185 55.536 1.00123.46 N
ANISOU 794 N ASN A 117 15471 13969 17469 1951 213 -2672 N
ATOM 795 CA ASN A 117 -3.608 41.199 56.491 1.00120.77 C
ANISOU 795 CA ASN A 117 15290 13987 16608 1741 209 -2802 C
ATOM 796 C ASN A 117 -4.747 40.543 57.262 1.00115.54 C
ANISOU 796 C ASN A 117 14636 13650 15612 1744 439 -3030 C
ATOM 797 O ASN A 117 -4.632 39.378 57.656 1.00110.66 O
ANISOU 797 O ASN A 117 14160 13360 14524 1582 422 -2935 O
ATOM 798 CB ASN A 117 -2.617 41.852 57.455 1.00109.91 C
ANISOU 798 CB ASN A 117 14070 12465 15227 1580 111 -3128 C
ATOM 799 CG ASN A 117 -1.318 42.247 56.777 1.00123.92 C
ANISOU 799 CG ASN A 117 15821 14003 17258 1479 -102 -2913 C
ATOM 800 OD1 ASN A 117 -0.943 41.680 55.751 1.00122.71 O
ANISOU 800 OD1 ASN A 117 15586 13928 17112 1464 -179 -2521 O
ATOM 801 ND2 ASN A 117 -0.629 43.230 57.345 1.00136.67 N
ANISOU 801 ND2 ASN A 117 17491 15345 19092 1381 -173 -3209 N
ATOM 802 N THR A 118 -5.845 41.267 57.491 1.00105.70 N
ANISOU 802 N THR A 118 13234 12306 14622 1909 652 -3347 N
ATOM 803 CA THR A 118 -7.006 40.659 58.134 1.00 99.95 C
ANISOU 803 CA THR A 118 12444 11924 13609 1875 942 -3599 C
ATOM 804 C THR A 118 -7.652 39.626 57.220 1.00 99.89 C
ANISOU 804 C THR A 118 12291 12135 13527 1933 951 -3222 C
ATOM 805 O THR A 118 -7.969 38.511 57.650 1.00 96.50 O
ANISOU 805 O THR A 118 11957 12064 12646 1740 1071 -3188 O
ATOM 806 CB THR A 118 -8.020 41.735 58.525 1.00 95.12 C
ANISOU 806 CB THR A 118 11604 11149 13390 2070 1172 -4113 C
ATOM 807 OG1 THR A 118 -7.396 42.691 59.392 1.00116.39 O
ANISOU 807 OG1 THR A 118 14440 13627 16157 2005 1158 -4511 O
ATOM 808 CG2 THR A 118 -9.211 41.109 59.235 1.00 89.38 C
ANISOU 808 CG2 THR A 118 10762 10838 12362 1975 1545 -4448 C
ATOM 809 N ILE A 119 -7.853 39.987 55.949 1.00107.06 N
ANISOU 809 N ILE A 119 12998 12818 14861 2174 806 -2927 N
ATOM 810 CA ILE A 119 -8.443 39.063 54.983 1.00 93.51 C
ANISOU 810 CA ILE A 119 11134 11303 13093 2239 774 -2587 C
ATOM 811 C ILE A 119 -7.582 37.815 54.849 1.00 98.35 C
ANISOU 811 C ILE A 119 11952 12149 13268 2015 646 -2259 C
ATOM 812 O ILE A 119 -8.072 36.685 54.961 1.00 99.58 O
ANISOU 812 O ILE A 119 12113 12606 13118 1900 734 -2195 O
ATOM 813 CB ILE A 119 -8.625 39.759 53.624 1.00 91.76 C
ANISOU 813 CB ILE A 119 10742 10778 13345 2511 568 -2295 C
ATOM 814 CG1 ILE A 119 -9.650 40.886 53.729 1.00100.54 C
ANISOU 814 CG1 ILE A 119 11616 11622 14962 2795 628 -2632 C
ATOM 815 CG2 ILE A 119 -9.030 38.753 52.560 1.00 93.93 C
ANISOU 815 CG2 ILE A 119 10905 11285 13499 2546 484 -1928 C
ATOM 816 CD1 ILE A 119 -9.670 41.775 52.518 1.00105.59 C
ANISOU 816 CD1 ILE A 119 12200 11845 16074 3047 337 -2316 C
ATOM 817 N LEU A 120 -6.283 38.009 54.598 1.00102.43 N
ANISOU 817 N LEU A 120 12617 12506 13794 1946 429 -2074 N
ATOM 818 CA LEU A 120 -5.355 36.891 54.463 1.00 92.07 C
ANISOU 818 CA LEU A 120 11449 11372 12163 1778 260 -1830 C
ATOM 819 C LEU A 120 -5.446 35.950 55.657 1.00100.21 C
ANISOU 819 C LEU A 120 12698 12655 12723 1569 317 -1984 C
ATOM 820 O LEU A 120 -5.525 34.726 55.497 1.00 97.72 O
ANISOU 820 O LEU A 120 12440 12536 12150 1480 258 -1790 O
ATOM 821 CB LEU A 120 -3.928 37.422 54.309 1.00 82.71 C
ANISOU 821 CB LEU A 120 10340 9980 11105 1712 59 -1769 C
ATOM 822 CG LEU A 120 -3.582 38.173 53.022 1.00 90.00 C
ANISOU 822 CG LEU A 120 11127 10673 12396 1807 -12 -1516 C
ATOM 823 CD1 LEU A 120 -2.204 38.804 53.131 1.00 90.80 C
ANISOU 823 CD1 LEU A 120 11291 10576 12631 1664 -138 -1560 C
ATOM 824 CD2 LEU A 120 -3.652 37.244 51.823 1.00 95.81 C
ANISOU 824 CD2 LEU A 120 11758 11604 13041 1834 -70 -1176 C
ATOM 825 N ASN A 121 -5.446 36.511 56.868 1.00111.59 N
ANISOU 825 N ASN A 121 14292 14077 14029 1466 422 -2332 N
ATOM 826 CA ASN A 121 -5.539 35.686 58.067 1.00109.59 C
ANISOU 826 CA ASN A 121 14328 14070 13241 1210 473 -2457 C
ATOM 827 C ASN A 121 -6.917 35.049 58.192 1.00109.13 C
ANISOU 827 C ASN A 121 14191 14265 13010 1139 782 -2506 C
ATOM 828 O ASN A 121 -7.040 33.913 58.664 1.00109.49 O
ANISOU 828 O ASN A 121 14464 14517 12619 905 780 -2384 O
ATOM 829 CB ASN A 121 -5.215 36.524 59.303 1.00105.72 C
ANISOU 829 CB ASN A 121 14030 13531 12606 1094 524 -2858 C
ATOM 830 CG ASN A 121 -3.723 36.691 59.520 1.00118.66 C
ANISOU 830 CG ASN A 121 15839 15016 14231 1041 158 -2815 C
ATOM 831 OD1 ASN A 121 -2.957 35.732 59.423 1.00125.15 O
ANISOU 831 OD1 ASN A 121 16800 15897 14853 964 -134 -2557 O
ATOM 832 ND2 ASN A 121 -3.302 37.917 59.810 1.00127.93 N
ANISOU 832 ND2 ASN A 121 16971 15968 15667 1089 152 -3103 N
ATOM 833 N THR A 122 -7.964 35.764 57.775 1.00101.59 N
ANISOU 833 N THR A 122 12906 13274 12420 1330 1028 -2690 N
ATOM 834 CA THR A 122 -9.306 35.193 57.804 1.00 95.58 C
ANISOU 834 CA THR A 122 11968 12768 11580 1269 1332 -2788 C
ATOM 835 C THR A 122 -9.407 33.998 56.865 1.00 96.26 C
ANISOU 835 C THR A 122 12004 12953 11616 1260 1187 -2374 C
ATOM 836 O THR A 122 -9.962 32.953 57.224 1.00 96.32 O
ANISOU 836 O THR A 122 12104 13198 11294 1019 1328 -2333 O
ATOM 837 CB THR A 122 -10.340 36.254 57.429 1.00 84.70 C
ANISOU 837 CB THR A 122 10174 11285 10722 1551 1531 -3095 C
ATOM 838 OG1 THR A 122 -10.202 37.385 58.298 1.00104.86 O
ANISOU 838 OG1 THR A 122 12767 13703 13372 1575 1651 -3532 O
ATOM 839 CG2 THR A 122 -11.746 35.690 57.555 1.00 86.85 C
ANISOU 839 CG2 THR A 122 10191 11858 10950 1468 1871 -3296 C
ATOM 840 N MET A 123 -8.868 34.137 55.653 1.00100.10 N
ANISOU 840 N MET A 123 12359 13259 12414 1489 917 -2077 N
ATOM 841 CA MET A 123 -8.912 33.046 54.685 1.00 98.06 C
ANISOU 841 CA MET A 123 12035 13098 12124 1496 771 -1738 C
ATOM 842 C MET A 123 -8.089 31.857 55.164 1.00 98.78 C
ANISOU 842 C MET A 123 12465 13260 11807 1253 590 -1556 C
ATOM 843 O MET A 123 -8.531 30.705 55.077 1.00 95.32 O
ANISOU 843 O MET A 123 12070 12966 11181 1110 604 -1424 O
ATOM 844 CB MET A 123 -8.420 33.547 53.326 1.00 98.14 C
ANISOU 844 CB MET A 123 11872 12928 12490 1750 544 -1495 C
ATOM 845 CG MET A 123 -9.337 34.596 52.702 1.00 88.86 C
ANISOU 845 CG MET A 123 10394 11634 11736 2015 621 -1590 C
ATOM 846 SD MET A 123 -9.021 34.918 50.956 1.00 87.69 S
ANISOU 846 SD MET A 123 10109 11339 11868 2238 348 -1205 S
ATOM 847 CE MET A 123 -7.298 35.399 51.000 1.00 80.01 C
ANISOU 847 CE MET A 123 9383 10160 10858 2133 188 -1078 C
ATOM 848 N SER A 124 -6.884 32.120 55.681 1.00100.12 N
ANISOU 848 N SER A 124 12872 13298 11872 1207 382 -1558 N
ATOM 849 CA SER A 124 -6.060 31.047 56.230 1.00100.82 C
ANISOU 849 CA SER A 124 13291 13404 11612 1015 122 -1410 C
ATOM 850 C SER A 124 -6.781 30.325 57.360 1.00 99.32 C
ANISOU 850 C SER A 124 13392 13386 10959 705 293 -1475 C
ATOM 851 O SER A 124 -6.645 29.106 57.516 1.00100.77 O
ANISOU 851 O SER A 124 13812 13592 10886 536 120 -1261 O
ATOM 852 CB SER A 124 -4.727 31.611 56.721 1.00112.84 C
ANISOU 852 CB SER A 124 14975 14767 13133 1025 -140 -1485 C
ATOM 853 OG SER A 124 -3.952 30.612 57.359 1.00126.75 O
ANISOU 853 OG SER A 124 17064 16520 14577 870 -464 -1371 O
ATOM 854 N THR A 125 -7.560 31.061 58.154 1.00101.85 N
ANISOU 854 N THR A 125 13706 13819 11171 606 643 -1784 N
ATOM 855 CA THR A 125 -8.300 30.436 59.242 1.00109.19 C
ANISOU 855 CA THR A 125 14915 14968 11605 235 896 -1878 C
ATOM 856 C THR A 125 -9.445 29.575 58.723 1.00111.97 C
ANISOU 856 C THR A 125 15075 15477 11990 135 1124 -1778 C
ATOM 857 O THR A 125 -9.748 28.532 59.309 1.00117.10 O
ANISOU 857 O THR A 125 16032 16238 12225 -217 1177 -1646 O
ATOM 858 CB THR A 125 -8.829 31.510 60.195 1.00108.26 C
ANISOU 858 CB THR A 125 14780 14972 11384 150 1265 -2333 C
ATOM 859 OG1 THR A 125 -7.732 32.280 60.702 1.00117.78 O
ANISOU 859 OG1 THR A 125 16176 16019 12556 217 1024 -2445 O
ATOM 860 CG2 THR A 125 -9.575 30.879 61.361 1.00 97.73 C
ANISOU 860 CG2 THR A 125 13759 13924 9451 -313 1592 -2456 C
ATOM 861 N ILE A 126 -10.077 29.978 57.620 1.00105.54 N
ANISOU 861 N ILE A 126 13781 14657 11663 421 1226 -1822 N
ATOM 862 CA ILE A 126 -11.259 29.265 57.142 1.00101.51 C
ANISOU 862 CA ILE A 126 13020 14318 11229 333 1449 -1807 C
ATOM 863 C ILE A 126 -10.867 27.923 56.532 1.00 98.52 C
ANISOU 863 C ILE A 126 12791 13871 10772 260 1146 -1422 C
ATOM 864 O ILE A 126 -11.496 26.895 56.803 1.00 95.89 O
ANISOU 864 O ILE A 126 12576 13650 10208 -50 1273 -1344 O
ATOM 865 CB ILE A 126 -12.042 30.139 56.147 1.00 92.89 C
ANISOU 865 CB ILE A 126 11378 13225 10691 692 1562 -1980 C
ATOM 866 CG1 ILE A 126 -12.665 31.331 56.876 1.00 99.83 C
ANISOU 866 CG1 ILE A 126 12078 14164 11689 738 1900 -2446 C
ATOM 867 CG2 ILE A 126 -13.120 29.322 55.455 1.00 88.09 C
ANISOU 867 CG2 ILE A 126 10472 12781 10217 643 1678 -1940 C
ATOM 868 CD1 ILE A 126 -13.432 32.267 55.972 1.00108.51 C
ANISOU 868 CD1 ILE A 126 12653 15188 13387 1133 1930 -2629 C
ATOM 869 N TYR A 127 -9.829 27.914 55.693 1.00 93.06 N
ANISOU 869 N TYR A 127 12082 12988 10290 523 759 -1208 N
ATOM 870 CA TYR A 127 -9.334 26.665 55.120 1.00 87.51 C
ANISOU 870 CA TYR A 127 11500 12194 9557 491 444 -918 C
ATOM 871 C TYR A 127 -8.866 25.702 56.207 1.00 96.81 C
ANISOU 871 C TYR A 127 13200 13294 10289 160 278 -770 C
ATOM 872 O TYR A 127 -9.366 24.577 56.321 1.00 93.83 O
ANISOU 872 O TYR A 127 12978 12926 9746 -94 288 -628 O
ATOM 873 CB TYR A 127 -8.200 26.969 54.138 1.00 83.10 C
ANISOU 873 CB TYR A 127 10808 11481 9287 809 112 -807 C
ATOM 874 CG TYR A 127 -7.623 25.768 53.419 1.00 77.78 C
ANISOU 874 CG TYR A 127 10170 10719 8665 838 -210 -605 C
ATOM 875 CD1 TYR A 127 -8.191 25.293 52.246 1.00 77.63 C
ANISOU 875 CD1 TYR A 127 9856 10782 8857 941 -190 -557 C
ATOM 876 CD2 TYR A 127 -6.479 25.136 53.895 1.00 98.96 C
ANISOU 876 CD2 TYR A 127 13159 13223 11218 788 -571 -504 C
ATOM 877 CE1 TYR A 127 -7.653 24.206 51.584 1.00 82.52 C
ANISOU 877 CE1 TYR A 127 10490 11319 9546 974 -473 -444 C
ATOM 878 CE2 TYR A 127 -5.935 24.049 53.236 1.00 89.45 C
ANISOU 878 CE2 TYR A 127 11946 11906 10137 853 -884 -390 C
ATOM 879 CZ TYR A 127 -6.528 23.589 52.080 1.00 75.60 C
ANISOU 879 CZ TYR A 127 9895 10244 8585 939 -809 -376 C
ATOM 880 OH TYR A 127 -6.001 22.510 51.408 1.00 75.62 O
ANISOU 880 OH TYR A 127 9866 10137 8729 1008 -1103 -331 O
ATOM 881 N SER A 128 -7.903 26.138 57.024 1.00116.65 N
ANISOU 881 N SER A 128 16012 15705 12605 145 87 -792 N
ATOM 882 CA SER A 128 -7.268 25.248 57.991 1.00114.95 C
ANISOU 882 CA SER A 128 16339 15363 11974 -117 -220 -606 C
ATOM 883 C SER A 128 -8.207 24.813 59.110 1.00119.62 C
ANISOU 883 C SER A 128 17287 16111 12053 -588 92 -606 C
ATOM 884 O SER A 128 -7.949 23.788 59.750 1.00131.62 O
ANISOU 884 O SER A 128 19297 17504 13208 -872 -162 -352 O
ATOM 885 CB SER A 128 -6.027 25.924 58.577 1.00118.63 C
ANISOU 885 CB SER A 128 16995 15707 12370 -3 -527 -676 C
ATOM 886 OG SER A 128 -6.371 27.114 59.265 1.00122.25 O
ANISOU 886 OG SER A 128 17429 16316 12704 -57 -194 -964 O
ATOM 887 N THR A 129 -9.282 25.560 59.368 1.00112.36 N
ANISOU 887 N THR A 129 16138 15453 11101 -693 628 -895 N
ATOM 888 CA THR A 129 -10.280 25.164 60.354 1.00107.84 C
ANISOU 888 CA THR A 129 15822 15101 10050 -1194 1038 -963 C
ATOM 889 C THR A 129 -11.599 24.735 59.727 1.00114.82 C
ANISOU 889 C THR A 129 16314 16157 11156 -1301 1428 -1037 C
ATOM 890 O THR A 129 -12.542 24.419 60.462 1.00112.61 O
ANISOU 890 O THR A 129 16154 16101 10530 -1756 1856 -1145 O
ATOM 891 CB THR A 129 -10.540 26.302 61.351 1.00123.10 C
ANISOU 891 CB THR A 129 17791 17257 11726 -1310 1411 -1354 C
ATOM 892 OG1 THR A 129 -11.243 27.368 60.699 1.00105.03 O
ANISOU 892 OG1 THR A 129 14876 15087 9944 -995 1749 -1720 O
ATOM 893 CG2 THR A 129 -9.230 26.831 61.919 1.00141.96 C
ANISOU 893 CG2 THR A 129 20509 19481 13947 -1180 1005 -1335 C
ATOM 894 N GLY A 130 -11.690 24.707 58.399 1.00123.73 N
ANISOU 894 N GLY A 130 16977 17208 12827 -930 1297 -1000 N
ATOM 895 CA GLY A 130 -12.948 24.405 57.741 1.00120.04 C
ANISOU 895 CA GLY A 130 16072 16915 12622 -984 1619 -1121 C
ATOM 896 C GLY A 130 -13.347 22.961 57.950 1.00115.60 C
ANISOU 896 C GLY A 130 15803 16316 11804 -1427 1618 -872 C
ATOM 897 O GLY A 130 -12.584 22.042 57.605 1.00117.10 O
ANISOU 897 O GLY A 130 16265 16231 11998 -1390 1163 -541 O
ATOM 898 N LYS A 131 -14.535 22.738 58.503 1.00119.01 N
ANISOU 898 N LYS A 131 16167 17005 12045 -1860 2124 -1055 N
ATOM 899 CA LYS A 131 -15.023 21.403 58.808 1.00128.05 C
ANISOU 899 CA LYS A 131 17622 18113 12919 -2387 2197 -824 C
ATOM 900 C LYS A 131 -16.352 21.143 58.112 1.00134.01 C
ANISOU 900 C LYS A 131 17795 19084 14039 -2477 2563 -1057 C
ATOM 901 O LYS A 131 -17.158 22.056 57.908 1.00138.57 O
ANISOU 901 O LYS A 131 17807 19940 14902 -2306 2931 -1478 O
ATOM 902 CB LYS A 131 -15.162 21.204 60.324 1.00142.04 C
ANISOU 902 CB LYS A 131 19986 20006 13976 -3008 2490 -784 C
ATOM 903 CG LYS A 131 -16.106 22.162 61.029 1.00146.36 C
ANISOU 903 CG LYS A 131 20246 20987 14379 -3211 3169 -1289 C
ATOM 904 CD LYS A 131 -16.405 21.670 62.439 1.00155.13 C
ANISOU 904 CD LYS A 131 21974 22268 14701 -3973 3525 -1222 C
ATOM 905 CE LYS A 131 -15.267 21.993 63.399 1.00158.31 C
ANISOU 905 CE LYS A 131 23046 22550 14556 -4000 3203 -1044 C
ATOM 906 NZ LYS A 131 -15.288 23.403 63.872 1.00164.25 N
ANISOU 906 NZ LYS A 131 23544 23572 15293 -3793 3511 -1551 N
ATOM 907 N VAL A 132 -16.561 19.883 57.738 1.00142.83 N
ANISOU 907 N VAL A 132 19041 20039 15190 -2729 2416 -803 N
ATOM 908 CA VAL A 132 -17.767 19.433 57.052 1.00142.72 C
ANISOU 908 CA VAL A 132 18505 20194 15526 -2864 2691 -999 C
ATOM 909 C VAL A 132 -18.393 18.319 57.879 1.00151.25 C
ANISOU 909 C VAL A 132 19983 21281 16204 -3638 2987 -850 C
ATOM 910 O VAL A 132 -17.698 17.385 58.295 1.00160.27 O
ANISOU 910 O VAL A 132 21796 22083 17017 -3904 2651 -414 O
ATOM 911 CB VAL A 132 -17.461 18.952 55.621 1.00121.20 C
ANISOU 911 CB VAL A 132 15500 17257 13294 -2431 2216 -873 C
ATOM 912 CG1 VAL A 132 -18.550 18.013 55.117 1.00120.47 C
ANISOU 912 CG1 VAL A 132 15106 17238 13432 -2746 2391 -958 C
ATOM 913 CG2 VAL A 132 -17.301 20.141 54.687 1.00116.72 C
ANISOU 913 CG2 VAL A 132 14399 16801 13150 -1771 2092 -1098 C
ATOM 914 N CYS A 133 -19.697 18.417 58.113 1.00145.01 N
ANISOU 914 N CYS A 133 18777 20858 15462 -4009 3600 -1218 N
ATOM 915 CA CYS A 133 -20.399 17.494 58.989 1.00150.81 C
ANISOU 915 CA CYS A 133 19861 21670 15768 -4849 4018 -1129 C
ATOM 916 C CYS A 133 -21.382 16.640 58.196 1.00155.72 C
ANISOU 916 C CYS A 133 20032 22317 16818 -5061 4136 -1231 C
ATOM 917 O CYS A 133 -21.860 17.037 57.130 1.00149.71 O
ANISOU 917 O CYS A 133 18534 21690 16659 -4594 4082 -1546 O
ATOM 918 CB CYS A 133 -21.127 18.250 60.106 1.00153.28 C
ANISOU 918 CB CYS A 133 20088 22447 15705 -5262 4744 -1538 C
ATOM 919 SG CYS A 133 -20.012 19.173 61.206 1.00181.93 S
ANISOU 919 SG CYS A 133 24330 26063 18733 -5136 4630 -1449 S
ATOM 920 N ASN A 134 -21.675 15.461 58.738 1.00180.63 N
ANISOU 920 N ASN A 134 23667 25322 19641 -5792 4268 -947 N
ATOM 921 CA ASN A 134 -22.505 14.489 58.041 1.00186.18 C
ANISOU 921 CA ASN A 134 24044 25968 20730 -6071 4327 -994 C
ATOM 922 C ASN A 134 -23.911 15.038 57.811 1.00186.97 C
ANISOU 922 C ASN A 134 23232 26602 21205 -6171 4960 -1640 C
ATOM 923 O ASN A 134 -24.465 15.719 58.682 1.00184.76 O
ANISOU 923 O ASN A 134 22815 26729 20658 -6469 5569 -1982 O
ATOM 924 CB ASN A 134 -22.592 13.192 58.846 1.00194.89 C
ANISOU 924 CB ASN A 134 25905 26791 21354 -6943 4413 -558 C
ATOM 925 CG ASN A 134 -23.094 12.022 58.022 1.00197.95 C
ANISOU 925 CG ASN A 134 26112 26921 22180 -7154 4248 -485 C
ATOM 926 OD1 ASN A 134 -22.526 11.687 56.983 1.00193.88 O
ANISOU 926 OD1 ASN A 134 25486 26078 22102 -6608 3640 -371 O
ATOM 927 ND2 ASN A 134 -24.171 11.396 58.483 1.00195.44 N
ANISOU 927 ND2 ASN A 134 25746 26767 21745 -7980 4816 -590 N
ATOM 928 N PRO A 135 -24.514 14.766 56.655 1.00185.62 N
ANISOU 928 N PRO A 135 22403 26456 21668 -5919 4819 -1866 N
ATOM 929 CA PRO A 135 -25.954 14.999 56.515 1.00188.66 C
ANISOU 929 CA PRO A 135 21947 27311 22426 -6160 5400 -2468 C
ATOM 930 C PRO A 135 -26.715 14.035 57.405 1.00195.39 C
ANISOU 930 C PRO A 135 23071 28244 22923 -7199 5977 -2431 C
ATOM 931 O PRO A 135 -26.352 12.862 57.527 1.00195.69 O
ANISOU 931 O PRO A 135 23759 27869 22727 -7641 5741 -1934 O
ATOM 932 CB PRO A 135 -26.222 14.722 55.031 1.00174.55 C
ANISOU 932 CB PRO A 135 19560 25433 21328 -5667 4945 -2595 C
ATOM 933 CG PRO A 135 -25.098 13.850 54.597 1.00172.72 C
ANISOU 933 CG PRO A 135 19992 24654 20981 -5517 4283 -2017 C
ATOM 934 CD PRO A 135 -23.911 14.267 55.409 1.00173.70 C
ANISOU 934 CD PRO A 135 20850 24581 20569 -5390 4115 -1639 C
ATOM 935 N ASP A 136 -27.764 14.549 58.045 1.00212.21 N
ANISOU 935 N ASP A 136 24708 30900 25024 -7605 6743 -2976 N
ATOM 936 CA ASP A 136 -28.626 13.812 58.964 1.00216.79 C
ANISOU 936 CA ASP A 136 25513 31585 25272 -8489 7276 -3025 C
ATOM 937 C ASP A 136 -27.908 13.417 60.247 1.00205.39 C
ANISOU 937 C ASP A 136 25183 29925 22929 -9050 7335 -2483 C
ATOM 938 O ASP A 136 -28.463 12.657 61.049 1.00199.89 O
ANISOU 938 O ASP A 136 24880 29195 21876 -9754 7615 -2378 O
ATOM 939 CB ASP A 136 -29.223 12.565 58.300 1.00214.58 C
ANISOU 939 CB ASP A 136 25075 31104 25351 -8893 7189 -2935 C
ATOM 940 CG ASP A 136 -29.979 12.893 57.030 1.00218.64 C
ANISOU 940 CG ASP A 136 24508 31830 26735 -8336 7047 -3476 C
ATOM 941 OD1 ASP A 136 -30.282 14.084 56.814 1.00224.48 O
ANISOU 941 OD1 ASP A 136 24614 32885 27794 -7700 7081 -3960 O
ATOM 942 OD2 ASP A 136 -30.255 11.965 56.241 1.00221.58 O1-
ANISOU 942 OD2 ASP A 136 24699 32010 27481 -8507 6830 -3409 O1-
ATOM 943 N ASN A 137 -26.687 13.901 60.462 1.00187.04 N
ANISOU 943 N ASN A 137 23395 27447 20223 -8748 7037 -2133 N
ATOM 944 CA ASN A 137 -25.973 13.702 61.725 1.00194.83 C
ANISOU 944 CA ASN A 137 25424 28250 20351 -9159 6993 -1664 C
ATOM 945 C ASN A 137 -25.023 14.871 61.920 1.00197.41 C
ANISOU 945 C ASN A 137 25868 28670 20468 -8577 6824 -1697 C
ATOM 946 O ASN A 137 -23.833 14.794 61.589 1.00195.72 O
ANISOU 946 O ASN A 137 26119 28012 20234 -8072 6095 -1236 O
ATOM 947 CB ASN A 137 -25.216 12.372 61.742 1.00192.65 C
ANISOU 947 CB ASN A 137 26080 27368 19750 -9592 6513 -868 C
ATOM 948 CG ASN A 137 -24.611 12.059 63.105 1.00205.19 C
ANISOU 948 CG ASN A 137 28752 28739 20471 -10026 6382 -385 C
ATOM 949 OD1 ASN A 137 -24.863 12.757 64.087 1.00191.36 O
ANISOU 949 OD1 ASN A 137 27041 27341 18327 -10125 6740 -675 O
ATOM 950 ND2 ASN A 137 -23.809 11.002 63.166 1.00211.65 N
ANISOU 950 ND2 ASN A 137 30441 28944 21030 -10261 5808 335 N
ATOM 951 N PRO A 138 -25.524 15.993 62.447 1.00208.08 N
ANISOU 951 N PRO A 138 26772 30434 21853 -8351 7202 -2278 N
ATOM 952 CA PRO A 138 -24.651 17.163 62.645 1.00209.84 C
ANISOU 952 CA PRO A 138 27078 30726 21927 -7784 7040 -2362 C
ATOM 953 C PRO A 138 -23.446 16.876 63.521 1.00210.44 C
ANISOU 953 C PRO A 138 28257 30504 21195 -8014 6693 -1750 C
ATOM 954 O PRO A 138 -22.417 17.550 63.391 1.00206.84 O
ANISOU 954 O PRO A 138 27980 29904 20705 -7438 6268 -1631 O
ATOM 955 CB PRO A 138 -25.593 18.185 63.298 1.00214.26 C
ANISOU 955 CB PRO A 138 27069 31711 22629 -7714 7537 -3082 C
ATOM 956 CG PRO A 138 -26.954 17.789 62.820 1.00214.10 C
ANISOU 956 CG PRO A 138 26311 31876 23161 -7902 7856 -3489 C
ATOM 957 CD PRO A 138 -26.926 16.286 62.793 1.00208.36 C
ANISOU 957 CD PRO A 138 26146 30866 22157 -8556 7758 -2932 C
ATOM 958 N GLN A 139 -23.549 15.886 64.409 1.00212.36 N
ANISOU 958 N GLN A 139 29232 30571 20886 -8733 6709 -1359 N
ATOM 959 CA GLN A 139 -22.442 15.539 65.293 1.00215.55 C
ANISOU 959 CA GLN A 139 30709 30642 20549 -8936 6262 -756 C
ATOM 960 C GLN A 139 -21.244 15.021 64.506 1.00210.92 C
ANISOU 960 C GLN A 139 30573 29537 20030 -8597 5525 -147 C
ATOM 961 O GLN A 139 -20.101 15.429 64.746 1.00197.09 O
ANISOU 961 O GLN A 139 29256 27565 18064 -8166 4986 88 O
ATOM 962 CB GLN A 139 -22.916 14.504 66.311 1.00214.62 C
ANISOU 962 CB GLN A 139 31225 30412 19909 -9770 6397 -470 C
ATOM 963 CG GLN A 139 -21.814 13.803 67.069 1.00213.36 C
ANISOU 963 CG GLN A 139 32208 29771 19090 -10000 5771 264 C
ATOM 964 CD GLN A 139 -22.170 12.364 67.381 1.00221.25 C
ANISOU 964 CD GLN A 139 33777 30416 19871 -10696 5667 732 C
ATOM 965 OE1 GLN A 139 -23.214 11.865 66.955 1.00229.74 O
ANISOU 965 OE1 GLN A 139 34387 31606 21299 -11013 6073 517 O
ATOM 966 NE2 GLN A 139 -21.301 11.685 68.116 1.00219.79 N
ANISOU 966 NE2 GLN A 139 34587 29776 19146 -10910 5078 1360 N
ATOM 967 N GLU A 140 -21.486 14.110 63.565 1.00202.85 N
ANISOU 967 N GLU A 140 29331 28191 19551 -8543 5255 33 N
ATOM 968 CA GLU A 140 -20.410 13.544 62.759 1.00193.17 C
ANISOU 968 CA GLU A 140 28357 26344 18696 -7959 4330 489 C
ATOM 969 C GLU A 140 -19.839 14.613 61.838 1.00185.69 C
ANISOU 969 C GLU A 140 26760 25458 18336 -6940 4000 173 C
ATOM 970 O GLU A 140 -20.573 15.206 61.042 1.00183.65 O
ANISOU 970 O GLU A 140 25616 25514 18648 -6599 4297 -326 O
ATOM 971 CB GLU A 140 -20.927 12.363 61.945 1.00187.25 C
ANISOU 971 CB GLU A 140 27445 25286 18417 -8167 4198 641 C
ATOM 972 CG GLU A 140 -19.903 11.784 60.986 1.00195.17 C
ANISOU 972 CG GLU A 140 28569 25687 19900 -7525 3294 978 C
ATOM 973 CD GLU A 140 -20.486 10.709 60.091 1.00202.51 C
ANISOU 973 CD GLU A 140 29228 26354 21363 -7681 3194 1006 C
ATOM 974 OE1 GLU A 140 -21.482 10.073 60.495 1.00197.94 O
ANISOU 974 OE1 GLU A 140 28718 25874 20615 -8483 3700 1004 O
ATOM 975 OE2 GLU A 140 -19.943 10.497 58.986 1.00197.91 O1-
ANISOU 975 OE2 GLU A 140 28361 25478 21359 -7033 2627 1003 O1-
ATOM 976 N CYS A 141 -18.535 14.860 61.944 1.00174.46 N
ANISOU 976 N CYS A 141 25779 23726 16783 -6473 3368 463 N
ATOM 977 CA CYS A 141 -17.882 15.894 61.157 1.00170.17 C
ANISOU 977 CA CYS A 141 24716 23220 16721 -5584 3063 212 C
ATOM 978 C CYS A 141 -16.496 15.427 60.739 1.00162.89 C
ANISOU 978 C CYS A 141 24198 21753 15940 -5118 2193 638 C
ATOM 979 O CYS A 141 -15.873 14.596 61.406 1.00173.28 O
ANISOU 979 O CYS A 141 26304 22690 16843 -5436 1800 1108 O
ATOM 980 CB CYS A 141 -17.778 17.216 61.930 1.00180.78 C
ANISOU 980 CB CYS A 141 26000 24945 17743 -5478 3400 -123 C
ATOM 981 SG CYS A 141 -19.358 17.820 62.578 1.00210.92 S
ANISOU 981 SG CYS A 141 29326 29432 21381 -6035 4461 -736 S
ATOM 982 N LEU A 142 -16.021 15.977 59.624 1.00134.23 N
ANISOU 982 N LEU A 142 20012 18084 12903 -4366 1887 454 N
ATOM 983 CA LEU A 142 -14.740 15.596 59.044 1.00130.41 C
ANISOU 983 CA LEU A 142 19730 17148 12670 -3870 1124 730 C
ATOM 984 C LEU A 142 -14.022 16.837 58.546 1.00126.99 C
ANISOU 984 C LEU A 142 18889 16852 12510 -3184 982 482 C
ATOM 985 O LEU A 142 -14.623 17.676 57.868 1.00125.86 O
ANISOU 985 O LEU A 142 18080 17027 12716 -2897 1309 117 O
ATOM 986 CB LEU A 142 -14.926 14.600 57.892 1.00120.71 C
ANISOU 986 CB LEU A 142 18234 15659 11970 -3741 858 790 C
ATOM 987 CG LEU A 142 -15.565 13.260 58.253 1.00123.47 C
ANISOU 987 CG LEU A 142 18994 15763 12154 -4413 917 1061 C
ATOM 988 CD1 LEU A 142 -15.873 12.454 57.007 1.00122.18 C
ANISOU 988 CD1 LEU A 142 18420 15413 12589 -4239 722 984 C
ATOM 989 CD2 LEU A 142 -14.660 12.474 59.192 1.00140.12 C
ANISOU 989 CD2 LEU A 142 22035 17383 13822 -4685 404 1572 C
ATOM 990 N LEU A 143 -12.743 16.949 58.881 1.00134.92 N
ANISOU 990 N LEU A 143 20294 17595 13375 -2935 468 684 N
ATOM 991 CA LEU A 143 -11.915 18.029 58.372 1.00128.59 C
ANISOU 991 CA LEU A 143 19144 16857 12857 -2322 280 486 C
ATOM 992 C LEU A 143 -11.308 17.592 57.044 1.00113.99 C
ANISOU 992 C LEU A 143 16967 14772 11573 -1840 -163 512 C
ATOM 993 O LEU A 143 -11.466 16.445 56.617 1.00115.91 O
ANISOU 993 O LEU A 143 17293 14774 11975 -1964 -366 669 O
ATOM 994 CB LEU A 143 -10.817 18.377 59.385 1.00127.56 C
ANISOU 994 CB LEU A 143 19554 16590 12325 -2309 -54 630 C
ATOM 995 CG LEU A 143 -11.230 18.417 60.862 1.00120.06 C
ANISOU 995 CG LEU A 143 19175 15792 10649 -2907 245 710 C
ATOM 996 CD1 LEU A 143 -10.132 19.016 61.727 1.00147.32 C
ANISOU 996 CD1 LEU A 143 23044 19178 13754 -2795 -98 755 C
ATOM 997 CD2 LEU A 143 -12.523 19.165 61.073 1.00129.73 C
ANISOU 997 CD2 LEU A 143 20011 17501 11781 -3156 1037 331 C
ATOM 998 N LEU A 144 -10.613 18.513 56.375 1.00109.96 N
ANISOU 998 N LEU A 144 16084 14331 11362 -1318 -294 335 N
ATOM 999 CA LEU A 144 -9.892 18.113 55.171 1.00114.32 C
ANISOU 999 CA LEU A 144 16368 14694 12374 -899 -701 334 C
ATOM 1000 C LEU A 144 -8.913 16.997 55.495 1.00125.72 C
ANISOU 1000 C LEU A 144 18294 15692 13783 -933 -1292 595 C
ATOM 1001 O LEU A 144 -8.821 15.999 54.774 1.00128.08 O
ANISOU 1001 O LEU A 144 18529 15759 14376 -863 -1561 640 O
ATOM 1002 CB LEU A 144 -9.152 19.305 54.561 1.00112.54 C
ANISOU 1002 CB LEU A 144 15771 14600 12390 -420 -747 143 C
ATOM 1003 CG LEU A 144 -8.510 19.022 53.198 1.00 95.11 C
ANISOU 1003 CG LEU A 144 13208 12307 10620 -27 -1042 75 C
ATOM 1004 CD1 LEU A 144 -9.528 19.104 52.069 1.00 94.99 C
ANISOU 1004 CD1 LEU A 144 12703 12536 10854 52 -759 -74 C
ATOM 1005 CD2 LEU A 144 -7.355 19.970 52.945 1.00103.47 C
ANISOU 1005 CD2 LEU A 144 14121 13379 11812 330 -1211 -26 C
ATOM 1006 N GLU A 145 -8.183 17.150 56.595 1.00127.73 N
ANISOU 1006 N GLU A 145 19036 15804 13691 -1032 -1534 745 N
ATOM 1007 CA GLU A 145 -7.342 16.111 57.138 1.00118.00 C
ANISOU 1007 CA GLU A 145 18350 14114 12370 -1107 -2148 1026 C
ATOM 1008 C GLU A 145 -7.866 15.722 58.512 1.00118.01 C
ANISOU 1008 C GLU A 145 19039 14056 11745 -1697 -2052 1317 C
ATOM 1009 O GLU A 145 -8.108 16.606 59.347 1.00120.02 O
ANISOU 1009 O GLU A 145 19425 14603 11574 -1887 -1714 1249 O
ATOM 1010 CB GLU A 145 -5.886 16.573 57.243 1.00111.88 C
ANISOU 1010 CB GLU A 145 17588 13197 11726 -702 -2641 960 C
ATOM 1011 CG GLU A 145 -4.898 15.446 57.485 1.00122.62 C
ANISOU 1011 CG GLU A 145 19347 14032 13213 -614 -3402 1169 C
ATOM 1012 CD GLU A 145 -4.522 14.709 56.215 1.00125.21 C
ANISOU 1012 CD GLU A 145 19256 14156 14163 -258 -3670 1011 C
ATOM 1013 OE1 GLU A 145 -4.786 15.240 55.118 1.00123.54 O
ANISOU 1013 OE1 GLU A 145 18440 14252 14247 -29 -3308 734 O
ATOM 1014 OE2 GLU A 145 -3.952 13.603 56.311 1.00133.40 O1-
ANISOU 1014 OE2 GLU A 145 20582 14713 15391 -205 -4266 1151 O1-
ATOM 1015 N PRO A 146 -8.056 14.426 58.793 1.00124.01 N
ANISOU 1015 N PRO A 146 20270 14438 12411 -2028 -2329 1636 N
ATOM 1016 CA PRO A 146 -7.709 13.322 57.906 1.00127.11 C
ANISOU 1016 CA PRO A 146 20557 14417 13321 -1807 -2787 1687 C
ATOM 1017 C PRO A 146 -8.858 12.769 57.067 1.00139.21 C
ANISOU 1017 C PRO A 146 21740 16042 15112 -1989 -2395 1592 C
ATOM 1018 O PRO A 146 -8.601 12.142 56.047 1.00149.86 O
ANISOU 1018 O PRO A 146 22787 17180 16974 -1693 -2669 1475 O
ATOM 1019 CB PRO A 146 -7.252 12.256 58.888 1.00123.50 C
ANISOU 1019 CB PRO A 146 20930 13418 12575 -2110 -3379 2128 C
ATOM 1020 CG PRO A 146 -8.183 12.461 60.060 1.00135.17 C
ANISOU 1020 CG PRO A 146 22903 15139 13317 -2785 -2889 2344 C
ATOM 1021 CD PRO A 146 -8.542 13.937 60.094 1.00135.21 C
ANISOU 1021 CD PRO A 146 22439 15767 13166 -2681 -2256 1983 C
ATOM 1022 N GLY A 147 -10.100 12.975 57.507 1.00139.15 N
ANISOU 1022 N GLY A 147 21756 16354 14761 -2484 -1769 1599 N
ATOM 1023 CA GLY A 147 -11.257 12.348 56.895 1.00138.58 C
ANISOU 1023 CA GLY A 147 21411 16348 14896 -2760 -1419 1524 C
ATOM 1024 C GLY A 147 -11.510 12.598 55.420 1.00122.73 C
ANISOU 1024 C GLY A 147 18613 14556 13461 -2314 -1298 1156 C
ATOM 1025 O GLY A 147 -11.521 11.656 54.623 1.00126.37 O
ANISOU 1025 O GLY A 147 18957 14749 14308 -2238 -1560 1135 O
ATOM 1026 N LEU A 148 -11.716 13.859 55.039 1.00118.83 N
ANISOU 1026 N LEU A 148 17601 14530 13021 -2026 -929 860 N
ATOM 1027 CA LEU A 148 -12.101 14.159 53.663 1.00111.43 C
ANISOU 1027 CA LEU A 148 15961 13838 12538 -1665 -794 547 C
ATOM 1028 C LEU A 148 -11.003 13.741 52.694 1.00110.96 C
ANISOU 1028 C LEU A 148 15770 13518 12872 -1187 -1328 492 C
ATOM 1029 O LEU A 148 -11.272 13.134 51.650 1.00117.10 O
ANISOU 1029 O LEU A 148 16231 14264 13997 -1076 -1409 344 O
ATOM 1030 CB LEU A 148 -12.408 15.648 53.533 1.00104.81 C
ANISOU 1030 CB LEU A 148 14689 13464 11671 -1432 -391 298 C
ATOM 1031 CG LEU A 148 -13.688 16.145 54.208 1.00110.01 C
ANISOU 1031 CG LEU A 148 15242 14468 12087 -1828 219 178 C
ATOM 1032 CD1 LEU A 148 -13.962 17.586 53.843 1.00105.39 C
ANISOU 1032 CD1 LEU A 148 14146 14261 11637 -1480 512 -117 C
ATOM 1033 CD2 LEU A 148 -14.864 15.288 53.808 1.00111.59 C
ANISOU 1033 CD2 LEU A 148 15229 14720 12451 -2168 444 107 C
ATOM 1034 N ASN A 149 -9.748 14.023 53.048 1.00109.79 N
ANISOU 1034 N ASN A 149 15848 13191 12676 -921 -1700 569 N
ATOM 1035 CA ASN A 149 -8.640 13.649 52.178 1.00111.76 C
ANISOU 1035 CA ASN A 149 15922 13222 13320 -477 -2175 444 C
ATOM 1036 C ASN A 149 -8.567 12.136 52.004 1.00113.70 C
ANISOU 1036 C ASN A 149 16406 12994 13802 -596 -2580 535 C
ATOM 1037 O ASN A 149 -8.208 11.649 50.927 1.00111.80 O
ANISOU 1037 O ASN A 149 15838 12671 13970 -302 -2798 303 O
ATOM 1038 CB ASN A 149 -7.324 14.208 52.716 1.00110.19 C
ANISOU 1038 CB ASN A 149 15903 12911 13052 -214 -2503 478 C
ATOM 1039 CG ASN A 149 -7.006 15.587 52.152 1.00107.06 C
ANISOU 1039 CG ASN A 149 15044 12914 12719 120 -2247 246 C
ATOM 1040 OD1 ASN A 149 -7.362 15.896 51.016 1.00 91.00 O
ANISOU 1040 OD1 ASN A 149 12530 11141 10904 303 -2029 41 O
ATOM 1041 ND2 ASN A 149 -6.314 16.408 52.933 1.00101.91 N
ANISOU 1041 ND2 ASN A 149 14566 12286 11867 183 -2307 287 N
ATOM 1042 N GLU A 150 -8.928 11.374 53.041 1.00117.91 N
ANISOU 1042 N GLU A 150 17522 13204 14072 -1055 -2677 861 N
ATOM 1043 CA GLU A 150 -8.981 9.923 52.897 1.00127.81 C
ANISOU 1043 CA GLU A 150 19043 13943 15577 -1220 -3059 976 C
ATOM 1044 C GLU A 150 -9.989 9.532 51.829 1.00130.52 C
ANISOU 1044 C GLU A 150 18920 14466 16205 -1296 -2757 734 C
ATOM 1045 O GLU A 150 -9.666 8.808 50.881 1.00126.99 O
ANISOU 1045 O GLU A 150 18241 13807 16203 -1043 -3061 518 O
ATOM 1046 CB GLU A 150 -9.351 9.263 54.225 1.00126.89 C
ANISOU 1046 CB GLU A 150 19690 13478 15045 -1806 -3141 1429 C
ATOM 1047 CG GLU A 150 -9.122 7.760 54.230 1.00145.49 C
ANISOU 1047 CG GLU A 150 22460 15136 17683 -1938 -3708 1625 C
ATOM 1048 CD GLU A 150 -10.337 6.984 53.774 1.00160.05 C
ANISOU 1048 CD GLU A 150 24190 16948 19672 -2353 -3399 1592 C
ATOM 1049 OE1 GLU A 150 -11.464 7.489 53.954 1.00161.21 O
ANISOU 1049 OE1 GLU A 150 24173 17554 19526 -2737 -2746 1567 O
ATOM 1050 OE2 GLU A 150 -10.166 5.879 53.219 1.00158.16 O1-
ANISOU 1050 OE2 GLU A 150 23984 16225 19884 -2284 -3812 1542 O1-
ATOM 1051 N ILE A 151 -11.226 10.013 51.975 1.00126.99 N
ANISOU 1051 N ILE A 151 18304 14426 15522 -1642 -2164 717 N
ATOM 1052 CA ILE A 151 -12.294 9.646 51.050 1.00115.89 C
ANISOU 1052 CA ILE A 151 16450 13209 14374 -1761 -1890 481 C
ATOM 1053 C ILE A 151 -11.862 9.914 49.614 1.00116.20 C
ANISOU 1053 C ILE A 151 15901 13454 14796 -1206 -2021 106 C
ATOM 1054 O ILE A 151 -11.872 9.020 48.762 1.00122.45 O
ANISOU 1054 O ILE A 151 16533 14050 15943 -1127 -2255 -76 O
ATOM 1055 CB ILE A 151 -13.587 10.400 51.395 1.00116.01 C
ANISOU 1055 CB ILE A 151 16236 13719 14123 -2106 -1229 426 C
ATOM 1056 CG1 ILE A 151 -14.040 10.074 52.821 1.00123.71 C
ANISOU 1056 CG1 ILE A 151 17812 14539 14654 -2746 -1030 765 C
ATOM 1057 CG2 ILE A 151 -14.661 10.061 50.392 1.00121.26 C
ANISOU 1057 CG2 ILE A 151 16376 14597 15100 -2184 -1009 141 C
ATOM 1058 CD1 ILE A 151 -15.312 10.767 53.219 1.00120.26 C
ANISOU 1058 CD1 ILE A 151 17106 14604 13982 -3116 -337 628 C
ATOM 1059 N MET A 152 -11.444 11.150 49.335 1.00107.47 N
ANISOU 1059 N MET A 152 14497 12734 13604 -838 -1875 -18 N
ATOM 1060 CA MET A 152 -11.070 11.505 47.971 1.00104.05 C
ANISOU 1060 CA MET A 152 13544 12554 13435 -381 -1940 -342 C
ATOM 1061 C MET A 152 -9.894 10.674 47.470 1.00115.31 C
ANISOU 1061 C MET A 152 15029 13610 15173 -92 -2453 -470 C
ATOM 1062 O MET A 152 -9.851 10.295 46.293 1.00110.13 O
ANISOU 1062 O MET A 152 14016 13040 14787 111 -2542 -777 O
ATOM 1063 CB MET A 152 -10.743 12.995 47.889 1.00 98.10 C
ANISOU 1063 CB MET A 152 12561 12201 12512 -96 -1716 -385 C
ATOM 1064 CG MET A 152 -11.857 13.896 48.383 1.00 98.82 C
ANISOU 1064 CG MET A 152 12542 12636 12368 -312 -1234 -334 C
ATOM 1065 SD MET A 152 -13.297 13.790 47.306 1.00113.33 S
ANISOU 1065 SD MET A 152 13843 14818 14400 -382 -973 -584 S
ATOM 1066 CE MET A 152 -12.572 14.260 45.738 1.00118.56 C
ANISOU 1066 CE MET A 152 14101 15705 15240 146 -1180 -814 C
ATOM 1067 N ALA A 153 -8.937 10.372 48.346 1.00123.56 N
ANISOU 1067 N ALA A 153 16506 14249 16194 -64 -2814 -277 N
ATOM 1068 CA ALA A 153 -7.689 9.754 47.921 1.00125.74 C
ANISOU 1068 CA ALA A 153 16759 14192 16824 291 -3322 -466 C
ATOM 1069 C ALA A 153 -7.691 8.234 48.013 1.00130.61 C
ANISOU 1069 C ALA A 153 17668 14208 17751 148 -3753 -438 C
ATOM 1070 O ALA A 153 -6.761 7.602 47.506 1.00137.15 O
ANISOU 1070 O ALA A 153 18390 14743 18979 471 -4183 -699 O
ATOM 1071 CB ALA A 153 -6.513 10.305 48.739 1.00116.19 C
ANISOU 1071 CB ALA A 153 15784 12853 15509 486 -3576 -337 C
ATOM 1072 N ASN A 154 -8.695 7.631 48.630 1.00120.89 N
ANISOU 1072 N ASN A 154 16786 12770 16378 -336 -3646 -161 N
ATOM 1073 CA ASN A 154 -8.721 6.176 48.766 1.00123.49 C
ANISOU 1073 CA ASN A 154 17460 12447 17015 -523 -4078 -85 C
ATOM 1074 C ASN A 154 -10.073 5.531 48.491 1.00122.13 C
ANISOU 1074 C ASN A 154 17242 12281 16879 -974 -3792 -86 C
ATOM 1075 O ASN A 154 -10.094 4.380 48.045 1.00117.64 O
ANISOU 1075 O ASN A 154 16715 11269 16715 -1008 -4116 -224 O
ATOM 1076 CB ASN A 154 -8.259 5.777 50.175 1.00131.22 C
ANISOU 1076 CB ASN A 154 19184 12881 17793 -751 -4468 394 C
ATOM 1077 CG ASN A 154 -6.945 5.026 50.166 1.00142.72 C
ANISOU 1077 CG ASN A 154 20806 13735 19687 -355 -5224 305 C
ATOM 1078 OD1 ASN A 154 -6.347 4.800 49.116 1.00150.16 O
ANISOU 1078 OD1 ASN A 154 21272 14687 21096 85 -5408 -164 O
ATOM 1079 ND2 ASN A 154 -6.480 4.640 51.349 1.00141.91 N
ANISOU 1079 ND2 ASN A 154 21378 13112 19428 -510 -5682 734 N
ATOM 1080 N SER A 155 -11.189 6.220 48.715 1.00120.03 N
ANISOU 1080 N SER A 155 16850 12492 16266 -1310 -3213 10 N
ATOM 1081 CA SER A 155 -12.522 5.658 48.522 1.00115.29 C
ANISOU 1081 CA SER A 155 16152 11938 15715 -1780 -2909 -22 C
ATOM 1082 C SER A 155 -12.823 5.420 47.043 1.00108.73 C
ANISOU 1082 C SER A 155 14707 11339 15265 -1521 -2900 -512 C
ATOM 1083 O SER A 155 -12.146 5.930 46.146 1.00121.43 O
ANISOU 1083 O SER A 155 15927 13224 16988 -1012 -2988 -819 O
ATOM 1084 CB SER A 155 -13.591 6.578 49.122 1.00123.68 C
ANISOU 1084 CB SER A 155 17127 13516 16351 -2146 -2277 108 C
ATOM 1085 OG SER A 155 -14.907 6.177 48.771 1.00114.72 O
ANISOU 1085 OG SER A 155 15720 12542 15326 -2546 -1940 -36 O
ATOM 1086 N LEU A 156 -13.882 4.645 46.798 1.00111.18 N
ANISOU 1086 N LEU A 156 14941 11560 15742 -1925 -2772 -592 N
ATOM 1087 CA LEU A 156 -14.261 4.211 45.457 1.00110.28 C
ANISOU 1087 CA LEU A 156 14313 11599 15988 -1765 -2822 -1063 C
ATOM 1088 C LEU A 156 -15.775 4.224 45.290 1.00106.18 C
ANISOU 1088 C LEU A 156 13485 11419 15439 -2205 -2384 -1158 C
ATOM 1089 O LEU A 156 -16.369 3.273 44.771 1.00105.91 O
ANISOU 1089 O LEU A 156 13331 11186 15725 -2437 -2476 -1373 O
ATOM 1090 CB LEU A 156 -13.714 2.816 45.156 1.00103.12 C
ANISOU 1090 CB LEU A 156 13631 10005 15547 -1731 -3358 -1196 C
ATOM 1091 CG LEU A 156 -12.205 2.611 45.039 1.00113.60 C
ANISOU 1091 CG LEU A 156 15100 10974 17088 -1216 -3874 -1289 C
ATOM 1092 CD1 LEU A 156 -11.906 1.150 44.742 1.00103.33 C
ANISOU 1092 CD1 LEU A 156 13979 8950 16332 -1228 -4392 -1478 C
ATOM 1093 CD2 LEU A 156 -11.632 3.504 43.948 1.00111.70 C
ANISOU 1093 CD2 LEU A 156 14292 11332 16816 -663 -3772 -1703 C
ATOM 1094 N ASP A 157 -16.429 5.291 45.742 1.00124.01 N
ANISOU 1094 N ASP A 157 15581 14179 17358 -2328 -1914 -1043 N
ATOM 1095 CA ASP A 157 -17.866 5.447 45.556 1.00120.86 C
ANISOU 1095 CA ASP A 157 14770 14175 16977 -2683 -1489 -1212 C
ATOM 1096 C ASP A 157 -18.123 6.819 44.954 1.00116.90 C
ANISOU 1096 C ASP A 157 13723 14361 16333 -2282 -1241 -1418 C
ATOM 1097 O ASP A 157 -17.758 7.839 45.550 1.00126.52 O
ANISOU 1097 O ASP A 157 15042 15774 17255 -2122 -1071 -1228 O
ATOM 1098 CB ASP A 157 -18.628 5.276 46.874 1.00127.16 C
ANISOU 1098 CB ASP A 157 15922 14850 17543 -3363 -1115 -888 C
ATOM 1099 CG ASP A 157 -20.131 5.456 46.710 1.00131.19 C
ANISOU 1099 CG ASP A 157 15915 15802 18130 -3744 -638 -1140 C
ATOM 1100 OD1 ASP A 157 -20.622 5.439 45.560 1.00144.33 O
ANISOU 1100 OD1 ASP A 157 17009 17744 20086 -3527 -705 -1541 O
ATOM 1101 OD2 ASP A 157 -20.825 5.613 47.736 1.00131.45 O1-
ANISOU 1101 OD2 ASP A 157 16097 15924 17924 -4272 -198 -965 O1-
ATOM 1102 N TYR A 158 -18.748 6.834 43.775 1.00115.85 N
ANISOU 1102 N TYR A 158 13039 14565 16414 -2125 -1262 -1804 N
ATOM 1103 CA TYR A 158 -19.042 8.086 43.084 1.00109.69 C
ANISOU 1103 CA TYR A 158 11763 14391 15525 -1736 -1120 -1982 C
ATOM 1104 C TYR A 158 -19.874 9.015 43.961 1.00111.30 C
ANISOU 1104 C TYR A 158 11841 14897 15550 -1947 -659 -1867 C
ATOM 1105 O TYR A 158 -19.529 10.188 44.147 1.00115.00 O
ANISOU 1105 O TYR A 158 12274 15614 15809 -1636 -549 -1769 O
ATOM 1106 CB TYR A 158 -19.763 7.785 41.767 1.00108.16 C
ANISOU 1106 CB TYR A 158 11045 14476 15576 -1641 -1256 -2401 C
ATOM 1107 CG TYR A 158 -20.011 8.978 40.863 1.00115.07 C
ANISOU 1107 CG TYR A 158 11455 15924 16341 -1206 -1246 -2569 C
ATOM 1108 CD1 TYR A 158 -21.057 9.861 41.109 1.00119.58 C
ANISOU 1108 CD1 TYR A 158 11662 16872 16901 -1262 -955 -2607 C
ATOM 1109 CD2 TYR A 158 -19.219 9.200 39.745 1.00111.39 C
ANISOU 1109 CD2 TYR A 158 10916 15614 15793 -755 -1542 -2707 C
ATOM 1110 CE1 TYR A 158 -21.289 10.944 40.278 1.00113.62 C
ANISOU 1110 CE1 TYR A 158 10526 16565 16079 -845 -1032 -2725 C
ATOM 1111 CE2 TYR A 158 -19.446 10.277 38.907 1.00104.86 C
ANISOU 1111 CE2 TYR A 158 9749 15274 14820 -402 -1572 -2796 C
ATOM 1112 CZ TYR A 158 -20.480 11.146 39.178 1.00101.59 C
ANISOU 1112 CZ TYR A 158 9018 15160 14421 -432 -1354 -2780 C
ATOM 1113 OH TYR A 158 -20.703 12.219 38.345 1.00 99.42 O
ANISOU 1113 OH TYR A 158 8448 15296 14030 -59 -1465 -2832 O
ATOM 1114 N ASN A 159 -20.974 8.501 44.516 1.00112.23 N
ANISOU 1114 N ASN A 159 11877 14994 15770 -2499 -366 -1914 N
ATOM 1115 CA ASN A 159 -21.864 9.340 45.312 1.00114.36 C
ANISOU 1115 CA ASN A 159 11935 15602 15914 -2729 125 -1920 C
ATOM 1116 C ASN A 159 -21.204 9.776 46.615 1.00122.13 C
ANISOU 1116 C ASN A 159 13462 16423 16520 -2850 316 -1552 C
ATOM 1117 O ASN A 159 -21.392 10.916 47.058 1.00121.78 O
ANISOU 1117 O ASN A 159 13260 16701 16309 -2715 602 -1570 O
ATOM 1118 CB ASN A 159 -23.171 8.600 45.589 1.00118.07 C
ANISOU 1118 CB ASN A 159 12163 16104 16593 -3360 434 -2108 C
ATOM 1119 CG ASN A 159 -24.057 8.512 44.364 1.00113.21 C
ANISOU 1119 CG ASN A 159 10859 15806 16350 -3212 305 -2554 C
ATOM 1120 OD1 ASN A 159 -24.121 9.443 43.560 1.00114.48 O
ANISOU 1120 OD1 ASN A 159 10601 16346 16551 -2688 170 -2738 O
ATOM 1121 ND2 ASN A 159 -24.743 7.386 44.209 1.00134.41 N
ANISOU 1121 ND2 ASN A 159 13448 18317 19306 -3688 311 -2719 N
ATOM 1122 N GLU A 160 -20.435 8.885 47.248 1.00118.22 N
ANISOU 1122 N GLU A 160 13612 15410 15896 -3095 122 -1231 N
ATOM 1123 CA GLU A 160 -19.698 9.268 48.451 1.00117.10 C
ANISOU 1123 CA GLU A 160 14037 15100 15356 -3180 201 -868 C
ATOM 1124 C GLU A 160 -18.669 10.346 48.145 1.00113.20 C
ANISOU 1124 C GLU A 160 13505 14754 14751 -2531 5 -844 C
ATOM 1125 O GLU A 160 -18.602 11.370 48.836 1.00111.16 O
ANISOU 1125 O GLU A 160 13287 14718 14230 -2470 263 -774 O
ATOM 1126 CB GLU A 160 -19.009 8.053 49.071 1.00120.76 C
ANISOU 1126 CB GLU A 160 15216 14919 15746 -3504 -113 -514 C
ATOM 1127 CG GLU A 160 -18.281 8.384 50.365 1.00120.25 C
ANISOU 1127 CG GLU A 160 15788 14675 15228 -3634 -90 -121 C
ATOM 1128 CD GLU A 160 -17.444 7.234 50.883 1.00123.53 C
ANISOU 1128 CD GLU A 160 16935 14396 15604 -3832 -562 254 C
ATOM 1129 OE1 GLU A 160 -17.113 6.331 50.087 1.00121.37 O
ANISOU 1129 OE1 GLU A 160 16633 13763 15720 -3666 -987 163 O
ATOM 1130 OE2 GLU A 160 -17.115 7.235 52.088 1.00131.49 O1-
ANISOU 1130 OE2 GLU A 160 18557 15208 16196 -4145 -536 624 O1-
ATOM 1131 N ARG A 161 -17.841 10.121 47.121 1.00118.81 N
ANISOU 1131 N ARG A 161 14141 15343 15660 -2072 -434 -927 N
ATOM 1132 CA ARG A 161 -16.826 11.104 46.755 1.00114.67 C
ANISOU 1132 CA ARG A 161 13568 14959 15041 -1509 -601 -916 C
ATOM 1133 C ARG A 161 -17.443 12.453 46.418 1.00118.04 C
ANISOU 1133 C ARG A 161 13510 15907 15434 -1264 -312 -1088 C
ATOM 1134 O ARG A 161 -16.940 13.495 46.853 1.00124.51 O
ANISOU 1134 O ARG A 161 14413 16836 16059 -1047 -223 -983 O
ATOM 1135 CB ARG A 161 -16.001 10.608 45.571 1.00103.44 C
ANISOU 1135 CB ARG A 161 12043 13411 13848 -1119 -1037 -1074 C
ATOM 1136 CG ARG A 161 -14.897 9.649 45.924 1.00104.21 C
ANISOU 1136 CG ARG A 161 12627 12962 14008 -1123 -1431 -916 C
ATOM 1137 CD ARG A 161 -13.829 9.770 44.869 1.00 97.83 C
ANISOU 1137 CD ARG A 161 11634 12196 13340 -606 -1748 -1125 C
ATOM 1138 NE ARG A 161 -12.872 8.675 44.867 1.00115.38 N
ANISOU 1138 NE ARG A 161 14151 13900 15788 -538 -2188 -1142 N
ATOM 1139 CZ ARG A 161 -11.737 8.691 44.182 1.00134.41 C
ANISOU 1139 CZ ARG A 161 16453 16282 18333 -119 -2466 -1343 C
ATOM 1140 NH1 ARG A 161 -11.363 9.756 43.491 1.00134.77 N
ANISOU 1140 NH1 ARG A 161 16178 16780 18247 218 -2332 -1478 N
ATOM 1141 NH2 ARG A 161 -10.954 7.617 44.198 1.00147.97 N
ANISOU 1141 NH2 ARG A 161 18389 17491 20342 -50 -2888 -1424 N
ATOM 1142 N LEU A 162 -18.520 12.454 45.625 1.00114.65 N
ANISOU 1142 N LEU A 162 12566 15771 15224 -1278 -212 -1366 N
ATOM 1143 CA LEU A 162 -19.201 13.700 45.292 1.00109.43 C
ANISOU 1143 CA LEU A 162 11428 15552 14598 -1026 -11 -1538 C
ATOM 1144 C LEU A 162 -19.556 14.494 46.540 1.00112.87 C
ANISOU 1144 C LEU A 162 11948 16087 14849 -1222 403 -1466 C
ATOM 1145 O LEU A 162 -19.484 15.727 46.533 1.00109.44 O
ANISOU 1145 O LEU A 162 11343 15864 14377 -897 485 -1501 O
ATOM 1146 CB LEU A 162 -20.460 13.402 44.470 1.00101.82 C
ANISOU 1146 CB LEU A 162 9913 14848 13926 -1110 16 -1862 C
ATOM 1147 CG LEU A 162 -21.355 14.591 44.116 1.00102.84 C
ANISOU 1147 CG LEU A 162 9492 15400 14184 -855 155 -2081 C
ATOM 1148 CD1 LEU A 162 -20.534 15.747 43.569 1.00100.42 C
ANISOU 1148 CD1 LEU A 162 9213 15188 13753 -306 -53 -1962 C
ATOM 1149 CD2 LEU A 162 -22.445 14.191 43.131 1.00110.35 C
ANISOU 1149 CD2 LEU A 162 9898 16584 15445 -874 34 -2414 C
ATOM 1150 N TRP A 163 -19.920 13.807 47.623 1.00107.55 N
ANISOU 1150 N TRP A 163 11568 15252 14045 -1773 666 -1369 N
ATOM 1151 CA TRP A 163 -20.191 14.483 48.886 1.00109.80 C
ANISOU 1151 CA TRP A 163 11997 15652 14072 -2024 1094 -1326 C
ATOM 1152 C TRP A 163 -18.962 15.235 49.390 1.00112.04 C
ANISOU 1152 C TRP A 163 12686 15807 14076 -1730 957 -1089 C
ATOM 1153 O TRP A 163 -19.010 16.451 49.609 1.00105.19 O
ANISOU 1153 O TRP A 163 11635 15166 13165 -1486 1135 -1193 O
ATOM 1154 CB TRP A 163 -20.667 13.472 49.931 1.00118.66 C
ANISOU 1154 CB TRP A 163 13482 16596 15007 -2746 1373 -1203 C
ATOM 1155 CG TRP A 163 -21.069 14.142 51.191 1.00127.04 C
ANISOU 1155 CG TRP A 163 14654 17861 15755 -3070 1879 -1229 C
ATOM 1156 CD1 TRP A 163 -22.099 15.020 51.357 1.00126.44 C
ANISOU 1156 CD1 TRP A 163 14029 18214 15797 -3088 2330 -1603 C
ATOM 1157 CD2 TRP A 163 -20.401 14.060 52.454 1.00129.87 C
ANISOU 1157 CD2 TRP A 163 15705 18016 15624 -3382 1961 -911 C
ATOM 1158 NE1 TRP A 163 -22.138 15.461 52.657 1.00132.39 N
ANISOU 1158 NE1 TRP A 163 15079 19069 16156 -3427 2749 -1576 N
ATOM 1159 CE2 TRP A 163 -21.103 14.888 53.350 1.00134.67 C
ANISOU 1159 CE2 TRP A 163 16157 18984 16026 -3626 2525 -1132 C
ATOM 1160 CE3 TRP A 163 -19.288 13.353 52.919 1.00121.78 C
ANISOU 1160 CE3 TRP A 163 15410 16536 14325 -3472 1580 -486 C
ATOM 1161 CZ2 TRP A 163 -20.726 15.033 54.683 1.00143.75 C
ANISOU 1161 CZ2 TRP A 163 17893 20091 16634 -3993 2744 -931 C
ATOM 1162 CZ3 TRP A 163 -18.918 13.496 54.245 1.00123.75 C
ANISOU 1162 CZ3 TRP A 163 16251 16713 14057 -3815 1737 -248 C
ATOM 1163 CH2 TRP A 163 -19.636 14.328 55.111 1.00145.76 C
ANISOU 1163 CH2 TRP A 163 18905 19902 16576 -4091 2328 -464 C
ATOM 1164 N ALA A 164 -17.847 14.523 49.595 1.00117.28 N
ANISOU 1164 N ALA A 164 13888 16083 14591 -1744 615 -798 N
ATOM 1165 CA ALA A 164 -16.643 15.167 50.119 1.00114.59 C
ANISOU 1165 CA ALA A 164 13918 15612 14010 -1493 452 -600 C
ATOM 1166 C ALA A 164 -16.147 16.267 49.188 1.00107.68 C
ANISOU 1166 C ALA A 164 12690 14929 13293 -900 306 -722 C
ATOM 1167 O ALA A 164 -15.762 17.351 49.644 1.00110.25 O
ANISOU 1167 O ALA A 164 13060 15348 13482 -718 408 -707 O
ATOM 1168 CB ALA A 164 -15.545 14.126 50.344 1.00116.37 C
ANISOU 1168 CB ALA A 164 14693 15366 14158 -1552 18 -322 C
ATOM 1169 N TRP A 165 -16.152 16.006 47.881 1.00107.35 N
ANISOU 1169 N TRP A 165 12325 14944 13517 -626 65 -845 N
ATOM 1170 CA TRP A 165 -15.709 17.005 46.914 1.00 98.58 C
ANISOU 1170 CA TRP A 165 10931 14022 12503 -129 -76 -920 C
ATOM 1171 C TRP A 165 -16.613 18.233 46.937 1.00 98.53 C
ANISOU 1171 C TRP A 165 10545 14328 12564 -6 207 -1074 C
ATOM 1172 O TRP A 165 -16.133 19.373 46.963 1.00 94.79 O
ANISOU 1172 O TRP A 165 10062 13906 12046 281 210 -1036 O
ATOM 1173 CB TRP A 165 -15.675 16.383 45.517 1.00 95.19 C
ANISOU 1173 CB TRP A 165 10256 13638 12274 55 -362 -1045 C
ATOM 1174 CG TRP A 165 -15.101 17.269 44.455 1.00 96.14 C
ANISOU 1174 CG TRP A 165 10178 13940 12409 495 -528 -1076 C
ATOM 1175 CD1 TRP A 165 -13.814 17.279 44.001 1.00 94.27 C
ANISOU 1175 CD1 TRP A 165 10102 13602 12114 720 -762 -1016 C
ATOM 1176 CD2 TRP A 165 -15.796 18.276 43.711 1.00 99.57 C
ANISOU 1176 CD2 TRP A 165 10229 14682 12921 733 -481 -1173 C
ATOM 1177 NE1 TRP A 165 -13.666 18.228 43.019 1.00 94.95 N
ANISOU 1177 NE1 TRP A 165 9962 13933 12180 1024 -812 -1044 N
ATOM 1178 CE2 TRP A 165 -14.869 18.855 42.824 1.00101.55 C
ANISOU 1178 CE2 TRP A 165 10496 14994 13093 1052 -681 -1109 C
ATOM 1179 CE3 TRP A 165 -17.114 18.744 43.709 1.00 87.53 C
ANISOU 1179 CE3 TRP A 165 8338 13374 11544 705 -310 -1322 C
ATOM 1180 CZ2 TRP A 165 -15.216 19.877 41.946 1.00100.08 C
ANISOU 1180 CZ2 TRP A 165 10058 15045 12924 1320 -744 -1115 C
ATOM 1181 CZ3 TRP A 165 -17.456 19.759 42.838 1.00 81.01 C
ANISOU 1181 CZ3 TRP A 165 7214 12765 10800 1038 -422 -1365 C
ATOM 1182 CH2 TRP A 165 -16.511 20.315 41.967 1.00 77.97 C
ANISOU 1182 CH2 TRP A 165 6937 12402 10285 1331 -652 -1226 C
ATOM 1183 N GLU A 166 -17.931 18.018 46.934 1.00105.30 N
ANISOU 1183 N GLU A 166 11061 15371 13576 -221 434 -1278 N
ATOM 1184 CA GLU A 166 -18.869 19.134 46.842 1.00 97.24 C
ANISOU 1184 CA GLU A 166 9584 14634 12728 -47 641 -1501 C
ATOM 1185 C GLU A 166 -18.956 19.901 48.157 1.00103.75 C
ANISOU 1185 C GLU A 166 10548 15478 13396 -192 1008 -1533 C
ATOM 1186 O GLU A 166 -18.901 21.137 48.168 1.00102.79 O
ANISOU 1186 O GLU A 166 10276 15433 13347 123 1044 -1605 O
ATOM 1187 CB GLU A 166 -20.250 18.619 46.430 1.00 90.83 C
ANISOU 1187 CB GLU A 166 8292 14031 12187 -232 752 -1781 C
ATOM 1188 CG GLU A 166 -21.391 19.609 46.601 1.00107.15 C
ANISOU 1188 CG GLU A 166 9839 16372 14501 -130 1009 -2093 C
ATOM 1189 CD GLU A 166 -21.314 20.777 45.638 1.00106.50 C
ANISOU 1189 CD GLU A 166 9482 16378 14603 442 710 -2114 C
ATOM 1190 OE1 GLU A 166 -20.538 20.706 44.662 1.00 99.09 O
ANISOU 1190 OE1 GLU A 166 8699 15366 13584 703 332 -1912 O
ATOM 1191 OE2 GLU A 166 -22.041 21.768 45.857 1.00102.78 O1-
ANISOU 1191 OE2 GLU A 166 8645 16044 14363 618 854 -2346 O1-
ATOM 1192 N SER A 167 -19.099 19.185 49.276 1.00105.73 N
ANISOU 1192 N SER A 167 11110 15649 13414 -690 1278 -1485 N
ATOM 1193 CA SER A 167 -19.313 19.852 50.558 1.00106.41 C
ANISOU 1193 CA SER A 167 11319 15822 13289 -904 1684 -1579 C
ATOM 1194 C SER A 167 -18.122 20.719 50.943 1.00107.48 C
ANISOU 1194 C SER A 167 11802 15812 13225 -624 1537 -1407 C
ATOM 1195 O SER A 167 -18.293 21.792 51.534 1.00107.31 O
ANISOU 1195 O SER A 167 11683 15906 13184 -533 1778 -1584 O
ATOM 1196 CB SER A 167 -19.600 18.819 51.648 1.00112.96 C
ANISOU 1196 CB SER A 167 12527 16587 13804 -1562 1970 -1492 C
ATOM 1197 OG SER A 167 -20.747 18.049 51.332 1.00111.31 O
ANISOU 1197 OG SER A 167 11965 16516 13810 -1879 2154 -1683 O
ATOM 1198 N TRP A 168 -16.906 20.272 50.619 1.00103.78 N
ANISOU 1198 N TRP A 168 11704 15083 12643 -487 1142 -1113 N
ATOM 1199 CA TRP A 168 -15.730 21.096 50.882 1.00104.32 C
ANISOU 1199 CA TRP A 168 12038 15021 12578 -216 975 -983 C
ATOM 1200 C TRP A 168 -15.799 22.416 50.124 1.00104.65 C
ANISOU 1200 C TRP A 168 11690 15184 12889 247 937 -1119 C
ATOM 1201 O TRP A 168 -15.434 23.467 50.660 1.00117.64 O
ANISOU 1201 O TRP A 168 13406 16809 14482 382 1024 -1165 O
ATOM 1202 CB TRP A 168 -14.456 20.341 50.510 1.00101.78 C
ANISOU 1202 CB TRP A 168 12060 14424 12188 -122 543 -722 C
ATOM 1203 CG TRP A 168 -13.219 21.160 50.702 1.00 97.98 C
ANISOU 1203 CG TRP A 168 11781 13824 11622 145 361 -628 C
ATOM 1204 CD1 TRP A 168 -12.423 21.679 49.725 1.00 92.35 C
ANISOU 1204 CD1 TRP A 168 10917 13090 11081 528 116 -602 C
ATOM 1205 CD2 TRP A 168 -12.636 21.561 51.948 1.00101.53 C
ANISOU 1205 CD2 TRP A 168 12616 14178 11781 8 420 -568 C
ATOM 1206 NE1 TRP A 168 -11.381 22.377 50.283 1.00101.26 N
ANISOU 1206 NE1 TRP A 168 12278 14101 12095 633 30 -541 N
ATOM 1207 CE2 TRP A 168 -11.488 22.319 51.647 1.00104.62 C
ANISOU 1207 CE2 TRP A 168 13032 14476 12242 340 187 -526 C
ATOM 1208 CE3 TRP A 168 -12.970 21.350 53.290 1.00105.09 C
ANISOU 1208 CE3 TRP A 168 13411 14634 11883 -400 654 -554 C
ATOM 1209 CZ2 TRP A 168 -10.674 22.868 52.634 1.00 99.22 C
ANISOU 1209 CZ2 TRP A 168 12668 13689 11342 310 143 -495 C
ATOM 1210 CZ3 TRP A 168 -12.159 21.896 54.269 1.00102.86 C
ANISOU 1210 CZ3 TRP A 168 13490 14268 11326 -427 602 -506 C
ATOM 1211 CH2 TRP A 168 -11.026 22.647 53.936 1.00101.23 C
ANISOU 1211 CH2 TRP A 168 13265 13954 11246 -57 331 -489 C
ATOM 1212 N ARG A 169 -16.264 22.382 48.876 1.00 87.61 N
ANISOU 1212 N ARG A 169 9147 13129 11011 483 776 -1177 N
ATOM 1213 CA ARG A 169 -16.330 23.591 48.067 1.00 89.54 C
ANISOU 1213 CA ARG A 169 9087 13443 11492 911 662 -1236 C
ATOM 1214 C ARG A 169 -17.558 24.439 48.362 1.00 97.46 C
ANISOU 1214 C ARG A 169 9678 14613 12739 974 928 -1541 C
ATOM 1215 O ARG A 169 -17.615 25.591 47.916 1.00 99.29 O
ANISOU 1215 O ARG A 169 9712 14826 13187 1334 822 -1586 O
ATOM 1216 CB ARG A 169 -16.307 23.230 46.582 1.00 80.13 C
ANISOU 1216 CB ARG A 169 7698 12308 10438 1129 334 -1162 C
ATOM 1217 CG ARG A 169 -14.939 22.828 46.076 1.00 72.64 C
ANISOU 1217 CG ARG A 169 7059 11214 9326 1207 58 -937 C
ATOM 1218 CD ARG A 169 -15.048 21.956 44.843 1.00 86.00 C
ANISOU 1218 CD ARG A 169 8601 12999 11075 1250 -181 -946 C
ATOM 1219 NE ARG A 169 -13.737 21.608 44.309 1.00 89.30 N
ANISOU 1219 NE ARG A 169 9246 13314 11371 1337 -409 -819 N
ATOM 1220 CZ ARG A 169 -12.943 20.678 44.820 1.00 90.67 C
ANISOU 1220 CZ ARG A 169 9706 13293 11453 1172 -479 -774 C
ATOM 1221 NH1 ARG A 169 -13.298 19.973 45.882 1.00 86.01 N
ANISOU 1221 NH1 ARG A 169 9299 12567 10813 874 -357 -770 N
ATOM 1222 NH2 ARG A 169 -11.767 20.444 44.247 1.00106.43 N
ANISOU 1222 NH2 ARG A 169 11808 15221 13409 1297 -687 -740 N
ATOM 1223 N SER A 170 -18.533 23.909 49.096 1.00113.88 N
ANISOU 1223 N SER A 170 11617 16840 14812 624 1268 -1766 N
ATOM 1224 CA SER A 170 -19.769 24.629 49.375 1.00121.19 C
ANISOU 1224 CA SER A 170 12053 17962 16033 673 1554 -2158 C
ATOM 1225 C SER A 170 -19.775 25.319 50.730 1.00132.74 C
ANISOU 1225 C SER A 170 13646 19445 17345 512 1949 -2360 C
ATOM 1226 O SER A 170 -20.397 26.375 50.870 1.00140.72 O
ANISOU 1226 O SER A 170 14284 20528 18656 744 2087 -2687 O
ATOM 1227 CB SER A 170 -20.965 23.676 49.297 1.00111.02 C
ANISOU 1227 CB SER A 170 10413 16890 14879 352 1751 -2386 C
ATOM 1228 OG SER A 170 -20.915 22.716 50.338 1.00137.73 O
ANISOU 1228 OG SER A 170 14152 20274 17906 -214 2068 -2331 O
ATOM 1229 N GLU A 171 -19.106 24.749 51.732 1.00133.22 N
ANISOU 1229 N GLU A 171 14232 19434 16952 127 2103 -2194 N
ATOM 1230 CA GLU A 171 -19.070 25.342 53.061 1.00136.99 C
ANISOU 1230 CA GLU A 171 14897 19966 17186 -79 2476 -2392 C
ATOM 1231 C GLU A 171 -17.756 26.043 53.368 1.00122.52 C
ANISOU 1231 C GLU A 171 13490 17901 15160 128 2254 -2185 C
ATOM 1232 O GLU A 171 -17.728 26.918 54.240 1.00127.82 O
ANISOU 1232 O GLU A 171 14210 18604 15753 120 2491 -2421 O
ATOM 1233 CB GLU A 171 -19.342 24.269 54.121 1.00142.03 C
ANISOU 1233 CB GLU A 171 15868 20716 17380 -732 2826 -2370 C
ATOM 1234 CG GLU A 171 -20.768 23.744 54.086 1.00162.55 C
ANISOU 1234 CG GLU A 171 17993 23594 20173 -1040 3199 -2691 C
ATOM 1235 CD GLU A 171 -20.889 22.326 54.602 1.00172.58 C
ANISOU 1235 CD GLU A 171 19648 24862 21062 -1678 3353 -2477 C
ATOM 1236 OE1 GLU A 171 -20.200 21.985 55.587 1.00191.39 O
ANISOU 1236 OE1 GLU A 171 22665 27136 22918 -2026 3410 -2236 O
ATOM 1237 OE2 GLU A 171 -21.675 21.551 54.019 1.00150.82 O1-
ANISOU 1237 OE2 GLU A 171 16575 22190 18538 -1840 3384 -2542 O1-
ATOM 1238 N VAL A 172 -16.681 25.687 52.673 1.00101.07 N
ANISOU 1238 N VAL A 172 11044 14970 12389 301 1821 -1805 N
ATOM 1239 CA VAL A 172 -15.400 26.361 52.818 1.00106.93 C
ANISOU 1239 CA VAL A 172 12107 15498 13022 510 1585 -1634 C
ATOM 1240 C VAL A 172 -15.147 27.334 51.674 1.00102.02 C
ANISOU 1240 C VAL A 172 11209 14771 12783 1001 1315 -1592 C
ATOM 1241 O VAL A 172 -14.640 28.433 51.894 1.00104.90 O
ANISOU 1241 O VAL A 172 11626 15007 13225 1202 1285 -1645 O
ATOM 1242 CB VAL A 172 -14.265 25.321 52.930 1.00110.22 C
ANISOU 1242 CB VAL A 172 13015 15741 13123 339 1295 -1281 C
ATOM 1243 CG1 VAL A 172 -12.914 26.005 53.081 1.00105.76 C
ANISOU 1243 CG1 VAL A 172 12718 14978 12490 543 1044 -1156 C
ATOM 1244 CG2 VAL A 172 -14.532 24.391 54.100 1.00120.73 C
ANISOU 1244 CG2 VAL A 172 14708 17121 14041 -178 1512 -1257 C
ATOM 1245 N GLY A 173 -15.515 26.956 50.449 1.00101.34 N
ANISOU 1245 N GLY A 173 12401 13929 12176 897 1111 -1963 N
ATOM 1246 CA GLY A 173 -15.282 27.838 49.317 1.00106.49 C
ANISOU 1246 CA GLY A 173 13063 14406 12994 1081 922 -1954 C
ATOM 1247 C GLY A 173 -16.155 29.078 49.344 1.00102.25 C
ANISOU 1247 C GLY A 173 12368 13872 12611 1314 934 -2136 C
ATOM 1248 O GLY A 173 -15.706 30.172 48.989 1.00 97.46 O
ANISOU 1248 O GLY A 173 11857 13078 12096 1475 801 -2161 O
ATOM 1249 N LYS A 174 -17.411 28.929 49.771 1.00107.84 N
ANISOU 1249 N LYS A 174 12825 14789 13362 1336 1088 -2268 N
ATOM 1250 CA LYS A 174 -18.345 30.050 49.726 1.00100.85 C
ANISOU 1250 CA LYS A 174 11741 13912 12665 1588 1089 -2463 C
ATOM 1251 C LYS A 174 -17.995 31.111 50.763 1.00114.05 C
ANISOU 1251 C LYS A 174 13529 15514 14290 1718 1169 -2657 C
ATOM 1252 O LYS A 174 -18.168 32.310 50.512 1.00112.03 O
ANISOU 1252 O LYS A 174 13249 15101 14217 1960 1062 -2780 O
ATOM 1253 CB LYS A 174 -19.772 29.542 49.922 1.00101.33 C
ANISOU 1253 CB LYS A 174 11466 14250 12786 1566 1246 -2566 C
ATOM 1254 CG LYS A 174 -20.288 28.726 48.748 1.00103.07 C
ANISOU 1254 CG LYS A 174 11535 14514 13111 1484 1123 -2414 C
ATOM 1255 CD LYS A 174 -21.785 28.492 48.837 1.00115.47 C
ANISOU 1255 CD LYS A 174 12729 16344 14799 1505 1244 -2539 C
ATOM 1256 CE LYS A 174 -22.274 27.686 47.645 1.00118.38 C
ANISOU 1256 CE LYS A 174 12959 16750 15270 1411 1095 -2393 C
ATOM 1257 NZ LYS A 174 -23.747 27.473 47.676 1.00107.84 N
ANISOU 1257 NZ LYS A 174 11229 15677 14070 1423 1192 -2511 N
ATOM 1258 N GLN A 175 -17.507 30.692 51.936 1.00116.70 N
ANISOU 1258 N GLN A 175 14000 15957 14384 1556 1338 -2688 N
ATOM 1259 CA GLN A 175 -16.994 31.655 52.906 1.00109.30 C
ANISOU 1259 CA GLN A 175 13219 14944 13367 1651 1391 -2869 C
ATOM 1260 C GLN A 175 -15.854 32.472 52.314 1.00106.76 C
ANISOU 1260 C GLN A 175 13143 14295 13126 1737 1154 -2782 C
ATOM 1261 O GLN A 175 -15.749 33.680 52.559 1.00107.43 O
ANISOU 1261 O GLN A 175 13287 14221 13311 1924 1100 -2952 O
ATOM 1262 CB GLN A 175 -16.516 30.938 54.169 1.00106.97 C
ANISOU 1262 CB GLN A 175 13063 14822 12759 1419 1574 -2861 C
ATOM 1263 CG GLN A 175 -17.587 30.202 54.947 1.00115.61 C
ANISOU 1263 CG GLN A 175 13937 16264 13726 1292 1834 -2946 C
ATOM 1264 CD GLN A 175 -17.049 29.624 56.242 1.00118.03 C
ANISOU 1264 CD GLN A 175 14419 16730 13698 1058 1991 -2920 C
ATOM 1265 OE1 GLN A 175 -16.319 30.291 56.976 1.00115.17 O
ANISOU 1265 OE1 GLN A 175 14256 16297 13208 1095 1989 -3028 O
ATOM 1266 NE2 GLN A 175 -17.403 28.377 56.527 1.00124.81 N
ANISOU 1266 NE2 GLN A 175 15213 17799 14410 802 2108 -2766 N
ATOM 1267 N LEU A 176 -14.993 31.829 51.524 1.00 91.04 N
ANISOU 1267 N LEU A 176 11289 12200 11100 1598 1010 -2526 N
ATOM 1268 CA LEU A 176 -13.819 32.477 50.959 1.00 89.73 C
ANISOU 1268 CA LEU A 176 11348 11768 10977 1626 804 -2414 C
ATOM 1269 C LEU A 176 -14.138 33.358 49.760 1.00 87.39 C
ANISOU 1269 C LEU A 176 10985 11289 10932 1813 603 -2379 C
ATOM 1270 O LEU A 176 -13.286 34.162 49.364 1.00 88.92 O
ANISOU 1270 O LEU A 176 11354 11251 11182 1853 434 -2312 O
ATOM 1271 CB LEU A 176 -12.793 31.418 50.548 1.00 83.26 C
ANISOU 1271 CB LEU A 176 10669 10942 10024 1413 741 -2174 C
ATOM 1272 CG LEU A 176 -12.285 30.516 51.673 1.00 87.38 C
ANISOU 1272 CG LEU A 176 11300 11598 10305 1216 880 -2153 C
ATOM 1273 CD1 LEU A 176 -11.585 29.287 51.111 1.00 78.01 C
ANISOU 1273 CD1 LEU A 176 10178 10412 9052 1039 811 -1930 C
ATOM 1274 CD2 LEU A 176 -11.371 31.288 52.609 1.00 99.44 C
ANISOU 1274 CD2 LEU A 176 13034 13028 11722 1221 872 -2243 C
ATOM 1275 N ARG A 177 -15.331 33.232 49.177 1.00 92.84 N
ANISOU 1275 N ARG A 177 11426 12078 11772 1914 603 -2409 N
ATOM 1276 CA ARG A 177 -15.624 33.953 47.939 1.00 94.61 C
ANISOU 1276 CA ARG A 177 11593 12136 12219 2070 377 -2327 C
ATOM 1277 C ARG A 177 -15.621 35.469 48.110 1.00 91.15 C
ANISOU 1277 C ARG A 177 11219 11454 11960 2297 262 -2464 C
ATOM 1278 O ARG A 177 -14.908 36.145 47.349 1.00 87.70 O
ANISOU 1278 O ARG A 177 10945 10779 11598 2316 45 -2315 O
ATOM 1279 CB ARG A 177 -16.946 33.453 47.347 1.00 88.31 C
ANISOU 1279 CB ARG A 177 10496 11517 11542 2125 391 -2338 C
ATOM 1280 CG ARG A 177 -17.379 34.216 46.109 1.00 98.47 C
ANISOU 1280 CG ARG A 177 11706 12652 13058 2298 138 -2254 C
ATOM 1281 CD ARG A 177 -16.276 34.240 45.060 1.00 98.97 C
ANISOU 1281 CD ARG A 177 11992 12554 13057 2185 -65 -1996 C
ATOM 1282 NE ARG A 177 -16.619 35.112 43.944 1.00118.43 N
ANISOU 1282 NE ARG A 177 14422 14859 15716 2337 -325 -1893 N
ATOM 1283 CZ ARG A 177 -17.071 34.686 42.773 1.00116.08 C
ANISOU 1283 CZ ARG A 177 14014 14644 15448 2307 -462 -1743 C
ATOM 1284 NH1 ARG A 177 -17.212 33.396 42.514 1.00113.42 N
ANISOU 1284 NH1 ARG A 177 13591 14529 14973 2132 -367 -1694 N
ATOM 1285 NH2 ARG A 177 -17.390 35.576 41.837 1.00107.22 N
ANISOU 1285 NH2 ARG A 177 12874 13368 14496 2449 -717 -1639 N
ATOM 1286 N PRO A 178 -16.366 36.070 49.047 1.00 94.66 N
ANISOU 1286 N PRO A 178 11546 11936 12485 2468 388 -2744 N
ATOM 1287 CA PRO A 178 -16.287 37.535 49.177 1.00 97.88 C
ANISOU 1287 CA PRO A 178 12040 12056 13092 2694 248 -2888 C
ATOM 1288 C PRO A 178 -14.920 38.014 49.622 1.00 98.99 C
ANISOU 1288 C PRO A 178 12501 11996 13116 2589 190 -2851 C
ATOM 1289 O PRO A 178 -14.486 39.098 49.211 1.00105.81 O
ANISOU 1289 O PRO A 178 13508 12551 14144 2690 -25 -2815 O
ATOM 1290 CB PRO A 178 -17.365 37.856 50.220 1.00106.84 C
ANISOU 1290 CB PRO A 178 12959 13340 14294 2879 449 -3242 C
ATOM 1291 CG PRO A 178 -17.490 36.614 51.014 1.00104.73 C
ANISOU 1291 CG PRO A 178 12619 13423 13750 2662 729 -3266 C
ATOM 1292 CD PRO A 178 -17.286 35.491 50.044 1.00 96.23 C
ANISOU 1292 CD PRO A 178 11532 12434 12596 2459 662 -2956 C
ATOM 1293 N LEU A 179 -14.226 37.229 50.448 1.00101.19 N
ANISOU 1293 N LEU A 179 12894 12435 13120 2378 360 -2846 N
ATOM 1294 CA LEU A 179 -12.881 37.598 50.877 1.00 97.06 C
ANISOU 1294 CA LEU A 179 12656 11748 12475 2258 296 -2802 C
ATOM 1295 C LEU A 179 -11.913 37.605 49.701 1.00 95.05 C
ANISOU 1295 C LEU A 179 12544 11323 12246 2142 77 -2494 C
ATOM 1296 O LEU A 179 -11.125 38.543 49.537 1.00 90.87 O
ANISOU 1296 O LEU A 179 12200 10534 11793 2150 -91 -2452 O
ATOM 1297 CB LEU A 179 -12.401 36.638 51.965 1.00 88.65 C
ANISOU 1297 CB LEU A 179 11661 10917 11107 2053 505 -2834 C
ATOM 1298 CG LEU A 179 -13.207 36.640 53.263 1.00 89.67 C
ANISOU 1298 CG LEU A 179 11679 11254 11136 2116 746 -3137 C
ATOM 1299 CD1 LEU A 179 -12.925 35.380 54.059 1.00 98.63 C
ANISOU 1299 CD1 LEU A 179 12844 12667 11962 1871 935 -3068 C
ATOM 1300 CD2 LEU A 179 -12.894 37.882 54.086 1.00 94.91 C
ANISOU 1300 CD2 LEU A 179 12488 11737 11838 2243 717 -3396 C
ATOM 1301 N TYR A 180 -11.958 36.559 48.868 1.00 85.21 N
ANISOU 1301 N TYR A 180 11213 10231 10933 2020 78 -2286 N
ATOM 1302 CA TYR A 180 -11.045 36.488 47.732 1.00 77.73 C
ANISOU 1302 CA TYR A 180 10381 9177 9975 1899 -102 -2014 C
ATOM 1303 C TYR A 180 -11.263 37.638 46.759 1.00 86.14 C
ANISOU 1303 C TYR A 180 11462 9999 11268 2039 -338 -1931 C
ATOM 1304 O TYR A 180 -10.321 38.055 46.077 1.00 89.69 O
ANISOU 1304 O TYR A 180 12068 10296 11713 1941 -500 -1740 O
ATOM 1305 CB TYR A 180 -11.190 35.154 47.001 1.00 74.63 C
ANISOU 1305 CB TYR A 180 9876 9001 9478 1768 -54 -1854 C
ATOM 1306 CG TYR A 180 -9.939 34.770 46.244 1.00 73.89 C
ANISOU 1306 CG TYR A 180 9922 8880 9273 1588 -152 -1630 C
ATOM 1307 CD1 TYR A 180 -8.872 34.162 46.889 1.00 77.01 C
ANISOU 1307 CD1 TYR A 180 10441 9328 9492 1427 -72 -1608 C
ATOM 1308 CD2 TYR A 180 -9.811 35.057 44.892 1.00 77.61 C
ANISOU 1308 CD2 TYR A 180 10395 9283 9811 1580 -330 -1445 C
ATOM 1309 CE1 TYR A 180 -7.722 33.823 46.201 1.00 75.00 C
ANISOU 1309 CE1 TYR A 180 10279 9066 9153 1281 -153 -1432 C
ATOM 1310 CE2 TYR A 180 -8.665 34.726 44.197 1.00 80.79 C
ANISOU 1310 CE2 TYR A 180 10902 9698 10096 1413 -395 -1265 C
ATOM 1311 CZ TYR A 180 -7.624 34.110 44.856 1.00 76.78 C
ANISOU 1311 CZ TYR A 180 10489 9247 9436 1272 -300 -1271 C
ATOM 1312 OH TYR A 180 -6.481 33.780 44.165 1.00 79.08 O
ANISOU 1312 OH TYR A 180 10850 9570 9626 1122 -357 -1117 O
ATOM 1313 N GLU A 181 -12.488 38.160 46.676 1.00 96.67 N
ANISOU 1313 N GLU A 181 12628 11296 12805 2262 -368 -2062 N
ATOM 1314 CA GLU A 181 -12.735 39.309 45.810 1.00104.06 C
ANISOU 1314 CA GLU A 181 13589 11965 13982 2412 -627 -1975 C
ATOM 1315 C GLU A 181 -12.033 40.554 46.336 1.00110.28 C
ANISOU 1315 C GLU A 181 14594 12439 14869 2461 -739 -2052 C
ATOM 1316 O GLU A 181 -11.435 41.311 45.561 1.00110.26 O
ANISOU 1316 O GLU A 181 14743 12196 14955 2419 -969 -1853 O
ATOM 1317 CB GLU A 181 -14.236 39.559 45.673 1.00101.96 C
ANISOU 1317 CB GLU A 181 13069 11734 13939 2664 -644 -2120 C
ATOM 1318 CG GLU A 181 -14.987 38.459 44.949 1.00105.86 C
ANISOU 1318 CG GLU A 181 13343 12503 14376 2612 -594 -2017 C
ATOM 1319 CD GLU A 181 -16.477 38.721 44.880 1.00115.50 C
ANISOU 1319 CD GLU A 181 14279 13777 15828 2861 -612 -2175 C
ATOM 1320 OE1 GLU A 181 -16.952 39.648 45.570 1.00125.41 O
ANISOU 1320 OE1 GLU A 181 15489 14889 17272 3087 -610 -2412 O
ATOM 1321 OE2 GLU A 181 -17.173 38.003 44.132 1.00108.80 O1-
ANISOU 1321 OE2 GLU A 181 13242 13117 14982 2835 -633 -2079 O1-
ATOM 1322 N GLU A 182 -12.097 40.784 47.649 1.00110.33 N
ANISOU 1322 N GLU A 182 14621 12449 14850 2531 -582 -2340 N
ATOM 1323 CA GLU A 182 -11.402 41.923 48.237 1.00102.87 C
ANISOU 1323 CA GLU A 182 13891 11206 13988 2563 -685 -2449 C
ATOM 1324 C GLU A 182 -9.896 41.695 48.273 1.00 92.11 C
ANISOU 1324 C GLU A 182 12753 9824 12422 2286 -709 -2269 C
ATOM 1325 O GLU A 182 -9.121 42.654 48.166 1.00 89.40 O
ANISOU 1325 O GLU A 182 12605 9194 12169 2243 -890 -2207 O
ATOM 1326 CB GLU A 182 -11.939 42.187 49.642 1.00100.73 C
ANISOU 1326 CB GLU A 182 13568 10987 13718 2714 -498 -2842 C
ATOM 1327 CG GLU A 182 -11.674 43.585 50.165 1.00109.44 C
ANISOU 1327 CG GLU A 182 14841 11732 15010 2851 -641 -3039 C
ATOM 1328 CD GLU A 182 -12.272 43.803 51.539 1.00114.03 C
ANISOU 1328 CD GLU A 182 15350 12410 15565 3010 -434 -3468 C
ATOM 1329 OE1 GLU A 182 -13.014 42.914 52.009 1.00114.86 O
ANISOU 1329 OE1 GLU A 182 15249 12867 15525 3022 -183 -3589 O
ATOM 1330 OE2 GLU A 182 -12.008 44.861 52.147 1.00120.84 O1-
ANISOU 1330 OE2 GLU A 182 16363 13005 16548 3111 -520 -3689 O1-
ATOM 1331 N TYR A 183 -9.470 40.439 48.426 1.00 82.87 N
ANISOU 1331 N TYR A 183 11550 8944 10994 2097 -540 -2185 N
ATOM 1332 CA TYR A 183 -8.053 40.101 48.341 1.00 85.04 C
ANISOU 1332 CA TYR A 183 11991 9232 11090 1847 -568 -2002 C
ATOM 1333 C TYR A 183 -7.477 40.439 46.970 1.00 89.21 C
ANISOU 1333 C TYR A 183 12583 9627 11684 1748 -781 -1699 C
ATOM 1334 O TYR A 183 -6.315 40.846 46.870 1.00 90.66 O
ANISOU 1334 O TYR A 183 12932 9689 11827 1587 -881 -1578 O
ATOM 1335 CB TYR A 183 -7.880 38.613 48.682 1.00 89.13 C
ANISOU 1335 CB TYR A 183 12428 10076 11360 1703 -365 -1974 C
ATOM 1336 CG TYR A 183 -6.676 37.905 48.094 1.00 89.43 C
ANISOU 1336 CG TYR A 183 12539 10194 11246 1476 -402 -1733 C
ATOM 1337 CD1 TYR A 183 -5.454 37.895 48.755 1.00 88.21 C
ANISOU 1337 CD1 TYR A 183 12534 10021 10962 1323 -400 -1728 C
ATOM 1338 CD2 TYR A 183 -6.779 37.200 46.901 1.00 98.62 C
ANISOU 1338 CD2 TYR A 183 13604 11476 12392 1419 -434 -1533 C
ATOM 1339 CE1 TYR A 183 -4.361 37.229 48.225 1.00 92.69 C
ANISOU 1339 CE1 TYR A 183 13130 10679 11411 1136 -427 -1532 C
ATOM 1340 CE2 TYR A 183 -5.694 36.535 46.365 1.00 98.73 C
ANISOU 1340 CE2 TYR A 183 13660 11582 12270 1231 -451 -1354 C
ATOM 1341 CZ TYR A 183 -4.487 36.550 47.031 1.00 89.84 C
ANISOU 1341 CZ TYR A 183 12662 10433 11039 1098 -444 -1356 C
ATOM 1342 OH TYR A 183 -3.401 35.889 46.507 1.00 85.26 O
ANISOU 1342 OH TYR A 183 12093 9958 10345 930 -458 -1200 O
ATOM 1343 N VAL A 184 -8.278 40.305 45.910 1.00 94.57 N
ANISOU 1343 N VAL A 184 13131 10343 12458 1828 -856 -1572 N
ATOM 1344 CA VAL A 184 -7.803 40.654 44.574 1.00 88.33 C
ANISOU 1344 CA VAL A 184 12405 9457 11701 1723 -1060 -1275 C
ATOM 1345 C VAL A 184 -7.719 42.167 44.397 1.00 88.90 C
ANISOU 1345 C VAL A 184 12623 9154 12001 1800 -1301 -1236 C
ATOM 1346 O VAL A 184 -6.815 42.669 43.716 1.00 91.78 O
ANISOU 1346 O VAL A 184 13131 9388 12352 1630 -1459 -1002 O
ATOM 1347 CB VAL A 184 -8.706 39.999 43.510 1.00 79.72 C
ANISOU 1347 CB VAL A 184 11134 8542 10614 1774 -1080 -1156 C
ATOM 1348 CG1 VAL A 184 -8.402 40.549 42.123 1.00 97.47 C
ANISOU 1348 CG1 VAL A 184 13453 10682 12899 1688 -1316 -857 C
ATOM 1349 CG2 VAL A 184 -8.528 38.489 43.530 1.00 78.89 C
ANISOU 1349 CG2 VAL A 184 10927 8767 10282 1642 -880 -1151 C
ATOM 1350 N VAL A 185 -8.644 42.919 45.001 1.00 95.37 N
ANISOU 1350 N VAL A 185 13405 9790 13040 2051 -1334 -1466 N
ATOM 1351 CA VAL A 185 -8.604 44.378 44.901 1.00101.00 C
ANISOU 1351 CA VAL A 185 14269 10096 14012 2148 -1584 -1455 C
ATOM 1352 C VAL A 185 -7.329 44.920 45.533 1.00109.37 C
ANISOU 1352 C VAL A 185 15555 10985 15015 1971 -1615 -1470 C
ATOM 1353 O VAL A 185 -6.567 45.665 44.904 1.00113.42 O
ANISOU 1353 O VAL A 185 16233 11272 15591 1823 -1826 -1239 O
ATOM 1354 CB VAL A 185 -9.852 45.000 45.553 1.00 99.36 C
ANISOU 1354 CB VAL A 185 13950 9741 14060 2483 -1587 -1768 C
ATOM 1355 CG1 VAL A 185 -9.759 46.521 45.532 1.00102.35 C
ANISOU 1355 CG1 VAL A 185 14504 9647 14737 2598 -1864 -1786 C
ATOM 1356 CG2 VAL A 185 -11.115 44.526 44.856 1.00102.93 C
ANISOU 1356 CG2 VAL A 185 14156 10359 14595 2652 -1587 -1736 C
ATOM 1357 N LEU A 186 -7.079 44.550 46.791 1.00 98.92 N
ANISOU 1357 N LEU A 186 14242 9782 13563 1963 -1413 -1734 N
ATOM 1358 CA LEU A 186 -5.966 45.132 47.533 1.00 95.90 C
ANISOU 1358 CA LEU A 186 14065 9230 13143 1819 -1456 -1799 C
ATOM 1359 C LEU A 186 -4.623 44.673 46.981 1.00 97.95 C
ANISOU 1359 C LEU A 186 14404 9608 13205 1501 -1476 -1510 C
ATOM 1360 O LEU A 186 -3.699 45.482 46.839 1.00104.08 O
ANISOU 1360 O LEU A 186 15352 10156 14040 1344 -1645 -1390 O
ATOM 1361 CB LEU A 186 -6.094 44.779 49.013 1.00 96.23 C
ANISOU 1361 CB LEU A 186 14089 9416 13059 1886 -1235 -2150 C
ATOM 1362 CG LEU A 186 -7.250 45.479 49.729 1.00 88.94 C
ANISOU 1362 CG LEU A 186 13107 8348 12337 2192 -1214 -2500 C
ATOM 1363 CD1 LEU A 186 -7.426 44.933 51.134 1.00106.89 C
ANISOU 1363 CD1 LEU A 186 15337 10866 14411 2223 -952 -2826 C
ATOM 1364 CD2 LEU A 186 -7.029 46.982 49.755 1.00 98.93 C
ANISOU 1364 CD2 LEU A 186 14561 9148 13880 2270 -1472 -2567 C
ATOM 1365 N LYS A 187 -4.495 43.381 46.669 1.00 85.48 N
ANISOU 1365 N LYS A 187 12693 8382 11404 1401 -1309 -1406 N
ATOM 1366 CA LYS A 187 -3.246 42.880 46.106 1.00 89.07 C
ANISOU 1366 CA LYS A 187 13185 8978 11681 1125 -1314 -1161 C
ATOM 1367 C LYS A 187 -2.904 43.584 44.800 1.00102.58 C
ANISOU 1367 C LYS A 187 14962 10533 13481 1007 -1531 -853 C
ATOM 1368 O LYS A 187 -1.729 43.853 44.521 1.00105.25 O
ANISOU 1368 O LYS A 187 15396 10839 13754 771 -1606 -683 O
ATOM 1369 CB LYS A 187 -3.332 41.368 45.893 1.00 83.80 C
ANISOU 1369 CB LYS A 187 12352 8685 10802 1082 -1118 -1124 C
ATOM 1370 CG LYS A 187 -3.142 40.553 47.159 1.00 83.94 C
ANISOU 1370 CG LYS A 187 12348 8881 10663 1076 -922 -1333 C
ATOM 1371 CD LYS A 187 -1.722 40.697 47.668 1.00 93.07 C
ANISOU 1371 CD LYS A 187 13630 10012 11720 874 -955 -1303 C
ATOM 1372 CE LYS A 187 -1.433 39.743 48.810 1.00 88.65 C
ANISOU 1372 CE LYS A 187 13048 9660 10974 842 -787 -1453 C
ATOM 1373 NZ LYS A 187 -0.015 39.854 49.252 1.00 89.03 N
ANISOU 1373 NZ LYS A 187 13198 9698 10933 645 -845 -1410 N
ATOM 1374 N ASN A 188 -3.916 43.896 43.987 1.00104.43 N
ANISOU 1374 N ASN A 188 15138 10682 13857 1156 -1641 -768 N
ATOM 1375 CA ASN A 188 -3.662 44.638 42.757 1.00105.36 C
ANISOU 1375 CA ASN A 188 15340 10640 14051 1037 -1873 -452 C
ATOM 1376 C ASN A 188 -3.302 46.092 43.042 1.00114.00 C
ANISOU 1376 C ASN A 188 16640 11308 15367 1016 -2099 -438 C
ATOM 1377 O ASN A 188 -2.521 46.689 42.294 1.00126.26 O
ANISOU 1377 O ASN A 188 18313 12740 16921 792 -2268 -157 O
ATOM 1378 CB ASN A 188 -4.872 44.559 41.828 1.00112.11 C
ANISOU 1378 CB ASN A 188 16078 11524 14996 1206 -1957 -356 C
ATOM 1379 CG ASN A 188 -4.822 43.354 40.911 1.00108.20 C
ANISOU 1379 CG ASN A 188 15441 11411 14261 1089 -1840 -200 C
ATOM 1380 OD1 ASN A 188 -3.755 42.786 40.673 1.00104.54 O
ANISOU 1380 OD1 ASN A 188 14988 11146 13585 856 -1748 -92 O
ATOM 1381 ND2 ASN A 188 -5.976 42.959 40.387 1.00111.85 N
ANISOU 1381 ND2 ASN A 188 15758 11978 14764 1255 -1848 -207 N
ATOM 1382 N GLU A 189 -3.855 46.679 44.108 1.00114.17 N
ANISOU 1382 N GLU A 189 16706 11099 15574 1234 -2107 -742 N
ATOM 1383 CA GLU A 189 -3.459 48.034 44.482 1.00117.82 C
ANISOU 1383 CA GLU A 189 17379 11131 16258 1214 -2325 -774 C
ATOM 1384 C GLU A 189 -2.014 48.072 44.963 1.00117.65 C
ANISOU 1384 C GLU A 189 17478 11131 16091 922 -2295 -742 C
ATOM 1385 O GLU A 189 -1.261 48.987 44.610 1.00111.00 O
ANISOU 1385 O GLU A 189 16802 10026 15347 728 -2504 -550 O
ATOM 1386 CB GLU A 189 -4.386 48.594 45.560 1.00111.32 C
ANISOU 1386 CB GLU A 189 16558 10086 15652 1531 -2317 -1166 C
ATOM 1387 CG GLU A 189 -5.798 48.889 45.094 1.00135.60 C
ANISOU 1387 CG GLU A 189 19519 13042 18961 1840 -2415 -1207 C
ATOM 1388 CD GLU A 189 -6.603 49.643 46.135 1.00144.48 C
ANISOU 1388 CD GLU A 189 20652 13905 20339 2154 -2432 -1612 C
ATOM 1389 OE1 GLU A 189 -6.010 50.092 47.140 1.00132.38 O
ANISOU 1389 OE1 GLU A 189 19260 12230 18810 2110 -2409 -1838 O
ATOM 1390 OE2 GLU A 189 -7.829 49.788 45.947 1.00142.59 O1-
ANISOU 1390 OE2 GLU A 189 20268 13614 20294 2446 -2471 -1722 O1-
ATOM 1391 N MET A 190 -1.610 47.088 45.772 1.00114.97 N
ANISOU 1391 N MET A 190 17055 11102 15525 878 -2052 -915 N
ATOM 1392 CA MET A 190 -0.242 47.054 46.281 1.00117.73 C
ANISOU 1392 CA MET A 190 17493 11503 15738 615 -2030 -898 C
ATOM 1393 C MET A 190 0.770 46.871 45.154 1.00116.25 C
ANISOU 1393 C MET A 190 17292 11449 15427 310 -2086 -528 C
ATOM 1394 O MET A 190 1.855 47.464 45.183 1.00130.81 O
ANISOU 1394 O MET A 190 19250 13172 17282 66 -2199 -416 O
ATOM 1395 CB MET A 190 -0.106 45.942 47.324 1.00109.59 C
ANISOU 1395 CB MET A 190 16362 10792 14486 648 -1775 -1132 C
ATOM 1396 CG MET A 190 1.323 45.529 47.631 1.00107.76 C
ANISOU 1396 CG MET A 190 16150 10726 14067 373 -1732 -1060 C
ATOM 1397 SD MET A 190 1.847 44.081 46.693 1.00120.25 S
ANISOU 1397 SD MET A 190 17536 12749 15405 225 -1575 -818 S
ATOM 1398 CE MET A 190 3.622 44.296 46.731 1.00113.74 C
ANISOU 1398 CE MET A 190 16762 11959 14495 -117 -1650 -672 C
ATOM 1399 N ALA A 191 0.431 46.062 44.145 1.00 95.40 N
ANISOU 1399 N ALA A 191 14506 9076 12665 310 -2006 -346 N
ATOM 1400 CA ALA A 191 1.362 45.806 43.048 1.00106.51 C
ANISOU 1400 CA ALA A 191 15877 10673 13918 26 -2025 -25 C
ATOM 1401 C ALA A 191 1.439 46.982 42.080 1.00109.31 C
ANISOU 1401 C ALA A 191 16369 10747 14417 -108 -2287 271 C
ATOM 1402 O ALA A 191 2.518 47.291 41.562 1.00111.05 O
ANISOU 1402 O ALA A 191 16636 10996 14561 -413 -2354 506 O
ATOM 1403 CB ALA A 191 0.962 44.531 42.305 1.00105.06 C
ANISOU 1403 CB ALA A 191 15501 10874 13543 71 -1854 38 C
ATOM 1404 N ARG A 192 0.308 47.644 41.817 1.00114.07 N
ANISOU 1404 N ARG A 192 17029 11081 15232 107 -2444 274 N
ATOM 1405 CA ARG A 192 0.321 48.812 40.942 1.00113.89 C
ANISOU 1405 CA ARG A 192 17161 10739 15372 -9 -2733 573 C
ATOM 1406 C ARG A 192 1.088 49.966 41.572 1.00115.36 C
ANISOU 1406 C ARG A 192 17552 10543 15736 -155 -2909 555 C
ATOM 1407 O ARG A 192 1.835 50.672 40.884 1.00125.27 O
ANISOU 1407 O ARG A 192 18926 11664 17007 -445 -3085 867 O
ATOM 1408 CB ARG A 192 -1.111 49.229 40.608 1.00122.40 C
ANISOU 1408 CB ARG A 192 18239 11599 16671 296 -2882 554 C
ATOM 1409 CG ARG A 192 -1.732 48.394 39.511 1.00115.23 C
ANISOU 1409 CG ARG A 192 17171 11014 15597 331 -2821 727 C
ATOM 1410 CD ARG A 192 -3.242 48.356 39.608 1.00102.78 C
ANISOU 1410 CD ARG A 192 15498 9350 14203 703 -2857 555 C
ATOM 1411 NE ARG A 192 -3.798 47.355 38.705 1.00118.58 N
ANISOU 1411 NE ARG A 192 17322 11718 16014 728 -2760 665 N
ATOM 1412 CZ ARG A 192 -5.060 46.951 38.718 1.00130.35 C
ANISOU 1412 CZ ARG A 192 18661 13274 17590 1013 -2727 514 C
ATOM 1413 NH1 ARG A 192 -5.939 47.456 39.568 1.00133.82 N
ANISOU 1413 NH1 ARG A 192 19086 13460 18301 1316 -2768 240 N
ATOM 1414 NH2 ARG A 192 -5.448 46.010 37.862 1.00120.11 N
ANISOU 1414 NH2 ARG A 192 17213 12322 16100 990 -2647 621 N
ATOM 1415 N ALA A 193 0.917 50.171 42.880 1.00113.60 N
ANISOU 1415 N ALA A 193 17375 10150 15636 24 -2864 191 N
ATOM 1416 CA ALA A 193 1.698 51.185 43.579 1.00120.52 C
ANISOU 1416 CA ALA A 193 18444 10683 16664 -122 -3020 125 C
ATOM 1417 C ALA A 193 3.183 50.847 43.550 1.00119.51 C
ANISOU 1417 C ALA A 193 18295 10797 16318 -498 -2940 270 C
ATOM 1418 O ALA A 193 4.028 51.740 43.421 1.00128.31 O
ANISOU 1418 O ALA A 193 19556 11674 17524 -768 -3126 440 O
ATOM 1419 CB ALA A 193 1.204 51.329 45.017 1.00113.64 C
ANISOU 1419 CB ALA A 193 17608 9660 15911 149 -2953 -336 C
ATOM 1420 N ASN A 194 3.520 49.563 43.655 1.00113.32 N
ANISOU 1420 N ASN A 194 17318 10480 15260 -523 -2673 210 N
ATOM 1421 CA ASN A 194 4.901 49.113 43.546 1.00117.39 C
ANISOU 1421 CA ASN A 194 17760 11275 15570 -848 -2583 340 C
ATOM 1422 C ASN A 194 5.395 49.084 42.105 1.00118.09 C
ANISOU 1422 C ASN A 194 17792 11539 15536 -1119 -2622 743 C
ATOM 1423 O ASN A 194 6.460 48.510 41.839 1.00119.07 O
ANISOU 1423 O ASN A 194 17792 11989 15460 -1365 -2502 849 O
ATOM 1424 CB ASN A 194 5.050 47.728 44.181 1.00114.55 C
ANISOU 1424 CB ASN A 194 17213 11325 14987 -750 -2306 123 C
ATOM 1425 CG ASN A 194 5.721 47.780 45.535 1.00124.49 C
ANISOU 1425 CG ASN A 194 18522 12540 16240 -783 -2280 -136 C
ATOM 1426 OD1 ASN A 194 6.880 48.177 45.655 1.00149.47 O
ANISOU 1426 OD1 ASN A 194 21723 15678 19392 -1058 -2360 -48 O
ATOM 1427 ND2 ASN A 194 4.989 47.387 46.568 1.00117.88 N
ANISOU 1427 ND2 ASN A 194 17680 11709 15400 -517 -2171 -455 N
ATOM 1428 N HIS A 195 4.626 49.669 41.182 1.00119.72 N
ANISOU 1428 N HIS A 195 18080 11556 15854 -1070 -2788 960 N
ATOM 1429 CA HIS A 195 5.017 49.871 39.785 1.00122.79 C
ANISOU 1429 CA HIS A 195 18464 12062 16129 -1351 -2872 1374 C
ATOM 1430 C HIS A 195 5.073 48.549 39.020 1.00122.65 C
ANISOU 1430 C HIS A 195 18218 12580 15805 -1369 -2628 1434 C
ATOM 1431 O HIS A 195 5.929 48.344 38.158 1.00117.79 O
ANISOU 1431 O HIS A 195 17524 12243 14986 -1670 -2577 1680 O
ATOM 1432 CB HIS A 195 6.338 50.635 39.689 1.00121.05 C
ANISOU 1432 CB HIS A 195 18334 11748 15913 -1758 -2988 1586 C
ATOM 1433 CG HIS A 195 6.313 51.943 40.416 1.00126.05 C
ANISOU 1433 CG HIS A 195 19207 11827 16859 -1758 -3248 1519 C
ATOM 1434 ND1 HIS A 195 7.066 52.177 41.545 1.00141.17 N
ANISOU 1434 ND1 HIS A 195 21166 13631 18842 -1832 -3242 1291 N
ATOM 1435 CD2 HIS A 195 5.612 53.078 40.189 1.00124.03 C
ANISOU 1435 CD2 HIS A 195 19163 11082 16880 -1679 -3537 1633 C
ATOM 1436 CE1 HIS A 195 6.835 53.403 41.979 1.00150.50 C
ANISOU 1436 CE1 HIS A 195 22581 14280 20321 -1807 -3506 1250 C
ATOM 1437 NE2 HIS A 195 5.957 53.972 41.173 1.00140.18 N
ANISOU 1437 NE2 HIS A 195 21380 12722 19161 -1706 -3692 1455 N
ATOM 1438 N TYR A 196 4.145 47.654 39.342 1.00119.07 N
ANISOU 1438 N TYR A 196 17651 12270 15321 -1050 -2476 1193 N
ATOM 1439 CA TYR A 196 3.879 46.438 38.591 1.00114.84 C
ANISOU 1439 CA TYR A 196 16922 12165 14547 -1003 -2285 1220 C
ATOM 1440 C TYR A 196 2.489 46.548 37.974 1.00109.56 C
ANISOU 1440 C TYR A 196 16273 11392 13964 -772 -2390 1277 C
ATOM 1441 O TYR A 196 1.637 47.296 38.459 1.00112.49 O
ANISOU 1441 O TYR A 196 16757 11393 14590 -555 -2545 1180 O
ATOM 1442 CB TYR A 196 3.963 45.201 39.495 1.00115.65 C
ANISOU 1442 CB TYR A 196 16866 12530 14545 -844 -2029 899 C
ATOM 1443 CG TYR A 196 5.372 44.776 39.860 1.00113.78 C
ANISOU 1443 CG TYR A 196 16545 12517 14171 -1071 -1906 869 C
ATOM 1444 CD1 TYR A 196 6.106 43.929 39.038 1.00116.76 C
ANISOU 1444 CD1 TYR A 196 16748 13302 14312 -1245 -1759 981 C
ATOM 1445 CD2 TYR A 196 5.964 45.215 41.039 1.00119.47 C
ANISOU 1445 CD2 TYR A 196 17344 13048 15000 -1103 -1942 707 C
ATOM 1446 CE1 TYR A 196 7.396 43.539 39.377 1.00119.08 C
ANISOU 1446 CE1 TYR A 196 16933 13806 14508 -1430 -1655 939 C
ATOM 1447 CE2 TYR A 196 7.248 44.831 41.384 1.00126.71 C
ANISOU 1447 CE2 TYR A 196 18165 14174 15807 -1304 -1853 682 C
ATOM 1448 CZ TYR A 196 7.960 43.995 40.553 1.00122.47 C
ANISOU 1448 CZ TYR A 196 17437 14036 15060 -1459 -1710 800 C
ATOM 1449 OH TYR A 196 9.237 43.617 40.902 1.00123.45 O
ANISOU 1449 OH TYR A 196 17436 14371 15100 -1638 -1630 761 O
ATOM 1450 N GLU A 197 2.261 45.802 36.889 1.00110.56 N
ANISOU 1450 N GLU A 197 16277 11852 13879 -813 -2312 1420 N
ATOM 1451 CA GLU A 197 0.974 45.879 36.199 1.00123.90 C
ANISOU 1451 CA GLU A 197 17969 13477 15631 -619 -2432 1501 C
ATOM 1452 C GLU A 197 -0.162 45.417 37.104 1.00117.20 C
ANISOU 1452 C GLU A 197 17045 12552 14936 -243 -2350 1164 C
ATOM 1453 O GLU A 197 -1.070 46.188 37.434 1.00118.89 O
ANISOU 1453 O GLU A 197 17342 12424 15408 -26 -2518 1104 O
ATOM 1454 CB GLU A 197 1.000 45.046 34.918 1.00124.02 C
ANISOU 1454 CB GLU A 197 17857 13913 15353 -747 -2344 1677 C
ATOM 1455 CG GLU A 197 2.146 45.351 33.981 1.00130.46 C
ANISOU 1455 CG GLU A 197 18706 14906 15955 -1139 -2370 1991 C
ATOM 1456 CD GLU A 197 2.207 44.376 32.826 1.00133.25 C
ANISOU 1456 CD GLU A 197 18910 15735 15984 -1247 -2233 2083 C
ATOM 1457 OE1 GLU A 197 1.399 43.423 32.809 1.00115.92 O
ANISOU 1457 OE1 GLU A 197 16591 13708 13747 -1018 -2122 1890 O
ATOM 1458 OE2 GLU A 197 3.059 44.562 31.933 1.00139.31 O1-
ANISOU 1458 OE2 GLU A 197 19682 16716 16534 -1571 -2233 2338 O1-
ATOM 1459 N ASP A 198 -0.134 44.149 37.498 1.00111.47 N
ANISOU 1459 N ASP A 198 16152 12144 14056 -166 -2094 943 N
ATOM 1460 CA ASP A 198 -1.099 43.590 38.430 1.00106.10 C
ANISOU 1460 CA ASP A 198 15386 11448 13479 140 -1977 628 C
ATOM 1461 C ASP A 198 -0.364 42.620 39.344 1.00113.50 C
ANISOU 1461 C ASP A 198 16239 12602 14284 105 -1737 409 C
ATOM 1462 O ASP A 198 0.826 42.350 39.163 1.00116.14 O
ANISOU 1462 O ASP A 198 16558 13107 14464 -126 -1669 496 O
ATOM 1463 CB ASP A 198 -2.260 42.910 37.691 1.00109.29 C
ANISOU 1463 CB ASP A 198 15656 12030 13840 301 -1960 636 C
ATOM 1464 CG ASP A 198 -1.788 41.972 36.597 1.00108.60 C
ANISOU 1464 CG ASP A 198 15463 12331 13467 114 -1860 786 C
ATOM 1465 OD1 ASP A 198 -1.341 40.852 36.921 1.00108.65 O
ANISOU 1465 OD1 ASP A 198 15354 12604 13323 89 -1641 630 O
ATOM 1466 OD2 ASP A 198 -1.863 42.358 35.411 1.00110.95 O1-
ANISOU 1466 OD2 ASP A 198 15799 12668 13691 -8 -2009 1055 O1-
ATOM 1467 N TYR A 199 -1.082 42.102 40.345 1.00109.51 N
ANISOU 1467 N TYR A 199 15670 12097 13843 334 -1613 128 N
ATOM 1468 CA TYR A 199 -0.452 41.220 41.324 1.00102.41 C
ANISOU 1468 CA TYR A 199 14713 11368 12829 311 -1416 -68 C
ATOM 1469 C TYR A 199 0.195 40.012 40.660 1.00 93.16 C
ANISOU 1469 C TYR A 199 13407 10558 11431 173 -1274 6 C
ATOM 1470 O TYR A 199 1.206 39.499 41.154 1.00 96.51 O
ANISOU 1470 O TYR A 199 13804 11111 11756 60 -1174 -52 O
ATOM 1471 CB TYR A 199 -1.477 40.774 42.367 1.00 98.93 C
ANISOU 1471 CB TYR A 199 14216 10914 12459 562 -1300 -347 C
ATOM 1472 CG TYR A 199 -0.876 40.075 43.565 1.00 93.53 C
ANISOU 1472 CG TYR A 199 13519 10342 11675 538 -1139 -539 C
ATOM 1473 CD1 TYR A 199 0.263 40.571 44.187 1.00 89.93 C
ANISOU 1473 CD1 TYR A 199 13172 9791 11208 390 -1181 -548 C
ATOM 1474 CD2 TYR A 199 -1.451 38.922 44.080 1.00 94.48 C
ANISOU 1474 CD2 TYR A 199 13522 10662 11713 650 -963 -697 C
ATOM 1475 CE1 TYR A 199 0.814 39.935 45.284 1.00 93.38 C
ANISOU 1475 CE1 TYR A 199 13601 10337 11545 367 -1062 -707 C
ATOM 1476 CE2 TYR A 199 -0.910 38.281 45.176 1.00 85.52 C
ANISOU 1476 CE2 TYR A 199 12391 9623 10478 618 -842 -840 C
ATOM 1477 CZ TYR A 199 0.224 38.788 45.772 1.00 85.46 C
ANISOU 1477 CZ TYR A 199 12492 9526 10452 483 -896 -844 C
ATOM 1478 OH TYR A 199 0.763 38.150 46.866 1.00 92.42 O
ANISOU 1478 OH TYR A 199 13381 10509 11225 449 -801 -972 O
ATOM 1479 N GLY A 200 -0.360 39.552 39.537 1.00 89.41 N
ANISOU 1479 N GLY A 200 12844 10250 10878 184 -1277 120 N
ATOM 1480 CA GLY A 200 0.266 38.462 38.807 1.00 89.94 C
ANISOU 1480 CA GLY A 200 12786 10653 10733 55 -1153 168 C
ATOM 1481 C GLY A 200 1.595 38.857 38.193 1.00 91.09 C
ANISOU 1481 C GLY A 200 12960 10886 10765 -214 -1187 356 C
ATOM 1482 O GLY A 200 2.564 38.094 38.246 1.00 91.14 O
ANISOU 1482 O GLY A 200 12872 11114 10644 -320 -1059 306 O
ATOM 1483 N ASP A 201 1.659 40.049 37.591 1.00 96.51 N
ANISOU 1483 N ASP A 201 13765 11401 11504 -332 -1366 580 N
ATOM 1484 CA ASP A 201 2.930 40.559 37.084 1.00 97.31 C
ANISOU 1484 CA ASP A 201 13896 11571 11506 -624 -1403 777 C
ATOM 1485 C ASP A 201 3.961 40.659 38.200 1.00103.86 C
ANISOU 1485 C ASP A 201 14742 12333 12387 -696 -1351 654 C
ATOM 1486 O ASP A 201 5.144 40.364 37.995 1.00108.01 O
ANISOU 1486 O ASP A 201 15182 13072 12785 -897 -1272 700 O
ATOM 1487 CB ASP A 201 2.725 41.922 36.426 1.00103.21 C
ANISOU 1487 CB ASP A 201 14804 12072 12340 -739 -1638 1051 C
ATOM 1488 CG ASP A 201 4.009 42.494 35.860 1.00106.03 C
ANISOU 1488 CG ASP A 201 15192 12511 12585 -1084 -1679 1288 C
ATOM 1489 OD1 ASP A 201 4.676 41.792 35.071 1.00113.04 O
ANISOU 1489 OD1 ASP A 201 15943 13772 13235 -1248 -1545 1350 O
ATOM 1490 OD2 ASP A 201 4.357 43.641 36.213 1.00102.67 O1-
ANISOU 1490 OD2 ASP A 201 14919 11780 12310 -1196 -1840 1398 O1-
ATOM 1491 N TYR A 202 3.523 41.081 39.389 1.00113.19 N
ANISOU 1491 N TYR A 202 16023 13234 13751 -533 -1398 485 N
ATOM 1492 CA TYR A 202 4.390 41.103 40.562 1.00104.07 C
ANISOU 1492 CA TYR A 202 14890 12022 12632 -580 -1357 337 C
ATOM 1493 C TYR A 202 4.988 39.726 40.832 1.00101.80 C
ANISOU 1493 C TYR A 202 14430 12053 12194 -573 -1164 201 C
ATOM 1494 O TYR A 202 6.207 39.582 40.983 1.00109.78 O
ANISOU 1494 O TYR A 202 15379 13191 13139 -744 -1131 218 O
ATOM 1495 CB TYR A 202 3.587 41.608 41.763 1.00107.46 C
ANISOU 1495 CB TYR A 202 15440 12149 13242 -367 -1411 133 C
ATOM 1496 CG TYR A 202 4.309 41.586 43.089 1.00122.20 C
ANISOU 1496 CG TYR A 202 17344 13964 15124 -389 -1376 -52 C
ATOM 1497 CD1 TYR A 202 5.179 42.607 43.446 1.00127.97 C
ANISOU 1497 CD1 TYR A 202 18194 14496 15933 -569 -1510 0 C
ATOM 1498 CD2 TYR A 202 4.093 40.559 43.999 1.00112.70 C
ANISOU 1498 CD2 TYR A 202 16067 12902 13853 -244 -1225 -271 C
ATOM 1499 CE1 TYR A 202 5.831 42.594 44.663 1.00128.25 C
ANISOU 1499 CE1 TYR A 202 18265 14494 15969 -596 -1497 -175 C
ATOM 1500 CE2 TYR A 202 4.738 40.539 45.218 1.00115.75 C
ANISOU 1500 CE2 TYR A 202 16498 13252 14228 -272 -1212 -425 C
ATOM 1501 CZ TYR A 202 5.605 41.559 45.545 1.00132.81 C
ANISOU 1501 CZ TYR A 202 18770 15232 16459 -444 -1350 -385 C
ATOM 1502 OH TYR A 202 6.251 41.545 46.759 1.00143.04 O
ANISOU 1502 OH TYR A 202 20111 16505 17731 -480 -1355 -544 O
ATOM 1503 N TRP A 203 4.138 38.695 40.877 1.00 83.31 N
ANISOU 1503 N TRP A 203 12003 9837 9812 -376 -1050 68 N
ATOM 1504 CA TRP A 203 4.623 37.337 41.109 1.00 81.04 C
ANISOU 1504 CA TRP A 203 11567 9813 9413 -352 -892 -57 C
ATOM 1505 C TRP A 203 5.578 36.876 40.018 1.00 81.38 C
ANISOU 1505 C TRP A 203 11471 10142 9306 -530 -834 59 C
ATOM 1506 O TRP A 203 6.522 36.130 40.297 1.00 81.12 O
ANISOU 1506 O TRP A 203 11322 10283 9215 -577 -749 -20 O
ATOM 1507 CB TRP A 203 3.455 36.359 41.198 1.00 80.20 C
ANISOU 1507 CB TRP A 203 11403 9770 9301 -138 -799 -189 C
ATOM 1508 CG TRP A 203 2.796 36.311 42.526 1.00 76.51 C
ANISOU 1508 CG TRP A 203 11003 9144 8923 25 -776 -369 C
ATOM 1509 CD1 TRP A 203 3.203 36.930 43.670 1.00 76.02 C
ANISOU 1509 CD1 TRP A 203 11047 8914 8922 11 -821 -451 C
ATOM 1510 CD2 TRP A 203 1.626 35.564 42.865 1.00 74.86 C
ANISOU 1510 CD2 TRP A 203 10752 8962 8731 209 -693 -498 C
ATOM 1511 NE1 TRP A 203 2.342 36.631 44.699 1.00 76.02 N
ANISOU 1511 NE1 TRP A 203 11079 8850 8956 178 -761 -628 N
ATOM 1512 CE2 TRP A 203 1.366 35.792 44.229 1.00 74.17 C
ANISOU 1512 CE2 TRP A 203 10747 8735 8699 296 -677 -652 C
ATOM 1513 CE3 TRP A 203 0.766 34.732 42.143 1.00 74.41 C
ANISOU 1513 CE3 TRP A 203 10592 9043 8639 293 -633 -503 C
ATOM 1514 CZ2 TRP A 203 0.283 35.215 44.888 1.00 70.87 C
ANISOU 1514 CZ2 TRP A 203 10300 8331 8294 452 -585 -795 C
ATOM 1515 CZ3 TRP A 203 -0.308 34.163 42.796 1.00 70.05 C
ANISOU 1515 CZ3 TRP A 203 10010 8480 8124 447 -558 -642 C
ATOM 1516 CH2 TRP A 203 -0.542 34.407 44.155 1.00 69.93 C
ANISOU 1516 CH2 TRP A 203 10069 8344 8158 521 -526 -780 C
ATOM 1517 N ARG A 204 5.343 37.287 38.771 1.00 88.40 N
ANISOU 1517 N ARG A 204 12361 11099 10126 -626 -880 240 N
ATOM 1518 CA ARG A 204 6.232 36.889 37.689 1.00 90.36 C
ANISOU 1518 CA ARG A 204 12471 11662 10200 -810 -806 338 C
ATOM 1519 C ARG A 204 7.599 37.553 37.785 1.00 90.30 C
ANISOU 1519 C ARG A 204 12447 11685 10178 -1056 -835 442 C
ATOM 1520 O ARG A 204 8.521 37.132 37.079 1.00 98.41 O
ANISOU 1520 O ARG A 204 13317 13013 11062 -1210 -741 477 O
ATOM 1521 CB ARG A 204 5.580 37.198 36.337 1.00102.45 C
ANISOU 1521 CB ARG A 204 14025 13276 11626 -870 -859 520 C
ATOM 1522 CG ARG A 204 4.346 36.351 36.060 1.00 88.38 C
ANISOU 1522 CG ARG A 204 12206 11546 9829 -656 -818 408 C
ATOM 1523 CD ARG A 204 3.826 36.529 34.641 1.00 88.79 C
ANISOU 1523 CD ARG A 204 12259 11742 9736 -736 -874 584 C
ATOM 1524 NE ARG A 204 3.211 37.832 34.411 1.00 91.02 N
ANISOU 1524 NE ARG A 204 12706 11764 10114 -768 -1075 800 N
ATOM 1525 CZ ARG A 204 1.942 38.119 34.671 1.00 97.70 C
ANISOU 1525 CZ ARG A 204 13627 12382 11112 -566 -1181 775 C
ATOM 1526 NH1 ARG A 204 1.130 37.228 35.217 1.00 89.85 N
ANISOU 1526 NH1 ARG A 204 12561 11397 10183 -341 -1094 553 N
ATOM 1527 NH2 ARG A 204 1.476 39.329 34.375 1.00 95.52 N
ANISOU 1527 NH2 ARG A 204 13494 11860 10938 -595 -1386 980 N
ATOM 1528 N GLY A 205 7.757 38.555 38.655 1.00 93.09 N
ANISOU 1528 N GLY A 205 12944 11747 10678 -1097 -959 470 N
ATOM 1529 CA GLY A 205 9.030 39.233 38.824 1.00103.11 C
ANISOU 1529 CA GLY A 205 14201 13021 11955 -1347 -1008 566 C
ATOM 1530 C GLY A 205 10.162 38.346 39.304 1.00 99.45 C
ANISOU 1530 C GLY A 205 13547 12796 11444 -1377 -890 420 C
ATOM 1531 O GLY A 205 11.330 38.685 39.087 1.00109.02 O
ANISOU 1531 O GLY A 205 14665 14142 12617 -1614 -891 512 O
ATOM 1532 N ASP A 206 9.849 37.215 39.945 1.00 92.14 N
ANISOU 1532 N ASP A 206 12554 11925 10529 -1149 -798 206 N
ATOM 1533 CA ASP A 206 10.894 36.315 40.424 1.00 91.21 C
ANISOU 1533 CA ASP A 206 12256 12008 10392 -1147 -717 70 C
ATOM 1534 C ASP A 206 11.756 35.766 39.293 1.00 92.64 C
ANISOU 1534 C ASP A 206 12205 12558 10435 -1279 -598 108 C
ATOM 1535 O ASP A 206 12.875 35.306 39.546 1.00101.35 O
ANISOU 1535 O ASP A 206 13129 13839 11540 -1335 -554 31 O
ATOM 1536 CB ASP A 206 10.276 35.156 41.207 1.00 88.42 C
ANISOU 1536 CB ASP A 206 11893 11630 10074 -882 -658 -134 C
ATOM 1537 CG ASP A 206 11.319 34.299 41.898 1.00100.72 C
ANISOU 1537 CG ASP A 206 13297 13322 11649 -860 -626 -262 C
ATOM 1538 OD1 ASP A 206 11.753 34.666 43.011 1.00117.00 O
ANISOU 1538 OD1 ASP A 206 15428 15244 13784 -884 -716 -300 O
ATOM 1539 OD2 ASP A 206 11.714 33.263 41.322 1.00 91.65 O1-
ANISOU 1539 OD2 ASP A 206 11959 12417 10447 -813 -525 -335 O1-
ATOM 1540 N TYR A 207 11.267 35.801 38.058 1.00 82.47 N
ANISOU 1540 N TYR A 207 10907 11405 9024 -1328 -550 214 N
ATOM 1541 CA TYR A 207 12.027 35.319 36.916 1.00 82.83 C
ANISOU 1541 CA TYR A 207 10735 11835 8901 -1463 -420 233 C
ATOM 1542 C TYR A 207 12.639 36.448 36.102 1.00 85.18 C
ANISOU 1542 C TYR A 207 11038 12227 9099 -1789 -457 486 C
ATOM 1543 O TYR A 207 13.323 36.179 35.111 1.00 88.57 O
ANISOU 1543 O TYR A 207 11280 13014 9356 -1946 -336 519 O
ATOM 1544 CB TYR A 207 11.135 34.453 36.022 1.00 79.82 C
ANISOU 1544 CB TYR A 207 10322 11604 8403 -1318 -330 162 C
ATOM 1545 CG TYR A 207 10.561 33.251 36.738 1.00 77.96 C
ANISOU 1545 CG TYR A 207 10067 11291 8262 -1028 -290 -74 C
ATOM 1546 CD1 TYR A 207 9.403 33.360 37.495 1.00 76.52 C
ANISOU 1546 CD1 TYR A 207 10070 10809 8196 -855 -372 -97 C
ATOM 1547 CD2 TYR A 207 11.189 32.015 36.674 1.00 77.70 C
ANISOU 1547 CD2 TYR A 207 9827 11484 8212 -933 -175 -273 C
ATOM 1548 CE1 TYR A 207 8.877 32.271 38.156 1.00 74.05 C
ANISOU 1548 CE1 TYR A 207 9744 10436 7957 -630 -334 -284 C
ATOM 1549 CE2 TYR A 207 10.670 30.918 37.334 1.00 75.23 C
ANISOU 1549 CE2 TYR A 207 9517 11070 7998 -690 -162 -460 C
ATOM 1550 CZ TYR A 207 9.515 31.053 38.073 1.00 73.18 C
ANISOU 1550 CZ TYR A 207 9450 10524 7830 -557 -239 -450 C
ATOM 1551 OH TYR A 207 8.994 29.965 38.732 1.00 70.90 O
ANISOU 1551 OH TYR A 207 9166 10147 7626 -352 -224 -609 O
ATOM 1552 N GLU A 208 12.421 37.698 36.501 1.00 85.84 N
ANISOU 1552 N GLU A 208 11330 11999 9286 -1903 -621 660 N
ATOM 1553 CA GLU A 208 12.919 38.831 35.738 1.00 87.82 C
ANISOU 1553 CA GLU A 208 11621 12286 9458 -2235 -688 939 C
ATOM 1554 C GLU A 208 14.432 38.962 35.882 1.00 89.56 C
ANISOU 1554 C GLU A 208 11645 12720 9664 -2480 -637 951 C
ATOM 1555 O GLU A 208 15.009 38.668 36.932 1.00 90.75 O
ANISOU 1555 O GLU A 208 11725 12811 9945 -2400 -646 785 O
ATOM 1556 CB GLU A 208 12.231 40.119 36.191 1.00 88.20 C
ANISOU 1556 CB GLU A 208 11961 11884 9669 -2264 -907 1101 C
ATOM 1557 CG GLU A 208 12.583 41.346 35.368 1.00 92.67 C
ANISOU 1557 CG GLU A 208 12618 12417 10176 -2611 -1020 1433 C
ATOM 1558 CD GLU A 208 11.709 42.539 35.698 1.00108.65 C
ANISOU 1558 CD GLU A 208 14942 13957 12385 -2583 -1257 1577 C
ATOM 1559 OE1 GLU A 208 11.027 42.511 36.745 1.00111.63 O
ANISOU 1559 OE1 GLU A 208 15434 14033 12946 -2317 -1321 1388 O
ATOM 1560 OE2 GLU A 208 11.700 43.504 34.905 1.00118.94 O1-
ANISOU 1560 OE2 GLU A 208 16362 15180 13647 -2828 -1384 1878 O1-
ATOM 1561 N VAL A 209 15.074 39.396 34.798 1.00 81.21 N
ANISOU 1561 N VAL A 209 10489 11936 8432 -2792 -583 1155 N
ATOM 1562 CA VAL A 209 16.516 39.621 34.752 1.00 82.83 C
ANISOU 1562 CA VAL A 209 10476 12394 8602 -3078 -522 1200 C
ATOM 1563 C VAL A 209 16.770 40.862 33.909 1.00 85.30 C
ANISOU 1563 C VAL A 209 10884 12715 8809 -3477 -603 1558 C
ATOM 1564 O VAL A 209 16.246 40.975 32.795 1.00110.25 O
ANISOU 1564 O VAL A 209 14102 16012 11777 -3564 -573 1726 O
ATOM 1565 CB VAL A 209 17.273 38.414 34.160 1.00 82.76 C
ANISOU 1565 CB VAL A 209 10116 12895 8433 -3041 -282 1005 C
ATOM 1566 CG1 VAL A 209 18.742 38.752 33.988 1.00 84.71 C
ANISOU 1566 CG1 VAL A 209 10108 13442 8635 -3366 -212 1073 C
ATOM 1567 CG2 VAL A 209 17.100 37.170 35.024 1.00 81.58 C
ANISOU 1567 CG2 VAL A 209 9877 12705 8413 -2661 -231 672 C
ATOM 1568 N ASN A 210 17.574 41.790 34.427 1.00100.69 N
ANISOU 1568 N ASN A 210 12857 14519 10880 -3736 -720 1685 N
ATOM 1569 CA ASN A 210 17.896 43.015 33.711 1.00102.54 C
ANISOU 1569 CA ASN A 210 13194 14725 11042 -4154 -821 2049 C
ATOM 1570 C ASN A 210 19.391 43.299 33.789 1.00103.84 C
ANISOU 1570 C ASN A 210 13112 15147 11195 -4502 -764 2101 C
ATOM 1571 O ASN A 210 20.079 42.856 34.713 1.00115.65 O
ANISOU 1571 O ASN A 210 14440 16674 12826 -4400 -737 1871 O
ATOM 1572 CB ASN A 210 17.116 44.216 34.263 1.00114.45 C
ANISOU 1572 CB ASN A 210 15076 15642 12769 -4155 -1106 2217 C
ATOM 1573 CG ASN A 210 15.630 44.123 33.982 1.00122.30 C
ANISOU 1573 CG ASN A 210 16297 16407 13766 -3870 -1177 2227 C
ATOM 1574 OD1 ASN A 210 15.192 44.237 32.836 1.00117.24 O
ANISOU 1574 OD1 ASN A 210 15699 15912 12934 -3976 -1164 2437 O
ATOM 1575 ND2 ASN A 210 14.845 43.915 35.031 1.00116.34 N
ANISOU 1575 ND2 ASN A 210 15678 15311 13216 -3516 -1256 1999 N
ATOM 1576 N GLY A 211 19.886 44.036 32.794 1.00120.11 N
ANISOU 1576 N GLY A 211 15144 17408 13083 -4927 -751 2419 N
ATOM 1577 CA GLY A 211 21.247 44.533 32.785 1.00123.51 C
ANISOU 1577 CA GLY A 211 15363 18061 13505 -5334 -721 2536 C
ATOM 1578 C GLY A 211 22.333 43.522 32.493 1.00125.23 C
ANISOU 1578 C GLY A 211 15125 18880 13576 -5360 -441 2321 C
ATOM 1579 O GLY A 211 23.507 43.814 32.750 1.00128.66 O
ANISOU 1579 O GLY A 211 15336 19488 14062 -5634 -420 2343 O
ATOM 1580 N VAL A 212 21.994 42.346 31.970 1.00123.74 N
ANISOU 1580 N VAL A 212 14780 19012 13223 -5081 -233 2098 N
ATOM 1581 CA VAL A 212 22.971 41.306 31.652 1.00127.08 C
ANISOU 1581 CA VAL A 212 14759 20001 13524 -5053 35 1847 C
ATOM 1582 C VAL A 212 22.738 40.916 30.197 1.00131.70 C
ANISOU 1582 C VAL A 212 15251 21038 13752 -5149 246 1910 C
ATOM 1583 O VAL A 212 21.803 40.168 29.891 1.00126.11 O
ANISOU 1583 O VAL A 212 14635 20315 12965 -4834 296 1763 O
ATOM 1584 CB VAL A 212 22.857 40.087 32.577 1.00121.34 C
ANISOU 1584 CB VAL A 212 13915 19209 12979 -4570 72 1437 C
ATOM 1585 CG1 VAL A 212 24.084 39.194 32.439 1.00127.13 C
ANISOU 1585 CG1 VAL A 212 14170 20462 13672 -4565 293 1185 C
ATOM 1586 CG2 VAL A 212 22.670 40.523 34.025 1.00120.44 C
ANISOU 1586 CG2 VAL A 212 14017 18567 13179 -4431 -176 1399 C
ATOM 1587 N ASP A 213 23.587 41.417 29.298 1.00145.75 N
ANISOU 1587 N ASP A 213 16843 23235 15301 -5599 372 2126 N
ATOM 1588 CA ASP A 213 23.403 41.192 27.869 1.00154.39 C
ANISOU 1588 CA ASP A 213 17869 24789 16005 -5760 566 2226 C
ATOM 1589 C ASP A 213 23.418 39.704 27.541 1.00141.95 C
ANISOU 1589 C ASP A 213 16008 23612 14315 -5404 821 1799 C
ATOM 1590 O ASP A 213 24.353 38.983 27.901 1.00140.16 O
ANISOU 1590 O ASP A 213 15415 23661 14179 -5296 973 1500 O
ATOM 1591 CB ASP A 213 24.493 41.914 27.077 1.00171.63 C
ANISOU 1591 CB ASP A 213 19840 27416 17956 -6329 688 2500 C
ATOM 1592 CG ASP A 213 24.194 43.388 26.881 1.00175.42 C
ANISOU 1592 CG ASP A 213 20674 27549 18430 -6737 441 3008 C
ATOM 1593 OD1 ASP A 213 24.271 44.150 27.869 1.00181.04 O
ANISOU 1593 OD1 ASP A 213 21561 27770 19458 -6778 198 3111 O
ATOM 1594 OD2 ASP A 213 23.883 43.785 25.739 1.00160.76 O1-
ANISOU 1594 OD2 ASP A 213 18928 25904 16249 -7019 476 3304 O1-
ATOM 1595 N GLY A 214 22.373 39.248 26.850 1.00131.74 N
ANISOU 1595 N GLY A 214 14883 22335 12838 -5218 850 1767 N
ATOM 1596 CA GLY A 214 22.250 37.862 26.461 1.00137.75 C
ANISOU 1596 CA GLY A 214 15424 23428 13487 -4886 1066 1368 C
ATOM 1597 C GLY A 214 21.634 36.953 27.502 1.00132.42 C
ANISOU 1597 C GLY A 214 14820 22370 13122 -4363 975 1041 C
ATOM 1598 O GLY A 214 21.328 35.796 27.185 1.00133.83 O
ANISOU 1598 O GLY A 214 14882 22733 13234 -4063 1112 723 O
ATOM 1599 N TYR A 215 21.439 37.435 28.731 1.00115.73 N
ANISOU 1599 N TYR A 215 12902 19732 11338 -4257 745 1105 N
ATOM 1600 CA TYR A 215 20.877 36.616 29.797 1.00112.04 C
ANISOU 1600 CA TYR A 215 12511 18909 11151 -3796 654 823 C
ATOM 1601 C TYR A 215 19.679 37.268 30.477 1.00113.86 C
ANISOU 1601 C TYR A 215 13166 18543 11554 -3674 395 996 C
ATOM 1602 O TYR A 215 19.245 36.784 31.528 1.00117.97 O
ANISOU 1602 O TYR A 215 13774 18732 12316 -3345 298 808 O
ATOM 1603 CB TYR A 215 21.954 36.282 30.836 1.00114.47 C
ANISOU 1603 CB TYR A 215 12563 19221 11710 -3712 655 620 C
ATOM 1604 CG TYR A 215 22.999 35.319 30.324 1.00115.27 C
ANISOU 1604 CG TYR A 215 12210 19873 11715 -3680 909 334 C
ATOM 1605 CD1 TYR A 215 22.828 33.948 30.455 1.00110.42 C
ANISOU 1605 CD1 TYR A 215 11454 19325 11177 -3274 998 -41 C
ATOM 1606 CD2 TYR A 215 24.148 35.778 29.693 1.00130.93 C
ANISOU 1606 CD2 TYR A 215 13899 22309 13538 -4057 1059 432 C
ATOM 1607 CE1 TYR A 215 23.775 33.060 29.985 1.00110.98 C
ANISOU 1607 CE1 TYR A 215 11101 19877 11188 -3211 1220 -336 C
ATOM 1608 CE2 TYR A 215 25.101 34.897 29.217 1.00134.99 C
ANISOU 1608 CE2 TYR A 215 13968 23350 13973 -4008 1304 137 C
ATOM 1609 CZ TYR A 215 24.909 33.539 29.366 1.00128.52 C
ANISOU 1609 CZ TYR A 215 13015 22567 13251 -3568 1380 -259 C
ATOM 1610 OH TYR A 215 25.855 32.659 28.894 1.00135.26 O
ANISOU 1610 OH TYR A 215 13416 23922 14054 -3489 1613 -584 O
ATOM 1611 N ASP A 216 19.128 38.338 29.907 1.00105.26 N
ANISOU 1611 N ASP A 216 12333 17314 10345 -3926 276 1346 N
ATOM 1612 CA ASP A 216 17.943 38.960 30.474 1.00101.38 C
ANISOU 1612 CA ASP A 216 12224 16269 10028 -3786 32 1486 C
ATOM 1613 C ASP A 216 16.741 38.023 30.373 1.00 99.15 C
ANISOU 1613 C ASP A 216 12038 15903 9733 -3403 51 1286 C
ATOM 1614 O ASP A 216 16.771 36.985 29.705 1.00 98.65 O
ANISOU 1614 O ASP A 216 11784 16201 9498 -3287 238 1079 O
ATOM 1615 CB ASP A 216 17.631 40.282 29.772 1.00101.96 C
ANISOU 1615 CB ASP A 216 12537 16219 9984 -4135 -115 1913 C
ATOM 1616 CG ASP A 216 18.671 41.348 30.043 1.00108.07 C
ANISOU 1616 CG ASP A 216 13282 16950 10831 -4522 -193 2141 C
ATOM 1617 OD1 ASP A 216 19.096 41.481 31.208 1.00125.16 O
ANISOU 1617 OD1 ASP A 216 15433 18860 13260 -4442 -279 2022 O
ATOM 1618 OD2 ASP A 216 19.055 42.063 29.093 1.00114.08 O1-
ANISOU 1618 OD2 ASP A 216 14040 17930 11375 -4924 -177 2451 O1-
ATOM 1619 N TYR A 217 15.665 38.408 31.056 1.00 92.38 N
ANISOU 1619 N TYR A 217 11473 14558 9068 -3210 -146 1337 N
ATOM 1620 CA TYR A 217 14.410 37.669 31.009 1.00 91.40 C
ANISOU 1620 CA TYR A 217 11462 14311 8955 -2877 -158 1188 C
ATOM 1621 C TYR A 217 13.293 38.623 31.397 1.00 91.62 C
ANISOU 1621 C TYR A 217 11823 13851 9138 -2818 -398 1384 C
ATOM 1622 O TYR A 217 13.394 39.313 32.415 1.00 97.11 O
ANISOU 1622 O TYR A 217 12643 14190 10064 -2813 -538 1420 O
ATOM 1623 CB TYR A 217 14.438 36.458 31.950 1.00 90.09 C
ANISOU 1623 CB TYR A 217 11168 14104 8959 -2529 -80 823 C
ATOM 1624 CG TYR A 217 13.420 35.386 31.621 1.00 88.12 C
ANISOU 1624 CG TYR A 217 10931 13894 8656 -2239 -20 628 C
ATOM 1625 CD1 TYR A 217 12.128 35.446 32.126 1.00 86.51 C
ANISOU 1625 CD1 TYR A 217 10958 13322 8592 -2015 -155 628 C
ATOM 1626 CD2 TYR A 217 13.757 34.307 30.814 1.00 88.02 C
ANISOU 1626 CD2 TYR A 217 10688 14292 8463 -2192 172 425 C
ATOM 1627 CE1 TYR A 217 11.196 34.466 31.829 1.00 87.94 C
ANISOU 1627 CE1 TYR A 217 11138 13543 8733 -1776 -107 457 C
ATOM 1628 CE2 TYR A 217 12.833 33.321 30.512 1.00100.96 C
ANISOU 1628 CE2 TYR A 217 12345 15949 10065 -1943 211 238 C
ATOM 1629 CZ TYR A 217 11.554 33.406 31.022 1.00 96.56 C
ANISOU 1629 CZ TYR A 217 12018 15020 9649 -1747 67 267 C
ATOM 1630 OH TYR A 217 10.629 32.430 30.727 1.00 86.08 O
ANISOU 1630 OH TYR A 217 10700 13714 8294 -1525 98 89 O
ATOM 1631 N SER A 218 12.245 38.671 30.584 1.00112.73 N
ANISOU 1631 N SER A 218 14630 16514 11689 -2771 -452 1496 N
ATOM 1632 CA SER A 218 11.110 39.538 30.857 1.00107.95 C
ANISOU 1632 CA SER A 218 14313 15460 11241 -2684 -686 1667 C
ATOM 1633 C SER A 218 10.119 38.843 31.780 1.00101.24 C
ANISOU 1633 C SER A 218 13519 14353 10595 -2283 -705 1401 C
ATOM 1634 O SER A 218 9.999 37.615 31.783 1.00105.64 O
ANISOU 1634 O SER A 218 13927 15113 11100 -2086 -554 1142 O
ATOM 1635 CB SER A 218 10.412 39.941 29.556 1.00113.26 C
ANISOU 1635 CB SER A 218 15097 16239 11697 -2818 -766 1931 C
ATOM 1636 OG SER A 218 9.053 40.272 29.787 1.00106.19 O
ANISOU 1636 OG SER A 218 14415 14969 10964 -2591 -956 1974 O
ATOM 1637 N ARG A 219 9.412 39.647 32.578 1.00 97.70 N
ANISOU 1637 N ARG A 219 13286 13451 10383 -2172 -894 1460 N
ATOM 1638 CA ARG A 219 8.332 39.103 33.396 1.00102.52 C
ANISOU 1638 CA ARG A 219 13957 13829 11166 -1816 -915 1237 C
ATOM 1639 C ARG A 219 7.277 38.429 32.527 1.00109.50 C
ANISOU 1639 C ARG A 219 14823 14862 11921 -1673 -887 1210 C
ATOM 1640 O ARG A 219 6.785 37.346 32.863 1.00109.86 O
ANISOU 1640 O ARG A 219 14783 14966 11993 -1433 -785 962 O
ATOM 1641 CB ARG A 219 7.697 40.209 34.238 1.00107.39 C
ANISOU 1641 CB ARG A 219 14803 13962 12037 -1736 -1123 1310 C
ATOM 1642 CG ARG A 219 8.580 40.746 35.347 1.00 98.51 C
ANISOU 1642 CG ARG A 219 13712 12647 11071 -1817 -1160 1258 C
ATOM 1643 CD ARG A 219 7.769 41.582 36.316 1.00 98.87 C
ANISOU 1643 CD ARG A 219 13970 12223 11373 -1650 -1336 1218 C
ATOM 1644 NE ARG A 219 7.182 42.745 35.661 1.00108.60 N
ANISOU 1644 NE ARG A 219 15387 13209 12668 -1741 -1544 1486 N
ATOM 1645 CZ ARG A 219 7.704 43.964 35.684 1.00118.28 C
ANISOU 1645 CZ ARG A 219 16754 14197 13991 -1971 -1714 1692 C
ATOM 1646 NH1 ARG A 219 8.833 44.220 36.326 1.00111.66 N
ANISOU 1646 NH1 ARG A 219 15887 13348 13192 -2148 -1696 1656 N
ATOM 1647 NH2 ARG A 219 7.077 44.950 35.049 1.00139.14 N
ANISOU 1647 NH2 ARG A 219 19572 16592 16704 -2029 -1927 1946 N
ATOM 1648 N GLY A 220 6.924 39.051 31.401 1.00 97.95 N
ANISOU 1648 N GLY A 220 13442 13460 10314 -1834 -990 1475 N
ATOM 1649 CA GLY A 220 5.938 38.460 30.515 1.00102.37 C
ANISOU 1649 CA GLY A 220 13985 14179 10732 -1723 -988 1462 C
ATOM 1650 C GLY A 220 6.420 37.203 29.818 1.00 97.07 C
ANISOU 1650 C GLY A 220 13100 13969 9812 -1747 -767 1281 C
ATOM 1651 O GLY A 220 5.623 36.299 29.552 1.00111.05 O
ANISOU 1651 O GLY A 220 14820 15836 11539 -1559 -722 1114 O
ATOM 1652 N GLN A 221 7.723 37.121 29.521 1.00 93.63 N
ANISOU 1652 N GLN A 221 12526 13825 9224 -1974 -628 1291 N
ATOM 1653 CA GLN A 221 8.269 35.967 28.809 1.00 98.35 C
ANISOU 1653 CA GLN A 221 12902 14879 9588 -1995 -411 1092 C
ATOM 1654 C GLN A 221 7.981 34.649 29.520 1.00 96.80 C
ANISOU 1654 C GLN A 221 12595 14657 9528 -1680 -302 728 C
ATOM 1655 O GLN A 221 7.990 33.595 28.874 1.00103.75 O
ANISOU 1655 O GLN A 221 13334 15838 10250 -1620 -168 532 O
ATOM 1656 CB GLN A 221 9.780 36.143 28.614 1.00 94.43 C
ANISOU 1656 CB GLN A 221 12242 14670 8968 -2264 -275 1129 C
ATOM 1657 CG GLN A 221 10.442 35.082 27.736 1.00 94.33 C
ANISOU 1657 CG GLN A 221 11979 15172 8691 -2312 -42 924 C
ATOM 1658 CD GLN A 221 10.304 35.377 26.257 1.00134.72 C
ANISOU 1658 CD GLN A 221 17112 20630 13445 -2561 -28 1125 C
ATOM 1659 OE1 GLN A 221 10.100 36.523 25.858 1.00146.62 O
ANISOU 1659 OE1 GLN A 221 18792 22032 14884 -2787 -184 1482 O
ATOM 1660 NE2 GLN A 221 10.414 34.340 25.433 1.00134.28 N
ANISOU 1660 NE2 GLN A 221 16885 20983 13153 -2525 148 896 N
ATOM 1661 N LEU A 222 7.717 34.681 30.829 1.00 95.30 N
ANISOU 1661 N LEU A 222 12476 14114 9620 -1488 -364 631 N
ATOM 1662 CA LEU A 222 7.348 33.459 31.535 1.00 97.11 C
ANISOU 1662 CA LEU A 222 12630 14291 9978 -1209 -285 329 C
ATOM 1663 C LEU A 222 6.063 32.862 30.968 1.00 93.47 C
ANISOU 1663 C LEU A 222 12205 13845 9463 -1057 -313 264 C
ATOM 1664 O LEU A 222 6.024 31.678 30.617 1.00 98.11 O
ANISOU 1664 O LEU A 222 12665 14636 9975 -958 -200 42 O
ATOM 1665 CB LEU A 222 7.209 33.735 33.033 1.00 83.11 C
ANISOU 1665 CB LEU A 222 10953 12147 8479 -1064 -359 278 C
ATOM 1666 CG LEU A 222 6.888 32.489 33.862 1.00 81.05 C
ANISOU 1666 CG LEU A 222 10626 11824 8344 -809 -287 1 C
ATOM 1667 CD1 LEU A 222 8.083 31.547 33.903 1.00 80.29 C
ANISOU 1667 CD1 LEU A 222 10325 11972 8211 -817 -146 -182 C
ATOM 1668 CD2 LEU A 222 6.437 32.857 35.269 1.00 79.92 C
ANISOU 1668 CD2 LEU A 222 10616 11323 8427 -673 -374 -23 C
ATOM 1669 N ILE A 223 5.005 33.676 30.853 1.00 82.33 N
ANISOU 1669 N ILE A 223 10961 12215 8104 -1035 -478 448 N
ATOM 1670 CA ILE A 223 3.737 33.201 30.292 1.00 89.59 C
ANISOU 1670 CA ILE A 223 11904 13154 8983 -904 -531 406 C
ATOM 1671 C ILE A 223 3.962 32.541 28.936 1.00 93.11 C
ANISOU 1671 C ILE A 223 12238 14009 9129 -1021 -441 363 C
ATOM 1672 O ILE A 223 3.480 31.434 28.675 1.00 87.85 O
ANISOU 1672 O ILE A 223 11490 13465 8424 -890 -376 146 O
ATOM 1673 CB ILE A 223 2.725 34.356 30.186 1.00 86.81 C
ANISOU 1673 CB ILE A 223 11726 12541 8716 -898 -746 652 C
ATOM 1674 CG1 ILE A 223 2.610 35.109 31.512 1.00 83.39 C
ANISOU 1674 CG1 ILE A 223 11401 11716 8566 -793 -825 667 C
ATOM 1675 CG2 ILE A 223 1.372 33.826 29.758 1.00 88.20 C
ANISOU 1675 CG2 ILE A 223 11898 12724 8890 -738 -811 586 C
ATOM 1676 CD1 ILE A 223 1.481 36.117 31.530 1.00 84.04 C
ANISOU 1676 CD1 ILE A 223 11633 11505 8793 -713 -1037 837 C
ATOM 1677 N GLU A 224 4.686 33.228 28.051 1.00 97.94 N
ANISOU 1677 N GLU A 224 12852 14844 9518 -1285 -439 570 N
ATOM 1678 CA GLU A 224 5.117 32.635 26.788 1.00 94.42 C
ANISOU 1678 CA GLU A 224 12284 14849 8744 -1429 -317 508 C
ATOM 1679 C GLU A 224 5.779 31.277 26.998 1.00105.06 C
ANISOU 1679 C GLU A 224 13430 16393 10094 -1308 -111 142 C
ATOM 1680 O GLU A 224 5.295 30.251 26.506 1.00109.00 O
ANISOU 1680 O GLU A 224 13862 17045 10510 -1195 -58 -76 O
ATOM 1681 CB GLU A 224 6.076 33.578 26.072 1.00 96.51 C
ANISOU 1681 CB GLU A 224 12553 15333 8784 -1760 -304 774 C
ATOM 1682 CG GLU A 224 6.687 32.974 24.826 1.00123.43 C
ANISOU 1682 CG GLU A 224 15808 19265 11824 -1931 -136 682 C
ATOM 1683 CD GLU A 224 7.644 33.923 24.122 1.00144.74 C
ANISOU 1683 CD GLU A 224 18500 22216 14276 -2297 -107 967 C
ATOM 1684 OE1 GLU A 224 7.590 35.138 24.426 1.00137.08 O
ANISOU 1684 OE1 GLU A 224 17695 20973 13416 -2427 -276 1290 O
ATOM 1685 OE2 GLU A 224 8.401 33.467 23.229 1.00158.87 O1-
ANISOU 1685 OE2 GLU A 224 20125 24480 15759 -2462 78 868 O1-
ATOM 1686 N ASP A 225 6.902 31.252 27.720 1.00101.71 N
ANISOU 1686 N ASP A 225 12907 15960 9780 -1328 -9 67 N
ATOM 1687 CA ASP A 225 7.688 30.027 27.808 1.00 91.88 C
ANISOU 1687 CA ASP A 225 11451 14926 8535 -1226 173 -263 C
ATOM 1688 C ASP A 225 6.984 28.958 28.633 1.00 88.16 C
ANISOU 1688 C ASP A 225 10984 14212 8300 -929 156 -513 C
ATOM 1689 O ASP A 225 7.197 27.763 28.403 1.00 86.36 O
ANISOU 1689 O ASP A 225 10617 14143 8053 -814 264 -800 O
ATOM 1690 CB ASP A 225 9.068 30.344 28.378 1.00 98.32 C
ANISOU 1690 CB ASP A 225 12145 15791 9421 -1330 256 -256 C
ATOM 1691 CG ASP A 225 9.935 31.114 27.399 1.00112.49 C
ANISOU 1691 CG ASP A 225 13868 17934 10939 -1654 327 -65 C
ATOM 1692 OD1 ASP A 225 9.750 30.951 26.172 1.00108.34 O
ANISOU 1692 OD1 ASP A 225 13310 17735 10118 -1770 386 -57 O
ATOM 1693 OD2 ASP A 225 10.766 31.922 27.859 1.00115.77 O1-
ANISOU 1693 OD2 ASP A 225 14270 18297 11422 -1812 315 92 O1-
ATOM 1694 N VAL A 226 6.149 29.359 29.594 1.00 86.20 N
ANISOU 1694 N VAL A 226 10892 13582 8277 -810 23 -415 N
ATOM 1695 CA VAL A 226 5.256 28.400 30.238 1.00 75.78 C
ANISOU 1695 CA VAL A 226 9594 12059 7140 -568 -1 -607 C
ATOM 1696 C VAL A 226 4.333 27.769 29.205 1.00 85.50 C
ANISOU 1696 C VAL A 226 10819 13447 8222 -538 -14 -695 C
ATOM 1697 O VAL A 226 4.246 26.541 29.090 1.00 82.10 O
ANISOU 1697 O VAL A 226 10296 13088 7811 -417 54 -957 O
ATOM 1698 CB VAL A 226 4.453 29.072 31.366 1.00 75.45 C
ANISOU 1698 CB VAL A 226 9712 11630 7326 -472 -129 -477 C
ATOM 1699 CG1 VAL A 226 3.323 28.170 31.800 1.00 73.78 C
ANISOU 1699 CG1 VAL A 226 9523 11262 7249 -272 -154 -632 C
ATOM 1700 CG2 VAL A 226 5.353 29.356 32.553 1.00 96.55 C
ANISOU 1700 CG2 VAL A 226 12382 14143 10161 -464 -111 -477 C
ATOM 1701 N GLU A 227 3.641 28.608 28.427 1.00107.08 N
ANISOU 1701 N GLU A 227 13653 16224 10809 -652 -121 -473 N
ATOM 1702 CA GLU A 227 2.692 28.112 27.433 1.00 93.57 C
ANISOU 1702 CA GLU A 227 11944 14663 8944 -638 -166 -531 C
ATOM 1703 C GLU A 227 3.395 27.348 26.322 1.00 90.37 C
ANISOU 1703 C GLU A 227 11401 14669 8267 -732 -28 -720 C
ATOM 1704 O GLU A 227 2.994 26.229 25.978 1.00 85.74 O
ANISOU 1704 O GLU A 227 10750 14170 7658 -627 7 -976 O
ATOM 1705 CB GLU A 227 1.888 29.274 26.847 1.00 97.97 C
ANISOU 1705 CB GLU A 227 12640 15179 9406 -747 -340 -219 C
ATOM 1706 CG GLU A 227 0.929 29.921 27.823 1.00 95.19 C
ANISOU 1706 CG GLU A 227 12408 14430 9331 -610 -487 -91 C
ATOM 1707 CD GLU A 227 0.155 31.091 27.228 1.00131.78 C
ANISOU 1707 CD GLU A 227 17169 18995 13906 -693 -688 213 C
ATOM 1708 OE1 GLU A 227 0.471 31.528 26.096 1.00110.27 O
ANISOU 1708 OE1 GLU A 227 14466 16522 10909 -896 -723 382 O
ATOM 1709 OE2 GLU A 227 -0.780 31.570 27.905 1.00137.69 O1-
ANISOU 1709 OE2 GLU A 227 17993 19440 14884 -552 -815 283 O1-
ATOM 1710 N HIS A 228 4.442 27.943 25.738 1.00 98.74 N
ANISOU 1710 N HIS A 228 12410 15993 9114 -939 53 -607 N
ATOM 1711 CA HIS A 228 5.128 27.306 24.617 1.00106.20 C
ANISOU 1711 CA HIS A 228 13207 17382 9762 -1045 205 -795 C
ATOM 1712 C HIS A 228 5.688 25.941 24.990 1.00106.74 C
ANISOU 1712 C HIS A 228 13108 17487 9961 -858 349 -1193 C
ATOM 1713 O HIS A 228 5.844 25.079 24.117 1.00108.04 O
ANISOU 1713 O HIS A 228 13161 17949 9940 -853 448 -1453 O
ATOM 1714 CB HIS A 228 6.250 28.201 24.091 1.00 98.65 C
ANISOU 1714 CB HIS A 228 12199 16706 8576 -1315 290 -600 C
ATOM 1715 CG HIS A 228 6.878 27.694 22.828 1.00124.62 C
ANISOU 1715 CG HIS A 228 15337 20512 11502 -1459 456 -770 C
ATOM 1716 ND1 HIS A 228 7.854 26.721 22.825 1.00129.24 N
ANISOU 1716 ND1 HIS A 228 15699 21317 12088 -1377 658 -1123 N
ATOM 1717 CD2 HIS A 228 6.659 28.010 21.530 1.00130.94 C
ANISOU 1717 CD2 HIS A 228 16172 21663 11916 -1673 449 -649 C
ATOM 1718 CE1 HIS A 228 8.215 26.466 21.580 1.00133.35 C
ANISOU 1718 CE1 HIS A 228 16114 22316 12238 -1530 788 -1239 C
ATOM 1719 NE2 HIS A 228 7.505 27.235 20.775 1.00135.78 N
ANISOU 1719 NE2 HIS A 228 16582 22723 12286 -1725 667 -948 N
ATOM 1720 N THR A 229 6.005 25.723 26.265 1.00111.10 N
ANISOU 1720 N THR A 229 13643 17740 10830 -703 350 -1253 N
ATOM 1721 CA THR A 229 6.474 24.412 26.697 1.00113.44 C
ANISOU 1721 CA THR A 229 13799 18009 11292 -508 442 -1604 C
ATOM 1722 C THR A 229 5.333 23.487 27.093 1.00104.68 C
ANISOU 1722 C THR A 229 12766 16635 10370 -311 349 -1753 C
ATOM 1723 O THR A 229 5.468 22.264 26.965 1.00106.01 O
ANISOU 1723 O THR A 229 12838 16842 10601 -178 404 -2067 O
ATOM 1724 CB THR A 229 7.457 24.548 27.862 1.00101.72 C
ANISOU 1724 CB THR A 229 12250 16357 10042 -450 474 -1594 C
ATOM 1725 OG1 THR A 229 6.881 25.363 28.892 1.00 88.12 O
ANISOU 1725 OG1 THR A 229 10701 14277 8505 -435 340 -1342 O
ATOM 1726 CG2 THR A 229 8.766 25.171 27.386 1.00102.94 C
ANISOU 1726 CG2 THR A 229 12259 16836 10019 -644 598 -1531 C
ATOM 1727 N PHE A 230 4.212 24.036 27.568 1.00 94.88 N
ANISOU 1727 N PHE A 230 11690 15127 9235 -292 207 -1543 N
ATOM 1728 CA PHE A 230 3.051 23.197 27.849 1.00 97.41 C
ANISOU 1728 CA PHE A 230 12066 15239 9707 -143 125 -1667 C
ATOM 1729 C PHE A 230 2.494 22.586 26.570 1.00103.17 C
ANISOU 1729 C PHE A 230 12765 16217 10219 -181 120 -1826 C
ATOM 1730 O PHE A 230 2.016 21.446 26.577 1.00110.08 O
ANISOU 1730 O PHE A 230 13613 17017 11196 -64 106 -2069 O
ATOM 1731 CB PHE A 230 1.972 24.003 28.570 1.00 95.48 C
ANISOU 1731 CB PHE A 230 11970 14704 9604 -122 -11 -1417 C
ATOM 1732 CG PHE A 230 0.732 23.210 28.879 1.00 85.56 C
ANISOU 1732 CG PHE A 230 10749 13259 8501 3 -88 -1522 C
ATOM 1733 CD1 PHE A 230 0.751 22.213 29.842 1.00 84.33 C
ANISOU 1733 CD1 PHE A 230 10571 12889 8581 142 -64 -1691 C
ATOM 1734 CD2 PHE A 230 -0.449 23.455 28.200 1.00 89.94 C
ANISOU 1734 CD2 PHE A 230 11353 13856 8965 -34 -196 -1438 C
ATOM 1735 CE1 PHE A 230 -0.388 21.480 30.123 1.00 84.86 C
ANISOU 1735 CE1 PHE A 230 10666 12792 8784 221 -132 -1770 C
ATOM 1736 CE2 PHE A 230 -1.590 22.727 28.477 1.00 87.11 C
ANISOU 1736 CE2 PHE A 230 11002 13344 8753 60 -265 -1535 C
ATOM 1737 CZ PHE A 230 -1.560 21.738 29.439 1.00 84.06 C
ANISOU 1737 CZ PHE A 230 10594 12750 8595 177 -224 -1700 C
ATOM 1738 N GLU A 231 2.543 23.334 25.462 1.00 99.83 N
ANISOU 1738 N GLU A 231 12354 16090 9487 -362 118 -1684 N
ATOM 1739 CA GLU A 231 2.076 22.807 24.183 1.00101.84 C
ANISOU 1739 CA GLU A 231 12584 16630 9482 -423 110 -1834 C
ATOM 1740 C GLU A 231 2.800 21.517 23.816 1.00106.63 C
ANISOU 1740 C GLU A 231 13042 17415 10058 -340 250 -2243 C
ATOM 1741 O GLU A 231 2.198 20.597 23.250 1.00108.04 O
ANISOU 1741 O GLU A 231 13208 17650 10190 -288 219 -2484 O
ATOM 1742 CB GLU A 231 2.255 23.855 23.082 1.00108.70 C
ANISOU 1742 CB GLU A 231 13488 17827 9987 -660 99 -1594 C
ATOM 1743 CG GLU A 231 1.199 24.957 23.062 1.00114.58 C
ANISOU 1743 CG GLU A 231 14391 18415 10729 -728 -100 -1231 C
ATOM 1744 CD GLU A 231 -0.133 24.481 22.506 1.00131.89 C
ANISOU 1744 CD GLU A 231 16627 20607 12879 -683 -243 -1295 C
ATOM 1745 OE1 GLU A 231 -0.123 23.647 21.575 1.00117.25 O
ANISOU 1745 OE1 GLU A 231 14708 19033 10807 -717 -195 -1542 O
ATOM 1746 OE2 GLU A 231 -1.187 24.940 22.995 1.00140.64 O1-
ANISOU 1746 OE2 GLU A 231 17822 21444 14171 -614 -405 -1115 O1-
ATOM 1747 N GLU A 232 4.093 21.424 24.137 1.00108.99 N
ANISOU 1747 N GLU A 232 13217 17793 10400 -320 393 -2343 N
ATOM 1748 CA GLU A 232 4.830 20.197 23.860 1.00108.53 C
ANISOU 1748 CA GLU A 232 12998 17876 10364 -203 518 -2756 C
ATOM 1749 C GLU A 232 4.513 19.076 24.840 1.00104.48 C
ANISOU 1749 C GLU A 232 12494 16977 10226 30 454 -2959 C
ATOM 1750 O GLU A 232 4.872 17.925 24.567 1.00102.51 O
ANISOU 1750 O GLU A 232 12139 16776 10035 152 508 -3323 O
ATOM 1751 CB GLU A 232 6.342 20.449 23.862 1.00101.19 C
ANISOU 1751 CB GLU A 232 11896 17179 9372 -248 689 -2808 C
ATOM 1752 CG GLU A 232 6.791 21.744 23.206 1.00115.95 C
ANISOU 1752 CG GLU A 232 13767 19365 10923 -514 747 -2515 C
ATOM 1753 CD GLU A 232 8.304 21.881 23.182 1.00131.30 C
ANISOU 1753 CD GLU A 232 15502 21575 12812 -571 931 -2602 C
ATOM 1754 OE1 GLU A 232 8.965 21.024 22.559 1.00135.93 O
ANISOU 1754 OE1 GLU A 232 15899 22450 13298 -512 1079 -2965 O
ATOM 1755 OE2 GLU A 232 8.834 22.840 23.782 1.00129.92 O1-
ANISOU 1755 OE2 GLU A 232 15339 21322 12702 -674 925 -2325 O1-
ATOM 1756 N ILE A 233 3.860 19.370 25.966 1.00 98.36 N
ANISOU 1756 N ILE A 233 11843 15824 9706 88 337 -2740 N
ATOM 1757 CA ILE A 233 3.486 18.299 26.885 1.00 95.39 C
ANISOU 1757 CA ILE A 233 11491 15093 9659 272 267 -2897 C
ATOM 1758 C ILE A 233 2.193 17.633 26.434 1.00107.59 C
ANISOU 1758 C ILE A 233 13110 16565 11203 284 163 -3000 C
ATOM 1759 O ILE A 233 2.031 16.417 26.596 1.00106.62 O
ANISOU 1759 O ILE A 233 12968 16282 11261 404 130 -3260 O
ATOM 1760 CB ILE A 233 3.352 18.825 28.324 1.00 79.73 C
ANISOU 1760 CB ILE A 233 9601 12769 7925 317 202 -2640 C
ATOM 1761 CG1 ILE A 233 4.683 19.358 28.827 1.00 99.55 C
ANISOU 1761 CG1 ILE A 233 12027 15335 10463 308 287 -2572 C
ATOM 1762 CG2 ILE A 233 2.892 17.717 29.261 1.00 77.86 C
ANISOU 1762 CG2 ILE A 233 9404 12183 7995 470 124 -2764 C
ATOM 1763 CD1 ILE A 233 4.610 19.980 30.203 1.00112.41 C
ANISOU 1763 CD1 ILE A 233 13756 16663 12293 332 221 -2326 C
ATOM 1764 N LYS A 234 1.273 18.410 25.851 1.00 94.52 N
ANISOU 1764 N LYS A 234 11537 15018 9357 155 92 -2796 N
ATOM 1765 CA LYS A 234 -0.072 17.941 25.498 1.00 80.16 C
ANISOU 1765 CA LYS A 234 9782 13125 7548 148 -34 -2842 C
ATOM 1766 C LYS A 234 -0.125 16.543 24.891 1.00 91.52 C
ANISOU 1766 C LYS A 234 11163 14609 9000 213 -33 -3236 C
ATOM 1767 O LYS A 234 -0.968 15.751 25.332 1.00103.27 O
ANISOU 1767 O LYS A 234 12693 15837 10706 276 -132 -3318 O
ATOM 1768 CB LYS A 234 -0.737 18.957 24.555 1.00 97.33 C
ANISOU 1768 CB LYS A 234 12010 15538 9431 -11 -103 -2620 C
ATOM 1769 CG LYS A 234 -1.177 20.246 25.236 1.00 97.50 C
ANISOU 1769 CG LYS A 234 12122 15400 9525 -48 -176 -2234 C
ATOM 1770 CD LYS A 234 -1.963 21.142 24.289 1.00107.43 C
ANISOU 1770 CD LYS A 234 13436 16845 10536 -183 -292 -2017 C
ATOM 1771 CE LYS A 234 -2.455 22.391 25.001 1.00104.07 C
ANISOU 1771 CE LYS A 234 13098 16210 10233 -187 -386 -1664 C
ATOM 1772 NZ LYS A 234 -3.248 23.271 24.100 1.00 94.74 N
ANISOU 1772 NZ LYS A 234 11974 15173 8849 -299 -537 -1434 N
ATOM 1773 N PRO A 235 0.714 16.166 23.915 1.00 95.59 N
ANISOU 1773 N PRO A 235 11580 15439 9300 198 74 -3501 N
ATOM 1774 CA PRO A 235 0.643 14.780 23.412 1.00 98.91 C
ANISOU 1774 CA PRO A 235 11953 15854 9775 285 62 -3918 C
ATOM 1775 C PRO A 235 0.869 13.733 24.490 1.00100.23 C
ANISOU 1775 C PRO A 235 12113 15622 10348 466 29 -4076 C
ATOM 1776 O PRO A 235 0.159 12.720 24.521 1.00100.26 O
ANISOU 1776 O PRO A 235 12157 15417 10519 516 -76 -4262 O
ATOM 1777 CB PRO A 235 1.738 14.740 22.337 1.00 90.36 C
ANISOU 1777 CB PRO A 235 10740 15201 8391 250 223 -4166 C
ATOM 1778 CG PRO A 235 1.929 16.156 21.935 1.00 98.35 C
ANISOU 1778 CG PRO A 235 11770 16500 9099 68 274 -3826 C
ATOM 1779 CD PRO A 235 1.722 16.953 23.179 1.00 93.99 C
ANISOU 1779 CD PRO A 235 11300 15624 8787 87 212 -3452 C
ATOM 1780 N LEU A 236 1.834 13.954 25.386 1.00 91.70 N
ANISOU 1780 N LEU A 236 10987 14423 9432 552 99 -3989 N
ATOM 1781 CA LEU A 236 2.083 12.984 26.448 1.00 98.31 C
ANISOU 1781 CA LEU A 236 11830 14876 10649 718 42 -4100 C
ATOM 1782 C LEU A 236 0.966 12.999 27.487 1.00 96.55 C
ANISOU 1782 C LEU A 236 11747 14292 10646 697 -90 -3845 C
ATOM 1783 O LEU A 236 0.571 11.944 27.997 1.00 98.98 O
ANISOU 1783 O LEU A 236 12099 14293 11215 772 -189 -3966 O
ATOM 1784 CB LEU A 236 3.436 13.260 27.102 1.00103.88 C
ANISOU 1784 CB LEU A 236 12436 15582 11450 808 135 -4066 C
ATOM 1785 CG LEU A 236 3.782 12.435 28.343 1.00 84.31 C
ANISOU 1785 CG LEU A 236 9975 12701 9360 973 52 -4101 C
ATOM 1786 CD1 LEU A 236 3.739 10.944 28.031 1.00 91.06 C
ANISOU 1786 CD1 LEU A 236 10803 13390 10404 1109 -21 -4485 C
ATOM 1787 CD2 LEU A 236 5.141 12.840 28.893 1.00 88.46 C
ANISOU 1787 CD2 LEU A 236 10383 13284 9944 1045 133 -4054 C
ATOM 1788 N TYR A 237 0.440 14.183 27.812 1.00 88.71 N
ANISOU 1788 N TYR A 237 10820 13331 9554 591 -96 -3497 N
ATOM 1789 CA TYR A 237 -0.671 14.254 28.757 1.00 84.21 C
ANISOU 1789 CA TYR A 237 10357 12470 9167 568 -198 -3276 C
ATOM 1790 C TYR A 237 -1.947 13.684 28.153 1.00 95.83 C
ANISOU 1790 C TYR A 237 11860 13927 10623 504 -300 -3372 C
ATOM 1791 O TYR A 237 -2.703 12.981 28.836 1.00 91.21 O
ANISOU 1791 O TYR A 237 11327 13063 10268 514 -388 -3366 O
ATOM 1792 CB TYR A 237 -0.895 15.697 29.206 1.00 71.59 C
ANISOU 1792 CB TYR A 237 8807 10916 7477 492 -178 -2921 C
ATOM 1793 CG TYR A 237 -2.056 15.855 30.161 1.00 70.86 C
ANISOU 1793 CG TYR A 237 8799 10572 7552 474 -259 -2717 C
ATOM 1794 CD1 TYR A 237 -2.006 15.312 31.437 1.00 80.78 C
ANISOU 1794 CD1 TYR A 237 10099 11529 9063 539 -278 -2680 C
ATOM 1795 CD2 TYR A 237 -3.203 16.543 29.787 1.00 72.25 C
ANISOU 1795 CD2 TYR A 237 8999 10826 7626 390 -318 -2562 C
ATOM 1796 CE1 TYR A 237 -3.063 15.451 32.315 1.00 87.76 C
ANISOU 1796 CE1 TYR A 237 11045 12227 10072 505 -326 -2506 C
ATOM 1797 CE2 TYR A 237 -4.266 16.688 30.658 1.00 75.62 C
ANISOU 1797 CE2 TYR A 237 9468 11055 8210 382 -373 -2404 C
ATOM 1798 CZ TYR A 237 -4.189 16.140 31.920 1.00 83.69 C
ANISOU 1798 CZ TYR A 237 10528 11810 9461 432 -362 -2382 C
ATOM 1799 OH TYR A 237 -5.242 16.279 32.793 1.00 83.79 O
ANISOU 1799 OH TYR A 237 10567 11666 9602 407 -392 -2234 O
ATOM 1800 N GLU A 238 -2.200 13.976 26.874 1.00103.04 N
ANISOU 1800 N GLU A 238 12742 15151 11258 418 -298 -3451 N
ATOM 1801 CA GLU A 238 -3.416 13.502 26.219 1.00 99.51 C
ANISOU 1801 CA GLU A 238 12314 14724 10770 343 -414 -3541 C
ATOM 1802 C GLU A 238 -3.508 11.982 26.253 1.00106.98 C
ANISOU 1802 C GLU A 238 13260 15457 11931 406 -477 -3863 C
ATOM 1803 O GLU A 238 -4.596 11.421 26.433 1.00119.36 O
ANISOU 1803 O GLU A 238 14864 16847 13642 355 -594 -3868 O
ATOM 1804 CB GLU A 238 -3.455 14.007 24.777 1.00107.27 C
ANISOU 1804 CB GLU A 238 13267 16111 11382 241 -405 -3599 C
ATOM 1805 CG GLU A 238 -4.303 15.248 24.565 1.00108.03 C
ANISOU 1805 CG GLU A 238 13398 16331 11318 132 -473 -3266 C
ATOM 1806 CD GLU A 238 -4.289 15.715 23.123 1.00124.45 C
ANISOU 1806 CD GLU A 238 15463 18816 13007 12 -485 -3297 C
ATOM 1807 OE1 GLU A 238 -4.760 14.960 22.245 1.00127.63 O
ANISOU 1807 OE1 GLU A 238 15850 19344 13298 -32 -555 -3542 O
ATOM 1808 OE2 GLU A 238 -3.801 16.835 22.865 1.00119.77 O1-
ANISOU 1808 OE2 GLU A 238 14880 18417 12209 -52 -434 -3073 O1-
ATOM 1809 N HIS A 239 -2.375 11.297 26.083 1.00 88.39 N
ANISOU 1809 N HIS A 239 10855 13110 9618 517 -408 -4138 N
ATOM 1810 CA HIS A 239 -2.380 9.838 26.118 1.00 99.14 C
ANISOU 1810 CA HIS A 239 12224 14225 11218 598 -488 -4460 C
ATOM 1811 C HIS A 239 -2.526 9.325 27.545 1.00 94.91 C
ANISOU 1811 C HIS A 239 11758 13253 11050 654 -559 -4313 C
ATOM 1812 O HIS A 239 -3.325 8.418 27.810 1.00 97.76 O
ANISOU 1812 O HIS A 239 12177 13349 11620 619 -685 -4377 O
ATOM 1813 CB HIS A 239 -1.107 9.295 25.471 1.00 99.30 C
ANISOU 1813 CB HIS A 239 12150 14396 11183 725 -396 -4824 C
ATOM 1814 CG HIS A 239 -1.143 9.306 23.974 1.00 96.82 C
ANISOU 1814 CG HIS A 239 11782 14478 10529 657 -354 -5084 C
ATOM 1815 ND1 HIS A 239 -0.669 10.361 23.224 1.00122.07 N
ANISOU 1815 ND1 HIS A 239 14919 18105 13358 577 -224 -4991 N
ATOM 1816 CD2 HIS A 239 -1.603 8.391 23.088 1.00 90.07 C
ANISOU 1816 CD2 HIS A 239 10931 13660 9630 639 -431 -5432 C
ATOM 1817 CE1 HIS A 239 -0.831 10.094 21.940 1.00 93.04 C
ANISOU 1817 CE1 HIS A 239 11213 14738 9402 510 -216 -5262 C
ATOM 1818 NE2 HIS A 239 -1.397 8.906 21.831 1.00 90.33 N
ANISOU 1818 NE2 HIS A 239 10906 14165 9248 553 -341 -5548 N
ATOM 1819 N LEU A 240 -1.751 9.887 28.478 1.00 95.96 N
ANISOU 1819 N LEU A 240 11888 13315 11257 722 -487 -4108 N
ATOM 1820 CA LEU A 240 -1.935 9.577 29.894 1.00103.78 C
ANISOU 1820 CA LEU A 240 12959 13936 12538 745 -553 -3909 C
ATOM 1821 C LEU A 240 -3.384 9.790 30.310 1.00 99.66 C
ANISOU 1821 C LEU A 240 12505 13314 12048 602 -623 -3679 C
ATOM 1822 O LEU A 240 -3.934 9.018 31.103 1.00105.02 O
ANISOU 1822 O LEU A 240 13250 13686 12967 571 -715 -3630 O
ATOM 1823 CB LEU A 240 -0.991 10.439 30.740 1.00105.78 C
ANISOU 1823 CB LEU A 240 13199 14209 12786 806 -463 -3689 C
ATOM 1824 CG LEU A 240 -0.733 10.127 32.223 1.00 79.88 C
ANISOU 1824 CG LEU A 240 9991 10592 9770 857 -518 -3514 C
ATOM 1825 CD1 LEU A 240 -1.844 10.660 33.124 1.00 77.93 C
ANISOU 1825 CD1 LEU A 240 9835 10232 9544 734 -540 -3196 C
ATOM 1826 CD2 LEU A 240 -0.532 8.635 32.449 1.00 77.23 C
ANISOU 1826 CD2 LEU A 240 9684 9940 9720 947 -643 -3732 C
ATOM 1827 N HIS A 241 -4.025 10.826 29.765 1.00 97.04 N
ANISOU 1827 N HIS A 241 12149 13242 11480 508 -586 -3534 N
ATOM 1828 CA HIS A 241 -5.408 11.121 30.122 1.00100.20 C
ANISOU 1828 CA HIS A 241 12574 13584 11914 390 -647 -3328 C
ATOM 1829 C HIS A 241 -6.358 10.064 29.568 1.00 89.04 C
ANISOU 1829 C HIS A 241 11158 12088 10584 308 -769 -3521 C
ATOM 1830 O HIS A 241 -7.241 9.576 30.282 1.00 83.46 O
ANISOU 1830 O HIS A 241 10479 11160 10070 229 -839 -3426 O
ATOM 1831 CB HIS A 241 -5.789 12.513 29.615 1.00 99.32 C
ANISOU 1831 CB HIS A 241 12428 13758 11551 336 -605 -3135 C
ATOM 1832 CG HIS A 241 -7.182 12.926 29.975 1.00 91.56 C
ANISOU 1832 CG HIS A 241 11438 12738 10614 246 -664 -2934 C
ATOM 1833 ND1 HIS A 241 -8.293 12.475 29.295 1.00 83.34 N
ANISOU 1833 ND1 HIS A 241 10355 11749 9562 153 -770 -3025 N
ATOM 1834 CD2 HIS A 241 -7.643 13.749 30.945 1.00 91.06 C
ANISOU 1834 CD2 HIS A 241 11384 12602 10612 240 -630 -2668 C
ATOM 1835 CE1 HIS A 241 -9.378 13.002 29.833 1.00 86.29 C
ANISOU 1835 CE1 HIS A 241 10695 12092 10000 97 -797 -2816 C
ATOM 1836 NE2 HIS A 241 -9.011 13.780 30.836 1.00 80.97 N
ANISOU 1836 NE2 HIS A 241 10052 11343 9368 155 -706 -2608 N
ATOM 1837 N ALA A 242 -6.194 9.700 28.292 1.00 96.69 N
ANISOU 1837 N ALA A 242 12091 13249 11400 308 -795 -3799 N
ATOM 1838 CA ALA A 242 -7.062 8.698 27.685 1.00105.34 C
ANISOU 1838 CA ALA A 242 13186 14275 12563 222 -927 -4016 C
ATOM 1839 C ALA A 242 -6.809 7.300 28.233 1.00107.13 C
ANISOU 1839 C ALA A 242 13471 14128 13105 265 -1006 -4201 C
ATOM 1840 O ALA A 242 -7.698 6.446 28.150 1.00104.65 O
ANISOU 1840 O ALA A 242 13180 13647 12938 161 -1135 -4295 O
ATOM 1841 CB ALA A 242 -6.890 8.696 26.166 1.00105.23 C
ANISOU 1841 CB ALA A 242 13127 14587 12267 210 -933 -4288 C
ATOM 1842 N TYR A 243 -5.617 7.046 28.777 1.00 99.23 N
ANISOU 1842 N TYR A 243 12494 12986 12225 411 -951 -4251 N
ATOM 1843 CA TYR A 243 -5.351 5.764 29.420 1.00 90.19 C
ANISOU 1843 CA TYR A 243 11418 11440 11413 464 -1056 -4377 C
ATOM 1844 C TYR A 243 -5.950 5.714 30.819 1.00 83.70 C
ANISOU 1844 C TYR A 243 10669 10333 10799 374 -1098 -4044 C
ATOM 1845 O TYR A 243 -6.503 4.686 31.223 1.00 82.84 O
ANISOU 1845 O TYR A 243 10627 9914 10934 292 -1229 -4068 O
ATOM 1846 CB TYR A 243 -3.846 5.500 29.473 1.00 96.25 C
ANISOU 1846 CB TYR A 243 12161 12165 12245 669 -1003 -4558 C
ATOM 1847 CG TYR A 243 -3.472 4.292 30.301 1.00 99.87 C
ANISOU 1847 CG TYR A 243 12698 12172 13075 750 -1134 -4627 C
ATOM 1848 CD1 TYR A 243 -3.648 3.005 29.808 1.00108.41 C
ANISOU 1848 CD1 TYR A 243 13817 13020 14355 767 -1281 -4951 C
ATOM 1849 CD2 TYR A 243 -2.952 4.437 31.580 1.00 98.96 C
ANISOU 1849 CD2 TYR A 243 12632 11852 13117 803 -1132 -4364 C
ATOM 1850 CE1 TYR A 243 -3.312 1.897 30.565 1.00105.92 C
ANISOU 1850 CE1 TYR A 243 13589 12252 14404 839 -1432 -4994 C
ATOM 1851 CE2 TYR A 243 -2.615 3.336 32.344 1.00101.35 C
ANISOU 1851 CE2 TYR A 243 13020 11732 13757 869 -1282 -4392 C
ATOM 1852 CZ TYR A 243 -2.797 2.069 31.832 1.00110.23 C
ANISOU 1852 CZ TYR A 243 14184 12604 15095 889 -1436 -4698 C
ATOM 1853 OH TYR A 243 -2.462 0.969 32.588 1.00124.99 O
ANISOU 1853 OH TYR A 243 16152 14015 17324 954 -1614 -4709 O
ATOM 1854 N VAL A 244 -5.848 6.811 31.572 1.00 85.64 N
ANISOU 1854 N VAL A 244 10907 10686 10947 375 -988 -3734 N
ATOM 1855 CA VAL A 244 -6.482 6.868 32.885 1.00 89.01 C
ANISOU 1855 CA VAL A 244 11394 10909 11516 274 -1002 -3423 C
ATOM 1856 C VAL A 244 -7.999 6.850 32.743 1.00 92.49 C
ANISOU 1856 C VAL A 244 11804 11389 11950 86 -1050 -3339 C
ATOM 1857 O VAL A 244 -8.700 6.175 33.508 1.00 89.91 O
ANISOU 1857 O VAL A 244 11524 10824 11814 -43 -1121 -3227 O
ATOM 1858 CB VAL A 244 -5.996 8.109 33.655 1.00 93.51 C
ANISOU 1858 CB VAL A 244 11960 11609 11962 328 -871 -3157 C
ATOM 1859 CG1 VAL A 244 -6.870 8.358 34.873 1.00 91.92 C
ANISOU 1859 CG1 VAL A 244 11799 11293 11834 203 -857 -2855 C
ATOM 1860 CG2 VAL A 244 -4.543 7.937 34.066 1.00 92.54 C
ANISOU 1860 CG2 VAL A 244 11864 11383 11913 490 -854 -3209 C
ATOM 1861 N ARG A 245 -8.528 7.582 31.759 1.00105.15 N
ANISOU 1861 N ARG A 245 13319 13302 13330 55 -1020 -3383 N
ATOM 1862 CA ARG A 245 -9.970 7.589 31.529 1.00103.01 C
ANISOU 1862 CA ARG A 245 12986 13098 13056 -112 -1082 -3322 C
ATOM 1863 C ARG A 245 -10.471 6.208 31.132 1.00 92.80 C
ANISOU 1863 C ARG A 245 11718 11599 11942 -218 -1236 -3545 C
ATOM 1864 O ARG A 245 -11.541 5.776 31.577 1.00 99.00 O
ANISOU 1864 O ARG A 245 12484 12263 12869 -387 -1302 -3442 O
ATOM 1865 CB ARG A 245 -10.325 8.611 30.452 1.00 95.07 C
ANISOU 1865 CB ARG A 245 11888 12458 11776 -106 -1058 -3335 C
ATOM 1866 CG ARG A 245 -11.785 8.589 30.040 1.00 87.78 C
ANISOU 1866 CG ARG A 245 10872 11630 10848 -261 -1152 -3309 C
ATOM 1867 CD ARG A 245 -12.067 9.681 29.034 1.00 96.98 C
ANISOU 1867 CD ARG A 245 11959 13147 11743 -241 -1153 -3280 C
ATOM 1868 NE ARG A 245 -11.154 9.590 27.902 1.00 91.96 N
ANISOU 1868 NE ARG A 245 11356 12676 10907 -167 -1155 -3517 N
ATOM 1869 CZ ARG A 245 -11.009 10.530 26.979 1.00 93.21 C
ANISOU 1869 CZ ARG A 245 11482 13149 10784 -143 -1141 -3492 C
ATOM 1870 NH1 ARG A 245 -11.712 11.650 27.017 1.00 96.80 N
ANISOU 1870 NH1 ARG A 245 11876 13756 11147 -165 -1150 -3242 N
ATOM 1871 NH2 ARG A 245 -10.134 10.342 25.995 1.00 92.63 N
ANISOU 1871 NH2 ARG A 245 11435 13243 10516 -96 -1122 -3724 N
ATOM 1872 N ALA A 246 -9.717 5.505 30.284 1.00 92.39 N
ANISOU 1872 N ALA A 246 11700 11514 11891 -127 -1292 -3866 N
ATOM 1873 CA ALA A 246 -10.080 4.135 29.942 1.00 99.20 C
ANISOU 1873 CA ALA A 246 12607 12127 12957 -211 -1455 -4111 C
ATOM 1874 C ALA A 246 -10.125 3.254 31.185 1.00104.26 C
ANISOU 1874 C ALA A 246 13348 12349 13917 -277 -1526 -3966 C
ATOM 1875 O ALA A 246 -11.048 2.447 31.349 1.00102.36 O
ANISOU 1875 O ALA A 246 13127 11909 13855 -462 -1650 -3959 O
ATOM 1876 CB ALA A 246 -9.096 3.570 28.917 1.00108.51 C
ANISOU 1876 CB ALA A 246 13806 13334 14089 -61 -1485 -4510 C
ATOM 1877 N LYS A 247 -9.150 3.411 32.084 1.00112.44 N
ANISOU 1877 N LYS A 247 14448 13253 15022 -148 -1459 -3829 N
ATOM 1878 CA LYS A 247 -9.083 2.550 33.258 1.00109.93 C
ANISOU 1878 CA LYS A 247 14244 12534 14989 -209 -1548 -3676 C
ATOM 1879 C LYS A 247 -10.082 2.961 34.335 1.00106.23 C
ANISOU 1879 C LYS A 247 13767 12070 14526 -406 -1495 -3303 C
ATOM 1880 O LYS A 247 -10.553 2.101 35.088 1.00112.15 O
ANISOU 1880 O LYS A 247 14596 12526 15492 -569 -1596 -3178 O
ATOM 1881 CB LYS A 247 -7.662 2.538 33.825 1.00101.12 C
ANISOU 1881 CB LYS A 247 13194 11285 13943 2 -1521 -3668 C
ATOM 1882 CG LYS A 247 -6.611 2.013 32.850 1.00109.86 C
ANISOU 1882 CG LYS A 247 14286 12373 15082 211 -1567 -4064 C
ATOM 1883 CD LYS A 247 -6.770 0.526 32.573 1.00122.12 C
ANISOU 1883 CD LYS A 247 15922 13549 16930 179 -1776 -4317 C
ATOM 1884 CE LYS A 247 -6.247 -0.322 33.718 1.00123.68 C
ANISOU 1884 CE LYS A 247 16251 13293 17449 213 -1912 -4175 C
ATOM 1885 NZ LYS A 247 -6.371 -1.777 33.422 1.00137.41 N
ANISOU 1885 NZ LYS A 247 18085 14618 19508 190 -2143 -4428 N
ATOM 1886 N LEU A 248 -10.414 4.252 34.435 1.00 88.04 N
ANISOU 1886 N LEU A 248 11367 10092 11992 -400 -1340 -3126 N
ATOM 1887 CA LEU A 248 -11.494 4.656 35.331 1.00 88.65 C
ANISOU 1887 CA LEU A 248 11398 10221 12064 -582 -1277 -2832 C
ATOM 1888 C LEU A 248 -12.843 4.161 34.834 1.00102.88 C
ANISOU 1888 C LEU A 248 13112 12047 13929 -796 -1365 -2888 C
ATOM 1889 O LEU A 248 -13.714 3.816 35.642 1.00108.69 O
ANISOU 1889 O LEU A 248 13834 12683 14778 -1002 -1373 -2696 O
ATOM 1890 CB LEU A 248 -11.535 6.178 35.489 1.00 85.12 C
ANISOU 1890 CB LEU A 248 10862 10100 11382 -498 -1106 -2671 C
ATOM 1891 CG LEU A 248 -10.460 6.893 36.305 1.00 93.08 C
ANISOU 1891 CG LEU A 248 11938 11111 12317 -347 -997 -2526 C
ATOM 1892 CD1 LEU A 248 -10.833 8.358 36.473 1.00 87.19 C
ANISOU 1892 CD1 LEU A 248 11100 10656 11372 -312 -853 -2365 C
ATOM 1893 CD2 LEU A 248 -10.292 6.224 37.659 1.00 97.17 C
ANISOU 1893 CD2 LEU A 248 12574 11346 12999 -432 -1024 -2335 C
ATOM 1894 N MET A 249 -13.032 4.125 33.513 1.00117.44 N
ANISOU 1894 N MET A 249 14890 14046 15687 -765 -1432 -3147 N
ATOM 1895 CA MET A 249 -14.303 3.692 32.945 1.00112.13 C
ANISOU 1895 CA MET A 249 14119 13422 15062 -967 -1536 -3220 C
ATOM 1896 C MET A 249 -14.609 2.240 33.294 1.00118.92 C
ANISOU 1896 C MET A 249 15073 13903 16210 -1152 -1694 -3268 C
ATOM 1897 O MET A 249 -15.780 1.867 33.425 1.00132.87 O
ANISOU 1897 O MET A 249 16760 15652 18072 -1392 -1755 -3192 O
ATOM 1898 CB MET A 249 -14.274 3.906 31.431 1.00112.36 C
ANISOU 1898 CB MET A 249 14086 13691 14914 -887 -1595 -3506 C
ATOM 1899 CG MET A 249 -15.623 3.892 30.746 1.00127.25 C
ANISOU 1899 CG MET A 249 15829 15752 16768 -1068 -1689 -3551 C
ATOM 1900 SD MET A 249 -15.417 4.178 28.979 1.00137.94 S
ANISOU 1900 SD MET A 249 17142 17412 17857 -968 -1766 -3876 S
ATOM 1901 CE MET A 249 -14.458 2.737 28.521 1.00130.94 C
ANISOU 1901 CE MET A 249 16419 16204 17126 -912 -1884 -4255 C
ATOM 1902 N ASN A 250 -13.575 1.413 33.464 1.00113.85 N
ANISOU 1902 N ASN A 250 14591 12944 15724 -1049 -1773 -3387 N
ATOM 1903 CA ASN A 250 -13.780 0.056 33.955 1.00116.80 C
ANISOU 1903 CA ASN A 250 15084 12894 16402 -1220 -1942 -3382 C
ATOM 1904 C ASN A 250 -14.205 0.026 35.419 1.00103.41 C
ANISOU 1904 C ASN A 250 13424 11068 14797 -1402 -1888 -2991 C
ATOM 1905 O ASN A 250 -14.793 -0.968 35.859 1.00105.44 O
ANISOU 1905 O ASN A 250 13744 11043 15276 -1642 -2018 -2906 O
ATOM 1906 CB ASN A 250 -12.503 -0.772 33.785 1.00121.34 C
ANISOU 1906 CB ASN A 250 15815 13148 17142 -1023 -2056 -3611 C
ATOM 1907 CG ASN A 250 -12.180 -1.066 32.333 1.00138.47 C
ANISOU 1907 CG ASN A 250 17957 15399 19256 -890 -2133 -4052 C
ATOM 1908 OD1 ASN A 250 -13.048 -1.002 31.463 1.00132.22 O
ANISOU 1908 OD1 ASN A 250 17068 14804 18364 -1010 -2170 -4191 O
ATOM 1909 ND2 ASN A 250 -10.921 -1.398 32.066 1.00143.88 N
ANISOU 1909 ND2 ASN A 250 18718 15950 20002 -644 -2160 -4285 N
ATOM 1910 N ALA A 251 -13.926 1.089 36.179 1.00107.88 N
ANISOU 1910 N ALA A 251 13958 11840 15191 -1310 -1702 -2754 N
ATOM 1911 CA ALA A 251 -14.139 1.094 37.622 1.00116.22 C
ANISOU 1911 CA ALA A 251 15068 12797 16292 -1458 -1634 -2402 C
ATOM 1912 C ALA A 251 -15.420 1.795 38.055 1.00117.03 C
ANISOU 1912 C ALA A 251 14998 13194 16274 -1654 -1491 -2194 C
ATOM 1913 O ALA A 251 -15.936 1.491 39.137 1.00103.52 O
ANISOU 1913 O ALA A 251 13310 11397 14626 -1875 -1459 -1933 O
ATOM 1914 CB ALA A 251 -12.945 1.747 38.330 1.00109.94 C
ANISOU 1914 CB ALA A 251 14362 12016 15395 -1237 -1531 -2283 C
ATOM 1915 N TYR A 252 -15.923 2.742 37.264 1.00129.26 N
ANISOU 1915 N TYR A 252 16368 15095 17648 -1575 -1405 -2296 N
ATOM 1916 CA TYR A 252 -17.281 3.262 37.418 1.00129.36 C
ANISOU 1916 CA TYR A 252 16173 15377 17600 -1752 -1315 -2173 C
ATOM 1917 C TYR A 252 -17.895 3.335 36.027 1.00123.87 C
ANISOU 1917 C TYR A 252 15337 14859 16870 -1745 -1412 -2416 C
ATOM 1918 O TYR A 252 -17.856 4.382 35.368 1.00125.04 O
ANISOU 1918 O TYR A 252 15384 15295 16832 -1568 -1348 -2486 O
ATOM 1919 CB TYR A 252 -17.311 4.635 38.094 1.00119.41 C
ANISOU 1919 CB TYR A 252 14821 14406 16144 -1635 -1099 -1993 C
ATOM 1920 CG TYR A 252 -16.245 4.901 39.136 1.00118.87 C
ANISOU 1920 CG TYR A 252 14918 14224 16024 -1517 -1008 -1835 C
ATOM 1921 CD1 TYR A 252 -16.405 4.479 40.452 1.00127.78 C
ANISOU 1921 CD1 TYR A 252 16122 15223 17207 -1702 -958 -1590 C
ATOM 1922 CD2 TYR A 252 -15.091 5.599 38.812 1.00111.82 C
ANISOU 1922 CD2 TYR A 252 14098 13376 15010 -1240 -973 -1922 C
ATOM 1923 CE1 TYR A 252 -15.440 4.737 41.410 1.00125.35 C
ANISOU 1923 CE1 TYR A 252 15966 14829 16832 -1601 -894 -1442 C
ATOM 1924 CE2 TYR A 252 -14.119 5.857 39.762 1.00112.50 C
ANISOU 1924 CE2 TYR A 252 14321 13370 15052 -1140 -906 -1782 C
ATOM 1925 CZ TYR A 252 -14.300 5.428 41.059 1.00124.32 C
ANISOU 1925 CZ TYR A 252 15898 14735 16602 -1314 -874 -1546 C
ATOM 1926 OH TYR A 252 -13.333 5.687 42.005 1.00136.74 O
ANISOU 1926 OH TYR A 252 17611 16229 18115 -1221 -827 -1406 O
ATOM 1927 N PRO A 253 -18.478 2.233 35.547 1.00113.12 N
ANISOU 1927 N PRO A 253 13974 13325 15681 -1948 -1585 -2543 N
ATOM 1928 CA PRO A 253 -18.899 2.198 34.136 1.00131.27 C
ANISOU 1928 CA PRO A 253 16171 15773 17931 -1931 -1710 -2816 C
ATOM 1929 C PRO A 253 -20.078 3.100 33.826 1.00129.11 C
ANISOU 1929 C PRO A 253 15637 15880 17538 -1989 -1652 -2752 C
ATOM 1930 O PRO A 253 -20.096 3.742 32.768 1.00120.82 O
ANISOU 1930 O PRO A 253 14508 15071 16326 -1849 -1687 -2905 O
ATOM 1931 CB PRO A 253 -19.241 0.718 33.916 1.00137.28 C
ANISOU 1931 CB PRO A 253 17014 16205 18942 -2164 -1919 -2947 C
ATOM 1932 CG PRO A 253 -19.617 0.218 35.273 1.00139.29 C
ANISOU 1932 CG PRO A 253 17307 16261 19357 -2399 -1874 -2648 C
ATOM 1933 CD PRO A 253 -18.748 0.965 36.245 1.00112.32 C
ANISOU 1933 CD PRO A 253 13978 12876 15823 -2213 -1693 -2442 C
ATOM 1934 N SER A 254 -21.069 3.169 34.715 1.00132.65 N
ANISOU 1934 N SER A 254 15942 16400 18060 -2195 -1568 -2528 N
ATOM 1935 CA SER A 254 -22.267 3.955 34.446 1.00124.06 C
ANISOU 1935 CA SER A 254 14569 15664 16903 -2248 -1527 -2484 C
ATOM 1936 C SER A 254 -22.036 5.456 34.560 1.00124.10 C
ANISOU 1936 C SER A 254 14493 15951 16708 -1985 -1365 -2394 C
ATOM 1937 O SER A 254 -22.945 6.226 34.229 1.00108.15 O
ANISOU 1937 O SER A 254 12237 14221 14635 -1970 -1353 -2376 O
ATOM 1938 CB SER A 254 -23.385 3.541 35.405 1.00125.79 C
ANISOU 1938 CB SER A 254 14631 15894 17268 -2555 -1466 -2288 C
ATOM 1939 OG SER A 254 -23.016 3.787 36.751 1.00130.86 O
ANISOU 1939 OG SER A 254 15350 16482 17887 -2553 -1275 -2051 O
ATOM 1940 N TYR A 255 -20.852 5.891 34.999 1.00115.70 N
ANISOU 1940 N TYR A 255 13613 14800 15549 -1779 -1260 -2342 N
ATOM 1941 CA TYR A 255 -20.646 7.277 35.397 1.00102.32 C
ANISOU 1941 CA TYR A 255 11859 13319 13698 -1570 -1095 -2217 C
ATOM 1942 C TYR A 255 -19.695 8.068 34.506 1.00 99.18 C
ANISOU 1942 C TYR A 255 11551 13011 13122 -1301 -1118 -2329 C
ATOM 1943 O TYR A 255 -19.724 9.301 34.556 1.00 97.65 O
ANISOU 1943 O TYR A 255 11279 13018 12806 -1140 -1028 -2245 O
ATOM 1944 CB TYR A 255 -20.118 7.337 36.840 1.00102.43 C
ANISOU 1944 CB TYR A 255 11991 13205 13724 -1575 -927 -2018 C
ATOM 1945 CG TYR A 255 -21.093 6.864 37.902 1.00103.77 C
ANISOU 1945 CG TYR A 255 12049 13373 14006 -1843 -845 -1850 C
ATOM 1946 CD1 TYR A 255 -22.228 7.603 38.216 1.00103.15 C
ANISOU 1946 CD1 TYR A 255 11704 13581 13908 -1889 -731 -1772 C
ATOM 1947 CD2 TYR A 255 -20.869 5.684 38.602 1.00118.57 C
ANISOU 1947 CD2 TYR A 255 14078 14963 16008 -2052 -883 -1764 C
ATOM 1948 CE1 TYR A 255 -23.115 7.177 39.191 1.00108.42 C
ANISOU 1948 CE1 TYR A 255 12245 14292 14656 -2151 -629 -1626 C
ATOM 1949 CE2 TYR A 255 -21.750 5.250 39.577 1.00125.72 C
ANISOU 1949 CE2 TYR A 255 14886 15890 16990 -2334 -801 -1584 C
ATOM 1950 CZ TYR A 255 -22.871 6.000 39.867 1.00119.15 C
ANISOU 1950 CZ TYR A 255 13772 15385 16113 -2389 -660 -1522 C
ATOM 1951 OH TYR A 255 -23.750 5.572 40.836 1.00123.80 O
ANISOU 1951 OH TYR A 255 14241 16040 16758 -2686 -553 -1352 O
ATOM 1952 N ILE A 256 -18.858 7.411 33.702 1.00112.94 N
ANISOU 1952 N ILE A 256 13451 14613 14847 -1252 -1234 -2519 N
ATOM 1953 CA ILE A 256 -17.798 8.083 32.956 1.00113.58 C
ANISOU 1953 CA ILE A 256 13629 14784 14743 -1021 -1228 -2616 C
ATOM 1954 C ILE A 256 -18.048 7.923 31.462 1.00115.03 C
ANISOU 1954 C ILE A 256 13763 15114 14828 -1026 -1388 -2839 C
ATOM 1955 O ILE A 256 -18.449 6.849 31.000 1.00116.60 O
ANISOU 1955 O ILE A 256 13964 15203 15135 -1178 -1526 -3002 O
ATOM 1956 CB ILE A 256 -16.407 7.536 33.344 1.00118.16 C
ANISOU 1956 CB ILE A 256 14428 15113 15356 -927 -1196 -2666 C
ATOM 1957 CG1 ILE A 256 -16.041 7.974 34.763 1.00114.85 C
ANISOU 1957 CG1 ILE A 256 14065 14610 14963 -891 -1039 -2429 C
ATOM 1958 CG2 ILE A 256 -15.339 8.003 32.364 1.00113.46 C
ANISOU 1958 CG2 ILE A 256 13905 14630 14573 -729 -1204 -2822 C
ATOM 1959 CD1 ILE A 256 -15.043 7.064 35.442 1.00121.57 C
ANISOU 1959 CD1 ILE A 256 15107 15149 15936 -887 -1054 -2430 C
ATOM 1960 N SER A 257 -17.801 9.017 30.696 1.00119.26 N
ANISOU 1960 N SER A 257 14266 15901 15147 -869 -1381 -2839 N
ATOM 1961 CA SER A 257 -17.941 9.063 29.240 1.00122.54 C
ANISOU 1961 CA SER A 257 14648 16514 15396 -863 -1527 -3022 C
ATOM 1962 C SER A 257 -16.621 8.698 28.570 1.00113.88 C
ANISOU 1962 C SER A 257 13724 15374 14173 -758 -1527 -3230 C
ATOM 1963 O SER A 257 -15.567 9.203 28.977 1.00120.68 O
ANISOU 1963 O SER A 257 14681 16203 14967 -611 -1399 -3158 O
ATOM 1964 CB SER A 257 -18.377 10.447 28.782 1.00127.94 C
ANISOU 1964 CB SER A 257 15213 17491 15909 -766 -1535 -2880 C
ATOM 1965 OG SER A 257 -18.287 10.574 27.373 1.00110.82 O
ANISOU 1965 OG SER A 257 13053 15531 13524 -753 -1671 -3030 O
ATOM 1966 N PRO A 258 -16.638 7.840 27.547 1.00108.58 N
ANISOU 1966 N PRO A 258 13080 14712 13462 -828 -1665 -3504 N
ATOM 1967 CA PRO A 258 -15.394 7.450 26.870 1.00106.20 C
ANISOU 1967 CA PRO A 258 12916 14398 13037 -719 -1652 -3750 C
ATOM 1968 C PRO A 258 -14.811 8.508 25.945 1.00107.52 C
ANISOU 1968 C PRO A 258 13084 14892 12875 -600 -1611 -3750 C
ATOM 1969 O PRO A 258 -13.741 8.275 25.373 1.00106.67 O
ANISOU 1969 O PRO A 258 13065 14828 12636 -511 -1570 -3953 O
ATOM 1970 CB PRO A 258 -15.816 6.205 26.072 1.00 98.13 C
ANISOU 1970 CB PRO A 258 11905 13295 12083 -853 -1825 -4062 C
ATOM 1971 CG PRO A 258 -17.274 6.388 25.841 1.00107.19 C
ANISOU 1971 CG PRO A 258 12896 14582 13249 -1018 -1949 -3967 C
ATOM 1972 CD PRO A 258 -17.798 7.067 27.073 1.00106.19 C
ANISOU 1972 CD PRO A 258 12680 14408 13258 -1023 -1838 -3625 C
ATOM 1973 N ILE A 259 -15.477 9.650 25.762 1.00108.98 N
ANISOU 1973 N ILE A 259 13169 15310 12928 -600 -1628 -3530 N
ATOM 1974 CA ILE A 259 -14.914 10.768 25.013 1.00102.51 C
ANISOU 1974 CA ILE A 259 12369 14774 11807 -504 -1595 -3456 C
ATOM 1975 C ILE A 259 -14.918 12.062 25.809 1.00 97.84 C
ANISOU 1975 C ILE A 259 11747 14201 11227 -410 -1494 -3127 C
ATOM 1976 O ILE A 259 -14.464 13.088 25.301 1.00 93.70 O
ANISOU 1976 O ILE A 259 11247 13877 10479 -342 -1474 -3015 O
ATOM 1977 CB ILE A 259 -15.639 10.983 23.668 1.00 96.21 C
ANISOU 1977 CB ILE A 259 11504 14277 10776 -592 -1771 -3533 C
ATOM 1978 CG1 ILE A 259 -17.062 11.493 23.905 1.00101.98 C
ANISOU 1978 CG1 ILE A 259 12074 15056 11616 -658 -1885 -3324 C
ATOM 1979 CG2 ILE A 259 -15.643 9.705 22.842 1.00 96.02 C
ANISOU 1979 CG2 ILE A 259 11515 14242 10724 -690 -1878 -3898 C
ATOM 1980 CD1 ILE A 259 -17.748 11.984 22.650 1.00104.69 C
ANISOU 1980 CD1 ILE A 259 12346 15714 11718 -719 -2078 -3321 C
ATOM 1981 N GLY A 260 -15.430 12.054 27.039 1.00109.47 N
ANISOU 1981 N GLY A 260 13172 15476 12948 -416 -1434 -2970 N
ATOM 1982 CA GLY A 260 -15.562 13.267 27.814 1.00125.50 C
ANISOU 1982 CA GLY A 260 15162 17521 15001 -326 -1347 -2694 C
ATOM 1983 C GLY A 260 -14.372 13.524 28.718 1.00103.05 C
ANISOU 1983 C GLY A 260 12439 14528 12187 -218 -1177 -2619 C
ATOM 1984 O GLY A 260 -13.393 12.778 28.751 1.00 92.44 O
ANISOU 1984 O GLY A 260 11200 13072 10852 -199 -1126 -2770 O
ATOM 1985 N CYS A 261 -14.467 14.622 29.460 1.00 88.06 N
ANISOU 1985 N CYS A 261 10518 12628 10313 -137 -1100 -2393 N
ATOM 1986 CA CYS A 261 -13.476 14.935 30.472 1.00 93.90 C
ANISOU 1986 CA CYS A 261 11360 13224 11096 -49 -950 -2302 C
ATOM 1987 C CYS A 261 -13.639 14.012 31.676 1.00 98.16 C
ANISOU 1987 C CYS A 261 11913 13523 11858 -106 -883 -2309 C
ATOM 1988 O CYS A 261 -14.638 13.304 31.828 1.00 91.99 O
ANISOU 1988 O CYS A 261 11047 12693 11210 -221 -938 -2345 O
ATOM 1989 CB CYS A 261 -13.581 16.399 30.892 1.00106.08 C
ANISOU 1989 CB CYS A 261 12881 14825 12601 47 -905 -2079 C
ATOM 1990 SG CYS A 261 -13.550 17.559 29.511 1.00130.55 S
ANISOU 1990 SG CYS A 261 15970 18182 15451 85 -1022 -2002 S
ATOM 1991 N LEU A 262 -12.640 14.021 32.530 1.00100.51 N
ANISOU 1991 N LEU A 262 12320 13679 12192 -42 -775 -2262 N
ATOM 1992 CA LEU A 262 -12.705 13.149 33.695 1.00 97.02 C
ANISOU 1992 CA LEU A 262 11918 13008 11938 -108 -727 -2239 C
ATOM 1993 C LEU A 262 -13.425 13.860 34.833 1.00 90.69 C
ANISOU 1993 C LEU A 262 11055 12203 11201 -117 -636 -2043 C
ATOM 1994 O LEU A 262 -13.102 15.014 35.131 1.00 90.89 O
ANISOU 1994 O LEU A 262 11094 12296 11145 -10 -567 -1929 O
ATOM 1995 CB LEU A 262 -11.309 12.740 34.138 1.00 79.33 C
ANISOU 1995 CB LEU A 262 9817 10610 9714 -36 -676 -2280 C
ATOM 1996 CG LEU A 262 -10.698 11.614 33.302 1.00 79.35 C
ANISOU 1996 CG LEU A 262 9867 10544 9737 -39 -760 -2522 C
ATOM 1997 CD1 LEU A 262 -9.233 11.406 33.654 1.00 98.23 C
ANISOU 1997 CD1 LEU A 262 12361 12820 12143 73 -712 -2569 C
ATOM 1998 CD2 LEU A 262 -11.491 10.326 33.472 1.00102.16 C
ANISOU 1998 CD2 LEU A 262 12750 13251 12817 -180 -852 -2604 C
ATOM 1999 N PRO A 263 -14.410 13.223 35.468 1.00 82.76 N
ANISOU 1999 N PRO A 263 9977 11131 10337 -250 -632 -2009 N
ATOM 2000 CA PRO A 263 -15.062 13.847 36.627 1.00 83.43 C
ANISOU 2000 CA PRO A 263 9991 11240 10468 -263 -515 -1850 C
ATOM 2001 C PRO A 263 -14.046 14.199 37.704 1.00 92.10 C
ANISOU 2001 C PRO A 263 11232 12228 11533 -189 -403 -1752 C
ATOM 2002 O PRO A 263 -13.191 13.386 38.066 1.00104.14 O
ANISOU 2002 O PRO A 263 12893 13580 13097 -215 -412 -1771 O
ATOM 2003 CB PRO A 263 -16.045 12.769 37.095 1.00 93.84 C
ANISOU 2003 CB PRO A 263 11231 12489 11934 -464 -528 -1848 C
ATOM 2004 CG PRO A 263 -16.369 12.029 35.836 1.00 87.04 C
ANISOU 2004 CG PRO A 263 10326 11649 11096 -531 -686 -2009 C
ATOM 2005 CD PRO A 263 -15.044 11.939 35.122 1.00 87.31 C
ANISOU 2005 CD PRO A 263 10516 11626 11033 -410 -732 -2123 C
ATOM 2006 N ALA A 264 -14.148 15.430 38.213 1.00 88.96 N
ANISOU 2006 N ALA A 264 10802 11923 11076 -89 -313 -1654 N
ATOM 2007 CA ALA A 264 -13.107 15.969 39.084 1.00 81.32 C
ANISOU 2007 CA ALA A 264 9972 10878 10050 -5 -226 -1577 C
ATOM 2008 C ALA A 264 -12.935 15.133 40.344 1.00 92.24 C
ANISOU 2008 C ALA A 264 11441 12114 11492 -116 -162 -1509 C
ATOM 2009 O ALA A 264 -11.805 14.835 40.748 1.00 98.48 O
ANISOU 2009 O ALA A 264 12379 12773 12265 -88 -167 -1490 O
ATOM 2010 CB ALA A 264 -13.424 17.419 39.446 1.00 79.85 C
ANISOU 2010 CB ALA A 264 9728 10800 9812 109 -154 -1504 C
ATOM 2011 N HIS A 265 -14.040 14.731 40.972 1.00 98.64 N
ANISOU 2011 N HIS A 265 12153 12956 12370 -255 -108 -1462 N
ATOM 2012 CA HIS A 265 -13.953 14.043 42.254 1.00 97.10 C
ANISOU 2012 CA HIS A 265 12046 12650 12198 -389 -41 -1356 C
ATOM 2013 C HIS A 265 -13.291 12.675 42.151 1.00100.20 C
ANISOU 2013 C HIS A 265 12574 12819 12679 -481 -156 -1369 C
ATOM 2014 O HIS A 265 -12.912 12.115 43.185 1.00102.07 O
ANISOU 2014 O HIS A 265 12932 12923 12927 -572 -138 -1257 O
ATOM 2015 CB HIS A 265 -15.351 13.918 42.878 1.00101.74 C
ANISOU 2015 CB HIS A 265 12472 13361 12824 -546 55 -1302 C
ATOM 2016 CG HIS A 265 -16.351 13.196 42.024 1.00103.58 C
ANISOU 2016 CG HIS A 265 12555 13632 13169 -668 -32 -1372 C
ATOM 2017 ND1 HIS A 265 -16.671 13.594 40.743 1.00103.17 N
ANISOU 2017 ND1 HIS A 265 12392 13679 13130 -568 -128 -1487 N
ATOM 2018 CD2 HIS A 265 -17.151 12.137 42.297 1.00108.09 C
ANISOU 2018 CD2 HIS A 265 13064 14167 13838 -900 -45 -1334 C
ATOM 2019 CE1 HIS A 265 -17.591 12.785 40.248 1.00110.29 C
ANISOU 2019 CE1 HIS A 265 13170 14602 14134 -724 -203 -1535 C
ATOM 2020 NE2 HIS A 265 -17.902 11.894 41.172 1.00109.68 N
ANISOU 2020 NE2 HIS A 265 13117 14437 14120 -931 -153 -1445 N
ATOM 2021 N LEU A 266 -13.110 12.147 40.940 1.00105.17 N
ANISOU 2021 N LEU A 266 13193 13400 13366 -451 -282 -1508 N
ATOM 2022 CA LEU A 266 -12.600 10.800 40.713 1.00103.53 C
ANISOU 2022 CA LEU A 266 13094 12964 13280 -522 -410 -1570 C
ATOM 2023 C LEU A 266 -11.098 10.760 40.465 1.00 99.20 C
ANISOU 2023 C LEU A 266 12679 12302 12712 -359 -464 -1640 C
ATOM 2024 O LEU A 266 -10.591 9.758 39.948 1.00 96.82 O
ANISOU 2024 O LEU A 266 12440 11831 12518 -355 -584 -1761 O
ATOM 2025 CB LEU A 266 -13.332 10.164 39.529 1.00 97.28 C
ANISOU 2025 CB LEU A 266 12202 12193 12568 -592 -520 -1724 C
ATOM 2026 CG LEU A 266 -14.489 9.207 39.812 1.00 96.83 C
ANISOU 2026 CG LEU A 266 12078 12070 12644 -834 -558 -1681 C
ATOM 2027 CD1 LEU A 266 -15.513 9.832 40.722 1.00110.78 C
ANISOU 2027 CD1 LEU A 266 13717 14011 14365 -935 -412 -1524 C
ATOM 2028 CD2 LEU A 266 -15.142 8.793 38.502 1.00103.29 C
ANISOU 2028 CD2 LEU A 266 12787 12944 13514 -878 -680 -1863 C
ATOM 2029 N LEU A 267 -10.366 11.804 40.842 1.00 89.81 N
ANISOU 2029 N LEU A 267 11525 11197 11401 -226 -382 -1580 N
ATOM 2030 CA LEU A 267 -8.972 11.927 40.439 1.00 93.38 C
ANISOU 2030 CA LEU A 267 12054 11604 11823 -71 -422 -1663 C
ATOM 2031 C LEU A 267 -7.971 11.758 41.580 1.00 97.61 C
ANISOU 2031 C LEU A 267 12722 11987 12378 -44 -424 -1550 C
ATOM 2032 O LEU A 267 -6.790 12.054 41.389 1.00 98.79 O
ANISOU 2032 O LEU A 267 12910 12133 12495 90 -440 -1601 O
ATOM 2033 CB LEU A 267 -8.766 13.271 39.739 1.00 87.20 C
ANISOU 2033 CB LEU A 267 11203 11040 10888 55 -361 -1696 C
ATOM 2034 CG LEU A 267 -9.622 13.451 38.483 1.00 73.92 C
ANISOU 2034 CG LEU A 267 9399 9518 9170 42 -396 -1802 C
ATOM 2035 CD1 LEU A 267 -9.448 14.844 37.928 1.00 71.74 C
ANISOU 2035 CD1 LEU A 267 9078 9435 8744 148 -353 -1777 C
ATOM 2036 CD2 LEU A 267 -9.282 12.406 37.425 1.00 82.41 C
ANISOU 2036 CD2 LEU A 267 10480 10536 10298 41 -504 -2000 C
ATOM 2037 N GLY A 268 -8.396 11.287 42.754 1.00 93.93 N
ANISOU 2037 N GLY A 268 12322 11413 11954 -180 -413 -1392 N
ATOM 2038 CA GLY A 268 -7.461 10.947 43.812 1.00 96.29 C
ANISOU 2038 CA GLY A 268 12762 11551 12274 -174 -457 -1273 C
ATOM 2039 C GLY A 268 -7.116 12.049 44.797 1.00 98.48 C
ANISOU 2039 C GLY A 268 13080 11943 12395 -139 -352 -1146 C
ATOM 2040 O GLY A 268 -6.537 11.750 45.846 1.00 92.14 O
ANISOU 2040 O GLY A 268 12398 11026 11586 -175 -391 -1016 O
ATOM 2041 N ASP A 269 -7.423 13.306 44.492 1.00106.28 N
ANISOU 2041 N ASP A 269 13981 13138 13260 -68 -239 -1182 N
ATOM 2042 CA ASP A 269 -7.260 14.406 45.437 1.00 84.45 C
ANISOU 2042 CA ASP A 269 11254 10477 10356 -43 -138 -1087 C
ATOM 2043 C ASP A 269 -8.595 15.132 45.543 1.00101.70 C
ANISOU 2043 C ASP A 269 13326 12836 12478 -94 -9 -1080 C
ATOM 2044 O ASP A 269 -9.421 15.064 44.631 1.00117.02 O
ANISOU 2044 O ASP A 269 15144 14846 14473 -102 -12 -1160 O
ATOM 2045 CB ASP A 269 -6.164 15.382 44.990 1.00 86.60 C
ANISOU 2045 CB ASP A 269 11534 10806 10566 118 -143 -1149 C
ATOM 2046 CG ASP A 269 -4.763 14.797 45.094 1.00111.41 C
ANISOU 2046 CG ASP A 269 14760 13807 13764 181 -254 -1156 C
ATOM 2047 OD1 ASP A 269 -4.637 13.642 45.555 1.00122.34 O
ANISOU 2047 OD1 ASP A 269 16214 15022 15248 115 -344 -1106 O
ATOM 2048 OD2 ASP A 269 -3.791 15.470 44.678 1.00109.83 O1-
ANISOU 2048 OD2 ASP A 269 14544 13661 13523 293 -262 -1210 O1-
ATOM 2049 N MET A 270 -8.797 15.838 46.658 1.00 92.27 N
ANISOU 2049 N MET A 270 12164 11722 11172 -122 98 -1000 N
ATOM 2050 CA MET A 270 -9.981 16.672 46.762 1.00 88.21 C
ANISOU 2050 CA MET A 270 11520 11385 10612 -125 227 -1030 C
ATOM 2051 C MET A 270 -10.026 17.733 45.673 1.00 89.27 C
ANISOU 2051 C MET A 270 11560 11601 10756 36 215 -1133 C
ATOM 2052 O MET A 270 -11.106 18.021 45.137 1.00 99.25 O
ANISOU 2052 O MET A 270 12674 12975 12061 44 246 -1184 O
ATOM 2053 CB MET A 270 -10.065 17.320 48.139 1.00 96.37 C
ANISOU 2053 CB MET A 270 12611 12499 11509 -159 348 -968 C
ATOM 2054 CG MET A 270 -10.952 18.504 48.183 1.00 85.75 C
ANISOU 2054 CG MET A 270 11134 11320 10125 -79 471 -1050 C
ATOM 2055 SD MET A 270 -12.613 18.054 48.620 1.00 90.14 S
ANISOU 2055 SD MET A 270 11512 12040 10695 -237 608 -1045 S
ATOM 2056 CE MET A 270 -12.318 17.134 50.119 1.00 94.22 C
ANISOU 2056 CE MET A 270 12189 12529 11081 -458 657 -887 C
ATOM 2057 N TRP A 271 -8.862 18.266 45.287 1.00 97.18 N
ANISOU 2057 N TRP A 271 12642 12554 11728 152 154 -1153 N
ATOM 2058 CA TRP A 271 -8.724 19.306 44.285 1.00 99.82 C
ANISOU 2058 CA TRP A 271 12920 12955 12051 280 127 -1213 C
ATOM 2059 C TRP A 271 -8.232 18.766 42.937 1.00102.56 C
ANISOU 2059 C TRP A 271 13244 13286 12439 305 22 -1276 C
ATOM 2060 O TRP A 271 -8.166 19.522 41.957 1.00107.75 O
ANISOU 2060 O TRP A 271 13854 14020 13066 382 -12 -1309 O
ATOM 2061 CB TRP A 271 -7.766 20.396 44.792 1.00100.99 C
ANISOU 2061 CB TRP A 271 13168 13084 12121 362 140 -1186 C
ATOM 2062 CG TRP A 271 -7.968 20.694 46.258 1.00 98.98 C
ANISOU 2062 CG TRP A 271 12976 12834 11800 321 235 -1146 C
ATOM 2063 CD1 TRP A 271 -8.913 21.511 46.800 1.00 99.90 C
ANISOU 2063 CD1 TRP A 271 13029 13037 11890 347 336 -1178 C
ATOM 2064 CD2 TRP A 271 -7.168 20.215 47.359 1.00 97.84 C
ANISOU 2064 CD2 TRP A 271 12966 12618 11592 252 230 -1079 C
ATOM 2065 NE1 TRP A 271 -8.779 21.535 48.170 1.00105.60 N
ANISOU 2065 NE1 TRP A 271 13841 13767 12515 285 415 -1149 N
ATOM 2066 CE2 TRP A 271 -7.714 20.756 48.536 1.00116.52 C
ANISOU 2066 CE2 TRP A 271 15354 15053 13864 219 342 -1072 C
ATOM 2067 CE3 TRP A 271 -6.051 19.370 47.463 1.00103.29 C
ANISOU 2067 CE3 TRP A 271 13751 13196 12297 223 133 -1030 C
ATOM 2068 CZ2 TRP A 271 -7.188 20.487 49.802 1.00139.18 C
ANISOU 2068 CZ2 TRP A 271 18357 17901 16626 135 357 -1002 C
ATOM 2069 CZ3 TRP A 271 -5.526 19.102 48.732 1.00130.10 C
ANISOU 2069 CZ3 TRP A 271 17272 16545 15615 153 128 -946 C
ATOM 2070 CH2 TRP A 271 -6.100 19.661 49.878 1.00139.84 C
ANISOU 2070 CH2 TRP A 271 18542 17864 16725 99 237 -924 C
ATOM 2071 N GLY A 272 -7.898 17.483 42.854 1.00 97.80 N
ANISOU 2071 N GLY A 272 12676 12586 11899 241 -37 -1299 N
ATOM 2072 CA GLY A 272 -7.545 16.882 41.590 1.00 83.90 C
ANISOU 2072 CA GLY A 272 10880 10823 10174 266 -124 -1404 C
ATOM 2073 C GLY A 272 -6.235 17.402 41.025 1.00 99.25 C
ANISOU 2073 C GLY A 272 12861 12796 12054 364 -152 -1442 C
ATOM 2074 O GLY A 272 -6.122 17.645 39.823 1.00101.43 O
ANISOU 2074 O GLY A 272 13079 13177 12284 402 -184 -1518 O
ATOM 2075 N ARG A 273 -5.247 17.552 41.907 1.00 95.30 N
ANISOU 2075 N ARG A 273 12451 12220 11540 388 -144 -1384 N
ATOM 2076 CA ARG A 273 -3.905 18.018 41.599 1.00 83.30 C
ANISOU 2076 CA ARG A 273 10953 10727 9971 462 -164 -1405 C
ATOM 2077 C ARG A 273 -3.018 16.884 41.093 1.00 82.17 C
ANISOU 2077 C ARG A 273 10797 10520 9904 494 -235 -1519 C
ATOM 2078 O ARG A 273 -2.644 16.835 39.911 1.00105.86 O
ANISOU 2078 O ARG A 273 13727 13623 12872 533 -248 -1636 O
ATOM 2079 CB ARG A 273 -3.286 18.632 42.837 1.00 85.22 C
ANISOU 2079 CB ARG A 273 11285 10916 10178 466 -140 -1303 C
ATOM 2080 CG ARG A 273 -1.987 19.317 42.639 1.00 92.50 C
ANISOU 2080 CG ARG A 273 12215 11880 11049 520 -157 -1305 C
ATOM 2081 CD ARG A 273 -1.640 20.079 43.899 1.00 86.61 C
ANISOU 2081 CD ARG A 273 11561 11090 10256 506 -139 -1207 C
ATOM 2082 NE ARG A 273 -0.297 20.639 43.897 1.00 85.97 N
ANISOU 2082 NE ARG A 273 11488 11031 10144 534 -172 -1200 N
ATOM 2083 CZ ARG A 273 0.343 20.953 45.011 1.00 88.74 C
ANISOU 2083 CZ ARG A 273 11920 11326 10472 519 -196 -1137 C
ATOM 2084 NH1 ARG A 273 -0.188 20.705 46.197 1.00 77.07 N
ANISOU 2084 NH1 ARG A 273 10531 9776 8977 477 -185 -1077 N
ATOM 2085 NH2 ARG A 273 1.531 21.551 44.937 1.00 80.57 N
ANISOU 2085 NH2 ARG A 273 10871 10329 9414 530 -230 -1132 N
ATOM 2086 N PHE A 274 -2.613 16.001 42.003 1.00 84.22 N
ANISOU 2086 N PHE A 274 11126 10615 10260 482 -286 -1488 N
ATOM 2087 CA PHE A 274 -1.788 14.842 41.684 1.00101.33 C
ANISOU 2087 CA PHE A 274 13284 12671 12547 536 -378 -1602 C
ATOM 2088 C PHE A 274 -2.707 13.650 41.441 1.00 96.54 C
ANISOU 2088 C PHE A 274 12680 11944 12058 473 -433 -1662 C
ATOM 2089 O PHE A 274 -3.646 13.425 42.211 1.00103.45 O
ANISOU 2089 O PHE A 274 13606 12746 12954 365 -423 -1544 O
ATOM 2090 CB PHE A 274 -0.812 14.522 42.826 1.00100.39 C
ANISOU 2090 CB PHE A 274 13243 12407 12492 563 -446 -1516 C
ATOM 2091 CG PHE A 274 0.016 15.697 43.261 1.00 94.85 C
ANISOU 2091 CG PHE A 274 12549 11808 11681 594 -405 -1443 C
ATOM 2092 CD1 PHE A 274 1.063 16.149 42.482 1.00 99.42 C
ANISOU 2092 CD1 PHE A 274 13038 12509 12228 673 -394 -1539 C
ATOM 2093 CD2 PHE A 274 -0.279 16.371 44.439 1.00 89.10 C
ANISOU 2093 CD2 PHE A 274 11913 11067 10872 530 -371 -1287 C
ATOM 2094 CE1 PHE A 274 1.823 17.231 42.877 1.00 96.62 C
ANISOU 2094 CE1 PHE A 274 12688 12239 11786 675 -368 -1464 C
ATOM 2095 CE2 PHE A 274 0.480 17.462 44.840 1.00 76.55 C
ANISOU 2095 CE2 PHE A 274 10340 9554 9191 549 -349 -1236 C
ATOM 2096 CZ PHE A 274 1.532 17.890 44.053 1.00 78.16 C
ANISOU 2096 CZ PHE A 274 10457 9857 9385 616 -354 -1316 C
ATOM 2097 N TRP A 275 -2.458 12.902 40.366 1.00 79.20 N
ANISOU 2097 N TRP A 275 10423 9741 9930 526 -486 -1854 N
ATOM 2098 CA TRP A 275 -3.223 11.698 40.070 1.00 93.58 C
ANISOU 2098 CA TRP A 275 12252 11418 11885 464 -564 -1939 C
ATOM 2099 C TRP A 275 -2.589 10.454 40.688 1.00 91.04 C
ANISOU 2099 C TRP A 275 12010 10817 11766 493 -697 -1953 C
ATOM 2100 O TRP A 275 -2.841 9.334 40.225 1.00 99.66 O
ANISOU 2100 O TRP A 275 13106 11752 13007 482 -795 -2086 O
ATOM 2101 CB TRP A 275 -3.368 11.527 38.555 1.00105.48 C
ANISOU 2101 CB TRP A 275 13663 13061 13354 500 -566 -2166 C
ATOM 2102 CG TRP A 275 -4.240 12.568 37.903 1.00 92.06 C
ANISOU 2102 CG TRP A 275 11898 11601 11481 448 -483 -2129 C
ATOM 2103 CD1 TRP A 275 -4.815 13.656 38.500 1.00 93.03 C
ANISOU 2103 CD1 TRP A 275 12028 11812 11509 403 -406 -1942 C
ATOM 2104 CD2 TRP A 275 -4.610 12.627 36.523 1.00 80.16 C
ANISOU 2104 CD2 TRP A 275 10308 10270 9879 445 -486 -2288 C
ATOM 2105 NE1 TRP A 275 -5.531 14.378 37.576 1.00 81.68 N
ANISOU 2105 NE1 TRP A 275 10513 10571 9951 384 -378 -1962 N
ATOM 2106 CE2 TRP A 275 -5.421 13.768 36.354 1.00 93.47 C
ANISOU 2106 CE2 TRP A 275 11956 12132 11427 398 -429 -2159 C
ATOM 2107 CE3 TRP A 275 -4.341 11.822 35.413 1.00 85.41 C
ANISOU 2107 CE3 TRP A 275 10930 10966 10558 480 -540 -2538 C
ATOM 2108 CZ2 TRP A 275 -5.964 14.121 35.121 1.00111.44 C
ANISOU 2108 CZ2 TRP A 275 14158 14610 13574 376 -443 -2239 C
ATOM 2109 CZ3 TRP A 275 -4.880 12.173 34.190 1.00 84.91 C
ANISOU 2109 CZ3 TRP A 275 10796 11127 10337 445 -534 -2635 C
ATOM 2110 CH2 TRP A 275 -5.682 13.312 34.053 1.00 94.98 C
ANISOU 2110 CH2 TRP A 275 12042 12574 11472 389 -494 -2470 C
ATOM 2111 N THR A 276 -1.758 10.641 41.717 1.00 95.21 N
ANISOU 2111 N THR A 276 12602 11267 12306 532 -722 -1818 N
ATOM 2112 CA THR A 276 -0.940 9.550 42.239 1.00107.87 C
ANISOU 2112 CA THR A 276 14270 12608 14108 596 -879 -1828 C
ATOM 2113 C THR A 276 -1.787 8.416 42.798 1.00106.72 C
ANISOU 2113 C THR A 276 14232 12202 14113 461 -989 -1730 C
ATOM 2114 O THR A 276 -1.525 7.241 42.515 1.00118.76 O
ANISOU 2114 O THR A 276 15781 13491 15851 509 -1137 -1850 O
ATOM 2115 CB THR A 276 0.009 10.070 43.321 1.00100.36 C
ANISOU 2115 CB THR A 276 13369 11648 13116 640 -898 -1666 C
ATOM 2116 OG1 THR A 276 0.583 11.319 42.913 1.00 99.13 O
ANISOU 2116 OG1 THR A 276 13121 11749 12793 707 -778 -1708 O
ATOM 2117 CG2 THR A 276 1.108 9.055 43.584 1.00 85.99 C
ANISOU 2117 CG2 THR A 276 11569 9593 11512 765 -1079 -1722 C
ATOM 2118 N ASN A 277 -2.798 8.741 43.601 1.00 92.12 N
ANISOU 2118 N ASN A 277 12445 10391 12166 285 -921 -1520 N
ATOM 2119 CA ASN A 277 -3.570 7.711 44.285 1.00 99.39 C
ANISOU 2119 CA ASN A 277 13472 11085 13208 113 -1017 -1378 C
ATOM 2120 C ASN A 277 -4.409 6.860 43.339 1.00108.41 C
ANISOU 2120 C ASN A 277 14571 12139 14480 45 -1068 -1534 C
ATOM 2121 O ASN A 277 -5.025 5.888 43.792 1.00121.09 O
ANISOU 2121 O ASN A 277 16264 13526 16220 -115 -1169 -1430 O
ATOM 2122 CB ASN A 277 -4.462 8.361 45.342 1.00 96.28 C
ANISOU 2122 CB ASN A 277 13121 10821 12640 -67 -895 -1138 C
ATOM 2123 CG ASN A 277 -3.662 9.077 46.409 1.00102.24 C
ANISOU 2123 CG ASN A 277 13948 11632 13267 -27 -871 -983 C
ATOM 2124 OD1 ASN A 277 -2.915 8.455 47.165 1.00111.23 O
ANISOU 2124 OD1 ASN A 277 15198 12576 14490 -18 -1016 -870 O
ATOM 2125 ND2 ASN A 277 -3.808 10.395 46.471 1.00110.31 N
ANISOU 2125 ND2 ASN A 277 14910 12910 14092 0 -708 -980 N
ATOM 2126 N LEU A 278 -4.445 7.194 42.049 1.00 98.54 N
ANISOU 2126 N LEU A 278 13198 11057 13186 143 -1010 -1773 N
ATOM 2127 CA LEU A 278 -5.150 6.406 41.046 1.00100.70 C
ANISOU 2127 CA LEU A 278 13428 11266 13568 90 -1072 -1963 C
ATOM 2128 C LEU A 278 -4.340 5.210 40.558 1.00103.52 C
ANISOU 2128 C LEU A 278 13821 11351 14159 213 -1248 -2176 C
ATOM 2129 O LEU A 278 -4.819 4.474 39.687 1.00114.64 O
ANISOU 2129 O LEU A 278 15205 12680 15673 182 -1319 -2376 O
ATOM 2130 CB LEU A 278 -5.521 7.298 39.857 1.00 95.39 C
ANISOU 2130 CB LEU A 278 12615 10910 12718 138 -948 -2126 C
ATOM 2131 CG LEU A 278 -6.554 8.394 40.127 1.00 94.33 C
ANISOU 2131 CG LEU A 278 12421 11020 12400 28 -803 -1961 C
ATOM 2132 CD1 LEU A 278 -6.813 9.207 38.868 1.00 84.61 C
ANISOU 2132 CD1 LEU A 278 11066 10068 11016 90 -730 -2114 C
ATOM 2133 CD2 LEU A 278 -7.851 7.814 40.677 1.00105.98 C
ANISOU 2133 CD2 LEU A 278 13912 12403 13952 -193 -823 -1829 C
ATOM 2134 N TYR A 279 -3.134 5.007 41.098 1.00 95.64 N
ANISOU 2134 N TYR A 279 12874 10209 13255 357 -1328 -2151 N
ATOM 2135 CA TYR A 279 -2.265 3.922 40.648 1.00101.90 C
ANISOU 2135 CA TYR A 279 13679 10742 14297 520 -1500 -2381 C
ATOM 2136 C TYR A 279 -2.922 2.561 40.840 1.00104.28 C
ANISOU 2136 C TYR A 279 14099 10670 14854 388 -1692 -2364 C
ATOM 2137 O TYR A 279 -2.872 1.705 39.948 1.00103.75 O
ANISOU 2137 O TYR A 279 14011 10448 14960 459 -1798 -2648 O
ATOM 2138 CB TYR A 279 -0.933 3.986 41.399 1.00102.63 C
ANISOU 2138 CB TYR A 279 13795 10741 14458 684 -1572 -2303 C
ATOM 2139 CG TYR A 279 0.089 2.954 40.971 1.00103.64 C
ANISOU 2139 CG TYR A 279 13900 10614 14863 900 -1750 -2559 C
ATOM 2140 CD1 TYR A 279 0.786 3.087 39.777 1.00106.53 C
ANISOU 2140 CD1 TYR A 279 14106 11159 15210 1098 -1681 -2914 C
ATOM 2141 CD2 TYR A 279 0.363 1.850 41.770 1.00106.21 C
ANISOU 2141 CD2 TYR A 279 14362 10523 15470 908 -1991 -2446 C
ATOM 2142 CE1 TYR A 279 1.725 2.144 39.389 1.00105.88 C
ANISOU 2142 CE1 TYR A 279 13979 10859 15393 1318 -1832 -3187 C
ATOM 2143 CE2 TYR A 279 1.298 0.904 41.390 1.00107.43 C
ANISOU 2143 CE2 TYR A 279 14486 10417 15916 1136 -2172 -2697 C
ATOM 2144 CZ TYR A 279 1.976 1.056 40.199 1.00106.08 C
ANISOU 2144 CZ TYR A 279 14133 10442 15731 1351 -2084 -3086 C
ATOM 2145 OH TYR A 279 2.907 0.118 39.816 1.00 96.68 O
ANISOU 2145 OH TYR A 279 12886 9008 14839 1599 -2252 -3377 O
ATOM 2146 N SER A 280 -3.535 2.342 42.009 1.00107.19 N
ANISOU 2146 N SER A 280 14595 10890 15242 180 -1740 -2034 N
ATOM 2147 CA SER A 280 -4.213 1.080 42.289 1.00110.87 C
ANISOU 2147 CA SER A 280 15187 10995 15943 2 -1926 -1959 C
ATOM 2148 C SER A 280 -5.173 0.694 41.177 1.00121.98 C
ANISOU 2148 C SER A 280 16526 12431 17389 -92 -1918 -2190 C
ATOM 2149 O SER A 280 -5.362 -0.496 40.893 1.00124.16 O
ANISOU 2149 O SER A 280 16877 12372 17927 -139 -2110 -2306 O
ATOM 2150 CB SER A 280 -4.963 1.180 43.621 1.00111.11 C
ANISOU 2150 CB SER A 280 15330 11003 15884 -268 -1902 -1553 C
ATOM 2151 OG SER A 280 -5.900 2.244 43.602 1.00113.22 O
ANISOU 2151 OG SER A 280 15493 11646 15878 -397 -1666 -1475 O
ATOM 2152 N LEU A 281 -5.771 1.682 40.522 1.00127.17 N
ANISOU 2152 N LEU A 281 17044 13473 17800 -117 -1718 -2265 N
ATOM 2153 CA LEU A 281 -6.733 1.425 39.463 1.00121.95 C
ANISOU 2153 CA LEU A 281 16306 12890 17141 -217 -1713 -2469 C
ATOM 2154 C LEU A 281 -6.079 1.410 38.094 1.00117.03 C
ANISOU 2154 C LEU A 281 15589 12373 16506 5 -1715 -2869 C
ATOM 2155 O LEU A 281 -6.594 0.770 37.173 1.00121.36 O
ANISOU 2155 O LEU A 281 16113 12863 17135 -43 -1794 -3111 O
ATOM 2156 CB LEU A 281 -7.829 2.489 39.505 1.00107.97 C
ANISOU 2156 CB LEU A 281 14429 11480 15116 -372 -1520 -2318 C
ATOM 2157 CG LEU A 281 -8.422 2.762 40.890 1.00124.41 C
ANISOU 2157 CG LEU A 281 16569 13565 17139 -573 -1454 -1942 C
ATOM 2158 CD1 LEU A 281 -9.407 3.919 40.852 1.00121.40 C
ANISOU 2158 CD1 LEU A 281 16047 13562 16518 -664 -1252 -1852 C
ATOM 2159 CD2 LEU A 281 -9.097 1.515 41.426 1.00120.93 C
ANISOU 2159 CD2 LEU A 281 16238 12792 16918 -819 -1614 -1809 C
ATOM 2160 N THR A 282 -4.943 2.090 37.944 1.00115.08 N
ANISOU 2160 N THR A 282 15283 12294 16149 233 -1628 -2949 N
ATOM 2161 CA THR A 282 -4.313 2.257 36.641 1.00114.13 C
ANISOU 2161 CA THR A 282 15047 12369 15947 424 -1580 -3313 C
ATOM 2162 C THR A 282 -3.028 1.457 36.493 1.00115.81 C
ANISOU 2162 C THR A 282 15273 12350 16381 661 -1703 -3553 C
ATOM 2163 O THR A 282 -2.311 1.652 35.508 1.00109.22 O
ANISOU 2163 O THR A 282 14322 11715 15460 839 -1636 -3859 O
ATOM 2164 CB THR A 282 -4.010 3.733 36.387 1.00106.80 C
ANISOU 2164 CB THR A 282 14006 11871 14702 491 -1367 -3252 C
ATOM 2165 OG1 THR A 282 -3.188 4.228 37.450 1.00105.15 O
ANISOU 2165 OG1 THR A 282 13832 11633 14487 567 -1333 -3027 O
ATOM 2166 CG2 THR A 282 -5.297 4.555 36.296 1.00 94.15 C
ANISOU 2166 CG2 THR A 282 12361 10515 12896 300 -1256 -3083 C
ATOM 2167 N VAL A 283 -2.722 0.568 37.437 1.00118.69 N
ANISOU 2167 N VAL A 283 15765 12309 17024 666 -1886 -3421 N
ATOM 2168 CA VAL A 283 -1.425 -0.126 37.412 1.00113.83 C
ANISOU 2168 CA VAL A 283 15144 11460 16648 926 -2021 -3629 C
ATOM 2169 C VAL A 283 -1.309 -0.932 36.124 1.00114.63 C
ANISOU 2169 C VAL A 283 15184 11495 16874 1050 -2089 -4101 C
ATOM 2170 O VAL A 283 -2.209 -1.738 35.811 1.00105.82 O
ANISOU 2170 O VAL A 283 14148 10167 15891 903 -2209 -4186 O
ATOM 2171 CB VAL A 283 -1.262 -1.030 38.649 1.00112.76 C
ANISOU 2171 CB VAL A 283 15179 10852 16810 886 -2253 -3375 C
ATOM 2172 CG1 VAL A 283 -2.521 -1.857 38.895 1.00133.20 C
ANISOU 2172 CG1 VAL A 283 17911 13160 19537 610 -2385 -3239 C
ATOM 2173 CG2 VAL A 283 -0.027 -1.931 38.512 1.00104.96 C
ANISOU 2173 CG2 VAL A 283 14180 9561 16141 1174 -2445 -3634 C
ATOM 2174 N PRO A 284 -0.244 -0.749 35.339 1.00110.17 N
ANISOU 2174 N PRO A 284 14472 11122 16264 1303 -2013 -4430 N
ATOM 2175 CA PRO A 284 -0.160 -1.448 34.046 1.00 98.08 C
ANISOU 2175 CA PRO A 284 12873 9593 14801 1417 -2048 -4922 C
ATOM 2176 C PRO A 284 -0.116 -2.960 34.175 1.00100.12 C
ANISOU 2176 C PRO A 284 13248 9303 15489 1485 -2330 -5104 C
ATOM 2177 O PRO A 284 -0.824 -3.662 33.445 1.00116.48 O
ANISOU 2177 O PRO A 284 15364 11254 17639 1401 -2416 -5350 O
ATOM 2178 CB PRO A 284 1.136 -0.884 33.447 1.00 98.91 C
ANISOU 2178 CB PRO A 284 12783 10027 14771 1676 -1894 -5178 C
ATOM 2179 CG PRO A 284 1.277 0.463 34.099 1.00106.35 C
ANISOU 2179 CG PRO A 284 13687 11279 15440 1598 -1718 -4799 C
ATOM 2180 CD PRO A 284 0.850 0.216 35.513 1.00109.97 C
ANISOU 2180 CD PRO A 284 14319 11390 16074 1465 -1862 -4381 C
ATOM 2181 N PHE A 285 0.706 -3.485 35.082 1.00108.01 N
ANISOU 2181 N PHE A 285 14304 9952 16782 1634 -2498 -4991 N
ATOM 2182 CA PHE A 285 0.830 -4.926 35.303 1.00118.20 C
ANISOU 2182 CA PHE A 285 15723 10661 18526 1716 -2805 -5129 C
ATOM 2183 C PHE A 285 0.669 -5.160 36.804 1.00133.25 C
ANISOU 2183 C PHE A 285 17812 12213 20604 1576 -2979 -4619 C
ATOM 2184 O PHE A 285 1.644 -5.095 37.556 1.00136.86 O
ANISOU 2184 O PHE A 285 18257 12570 21175 1746 -3052 -4480 O
ATOM 2185 CB PHE A 285 2.159 -5.445 34.767 1.00121.26 C
ANISOU 2185 CB PHE A 285 15972 10964 19137 2098 -2870 -5574 C
ATOM 2186 CG PHE A 285 2.426 -5.062 33.336 1.00120.66 C
ANISOU 2186 CG PHE A 285 15695 11335 18814 2226 -2651 -6057 C
ATOM 2187 CD1 PHE A 285 1.919 -5.819 32.291 1.00125.70 C
ANISOU 2187 CD1 PHE A 285 16352 11886 19523 2217 -2712 -6478 C
ATOM 2188 CD2 PHE A 285 3.164 -3.929 33.037 1.00119.99 C
ANISOU 2188 CD2 PHE A 285 15411 11771 18408 2327 -2387 -6080 C
ATOM 2189 CE1 PHE A 285 2.161 -5.460 30.974 1.00128.47 C
ANISOU 2189 CE1 PHE A 285 16518 12713 19582 2301 -2493 -6871 C
ATOM 2190 CE2 PHE A 285 3.406 -3.564 31.728 1.00119.47 C
ANISOU 2190 CE2 PHE A 285 15167 12145 18080 2411 -2181 -6492 C
ATOM 2191 CZ PHE A 285 2.905 -4.330 30.694 1.00127.52 C
ANISOU 2191 CZ PHE A 285 16208 13098 19147 2407 -2237 -6913 C
ATOM 2192 N GLY A 286 -0.565 -5.444 37.225 1.00136.50 N
ANISOU 2192 N GLY A 286 18386 12455 21022 1252 -3050 -4344 N
ATOM 2193 CA GLY A 286 -0.885 -5.413 38.642 1.00129.86 C
ANISOU 2193 CA GLY A 286 17707 11422 20214 1047 -3140 -3811 C
ATOM 2194 C GLY A 286 -0.167 -6.468 39.465 1.00130.28 C
ANISOU 2194 C GLY A 286 17904 10919 20678 1168 -3465 -3704 C
ATOM 2195 O GLY A 286 0.194 -6.223 40.619 1.00127.33 O
ANISOU 2195 O GLY A 286 17608 10483 20289 1135 -3520 -3318 O
ATOM 2196 N GLN A 287 0.043 -7.655 38.893 1.00132.33 N
ANISOU 2196 N GLN A 287 18209 10760 21311 1310 -3702 -4044 N
ATOM 2197 CA GLN A 287 0.600 -8.757 39.674 1.00146.10 C
ANISOU 2197 CA GLN A 287 20116 11900 23494 1407 -4063 -3920 C
ATOM 2198 C GLN A 287 2.042 -8.487 40.087 1.00148.28 C
ANISOU 2198 C GLN A 287 20284 12207 23850 1750 -4102 -3939 C
ATOM 2199 O GLN A 287 2.447 -8.832 41.203 1.00153.23 O
ANISOU 2199 O GLN A 287 21045 12515 24660 1749 -4329 -3588 O
ATOM 2200 CB GLN A 287 0.497 -10.064 38.889 1.00151.86 C
ANISOU 2200 CB GLN A 287 20912 12159 24628 1504 -4314 -4331 C
ATOM 2201 CG GLN A 287 -0.928 -10.456 38.545 1.00155.75 C
ANISOU 2201 CG GLN A 287 21523 12563 25092 1141 -4327 -4298 C
ATOM 2202 CD GLN A 287 -1.771 -10.697 39.783 1.00165.11 C
ANISOU 2202 CD GLN A 287 22931 13498 26304 752 -4458 -3702 C
ATOM 2203 OE1 GLN A 287 -1.297 -11.260 40.770 1.00171.84 O
ANISOU 2203 OE1 GLN A 287 23940 13941 27412 773 -4715 -3407 O
ATOM 2204 NE2 GLN A 287 -3.027 -10.267 39.739 1.00174.57 N
ANISOU 2204 NE2 GLN A 287 24135 14962 27231 390 -4284 -3517 N
ATOM 2205 N LYS A 288 2.830 -7.876 39.212 1.00135.46 N
ANISOU 2205 N LYS A 288 18412 10973 22082 2029 -3893 -4330 N
ATOM 2206 CA LYS A 288 4.225 -7.606 39.541 1.00134.66 C
ANISOU 2206 CA LYS A 288 18166 10935 22063 2353 -3921 -4378 C
ATOM 2207 C LYS A 288 4.314 -6.461 40.544 1.00139.46 C
ANISOU 2207 C LYS A 288 18776 11875 22338 2206 -3766 -3903 C
ATOM 2208 O LYS A 288 3.774 -5.377 40.292 1.00130.43 O
ANISOU 2208 O LYS A 288 17562 11214 20783 2034 -3460 -3826 O
ATOM 2209 CB LYS A 288 5.020 -7.283 38.279 1.00117.68 C
ANISOU 2209 CB LYS A 288 15732 9146 19836 2661 -3719 -4942 C
ATOM 2210 CG LYS A 288 5.311 -8.506 37.422 1.00119.95 C
ANISOU 2210 CG LYS A 288 15963 9172 20438 2863 -3868 -5380 C
ATOM 2211 CD LYS A 288 6.244 -8.179 36.269 1.00141.76 C
ANISOU 2211 CD LYS A 288 18406 12408 23050 3138 -3626 -5856 C
ATOM 2212 CE LYS A 288 6.673 -9.444 35.538 1.00149.45 C
ANISOU 2212 CE LYS A 288 19296 13195 24294 3325 -3756 -6205 C
ATOM 2213 NZ LYS A 288 7.474 -9.151 34.317 1.00153.46 N
ANISOU 2213 NZ LYS A 288 19495 14197 24617 3546 -3499 -6681 N
ATOM 2214 N PRO A 289 4.979 -6.654 41.678 1.00139.31 N
ANISOU 2214 N PRO A 289 18839 11608 22485 2271 -3982 -3588 N
ATOM 2215 CA PRO A 289 4.993 -5.628 42.723 1.00130.24 C
ANISOU 2215 CA PRO A 289 17725 10743 21017 2102 -3860 -3129 C
ATOM 2216 C PRO A 289 6.042 -4.557 42.451 1.00129.63 C
ANISOU 2216 C PRO A 289 17388 11136 20729 2325 -3640 -3286 C
ATOM 2217 O PRO A 289 6.926 -4.703 41.605 1.00132.54 O
ANISOU 2217 O PRO A 289 17543 11580 21237 2634 -3617 -3715 O
ATOM 2218 CB PRO A 289 5.337 -6.433 43.977 1.00117.46 C
ANISOU 2218 CB PRO A 289 16310 8627 19693 2091 -4232 -2760 C
ATOM 2219 CG PRO A 289 6.260 -7.490 43.460 1.00124.97 C
ANISOU 2219 CG PRO A 289 17181 9182 21120 2461 -4500 -3143 C
ATOM 2220 CD PRO A 289 5.750 -7.847 42.075 1.00117.11 C
ANISOU 2220 CD PRO A 289 16101 8223 20173 2507 -4375 -3636 C
ATOM 2221 N ASN A 290 5.926 -3.463 43.198 1.00133.76 N
ANISOU 2221 N ASN A 290 17930 11986 20908 2150 -3475 -2934 N
ATOM 2222 CA ASN A 290 6.903 -2.390 43.119 1.00134.93 C
ANISOU 2222 CA ASN A 290 17858 12556 20852 2310 -3290 -3007 C
ATOM 2223 C ASN A 290 8.130 -2.719 43.963 1.00136.72 C
ANISOU 2223 C ASN A 290 18054 12564 21328 2528 -3552 -2895 C
ATOM 2224 O ASN A 290 8.092 -3.555 44.871 1.00143.43 O
ANISOU 2224 O ASN A 290 19102 12976 22420 2489 -3862 -2628 O
ATOM 2225 CB ASN A 290 6.295 -1.063 43.575 1.00131.08 C
ANISOU 2225 CB ASN A 290 17406 12482 19916 2044 -3026 -2700 C
ATOM 2226 CG ASN A 290 5.914 -0.166 42.414 1.00142.87 C
ANISOU 2226 CG ASN A 290 18739 14433 21114 2010 -2691 -2956 C
ATOM 2227 OD1 ASN A 290 6.588 -0.147 41.383 1.00149.70 O
ANISOU 2227 OD1 ASN A 290 19396 15463 22021 2229 -2605 -3345 O
ATOM 2228 ND2 ASN A 290 4.837 0.593 42.579 1.00126.79 N
ANISOU 2228 ND2 ASN A 290 16789 12615 18769 1736 -2505 -2736 N
ATOM 2229 N ILE A 291 9.230 -2.042 43.650 1.00130.11 N
ANISOU 2229 N ILE A 291 16962 12048 20427 2749 -3432 -3090 N
ATOM 2230 CA ILE A 291 10.497 -2.249 44.344 1.00128.60 C
ANISOU 2230 CA ILE A 291 16679 11718 20466 2984 -3666 -3029 C
ATOM 2231 C ILE A 291 10.411 -1.546 45.695 1.00128.96 C
ANISOU 2231 C ILE A 291 16881 11842 20277 2762 -3704 -2519 C
ATOM 2232 O ILE A 291 10.410 -0.315 45.763 1.00125.20 O
ANISOU 2232 O ILE A 291 16331 11799 19440 2640 -3447 -2429 O
ATOM 2233 CB ILE A 291 11.678 -1.724 43.521 1.00124.09 C
ANISOU 2233 CB ILE A 291 15749 11510 19888 3266 -3502 -3419 C
ATOM 2234 CG1 ILE A 291 11.870 -2.564 42.258 1.00129.44 C
ANISOU 2234 CG1 ILE A 291 16268 12086 20826 3516 -3496 -3956 C
ATOM 2235 CG2 ILE A 291 12.953 -1.739 44.348 1.00133.58 C
ANISOU 2235 CG2 ILE A 291 16833 12638 21282 3472 -3726 -3306 C
ATOM 2236 CD1 ILE A 291 13.073 -2.148 41.439 1.00133.27 C
ANISOU 2236 CD1 ILE A 291 16378 12945 21315 3797 -3331 -4364 C
ATOM 2237 N ASP A 292 10.335 -2.325 46.773 1.00127.83 N
ANISOU 2237 N ASP A 292 16964 11273 20331 2700 -4036 -2185 N
ATOM 2238 CA ASP A 292 10.265 -1.786 48.131 1.00129.74 C
ANISOU 2238 CA ASP A 292 17379 11568 20348 2482 -4107 -1698 C
ATOM 2239 C ASP A 292 11.380 -2.417 48.961 1.00146.51 C
ANISOU 2239 C ASP A 292 19502 13382 22782 2691 -4497 -1560 C
ATOM 2240 O ASP A 292 11.272 -3.572 49.384 1.00160.50 O
ANISOU 2240 O ASP A 292 21453 14657 24872 2713 -4835 -1421 O
ATOM 2241 CB ASP A 292 8.899 -2.037 48.758 1.00131.75 C
ANISOU 2241 CB ASP A 292 17946 11664 20451 2116 -4116 -1342 C
ATOM 2242 CG ASP A 292 8.680 -1.221 50.017 1.00120.82 C
ANISOU 2242 CG ASP A 292 16712 10479 18716 1856 -4075 -898 C
ATOM 2243 OD1 ASP A 292 8.628 0.024 49.917 1.00105.17 O
ANISOU 2243 OD1 ASP A 292 14625 8947 16387 1782 -3776 -924 O
ATOM 2244 OD2 ASP A 292 8.562 -1.823 51.104 1.00120.35 O1-
ANISOU 2244 OD2 ASP A 292 16883 10123 18722 1720 -4348 -526 O1-
ATOM 2245 N VAL A 293 12.440 -1.649 49.205 1.00150.23 N
ANISOU 2245 N VAL A 293 19773 14139 23168 2832 -4466 -1582 N
ATOM 2246 CA VAL A 293 13.605 -2.135 49.936 1.00152.94 C
ANISOU 2246 CA VAL A 293 20061 14248 23802 3058 -4835 -1477 C
ATOM 2247 C VAL A 293 13.420 -1.907 51.430 1.00144.37 C
ANISOU 2247 C VAL A 293 19239 13104 22508 2800 -5016 -935 C
ATOM 2248 O VAL A 293 14.362 -2.079 52.213 1.00137.59 O
ANISOU 2248 O VAL A 293 18354 12129 21795 2931 -5316 -770 O
ATOM 2249 CB VAL A 293 14.893 -1.457 49.435 1.00151.66 C
ANISOU 2249 CB VAL A 293 19518 14438 23668 3335 -4725 -1788 C
ATOM 2250 CG1 VAL A 293 15.097 -1.740 47.957 1.00151.20 C
ANISOU 2250 CG1 VAL A 293 19196 14461 23794 3583 -4542 -2337 C
ATOM 2251 CG2 VAL A 293 14.835 0.042 49.690 1.00146.37 C
ANISOU 2251 CG2 VAL A 293 18802 14290 22520 3116 -4416 -1652 C
ATOM 2252 N THR A 294 12.208 -1.517 51.835 1.00140.22 N
ANISOU 2252 N THR A 294 18961 12683 21635 2433 -4836 -664 N
ATOM 2253 CA THR A 294 11.932 -1.300 53.253 1.00140.49 C
ANISOU 2253 CA THR A 294 19256 12701 21421 2156 -4975 -162 C
ATOM 2254 C THR A 294 12.176 -2.568 54.061 1.00146.41 C
ANISOU 2254 C THR A 294 20212 12917 22500 2191 -5457 124 C
ATOM 2255 O THR A 294 12.796 -2.523 55.131 1.00141.80 O
ANISOU 2255 O THR A 294 19710 12291 21876 2173 -5717 432 O
ATOM 2256 CB THR A 294 10.495 -0.815 53.446 1.00132.59 C
ANISOU 2256 CB THR A 294 18463 11883 20034 1770 -4689 30 C
ATOM 2257 OG1 THR A 294 10.330 0.464 52.822 1.00144.28 O
ANISOU 2257 OG1 THR A 294 19765 13853 21201 1740 -4279 -189 O
ATOM 2258 CG2 THR A 294 10.161 -0.699 54.929 1.00129.96 C
ANISOU 2258 CG2 THR A 294 18410 11536 19434 1470 -4829 536 C
ATOM 2259 N ASP A 295 11.702 -3.710 53.561 1.00149.35 N
ANISOU 2259 N ASP A 295 20677 12866 23205 2237 -5603 32 N
ATOM 2260 CA ASP A 295 11.932 -4.971 54.255 1.00153.06 C
ANISOU 2260 CA ASP A 295 21351 12768 24036 2279 -6093 302 C
ATOM 2261 C ASP A 295 13.420 -5.291 54.331 1.00154.86 C
ANISOU 2261 C ASP A 295 21372 12839 24630 2684 -6419 169 C
ATOM 2262 O ASP A 295 13.892 -5.853 55.326 1.00136.03 O
ANISOU 2262 O ASP A 295 19141 10147 22398 2694 -6836 517 O
ATOM 2263 CB ASP A 295 11.172 -6.097 53.555 1.00158.43 C
ANISOU 2263 CB ASP A 295 22144 13015 25037 2270 -6176 159 C
ATOM 2264 CG ASP A 295 9.734 -6.204 54.020 1.00169.75 C
ANISOU 2264 CG ASP A 295 23884 14414 26198 1808 -6068 508 C
ATOM 2265 OD1 ASP A 295 9.408 -5.637 55.084 1.00164.81 O
ANISOU 2265 OD1 ASP A 295 23425 14005 25189 1509 -6023 921 O
ATOM 2266 OD2 ASP A 295 8.929 -6.852 53.318 1.00177.93 O1-
ANISOU 2266 OD2 ASP A 295 24981 15225 27398 1738 -6024 354 O1-
ATOM 2267 N ALA A 296 14.177 -4.928 53.293 1.00160.46 N
ANISOU 2267 N ALA A 296 21720 13774 25475 3014 -6238 -328 N
ATOM 2268 CA ALA A 296 15.613 -5.185 53.298 1.00162.25 C
ANISOU 2268 CA ALA A 296 21688 13904 26057 3415 -6516 -501 C
ATOM 2269 C ALA A 296 16.343 -4.302 54.301 1.00159.23 C
ANISOU 2269 C ALA A 296 21260 13832 25407 3352 -6577 -219 C
ATOM 2270 O ALA A 296 17.357 -4.722 54.869 1.00145.69 O
ANISOU 2270 O ALA A 296 19473 11912 23970 3575 -6966 -118 O
ATOM 2271 CB ALA A 296 16.188 -4.982 51.898 1.00165.46 C
ANISOU 2271 CB ALA A 296 21698 14536 26631 3749 -6259 -1119 C
ATOM 2272 N MET A 297 15.852 -3.081 54.528 1.00157.60 N
ANISOU 2272 N MET A 297 21092 14110 24679 3061 -6217 -100 N
ATOM 2273 CA MET A 297 16.492 -2.196 55.496 1.00157.95 C
ANISOU 2273 CA MET A 297 21115 14456 24445 2973 -6269 153 C
ATOM 2274 C MET A 297 16.312 -2.715 56.917 1.00161.52 C
ANISOU 2274 C MET A 297 21914 14618 24837 2761 -6658 704 C
ATOM 2275 O MET A 297 17.264 -2.736 57.707 1.00150.65 O
ANISOU 2275 O MET A 297 20499 13203 23539 2868 -6984 889 O
ATOM 2276 CB MET A 297 15.934 -0.777 55.365 1.00142.40 C
ANISOU 2276 CB MET A 297 19122 13035 21948 2712 -5793 123 C
ATOM 2277 CG MET A 297 16.265 -0.093 54.049 1.00136.99 C
ANISOU 2277 CG MET A 297 18084 12699 21266 2896 -5424 -371 C
ATOM 2278 SD MET A 297 15.346 1.439 53.798 1.00144.70 S
ANISOU 2278 SD MET A 297 19095 14217 21667 2569 -4889 -382 S
ATOM 2279 CE MET A 297 15.936 2.419 55.176 1.00141.37 C
ANISOU 2279 CE MET A 297 18742 14052 20920 2402 -4997 -36 C
ATOM 2280 N VAL A 298 15.094 -3.141 57.260 1.00155.91 N
ANISOU 2280 N VAL A 298 21541 13720 23978 2444 -6634 982 N
ATOM 2281 CA VAL A 298 14.843 -3.681 58.594 1.00146.60 C
ANISOU 2281 CA VAL A 298 20713 12279 22708 2196 -6991 1533 C
ATOM 2282 C VAL A 298 15.617 -4.977 58.799 1.00149.24 C
ANISOU 2282 C VAL A 298 21071 12043 23589 2472 -7545 1620 C
ATOM 2283 O VAL A 298 16.101 -5.261 59.902 1.00139.55 O
ANISOU 2283 O VAL A 298 20002 10658 22363 2423 -7941 2017 O
ATOM 2284 CB VAL A 298 13.331 -3.880 58.812 1.00134.88 C
ANISOU 2284 CB VAL A 298 19550 10741 20958 1782 -6812 1782 C
ATOM 2285 CG1 VAL A 298 13.056 -4.422 60.207 1.00125.84 C
ANISOU 2285 CG1 VAL A 298 18773 9367 19674 1484 -7161 2374 C
ATOM 2286 CG2 VAL A 298 12.588 -2.572 58.590 1.00132.96 C
ANISOU 2286 CG2 VAL A 298 19255 11055 20209 1550 -6278 1668 C
ATOM 2287 N ASP A 299 15.758 -5.777 57.738 1.00173.99 N
ANISOU 2287 N ASP A 299 24049 14858 27199 2776 -7596 1242 N
ATOM 2288 CA ASP A 299 16.471 -7.047 57.853 1.00179.21 C
ANISOU 2288 CA ASP A 299 24665 15132 28297 2969 -7962 1217 C
ATOM 2289 C ASP A 299 17.935 -6.842 58.217 1.00166.52 C
ANISOU 2289 C ASP A 299 22785 13671 26813 3241 -8164 1149 C
ATOM 2290 O ASP A 299 18.529 -7.686 58.897 1.00158.32 O
ANISOU 2290 O ASP A 299 21796 12387 25970 3271 -8519 1341 O
ATOM 2291 CB ASP A 299 16.357 -7.836 56.548 1.00182.85 C
ANISOU 2291 CB ASP A 299 24953 15374 29149 3207 -7856 725 C
ATOM 2292 CG ASP A 299 14.979 -8.437 56.348 1.00193.51 C
ANISOU 2292 CG ASP A 299 26599 16460 30464 2915 -7778 846 C
ATOM 2293 OD1 ASP A 299 14.152 -8.357 57.280 1.00195.10 O
ANISOU 2293 OD1 ASP A 299 27138 16625 30366 2523 -7829 1337 O
ATOM 2294 OD2 ASP A 299 14.722 -8.987 55.256 1.00203.21 O1-
ANISOU 2294 OD2 ASP A 299 27715 17547 31950 3061 -7658 445 O1-
ATOM 2295 N GLN A 300 18.532 -5.735 57.780 1.00154.86 N
ANISOU 2295 N GLN A 300 21013 12595 25232 3430 -7952 881 N
ATOM 2296 CA GLN A 300 19.923 -5.427 58.076 1.00159.83 C
ANISOU 2296 CA GLN A 300 21346 13418 25962 3671 -8110 795 C
ATOM 2297 C GLN A 300 20.073 -4.471 59.255 1.00164.99 C
ANISOU 2297 C GLN A 300 22135 14358 26196 3440 -8196 1210 C
ATOM 2298 O GLN A 300 21.187 -4.016 59.532 1.00156.62 O
ANISOU 2298 O GLN A 300 20824 13523 25162 3602 -8303 1150 O
ATOM 2299 CB GLN A 300 20.606 -4.862 56.829 1.00159.38 C
ANISOU 2299 CB GLN A 300 20832 13656 26071 4020 -7828 213 C
ATOM 2300 CG GLN A 300 20.524 -5.800 55.629 1.00162.08 C
ANISOU 2300 CG GLN A 300 21024 13769 26792 4248 -7726 -242 C
ATOM 2301 CD GLN A 300 21.038 -5.175 54.347 1.00157.40 C
ANISOU 2301 CD GLN A 300 20001 13533 26272 4532 -7378 -816 C
ATOM 2302 OE1 GLN A 300 21.818 -4.224 54.374 1.00162.46 O
ANISOU 2302 OE1 GLN A 300 20371 14560 26798 4633 -7287 -907 O
ATOM 2303 NE2 GLN A 300 20.599 -5.709 53.212 1.00148.37 N
ANISOU 2303 NE2 GLN A 300 18789 12285 25300 4637 -7178 -1207 N
ATOM 2304 N ALA A 301 18.973 -4.158 59.947 1.00167.04 N
ANISOU 2304 N ALA A 301 22779 14634 26056 3051 -8143 1616 N
ATOM 2305 CA ALA A 301 18.997 -3.407 61.206 1.00158.93 C
ANISOU 2305 CA ALA A 301 21949 13865 24573 2763 -8238 2049 C
ATOM 2306 C ALA A 301 19.540 -1.991 61.019 1.00149.37 C
ANISOU 2306 C ALA A 301 20455 13246 23052 2774 -7898 1805 C
ATOM 2307 O ALA A 301 20.245 -1.458 61.879 1.00150.37 O
ANISOU 2307 O ALA A 301 20560 13575 22998 2730 -8080 1999 O
ATOM 2308 CB ALA A 301 19.790 -4.154 62.282 1.00145.34 C
ANISOU 2308 CB ALA A 301 20302 11962 22957 2742 -8660 2351 C
ATOM 2309 N TRP A 302 19.202 -1.375 59.891 1.00137.42 N
ANISOU 2309 N TRP A 302 18733 12008 21472 2818 -7417 1388 N
ATOM 2310 CA TRP A 302 19.572 0.013 59.652 1.00141.79 C
ANISOU 2310 CA TRP A 302 19051 13112 21712 2779 -7064 1173 C
ATOM 2311 C TRP A 302 18.813 0.930 60.605 1.00141.38 C
ANISOU 2311 C TRP A 302 19289 13362 21067 2349 -6884 1498 C
ATOM 2312 O TRP A 302 17.626 0.723 60.873 1.00150.36 O
ANISOU 2312 O TRP A 302 20736 14413 21980 2066 -6764 1710 O
ATOM 2313 CB TRP A 302 19.260 0.398 58.205 1.00149.46 C
ANISOU 2313 CB TRP A 302 19776 14281 22732 2892 -6602 692 C
ATOM 2314 CG TRP A 302 20.253 -0.108 57.199 1.00151.32 C
ANISOU 2314 CG TRP A 302 19620 14413 23462 3328 -6684 268 C
ATOM 2315 CD1 TRP A 302 20.987 -1.256 57.276 1.00148.09 C
ANISOU 2315 CD1 TRP A 302 19127 13582 23558 3644 -7124 252 C
ATOM 2316 CD2 TRP A 302 20.587 0.498 55.944 1.00146.25 C
ANISOU 2316 CD2 TRP A 302 18613 14099 22857 3496 -6308 -214 C
ATOM 2317 NE1 TRP A 302 21.774 -1.391 56.157 1.00148.54 N
ANISOU 2317 NE1 TRP A 302 18770 13705 23965 4014 -7031 -242 N
ATOM 2318 CE2 TRP A 302 21.545 -0.328 55.323 1.00147.98 C
ANISOU 2318 CE2 TRP A 302 18523 14108 23596 3915 -6525 -526 C
ATOM 2319 CE3 TRP A 302 20.176 1.663 55.289 1.00138.19 C
ANISOU 2319 CE3 TRP A 302 17497 13530 21478 3331 -5821 -407 C
ATOM 2320 CZ2 TRP A 302 22.098 -0.027 54.080 1.00144.99 C
ANISOU 2320 CZ2 TRP A 302 17738 13996 23354 4153 -6242 -1028 C
ATOM 2321 CZ3 TRP A 302 20.727 1.961 54.054 1.00138.53 C
ANISOU 2321 CZ3 TRP A 302 17159 13816 21660 3554 -5564 -868 C
ATOM 2322 CH2 TRP A 302 21.677 1.119 53.463 1.00141.32 C
ANISOU 2322 CH2 TRP A 302 17203 13991 22499 3951 -5762 -1177 C
ATOM 2323 N ASP A 303 19.499 1.942 61.126 1.00128.15 N
ANISOU 2323 N ASP A 303 17503 12046 19141 2297 -6866 1524 N
ATOM 2324 CA ASP A 303 18.850 2.984 61.908 1.00133.95 C
ANISOU 2324 CA ASP A 303 18463 13124 19307 1921 -6641 1731 C
ATOM 2325 C ASP A 303 18.880 4.296 61.130 1.00135.23 C
ANISOU 2325 C ASP A 303 18385 13725 19270 1911 -6181 1379 C
ATOM 2326 O ASP A 303 19.337 4.357 59.985 1.00136.43 O
ANISOU 2326 O ASP A 303 18216 13928 19692 2163 -6025 1005 O
ATOM 2327 CB ASP A 303 19.498 3.135 63.290 1.00143.12 C
ANISOU 2327 CB ASP A 303 19763 14339 20278 1804 -7014 2088 C
ATOM 2328 CG ASP A 303 20.992 3.409 63.223 1.00145.44 C
ANISOU 2328 CG ASP A 303 19705 14740 20815 2083 -7242 1922 C
ATOM 2329 OD1 ASP A 303 21.527 3.624 62.116 1.00144.94 O
ANISOU 2329 OD1 ASP A 303 19278 14773 21021 2343 -7058 1519 O
ATOM 2330 OD2 ASP A 303 21.633 3.421 64.295 1.00137.26 O1-
ANISOU 2330 OD2 ASP A 303 18751 13718 19685 2027 -7607 2200 O1-
ATOM 2331 N ALA A 304 18.381 5.355 61.771 1.00135.16 N
ANISOU 2331 N ALA A 304 18542 14036 18776 1609 -5968 1503 N
ATOM 2332 CA ALA A 304 18.319 6.655 61.110 1.00137.77 C
ANISOU 2332 CA ALA A 304 18692 14754 18900 1564 -5548 1211 C
ATOM 2333 C ALA A 304 19.707 7.155 60.735 1.00125.63 C
ANISOU 2333 C ALA A 304 16783 13393 17559 1791 -5628 978 C
ATOM 2334 O ALA A 304 19.892 7.754 59.669 1.00121.18 O
ANISOU 2334 O ALA A 304 15954 13027 17062 1893 -5331 648 O
ATOM 2335 CB ALA A 304 17.609 7.667 62.007 1.00140.58 C
ANISOU 2335 CB ALA A 304 19304 15383 18726 1217 -5365 1390 C
ATOM 2336 N GLN A 305 20.701 6.913 61.593 1.00114.65 N
ANISOU 2336 N GLN A 305 15359 11946 16258 1860 -6035 1156 N
ATOM 2337 CA GLN A 305 22.038 7.422 61.313 1.00127.90 C
ANISOU 2337 CA GLN A 305 16660 13822 18114 2051 -6120 946 C
ATOM 2338 C GLN A 305 22.688 6.692 60.144 1.00126.40 C
ANISOU 2338 C GLN A 305 16111 13490 18427 2420 -6143 630 C
ATOM 2339 O GLN A 305 23.466 7.297 59.399 1.00132.60 O
ANISOU 2339 O GLN A 305 16534 14527 19321 2552 -5987 332 O
ATOM 2340 CB GLN A 305 22.917 7.328 62.560 1.00124.77 C
ANISOU 2340 CB GLN A 305 16313 13407 17686 2028 -6576 1223 C
ATOM 2341 CG GLN A 305 24.138 8.236 62.504 1.00113.03 C
ANISOU 2341 CG GLN A 305 14485 12233 16228 2098 -6608 1046 C
ATOM 2342 CD GLN A 305 25.245 7.787 63.432 1.00133.62 C
ANISOU 2342 CD GLN A 305 17019 14751 19000 2209 -7138 1250 C
ATOM 2343 OE1 GLN A 305 26.381 7.577 63.005 1.00142.39 O
ANISOU 2343 OE1 GLN A 305 17740 15878 20484 2486 -7310 1064 O
ATOM 2344 NE2 GLN A 305 24.923 7.640 64.711 1.00149.27 N
ANISOU 2344 NE2 GLN A 305 19362 16658 20695 1988 -7403 1632 N
ATOM 2345 N ARG A 306 22.388 5.402 59.963 1.00128.65 N
ANISOU 2345 N ARG A 306 16483 13378 19019 2582 -6333 679 N
ATOM 2346 CA ARG A 306 22.876 4.702 58.780 1.00136.36 C
ANISOU 2346 CA ARG A 306 17132 14219 20461 2936 -6313 324 C
ATOM 2347 C ARG A 306 22.263 5.277 57.510 1.00125.32 C
ANISOU 2347 C ARG A 306 15614 13045 18958 2904 -5801 -14 C
ATOM 2348 O ARG A 306 22.926 5.350 56.468 1.00117.56 O
ANISOU 2348 O ARG A 306 14259 12202 18206 3135 -5658 -380 O
ATOM 2349 CB ARG A 306 22.581 3.205 58.880 1.00141.80 C
ANISOU 2349 CB ARG A 306 17985 14393 21498 3095 -6633 448 C
ATOM 2350 CG ARG A 306 22.940 2.450 57.611 1.00139.10 C
ANISOU 2350 CG ARG A 306 17334 13891 21625 3459 -6584 36 C
ATOM 2351 CD ARG A 306 24.442 2.449 57.386 1.00139.07 C
ANISOU 2351 CD ARG A 306 16881 14000 21961 3790 -6778 -198 C
ATOM 2352 NE ARG A 306 24.813 1.788 56.139 1.00141.81 N
ANISOU 2352 NE ARG A 306 16900 14249 22733 4145 -6692 -645 N
ATOM 2353 CZ ARG A 306 24.954 0.478 55.991 1.00145.62 C
ANISOU 2353 CZ ARG A 306 17378 14274 23678 4434 -7004 -707 C
ATOM 2354 NH1 ARG A 306 24.734 -0.359 56.991 1.00145.96 N
ANISOU 2354 NH1 ARG A 306 17738 13885 23834 4399 -7440 -317 N
ATOM 2355 NH2 ARG A 306 25.324 -0.004 54.808 1.00142.10 N
ANISOU 2355 NH2 ARG A 306 16605 13800 23586 4758 -6882 -1175 N
ATOM 2356 N ILE A 307 20.998 5.699 57.580 1.00120.84 N
ANISOU 2356 N ILE A 307 15348 12533 18033 2615 -5522 106 N
ATOM 2357 CA ILE A 307 20.326 6.270 56.415 1.00120.02 C
ANISOU 2357 CA ILE A 307 15159 12636 17806 2565 -5059 -177 C
ATOM 2358 C ILE A 307 21.051 7.528 55.952 1.00120.50 C
ANISOU 2358 C ILE A 307 14927 13127 17731 2551 -4822 -390 C
ATOM 2359 O ILE A 307 21.511 7.620 54.808 1.00112.70 O
ANISOU 2359 O ILE A 307 13620 12287 16916 2728 -4634 -730 O
ATOM 2360 CB ILE A 307 18.849 6.560 56.735 1.00115.86 C
ANISOU 2360 CB ILE A 307 15003 12104 16913 2248 -4838 22 C
ATOM 2361 CG1 ILE A 307 18.102 5.256 57.017 1.00123.76 C
ANISOU 2361 CG1 ILE A 307 16264 12680 18077 2246 -5044 210 C
ATOM 2362 CG2 ILE A 307 18.191 7.317 55.592 1.00112.15 C
ANISOU 2362 CG2 ILE A 307 14440 11884 16288 2184 -4379 -246 C
ATOM 2363 CD1 ILE A 307 16.652 5.452 57.401 1.00138.31 C
ANISOU 2363 CD1 ILE A 307 18450 14528 19574 1923 -4843 421 C
ATOM 2364 N PHE A 308 21.170 8.514 56.844 1.00127.13 N
ANISOU 2364 N PHE A 308 15876 14178 18251 2325 -4831 -195 N
ATOM 2365 CA PHE A 308 21.825 9.763 56.476 1.00116.01 C
ANISOU 2365 CA PHE A 308 14220 13155 16705 2268 -4624 -365 C
ATOM 2366 C PHE A 308 23.296 9.548 56.145 1.00110.68 C
ANISOU 2366 C PHE A 308 13124 12561 16368 2532 -4808 -558 C
ATOM 2367 O PHE A 308 23.863 10.291 55.336 1.00104.09 O
ANISOU 2367 O PHE A 308 11984 12028 15536 2555 -4581 -804 O
ATOM 2368 CB PHE A 308 21.671 10.784 57.604 1.00108.60 C
ANISOU 2368 CB PHE A 308 13505 12379 15378 1976 -4648 -121 C
ATOM 2369 CG PHE A 308 20.306 11.410 57.672 1.00116.27 C
ANISOU 2369 CG PHE A 308 14783 13409 15985 1714 -4344 -40 C
ATOM 2370 CD1 PHE A 308 19.297 10.823 58.419 1.00116.99 C
ANISOU 2370 CD1 PHE A 308 15228 13285 15936 1585 -4423 211 C
ATOM 2371 CD2 PHE A 308 20.030 12.583 56.988 1.00113.29 C
ANISOU 2371 CD2 PHE A 308 14330 13302 15414 1594 -3987 -209 C
ATOM 2372 CE1 PHE A 308 18.040 11.396 58.487 1.00109.35 C
ANISOU 2372 CE1 PHE A 308 14506 12396 14647 1355 -4137 264 C
ATOM 2373 CE2 PHE A 308 18.775 13.161 57.051 1.00108.81 C
ANISOU 2373 CE2 PHE A 308 14023 12777 14541 1381 -3726 -148 C
ATOM 2374 CZ PHE A 308 17.779 12.566 57.802 1.00106.21 C
ANISOU 2374 CZ PHE A 308 14018 12256 14081 1270 -3793 75 C
ATOM 2375 N LYS A 309 23.927 8.539 56.754 1.00131.97 N
ANISOU 2375 N LYS A 309 15789 14997 19356 2727 -5223 -444 N
ATOM 2376 CA LYS A 309 25.308 8.212 56.410 1.00139.27 C
ANISOU 2376 CA LYS A 309 16280 15981 20657 3022 -5415 -653 C
ATOM 2377 C LYS A 309 25.427 7.777 54.955 1.00136.19 C
ANISOU 2377 C LYS A 309 15585 15624 20538 3268 -5175 -1055 C
ATOM 2378 O LYS A 309 26.370 8.169 54.258 1.00133.16 O
ANISOU 2378 O LYS A 309 14787 15525 20284 3394 -5060 -1330 O
ATOM 2379 CB LYS A 309 25.841 7.116 57.335 1.00132.23 C
ANISOU 2379 CB LYS A 309 15443 14745 20053 3206 -5937 -440 C
ATOM 2380 CG LYS A 309 27.214 7.403 57.925 1.00123.40 C
ANISOU 2380 CG LYS A 309 14037 13785 19065 3299 -6241 -410 C
ATOM 2381 CD LYS A 309 27.140 8.435 59.033 1.00134.17 C
ANISOU 2381 CD LYS A 309 15629 15347 20004 2961 -6291 -123 C
ATOM 2382 CE LYS A 309 28.521 8.794 59.557 1.00154.99 C
ANISOU 2382 CE LYS A 309 17955 18174 22762 3033 -6584 -116 C
ATOM 2383 NZ LYS A 309 28.452 9.751 60.695 1.00144.08 N
ANISOU 2383 NZ LYS A 309 16820 16964 20962 2700 -6669 154 N
ATOM 2384 N GLU A 310 24.483 6.961 54.480 1.00120.28 N
ANISOU 2384 N GLU A 310 13760 13337 18602 3326 -5096 -1100 N
ATOM 2385 CA GLU A 310 24.512 6.538 53.084 1.00114.88 C
ANISOU 2385 CA GLU A 310 12817 12692 18140 3544 -4860 -1502 C
ATOM 2386 C GLU A 310 24.220 7.699 52.143 1.00116.71 C
ANISOU 2386 C GLU A 310 12937 13340 18067 3361 -4384 -1692 C
ATOM 2387 O GLU A 310 24.735 7.728 51.019 1.00109.29 O
ANISOU 2387 O GLU A 310 11650 12616 17260 3519 -4180 -2047 O
ATOM 2388 CB GLU A 310 23.517 5.400 52.856 1.00119.41 C
ANISOU 2388 CB GLU A 310 13653 12858 18860 3618 -4913 -1492 C
ATOM 2389 CG GLU A 310 23.926 4.082 53.493 1.00126.84 C
ANISOU 2389 CG GLU A 310 14641 13346 20207 3866 -5393 -1377 C
ATOM 2390 CD GLU A 310 25.060 3.405 52.746 1.00135.77 C
ANISOU 2390 CD GLU A 310 15327 14452 21809 4279 -5509 -1762 C
ATOM 2391 OE1 GLU A 310 25.244 3.706 51.548 1.00112.97 O
ANISOU 2391 OE1 GLU A 310 12146 11845 18931 4371 -5171 -2152 O
ATOM 2392 OE2 GLU A 310 25.768 2.576 53.357 1.00153.02 O1-
ANISOU 2392 OE2 GLU A 310 17448 16344 24349 4514 -5943 -1677 O1-
ATOM 2393 N ALA A 311 23.403 8.660 52.580 1.00106.15 N
ANISOU 2393 N ALA A 311 11888 12124 16320 3029 -4210 -1465 N
ATOM 2394 CA ALA A 311 23.169 9.855 51.776 1.00100.52 C
ANISOU 2394 CA ALA A 311 11085 11786 15321 2842 -3803 -1603 C
ATOM 2395 C ALA A 311 24.439 10.688 51.661 1.00101.41 C
ANISOU 2395 C ALA A 311 10831 12251 15449 2846 -3780 -1714 C
ATOM 2396 O ALA A 311 24.805 11.134 50.567 1.00 99.92 O
ANISOU 2396 O ALA A 311 10352 12358 15254 2870 -3506 -1981 O
ATOM 2397 CB ALA A 311 22.032 10.678 52.379 1.00107.48 C
ANISOU 2397 CB ALA A 311 12357 12680 15800 2512 -3665 -1335 C
ATOM 2398 N GLU A 312 25.119 10.911 52.789 1.00117.36 N
ANISOU 2398 N GLU A 312 12859 14257 17473 2802 -4072 -1504 N
ATOM 2399 CA GLU A 312 26.412 11.590 52.780 1.00122.61 C
ANISOU 2399 CA GLU A 312 13152 15234 18199 2812 -4110 -1599 C
ATOM 2400 C GLU A 312 27.375 10.926 51.806 1.00120.33 C
ANISOU 2400 C GLU A 312 12392 15049 18279 3129 -4096 -1952 C
ATOM 2401 O GLU A 312 28.043 11.599 51.012 1.00111.16 O
ANISOU 2401 O GLU A 312 10884 14256 17095 3099 -3865 -2167 O
ATOM 2402 CB GLU A 312 26.999 11.591 54.192 1.00132.05 C
ANISOU 2402 CB GLU A 312 14434 16328 19413 2775 -4514 -1326 C
ATOM 2403 CG GLU A 312 28.310 12.340 54.338 1.00129.46 C
ANISOU 2403 CG GLU A 312 13739 16315 19134 2747 -4593 -1390 C
ATOM 2404 CD GLU A 312 28.880 12.228 55.739 1.00126.98 C
ANISOU 2404 CD GLU A 312 13514 15884 18847 2726 -5034 -1122 C
ATOM 2405 OE1 GLU A 312 28.820 11.122 56.316 1.00131.71 O
ANISOU 2405 OE1 GLU A 312 14239 16154 19650 2913 -5361 -994 O
ATOM 2406 OE2 GLU A 312 29.385 13.243 56.262 1.00124.69 O1-
ANISOU 2406 OE2 GLU A 312 13177 15825 18374 2514 -5068 -1034 O1-
ATOM 2407 N LYS A 313 27.452 9.595 51.855 1.00123.61 N
ANISOU 2407 N LYS A 313 12789 15140 19039 3430 -4343 -2018 N
ATOM 2408 CA LYS A 313 28.347 8.858 50.971 1.00120.82 C
ANISOU 2408 CA LYS A 313 11984 14851 19069 3776 -4349 -2391 C
ATOM 2409 C LYS A 313 27.986 9.065 49.505 1.00120.14 C
ANISOU 2409 C LYS A 313 11748 15010 18888 3771 -3904 -2722 C
ATOM 2410 O LYS A 313 28.873 9.067 48.643 1.00116.99 O
ANISOU 2410 O LYS A 313 10899 14902 18650 3932 -3765 -3055 O
ATOM 2411 CB LYS A 313 28.310 7.374 51.341 1.00124.74 C
ANISOU 2411 CB LYS A 313 12568 14873 19953 4090 -4716 -2381 C
ATOM 2412 CG LYS A 313 29.142 6.457 50.465 1.00123.87 C
ANISOU 2412 CG LYS A 313 12020 14756 20289 4498 -4754 -2799 C
ATOM 2413 CD LYS A 313 28.686 5.014 50.635 1.00133.36 C
ANISOU 2413 CD LYS A 313 13426 15418 21825 4759 -5046 -2795 C
ATOM 2414 CE LYS A 313 29.283 4.380 51.883 1.00118.52 C
ANISOU 2414 CE LYS A 313 11600 13210 20222 4908 -5589 -2522 C
ATOM 2415 NZ LYS A 313 30.073 3.155 51.580 1.00123.88 N
ANISOU 2415 NZ LYS A 313 11969 13632 21467 5375 -5872 -2805 N
ATOM 2416 N PHE A 314 26.699 9.257 49.205 1.00117.35 N
ANISOU 2416 N PHE A 314 11752 14573 18263 3580 -3677 -2639 N
ATOM 2417 CA PHE A 314 26.282 9.480 47.824 1.00111.99 C
ANISOU 2417 CA PHE A 314 10964 14132 17456 3550 -3273 -2925 C
ATOM 2418 C PHE A 314 26.830 10.797 47.288 1.00110.01 C
ANISOU 2418 C PHE A 314 10463 14380 16956 3334 -2980 -2990 C
ATOM 2419 O PHE A 314 27.453 10.835 46.220 1.00105.52 O
ANISOU 2419 O PHE A 314 9515 14126 16451 3432 -2762 -3314 O
ATOM 2420 CB PHE A 314 24.756 9.453 47.728 1.00114.21 C
ANISOU 2420 CB PHE A 314 11690 14210 17496 3374 -3131 -2781 C
ATOM 2421 CG PHE A 314 24.216 10.060 46.463 1.00110.93 C
ANISOU 2421 CG PHE A 314 11227 14091 16830 3238 -2713 -2974 C
ATOM 2422 CD1 PHE A 314 24.234 9.347 45.275 1.00109.16 C
ANISOU 2422 CD1 PHE A 314 10804 13920 16752 3442 -2560 -3345 C
ATOM 2423 CD2 PHE A 314 23.686 11.340 46.463 1.00109.17 C
ANISOU 2423 CD2 PHE A 314 11167 14088 16225 2908 -2489 -2790 C
ATOM 2424 CE1 PHE A 314 23.736 9.902 44.111 1.00 94.89 C
ANISOU 2424 CE1 PHE A 314 8964 12406 14685 3302 -2192 -3506 C
ATOM 2425 CE2 PHE A 314 23.189 11.900 45.303 1.00 99.95 C
ANISOU 2425 CE2 PHE A 314 9966 13182 14827 2779 -2137 -2937 C
ATOM 2426 CZ PHE A 314 23.213 11.180 44.126 1.00 93.58 C
ANISOU 2426 CZ PHE A 314 8964 12451 14140 2967 -1989 -3285 C
ATOM 2427 N PHE A 315 26.592 11.895 48.011 1.00113.73 N
ANISOU 2427 N PHE A 315 11146 14932 17134 3024 -2970 -2688 N
ATOM 2428 CA PHE A 315 27.106 13.195 47.586 1.00114.73 C
ANISOU 2428 CA PHE A 315 11067 15489 17036 2786 -2728 -2710 C
ATOM 2429 C PHE A 315 28.626 13.185 47.496 1.00120.44 C
ANISOU 2429 C PHE A 315 11287 16478 17999 2927 -2821 -2889 C
ATOM 2430 O PHE A 315 29.207 13.703 46.537 1.00124.09 O
ANISOU 2430 O PHE A 315 11407 17335 18404 2869 -2556 -3100 O
ATOM 2431 CB PHE A 315 26.639 14.289 48.547 1.00111.81 C
ANISOU 2431 CB PHE A 315 11028 15090 16364 2460 -2770 -2362 C
ATOM 2432 CG PHE A 315 25.162 14.544 48.508 1.00105.36 C
ANISOU 2432 CG PHE A 315 10647 14108 15277 2288 -2612 -2214 C
ATOM 2433 CD1 PHE A 315 24.594 15.231 47.449 1.00104.35 C
ANISOU 2433 CD1 PHE A 315 10532 14194 14922 2131 -2263 -2304 C
ATOM 2434 CD2 PHE A 315 24.341 14.098 49.529 1.00109.52 C
ANISOU 2434 CD2 PHE A 315 11560 14282 15771 2275 -2816 -1976 C
ATOM 2435 CE1 PHE A 315 23.235 15.472 47.411 1.00111.98 C
ANISOU 2435 CE1 PHE A 315 11872 15015 15662 1987 -2132 -2174 C
ATOM 2436 CE2 PHE A 315 22.981 14.333 49.493 1.00107.89 C
ANISOU 2436 CE2 PHE A 315 11717 13952 15326 2118 -2660 -1855 C
ATOM 2437 CZ PHE A 315 22.427 15.023 48.434 1.00109.44 C
ANISOU 2437 CZ PHE A 315 11905 14353 15324 1985 -2323 -1960 C
ATOM 2438 N VAL A 316 29.290 12.601 48.497 1.00118.82 N
ANISOU 2438 N VAL A 316 11018 16073 18056 3102 -3203 -2797 N
ATOM 2439 CA VAL A 316 30.749 12.537 48.490 1.00116.91 C
ANISOU 2439 CA VAL A 316 10270 16071 18078 3258 -3331 -2965 C
ATOM 2440 C VAL A 316 31.249 11.792 47.260 1.00114.17 C
ANISOU 2440 C VAL A 316 9505 15896 17977 3549 -3153 -3398 C
ATOM 2441 O VAL A 316 32.306 12.123 46.707 1.00110.14 O
ANISOU 2441 O VAL A 316 8516 15784 17550 3577 -3029 -3618 O
ATOM 2442 CB VAL A 316 31.251 11.894 49.799 1.00114.64 C
ANISOU 2442 CB VAL A 316 10028 15481 18048 3428 -3821 -2775 C
ATOM 2443 CG1 VAL A 316 32.731 11.563 49.710 1.00111.90 C
ANISOU 2443 CG1 VAL A 316 9117 15338 18060 3678 -3986 -2999 C
ATOM 2444 CG2 VAL A 316 30.986 12.819 50.977 1.00118.24 C
ANISOU 2444 CG2 VAL A 316 10817 15890 18219 3105 -3966 -2392 C
ATOM 2445 N SER A 317 30.489 10.802 46.790 1.00117.84 N
ANISOU 2445 N SER A 317 10138 16088 18550 3754 -3123 -3541 N
ATOM 2446 CA SER A 317 30.891 10.017 45.630 1.00126.23 C
ANISOU 2446 CA SER A 317 10834 17285 19844 4049 -2962 -3990 C
ATOM 2447 C SER A 317 30.907 10.823 44.336 1.00130.36 C
ANISOU 2447 C SER A 317 11144 18308 20080 3855 -2489 -4208 C
ATOM 2448 O SER A 317 31.469 10.346 43.344 1.00131.90 O
ANISOU 2448 O SER A 317 10947 18743 20427 4068 -2319 -4611 O
ATOM 2449 CB SER A 317 29.967 8.809 45.475 1.00124.37 C
ANISOU 2449 CB SER A 317 10885 16601 19769 4274 -3058 -4074 C
ATOM 2450 OG SER A 317 28.674 9.209 45.058 1.00111.99 O
ANISOU 2450 OG SER A 317 9705 14998 17847 4021 -2802 -3962 O
ATOM 2451 N VAL A 318 30.314 12.016 44.311 1.00122.93 N
ANISOU 2451 N VAL A 318 10448 17529 18729 3461 -2280 -3958 N
ATOM 2452 CA VAL A 318 30.336 12.866 43.125 1.00114.93 C
ANISOU 2452 CA VAL A 318 9260 16987 17422 3235 -1859 -4104 C
ATOM 2453 C VAL A 318 31.232 14.078 43.299 1.00119.03 C
ANISOU 2453 C VAL A 318 9529 17894 17803 2960 -1789 -3977 C
ATOM 2454 O VAL A 318 31.278 14.934 42.403 1.00108.53 O
ANISOU 2454 O VAL A 318 8076 16959 16200 2708 -1457 -4027 O
ATOM 2455 CB VAL A 318 28.918 13.307 42.713 1.00100.46 C
ANISOU 2455 CB VAL A 318 7879 15059 15233 2995 -1644 -3950 C
ATOM 2456 CG1 VAL A 318 27.984 12.107 42.655 1.00110.81 C
ANISOU 2456 CG1 VAL A 318 9460 15955 16688 3235 -1745 -4042 C
ATOM 2457 CG2 VAL A 318 28.387 14.381 43.647 1.00 96.84 C
ANISOU 2457 CG2 VAL A 318 7788 14485 14521 2664 -1722 -3524 C
ATOM 2458 N GLY A 319 31.947 14.182 44.414 1.00130.92 N
ANISOU 2458 N GLY A 319 12263 18974 18506 4246 -1101 -4016 N
ATOM 2459 CA GLY A 319 32.880 15.266 44.626 1.00119.98 C
ANISOU 2459 CA GLY A 319 10468 17958 17162 4084 -990 -3939 C
ATOM 2460 C GLY A 319 32.415 16.362 45.555 1.00117.07 C
ANISOU 2460 C GLY A 319 10254 17649 16577 3768 -1240 -3519 C
ATOM 2461 O GLY A 319 33.089 17.393 45.647 1.00112.26 O
ANISOU 2461 O GLY A 319 9372 17351 15929 3558 -1128 -3447 O
ATOM 2462 N LEU A 320 31.286 16.173 46.253 1.00120.31 N
ANISOU 2462 N LEU A 320 11096 17762 16852 3712 -1552 -3255 N
ATOM 2463 CA LEU A 320 30.731 17.177 47.145 1.00115.69 C
ANISOU 2463 CA LEU A 320 10712 17194 16052 3419 -1750 -2881 C
ATOM 2464 C LEU A 320 31.158 16.905 48.586 1.00111.98 C
ANISOU 2464 C LEU A 320 10148 16532 15867 3554 -2177 -2666 C
ATOM 2465 O LEU A 320 31.400 15.754 48.960 1.00121.50 O
ANISOU 2465 O LEU A 320 11315 17464 17387 3878 -2404 -2739 O
ATOM 2466 CB LEU A 320 29.202 17.191 47.046 1.00115.26 C
ANISOU 2466 CB LEU A 320 11168 16941 15685 3250 -1793 -2734 C
ATOM 2467 CG LEU A 320 28.636 17.659 45.698 1.00102.90 C
ANISOU 2467 CG LEU A 320 9773 15557 13766 3054 -1464 -2872 C
ATOM 2468 CD1 LEU A 320 27.119 17.532 45.661 1.00 87.96 C
ANISOU 2468 CD1 LEU A 320 8317 13439 11664 2932 -1583 -2738 C
ATOM 2469 CD2 LEU A 320 29.064 19.085 45.374 1.00 90.87 C
ANISOU 2469 CD2 LEU A 320 8134 14391 12002 2760 -1247 -2790 C
ATOM 2470 N PRO A 321 31.273 17.941 49.417 1.00107.81 N
ANISOU 2470 N PRO A 321 9622 16118 15223 3307 -2314 -2397 N
ATOM 2471 CA PRO A 321 31.817 17.746 50.768 1.00129.67 C
ANISOU 2471 CA PRO A 321 12312 18729 18228 3405 -2743 -2200 C
ATOM 2472 C PRO A 321 30.884 16.940 51.660 1.00130.87 C
ANISOU 2472 C PRO A 321 12922 18444 18357 3484 -3057 -2006 C
ATOM 2473 O PRO A 321 29.667 16.915 51.462 1.00123.60 O
ANISOU 2473 O PRO A 321 12392 17384 17185 3347 -2945 -1943 O
ATOM 2474 CB PRO A 321 31.973 19.179 51.295 1.00132.73 C
ANISOU 2474 CB PRO A 321 12698 19345 18388 3040 -2748 -1976 C
ATOM 2475 CG PRO A 321 31.014 19.986 50.480 1.00118.41 C
ANISOU 2475 CG PRO A 321 11157 17653 16180 2765 -2402 -1963 C
ATOM 2476 CD PRO A 321 31.038 19.364 49.120 1.00 92.50 C
ANISOU 2476 CD PRO A 321 7754 14456 12936 2926 -2090 -2280 C
ATOM 2477 N ASN A 322 31.470 16.277 52.660 1.00118.34 N
ANISOU 2477 N ASN A 322 11285 16634 17044 3693 -3467 -1906 N
ATOM 2478 CA ASN A 322 30.638 15.609 53.648 1.00119.91 C
ANISOU 2478 CA ASN A 322 11978 16408 17173 3701 -3769 -1679 C
ATOM 2479 C ASN A 322 30.054 16.634 54.621 1.00113.66 C
ANISOU 2479 C ASN A 322 11523 15619 16043 3326 -3848 -1363 C
ATOM 2480 O ASN A 322 30.458 17.801 54.661 1.00114.78 O
ANISOU 2480 O ASN A 322 11496 16059 16055 3102 -3756 -1307 O
ATOM 2481 CB ASN A 322 31.411 14.496 54.383 1.00121.81 C
ANISOU 2481 CB ASN A 322 12143 16350 17789 4054 -4217 -1658 C
ATOM 2482 CG ASN A 322 32.588 15.000 55.230 1.00159.25 C
ANISOU 2482 CG ASN A 322 16578 21228 22701 4063 -4568 -1528 C
ATOM 2483 OD1 ASN A 322 32.615 16.143 55.682 1.00168.29 O
ANISOU 2483 OD1 ASN A 322 17756 22582 23604 3736 -4559 -1359 O
ATOM 2484 ND2 ASN A 322 33.557 14.107 55.475 1.00173.02 N
ANISOU 2484 ND2 ASN A 322 18034 22821 24885 4448 -4913 -1607 N
ATOM 2485 N MET A 323 29.074 16.186 55.401 1.00115.75 N
ANISOU 2485 N MET A 323 12289 15530 16160 3243 -3986 -1170 N
ATOM 2486 CA MET A 323 28.366 17.083 56.302 1.00120.71 C
ANISOU 2486 CA MET A 323 13290 16120 16456 2889 -3985 -906 C
ATOM 2487 C MET A 323 29.314 17.658 57.347 1.00125.09 C
ANISOU 2487 C MET A 323 13790 16735 17004 2801 -4312 -728 C
ATOM 2488 O MET A 323 30.277 17.013 57.768 1.00123.25 O
ANISOU 2488 O MET A 323 13385 16409 17035 3035 -4684 -724 O
ATOM 2489 CB MET A 323 27.221 16.345 56.994 1.00117.58 C
ANISOU 2489 CB MET A 323 13424 15309 15940 2820 -4053 -755 C
ATOM 2490 CG MET A 323 26.121 15.855 56.063 1.00116.79 C
ANISOU 2490 CG MET A 323 13414 15134 15827 2832 -3756 -906 C
ATOM 2491 SD MET A 323 25.174 17.173 55.278 1.00128.93 S
ANISOU 2491 SD MET A 323 14914 16973 17099 2539 -3325 -939 S
ATOM 2492 CE MET A 323 25.890 17.173 53.637 1.00114.04 C
ANISOU 2492 CE MET A 323 12554 15426 15349 2740 -3124 -1259 C
ATOM 2493 N THR A 324 29.034 18.892 57.761 1.00123.23 N
ANISOU 2493 N THR A 324 13705 16641 16474 2463 -4194 -586 N
ATOM 2494 CA THR A 324 29.769 19.476 58.872 1.00110.05 C
ANISOU 2494 CA THR A 324 12102 14985 14725 2308 -4520 -398 C
ATOM 2495 C THR A 324 29.494 18.688 60.147 1.00112.77 C
ANISOU 2495 C THR A 324 12945 14910 14992 2314 -4894 -178 C
ATOM 2496 O THR A 324 28.464 18.025 60.285 1.00112.60 O
ANISOU 2496 O THR A 324 13305 14600 14876 2310 -4788 -133 O
ATOM 2497 CB THR A 324 29.384 20.945 59.071 1.00108.58 C
ANISOU 2497 CB THR A 324 12074 14977 14206 1928 -4283 -301 C
ATOM 2498 OG1 THR A 324 28.007 21.038 59.463 1.00 87.60 O
ANISOU 2498 OG1 THR A 324 9922 12084 11278 1748 -4074 -188 O
ATOM 2499 CG2 THR A 324 29.601 21.737 57.790 1.00 91.44 C
ANISOU 2499 CG2 THR A 324 9492 13184 12068 1892 -3916 -491 C
ATOM 2500 N GLN A 325 30.447 18.748 61.079 1.00 97.73 N
ANISOU 2500 N GLN A 325 11041 12965 13125 2305 -5352 -38 N
ATOM 2501 CA GLN A 325 30.238 18.126 62.382 1.00109.10 C
ANISOU 2501 CA GLN A 325 13046 13997 14409 2252 -5746 209 C
ATOM 2502 C GLN A 325 29.012 18.708 63.074 1.00106.26 C
ANISOU 2502 C GLN A 325 13306 13475 13591 1868 -5474 369 C
ATOM 2503 O GLN A 325 28.241 17.978 63.708 1.00100.93 O
ANISOU 2503 O GLN A 325 13147 12433 12769 1819 -5511 497 O
ATOM 2504 CB GLN A 325 31.482 18.307 63.247 1.00110.51 C
ANISOU 2504 CB GLN A 325 13126 14201 14663 2254 -6314 341 C
ATOM 2505 CG GLN A 325 31.435 17.590 64.579 1.00100.28 C
ANISOU 2505 CG GLN A 325 12434 12466 13200 2220 -6817 610 C
ATOM 2506 CD GLN A 325 32.505 18.089 65.524 1.00153.11 C
ANISOU 2506 CD GLN A 325 19122 19209 19845 2099 -7373 770 C
ATOM 2507 OE1 GLN A 325 33.158 19.099 65.257 1.00150.21 O
ANISOU 2507 OE1 GLN A 325 18339 19209 19525 1969 -7323 686 O
ATOM 2508 NE2 GLN A 325 32.688 17.391 66.638 1.00167.41 N
ANISOU 2508 NE2 GLN A 325 21421 20642 21545 2101 -7875 1002 N
ATOM 2509 N GLY A 326 28.813 20.023 62.954 1.00100.27 N
ANISOU 2509 N GLY A 326 12508 12974 12618 1590 -5175 352 N
ATOM 2510 CA GLY A 326 27.626 20.642 63.515 1.00 98.00 C
ANISOU 2510 CA GLY A 326 12743 12543 11950 1259 -4848 458 C
ATOM 2511 C GLY A 326 26.337 20.061 62.971 1.00113.24 C
ANISOU 2511 C GLY A 326 14798 14323 13906 1312 -4464 381 C
ATOM 2512 O GLY A 326 25.307 20.084 63.648 1.00121.56 O
ANISOU 2512 O GLY A 326 16337 15135 14713 1090 -4268 485 O
ATOM 2513 N PHE A 327 26.371 19.534 61.745 1.00101.56 N
ANISOU 2513 N PHE A 327 12882 12982 12725 1584 -4339 184 N
ATOM 2514 CA PHE A 327 25.211 18.830 61.209 1.00 92.18 C
ANISOU 2514 CA PHE A 327 11798 11631 11594 1641 -4056 102 C
ATOM 2515 C PHE A 327 24.886 17.598 62.045 1.00 96.05 C
ANISOU 2515 C PHE A 327 12730 11691 12073 1673 -4284 233 C
ATOM 2516 O PHE A 327 23.743 17.408 62.475 1.00 94.31 O
ANISOU 2516 O PHE A 327 12905 11237 11692 1475 -4056 304 O
ATOM 2517 CB PHE A 327 25.464 18.439 59.752 1.00104.10 C
ANISOU 2517 CB PHE A 327 12798 13356 13398 1922 -3940 -144 C
ATOM 2518 CG PHE A 327 24.382 17.586 59.151 1.00105.74 C
ANISOU 2518 CG PHE A 327 13098 13387 13691 1992 -3732 -245 C
ATOM 2519 CD1 PHE A 327 23.248 18.162 58.607 1.00104.90 C
ANISOU 2519 CD1 PHE A 327 13005 13366 13486 1829 -3353 -300 C
ATOM 2520 CD2 PHE A 327 24.500 16.204 59.132 1.00100.00 C
ANISOU 2520 CD2 PHE A 327 12444 12388 13163 2220 -3943 -285 C
ATOM 2521 CE1 PHE A 327 22.256 17.379 58.052 1.00108.99 C
ANISOU 2521 CE1 PHE A 327 13578 13729 14104 1868 -3201 -398 C
ATOM 2522 CE2 PHE A 327 23.511 15.417 58.579 1.00 97.62 C
ANISOU 2522 CE2 PHE A 327 12240 11912 12938 2248 -3763 -386 C
ATOM 2523 CZ PHE A 327 22.387 16.005 58.039 1.00106.96 C
ANISOU 2523 CZ PHE A 327 13407 13210 14022 2058 -3398 -444 C
ATOM 2524 N TRP A 328 25.890 16.751 62.291 1.00 93.12 N
ANISOU 2524 N TRP A 328 12295 11197 11888 1919 -4733 266 N
ATOM 2525 CA TRP A 328 25.661 15.506 63.018 1.00 95.40 C
ANISOU 2525 CA TRP A 328 13031 11037 12178 1978 -4997 401 C
ATOM 2526 C TRP A 328 25.336 15.747 64.486 1.00100.68 C
ANISOU 2526 C TRP A 328 14356 11440 12457 1641 -5116 672 C
ATOM 2527 O TRP A 328 24.634 14.937 65.102 1.00 98.33 O
ANISOU 2527 O TRP A 328 14569 10758 12034 1532 -5121 794 O
ATOM 2528 CB TRP A 328 26.885 14.599 62.895 1.00 95.31 C
ANISOU 2528 CB TRP A 328 12764 10946 12502 2367 -5488 367 C
ATOM 2529 CG TRP A 328 27.132 14.131 61.500 1.00104.82 C
ANISOU 2529 CG TRP A 328 13421 12329 14078 2703 -5332 77 C
ATOM 2530 CD1 TRP A 328 28.100 14.570 60.646 1.00108.12 C
ANISOU 2530 CD1 TRP A 328 13217 13124 14740 2907 -5318 -118 C
ATOM 2531 CD2 TRP A 328 26.397 13.126 60.793 1.00113.67 C
ANISOU 2531 CD2 TRP A 328 14596 13248 15345 2842 -5147 -66 C
ATOM 2532 NE1 TRP A 328 28.012 13.903 59.448 1.00115.45 N
ANISOU 2532 NE1 TRP A 328 13839 14097 15931 3170 -5114 -382 N
ATOM 2533 CE2 TRP A 328 26.974 13.010 59.513 1.00116.08 C
ANISOU 2533 CE2 TRP A 328 14330 13820 15955 3139 -5029 -355 C
ATOM 2534 CE3 TRP A 328 25.307 12.313 61.117 1.00116.60 C
ANISOU 2534 CE3 TRP A 328 15456 13235 15611 2714 -5056 12 C
ATOM 2535 CZ2 TRP A 328 26.498 12.115 58.558 1.00119.97 C
ANISOU 2535 CZ2 TRP A 328 14759 14197 16626 3319 -4848 -570 C
ATOM 2536 CZ3 TRP A 328 24.835 11.425 60.168 1.00125.99 C
ANISOU 2536 CZ3 TRP A 328 16545 14314 17010 2886 -4894 -193 C
ATOM 2537 CH2 TRP A 328 25.428 11.336 58.903 1.00126.58 C
ANISOU 2537 CH2 TRP A 328 16078 14651 17365 3190 -4804 -483 C
ATOM 2538 N GLU A 329 25.833 16.839 65.063 1.00108.57 N
ANISOU 2538 N GLU A 329 15390 12623 13240 1445 -5198 762 N
ATOM 2539 CA GLU A 329 25.626 17.117 66.479 1.00105.71 C
ANISOU 2539 CA GLU A 329 15695 12011 12460 1107 -5325 1004 C
ATOM 2540 C GLU A 329 24.318 17.835 66.765 1.00106.75 C
ANISOU 2540 C GLU A 329 16166 12111 12284 744 -4760 1006 C
ATOM 2541 O GLU A 329 23.795 17.723 67.879 1.00106.53 O
ANISOU 2541 O GLU A 329 16790 11779 11909 454 -4729 1176 O
ATOM 2542 CB GLU A 329 26.775 17.969 67.022 1.00118.83 C
ANISOU 2542 CB GLU A 329 17274 13860 14014 1034 -5701 1089 C
ATOM 2543 CG GLU A 329 28.104 17.252 67.108 1.00126.63 C
ANISOU 2543 CG GLU A 329 18015 14811 15287 1350 -6356 1139 C
ATOM 2544 CD GLU A 329 29.239 18.194 67.450 1.00143.61 C
ANISOU 2544 CD GLU A 329 19933 17224 17407 1267 -6696 1178 C
ATOM 2545 OE1 GLU A 329 29.011 19.423 67.446 1.00137.20 O
ANISOU 2545 OE1 GLU A 329 19111 16647 16371 984 -6377 1137 O
ATOM 2546 OE2 GLU A 329 30.357 17.710 67.719 1.00165.85 O1-
ANISOU 2546 OE2 GLU A 329 22566 20001 20447 1485 -7294 1245 O1-
ATOM 2547 N ASN A 330 23.781 18.563 65.791 1.00109.26 N
ANISOU 2547 N ASN A 330 16070 12720 12722 754 -4311 818 N
ATOM 2548 CA ASN A 330 22.694 19.490 66.044 1.00109.59 C
ANISOU 2548 CA ASN A 330 16332 12779 12528 446 -3805 803 C
ATOM 2549 C ASN A 330 21.431 19.187 65.255 1.00102.56 C
ANISOU 2549 C ASN A 330 15281 11871 11815 473 -3350 661 C
ATOM 2550 O ASN A 330 20.398 19.806 65.527 1.00103.23 O
ANISOU 2550 O ASN A 330 15548 11916 11760 235 -2920 645 O
ATOM 2551 CB ASN A 330 23.156 20.923 65.739 1.00115.91 C
ANISOU 2551 CB ASN A 330 16843 13927 13272 378 -3706 735 C
ATOM 2552 CG ASN A 330 24.347 21.334 66.583 1.00112.27 C
ANISOU 2552 CG ASN A 330 16547 13490 12621 285 -4152 870 C
ATOM 2553 OD1 ASN A 330 24.369 21.119 67.795 1.00 99.12 O
ANISOU 2553 OD1 ASN A 330 15463 11546 10652 78 -4348 1045 O
ATOM 2554 ND2 ASN A 330 25.361 21.902 65.940 1.00104.41 N
ANISOU 2554 ND2 ASN A 330 15049 12822 11799 417 -4331 788 N
ATOM 2555 N SER A 331 21.476 18.268 64.297 1.00 94.98 N
ANISOU 2555 N SER A 331 13982 10933 11174 751 -3434 545 N
ATOM 2556 CA SER A 331 20.271 17.854 63.596 1.00105.00 C
ANISOU 2556 CA SER A 331 15136 12152 12609 750 -3074 418 C
ATOM 2557 C SER A 331 19.479 16.867 64.444 1.00104.24 C
ANISOU 2557 C SER A 331 15556 11639 12412 565 -3013 531 C
ATOM 2558 O SER A 331 20.031 16.158 65.290 1.00100.29 O
ANISOU 2558 O SER A 331 15454 10871 11782 551 -3351 693 O
ATOM 2559 CB SER A 331 20.616 17.212 62.253 1.00 97.65 C
ANISOU 2559 CB SER A 331 13712 11375 12015 1085 -3187 235 C
ATOM 2560 OG SER A 331 21.344 18.101 61.429 1.00 91.21 O
ANISOU 2560 OG SER A 331 12441 10942 11271 1222 -3199 126 O
ATOM 2561 N MET A 332 18.172 16.823 64.209 1.00106.59 N
ANISOU 2561 N MET A 332 15848 11875 12778 409 -2590 449 N
ATOM 2562 CA MET A 332 17.285 15.871 64.873 1.00112.06 C
ANISOU 2562 CA MET A 332 16975 12187 13414 191 -2444 524 C
ATOM 2563 C MET A 332 16.839 14.872 63.812 1.00109.86 C
ANISOU 2563 C MET A 332 16399 11869 13473 366 -2448 372 C
ATOM 2564 O MET A 332 15.927 15.152 63.030 1.00121.03 O
ANISOU 2564 O MET A 332 17476 13432 15076 338 -2137 217 O
ATOM 2565 CB MET A 332 16.094 16.574 65.517 1.00107.63 C
ANISOU 2565 CB MET A 332 16628 11567 12698 -165 -1922 530 C
ATOM 2566 CG MET A 332 15.415 15.755 66.603 1.00114.53 C
ANISOU 2566 CG MET A 332 18110 12027 13379 -488 -1764 660 C
ATOM 2567 SD MET A 332 13.925 16.541 67.238 1.00132.49 S
ANISOU 2567 SD MET A 332 20533 14251 15556 -895 -1040 600 S
ATOM 2568 CE MET A 332 12.824 16.335 65.846 1.00131.56 C
ANISOU 2568 CE MET A 332 19727 14306 15954 -766 -780 362 C
ATOM 2569 N LEU A 333 17.490 13.711 63.781 1.00 94.71 N
ANISOU 2569 N LEU A 333 14615 9732 11636 551 -2827 414 N
ATOM 2570 CA LEU A 333 17.223 12.697 62.772 1.00 93.85 C
ANISOU 2570 CA LEU A 333 14272 9554 11832 735 -2877 254 C
ATOM 2571 C LEU A 333 16.363 11.551 63.290 1.00 96.76 C
ANISOU 2571 C LEU A 333 15081 9486 12196 507 -2787 323 C
ATOM 2572 O LEU A 333 16.099 10.608 62.539 1.00103.99 O
ANISOU 2572 O LEU A 333 15881 10280 13350 621 -2842 195 O
ATOM 2573 CB LEU A 333 18.541 12.144 62.219 1.00 91.90 C
ANISOU 2573 CB LEU A 333 13821 9348 11748 1141 -3330 201 C
ATOM 2574 CG LEU A 333 19.607 13.176 61.853 1.00 88.99 C
ANISOU 2574 CG LEU A 333 13058 9379 11374 1342 -3462 156 C
ATOM 2575 CD1 LEU A 333 20.805 12.491 61.218 1.00 87.37 C
ANISOU 2575 CD1 LEU A 333 12585 9203 11409 1747 -3840 55 C
ATOM 2576 CD2 LEU A 333 19.031 14.233 60.926 1.00 87.00 C
ANISOU 2576 CD2 LEU A 333 12376 9509 11170 1295 -3106 -6 C
ATOM 2577 N THR A 334 15.949 11.592 64.555 1.00116.53 N
ANISOU 2577 N THR A 334 18124 11737 14415 166 -2643 517 N
ATOM 2578 CA THR A 334 15.047 10.608 65.137 1.00119.13 C
ANISOU 2578 CA THR A 334 18917 11649 14696 -139 -2474 595 C
ATOM 2579 C THR A 334 14.067 11.332 66.045 1.00131.54 C
ANISOU 2579 C THR A 334 20750 13198 16034 -577 -1973 662 C
ATOM 2580 O THR A 334 14.463 12.231 66.791 1.00142.87 O
ANISOU 2580 O THR A 334 22373 14728 17183 -662 -1949 769 O
ATOM 2581 CB THR A 334 15.787 9.529 65.961 1.00137.65 C
ANISOU 2581 CB THR A 334 21873 13552 16877 -107 -2912 814 C
ATOM 2582 OG1 THR A 334 16.071 10.028 67.275 1.00156.18 O
ANISOU 2582 OG1 THR A 334 24752 15781 18807 -345 -2943 1047 O
ATOM 2583 CG2 THR A 334 17.088 9.112 65.299 1.00135.59 C
ANISOU 2583 CG2 THR A 334 21344 13353 16821 387 -3452 767 C
ATOM 2584 N ASP A 335 12.795 10.947 65.980 1.00139.94 N
ANISOU 2584 N ASP A 335 21812 14131 17230 -864 -1562 580 N
ATOM 2585 CA ASP A 335 11.800 11.510 66.881 1.00153.20 C
ANISOU 2585 CA ASP A 335 23738 15745 18724 -1295 -1020 617 C
ATOM 2586 C ASP A 335 12.232 11.301 68.331 1.00158.85 C
ANISOU 2586 C ASP A 335 25270 16125 18962 -1552 -1101 878 C
ATOM 2587 O ASP A 335 12.420 10.149 68.754 1.00158.47 O
ANISOU 2587 O ASP A 335 25721 15684 18807 -1636 -1341 1026 O
ATOM 2588 CB ASP A 335 10.430 10.874 66.659 1.00158.95 C
ANISOU 2588 CB ASP A 335 24368 16322 19703 -1589 -607 499 C
ATOM 2589 CG ASP A 335 9.309 11.647 67.340 1.00162.29 C
ANISOU 2589 CG ASP A 335 24815 16781 20065 -1979 43 454 C
ATOM 2590 OD1 ASP A 335 9.589 12.710 67.930 1.00164.50 O
ANISOU 2590 OD1 ASP A 335 25203 17201 20098 -2001 179 500 O
ATOM 2591 OD2 ASP A 335 8.151 11.180 67.303 1.00153.33 O1-
ANISOU 2591 OD2 ASP A 335 23594 15522 19144 -2274 432 359 O1-
ATOM 2592 N PRO A 336 12.430 12.370 69.107 1.00155.44 N
ANISOU 2592 N PRO A 336 25038 15807 18214 -1680 -943 946 N
ATOM 2593 CA PRO A 336 12.567 12.181 70.558 1.00159.16 C
ANISOU 2593 CA PRO A 336 26369 15927 18177 -2036 -917 1180 C
ATOM 2594 C PRO A 336 11.370 11.463 71.137 1.00167.05 C
ANISOU 2594 C PRO A 336 27770 16589 19112 -2502 -421 1197 C
ATOM 2595 O PRO A 336 11.517 10.609 72.022 1.00166.34 O
ANISOU 2595 O PRO A 336 28429 16080 18693 -2749 -560 1413 O
ATOM 2596 CB PRO A 336 12.695 13.615 71.096 1.00157.90 C
ANISOU 2596 CB PRO A 336 26236 16003 17755 -2128 -681 1161 C
ATOM 2597 CG PRO A 336 12.230 14.508 69.988 1.00152.24 C
ANISOU 2597 CG PRO A 336 24683 15707 17454 -1907 -416 906 C
ATOM 2598 CD PRO A 336 12.520 13.784 68.715 1.00147.79 C
ANISOU 2598 CD PRO A 336 23587 15257 17310 -1534 -783 814 C
ATOM 2599 N GLY A 337 10.182 11.771 70.623 1.00175.67 N
ANISOU 2599 N GLY A 337 28364 17847 20535 -2632 139 975 N
ATOM 2600 CA GLY A 337 8.957 11.156 71.064 1.00176.28 C
ANISOU 2600 CA GLY A 337 28679 17658 20643 -3091 679 944 C
ATOM 2601 C GLY A 337 8.674 11.499 72.514 1.00181.35 C
ANISOU 2601 C GLY A 337 30072 18069 20763 -3565 1107 1072 C
ATOM 2602 O GLY A 337 9.220 12.448 73.087 1.00180.11 O
ANISOU 2602 O GLY A 337 30133 18025 20276 -3541 1084 1126 O
ATOM 2603 N ASN A 338 7.793 10.696 73.102 1.00185.25 N
ANISOU 2603 N ASN A 338 30993 18223 21172 -4033 1520 1111 N
ATOM 2604 CA ASN A 338 7.441 10.781 74.523 1.00193.94 C
ANISOU 2604 CA ASN A 338 32937 19026 21726 -4571 1982 1239 C
ATOM 2605 C ASN A 338 6.922 12.192 74.794 1.00188.46 C
ANISOU 2605 C ASN A 338 31965 18622 21018 -4656 2583 1043 C
ATOM 2606 O ASN A 338 6.027 12.660 74.070 1.00180.79 O
ANISOU 2606 O ASN A 338 30211 17921 20561 -4584 3006 780 O
ATOM 2607 CB ASN A 338 8.643 10.356 75.357 1.00193.85 C
ANISOU 2607 CB ASN A 338 33810 18709 21136 -4563 1361 1566 C
ATOM 2608 CG ASN A 338 9.093 8.940 75.060 1.00199.28 C
ANISOU 2608 CG ASN A 338 34749 19065 21903 -4444 783 1742 C
ATOM 2609 OD1 ASN A 338 8.506 8.246 74.229 1.00199.66 O
ANISOU 2609 OD1 ASN A 338 34344 19105 22413 -4394 860 1611 O
ATOM 2610 ND2 ASN A 338 10.141 8.501 75.746 1.00192.87 N
ANISOU 2610 ND2 ASN A 338 34675 17958 20648 -4395 172 2037 N
ATOM 2611 N VAL A 339 7.457 12.903 75.788 1.00179.48 N
ANISOU 2611 N VAL A 339 31438 17429 19328 -4791 2607 1156 N
ATOM 2612 CA VAL A 339 6.933 14.212 76.160 1.00180.63 C
ANISOU 2612 CA VAL A 339 31432 17779 19421 -4910 3232 960 C
ATOM 2613 C VAL A 339 7.318 15.262 75.125 1.00177.04 C
ANISOU 2613 C VAL A 339 30122 17778 19368 -4378 2986 796 C
ATOM 2614 O VAL A 339 6.514 16.134 74.773 1.00173.26 O
ANISOU 2614 O VAL A 339 29061 17532 19238 -4334 3507 546 O
ATOM 2615 CB VAL A 339 7.433 14.588 77.566 1.00184.02 C
ANISOU 2615 CB VAL A 339 32882 17967 19071 -5253 3296 1134 C
ATOM 2616 CG1 VAL A 339 6.560 13.939 78.630 1.00169.15 C
ANISOU 2616 CG1 VAL A 339 31757 15687 16825 -5900 3938 1184 C
ATOM 2617 CG2 VAL A 339 8.886 14.161 77.743 1.00177.94 C
ANISOU 2617 CG2 VAL A 339 32601 17076 17932 -5031 2352 1437 C
ATOM 2618 N GLN A 340 8.549 15.194 74.618 1.00170.96 N
ANISOU 2618 N GLN A 340 29259 17126 18571 -3969 2194 932 N
ATOM 2619 CA GLN A 340 9.065 16.197 73.694 1.00166.64 C
ANISOU 2619 CA GLN A 340 28008 16989 18317 -3504 1929 808 C
ATOM 2620 C GLN A 340 8.435 16.059 72.315 1.00170.61 C
ANISOU 2620 C GLN A 340 27577 17746 19500 -3214 1975 606 C
ATOM 2621 O GLN A 340 8.926 15.297 71.477 1.00173.59 O
ANISOU 2621 O GLN A 340 27683 18165 20108 -2932 1457 651 O
ATOM 2622 CB GLN A 340 10.587 16.085 73.592 1.00165.17 C
ANISOU 2622 CB GLN A 340 28000 16846 17911 -3193 1094 1008 C
ATOM 2623 CG GLN A 340 11.257 17.250 72.883 1.00159.79 C
ANISOU 2623 CG GLN A 340 26761 16561 17393 -2810 856 908 C
ATOM 2624 CD GLN A 340 12.770 17.152 72.919 1.00161.13 C
ANISOU 2624 CD GLN A 340 27117 16764 17339 -2563 78 1097 C
ATOM 2625 OE1 GLN A 340 13.333 16.343 73.658 1.00158.72 O
ANISOU 2625 OE1 GLN A 340 27446 16162 16696 -2693 -289 1319 O
ATOM 2626 NE2 GLN A 340 13.437 17.974 72.117 1.00152.95 N
ANISOU 2626 NE2 GLN A 340 25524 16082 16510 -2212 -187 1013 N
ATOM 2627 N LYS A 341 7.350 16.787 72.072 1.00176.13 N
ANISOU 2627 N LYS A 341 27792 18602 20528 -3276 2579 374 N
ATOM 2628 CA LYS A 341 6.745 16.783 70.750 1.00174.80 C
ANISOU 2628 CA LYS A 341 26734 18689 20994 -2998 2571 186 C
ATOM 2629 C LYS A 341 7.600 17.604 69.789 1.00163.95 C
ANISOU 2629 C LYS A 341 24874 17661 19759 -2515 2096 156 C
ATOM 2630 O LYS A 341 8.445 18.404 70.200 1.00167.06 O
ANISOU 2630 O LYS A 341 25530 18125 19821 -2434 1928 233 O
ATOM 2631 CB LYS A 341 5.323 17.344 70.810 1.00173.98 C
ANISOU 2631 CB LYS A 341 26231 18634 21240 -3194 3325 -48 C
ATOM 2632 CG LYS A 341 4.473 16.759 71.930 1.00178.61 C
ANISOU 2632 CG LYS A 341 27343 18890 21632 -3741 3942 -44 C
ATOM 2633 CD LYS A 341 3.266 15.987 71.416 1.00177.13 C
ANISOU 2633 CD LYS A 341 26663 18667 21972 -3909 4259 -191 C
ATOM 2634 CE LYS A 341 3.680 14.753 70.629 1.00176.24 C
ANISOU 2634 CE LYS A 341 26475 18495 21994 -3771 3652 -83 C
ATOM 2635 NZ LYS A 341 2.499 13.975 70.158 1.00180.24 N
ANISOU 2635 NZ LYS A 341 26541 18946 22996 -3988 3942 -230 N
ATOM 2636 N ALA A 342 7.372 17.402 68.492 1.00137.08 N
ANISOU 2636 N ALA A 342 20780 14470 16834 -2226 1883 40 N
ATOM 2637 CA ALA A 342 8.170 18.088 67.485 1.00128.28 C
ANISOU 2637 CA ALA A 342 19221 13677 15841 -1795 1445 11 C
ATOM 2638 C ALA A 342 7.459 18.051 66.139 1.00139.04 C
ANISOU 2638 C ALA A 342 19825 15255 17748 -1579 1420 -166 C
ATOM 2639 O ALA A 342 6.794 17.066 65.808 1.00152.45 O
ANISOU 2639 O ALA A 342 21383 16843 19698 -1688 1457 -219 O
ATOM 2640 CB ALA A 342 9.565 17.461 67.358 1.00125.46 C
ANISOU 2640 CB ALA A 342 19131 13300 15239 -1596 795 180 C
ATOM 2641 N VAL A 343 7.613 19.128 65.372 1.00130.03 N
ANISOU 2641 N VAL A 343 18237 14405 16766 -1295 1330 -250 N
ATOM 2642 CA VAL A 343 7.060 19.208 64.022 1.00131.89 C
ANISOU 2642 CA VAL A 343 17792 14859 17462 -1063 1210 -396 C
ATOM 2643 C VAL A 343 7.904 18.312 63.119 1.00129.85 C
ANISOU 2643 C VAL A 343 17467 14670 17202 -842 652 -357 C
ATOM 2644 O VAL A 343 9.068 18.617 62.843 1.00128.94 O
ANISOU 2644 O VAL A 343 17418 14695 16878 -617 293 -286 O
ATOM 2645 CB VAL A 343 7.033 20.654 63.511 1.00122.22 C
ANISOU 2645 CB VAL A 343 16204 13882 16352 -835 1256 -468 C
ATOM 2646 CG1 VAL A 343 6.384 20.726 62.132 1.00150.53 C
ANISOU 2646 CG1 VAL A 343 19136 17665 20392 -620 1101 -602 C
ATOM 2647 CG2 VAL A 343 6.305 21.555 64.499 1.00123.81 C
ANISOU 2647 CG2 VAL A 343 16534 13974 16535 -1030 1826 -522 C
ATOM 2648 N CYS A 344 7.320 17.212 62.647 1.00135.73 N
ANISOU 2648 N CYS A 344 18067 15311 18193 -915 597 -423 N
ATOM 2649 CA CYS A 344 8.082 16.137 62.021 1.00134.80 C
ANISOU 2649 CA CYS A 344 18022 15155 18042 -759 133 -396 C
ATOM 2650 C CYS A 344 8.207 16.261 60.508 1.00126.69 C
ANISOU 2650 C CYS A 344 16483 14400 17254 -454 -183 -527 C
ATOM 2651 O CYS A 344 8.865 15.413 59.895 1.00118.38 O
ANISOU 2651 O CYS A 344 15468 13328 16183 -298 -542 -543 O
ATOM 2652 CB CYS A 344 7.460 14.780 62.365 1.00143.66 C
ANISOU 2652 CB CYS A 344 19372 15960 19251 -1032 223 -394 C
ATOM 2653 SG CYS A 344 7.970 14.121 63.966 1.00158.26 S
ANISOU 2653 SG CYS A 344 22057 17420 20654 -1318 303 -171 S
ATOM 2654 N HIS A 345 7.590 17.266 59.890 1.00127.02 N
ANISOU 2654 N HIS A 345 16080 14669 17513 -366 -63 -624 N
ATOM 2655 CA HIS A 345 7.779 17.513 58.468 1.00129.99 C
ANISOU 2655 CA HIS A 345 16052 15304 18033 -93 -382 -725 C
ATOM 2656 C HIS A 345 9.271 17.583 58.147 1.00130.57 C
ANISOU 2656 C HIS A 345 16286 15508 17816 154 -726 -662 C
ATOM 2657 O HIS A 345 9.993 18.379 58.766 1.00132.99 O
ANISOU 2657 O HIS A 345 16780 15873 17879 189 -685 -557 O
ATOM 2658 CB HIS A 345 7.093 18.811 58.049 1.00126.19 C
ANISOU 2658 CB HIS A 345 15178 15021 17748 -15 -232 -782 C
ATOM 2659 CG HIS A 345 7.106 19.055 56.569 1.00134.93 C
ANISOU 2659 CG HIS A 345 15910 16364 18992 216 -559 -874 C
ATOM 2660 ND1 HIS A 345 6.521 18.196 55.664 1.00141.72 N
ANISOU 2660 ND1 HIS A 345 16543 17216 20088 200 -753 -994 N
ATOM 2661 CD2 HIS A 345 7.634 20.067 55.839 1.00136.01 C
ANISOU 2661 CD2 HIS A 345 15911 16736 19030 437 -729 -860 C
ATOM 2662 CE1 HIS A 345 6.690 18.666 54.441 1.00143.77 C
ANISOU 2662 CE1 HIS A 345 16563 17700 20364 405 -1036 -1049 C
ATOM 2663 NE2 HIS A 345 7.362 19.801 54.519 1.00148.76 N
ANISOU 2663 NE2 HIS A 345 17249 18480 20793 549 -1017 -964 N
ATOM 2664 N PRO A 346 9.771 16.767 57.219 1.00119.82 N
ANISOU 2664 N PRO A 346 14857 14187 16482 314 -1050 -739 N
ATOM 2665 CA PRO A 346 11.210 16.792 56.915 1.00111.34 C
ANISOU 2665 CA PRO A 346 13881 13241 15182 552 -1335 -708 C
ATOM 2666 C PRO A 346 11.619 18.139 56.340 1.00112.21 C
ANISOU 2666 C PRO A 346 13762 13663 15209 704 -1355 -709 C
ATOM 2667 O PRO A 346 11.100 18.582 55.312 1.00118.09 O
ANISOU 2667 O PRO A 346 14199 14580 16091 774 -1389 -805 O
ATOM 2668 CB PRO A 346 11.378 15.656 55.898 1.00103.73 C
ANISOU 2668 CB PRO A 346 12837 12246 14331 679 -1595 -848 C
ATOM 2669 CG PRO A 346 10.158 14.798 56.069 1.00116.95 C
ANISOU 2669 CG PRO A 346 14528 13678 16228 444 -1467 -900 C
ATOM 2670 CD PRO A 346 9.060 15.745 56.435 1.00123.33 C
ANISOU 2670 CD PRO A 346 15141 14546 17172 268 -1156 -876 C
ATOM 2671 N THR A 347 12.550 18.800 57.024 1.00 95.68 N
ANISOU 2671 N THR A 347 11851 11625 12878 733 -1356 -592 N
ATOM 2672 CA THR A 347 12.987 20.133 56.641 1.00 92.69 C
ANISOU 2672 CA THR A 347 11321 11504 12393 827 -1349 -572 C
ATOM 2673 C THR A 347 14.498 20.235 56.773 1.00 86.39 C
ANISOU 2673 C THR A 347 10634 10820 11373 948 -1556 -515 C
ATOM 2674 O THR A 347 15.103 19.638 57.666 1.00 96.54 O
ANISOU 2674 O THR A 347 12187 11943 12549 912 -1647 -430 O
ATOM 2675 CB THR A 347 12.314 21.216 57.495 1.00101.95 C
ANISOU 2675 CB THR A 347 12570 12624 13544 669 -1042 -495 C
ATOM 2676 OG1 THR A 347 12.270 20.791 58.862 1.00 95.88 O
ANISOU 2676 OG1 THR A 347 12170 11604 12655 476 -892 -399 O
ATOM 2677 CG2 THR A 347 10.897 21.472 57.002 1.00130.30 C
ANISOU 2677 CG2 THR A 347 15873 16203 17430 628 -865 -583 C
ATOM 2678 N ALA A 348 15.099 20.999 55.866 1.00 86.97 N
ANISOU 2678 N ALA A 348 10495 11165 11386 1079 -1643 -559 N
ATOM 2679 CA ALA A 348 16.533 21.259 55.862 1.00 84.41 C
ANISOU 2679 CA ALA A 348 10178 11001 10895 1178 -1809 -529 C
ATOM 2680 C ALA A 348 16.763 22.701 56.291 1.00 93.64 C
ANISOU 2680 C ALA A 348 11398 12281 11900 1077 -1690 -429 C
ATOM 2681 O ALA A 348 16.234 23.629 55.670 1.00100.65 O
ANISOU 2681 O ALA A 348 12150 13285 12806 1069 -1574 -449 O
ATOM 2682 CB ALA A 348 17.135 21.003 54.481 1.00 96.00 C
ANISOU 2682 CB ALA A 348 11388 12690 12397 1365 -1951 -677 C
ATOM 2683 N TRP A 349 17.551 22.884 57.344 1.00 89.79 N
ANISOU 2683 N TRP A 349 11130 11737 11249 998 -1750 -318 N
ATOM 2684 CA TRP A 349 17.760 24.193 57.943 1.00 79.17 C
ANISOU 2684 CA TRP A 349 9914 10442 9725 858 -1637 -224 C
ATOM 2685 C TRP A 349 19.102 24.766 57.507 1.00 79.52 C
ANISOU 2685 C TRP A 349 9812 10743 9660 913 -1808 -226 C
ATOM 2686 O TRP A 349 20.110 24.055 57.465 1.00 78.60 O
ANISOU 2686 O TRP A 349 9612 10687 9563 1017 -2038 -246 O
ATOM 2687 CB TRP A 349 17.700 24.102 59.470 1.00 83.03 C
ANISOU 2687 CB TRP A 349 10802 10685 10061 672 -1586 -103 C
ATOM 2688 CG TRP A 349 16.334 23.774 59.991 1.00 87.00 C
ANISOU 2688 CG TRP A 349 11462 10943 10652 552 -1314 -107 C
ATOM 2689 CD1 TRP A 349 15.634 22.623 59.781 1.00 91.73 C
ANISOU 2689 CD1 TRP A 349 12016 11404 11435 584 -1301 -161 C
ATOM 2690 CD2 TRP A 349 15.501 24.605 60.810 1.00 90.65 C
ANISOU 2690 CD2 TRP A 349 12137 11262 11041 364 -983 -75 C
ATOM 2691 NE1 TRP A 349 14.418 22.684 60.415 1.00 98.29 N
ANISOU 2691 NE1 TRP A 349 12985 12035 12326 409 -976 -161 N
ATOM 2692 CE2 TRP A 349 14.311 23.891 61.054 1.00 94.44 C
ANISOU 2692 CE2 TRP A 349 12650 11541 11690 286 -760 -117 C
ATOM 2693 CE3 TRP A 349 15.645 25.883 61.359 1.00 91.71 C
ANISOU 2693 CE3 TRP A 349 12445 11408 10995 245 -834 -32 C
ATOM 2694 CZ2 TRP A 349 13.273 24.410 61.824 1.00104.31 C
ANISOU 2694 CZ2 TRP A 349 14060 12620 12955 106 -363 -129 C
ATOM 2695 CZ3 TRP A 349 14.612 26.397 62.123 1.00 96.79 C
ANISOU 2695 CZ3 TRP A 349 13285 11855 11634 86 -451 -47 C
ATOM 2696 CH2 TRP A 349 13.441 25.662 62.347 1.00103.29 C
ANISOU 2696 CH2 TRP A 349 14098 12498 12649 24 -204 -101 C
ATOM 2697 N ASP A 350 19.102 26.053 57.171 1.00 93.96 N
ANISOU 2697 N ASP A 350 11595 12708 11398 843 -1687 -209 N
ATOM 2698 CA ASP A 350 20.319 26.814 56.894 1.00 88.35 C
ANISOU 2698 CA ASP A 350 10782 12227 10558 812 -1790 -196 C
ATOM 2699 C ASP A 350 20.303 27.997 57.858 1.00104.41 C
ANISOU 2699 C ASP A 350 13094 14173 12406 599 -1681 -87 C
ATOM 2700 O ASP A 350 19.829 29.083 57.518 1.00104.73 O
ANISOU 2700 O ASP A 350 13158 14232 12404 540 -1509 -78 O
ATOM 2701 CB ASP A 350 20.388 27.267 55.434 1.00 95.93 C
ANISOU 2701 CB ASP A 350 11480 13422 11547 895 -1745 -284 C
ATOM 2702 CG ASP A 350 21.655 28.046 55.121 1.00110.67 C
ANISOU 2702 CG ASP A 350 13235 15531 13283 817 -1802 -279 C
ATOM 2703 OD1 ASP A 350 22.554 28.107 55.985 1.00109.87 O
ANISOU 2703 OD1 ASP A 350 13192 15437 13117 727 -1928 -222 O
ATOM 2704 OD2 ASP A 350 21.750 28.603 54.007 1.00123.06 O1-
ANISOU 2704 OD2 ASP A 350 14669 17278 14808 823 -1730 -328 O1-
ATOM 2705 N LEU A 351 20.819 27.776 59.069 1.00 92.54 N
ANISOU 2705 N LEU A 351 11835 12546 10778 483 -1802 -5 N
ATOM 2706 CA LEU A 351 20.774 28.806 60.098 1.00 79.15 C
ANISOU 2706 CA LEU A 351 10481 10725 8866 253 -1696 82 C
ATOM 2707 C LEU A 351 21.776 29.923 59.847 1.00 77.49 C
ANISOU 2707 C LEU A 351 10200 10715 8528 139 -1772 100 C
ATOM 2708 O LEU A 351 21.604 31.025 60.379 1.00 78.55 O
ANISOU 2708 O LEU A 351 10592 10756 8495 -44 -1630 144 O
ATOM 2709 CB LEU A 351 21.028 28.187 61.475 1.00 80.34 C
ANISOU 2709 CB LEU A 351 10986 10669 8871 131 -1839 172 C
ATOM 2710 CG LEU A 351 20.036 27.125 61.961 1.00 84.06 C
ANISOU 2710 CG LEU A 351 11638 10887 9413 160 -1730 177 C
ATOM 2711 CD1 LEU A 351 20.446 25.722 61.522 1.00 81.91 C
ANISOU 2711 CD1 LEU A 351 11159 10644 9319 362 -1994 152 C
ATOM 2712 CD2 LEU A 351 19.878 27.195 63.471 1.00 88.09 C
ANISOU 2712 CD2 LEU A 351 12684 11132 9657 -85 -1680 279 C
ATOM 2713 N GLY A 352 22.807 29.667 59.050 1.00 75.28 N
ANISOU 2713 N GLY A 352 9581 10695 8328 230 -1962 53 N
ATOM 2714 CA GLY A 352 23.884 30.617 58.840 1.00 79.65 C
ANISOU 2714 CA GLY A 352 10031 11454 8778 82 -2038 64 C
ATOM 2715 C GLY A 352 25.033 30.388 59.807 1.00 99.27 C
ANISOU 2715 C GLY A 352 12567 13958 11193 -34 -2348 123 C
ATOM 2716 O GLY A 352 25.032 29.463 60.625 1.00 90.71 O
ANISOU 2716 O GLY A 352 11628 12716 10121 18 -2533 169 O
ATOM 2717 N LYS A 353 26.036 31.262 59.700 1.00 99.51 N
ANISOU 2717 N LYS A 353 12485 14177 11150 -212 -2429 129 N
ATOM 2718 CA LYS A 353 27.264 31.167 60.491 1.00 79.24 C
ANISOU 2718 CA LYS A 353 9877 11677 8554 -340 -2778 176 C
ATOM 2719 C LYS A 353 27.886 29.768 60.426 1.00 79.85 C
ANISOU 2719 C LYS A 353 9645 11819 8875 -87 -3069 136 C
ATOM 2720 O LYS A 353 28.630 29.372 61.332 1.00107.37 O
ANISOU 2720 O LYS A 353 13183 15252 12359 -130 -3431 205 O
ATOM 2721 CB LYS A 353 27.027 31.570 61.956 1.00 83.75 C
ANISOU 2721 CB LYS A 353 10987 11978 8856 -578 -2868 294 C
ATOM 2722 CG LYS A 353 26.889 33.072 62.215 1.00 85.33 C
ANISOU 2722 CG LYS A 353 11483 12123 8815 -876 -2678 320 C
ATOM 2723 CD LYS A 353 26.382 33.324 63.638 1.00106.80 C
ANISOU 2723 CD LYS A 353 14810 14521 11247 -1080 -2677 402 C
ATOM 2724 CE LYS A 353 26.584 34.766 64.105 1.00 98.49 C
ANISOU 2724 CE LYS A 353 14085 13399 9936 -1414 -2592 418 C
ATOM 2725 NZ LYS A 353 28.011 35.110 64.368 1.00 81.26 N
ANISOU 2725 NZ LYS A 353 11763 11404 7707 -1641 -2970 446 N
ATOM 2726 N GLY A 354 27.593 29.005 59.369 1.00 82.30 N
ANISOU 2726 N GLY A 354 9657 12220 9393 180 -2942 24 N
ATOM 2727 CA GLY A 354 28.109 27.663 59.201 1.00 89.80 C
ANISOU 2727 CA GLY A 354 10325 13195 10600 456 -3175 -42 C
ATOM 2728 C GLY A 354 27.229 26.548 59.732 1.00 88.83 C
ANISOU 2728 C GLY A 354 10483 12767 10500 613 -3232 6 C
ATOM 2729 O GLY A 354 27.575 25.371 59.557 1.00 82.18 O
ANISOU 2729 O GLY A 354 9449 11895 9880 863 -3423 -50 O
ATOM 2730 N ASP A 355 26.106 26.872 60.365 1.00 87.10 N
ANISOU 2730 N ASP A 355 10710 12308 10075 470 -3050 98 N
ATOM 2731 CA ASP A 355 25.254 25.881 61.012 1.00 89.25 C
ANISOU 2731 CA ASP A 355 11300 12273 10338 541 -3070 156 C
ATOM 2732 C ASP A 355 24.267 25.317 59.995 1.00 93.23 C
ANISOU 2732 C ASP A 355 11652 12766 11007 726 -2813 42 C
ATOM 2733 O ASP A 355 23.450 26.060 59.441 1.00 87.32 O
ANISOU 2733 O ASP A 355 10898 12062 10215 665 -2508 2 O
ATOM 2734 CB ASP A 355 24.517 26.517 62.191 1.00 86.77 C
ANISOU 2734 CB ASP A 355 11526 11712 9729 268 -2939 281 C
ATOM 2735 CG ASP A 355 23.937 25.495 63.149 1.00 93.64 C
ANISOU 2735 CG ASP A 355 12796 12252 10531 260 -3017 373 C
ATOM 2736 OD1 ASP A 355 23.772 24.320 62.758 1.00 97.24 O
ANISOU 2736 OD1 ASP A 355 13119 12638 11188 476 -3097 333 O
ATOM 2737 OD2 ASP A 355 23.636 25.876 64.300 1.00 90.59 O1-
ANISOU 2737 OD2 ASP A 355 12898 11657 9864 13 -2979 481 O1-
ATOM 2738 N PHE A 356 24.343 24.008 59.753 1.00 96.12 N
ANISOU 2738 N PHE A 356 11903 13049 11568 953 -2965 -12 N
ATOM 2739 CA PHE A 356 23.446 23.319 58.831 1.00 82.45 C
ANISOU 2739 CA PHE A 356 10054 11281 9994 1113 -2777 -130 C
ATOM 2740 C PHE A 356 22.838 22.116 59.532 1.00 86.56 C
ANISOU 2740 C PHE A 356 10866 11468 10556 1154 -2866 -71 C
ATOM 2741 O PHE A 356 23.566 21.286 60.085 1.00110.97 O
ANISOU 2741 O PHE A 356 14025 14434 13703 1254 -3182 -18 O
ATOM 2742 CB PHE A 356 24.180 22.868 57.566 1.00 79.92 C
ANISOU 2742 CB PHE A 356 9284 11200 9881 1351 -2829 -307 C
ATOM 2743 CG PHE A 356 24.830 23.986 56.811 1.00 80.91 C
ANISOU 2743 CG PHE A 356 9136 11654 9952 1279 -2715 -368 C
ATOM 2744 CD1 PHE A 356 24.076 24.820 56.005 1.00 90.99 C
ANISOU 2744 CD1 PHE A 356 10402 13035 11134 1192 -2435 -405 C
ATOM 2745 CD2 PHE A 356 26.195 24.196 56.896 1.00 91.06 C
ANISOU 2745 CD2 PHE A 356 10171 13132 11294 1289 -2901 -386 C
ATOM 2746 CE1 PHE A 356 24.670 25.849 55.304 1.00 91.41 C
ANISOU 2746 CE1 PHE A 356 10268 13358 11105 1097 -2328 -443 C
ATOM 2747 CE2 PHE A 356 26.795 25.224 56.197 1.00 92.93 C
ANISOU 2747 CE2 PHE A 356 10169 13667 11474 1176 -2762 -444 C
ATOM 2748 CZ PHE A 356 26.031 26.051 55.399 1.00 93.70 C
ANISOU 2748 CZ PHE A 356 10325 13844 11431 1070 -2466 -465 C
ATOM 2749 N ARG A 357 21.509 22.016 59.505 1.00 94.47 N
ANISOU 2749 N ARG A 357 12033 12311 11549 1073 -2601 -78 N
ATOM 2750 CA ARG A 357 20.806 20.962 60.221 1.00 95.57 C
ANISOU 2750 CA ARG A 357 12492 12116 11702 1035 -2617 -16 C
ATOM 2751 C ARG A 357 19.658 20.417 59.385 1.00 99.49 C
ANISOU 2751 C ARG A 357 12863 12559 12377 1092 -2402 -138 C
ATOM 2752 O ARG A 357 19.092 21.115 58.540 1.00 90.28 O
ANISOU 2752 O ARG A 357 11472 11570 11262 1090 -2192 -227 O
ATOM 2753 CB ARG A 357 20.257 21.456 61.564 1.00 91.61 C
ANISOU 2753 CB ARG A 357 12459 11399 10950 747 -2481 139 C
ATOM 2754 CG ARG A 357 21.279 22.140 62.444 1.00100.62 C
ANISOU 2754 CG ARG A 357 13786 12581 11863 629 -2697 262 C
ATOM 2755 CD ARG A 357 20.643 22.636 63.721 1.00107.96 C
ANISOU 2755 CD ARG A 357 15239 13281 12502 322 -2508 384 C
ATOM 2756 NE ARG A 357 21.528 23.525 64.460 1.00 93.81 N
ANISOU 2756 NE ARG A 357 13631 11553 10460 167 -2684 478 N
ATOM 2757 CZ ARG A 357 21.248 24.028 65.654 1.00 97.38 C
ANISOU 2757 CZ ARG A 357 14597 11810 10592 -120 -2578 580 C
ATOM 2758 NH1 ARG A 357 20.123 23.728 66.280 1.00 97.78 N
ANISOU 2758 NH1 ARG A 357 15021 11594 10538 -284 -2259 602 N
ATOM 2759 NH2 ARG A 357 22.116 24.852 66.233 1.00 98.19 N
ANISOU 2759 NH2 ARG A 357 14851 11986 10472 -268 -2778 649 N
ATOM 2760 N ILE A 358 19.320 19.156 59.642 1.00 92.77 N
ANISOU 2760 N ILE A 358 12184 11444 11622 1130 -2488 -132 N
ATOM 2761 CA ILE A 358 18.145 18.506 59.074 1.00 88.74 C
ANISOU 2761 CA ILE A 358 11622 10817 11276 1119 -2307 -233 C
ATOM 2762 C ILE A 358 17.269 18.043 60.228 1.00 95.15 C
ANISOU 2762 C ILE A 358 12856 11289 12009 877 -2167 -113 C
ATOM 2763 O ILE A 358 17.724 17.291 61.100 1.00107.55 O
ANISOU 2763 O ILE A 358 14766 12614 13485 849 -2369 7 O
ATOM 2764 CB ILE A 358 18.515 17.323 58.165 1.00 87.23 C
ANISOU 2764 CB ILE A 358 11251 10603 11289 1365 -2507 -376 C
ATOM 2765 CG1 ILE A 358 19.007 17.814 56.803 1.00 83.15 C
ANISOU 2765 CG1 ILE A 358 10315 10432 10845 1548 -2506 -544 C
ATOM 2766 CG2 ILE A 358 17.322 16.390 57.997 1.00 90.08 C
ANISOU 2766 CG2 ILE A 358 11713 10723 11791 1281 -2386 -436 C
ATOM 2767 CD1 ILE A 358 19.284 16.693 55.817 1.00 82.51 C
ANISOU 2767 CD1 ILE A 358 10074 10328 10948 1779 -2635 -731 C
ATOM 2768 N LEU A 359 16.022 18.499 60.240 1.00 86.86 N
ANISOU 2768 N LEU A 359 11787 10214 11002 698 -1823 -143 N
ATOM 2769 CA LEU A 359 15.014 18.026 61.179 1.00 90.28 C
ANISOU 2769 CA LEU A 359 12556 10340 11404 438 -1588 -75 C
ATOM 2770 C LEU A 359 14.157 16.991 60.460 1.00 94.18 C
ANISOU 2770 C LEU A 359 12896 10724 12166 454 -1547 -197 C
ATOM 2771 O LEU A 359 13.485 17.315 59.475 1.00113.28 O
ANISOU 2771 O LEU A 359 14940 13316 14786 510 -1435 -334 O
ATOM 2772 CB LEU A 359 14.170 19.195 61.690 1.00 91.00 C
ANISOU 2772 CB LEU A 359 12683 10467 11427 229 -1195 -62 C
ATOM 2773 CG LEU A 359 13.379 19.091 62.997 1.00 93.20 C
ANISOU 2773 CG LEU A 359 13397 10454 11561 -96 -871 25 C
ATOM 2774 CD1 LEU A 359 12.808 20.448 63.356 1.00 94.11 C
ANISOU 2774 CD1 LEU A 359 13483 10654 11622 -221 -499 -1 C
ATOM 2775 CD2 LEU A 359 12.253 18.083 62.874 1.00103.19 C
ANISOU 2775 CD2 LEU A 359 14634 11519 13054 -226 -683 -42 C
ATOM 2776 N MET A 360 14.182 15.751 60.944 1.00103.60 N
ANISOU 2776 N MET A 360 14401 11610 13353 395 -1669 -140 N
ATOM 2777 CA MET A 360 13.473 14.671 60.260 1.00109.80 C
ANISOU 2777 CA MET A 360 15077 12258 14384 396 -1672 -262 C
ATOM 2778 C MET A 360 13.242 13.521 61.225 1.00109.80 C
ANISOU 2778 C MET A 360 15570 11838 14312 195 -1683 -144 C
ATOM 2779 O MET A 360 14.204 12.914 61.705 1.00121.18 O
ANISOU 2779 O MET A 360 17320 13103 15619 303 -1993 -30 O
ATOM 2780 CB MET A 360 14.263 14.203 59.040 1.00102.12 C
ANISOU 2780 CB MET A 360 13818 11436 13546 727 -1987 -403 C
ATOM 2781 CG MET A 360 13.542 13.171 58.201 1.00104.54 C
ANISOU 2781 CG MET A 360 14012 11619 14091 727 -2004 -561 C
ATOM 2782 SD MET A 360 14.404 12.809 56.664 1.00110.46 S
ANISOU 2782 SD MET A 360 14434 12581 14957 1097 -2288 -776 S
ATOM 2783 CE MET A 360 13.399 11.466 56.044 1.00106.40 C
ANISOU 2783 CE MET A 360 13960 11798 14670 992 -2297 -934 C
ATOM 2784 N CYS A 361 11.972 13.213 61.495 1.00106.12 N
ANISOU 2784 N CYS A 361 15171 11200 13951 -102 -1357 -170 N
ATOM 2785 CA CYS A 361 11.596 12.104 62.374 1.00107.32 C
ANISOU 2785 CA CYS A 361 15819 10928 14028 -364 -1304 -61 C
ATOM 2786 C CYS A 361 11.679 10.793 61.587 1.00107.65 C
ANISOU 2786 C CYS A 361 15831 10793 14277 -229 -1575 -159 C
ATOM 2787 O CYS A 361 10.681 10.143 61.271 1.00126.56 O
ANISOU 2787 O CYS A 361 18160 13048 16877 -423 -1414 -257 O
ATOM 2788 CB CYS A 361 10.202 12.331 62.944 1.00114.59 C
ANISOU 2788 CB CYS A 361 16779 11753 15006 -764 -791 -76 C
ATOM 2789 SG CYS A 361 9.984 13.919 63.788 1.00127.02 S
ANISOU 2789 SG CYS A 361 18370 13515 16375 -908 -399 -20 S
ATOM 2790 N THR A 362 12.915 10.403 61.287 1.00 96.84 N
ANISOU 2790 N THR A 362 14508 9420 12868 105 -1993 -143 N
ATOM 2791 CA THR A 362 13.168 9.336 60.328 1.00 97.25 C
ANISOU 2791 CA THR A 362 14453 9364 13133 328 -2256 -291 C
ATOM 2792 C THR A 362 12.674 7.985 60.836 1.00103.70 C
ANISOU 2792 C THR A 362 15734 9689 13979 109 -2276 -226 C
ATOM 2793 O THR A 362 12.918 7.611 61.987 1.00109.09 O
ANISOU 2793 O THR A 362 16948 10054 14446 -37 -2336 -8 O
ATOM 2794 CB THR A 362 14.662 9.256 60.019 1.00 93.98 C
ANISOU 2794 CB THR A 362 13977 9038 12691 746 -2657 -296 C
ATOM 2795 OG1 THR A 362 15.154 10.561 59.686 1.00 91.84 O
ANISOU 2795 OG1 THR A 362 13335 9205 12356 885 -2614 -327 O
ATOM 2796 CG2 THR A 362 14.920 8.317 58.857 1.00 93.43 C
ANISOU 2796 CG2 THR A 362 13726 8914 12859 1012 -2860 -513 C
ATOM 2797 N LYS A 363 11.973 7.259 59.969 1.00126.62 N
ANISOU 2797 N LYS A 363 18470 12514 17127 61 -2242 -412 N
ATOM 2798 CA LYS A 363 11.695 5.842 60.146 1.00133.52 C
ANISOU 2798 CA LYS A 363 19748 12910 18072 -74 -2344 -398 C
ATOM 2799 C LYS A 363 12.606 5.031 59.229 1.00138.78 C
ANISOU 2799 C LYS A 363 20358 13494 18879 339 -2732 -550 C
ATOM 2800 O LYS A 363 13.354 5.574 58.414 1.00143.37 O
ANISOU 2800 O LYS A 363 20551 14415 19506 689 -2867 -683 O
ATOM 2801 CB LYS A 363 10.225 5.525 59.846 1.00140.84 C
ANISOU 2801 CB LYS A 363 20546 13769 19197 -462 -2029 -519 C
ATOM 2802 CG LYS A 363 9.217 6.510 60.415 1.00145.73 C
ANISOU 2802 CG LYS A 363 20995 14582 19793 -809 -1578 -467 C
ATOM 2803 CD LYS A 363 9.162 6.450 61.931 1.00142.07 C
ANISOU 2803 CD LYS A 363 21106 13826 19048 -1116 -1383 -212 C
ATOM 2804 CE LYS A 363 8.644 7.757 62.507 1.00150.10 C
ANISOU 2804 CE LYS A 363 21939 15120 19973 -1298 -975 -170 C
ATOM 2805 NZ LYS A 363 7.504 8.293 61.710 1.00165.81 N
ANISOU 2805 NZ LYS A 363 23310 17394 22297 -1405 -690 -381 N
ATOM 2806 N VAL A 364 12.533 3.709 59.363 1.00131.64 N
ANISOU 2806 N VAL A 364 19862 12112 18043 284 -2885 -540 N
ATOM 2807 CA VAL A 364 13.320 2.829 58.507 1.00126.84 C
ANISOU 2807 CA VAL A 364 19238 11356 17599 673 -3218 -716 C
ATOM 2808 C VAL A 364 12.432 2.328 57.375 1.00142.31 C
ANISOU 2808 C VAL A 364 20975 13322 19773 550 -3113 -992 C
ATOM 2809 O VAL A 364 11.969 1.182 57.386 1.00139.74 O
ANISOU 2809 O VAL A 364 20989 12562 19543 379 -3161 -1029 O
ATOM 2810 CB VAL A 364 13.940 1.665 59.303 1.00115.69 C
ANISOU 2810 CB VAL A 364 18442 9371 16145 763 -3525 -543 C
ATOM 2811 CG1 VAL A 364 14.928 0.894 58.439 1.00126.00 C
ANISOU 2811 CG1 VAL A 364 19670 10549 17654 1258 -3865 -745 C
ATOM 2812 CG2 VAL A 364 14.632 2.189 60.552 1.00115.34 C
ANISOU 2812 CG2 VAL A 364 18680 9299 15846 783 -3644 -235 C
ATOM 2813 N THR A 365 12.173 3.196 56.402 1.00145.49 N
ANISOU 2813 N THR A 365 20840 14202 20238 611 -2991 -1180 N
ATOM 2814 CA THR A 365 11.390 2.864 55.222 1.00133.24 C
ANISOU 2814 CA THR A 365 19043 12720 18864 512 -2951 -1451 C
ATOM 2815 C THR A 365 12.130 3.359 53.988 1.00130.11 C
ANISOU 2815 C THR A 365 18254 12707 18474 898 -3072 -1679 C
ATOM 2816 O THR A 365 13.090 4.129 54.080 1.00130.88 O
ANISOU 2816 O THR A 365 18190 13074 18463 1181 -3116 -1618 O
ATOM 2817 CB THR A 365 9.986 3.483 55.278 1.00137.63 C
ANISOU 2817 CB THR A 365 19338 13464 19490 80 -2649 -1440 C
ATOM 2818 OG1 THR A 365 10.098 4.909 55.375 1.00129.97 O
ANISOU 2818 OG1 THR A 365 18011 12949 18423 155 -2506 -1363 O
ATOM 2819 CG2 THR A 365 9.205 2.953 56.475 1.00133.83 C
ANISOU 2819 CG2 THR A 365 19247 12600 19001 -355 -2452 -1243 C
ATOM 2820 N MET A 366 11.679 2.907 52.816 1.00129.57 N
ANISOU 2820 N MET A 366 18054 12657 18518 876 -3119 -1950 N
ATOM 2821 CA MET A 366 12.280 3.391 51.579 1.00126.95 C
ANISOU 2821 CA MET A 366 17399 12693 18145 1181 -3189 -2181 C
ATOM 2822 C MET A 366 11.879 4.831 51.287 1.00122.61 C
ANISOU 2822 C MET A 366 16421 12652 17513 1097 -3039 -2136 C
ATOM 2823 O MET A 366 12.683 5.598 50.744 1.00120.52 O
ANISOU 2823 O MET A 366 15926 12730 17134 1364 -3053 -2194 O
ATOM 2824 CB MET A 366 11.893 2.486 50.408 1.00132.18 C
ANISOU 2824 CB MET A 366 18119 13206 18898 1152 -3295 -2492 C
ATOM 2825 CG MET A 366 12.523 2.900 49.084 1.00127.73 C
ANISOU 2825 CG MET A 366 17306 12989 18238 1436 -3341 -2753 C
ATOM 2826 SD MET A 366 12.129 1.787 47.723 1.00133.88 S
ANISOU 2826 SD MET A 366 18252 13554 19061 1388 -3472 -3142 S
ATOM 2827 CE MET A 366 13.034 2.554 46.381 1.00133.23 C
ANISOU 2827 CE MET A 366 17906 13944 18773 1716 -3445 -3389 C
ATOM 2828 N ASP A 367 10.656 5.220 51.650 1.00132.07 N
ANISOU 2828 N ASP A 367 17506 13889 18786 729 -2882 -2036 N
ATOM 2829 CA ASP A 367 10.192 6.572 51.359 1.00137.92 C
ANISOU 2829 CA ASP A 367 17844 15066 19494 668 -2760 -1998 C
ATOM 2830 C ASP A 367 10.916 7.617 52.201 1.00131.43 C
ANISOU 2830 C ASP A 367 16975 14442 18519 806 -2648 -1780 C
ATOM 2831 O ASP A 367 11.047 8.769 51.772 1.00126.11 O
ANISOU 2831 O ASP A 367 16006 14145 17763 900 -2602 -1776 O
ATOM 2832 CB ASP A 367 8.681 6.666 51.569 1.00146.96 C
ANISOU 2832 CB ASP A 367 18835 16172 20831 262 -2615 -1968 C
ATOM 2833 CG ASP A 367 7.894 6.052 50.424 1.00155.17 C
ANISOU 2833 CG ASP A 367 19764 17177 22016 120 -2773 -2210 C
ATOM 2834 OD1 ASP A 367 8.374 6.110 49.272 1.00137.86 O
ANISOU 2834 OD1 ASP A 367 17500 15163 19719 337 -2955 -2396 O
ATOM 2835 OD2 ASP A 367 6.798 5.508 50.676 1.00154.10 O1-
ANISOU 2835 OD2 ASP A 367 19628 16834 22089 -232 -2710 -2222 O1-
ATOM 2836 N ASP A 368 11.385 7.247 53.394 1.00132.18 N
ANISOU 2836 N ASP A 368 17392 14274 18557 800 -2625 -1592 N
ATOM 2837 CA ASP A 368 12.206 8.143 54.199 1.00127.52 C
ANISOU 2837 CA ASP A 368 16812 13843 17796 932 -2578 -1397 C
ATOM 2838 C ASP A 368 13.694 8.002 53.910 1.00115.91 C
ANISOU 2838 C ASP A 368 15362 12434 16246 1330 -2794 -1448 C
ATOM 2839 O ASP A 368 14.472 8.876 54.308 1.00109.10 O
ANISOU 2839 O ASP A 368 14409 11789 15253 1461 -2792 -1330 O
ATOM 2840 CB ASP A 368 11.948 7.914 55.693 1.00129.16 C
ANISOU 2840 CB ASP A 368 17389 13746 17940 692 -2460 -1151 C
ATOM 2841 CG ASP A 368 10.648 8.542 56.162 1.00140.58 C
ANISOU 2841 CG ASP A 368 18718 15254 19444 322 -2138 -1080 C
ATOM 2842 OD1 ASP A 368 9.907 9.079 55.312 1.00141.78 O
ANISOU 2842 OD1 ASP A 368 18479 15659 19732 271 -2061 -1217 O
ATOM 2843 OD2 ASP A 368 10.369 8.507 57.379 1.00134.08 O1-
ANISOU 2843 OD2 ASP A 368 18196 14218 18530 83 -1961 -894 O1-
ATOM 2844 N PHE A 369 14.107 6.927 53.236 1.00120.12 N
ANISOU 2844 N PHE A 369 15997 12770 16873 1518 -2970 -1636 N
ATOM 2845 CA PHE A 369 15.480 6.834 52.752 1.00117.90 C
ANISOU 2845 CA PHE A 369 15627 12593 16578 1921 -3128 -1751 C
ATOM 2846 C PHE A 369 15.721 7.829 51.624 1.00110.72 C
ANISOU 2846 C PHE A 369 14322 12161 15584 2031 -3042 -1910 C
ATOM 2847 O PHE A 369 16.707 8.576 51.638 1.00104.68 O
ANISOU 2847 O PHE A 369 13374 11662 14736 2229 -3044 -1876 O
ATOM 2848 CB PHE A 369 15.773 5.405 52.291 1.00121.07 C
ANISOU 2848 CB PHE A 369 16252 12625 17124 2096 -3296 -1946 C
ATOM 2849 CG PHE A 369 17.035 5.266 51.486 1.00112.04 C
ANISOU 2849 CG PHE A 369 14934 11615 16021 2515 -3390 -2163 C
ATOM 2850 CD1 PHE A 369 18.267 5.178 52.111 1.00124.40 C
ANISOU 2850 CD1 PHE A 369 16513 13114 17640 2819 -3544 -2070 C
ATOM 2851 CD2 PHE A 369 16.987 5.206 50.102 1.00107.06 C
ANISOU 2851 CD2 PHE A 369 14130 11168 15380 2594 -3324 -2470 C
ATOM 2852 CE1 PHE A 369 19.429 5.045 51.371 1.00121.84 C
ANISOU 2852 CE1 PHE A 369 15963 12920 17410 3207 -3590 -2297 C
ATOM 2853 CE2 PHE A 369 18.144 5.074 49.358 1.00112.15 C
ANISOU 2853 CE2 PHE A 369 14618 11936 16059 2959 -3338 -2699 C
ATOM 2854 CZ PHE A 369 19.366 4.990 49.993 1.00119.54 C
ANISOU 2854 CZ PHE A 369 15502 12816 17101 3273 -3451 -2621 C
ATOM 2855 N LEU A 370 14.821 7.850 50.638 1.00101.62 N
ANISOU 2855 N LEU A 370 13054 11113 14446 1881 -2983 -2077 N
ATOM 2856 CA LEU A 370 14.911 8.824 49.555 1.00 94.51 C
ANISOU 2856 CA LEU A 370 11852 10638 13421 1934 -2918 -2200 C
ATOM 2857 C LEU A 370 14.801 10.246 50.088 1.00 93.42 C
ANISOU 2857 C LEU A 370 11525 10794 13177 1834 -2791 -1982 C
ATOM 2858 O LEU A 370 15.560 11.135 49.684 1.00 93.46 O
ANISOU 2858 O LEU A 370 11344 11119 13049 1975 -2752 -1993 O
ATOM 2859 CB LEU A 370 13.817 8.556 48.523 1.00 99.32 C
ANISOU 2859 CB LEU A 370 12424 11253 14058 1745 -2945 -2380 C
ATOM 2860 CG LEU A 370 13.847 7.186 47.852 1.00 96.48 C
ANISOU 2860 CG LEU A 370 12282 10600 13777 1808 -3065 -2637 C
ATOM 2861 CD1 LEU A 370 12.675 7.040 46.895 1.00102.00 C
ANISOU 2861 CD1 LEU A 370 12942 11325 14487 1561 -3130 -2793 C
ATOM 2862 CD2 LEU A 370 15.170 7.006 47.133 1.00 98.59 C
ANISOU 2862 CD2 LEU A 370 12530 10972 13956 2160 -3071 -2844 C
ATOM 2863 N THR A 371 13.851 10.478 50.998 1.00 88.97 N
ANISOU 2863 N THR A 371 11020 10112 12673 1575 -2699 -1794 N
ATOM 2864 CA THR A 371 13.660 11.811 51.558 1.00 87.22 C
ANISOU 2864 CA THR A 371 10655 10120 12366 1475 -2552 -1605 C
ATOM 2865 C THR A 371 14.930 12.318 52.230 1.00 84.59 C
ANISOU 2865 C THR A 371 10357 9884 11897 1651 -2569 -1477 C
ATOM 2866 O THR A 371 15.206 13.522 52.211 1.00 81.69 O
ANISOU 2866 O THR A 371 9826 9803 11410 1662 -2487 -1402 O
ATOM 2867 CB THR A 371 12.496 11.791 52.552 1.00 90.20 C
ANISOU 2867 CB THR A 371 11129 10292 12849 1173 -2400 -1455 C
ATOM 2868 OG1 THR A 371 11.325 11.282 51.903 1.00 93.33 O
ANISOU 2868 OG1 THR A 371 11435 10606 13422 995 -2409 -1588 O
ATOM 2869 CG2 THR A 371 12.194 13.192 53.059 1.00 92.05 C
ANISOU 2869 CG2 THR A 371 11213 10744 13016 1078 -2214 -1301 C
ATOM 2870 N ALA A 372 15.724 11.412 52.808 1.00 98.41 N
ANISOU 2870 N ALA A 372 12323 11388 13680 1790 -2705 -1452 N
ATOM 2871 CA ALA A 372 16.974 11.817 53.442 1.00101.87 C
ANISOU 2871 CA ALA A 372 12765 11912 14029 1964 -2789 -1336 C
ATOM 2872 C ALA A 372 17.972 12.339 52.415 1.00100.22 C
ANISOU 2872 C ALA A 372 12255 12049 13775 2199 -2805 -1497 C
ATOM 2873 O ALA A 372 18.732 13.271 52.700 1.00104.45 O
ANISOU 2873 O ALA A 372 12659 12818 14210 2244 -2789 -1404 O
ATOM 2874 CB ALA A 372 17.568 10.654 54.231 1.00106.90 C
ANISOU 2874 CB ALA A 372 13697 12173 14748 2086 -2995 -1273 C
ATOM 2875 N HIS A 373 17.996 11.744 51.219 1.00 98.67 N
ANISOU 2875 N HIS A 373 11970 11883 13638 2324 -2819 -1750 N
ATOM 2876 CA HIS A 373 18.787 12.310 50.131 1.00 97.68 C
ANISOU 2876 CA HIS A 373 11582 12105 13426 2482 -2755 -1923 C
ATOM 2877 C HIS A 373 18.214 13.649 49.685 1.00100.92 C
ANISOU 2877 C HIS A 373 11846 12832 13666 2295 -2612 -1858 C
ATOM 2878 O HIS A 373 18.951 14.629 49.514 1.00101.17 O
ANISOU 2878 O HIS A 373 11710 13155 13575 2334 -2541 -1826 O
ATOM 2879 CB HIS A 373 18.832 11.345 48.948 1.00 92.48 C
ANISOU 2879 CB HIS A 373 10939 11376 12825 2621 -2772 -2226 C
ATOM 2880 CG HIS A 373 19.623 10.102 49.202 1.00 93.74 C
ANISOU 2880 CG HIS A 373 11204 11240 13174 2883 -2905 -2335 C
ATOM 2881 ND1 HIS A 373 19.213 9.120 50.078 1.00 96.23 N
ANISOU 2881 ND1 HIS A 373 11802 11131 13629 2851 -3051 -2230 N
ATOM 2882 CD2 HIS A 373 20.800 9.679 48.685 1.00 99.08 C
ANISOU 2882 CD2 HIS A 373 11743 11963 13941 3190 -2907 -2547 C
ATOM 2883 CE1 HIS A 373 20.106 8.147 50.091 1.00102.30 C
ANISOU 2883 CE1 HIS A 373 12624 11676 14569 3149 -3180 -2357 C
ATOM 2884 NE2 HIS A 373 21.079 8.462 49.255 1.00 95.62 N
ANISOU 2884 NE2 HIS A 373 11496 11116 13720 3374 -3088 -2562 N
ATOM 2885 N HIS A 374 16.894 13.698 49.488 1.00106.62 N
ANISOU 2885 N HIS A 374 12624 13485 14402 2089 -2584 -1838 N
ATOM 2886 CA HIS A 374 16.234 14.912 49.020 1.00112.77 C
ANISOU 2886 CA HIS A 374 13269 14513 15065 1940 -2496 -1777 C
ATOM 2887 C HIS A 374 16.497 16.086 49.957 1.00111.64 C
ANISOU 2887 C HIS A 374 13084 14489 14843 1874 -2401 -1548 C
ATOM 2888 O HIS A 374 16.880 17.175 49.514 1.00119.32 O
ANISOU 2888 O HIS A 374 13935 15736 15666 1876 -2337 -1522 O
ATOM 2889 CB HIS A 374 14.736 14.640 48.871 1.00120.28 C
ANISOU 2889 CB HIS A 374 14248 15316 16138 1742 -2519 -1782 C
ATOM 2890 CG HIS A 374 13.915 15.863 48.641 1.00116.24 C
ANISOU 2890 CG HIS A 374 13590 14988 15588 1606 -2462 -1682 C
ATOM 2891 ND1 HIS A 374 13.460 16.237 47.394 1.00114.07 N
ANISOU 2891 ND1 HIS A 374 13223 14882 15235 1582 -2549 -1787 N
ATOM 2892 CD2 HIS A 374 13.441 16.784 49.509 1.00116.80 C
ANISOU 2892 CD2 HIS A 374 13613 15069 15695 1494 -2341 -1488 C
ATOM 2893 CE1 HIS A 374 12.758 17.349 47.502 1.00115.22 C
ANISOU 2893 CE1 HIS A 374 13249 15129 15399 1487 -2512 -1648 C
ATOM 2894 NE2 HIS A 374 12.711 17.685 48.778 1.00117.28 N
ANISOU 2894 NE2 HIS A 374 13524 15292 15745 1436 -2362 -1480 N
ATOM 2895 N GLU A 375 16.299 15.884 51.262 1.00 96.80 N
ANISOU 2895 N GLU A 375 11353 12389 13037 1790 -2385 -1383 N
ATOM 2896 CA GLU A 375 16.541 16.964 52.215 1.00 92.57 C
ANISOU 2896 CA GLU A 375 10840 11935 12399 1705 -2294 -1181 C
ATOM 2897 C GLU A 375 18.020 17.326 52.283 1.00 92.29 C
ANISOU 2897 C GLU A 375 10731 12080 12255 1855 -2359 -1172 C
ATOM 2898 O GLU A 375 18.369 18.510 52.359 1.00 81.80 O
ANISOU 2898 O GLU A 375 9322 10964 10794 1800 -2283 -1086 O
ATOM 2899 CB GLU A 375 16.012 16.575 53.595 1.00 95.01 C
ANISOU 2899 CB GLU A 375 11393 11944 12762 1552 -2250 -1022 C
ATOM 2900 CG GLU A 375 14.501 16.434 53.656 1.00 89.75 C
ANISOU 2900 CG GLU A 375 10739 11130 12233 1352 -2115 -1023 C
ATOM 2901 CD GLU A 375 13.782 17.726 53.308 1.00 98.44 C
ANISOU 2901 CD GLU A 375 11644 12432 13326 1268 -1970 -994 C
ATOM 2902 OE1 GLU A 375 14.298 18.810 53.653 1.00107.65 O
ANISOU 2902 OE1 GLU A 375 12807 13748 14348 1275 -1902 -891 O
ATOM 2903 OE2 GLU A 375 12.699 17.657 52.690 1.00117.98 O1-
ANISOU 2903 OE2 GLU A 375 13973 14899 15957 1196 -1948 -1073 O1-
ATOM 2904 N MET A 376 18.904 16.326 52.253 1.00 96.87 N
ANISOU 2904 N MET A 376 11320 12567 12918 2046 -2502 -1267 N
ATOM 2905 CA MET A 376 20.334 16.619 52.235 1.00 98.37 C
ANISOU 2905 CA MET A 376 11351 12948 13076 2204 -2569 -1290 C
ATOM 2906 C MET A 376 20.740 17.344 50.959 1.00 95.64 C
ANISOU 2906 C MET A 376 10763 12950 12628 2241 -2444 -1440 C
ATOM 2907 O MET A 376 21.744 18.065 50.947 1.00 94.01 O
ANISOU 2907 O MET A 376 10391 12974 12354 2267 -2417 -1424 O
ATOM 2908 CB MET A 376 21.147 15.334 52.394 1.00 97.52 C
ANISOU 2908 CB MET A 376 11264 12643 13147 2445 -2758 -1386 C
ATOM 2909 CG MET A 376 22.626 15.578 52.663 1.00101.58 C
ANISOU 2909 CG MET A 376 11576 13314 13706 2611 -2871 -1383 C
ATOM 2910 SD MET A 376 23.536 14.103 53.161 1.00108.99 S
ANISOU 2910 SD MET A 376 12554 13941 14915 2927 -3168 -1439 S
ATOM 2911 CE MET A 376 22.819 13.771 54.769 1.00105.19 C
ANISOU 2911 CE MET A 376 12539 13061 14366 2737 -3348 -1130 C
ATOM 2912 N GLY A 377 19.981 17.162 49.876 1.00101.56 N
ANISOU 2912 N GLY A 377 11508 13734 13348 2216 -2375 -1584 N
ATOM 2913 CA GLY A 377 20.244 17.930 48.669 1.00101.15 C
ANISOU 2913 CA GLY A 377 11316 13990 13128 2198 -2255 -1696 C
ATOM 2914 C GLY A 377 20.155 19.423 48.914 1.00 98.46 C
ANISOU 2914 C GLY A 377 10950 13835 12626 2027 -2165 -1512 C
ATOM 2915 O GLY A 377 20.996 20.195 48.446 1.00 94.28 O
ANISOU 2915 O GLY A 377 10299 13562 11960 2013 -2074 -1536 O
ATOM 2916 N HIS A 378 19.133 19.848 49.662 1.00 92.00 N
ANISOU 2916 N HIS A 378 10252 12872 11831 1884 -2166 -1336 N
ATOM 2917 CA HIS A 378 19.023 21.253 50.038 1.00 90.94 C
ANISOU 2917 CA HIS A 378 10131 12853 11570 1739 -2076 -1163 C
ATOM 2918 C HIS A 378 20.239 21.700 50.836 1.00 97.42 C
ANISOU 2918 C HIS A 378 10916 13763 12337 1736 -2080 -1076 C
ATOM 2919 O HIS A 378 20.755 22.805 50.631 1.00 98.92 O
ANISOU 2919 O HIS A 378 11050 14156 12379 1650 -2003 -1023 O
ATOM 2920 CB HIS A 378 17.754 21.484 50.857 1.00 84.04 C
ANISOU 2920 CB HIS A 378 9381 11766 10783 1613 -2038 -1022 C
ATOM 2921 CG HIS A 378 16.488 21.206 50.110 1.00 88.01 C
ANISOU 2921 CG HIS A 378 9857 12198 11384 1588 -2059 -1093 C
ATOM 2922 ND1 HIS A 378 16.219 21.748 48.873 1.00104.14 N
ANISOU 2922 ND1 HIS A 378 11832 14411 13327 1588 -2089 -1156 N
ATOM 2923 CD2 HIS A 378 15.418 20.440 50.427 1.00110.22 C
ANISOU 2923 CD2 HIS A 378 12706 14785 14387 1539 -2075 -1109 C
ATOM 2924 CE1 HIS A 378 15.037 21.328 48.460 1.00105.67 C
ANISOU 2924 CE1 HIS A 378 12000 14490 13660 1556 -2164 -1208 C
ATOM 2925 NE2 HIS A 378 14.527 20.537 49.386 1.00116.11 N
ANISOU 2925 NE2 HIS A 378 13359 15579 15176 1520 -2140 -1187 N
ATOM 2926 N ILE A 379 20.695 20.858 51.766 1.00100.13 N
ANISOU 2926 N ILE A 379 11310 13938 12799 1814 -2199 -1049 N
ATOM 2927 CA ILE A 379 21.859 21.193 52.582 1.00100.90 C
ANISOU 2927 CA ILE A 379 11365 14102 12869 1812 -2281 -962 C
ATOM 2928 C ILE A 379 23.066 21.468 51.694 1.00106.03 C
ANISOU 2928 C ILE A 379 11736 15053 13498 1895 -2245 -1101 C
ATOM 2929 O ILE A 379 23.800 22.442 51.896 1.00106.02 O
ANISOU 2929 O ILE A 379 11648 15236 13398 1785 -2213 -1031 O
ATOM 2930 CB ILE A 379 22.147 20.066 53.591 1.00 93.88 C
ANISOU 2930 CB ILE A 379 10598 12951 12122 1916 -2483 -916 C
ATOM 2931 CG1 ILE A 379 20.981 19.907 54.570 1.00 82.74 C
ANISOU 2931 CG1 ILE A 379 9504 11246 10688 1764 -2456 -766 C
ATOM 2932 CG2 ILE A 379 23.437 20.338 54.345 1.00 95.75 C
ANISOU 2932 CG2 ILE A 379 10756 13267 12358 1937 -2649 -838 C
ATOM 2933 CD1 ILE A 379 20.776 21.096 55.481 1.00 83.27 C
ANISOU 2933 CD1 ILE A 379 9734 11322 10582 1544 -2363 -586 C
ATOM 2934 N GLN A 380 23.282 20.613 50.690 1.00102.00 N
ANISOU 2934 N GLN A 380 11090 14589 13076 2067 -2223 -1317 N
ATOM 2935 CA GLN A 380 24.401 20.807 49.772 1.00100.38 C
ANISOU 2935 CA GLN A 380 10615 14672 12855 2136 -2114 -1490 C
ATOM 2936 C GLN A 380 24.289 22.136 49.035 1.00 99.82 C
ANISOU 2936 C GLN A 380 10546 14848 12532 1927 -1923 -1453 C
ATOM 2937 O GLN A 380 25.284 22.853 48.874 1.00 97.58 O
ANISOU 2937 O GLN A 380 10085 14802 12188 1848 -1830 -1466 O
ATOM 2938 CB GLN A 380 24.469 19.647 48.778 1.00100.48 C
ANISOU 2938 CB GLN A 380 10555 14652 12972 2342 -2075 -1755 C
ATOM 2939 CG GLN A 380 25.041 18.363 49.354 1.00101.76 C
ANISOU 2939 CG GLN A 380 10646 14602 13416 2598 -2257 -1834 C
ATOM 2940 CD GLN A 380 26.551 18.410 49.484 1.00 98.58 C
ANISOU 2940 CD GLN A 380 9898 14381 13175 2734 -2276 -1918 C
ATOM 2941 OE1 GLN A 380 27.203 19.307 48.949 1.00 92.62 O
ANISOU 2941 OE1 GLN A 380 8938 13939 12316 2622 -2092 -1968 O
ATOM 2942 NE2 GLN A 380 27.114 17.445 50.200 1.00 98.89 N
ANISOU 2942 NE2 GLN A 380 9870 14215 13489 2967 -2511 -1929 N
ATOM 2943 N TYR A 381 23.083 22.479 48.576 1.00 94.72 N
ANISOU 2943 N TYR A 381 10099 14136 11755 1828 -1877 -1402 N
ATOM 2944 CA TYR A 381 22.875 23.774 47.934 1.00 99.14 C
ANISOU 2944 CA TYR A 381 10726 14869 12074 1639 -1748 -1328 C
ATOM 2945 C TYR A 381 23.107 24.912 48.921 1.00 95.10 C
ANISOU 2945 C TYR A 381 10261 14368 11504 1474 -1747 -1116 C
ATOM 2946 O TYR A 381 23.670 25.953 48.561 1.00 96.47 O
ANISOU 2946 O TYR A 381 10410 14735 11511 1322 -1634 -1079 O
ATOM 2947 CB TYR A 381 21.462 23.839 47.348 1.00102.67 C
ANISOU 2947 CB TYR A 381 11359 15197 12454 1602 -1778 -1302 C
ATOM 2948 CG TYR A 381 21.286 24.787 46.177 1.00 97.39 C
ANISOU 2948 CG TYR A 381 10781 14698 11525 1474 -1691 -1299 C
ATOM 2949 CD1 TYR A 381 22.291 25.669 45.805 1.00 95.21 C
ANISOU 2949 CD1 TYR A 381 10460 14654 11062 1348 -1543 -1291 C
ATOM 2950 CD2 TYR A 381 20.105 24.798 45.443 1.00 87.63 C
ANISOU 2950 CD2 TYR A 381 9689 13376 10229 1458 -1780 -1296 C
ATOM 2951 CE1 TYR A 381 22.124 26.534 44.738 1.00100.74 C
ANISOU 2951 CE1 TYR A 381 11316 15476 11483 1204 -1469 -1266 C
ATOM 2952 CE2 TYR A 381 19.931 25.659 44.374 1.00 87.03 C
ANISOU 2952 CE2 TYR A 381 9754 13424 9890 1340 -1758 -1267 C
ATOM 2953 CZ TYR A 381 20.945 26.524 44.026 1.00 92.87 C
ANISOU 2953 CZ TYR A 381 10507 14373 10408 1210 -1594 -1246 C
ATOM 2954 OH TYR A 381 20.779 27.383 42.963 1.00 93.31 O
ANISOU 2954 OH TYR A 381 10771 14522 10162 1066 -1574 -1197 O
ATOM 2955 N ASP A 382 22.692 24.725 50.178 1.00 87.93 N
ANISOU 2955 N ASP A 382 9462 13239 10709 1477 -1858 -983 N
ATOM 2956 CA ASP A 382 22.892 25.758 51.190 1.00 93.51 C
ANISOU 2956 CA ASP A 382 10272 13923 11335 1308 -1858 -801 C
ATOM 2957 C ASP A 382 24.370 25.950 51.507 1.00100.42 C
ANISOU 2957 C ASP A 382 10956 14980 12219 1271 -1904 -819 C
ATOM 2958 O ASP A 382 24.827 27.084 51.695 1.00 96.66 O
ANISOU 2958 O ASP A 382 10503 14618 11607 1079 -1847 -729 O
ATOM 2959 CB ASP A 382 22.111 25.410 52.458 1.00 89.82 C
ANISOU 2959 CB ASP A 382 10010 13165 10953 1299 -1937 -678 C
ATOM 2960 CG ASP A 382 20.611 25.538 52.273 1.00 93.71 C
ANISOU 2960 CG ASP A 382 10645 13494 11468 1280 -1851 -644 C
ATOM 2961 OD1 ASP A 382 20.184 26.356 51.432 1.00 93.20 O
ANISOU 2961 OD1 ASP A 382 10578 13523 11312 1231 -1766 -640 O
ATOM 2962 OD2 ASP A 382 19.859 24.822 52.967 1.00 94.49 O1-
ANISOU 2962 OD2 ASP A 382 10854 13362 11687 1305 -1877 -617 O1-
ATOM 2963 N MET A 383 25.135 24.857 51.575 1.00101.67 N
ANISOU 2963 N MET A 383 10912 15155 12563 1453 -2022 -940 N
ATOM 2964 CA MET A 383 26.563 24.980 51.849 1.00 93.95 C
ANISOU 2964 CA MET A 383 9669 14360 11668 1444 -2096 -975 C
ATOM 2965 C MET A 383 27.300 25.611 50.673 1.00103.87 C
ANISOU 2965 C MET A 383 10692 15936 12836 1355 -1873 -1108 C
ATOM 2966 O MET A 383 28.231 26.400 50.869 1.00 99.42 O
ANISOU 2966 O MET A 383 9974 15556 12243 1188 -1851 -1076 O
ATOM 2967 CB MET A 383 27.162 23.610 52.182 1.00 91.01 C
ANISOU 2967 CB MET A 383 9117 13892 11569 1710 -2299 -1079 C
ATOM 2968 CG MET A 383 26.620 22.974 53.456 1.00 98.22 C
ANISOU 2968 CG MET A 383 10304 14474 12540 1758 -2542 -924 C
ATOM 2969 SD MET A 383 27.468 21.451 53.946 1.00 77.65 S
ANISOU 2969 SD MET A 383 7534 11711 10259 2073 -2857 -1003 S
ATOM 2970 CE MET A 383 27.290 20.446 52.473 1.00121.21 C
ANISOU 2970 CE MET A 383 12869 17268 15918 2326 -2669 -1295 C
ATOM 2971 N ALA A 384 26.880 25.294 49.445 1.00 98.22 N
ANISOU 2971 N ALA A 384 9980 15286 12055 1428 -1702 -1258 N
ATOM 2972 CA ALA A 384 27.658 25.678 48.271 1.00 92.26 C
ANISOU 2972 CA ALA A 384 9030 14825 11199 1347 -1457 -1418 C
ATOM 2973 C ALA A 384 27.653 27.184 48.033 1.00 88.29 C
ANISOU 2973 C ALA A 384 8672 14451 10423 1034 -1315 -1278 C
ATOM 2974 O ALA A 384 28.666 27.736 47.588 1.00 92.38 O
ANISOU 2974 O ALA A 384 8990 15220 10888 879 -1144 -1350 O
ATOM 2975 CB ALA A 384 27.141 24.946 47.034 1.00 89.79 C
ANISOU 2975 CB ALA A 384 8780 14515 10821 1477 -1326 -1612 C
ATOM 2976 N TYR A 385 26.541 27.869 48.304 1.00 82.95 N
ANISOU 2976 N TYR A 385 8331 13596 9590 934 -1366 -1089 N
ATOM 2977 CA TYR A 385 26.493 29.312 48.104 1.00 84.10 C
ANISOU 2977 CA TYR A 385 8660 13805 9490 659 -1254 -947 C
ATOM 2978 C TYR A 385 26.620 30.093 49.405 1.00 99.42 C
ANISOU 2978 C TYR A 385 10696 15635 11444 511 -1366 -761 C
ATOM 2979 O TYR A 385 26.327 31.293 49.421 1.00 97.25 O
ANISOU 2979 O TYR A 385 10654 15316 10980 305 -1302 -621 O
ATOM 2980 CB TYR A 385 25.211 29.733 47.368 1.00104.91 C
ANISOU 2980 CB TYR A 385 11611 16312 11937 644 -1228 -871 C
ATOM 2981 CG TYR A 385 23.875 29.354 47.996 1.00 98.97 C
ANISOU 2981 CG TYR A 385 11026 15272 11307 791 -1388 -779 C
ATOM 2982 CD1 TYR A 385 23.582 29.664 49.320 1.00 90.55 C
ANISOU 2982 CD1 TYR A 385 10054 14018 10331 760 -1474 -635 C
ATOM 2983 CD2 TYR A 385 22.878 28.760 47.235 1.00 95.32 C
ANISOU 2983 CD2 TYR A 385 10645 14723 10850 924 -1434 -843 C
ATOM 2984 CE1 TYR A 385 22.361 29.343 49.880 1.00 95.58 C
ANISOU 2984 CE1 TYR A 385 10830 14401 11084 863 -1550 -570 C
ATOM 2985 CE2 TYR A 385 21.648 28.441 47.787 1.00 98.97 C
ANISOU 2985 CE2 TYR A 385 11208 14936 11458 1026 -1552 -771 C
ATOM 2986 CZ TYR A 385 21.396 28.736 49.109 1.00 95.24 C
ANISOU 2986 CZ TYR A 385 10801 14292 11094 996 -1584 -639 C
ATOM 2987 OH TYR A 385 20.176 28.420 49.661 1.00 91.66 O
ANISOU 2987 OH TYR A 385 10433 13598 10796 1072 -1637 -588 O
ATOM 2988 N ALA A 386 27.032 29.444 50.496 1.00107.53 N
ANISOU 2988 N ALA A 386 11595 16590 12673 608 -1549 -756 N
ATOM 2989 CA ALA A 386 27.129 30.138 51.775 1.00 82.53 C
ANISOU 2989 CA ALA A 386 8585 13298 9473 447 -1675 -588 C
ATOM 2990 C ALA A 386 28.184 31.234 51.764 1.00 80.13 C
ANISOU 2990 C ALA A 386 8189 13193 9064 159 -1609 -557 C
ATOM 2991 O ALA A 386 28.072 32.189 52.541 1.00 80.21 O
ANISOU 2991 O ALA A 386 8440 13089 8948 -48 -1648 -412 O
ATOM 2992 CB ALA A 386 27.423 29.142 52.896 1.00 79.69 C
ANISOU 2992 CB ALA A 386 8148 12815 9316 597 -1928 -582 C
ATOM 2993 N ALA A 387 29.200 31.122 50.906 1.00 78.97 N
ANISOU 2993 N ALA A 387 7704 13333 8968 123 -1485 -706 N
ATOM 2994 CA ALA A 387 30.211 32.168 50.793 1.00 82.46 C
ANISOU 2994 CA ALA A 387 8028 13981 9320 -196 -1381 -691 C
ATOM 2995 C ALA A 387 29.700 33.402 50.063 1.00 84.16 C
ANISOU 2995 C ALA A 387 8575 14176 9226 -438 -1164 -593 C
ATOM 2996 O ALA A 387 30.351 34.450 50.123 1.00 90.71 O
ANISOU 2996 O ALA A 387 9431 15099 9938 -757 -1087 -534 O
ATOM 2997 CB ALA A 387 31.453 31.626 50.086 1.00 98.80 C
ANISOU 2997 CB ALA A 387 9595 16370 11575 -166 -1262 -907 C
ATOM 2998 N GLN A 388 28.564 33.302 49.375 1.00 94.79 N
ANISOU 2998 N GLN A 388 10178 15387 10450 -303 -1093 -570 N
ATOM 2999 CA GLN A 388 27.937 34.463 48.772 1.00 81.43 C
ANISOU 2999 CA GLN A 388 8853 13605 8483 -487 -967 -442 C
ATOM 3000 C GLN A 388 27.455 35.418 49.863 1.00 80.77 C
ANISOU 3000 C GLN A 388 9081 13265 8344 -613 -1070 -255 C
ATOM 3001 O GLN A 388 27.347 35.033 51.031 1.00 93.89 O
ANISOU 3001 O GLN A 388 10729 14796 10149 -525 -1233 -228 O
ATOM 3002 CB GLN A 388 26.763 34.030 47.894 1.00 80.14 C
ANISOU 3002 CB GLN A 388 8866 13329 8253 -276 -957 -457 C
ATOM 3003 CG GLN A 388 27.154 33.190 46.687 1.00 82.24 C
ANISOU 3003 CG GLN A 388 8931 13820 8497 -186 -824 -654 C
ATOM 3004 CD GLN A 388 27.759 34.017 45.569 1.00 98.05 C
ANISOU 3004 CD GLN A 388 11028 16014 10213 -471 -581 -669 C
ATOM 3005 OE1 GLN A 388 27.627 35.240 45.547 1.00 88.05 O
ANISOU 3005 OE1 GLN A 388 10051 14661 8742 -711 -548 -499 O
ATOM 3006 NE2 GLN A 388 28.428 33.351 44.633 1.00 97.19 N
ANISOU 3006 NE2 GLN A 388 10706 16146 10078 -457 -389 -879 N
ATOM 3007 N PRO A 389 27.172 36.675 49.514 1.00 87.32 N
ANISOU 3007 N PRO A 389 10232 13995 8949 -826 -973 -128 N
ATOM 3008 CA PRO A 389 26.585 37.601 50.492 1.00 91.78 C
ANISOU 3008 CA PRO A 389 11138 14268 9465 -913 -1037 25 C
ATOM 3009 C PRO A 389 25.289 37.056 51.074 1.00 89.55 C
ANISOU 3009 C PRO A 389 10976 13723 9325 -620 -1134 52 C
ATOM 3010 O PRO A 389 24.699 36.095 50.575 1.00101.48 O
ANISOU 3010 O PRO A 389 12356 15254 10947 -368 -1166 -21 O
ATOM 3011 CB PRO A 389 26.342 38.870 49.671 1.00 89.78 C
ANISOU 3011 CB PRO A 389 11218 13929 8967 -1112 -915 141 C
ATOM 3012 CG PRO A 389 27.401 38.825 48.628 1.00 94.39 C
ANISOU 3012 CG PRO A 389 11598 14833 9431 -1306 -765 55 C
ATOM 3013 CD PRO A 389 27.559 37.369 48.272 1.00 90.04 C
ANISOU 3013 CD PRO A 389 10665 14487 9058 -1044 -783 -124 C
ATOM 3014 N PHE A 390 24.834 37.697 52.154 1.00 87.77 N
ANISOU 3014 N PHE A 390 11017 13239 9094 -678 -1159 144 N
ATOM 3015 CA PHE A 390 23.679 37.179 52.880 1.00 88.33 C
ANISOU 3015 CA PHE A 390 11182 13064 9316 -444 -1196 151 C
ATOM 3016 C PHE A 390 22.401 37.276 52.054 1.00105.03 C
ANISOU 3016 C PHE A 390 13387 15035 11484 -241 -1156 180 C
ATOM 3017 O PHE A 390 21.582 36.350 52.062 1.00 98.77 O
ANISOU 3017 O PHE A 390 12477 14184 10868 -7 -1196 126 O
ATOM 3018 CB PHE A 390 23.524 37.911 54.215 1.00 87.36 C
ANISOU 3018 CB PHE A 390 11360 12691 9140 -584 -1176 219 C
ATOM 3019 CG PHE A 390 22.272 37.548 54.965 1.00 89.60 C
ANISOU 3019 CG PHE A 390 11781 12701 9561 -388 -1128 218 C
ATOM 3020 CD1 PHE A 390 22.208 36.384 55.713 1.00 92.60 C
ANISOU 3020 CD1 PHE A 390 12051 13078 10053 -281 -1202 165 C
ATOM 3021 CD2 PHE A 390 21.174 38.392 54.953 1.00 89.52 C
ANISOU 3021 CD2 PHE A 390 12014 12419 9582 -321 -997 267 C
ATOM 3022 CE1 PHE A 390 21.058 36.052 56.408 1.00 89.52 C
ANISOU 3022 CE1 PHE A 390 11795 12438 9779 -149 -1107 157 C
ATOM 3023 CE2 PHE A 390 20.026 38.070 55.650 1.00 90.08 C
ANISOU 3023 CE2 PHE A 390 12160 12249 9815 -157 -899 240 C
ATOM 3024 CZ PHE A 390 19.967 36.900 56.379 1.00 89.03 C
ANISOU 3024 CZ PHE A 390 11923 12135 9768 -93 -933 183 C
ATOM 3025 N LEU A 391 22.212 38.378 51.331 1.00106.20 N
ANISOU 3025 N LEU A 391 13748 15112 11491 -336 -1105 269 N
ATOM 3026 CA LEU A 391 21.017 38.536 50.510 1.00 95.73 C
ANISOU 3026 CA LEU A 391 12509 13636 10226 -138 -1139 314 C
ATOM 3027 C LEU A 391 21.070 37.734 49.215 1.00 95.50 C
ANISOU 3027 C LEU A 391 12291 13833 10161 -42 -1209 247 C
ATOM 3028 O LEU A 391 20.112 37.785 48.437 1.00 94.58 O
ANISOU 3028 O LEU A 391 12242 13613 10080 111 -1298 284 O
ATOM 3029 CB LEU A 391 20.785 40.016 50.192 1.00 96.74 C
ANISOU 3029 CB LEU A 391 12986 13559 10210 -259 -1107 453 C
ATOM 3030 CG LEU A 391 20.467 40.901 51.399 1.00 94.79 C
ANISOU 3030 CG LEU A 391 12993 13009 10012 -315 -1018 503 C
ATOM 3031 CD1 LEU A 391 20.455 42.375 51.010 1.00 97.58 C
ANISOU 3031 CD1 LEU A 391 13717 13156 10204 -461 -993 635 C
ATOM 3032 CD2 LEU A 391 19.147 40.486 52.038 1.00 94.29 C
ANISOU 3032 CD2 LEU A 391 12878 12712 10236 -34 -995 461 C
ATOM 3033 N LEU A 392 22.150 36.988 48.967 1.00 83.07 N
ANISOU 3033 N LEU A 392 10483 12551 8529 -120 -1181 137 N
ATOM 3034 CA LEU A 392 22.297 36.206 47.745 1.00 84.59 C
ANISOU 3034 CA LEU A 392 10526 12956 8660 -47 -1198 35 C
ATOM 3035 C LEU A 392 22.411 34.710 48.024 1.00 82.10 C
ANISOU 3035 C LEU A 392 9899 12749 8548 143 -1244 -125 C
ATOM 3036 O LEU A 392 22.878 33.958 47.163 1.00 82.61 O
ANISOU 3036 O LEU A 392 9802 13021 8565 179 -1217 -258 O
ATOM 3037 CB LEU A 392 23.509 36.690 46.947 1.00 87.00 C
ANISOU 3037 CB LEU A 392 10841 13509 8707 -314 -1063 15 C
ATOM 3038 CG LEU A 392 23.494 38.167 46.553 1.00 86.75 C
ANISOU 3038 CG LEU A 392 11174 13358 8431 -547 -1015 184 C
ATOM 3039 CD1 LEU A 392 24.710 38.514 45.709 1.00 91.51 C
ANISOU 3039 CD1 LEU A 392 11772 14226 8771 -852 -835 146 C
ATOM 3040 CD2 LEU A 392 22.208 38.511 45.820 1.00 88.00 C
ANISOU 3040 CD2 LEU A 392 11598 13292 8546 -390 -1158 294 C
ATOM 3041 N ARG A 393 21.991 34.261 49.208 1.00 79.61 N
ANISOU 3041 N ARG A 393 9532 12275 8442 256 -1298 -121 N
ATOM 3042 CA ARG A 393 22.043 32.844 49.571 1.00 96.88 C
ANISOU 3042 CA ARG A 393 11485 14503 10822 431 -1364 -246 C
ATOM 3043 C ARG A 393 20.656 32.232 49.391 1.00101.98 C
ANISOU 3043 C ARG A 393 12149 14969 11629 636 -1439 -262 C
ATOM 3044 O ARG A 393 19.886 32.061 50.336 1.00 98.91 O
ANISOU 3044 O ARG A 393 11806 14369 11404 703 -1448 -222 O
ATOM 3045 CB ARG A 393 22.549 32.665 50.997 1.00 83.91 C
ANISOU 3045 CB ARG A 393 9816 12795 9272 383 -1395 -222 C
ATOM 3046 CG ARG A 393 23.973 33.115 51.211 1.00 79.95 C
ANISOU 3046 CG ARG A 393 9220 12489 8668 180 -1377 -226 C
ATOM 3047 CD ARG A 393 24.317 33.091 52.682 1.00 92.58 C
ANISOU 3047 CD ARG A 393 10880 13975 10322 109 -1471 -170 C
ATOM 3048 NE ARG A 393 25.613 33.699 52.950 1.00 92.93 N
ANISOU 3048 NE ARG A 393 10840 14188 10280 -126 -1494 -158 N
ATOM 3049 CZ ARG A 393 26.021 34.079 54.152 1.00 95.82 C
ANISOU 3049 CZ ARG A 393 11333 14462 10611 -282 -1594 -86 C
ATOM 3050 NH1 ARG A 393 25.253 33.930 55.219 1.00 98.34 N
ANISOU 3050 NH1 ARG A 393 11908 14517 10940 -236 -1641 -21 N
ATOM 3051 NH2 ARG A 393 27.226 34.623 54.286 1.00 98.58 N
ANISOU 3051 NH2 ARG A 393 11561 14990 10905 -517 -1640 -87 N
ATOM 3052 N ASN A 394 20.352 31.884 48.146 1.00 86.44 N
ANISOU 3052 N ASN A 394 10148 13091 9606 708 -1486 -332 N
ATOM 3053 CA ASN A 394 19.085 31.259 47.799 1.00 89.19 C
ANISOU 3053 CA ASN A 394 10477 13300 10112 878 -1599 -364 C
ATOM 3054 C ASN A 394 19.217 30.703 46.392 1.00 95.44 C
ANISOU 3054 C ASN A 394 11240 14257 10767 910 -1658 -484 C
ATOM 3055 O ASN A 394 20.067 31.146 45.614 1.00 98.67 O
ANISOU 3055 O ASN A 394 11712 14853 10925 782 -1578 -503 O
ATOM 3056 CB ASN A 394 17.923 32.255 47.884 1.00 96.81 C
ANISOU 3056 CB ASN A 394 11597 14046 11140 895 -1639 -223 C
ATOM 3057 CG ASN A 394 16.647 31.620 48.398 1.00117.38 C
ANISOU 3057 CG ASN A 394 14098 16448 14053 1046 -1694 -247 C
ATOM 3058 OD1 ASN A 394 16.297 30.501 48.020 1.00117.10 O
ANISOU 3058 OD1 ASN A 394 13926 16440 14128 1140 -1784 -360 O
ATOM 3059 ND2 ASN A 394 15.946 32.333 49.272 1.00115.57 N
ANISOU 3059 ND2 ASN A 394 13936 16004 13970 1054 -1614 -156 N
ATOM 3060 N GLY A 395 18.372 29.722 46.077 1.00 92.14 N
ANISOU 3060 N GLY A 395 10746 13763 10502 1052 -1781 -576 N
ATOM 3061 CA GLY A 395 18.337 29.150 44.744 1.00100.85 C
ANISOU 3061 CA GLY A 395 11877 14982 11458 1076 -1860 -705 C
ATOM 3062 C GLY A 395 18.170 30.212 43.677 1.00106.70 C
ANISOU 3062 C GLY A 395 12855 15770 11918 963 -1918 -603 C
ATOM 3063 O GLY A 395 17.637 31.289 43.961 1.00102.36 O
ANISOU 3063 O GLY A 395 12423 15082 11387 932 -1967 -424 O
ATOM 3064 N ALA A 396 18.627 29.922 42.455 1.00103.94 N
ANISOU 3064 N ALA A 396 12610 15587 11294 898 -1905 -720 N
ATOM 3065 CA ALA A 396 18.651 30.925 41.392 1.00 85.59 C
ANISOU 3065 CA ALA A 396 10589 13313 8620 743 -1944 -614 C
ATOM 3066 C ALA A 396 17.308 31.637 41.265 1.00 90.57 C
ANISOU 3066 C ALA A 396 11365 13714 9334 806 -2228 -427 C
ATOM 3067 O ALA A 396 17.248 32.870 41.191 1.00 93.99 O
ANISOU 3067 O ALA A 396 12007 14067 9637 716 -2254 -237 O
ATOM 3068 CB ALA A 396 19.045 30.272 40.070 1.00 87.46 C
ANISOU 3068 CB ALA A 396 10958 13720 8553 676 -1913 -797 C
ATOM 3069 N ASN A 397 16.218 30.874 41.248 1.00100.51 N
ANISOU 3069 N ASN A 397 12500 14848 10842 961 -2451 -482 N
ATOM 3070 CA ASN A 397 14.872 31.428 41.305 1.00 97.55 C
ANISOU 3070 CA ASN A 397 12135 14247 10684 1065 -2725 -331 C
ATOM 3071 C ASN A 397 14.044 30.547 42.238 1.00 99.26 C
ANISOU 3071 C ASN A 397 12027 14334 11354 1219 -2752 -411 C
ATOM 3072 O ASN A 397 14.580 29.690 42.948 1.00106.30 O
ANISOU 3072 O ASN A 397 12755 15282 12351 1233 -2559 -536 O
ATOM 3073 CB ASN A 397 14.278 31.564 39.895 1.00 87.04 C
ANISOU 3073 CB ASN A 397 11054 12904 9114 1032 -3053 -296 C
ATOM 3074 CG ASN A 397 14.233 30.248 39.139 1.00 91.23 C
ANISOU 3074 CG ASN A 397 11564 13543 9558 1028 -3145 -517 C
ATOM 3075 OD1 ASN A 397 13.971 29.189 39.709 1.00 95.45 O
ANISOU 3075 OD1 ASN A 397 11829 14051 10388 1126 -3110 -662 O
ATOM 3076 ND2 ASN A 397 14.488 30.314 37.838 1.00 92.84 N
ANISOU 3076 ND2 ASN A 397 12102 13845 9329 895 -3256 -545 N
ATOM 3077 N GLU A 398 12.723 30.753 42.239 1.00 83.06 N
ANISOU 3077 N GLU A 398 9878 12095 9585 1328 -2996 -336 N
ATOM 3078 CA GLU A 398 11.879 30.057 43.204 1.00 92.54 C
ANISOU 3078 CA GLU A 398 10767 13159 11236 1434 -2962 -401 C
ATOM 3079 C GLU A 398 11.821 28.554 42.960 1.00 94.42 C
ANISOU 3079 C GLU A 398 10883 13460 11531 1430 -3011 -602 C
ATOM 3080 O GLU A 398 11.391 27.816 43.852 1.00109.70 O
ANISOU 3080 O GLU A 398 12602 15296 13784 1468 -2912 -671 O
ATOM 3081 CB GLU A 398 10.454 30.617 43.195 1.00 83.25 C
ANISOU 3081 CB GLU A 398 9448 11778 10405 1552 -3200 -301 C
ATOM 3082 CG GLU A 398 9.714 30.455 41.879 1.00 99.25 C
ANISOU 3082 CG GLU A 398 11524 13806 12380 1571 -3630 -304 C
ATOM 3083 CD GLU A 398 8.362 31.146 41.883 1.00103.13 C
ANISOU 3083 CD GLU A 398 11830 14090 13265 1717 -3902 -189 C
ATOM 3084 OE1 GLU A 398 8.123 31.986 42.777 1.00101.45 O
ANISOU 3084 OE1 GLU A 398 11524 13730 13292 1807 -3720 -94 O
ATOM 3085 OE2 GLU A 398 7.533 30.837 41.001 1.00 93.94 O1-
ANISOU 3085 OE2 GLU A 398 10606 12900 12188 1746 -4305 -206 O1-
ATOM 3086 N GLY A 399 12.244 28.085 41.789 1.00 86.12 N
ANISOU 3086 N GLY A 399 10006 12549 10166 1368 -3140 -704 N
ATOM 3087 CA GLY A 399 12.129 26.678 41.464 1.00 92.95 C
ANISOU 3087 CA GLY A 399 10800 13436 11082 1367 -3208 -912 C
ATOM 3088 C GLY A 399 13.431 25.903 41.494 1.00 98.38 C
ANISOU 3088 C GLY A 399 11548 14269 11562 1340 -2954 -1076 C
ATOM 3089 O GLY A 399 13.421 24.671 41.405 1.00101.44 O
ANISOU 3089 O GLY A 399 11880 14632 12029 1364 -2968 -1260 O
ATOM 3090 N PHE A 400 14.559 26.604 41.629 1.00 99.16 N
ANISOU 3090 N PHE A 400 11746 14504 11426 1293 -2726 -1019 N
ATOM 3091 CA PHE A 400 15.856 25.938 41.543 1.00 93.55 C
ANISOU 3091 CA PHE A 400 11043 13952 10549 1281 -2495 -1188 C
ATOM 3092 C PHE A 400 16.109 25.038 42.746 1.00 87.52 C
ANISOU 3092 C PHE A 400 10063 13101 10090 1380 -2368 -1256 C
ATOM 3093 O PHE A 400 16.566 23.899 42.594 1.00 83.23 O
ANISOU 3093 O PHE A 400 9480 12572 9570 1442 -2322 -1451 O
ATOM 3094 CB PHE A 400 16.975 26.968 41.406 1.00 92.76 C
ANISOU 3094 CB PHE A 400 11055 14027 10162 1174 -2287 -1107 C
ATOM 3095 CG PHE A 400 17.488 27.121 40.006 1.00 96.95 C
ANISOU 3095 CG PHE A 400 11836 14727 10273 1053 -2261 -1198 C
ATOM 3096 CD1 PHE A 400 16.668 27.604 38.999 1.00 91.94 C
ANISOU 3096 CD1 PHE A 400 11459 14044 9428 981 -2519 -1115 C
ATOM 3097 CD2 PHE A 400 18.787 26.760 39.692 1.00 98.87 C
ANISOU 3097 CD2 PHE A 400 12062 15171 10334 1006 -1980 -1374 C
ATOM 3098 CE1 PHE A 400 17.143 27.738 37.706 1.00 93.26 C
ANISOU 3098 CE1 PHE A 400 11938 14354 9143 832 -2485 -1194 C
ATOM 3099 CE2 PHE A 400 19.267 26.891 38.403 1.00110.68 C
ANISOU 3099 CE2 PHE A 400 13815 16822 11415 863 -1888 -1480 C
ATOM 3100 CZ PHE A 400 18.444 27.379 37.409 1.00104.89 C
ANISOU 3100 CZ PHE A 400 13413 16033 10408 760 -2136 -1385 C
ATOM 3101 N HIS A 401 15.828 25.535 43.953 1.00 85.77 N
ANISOU 3101 N HIS A 401 9739 12763 10087 1394 -2309 -1098 N
ATOM 3102 CA HIS A 401 16.187 24.798 45.162 1.00 88.13 C
ANISOU 3102 CA HIS A 401 9911 12970 10603 1454 -2193 -1126 C
ATOM 3103 C HIS A 401 15.479 23.450 45.219 1.00 88.52 C
ANISOU 3103 C HIS A 401 9898 12860 10876 1516 -2300 -1258 C
ATOM 3104 O HIS A 401 16.107 22.414 45.469 1.00 79.15 O
ANISOU 3104 O HIS A 401 8685 11646 9743 1586 -2254 -1386 O
ATOM 3105 CB HIS A 401 15.859 25.632 46.398 1.00 92.63 C
ANISOU 3105 CB HIS A 401 10458 13420 11316 1419 -2108 -937 C
ATOM 3106 CG HIS A 401 16.952 25.646 47.419 1.00101.46 C
ANISOU 3106 CG HIS A 401 11563 14572 12415 1406 -1960 -904 C
ATOM 3107 ND1 HIS A 401 17.512 24.493 47.925 1.00101.37 N
ANISOU 3107 ND1 HIS A 401 11491 14519 12506 1479 -1954 -1005 N
ATOM 3108 CD2 HIS A 401 17.595 26.673 48.023 1.00 94.29 C
ANISOU 3108 CD2 HIS A 401 10707 13719 11401 1323 -1851 -778 C
ATOM 3109 CE1 HIS A 401 18.450 24.809 48.799 1.00 88.25 C
ANISOU 3109 CE1 HIS A 401 9827 12896 10808 1450 -1878 -934 C
ATOM 3110 NE2 HIS A 401 18.521 26.126 48.877 1.00 89.54 N
ANISOU 3110 NE2 HIS A 401 10056 13126 10839 1340 -1807 -804 N
ATOM 3111 N GLU A 402 14.167 23.444 44.982 1.00 92.05 N
ANISOU 3111 N GLU A 402 10312 13184 11480 1491 -2459 -1230 N
ATOM 3112 CA GLU A 402 13.401 22.204 45.018 1.00 83.80 C
ANISOU 3112 CA GLU A 402 9204 11975 10660 1501 -2565 -1354 C
ATOM 3113 C GLU A 402 13.745 21.269 43.867 1.00 77.75 C
ANISOU 3113 C GLU A 402 8538 11274 9731 1522 -2673 -1572 C
ATOM 3114 O GLU A 402 13.499 20.062 43.974 1.00 76.49 O
ANISOU 3114 O GLU A 402 8371 10969 9725 1538 -2720 -1708 O
ATOM 3115 CB GLU A 402 11.908 22.527 45.021 1.00 99.30 C
ANISOU 3115 CB GLU A 402 11045 13812 12872 1450 -2712 -1278 C
ATOM 3116 CG GLU A 402 11.068 21.533 45.776 1.00120.62 C
ANISOU 3116 CG GLU A 402 13623 16298 15908 1408 -2697 -1328 C
ATOM 3117 CD GLU A 402 11.550 21.346 47.192 1.00126.66 C
ANISOU 3117 CD GLU A 402 14414 16956 16755 1405 -2448 -1255 C
ATOM 3118 OE1 GLU A 402 11.482 22.301 47.994 1.00128.17 O
ANISOU 3118 OE1 GLU A 402 14585 17133 16981 1389 -2296 -1107 O
ATOM 3119 OE2 GLU A 402 12.003 20.232 47.491 1.00126.28 O1-
ANISOU 3119 OE2 GLU A 402 14442 16817 16722 1417 -2423 -1349 O1-
ATOM 3120 N ALA A 403 14.310 21.790 42.776 1.00 83.10 N
ANISOU 3120 N ALA A 403 9346 12145 10083 1505 -2692 -1616 N
ATOM 3121 CA ALA A 403 14.747 20.928 41.682 1.00 85.66 C
ANISOU 3121 CA ALA A 403 9811 12534 10204 1514 -2730 -1854 C
ATOM 3122 C ALA A 403 16.022 20.172 42.038 1.00 88.35 C
ANISOU 3122 C ALA A 403 10120 12908 10542 1626 -2507 -2003 C
ATOM 3123 O ALA A 403 16.161 18.992 41.698 1.00 87.65 O
ANISOU 3123 O ALA A 403 10083 12730 10491 1689 -2524 -2220 O
ATOM 3124 CB ALA A 403 14.952 21.756 40.412 1.00 94.49 C
ANISOU 3124 CB ALA A 403 11130 13841 10931 1426 -2784 -1853 C
ATOM 3125 N VAL A 404 16.963 20.840 42.713 1.00102.35 N
ANISOU 3125 N VAL A 404 11804 14793 12290 1658 -2319 -1895 N
ATOM 3126 CA VAL A 404 18.176 20.169 43.180 1.00 98.98 C
ANISOU 3126 CA VAL A 404 11282 14390 11937 1787 -2157 -2014 C
ATOM 3127 C VAL A 404 17.821 19.025 44.119 1.00 94.38 C
ANISOU 3127 C VAL A 404 10655 13538 11667 1882 -2238 -2035 C
ATOM 3128 O VAL A 404 18.350 17.913 44.004 1.00 99.22 O
ANISOU 3128 O VAL A 404 11272 14064 12362 2014 -2221 -2229 O
ATOM 3129 CB VAL A 404 19.118 21.179 43.862 1.00 79.68 C
ANISOU 3129 CB VAL A 404 8728 12101 9446 1766 -2003 -1860 C
ATOM 3130 CG1 VAL A 404 20.225 20.453 44.610 1.00 92.59 C
ANISOU 3130 CG1 VAL A 404 10210 13714 11257 1916 -1923 -1942 C
ATOM 3131 CG2 VAL A 404 19.706 22.118 42.834 1.00 82.91 C
ANISOU 3131 CG2 VAL A 404 9206 12770 9527 1656 -1875 -1883 C
ATOM 3132 N GLY A 405 16.917 19.284 45.066 1.00 87.14 N
ANISOU 3132 N GLY A 405 9716 12465 10929 1812 -2309 -1842 N
ATOM 3133 CA GLY A 405 16.513 18.250 46.001 1.00 94.56 C
ANISOU 3133 CA GLY A 405 10667 13130 12130 1847 -2363 -1837 C
ATOM 3134 C GLY A 405 15.906 17.030 45.336 1.00101.63 C
ANISOU 3134 C GLY A 405 11647 13860 13108 1855 -2485 -2035 C
ATOM 3135 O GLY A 405 16.095 15.907 45.810 1.00106.71 O
ANISOU 3135 O GLY A 405 12347 14288 13911 1935 -2509 -2115 O
ATOM 3136 N GLU A 406 15.187 17.225 44.228 1.00 97.79 N
ANISOU 3136 N GLU A 406 11202 13450 12505 1765 -2594 -2114 N
ATOM 3137 CA GLU A 406 14.472 16.115 43.604 1.00101.95 C
ANISOU 3137 CA GLU A 406 11825 13804 13106 1724 -2747 -2301 C
ATOM 3138 C GLU A 406 15.421 15.156 42.895 1.00107.50 C
ANISOU 3138 C GLU A 406 12653 14499 13694 1861 -2695 -2573 C
ATOM 3139 O GLU A 406 15.309 13.934 43.053 1.00110.77 O
ANISOU 3139 O GLU A 406 13155 14666 14268 1907 -2747 -2712 O
ATOM 3140 CB GLU A 406 13.420 16.646 42.630 1.00113.30 C
ANISOU 3140 CB GLU A 406 13277 15324 14447 1578 -2938 -2297 C
ATOM 3141 CG GLU A 406 12.173 17.185 43.303 1.00124.08 C
ANISOU 3141 CG GLU A 406 14478 16600 16066 1459 -3025 -2097 C
ATOM 3142 CD GLU A 406 11.352 16.095 43.965 1.00129.23 C
ANISOU 3142 CD GLU A 406 15090 16973 17038 1376 -3069 -2138 C
ATOM 3143 OE1 GLU A 406 11.480 14.919 43.560 1.00112.70 O
ANISOU 3143 OE1 GLU A 406 13134 14743 14944 1381 -3136 -2338 O
ATOM 3144 OE2 GLU A 406 10.582 16.413 44.895 1.00148.95 O1-
ANISOU 3144 OE2 GLU A 406 17436 19374 19786 1292 -3011 -1981 O1-
ATOM 3145 N ILE A 407 16.361 15.685 42.106 1.00 96.17 N
ANISOU 3145 N ILE A 407 11238 13314 11988 1921 -2567 -2665 N
ATOM 3146 CA ILE A 407 17.239 14.840 41.305 1.00 97.16 C
ANISOU 3146 CA ILE A 407 11469 13449 12000 2050 -2461 -2967 C
ATOM 3147 C ILE A 407 18.058 13.878 42.151 1.00102.62 C
ANISOU 3147 C ILE A 407 12087 13951 12950 2267 -2383 -3042 C
ATOM 3148 O ILE A 407 18.638 12.931 41.611 1.00106.82 O
ANISOU 3148 O ILE A 407 12702 14396 13489 2412 -2315 -3318 O
ATOM 3149 CB ILE A 407 18.179 15.699 40.430 1.00 97.74 C
ANISOU 3149 CB ILE A 407 11548 13846 11744 2046 -2261 -3038 C
ATOM 3150 CG1 ILE A 407 19.156 16.495 41.296 1.00 96.81 C
ANISOU 3150 CG1 ILE A 407 11204 13886 11695 2122 -2091 -2868 C
ATOM 3151 CG2 ILE A 407 17.375 16.644 39.565 1.00 97.47 C
ANISOU 3151 CG2 ILE A 407 11656 13957 11422 1834 -2388 -2941 C
ATOM 3152 CD1 ILE A 407 20.110 17.366 40.496 1.00106.35 C
ANISOU 3152 CD1 ILE A 407 12395 15411 12600 2074 -1858 -2931 C
ATOM 3153 N MET A 408 18.116 14.093 43.466 1.00105.67 N
ANISOU 3153 N MET A 408 12350 14253 13547 2297 -2403 -2805 N
ATOM 3154 CA MET A 408 18.842 13.177 44.337 1.00104.49 C
ANISOU 3154 CA MET A 408 12173 13886 13643 2501 -2405 -2834 C
ATOM 3155 C MET A 408 18.072 11.875 44.529 1.00112.71 C
ANISOU 3155 C MET A 408 13405 14548 14871 2491 -2554 -2917 C
ATOM 3156 O MET A 408 18.648 10.785 44.437 1.00108.70 O
ANISOU 3156 O MET A 408 12978 13836 14488 2686 -2562 -3114 O
ATOM 3157 CB MET A 408 19.127 13.850 45.679 1.00 97.36 C
ANISOU 3157 CB MET A 408 11150 13000 12843 2494 -2410 -2543 C
ATOM 3158 CG MET A 408 19.800 15.208 45.542 1.00102.39 C
ANISOU 3158 CG MET A 408 11616 13989 13296 2452 -2274 -2444 C
ATOM 3159 SD MET A 408 21.219 15.138 44.427 1.00 99.95 S
ANISOU 3159 SD MET A 408 11168 13938 12870 2625 -2074 -2738 S
ATOM 3160 CE MET A 408 21.513 16.878 44.121 1.00 90.39 C
ANISOU 3160 CE MET A 408 9851 13115 11380 2432 -1923 -2578 C
ATOM 3161 N SER A 409 16.767 11.965 44.793 1.00111.56 N
ANISOU 3161 N SER A 409 13326 14288 14774 2263 -2666 -2780 N
ATOM 3162 CA SER A 409 15.960 10.760 44.937 1.00108.91 C
ANISOU 3162 CA SER A 409 13172 13596 14614 2189 -2796 -2859 C
ATOM 3163 C SER A 409 15.583 10.139 43.597 1.00106.34 C
ANISOU 3163 C SER A 409 12988 13241 14175 2141 -2866 -3151 C
ATOM 3164 O SER A 409 15.019 9.040 43.582 1.00103.05 O
ANISOU 3164 O SER A 409 12748 12512 13896 2078 -2977 -3266 O
ATOM 3165 CB SER A 409 14.700 11.052 45.757 1.00 99.83 C
ANISOU 3165 CB SER A 409 11997 12334 13598 1936 -2852 -2624 C
ATOM 3166 OG SER A 409 14.041 12.218 45.300 1.00 97.65 O
ANISOU 3166 OG SER A 409 11569 12326 13207 1788 -2853 -2533 O
ATOM 3167 N LEU A 410 15.864 10.814 42.480 1.00110.35 N
ANISOU 3167 N LEU A 410 13469 14049 14410 2138 -2808 -3271 N
ATOM 3168 CA LEU A 410 15.851 10.135 41.188 1.00107.80 C
ANISOU 3168 CA LEU A 410 13350 13693 13915 2133 -2839 -3595 C
ATOM 3169 C LEU A 410 16.959 9.093 41.126 1.00116.28 C
ANISOU 3169 C LEU A 410 14515 14593 15074 2409 -2708 -3850 C
ATOM 3170 O LEU A 410 16.710 7.912 40.857 1.00119.09 O
ANISOU 3170 O LEU A 410 15088 14642 15519 2428 -2787 -4063 O
ATOM 3171 CB LEU A 410 16.008 11.147 40.049 1.00111.75 C
ANISOU 3171 CB LEU A 410 13859 14551 14050 2053 -2781 -3648 C
ATOM 3172 CG LEU A 410 14.808 11.990 39.611 1.00103.15 C
ANISOU 3172 CG LEU A 410 12768 13591 12834 1792 -2992 -3492 C
ATOM 3173 CD1 LEU A 410 15.195 12.881 38.442 1.00102.35 C
ANISOU 3173 CD1 LEU A 410 12768 13800 12318 1738 -2931 -3556 C
ATOM 3174 CD2 LEU A 410 13.635 11.102 39.230 1.00108.67 C
ANISOU 3174 CD2 LEU A 410 13618 14045 13626 1611 -3255 -3610 C
ATOM 3175 N SER A 411 18.196 9.518 41.389 1.00112.79 N
ANISOU 3175 N SER A 411 13891 14330 14635 2631 -2514 -3837 N
ATOM 3176 CA SER A 411 19.330 8.604 41.328 1.00110.61 C
ANISOU 3176 CA SER A 411 13621 13906 14500 2942 -2385 -4090 C
ATOM 3177 C SER A 411 19.250 7.560 42.434 1.00111.11 C
ANISOU 3177 C SER A 411 13760 13546 14912 3071 -2544 -4006 C
ATOM 3178 O SER A 411 19.491 6.369 42.199 1.00113.30 O
ANISOU 3178 O SER A 411 14215 13509 15324 3239 -2561 -4253 O
ATOM 3179 CB SER A 411 20.635 9.393 41.427 1.00102.40 C
ANISOU 3179 CB SER A 411 12291 13180 13436 3123 -2162 -4072 C
ATOM 3180 OG SER A 411 20.745 10.332 40.371 1.00101.86 O
ANISOU 3180 OG SER A 411 12211 13478 13013 2976 -1989 -4150 O
ATOM 3181 N ALA A 412 18.893 7.988 43.646 1.00104.73 N
ANISOU 3181 N ALA A 412 12865 12696 14232 2979 -2655 -3659 N
ATOM 3182 CA ALA A 412 18.970 7.107 44.805 1.00 98.99 C
ANISOU 3182 CA ALA A 412 12246 11576 13789 3092 -2798 -3535 C
ATOM 3183 C ALA A 412 17.972 5.961 44.739 1.00114.76 C
ANISOU 3183 C ALA A 412 14557 13163 15883 2948 -2941 -3622 C
ATOM 3184 O ALA A 412 18.174 4.940 45.406 1.00114.42 O
ANISOU 3184 O ALA A 412 14695 12720 16058 3081 -3050 -3614 O
ATOM 3185 CB ALA A 412 18.755 7.913 46.087 1.00 96.48 C
ANISOU 3185 CB ALA A 412 11825 11322 13512 2966 -2852 -3149 C
ATOM 3186 N ALA A 413 16.912 6.093 43.945 1.00128.27 N
ANISOU 3186 N ALA A 413 16346 14947 17443 2670 -2970 -3703 N
ATOM 3187 CA ALA A 413 15.844 5.104 43.922 1.00119.77 C
ANISOU 3187 CA ALA A 413 15531 13505 16470 2457 -3119 -3766 C
ATOM 3188 C ALA A 413 15.947 4.119 42.766 1.00125.40 C
ANISOU 3188 C ALA A 413 16485 14040 17120 2526 -3134 -4159 C
ATOM 3189 O ALA A 413 15.204 3.132 42.752 1.00129.70 O
ANISOU 3189 O ALA A 413 17286 14221 17774 2369 -3267 -4246 O
ATOM 3190 CB ALA A 413 14.480 5.800 43.869 1.00113.82 C
ANISOU 3190 CB ALA A 413 14686 12904 15656 2078 -3194 -3603 C
ATOM 3191 N THR A 414 16.835 4.357 41.803 1.00123.07 N
ANISOU 3191 N THR A 414 16137 13981 16644 2729 -2977 -4409 N
ATOM 3192 CA THR A 414 16.956 3.457 40.669 1.00128.08 C
ANISOU 3192 CA THR A 414 17042 14448 17177 2786 -2946 -4816 C
ATOM 3193 C THR A 414 17.412 2.075 41.139 1.00133.45 C
ANISOU 3193 C THR A 414 17941 14618 18146 3034 -2986 -4958 C
ATOM 3194 O THR A 414 18.072 1.950 42.175 1.00134.77 O
ANISOU 3194 O THR A 414 17998 14652 18556 3269 -2997 -4779 O
ATOM 3195 CB THR A 414 17.948 4.011 39.647 1.00119.90 C
ANISOU 3195 CB THR A 414 15906 13766 15886 2964 -2691 -5059 C
ATOM 3196 OG1 THR A 414 19.217 4.224 40.277 1.00125.80 O
ANISOU 3196 OG1 THR A 414 16387 14597 16814 3311 -2527 -5002 O
ATOM 3197 CG2 THR A 414 17.444 5.325 39.071 1.00122.82 C
ANISOU 3197 CG2 THR A 414 16152 14584 15929 2696 -2687 -4922 C
ATOM 3198 N PRO A 415 17.058 1.015 40.404 1.00136.18 N
ANISOU 3198 N PRO A 415 18634 14641 18469 2979 -3041 -5273 N
ATOM 3199 CA PRO A 415 17.558 -0.317 40.782 1.00144.42 C
ANISOU 3199 CA PRO A 415 19924 15154 19795 3251 -3077 -5432 C
ATOM 3200 C PRO A 415 19.071 -0.409 40.749 1.00149.46 C
ANISOU 3200 C PRO A 415 20391 15831 20565 3752 -2872 -5605 C
ATOM 3201 O PRO A 415 19.665 -1.092 41.592 1.00146.02 O
ANISOU 3201 O PRO A 415 19984 15045 20454 4048 -2953 -5538 O
ATOM 3202 CB PRO A 415 16.905 -1.246 39.746 1.00149.93 C
ANISOU 3202 CB PRO A 415 21028 15574 20364 3064 -3137 -5792 C
ATOM 3203 CG PRO A 415 15.745 -0.476 39.206 1.00145.67 C
ANISOU 3203 CG PRO A 415 20444 15352 19552 2610 -3251 -5696 C
ATOM 3204 CD PRO A 415 16.161 0.960 39.238 1.00144.17 C
ANISOU 3204 CD PRO A 415 19860 15718 19201 2658 -3114 -5489 C
ATOM 3205 N LYS A 416 19.713 0.276 39.799 1.00158.78 N
ANISOU 3205 N LYS A 416 21390 17426 21513 3843 -2613 -5822 N
ATOM 3206 CA LYS A 416 21.169 0.245 39.707 1.00157.81 C
ANISOU 3206 CA LYS A 416 21024 17386 21550 4301 -2368 -6019 C
ATOM 3207 C LYS A 416 21.820 0.749 40.990 1.00143.15 C
ANISOU 3207 C LYS A 416 18806 15616 19968 4503 -2456 -5655 C
ATOM 3208 O LYS A 416 22.843 0.212 41.429 1.00143.76 O
ANISOU 3208 O LYS A 416 18754 15490 20380 4921 -2446 -5735 O
ATOM 3209 CB LYS A 416 21.631 1.073 38.507 1.00158.87 C
ANISOU 3209 CB LYS A 416 21022 18009 21334 4258 -2037 -6265 C
ATOM 3210 CG LYS A 416 23.115 1.403 38.507 1.00166.99 C
ANISOU 3210 CG LYS A 416 21652 19268 22527 4654 -1737 -6399 C
ATOM 3211 CD LYS A 416 23.477 2.333 37.361 1.00159.20 C
ANISOU 3211 CD LYS A 416 20564 18786 21141 4518 -1380 -6597 C
ATOM 3212 CE LYS A 416 24.820 3.003 37.602 1.00170.63 C
ANISOU 3212 CE LYS A 416 21503 20565 22764 4798 -1108 -6596 C
ATOM 3213 NZ LYS A 416 25.932 2.291 36.914 1.00180.87 N
ANISOU 3213 NZ LYS A 416 22724 21768 24231 5173 -737 -7093 N
ATOM 3214 N HIS A 417 21.234 1.773 41.614 1.00120.81 N
ANISOU 3214 N HIS A 417 15820 13070 17014 4216 -2565 -5260 N
ATOM 3215 CA HIS A 417 21.825 2.331 42.825 1.00126.10 C
ANISOU 3215 CA HIS A 417 16192 13837 17884 4358 -2656 -4916 C
ATOM 3216 C HIS A 417 21.534 1.469 44.049 1.00133.08 C
ANISOU 3216 C HIS A 417 17301 14215 19048 4408 -2954 -4678 C
ATOM 3217 O HIS A 417 22.428 1.236 44.870 1.00137.57 O
ANISOU 3217 O HIS A 417 17744 14635 19890 4727 -3063 -4570 O
ATOM 3218 CB HIS A 417 21.324 3.756 43.053 1.00120.26 C
ANISOU 3218 CB HIS A 417 15244 13553 16895 4036 -2635 -4601 C
ATOM 3219 CG HIS A 417 21.946 4.428 44.237 1.00117.37 C
ANISOU 3219 CG HIS A 417 14602 13316 16679 4143 -2714 -4269 C
ATOM 3220 ND1 HIS A 417 23.167 5.063 44.176 1.00122.04 N
ANISOU 3220 ND1 HIS A 417 14820 14226 17324 4377 -2559 -4318 N
ATOM 3221 CD2 HIS A 417 21.521 4.551 45.517 1.00120.67 C
ANISOU 3221 CD2 HIS A 417 15082 13578 17190 4022 -2928 -3895 C
ATOM 3222 CE1 HIS A 417 23.465 5.555 45.366 1.00124.24 C
ANISOU 3222 CE1 HIS A 417 14945 14539 17722 4397 -2718 -3982 C
ATOM 3223 NE2 HIS A 417 22.483 5.258 46.197 1.00124.40 N
ANISOU 3223 NE2 HIS A 417 15250 14270 17747 4186 -2934 -3722 N
ATOM 3224 N LEU A 418 20.292 0.994 44.193 1.00138.35 N
ANISOU 3224 N LEU A 418 18308 14608 19651 4078 -3101 -4587 N
ATOM 3225 CA LEU A 418 19.940 0.186 45.358 1.00141.40 C
ANISOU 3225 CA LEU A 418 18972 14498 20256 4053 -3353 -4345 C
ATOM 3226 C LEU A 418 20.741 -1.108 45.413 1.00140.17 C
ANISOU 3226 C LEU A 418 19022 13839 20398 4468 -3449 -4559 C
ATOM 3227 O LEU A 418 21.011 -1.624 46.504 1.00135.12 O
ANISOU 3227 O LEU A 418 18527 12832 19979 4612 -3675 -4329 O
ATOM 3228 CB LEU A 418 18.442 -0.121 45.355 1.00149.95 C
ANISOU 3228 CB LEU A 418 20354 15391 21230 3585 -3439 -4264 C
ATOM 3229 CG LEU A 418 17.492 1.056 45.585 1.00139.29 C
ANISOU 3229 CG LEU A 418 18812 14430 19681 3179 -3398 -3993 C
ATOM 3230 CD1 LEU A 418 16.056 0.641 45.327 1.00129.69 C
ANISOU 3230 CD1 LEU A 418 17822 13034 18418 2747 -3471 -4013 C
ATOM 3231 CD2 LEU A 418 17.645 1.590 47.000 1.00129.02 C
ANISOU 3231 CD2 LEU A 418 17425 13145 18453 3160 -3466 -3585 C
ATOM 3232 N LYS A 419 21.124 -1.649 44.256 1.00146.14 N
ANISOU 3232 N LYS A 419 19825 14544 21156 4666 -3286 -4999 N
ATOM 3233 CA LYS A 419 21.932 -2.862 44.240 1.00143.12 C
ANISOU 3233 CA LYS A 419 19614 13669 21096 5112 -3348 -5247 C
ATOM 3234 C LYS A 419 23.354 -2.588 44.708 1.00143.94 C
ANISOU 3234 C LYS A 419 19314 13899 21477 5598 -3347 -5214 C
ATOM 3235 O LYS A 419 23.989 -3.459 45.315 1.00141.70 O
ANISOU 3235 O LYS A 419 19135 13159 21547 5972 -3555 -5204 O
ATOM 3236 CB LYS A 419 21.936 -3.458 42.832 1.00144.96 C
ANISOU 3236 CB LYS A 419 20020 13829 21230 5172 -3123 -5765 C
ATOM 3237 CG LYS A 419 20.572 -3.963 42.379 1.00150.58 C
ANISOU 3237 CG LYS A 419 21174 14312 21727 4714 -3203 -5831 C
ATOM 3238 CD LYS A 419 20.663 -5.282 41.632 1.00157.41 C
ANISOU 3238 CD LYS A 419 22451 14666 22693 4885 -3171 -6272 C
ATOM 3239 CE LYS A 419 21.285 -5.097 40.256 1.00153.93 C
ANISOU 3239 CE LYS A 419 21900 14517 22070 5055 -2822 -6754 C
ATOM 3240 NZ LYS A 419 20.714 -6.052 39.266 1.00167.70 N
ANISOU 3240 NZ LYS A 419 24142 15907 23669 4902 -2787 -7161 N
ATOM 3241 N SER A 420 23.858 -1.382 44.454 1.00142.85 N
ANISOU 3241 N SER A 420 18716 14361 21202 5588 -3145 -5186 N
ATOM 3242 CA SER A 420 25.245 -1.056 44.749 1.00137.48 C
ANISOU 3242 CA SER A 420 17575 13866 20796 6018 -3111 -5207 C
ATOM 3243 C SER A 420 25.493 -0.771 46.223 1.00138.24 C
ANISOU 3243 C SER A 420 17585 13883 21058 6061 -3456 -4742 C
ATOM 3244 O SER A 420 26.652 -0.760 46.649 1.00152.70 O
ANISOU 3244 O SER A 420 19083 15730 23207 6459 -3555 -4735 O
ATOM 3245 CB SER A 420 25.673 0.149 43.917 1.00136.24 C
ANISOU 3245 CB SER A 420 16989 14372 20404 5929 -2750 -5346 C
ATOM 3246 OG SER A 420 24.997 1.316 44.350 1.00125.58 O
ANISOU 3246 OG SER A 420 15567 13393 18756 5513 -2793 -4977 O
ATOM 3247 N ILE A 421 24.443 -0.535 47.007 1.00127.06 N
ANISOU 3247 N ILE A 421 16454 12384 19437 5654 -3638 -4366 N
ATOM 3248 CA ILE A 421 24.578 -0.312 48.439 1.00119.20 C
ANISOU 3248 CA ILE A 421 15494 11269 18526 5636 -3958 -3923 C
ATOM 3249 C ILE A 421 24.065 -1.497 49.245 1.00133.13 C
ANISOU 3249 C ILE A 421 17809 12356 20419 5619 -4273 -3754 C
ATOM 3250 O ILE A 421 23.959 -1.409 50.472 1.00147.91 O
ANISOU 3250 O ILE A 421 19859 14058 22282 5514 -4543 -3361 O
ATOM 3251 CB ILE A 421 23.886 0.991 48.873 1.00113.29 C
ANISOU 3251 CB ILE A 421 14643 10958 17443 5183 -3885 -3600 C
ATOM 3252 CG1 ILE A 421 22.378 0.905 48.634 1.00118.59 C
ANISOU 3252 CG1 ILE A 421 15660 11545 17854 4708 -3800 -3554 C
ATOM 3253 CG2 ILE A 421 24.486 2.184 48.138 1.00119.47 C
ANISOU 3253 CG2 ILE A 421 14917 12374 18102 5204 -3601 -3736 C
ATOM 3254 CD1 ILE A 421 21.626 2.136 49.087 1.00131.97 C
ANISOU 3254 CD1 ILE A 421 17254 13616 19272 4291 -3722 -3251 C
ATOM 3255 N GLY A 422 23.737 -2.605 48.585 1.00142.70 N
ANISOU 3255 N GLY A 422 19341 13158 21721 5693 -4239 -4043 N
ATOM 3256 CA GLY A 422 23.384 -3.820 49.291 1.00143.60 C
ANISOU 3256 CA GLY A 422 20001 12571 21989 5714 -4538 -3911 C
ATOM 3257 C GLY A 422 21.987 -3.867 49.864 1.00153.92 C
ANISOU 3257 C GLY A 422 21738 13707 23039 5142 -4585 -3622 C
ATOM 3258 O GLY A 422 21.759 -4.565 50.857 1.00159.78 O
ANISOU 3258 O GLY A 422 22918 13938 23852 5082 -4859 -3354 O
ATOM 3259 N LEU A 423 21.038 -3.141 49.275 1.00150.00 N
ANISOU 3259 N LEU A 423 21127 13612 22253 4712 -4327 -3666 N
ATOM 3260 CA LEU A 423 19.643 -3.220 49.690 1.00145.63 C
ANISOU 3260 CA LEU A 423 20909 12910 21516 4161 -4326 -3455 C
ATOM 3261 C LEU A 423 18.760 -3.969 48.708 1.00163.29 C
ANISOU 3261 C LEU A 423 23395 14936 23712 3935 -4227 -3762 C
ATOM 3262 O LEU A 423 17.736 -4.520 49.115 1.00177.97 O
ANISOU 3262 O LEU A 423 25629 16452 25539 3550 -4291 -3631 O
ATOM 3263 CB LEU A 423 19.064 -1.817 49.908 1.00140.57 C
ANISOU 3263 CB LEU A 423 19954 12841 20617 3800 -4158 -3231 C
ATOM 3264 CG LEU A 423 19.441 -1.130 51.221 1.00150.59 C
ANISOU 3264 CG LEU A 423 21167 14206 21847 3793 -4280 -2823 C
ATOM 3265 CD1 LEU A 423 18.721 0.203 51.355 1.00147.10 C
ANISOU 3265 CD1 LEU A 423 20463 14273 21156 3412 -4075 -2647 C
ATOM 3266 CD2 LEU A 423 19.130 -2.035 52.405 1.00150.61 C
ANISOU 3266 CD2 LEU A 423 21712 13605 21908 3670 -4519 -2542 C
ATOM 3267 N LEU A 424 19.127 -4.006 47.432 1.00159.33 N
ANISOU 3267 N LEU A 424 22713 14626 23198 4134 -4064 -4173 N
ATOM 3268 CA LEU A 424 18.373 -4.724 46.414 1.00150.40 C
ANISOU 3268 CA LEU A 424 21848 13296 22001 3930 -3995 -4503 C
ATOM 3269 C LEU A 424 19.187 -5.928 45.963 1.00149.29 C
ANISOU 3269 C LEU A 424 21956 12669 22098 4378 -4047 -4846 C
ATOM 3270 O LEU A 424 20.378 -5.798 45.660 1.00140.34 O
ANISOU 3270 O LEU A 424 20547 11676 21101 4861 -3965 -5030 O
ATOM 3271 CB LEU A 424 18.043 -3.809 45.233 1.00144.89 C
ANISOU 3271 CB LEU A 424 20837 13182 21034 3749 -3766 -4720 C
ATOM 3272 CG LEU A 424 16.971 -4.302 44.261 1.00147.87 C
ANISOU 3272 CG LEU A 424 21475 13445 21265 3381 -3750 -4982 C
ATOM 3273 CD1 LEU A 424 15.698 -4.664 45.008 1.00148.63 C
ANISOU 3273 CD1 LEU A 424 21830 13247 21394 2895 -3901 -4718 C
ATOM 3274 CD2 LEU A 424 16.688 -3.242 43.212 1.00148.46 C
ANISOU 3274 CD2 LEU A 424 21244 14124 21042 3205 -3585 -5119 C
ATOM 3275 N SER A 425 18.544 -7.092 45.929 1.00163.80 N
ANISOU 3275 N SER A 425 24303 13926 24009 4213 -4168 -4942 N
ATOM 3276 CA SER A 425 19.258 -8.335 45.680 1.00171.36 C
ANISOU 3276 CA SER A 425 25580 14300 25230 4644 -4252 -5232 C
ATOM 3277 C SER A 425 19.930 -8.303 44.309 1.00176.28 C
ANISOU 3277 C SER A 425 25999 15158 25820 4954 -3991 -5749 C
ATOM 3278 O SER A 425 19.334 -7.827 43.334 1.00178.27 O
ANISOU 3278 O SER A 425 26170 15784 25780 4644 -3805 -5951 O
ATOM 3279 CB SER A 425 18.303 -9.528 45.763 1.00163.70 C
ANISOU 3279 CB SER A 425 25229 12679 24292 4316 -4401 -5267 C
ATOM 3280 OG SER A 425 17.498 -9.460 46.926 1.00155.78 O
ANISOU 3280 OG SER A 425 24416 11525 23250 3902 -4558 -4806 O
ATOM 3281 N PRO A 426 21.166 -8.798 44.195 1.00170.66 N
ANISOU 3281 N PRO A 426 25208 14232 25404 5560 -3968 -5979 N
ATOM 3282 CA PRO A 426 21.812 -8.880 42.874 1.00176.15 C
ANISOU 3282 CA PRO A 426 25760 15095 26073 5849 -3651 -6522 C
ATOM 3283 C PRO A 426 21.079 -9.779 41.891 1.00175.85 C
ANISOU 3283 C PRO A 426 26229 14700 25887 5616 -3580 -6916 C
ATOM 3284 O PRO A 426 21.480 -9.839 40.721 1.00172.94 O
ANISOU 3284 O PRO A 426 25800 14522 25385 5731 -3263 -7336 O
ATOM 3285 CB PRO A 426 23.206 -9.437 43.198 1.00164.73 C
ANISOU 3285 CB PRO A 426 24107 13466 25017 6451 -3633 -6540 C
ATOM 3286 CG PRO A 426 23.437 -9.070 44.629 1.00155.99 C
ANISOU 3286 CG PRO A 426 22856 12326 24088 6530 -3963 -6028 C
ATOM 3287 CD PRO A 426 22.089 -9.155 45.286 1.00153.05 C
ANISOU 3287 CD PRO A 426 22944 11664 23543 6018 -4221 -5740 C
ATOM 3288 N ASP A 427 20.030 -10.476 42.322 1.00177.76 N
ANISOU 3288 N ASP A 427 26954 14481 26104 5223 -3823 -6748 N
ATOM 3289 CA ASP A 427 19.251 -11.348 41.457 1.00180.63 C
ANISOU 3289 CA ASP A 427 27791 14534 26305 4898 -3778 -7050 C
ATOM 3290 C ASP A 427 17.957 -10.697 40.983 1.00186.01 C
ANISOU 3290 C ASP A 427 28489 15567 26620 4255 -3800 -7023 C
ATOM 3291 O ASP A 427 17.077 -11.393 40.468 1.00179.97 O
ANISOU 3291 O ASP A 427 28153 14488 25741 3883 -3881 -7215 O
ATOM 3292 CB ASP A 427 18.954 -12.665 42.174 1.00175.18 C
ANISOU 3292 CB ASP A 427 27597 13139 25825 4818 -3985 -6851 C
ATOM 3293 CG ASP A 427 20.140 -13.608 42.168 1.00187.27 C
ANISOU 3293 CG ASP A 427 29162 14344 27646 5368 -3880 -6960 C
ATOM 3294 OD1 ASP A 427 20.979 -13.502 41.247 1.00189.80 O
ANISOU 3294 OD1 ASP A 427 29237 14914 27962 5705 -3571 -7326 O
ATOM 3295 OD2 ASP A 427 20.239 -14.451 43.084 1.00198.83 O1-
ANISOU 3295 OD2 ASP A 427 30902 15303 29341 5453 -4096 -6680 O1-
ATOM 3296 N PHE A 428 17.820 -9.386 41.154 1.00192.46 N
ANISOU 3296 N PHE A 428 28818 17054 27253 4088 -3732 -6748 N
ATOM 3297 CA PHE A 428 16.714 -8.626 40.588 1.00196.71 C
ANISOU 3297 CA PHE A 428 29252 18043 27447 3529 -3724 -6703 C
ATOM 3298 C PHE A 428 17.201 -7.943 39.319 1.00204.23 C
ANISOU 3298 C PHE A 428 29988 19504 28106 3647 -3460 -7051 C
ATOM 3299 O PHE A 428 18.248 -7.287 39.326 1.00200.61 O
ANISOU 3299 O PHE A 428 29153 19391 27679 4032 -3260 -7056 O
ATOM 3300 CB PHE A 428 16.188 -7.591 41.587 1.00182.69 C
ANISOU 3300 CB PHE A 428 27114 16646 25652 3258 -3811 -6178 C
ATOM 3301 CG PHE A 428 14.958 -6.857 41.119 1.00193.23 C
ANISOU 3301 CG PHE A 428 28319 18380 26718 2697 -3851 -6101 C
ATOM 3302 CD1 PHE A 428 15.061 -5.760 40.276 1.00189.39 C
ANISOU 3302 CD1 PHE A 428 27501 18512 25945 2670 -3710 -6191 C
ATOM 3303 CD2 PHE A 428 13.699 -7.258 41.533 1.00199.80 C
ANISOU 3303 CD2 PHE A 428 29353 18959 27604 2191 -4038 -5933 C
ATOM 3304 CE1 PHE A 428 13.933 -5.090 39.846 1.00191.76 C
ANISOU 3304 CE1 PHE A 428 27682 19148 26031 2190 -3805 -6108 C
ATOM 3305 CE2 PHE A 428 12.567 -6.588 41.110 1.00196.95 C
ANISOU 3305 CE2 PHE A 428 28806 18960 27065 1704 -4104 -5870 C
ATOM 3306 CZ PHE A 428 12.684 -5.502 40.267 1.00194.93 C
ANISOU 3306 CZ PHE A 428 28225 19300 26538 1723 -4013 -5952 C
ATOM 3307 N GLN A 429 16.450 -8.102 38.233 1.00207.77 N
ANISOU 3307 N GLN A 429 30694 19991 28259 3290 -3466 -7341 N
ATOM 3308 CA GLN A 429 16.815 -7.522 36.949 1.00207.78 C
ANISOU 3308 CA GLN A 429 30616 20430 27902 3328 -3225 -7685 C
ATOM 3309 C GLN A 429 15.605 -6.838 36.333 1.00196.30 C
ANISOU 3309 C GLN A 429 29156 19342 26085 2750 -3383 -7607 C
ATOM 3310 O GLN A 429 14.494 -7.377 36.363 1.00182.87 O
ANISOU 3310 O GLN A 429 27724 17365 24395 2329 -3647 -7573 O
ATOM 3311 CB GLN A 429 17.367 -8.586 35.995 1.00202.51 C
ANISOU 3311 CB GLN A 429 30389 19356 27199 3573 -3051 -8258 C
ATOM 3312 CG GLN A 429 18.222 -8.021 34.874 1.00205.08 C
ANISOU 3312 CG GLN A 429 30593 20104 27224 3789 -2672 -8625 C
ATOM 3313 CD GLN A 429 19.534 -7.450 35.376 1.00199.13 C
ANISOU 3313 CD GLN A 429 29332 19618 26710 4314 -2409 -8530 C
ATOM 3314 OE1 GLN A 429 19.696 -6.234 35.480 1.00185.23 O
ANISOU 3314 OE1 GLN A 429 27138 18439 24803 4253 -2326 -8278 O
ATOM 3315 NE2 GLN A 429 20.478 -8.328 35.694 1.00188.50 N
ANISOU 3315 NE2 GLN A 429 28031 17832 25759 4835 -2298 -8731 N
ATOM 3316 N GLU A 430 15.829 -5.652 35.771 1.00186.78 N
ANISOU 3316 N GLU A 430 27641 18747 24578 2727 -3235 -7577 N
ATOM 3317 CA GLU A 430 14.734 -4.855 35.231 1.00178.01 C
ANISOU 3317 CA GLU A 430 26472 18017 23147 2228 -3429 -7452 C
ATOM 3318 C GLU A 430 14.174 -5.509 33.976 1.00189.53 C
ANISOU 3318 C GLU A 430 28431 19292 24289 1939 -3531 -7874 C
ATOM 3319 O GLU A 430 14.875 -5.639 32.967 1.00199.54 O
ANISOU 3319 O GLU A 430 29930 20611 25274 2111 -3285 -8278 O
ATOM 3320 CB GLU A 430 15.200 -3.435 34.915 1.00183.97 C
ANISOU 3320 CB GLU A 430 26838 19424 23640 2300 -3250 -7316 C
ATOM 3321 CG GLU A 430 15.868 -2.702 36.065 1.00180.45 C
ANISOU 3321 CG GLU A 430 25908 19195 23460 2586 -3134 -6936 C
ATOM 3322 CD GLU A 430 17.348 -3.010 36.166 1.00182.38 C
ANISOU 3322 CD GLU A 430 26068 19358 23870 3130 -2814 -7139 C
ATOM 3323 OE1 GLU A 430 18.053 -2.862 35.146 1.00180.50 O
ANISOU 3323 OE1 GLU A 430 25893 19314 23375 3275 -2530 -7490 O
ATOM 3324 OE2 GLU A 430 17.806 -3.401 37.261 1.00185.18 O1-
ANISOU 3324 OE2 GLU A 430 26295 19450 24614 3405 -2848 -6954 O1-
ATOM 3325 N ASP A 431 12.917 -5.924 34.043 1.00198.20 N
ANISOU 3325 N ASP A 431 29700 20176 25433 1479 -3881 -7794 N
ATOM 3326 CA ASP A 431 12.148 -6.310 32.873 1.00197.31 C
ANISOU 3326 CA ASP A 431 30002 19981 24984 1083 -4088 -8116 C
ATOM 3327 C ASP A 431 11.312 -5.122 32.411 1.00180.47 C
ANISOU 3327 C ASP A 431 27610 18390 22571 712 -4322 -7897 C
ATOM 3328 O ASP A 431 11.068 -4.179 33.167 1.00171.98 O
ANISOU 3328 O ASP A 431 26046 17643 21654 696 -4366 -7474 O
ATOM 3329 CB ASP A 431 11.258 -7.514 33.187 1.00192.17 C
ANISOU 3329 CB ASP A 431 29685 18749 24581 771 -4365 -8177 C
ATOM 3330 CG ASP A 431 10.212 -7.203 34.235 1.00182.58 C
ANISOU 3330 CG ASP A 431 28108 17578 23685 440 -4621 -7709 C
ATOM 3331 OD1 ASP A 431 9.161 -6.645 33.874 1.00177.36 O
ANISOU 3331 OD1 ASP A 431 27288 17196 22905 6 -4904 -7595 O
ATOM 3332 OD2 ASP A 431 10.444 -7.506 35.424 1.00178.34 O1-
ANISOU 3332 OD2 ASP A 431 27448 16793 23522 615 -4539 -7457 O1-
ATOM 3333 N ASN A 432 10.873 -5.171 31.152 1.00165.00 N
ANISOU 3333 N ASN A 432 18469 15568 28654 3085 -2078 -6878 N
ATOM 3334 CA ASN A 432 10.152 -4.028 30.602 1.00153.20 C
ANISOU 3334 CA ASN A 432 17042 14571 26596 2887 -1879 -6971 C
ATOM 3335 C ASN A 432 8.801 -3.794 31.271 1.00154.79 C
ANISOU 3335 C ASN A 432 17513 14468 26831 2613 -1920 -6543 C
ATOM 3336 O ASN A 432 8.200 -2.738 31.047 1.00152.16 O
ANISOU 3336 O ASN A 432 17271 14632 25910 2386 -1759 -6378 O
ATOM 3337 CB ASN A 432 9.959 -4.193 29.092 1.00155.61 C
ANISOU 3337 CB ASN A 432 17167 15312 26647 2840 -1764 -7616 C
ATOM 3338 CG ASN A 432 9.074 -5.371 28.737 1.00165.45 C
ANISOU 3338 CG ASN A 432 18422 16150 28290 2726 -1899 -7796 C
ATOM 3339 OD1 ASN A 432 8.963 -6.333 29.496 1.00159.79 O
ANISOU 3339 OD1 ASN A 432 17780 14809 28125 2752 -2087 -7538 O
ATOM 3340 ND2 ASN A 432 8.433 -5.297 27.576 1.00165.92 N
ANISOU 3340 ND2 ASN A 432 18406 16577 28058 2590 -1808 -8223 N
ATOM 3341 N GLU A 433 8.317 -4.730 32.092 1.00153.03 N
ANISOU 3341 N GLU A 433 17420 13605 27118 2542 -2106 -6188 N
ATOM 3342 CA GLU A 433 7.000 -4.571 32.704 1.00140.55 C
ANISOU 3342 CA GLU A 433 16071 11769 25564 2241 -2127 -5773 C
ATOM 3343 C GLU A 433 7.069 -3.745 33.987 1.00130.82 C
ANISOU 3343 C GLU A 433 15031 10644 24032 2135 -2092 -4994 C
ATOM 3344 O GLU A 433 6.273 -2.819 34.175 1.00116.43 O
ANISOU 3344 O GLU A 433 13338 9168 21733 1879 -1959 -4680 O
ATOM 3345 CB GLU A 433 6.373 -5.941 32.970 1.00132.63 C
ANISOU 3345 CB GLU A 433 15114 10149 25129 2137 -2303 -5676 C
ATOM 3346 CG GLU A 433 5.889 -6.648 31.712 1.00143.32 C
ANISOU 3346 CG GLU A 433 16312 11590 26554 2082 -2295 -6273 C
ATOM 3347 CD GLU A 433 4.940 -7.792 32.010 1.00152.57 C
ANISOU 3347 CD GLU A 433 17562 12193 28216 1890 -2440 -6119 C
ATOM 3348 OE1 GLU A 433 4.689 -8.063 33.203 1.00154.21 O
ANISOU 3348 OE1 GLU A 433 17948 11949 28694 1792 -2539 -5529 O
ATOM 3349 OE2 GLU A 433 4.451 -8.425 31.050 1.00159.55 O1-
ANISOU 3349 OE2 GLU A 433 18322 13100 29198 1830 -2454 -6581 O1-
ATOM 3350 N THR A 434 8.005 -4.064 34.889 1.00152.49 N
ANISOU 3350 N THR A 434 17789 13099 27051 2336 -2223 -4687 N
ATOM 3351 CA THR A 434 8.183 -3.217 36.066 1.00144.12 C
ANISOU 3351 CA THR A 434 16894 12219 25647 2250 -2189 -4001 C
ATOM 3352 C THR A 434 8.649 -1.822 35.676 1.00130.82 C
ANISOU 3352 C THR A 434 15151 11296 23258 2243 -1975 -4050 C
ATOM 3353 O THR A 434 8.378 -0.853 36.394 1.00118.88 O
ANISOU 3353 O THR A 434 13791 10059 21317 2072 -1885 -3562 O
ATOM 3354 CB THR A 434 9.177 -3.846 37.046 1.00141.81 C
ANISOU 3354 CB THR A 434 16606 11501 25774 2489 -2398 -3695 C
ATOM 3355 OG1 THR A 434 10.354 -4.265 36.344 1.00145.38 O
ANISOU 3355 OG1 THR A 434 16803 11971 26464 2838 -2453 -4235 O
ATOM 3356 CG2 THR A 434 8.550 -5.036 37.756 1.00127.46 C
ANISOU 3356 CG2 THR A 434 14931 8917 24580 2409 -2613 -3397 C
ATOM 3357 N GLU A 435 9.344 -1.706 34.543 1.00150.96 N
ANISOU 3357 N GLU A 435 17479 14193 25685 2418 -1888 -4641 N
ATOM 3358 CA GLU A 435 9.771 -0.402 34.048 1.00154.36 C
ANISOU 3358 CA GLU A 435 17848 15348 25453 2382 -1678 -4707 C
ATOM 3359 C GLU A 435 8.576 0.500 33.763 1.00142.49 C
ANISOU 3359 C GLU A 435 16490 14190 23460 2071 -1530 -4563 C
ATOM 3360 O GLU A 435 8.618 1.706 34.035 1.00131.73 O
ANISOU 3360 O GLU A 435 15209 13260 21581 1956 -1404 -4253 O
ATOM 3361 CB GLU A 435 10.627 -0.592 32.795 1.00166.50 C
ANISOU 3361 CB GLU A 435 19108 17182 26974 2598 -1605 -5406 C
ATOM 3362 CG GLU A 435 11.064 0.681 32.101 1.00177.14 C
ANISOU 3362 CG GLU A 435 20372 19288 27643 2537 -1378 -5524 C
ATOM 3363 CD GLU A 435 11.474 0.428 30.656 1.00188.19 C
ANISOU 3363 CD GLU A 435 21520 21018 28964 2658 -1274 -6263 C
ATOM 3364 OE1 GLU A 435 10.789 -0.361 29.967 1.00175.68 O
ANISOU 3364 OE1 GLU A 435 19904 19222 27623 2641 -1325 -6668 O
ATOM 3365 OE2 GLU A 435 12.478 1.019 30.207 1.00188.87 O1-
ANISOU 3365 OE2 GLU A 435 21432 21593 28735 2755 -1137 -6450 O1-
ATOM 3366 N ILE A 436 7.492 -0.070 33.237 1.00128.01 N
ANISOU 3366 N ILE A 436 14682 12150 21805 1934 -1560 -4787 N
ATOM 3367 CA ILE A 436 6.319 0.731 32.903 1.00123.74 C
ANISOU 3367 CA ILE A 436 14248 11933 20835 1660 -1443 -4689 C
ATOM 3368 C ILE A 436 5.527 1.084 34.157 1.00119.21 C
ANISOU 3368 C ILE A 436 13896 11176 20223 1452 -1460 -4030 C
ATOM 3369 O ILE A 436 5.058 2.219 34.303 1.00123.20 O
ANISOU 3369 O ILE A 436 14498 12071 20241 1289 -1338 -3763 O
ATOM 3370 CB ILE A 436 5.453 -0.010 31.867 1.00127.53 C
ANISOU 3370 CB ILE A 436 14646 12291 21517 1587 -1481 -5198 C
ATOM 3371 CG1 ILE A 436 6.166 -0.051 30.514 1.00131.38 C
ANISOU 3371 CG1 ILE A 436 14916 13156 21845 1756 -1412 -5867 C
ATOM 3372 CG2 ILE A 436 4.092 0.654 31.723 1.00126.53 C
ANISOU 3372 CG2 ILE A 436 14633 12385 21058 1298 -1412 -5026 C
ATOM 3373 CD1 ILE A 436 6.474 1.318 29.942 1.00129.77 C
ANISOU 3373 CD1 ILE A 436 14694 13686 20926 1703 -1224 -5853 C
ATOM 3374 N ASN A 437 5.364 0.126 35.076 1.00114.67 N
ANISOU 3374 N ASN A 437 13400 10012 20157 1451 -1610 -3758 N
ATOM 3375 CA ASN A 437 4.634 0.397 36.312 1.00110.04 C
ANISOU 3375 CA ASN A 437 13015 9274 19523 1242 -1613 -3129 C
ATOM 3376 C ASN A 437 5.183 1.628 37.013 1.00111.85 C
ANISOU 3376 C ASN A 437 13327 9914 19257 1246 -1513 -2733 C
ATOM 3377 O ASN A 437 4.432 2.528 37.406 1.00107.53 O
ANISOU 3377 O ASN A 437 12897 9624 18338 1046 -1406 -2428 O
ATOM 3378 CB ASN A 437 4.712 -0.812 37.247 1.00105.52 C
ANISOU 3378 CB ASN A 437 12512 8031 19551 1278 -1801 -2854 C
ATOM 3379 CG ASN A 437 3.791 -1.937 36.833 1.00119.30 C
ANISOU 3379 CG ASN A 437 14233 9305 21790 1160 -1895 -3093 C
ATOM 3380 OD1 ASN A 437 3.303 -1.976 35.706 1.00118.36 O
ANISOU 3380 OD1 ASN A 437 14004 9347 21621 1119 -1845 -3587 O
ATOM 3381 ND2 ASN A 437 3.568 -2.875 37.742 1.00134.21 N
ANISOU 3381 ND2 ASN A 437 16225 10605 24162 1099 -2043 -2740 N
ATOM 3382 N PHE A 438 6.503 1.683 37.168 1.00114.00 N
ANISOU 3382 N PHE A 438 13521 10253 19539 1479 -1554 -2762 N
ATOM 3383 CA PHE A 438 7.128 2.808 37.849 1.00114.95 C
ANISOU 3383 CA PHE A 438 13704 10742 19228 1486 -1479 -2413 C
ATOM 3384 C PHE A 438 6.884 4.104 37.098 1.00111.10 C
ANISOU 3384 C PHE A 438 13202 10844 18165 1377 -1290 -2552 C
ATOM 3385 O PHE A 438 6.482 5.113 37.688 1.00110.56 O
ANISOU 3385 O PHE A 438 13265 11016 17725 1224 -1205 -2195 O
ATOM 3386 CB PHE A 438 8.621 2.531 37.994 1.00112.75 C
ANISOU 3386 CB PHE A 438 13294 10431 19113 1767 -1570 -2504 C
ATOM 3387 CG PHE A 438 9.438 3.714 38.416 1.00112.66 C
ANISOU 3387 CG PHE A 438 13288 10866 18654 1791 -1488 -2287 C
ATOM 3388 CD1 PHE A 438 9.481 4.125 39.740 1.00119.41 C
ANISOU 3388 CD1 PHE A 438 14299 11684 19386 1719 -1535 -1739 C
ATOM 3389 CD2 PHE A 438 10.205 4.388 37.485 1.00115.21 C
ANISOU 3389 CD2 PHE A 438 13446 11649 18680 1878 -1366 -2643 C
ATOM 3390 CE1 PHE A 438 10.267 5.202 40.116 1.00128.59 C
ANISOU 3390 CE1 PHE A 438 15454 13245 20160 1738 -1473 -1578 C
ATOM 3391 CE2 PHE A 438 10.986 5.459 37.851 1.00109.94 C
ANISOU 3391 CE2 PHE A 438 12770 11368 17635 1881 -1295 -2454 C
ATOM 3392 CZ PHE A 438 11.020 5.869 39.167 1.00123.88 C
ANISOU 3392 CZ PHE A 438 14690 13072 19305 1815 -1356 -1935 C
ATOM 3393 N LEU A 439 7.114 4.093 35.784 1.00107.32 N
ANISOU 3393 N LEU A 439 12566 10607 17606 1453 -1229 -3072 N
ATOM 3394 CA LEU A 439 6.990 5.327 35.019 1.00103.20 C
ANISOU 3394 CA LEU A 439 12031 10652 16527 1356 -1067 -3180 C
ATOM 3395 C LEU A 439 5.562 5.850 35.039 1.00101.59 C
ANISOU 3395 C LEU A 439 11964 10522 16113 1112 -1014 -2999 C
ATOM 3396 O LEU A 439 5.349 7.059 34.899 1.00 96.67 O
ANISOU 3396 O LEU A 439 11402 10299 15031 1007 -906 -2866 O
ATOM 3397 CB LEU A 439 7.474 5.114 33.587 1.00104.10 C
ANISOU 3397 CB LEU A 439 11947 11023 16583 1469 -1014 -3774 C
ATOM 3398 CG LEU A 439 8.885 5.615 33.270 1.00 90.71 C
ANISOU 3398 CG LEU A 439 10104 9689 14674 1625 -936 -3922 C
ATOM 3399 CD1 LEU A 439 9.922 4.691 33.883 1.00111.11 C
ANISOU 3399 CD1 LEU A 439 12581 11916 17719 1864 -1063 -3946 C
ATOM 3400 CD2 LEU A 439 9.088 5.705 31.777 1.00111.92 C
ANISOU 3400 CD2 LEU A 439 12620 12776 17127 1653 -829 -4465 C
ATOM 3401 N LEU A 440 4.573 4.974 35.223 1.00105.68 N
ANISOU 3401 N LEU A 440 12523 10653 16979 1018 -1095 -2988 N
ATOM 3402 CA LEU A 440 3.201 5.455 35.333 1.00104.75 C
ANISOU 3402 CA LEU A 440 12505 10608 16687 788 -1046 -2806 C
ATOM 3403 C LEU A 440 2.987 6.196 36.643 1.00105.80 C
ANISOU 3403 C LEU A 440 12798 10761 16640 683 -1004 -2250 C
ATOM 3404 O LEU A 440 2.436 7.304 36.661 1.00105.86 O
ANISOU 3404 O LEU A 440 12870 11093 16258 566 -909 -2101 O
ATOM 3405 CB LEU A 440 2.214 4.294 35.229 1.00101.78 C
ANISOU 3405 CB LEU A 440 12108 9810 16754 689 -1138 -2939 C
ATOM 3406 CG LEU A 440 0.766 4.770 35.327 1.00 98.95 C
ANISOU 3406 CG LEU A 440 11813 9551 16234 449 -1086 -2775 C
ATOM 3407 CD1 LEU A 440 0.157 5.042 33.954 1.00 98.40 C
ANISOU 3407 CD1 LEU A 440 11639 9795 15954 404 -1065 -3207 C
ATOM 3408 CD2 LEU A 440 -0.032 3.753 36.097 1.00100.94 C
ANISOU 3408 CD2 LEU A 440 12108 9303 16942 308 -1162 -2575 C
ATOM 3409 N LYS A 441 3.386 5.570 37.757 1.00111.15 N
ANISOU 3409 N LYS A 441 13541 11086 17607 725 -1086 -1943 N
ATOM 3410 CA LYS A 441 3.326 6.213 39.064 1.00111.55 C
ANISOU 3410 CA LYS A 441 13738 11180 17468 639 -1052 -1431 C
ATOM 3411 C LYS A 441 3.973 7.582 38.992 1.00110.19 C
ANISOU 3411 C LYS A 441 13580 11476 16813 682 -955 -1384 C
ATOM 3412 O LYS A 441 3.456 8.567 39.527 1.00109.75 O
ANISOU 3412 O LYS A 441 13625 11634 16442 556 -872 -1123 O
ATOM 3413 CB LYS A 441 4.052 5.358 40.107 1.00122.31 C
ANISOU 3413 CB LYS A 441 15146 12161 19165 737 -1182 -1156 C
ATOM 3414 CG LYS A 441 4.284 6.068 41.422 1.00133.43 C
ANISOU 3414 CG LYS A 441 16690 13690 20317 684 -1160 -667 C
ATOM 3415 CD LYS A 441 3.236 5.731 42.468 1.00145.16 C
ANISOU 3415 CD LYS A 441 18306 14951 21896 475 -1156 -265 C
ATOM 3416 CE LYS A 441 3.456 4.352 43.069 1.00150.97 C
ANISOU 3416 CE LYS A 441 19072 15163 23125 512 -1322 -81 C
ATOM 3417 NZ LYS A 441 2.627 4.194 44.297 1.00156.78 N
ANISOU 3417 NZ LYS A 441 19953 15765 23852 290 -1300 411 N
ATOM 3418 N GLN A 442 5.131 7.647 38.334 1.00102.48 N
ANISOU 3418 N GLN A 442 12490 10655 15793 857 -964 -1650 N
ATOM 3419 CA GLN A 442 5.798 8.928 38.150 1.00 99.54 C
ANISOU 3419 CA GLN A 442 12115 10724 14983 875 -869 -1628 C
ATOM 3420 C GLN A 442 4.979 9.842 37.253 1.00104.99 C
ANISOU 3420 C GLN A 442 12817 11748 15326 748 -764 -1767 C
ATOM 3421 O GLN A 442 4.874 11.046 37.515 1.00105.23 O
ANISOU 3421 O GLN A 442 12932 12049 15002 666 -689 -1565 O
ATOM 3422 CB GLN A 442 7.198 8.709 37.583 1.00100.75 C
ANISOU 3422 CB GLN A 442 12110 10984 15189 1073 -889 -1907 C
ATOM 3423 CG GLN A 442 8.109 7.920 38.511 1.00102.14 C
ANISOU 3423 CG GLN A 442 12260 10851 15696 1229 -1020 -1746 C
ATOM 3424 CD GLN A 442 8.572 8.744 39.696 1.00 99.78 C
ANISOU 3424 CD GLN A 442 12066 10676 15169 1196 -1024 -1326 C
ATOM 3425 OE1 GLN A 442 8.103 8.560 40.819 1.00103.85 O
ANISOU 3425 OE1 GLN A 442 12721 10976 15760 1120 -1083 -953 O
ATOM 3426 NE2 GLN A 442 9.493 9.668 39.447 1.00 96.42 N
ANISOU 3426 NE2 GLN A 442 11568 10617 14448 1236 -956 -1390 N
ATOM 3427 N ALA A 443 4.375 9.290 36.200 1.00102.73 N
ANISOU 3427 N ALA A 443 12448 11437 15146 732 -773 -2112 N
ATOM 3428 CA ALA A 443 3.588 10.124 35.301 1.00 88.82 C
ANISOU 3428 CA ALA A 443 10693 10003 13052 622 -704 -2237 C
ATOM 3429 C ALA A 443 2.336 10.644 35.991 1.00 88.78 C
ANISOU 3429 C ALA A 443 10808 9958 12965 459 -685 -1931 C
ATOM 3430 O ALA A 443 1.936 11.794 35.781 1.00 85.82 O
ANISOU 3430 O ALA A 443 10488 9878 12244 386 -627 -1840 O
ATOM 3431 CB ALA A 443 3.220 9.344 34.039 1.00 84.23 C
ANISOU 3431 CB ALA A 443 9986 9418 12601 642 -739 -2697 C
ATOM 3432 N LEU A 444 1.711 9.814 36.830 1.00 83.16 N
ANISOU 3432 N LEU A 444 10134 8885 12579 397 -733 -1763 N
ATOM 3433 CA LEU A 444 0.510 10.246 37.537 1.00 79.45 C
ANISOU 3433 CA LEU A 444 9748 8398 12041 235 -694 -1489 C
ATOM 3434 C LEU A 444 0.799 11.412 38.471 1.00 87.62 C
ANISOU 3434 C LEU A 444 10897 9624 12771 218 -625 -1147 C
ATOM 3435 O LEU A 444 -0.080 12.248 38.710 1.00 90.55 O
ANISOU 3435 O LEU A 444 11316 10146 12942 116 -568 -1013 O
ATOM 3436 CB LEU A 444 -0.092 9.079 38.319 1.00 83.10 C
ANISOU 3436 CB LEU A 444 10222 8441 12909 149 -744 -1344 C
ATOM 3437 CG LEU A 444 -0.814 7.990 37.525 1.00 92.51 C
ANISOU 3437 CG LEU A 444 11309 9405 14437 97 -812 -1656 C
ATOM 3438 CD1 LEU A 444 -1.389 6.944 38.466 1.00 87.95 C
ANISOU 3438 CD1 LEU A 444 10764 8396 14257 -25 -853 -1423 C
ATOM 3439 CD2 LEU A 444 -1.908 8.604 36.668 1.00102.32 C
ANISOU 3439 CD2 LEU A 444 12492 10918 15468 -3 -779 -1842 C
ATOM 3440 N THR A 445 2.020 11.492 38.999 1.00 97.43 N
ANISOU 3440 N THR A 445 12169 10864 13986 323 -639 -1030 N
ATOM 3441 CA THR A 445 2.395 12.545 39.935 1.00 83.38 C
ANISOU 3441 CA THR A 445 10493 9254 11936 306 -590 -732 C
ATOM 3442 C THR A 445 3.051 13.726 39.229 1.00 86.15 C
ANISOU 3442 C THR A 445 10833 9955 11945 349 -544 -843 C
ATOM 3443 O THR A 445 2.671 14.880 39.453 1.00 86.34 O
ANISOU 3443 O THR A 445 10933 10173 11700 280 -489 -707 O
ATOM 3444 CB THR A 445 3.350 11.989 40.995 1.00 82.82 C
ANISOU 3444 CB THR A 445 10456 8992 12020 382 -654 -515 C
ATOM 3445 OG1 THR A 445 2.726 10.894 41.671 1.00 88.60 O
ANISOU 3445 OG1 THR A 445 11216 9382 13068 319 -704 -360 O
ATOM 3446 CG2 THR A 445 3.697 13.067 42.011 1.00 95.57 C
ANISOU 3446 CG2 THR A 445 12173 10796 13342 350 -613 -229 C
ATOM 3447 N ILE A 446 4.034 13.449 38.378 1.00 94.93 N
ANISOU 3447 N ILE A 446 11844 11147 13078 457 -562 -1091 N
ATOM 3448 CA ILE A 446 4.809 14.513 37.748 1.00 98.63 C
ANISOU 3448 CA ILE A 446 12294 11954 13227 474 -508 -1166 C
ATOM 3449 C ILE A 446 4.048 15.108 36.569 1.00 94.72 C
ANISOU 3449 C ILE A 446 11789 11687 12513 404 -472 -1338 C
ATOM 3450 O ILE A 446 3.831 16.323 36.497 1.00 93.77 O
ANISOU 3450 O ILE A 446 11746 11776 12107 335 -434 -1211 O
ATOM 3451 CB ILE A 446 6.190 13.983 37.324 1.00 89.29 C
ANISOU 3451 CB ILE A 446 10979 10809 12138 610 -524 -1369 C
ATOM 3452 CG1 ILE A 446 6.938 13.435 38.542 1.00 96.37 C
ANISOU 3452 CG1 ILE A 446 11885 11479 13253 694 -595 -1165 C
ATOM 3453 CG2 ILE A 446 6.996 15.072 36.641 1.00 83.05 C
ANISOU 3453 CG2 ILE A 446 10153 10393 11010 591 -449 -1437 C
ATOM 3454 CD1 ILE A 446 8.186 12.653 38.197 1.00100.16 C
ANISOU 3454 CD1 ILE A 446 12201 11921 13934 863 -642 -1388 C
ATOM 3455 N VAL A 447 3.630 14.259 35.627 1.00 91.07 N
ANISOU 3455 N VAL A 447 11233 11180 12191 425 -502 -1632 N
ATOM 3456 CA VAL A 447 2.908 14.749 34.456 1.00 86.27 C
ANISOU 3456 CA VAL A 447 10607 10813 11358 363 -494 -1804 C
ATOM 3457 C VAL A 447 1.505 15.198 34.840 1.00 88.50 C
ANISOU 3457 C VAL A 447 10970 11039 11616 261 -512 -1629 C
ATOM 3458 O VAL A 447 1.015 16.224 34.354 1.00 82.27 O
ANISOU 3458 O VAL A 447 10226 10477 10557 209 -508 -1581 O
ATOM 3459 CB VAL A 447 2.873 13.671 33.357 1.00 78.24 C
ANISOU 3459 CB VAL A 447 9453 9783 10491 413 -530 -2210 C
ATOM 3460 CG1 VAL A 447 2.045 14.144 32.176 1.00 80.36 C
ANISOU 3460 CG1 VAL A 447 9705 10323 10505 341 -546 -2377 C
ATOM 3461 CG2 VAL A 447 4.279 13.323 32.914 1.00 78.28 C
ANISOU 3461 CG2 VAL A 447 9348 9896 10498 528 -495 -2423 C
ATOM 3462 N GLY A 448 0.841 14.447 35.721 1.00 80.12 N
ANISOU 3462 N GLY A 448 9920 9678 10843 230 -535 -1522 N
ATOM 3463 CA GLY A 448 -0.542 14.752 36.051 1.00 75.13 C
ANISOU 3463 CA GLY A 448 9319 9010 10217 130 -538 -1400 C
ATOM 3464 C GLY A 448 -0.731 16.151 36.603 1.00 78.65 C
ANISOU 3464 C GLY A 448 9868 9622 10394 99 -493 -1146 C
ATOM 3465 O GLY A 448 -1.724 16.818 36.300 1.00 95.60 O
ANISOU 3465 O GLY A 448 12016 11884 12423 53 -507 -1138 O
ATOM 3466 N THR A 449 0.225 16.624 37.405 1.00 83.09 N
ANISOU 3466 N THR A 449 10508 10193 10869 132 -454 -955 N
ATOM 3467 CA THR A 449 0.087 17.921 38.059 1.00 88.98 C
ANISOU 3467 CA THR A 449 11355 11056 11398 102 -416 -732 C
ATOM 3468 C THR A 449 0.358 19.100 37.131 1.00 83.00 C
ANISOU 3468 C THR A 449 10628 10557 10351 108 -426 -776 C
ATOM 3469 O THR A 449 -0.124 20.204 37.408 1.00 79.03 O
ANISOU 3469 O THR A 449 10198 10127 9703 82 -422 -640 O
ATOM 3470 CB THR A 449 1.020 18.006 39.275 1.00 78.14 C
ANISOU 3470 CB THR A 449 10051 9609 10031 121 -386 -526 C
ATOM 3471 OG1 THR A 449 0.628 19.107 40.105 1.00 76.46 O
ANISOU 3471 OG1 THR A 449 9930 9464 9659 79 -349 -334 O
ATOM 3472 CG2 THR A 449 2.473 18.189 38.842 1.00 72.91 C
ANISOU 3472 CG2 THR A 449 9370 9066 9266 185 -392 -592 C
ATOM 3473 N LEU A 450 1.096 18.896 36.040 1.00 81.40 N
ANISOU 3473 N LEU A 450 10368 10494 10064 138 -439 -962 N
ATOM 3474 CA LEU A 450 1.499 20.021 35.196 1.00 80.23 C
ANISOU 3474 CA LEU A 450 10261 10607 9617 116 -440 -953 C
ATOM 3475 C LEU A 450 0.324 20.762 34.567 1.00 90.81 C
ANISOU 3475 C LEU A 450 11631 12050 10823 81 -500 -938 C
ATOM 3476 O LEU A 450 0.316 22.005 34.618 1.00 91.80 O
ANISOU 3476 O LEU A 450 11849 12262 10766 56 -512 -770 O
ATOM 3477 CB LEU A 450 2.496 19.530 34.141 1.00 77.88 C
ANISOU 3477 CB LEU A 450 9871 10479 9243 142 -421 -1177 C
ATOM 3478 CG LEU A 450 3.809 19.038 34.749 1.00 93.18 C
ANISOU 3478 CG LEU A 450 11763 12347 11295 196 -374 -1177 C
ATOM 3479 CD1 LEU A 450 4.744 18.514 33.678 1.00106.72 C
ANISOU 3479 CD1 LEU A 450 13348 14249 12950 236 -341 -1448 C
ATOM 3480 CD2 LEU A 450 4.469 20.158 35.544 1.00 88.44 C
ANISOU 3480 CD2 LEU A 450 11257 11792 10555 157 -343 -925 C
ATOM 3481 N PRO A 451 -0.675 20.104 33.963 1.00 99.27 N
ANISOU 3481 N PRO A 451 12623 13108 11986 81 -557 -1106 N
ATOM 3482 CA PRO A 451 -1.828 20.875 33.461 1.00 83.41 C
ANISOU 3482 CA PRO A 451 10629 11199 9862 64 -639 -1070 C
ATOM 3483 C PRO A 451 -2.594 21.571 34.570 1.00 87.08 C
ANISOU 3483 C PRO A 451 11150 11530 10406 66 -630 -865 C
ATOM 3484 O PRO A 451 -2.884 22.770 34.468 1.00 84.90 O
ANISOU 3484 O PRO A 451 10947 11332 9980 75 -676 -734 O
ATOM 3485 CB PRO A 451 -2.677 19.809 32.753 1.00 83.99 C
ANISOU 3485 CB PRO A 451 10575 11263 10073 58 -701 -1323 C
ATOM 3486 CG PRO A 451 -1.726 18.711 32.442 1.00 83.79 C
ANISOU 3486 CG PRO A 451 10485 11211 10139 76 -657 -1528 C
ATOM 3487 CD PRO A 451 -0.789 18.681 33.604 1.00 97.60 C
ANISOU 3487 CD PRO A 451 12294 12799 11991 98 -569 -1356 C
ATOM 3488 N PHE A 452 -2.938 20.832 35.628 1.00 90.98 N
ANISOU 3488 N PHE A 452 11608 11822 11138 55 -572 -839 N
ATOM 3489 CA PHE A 452 -3.554 21.422 36.813 1.00 84.13 C
ANISOU 3489 CA PHE A 452 10781 10860 10325 49 -529 -665 C
ATOM 3490 C PHE A 452 -2.802 22.669 37.261 1.00 77.10 C
ANISOU 3490 C PHE A 452 10018 10021 9254 68 -509 -494 C
ATOM 3491 O PHE A 452 -3.408 23.705 37.558 1.00 75.09 O
ANISOU 3491 O PHE A 452 9804 9781 8945 89 -531 -407 O
ATOM 3492 CB PHE A 452 -3.594 20.377 37.932 1.00 83.38 C
ANISOU 3492 CB PHE A 452 10653 10572 10455 10 -448 -620 C
ATOM 3493 CG PHE A 452 -4.168 20.878 39.227 1.00 75.94 C
ANISOU 3493 CG PHE A 452 9741 9576 9536 -12 -378 -454 C
ATOM 3494 CD1 PHE A 452 -3.371 21.533 40.153 1.00 71.93 C
ANISOU 3494 CD1 PHE A 452 9343 9072 8917 1 -327 -298 C
ATOM 3495 CD2 PHE A 452 -5.498 20.666 39.534 1.00 88.67 C
ANISOU 3495 CD2 PHE A 452 11255 11157 11277 -53 -356 -478 C
ATOM 3496 CE1 PHE A 452 -3.898 21.985 41.346 1.00 76.62 C
ANISOU 3496 CE1 PHE A 452 9958 9652 9504 -20 -255 -183 C
ATOM 3497 CE2 PHE A 452 -6.026 21.114 40.725 1.00 83.49 C
ANISOU 3497 CE2 PHE A 452 10606 10495 10621 -77 -268 -355 C
ATOM 3498 CZ PHE A 452 -5.228 21.771 41.633 1.00 74.36 C
ANISOU 3498 CZ PHE A 452 9570 9354 9331 -57 -216 -214 C
ATOM 3499 N THR A 453 -1.472 22.586 37.299 1.00 72.92 N
ANISOU 3499 N THR A 453 9538 9514 8653 64 -474 -465 N
ATOM 3500 CA THR A 453 -0.669 23.697 37.799 1.00 74.98 C
ANISOU 3500 CA THR A 453 9909 9810 8770 57 -454 -314 C
ATOM 3501 C THR A 453 -0.674 24.868 36.822 1.00 73.47 C
ANISOU 3501 C THR A 453 9777 9755 8383 49 -526 -279 C
ATOM 3502 O THR A 453 -0.858 26.022 37.226 1.00 72.12 O
ANISOU 3502 O THR A 453 9692 9555 8156 53 -549 -158 O
ATOM 3503 CB THR A 453 0.758 23.223 38.075 1.00 76.80 C
ANISOU 3503 CB THR A 453 10142 10044 8997 50 -407 -306 C
ATOM 3504 OG1 THR A 453 0.742 22.261 39.137 1.00 83.14 O
ANISOU 3504 OG1 THR A 453 10915 10692 9981 61 -366 -275 O
ATOM 3505 CG2 THR A 453 1.650 24.391 38.467 1.00 76.29 C
ANISOU 3505 CG2 THR A 453 10172 10035 8781 20 -397 -173 C
ATOM 3506 N TYR A 454 -0.471 24.592 35.531 1.00 77.58 N
ANISOU 3506 N TYR A 454 10256 10424 8796 36 -566 -385 N
ATOM 3507 CA TYR A 454 -0.476 25.670 34.547 1.00 81.36 C
ANISOU 3507 CA TYR A 454 10803 11050 9060 9 -644 -310 C
ATOM 3508 C TYR A 454 -1.843 26.336 34.474 1.00 81.51 C
ANISOU 3508 C TYR A 454 10837 11020 9113 58 -748 -260 C
ATOM 3509 O TYR A 454 -1.939 27.561 34.329 1.00 78.93 O
ANISOU 3509 O TYR A 454 10607 10691 8691 58 -820 -111 O
ATOM 3510 CB TYR A 454 -0.069 25.143 33.170 1.00 78.51 C
ANISOU 3510 CB TYR A 454 10381 10908 8540 -23 -661 -450 C
ATOM 3511 CG TYR A 454 -0.506 26.048 32.038 1.00 79.00 C
ANISOU 3511 CG TYR A 454 10500 11139 8378 -50 -774 -370 C
ATOM 3512 CD1 TYR A 454 -0.029 27.350 31.945 1.00 84.57 C
ANISOU 3512 CD1 TYR A 454 11332 11872 8927 -107 -801 -147 C
ATOM 3513 CD2 TYR A 454 -1.401 25.609 31.071 1.00 77.45 C
ANISOU 3513 CD2 TYR A 454 10233 11066 8129 -26 -870 -505 C
ATOM 3514 CE1 TYR A 454 -0.426 28.188 30.921 1.00 91.27 C
ANISOU 3514 CE1 TYR A 454 12250 12855 9575 -137 -925 -26 C
ATOM 3515 CE2 TYR A 454 -1.803 26.442 30.040 1.00 80.97 C
ANISOU 3515 CE2 TYR A 454 10736 11681 8348 -48 -999 -402 C
ATOM 3516 CZ TYR A 454 -1.312 27.729 29.971 1.00 90.04 C
ANISOU 3516 CZ TYR A 454 12025 12841 9344 -101 -1028 -144 C
ATOM 3517 OH TYR A 454 -1.712 28.558 28.949 1.00111.26 O
ANISOU 3517 OH TYR A 454 14786 15678 11811 -126 -1176 4 O
ATOM 3518 N MET A 455 -2.913 25.548 34.582 1.00 83.92 N
ANISOU 3518 N MET A 455 11035 11273 9579 99 -765 -386 N
ATOM 3519 CA MET A 455 -4.255 26.108 34.466 1.00 83.99 C
ANISOU 3519 CA MET A 455 11013 11261 9640 157 -870 -371 C
ATOM 3520 C MET A 455 -4.638 26.904 35.709 1.00 87.57 C
ANISOU 3520 C MET A 455 11510 11559 10205 201 -834 -263 C
ATOM 3521 O MET A 455 -5.268 27.963 35.600 1.00 93.17 O
ANISOU 3521 O MET A 455 12252 12244 10903 263 -932 -190 O
ATOM 3522 CB MET A 455 -5.266 24.992 34.203 1.00 73.26 C
ANISOU 3522 CB MET A 455 9496 9910 8430 166 -892 -558 C
ATOM 3523 CG MET A 455 -6.703 25.464 34.149 1.00 73.92 C
ANISOU 3523 CG MET A 455 9500 9987 8601 231 -998 -571 C
ATOM 3524 SD MET A 455 -7.577 25.119 35.684 1.00 81.31 S
ANISOU 3524 SD MET A 455 10336 10754 9806 239 -876 -588 S
ATOM 3525 CE MET A 455 -8.624 26.564 35.791 1.00 77.70 C
ANISOU 3525 CE MET A 455 9865 10292 9365 359 -991 -518 C
ATOM 3526 N LEU A 456 -4.270 26.416 36.899 1.00 73.00 N
ANISOU 3526 N LEU A 456 9660 9610 8465 176 -703 -259 N
ATOM 3527 CA LEU A 456 -4.597 27.145 38.122 1.00 72.42 C
ANISOU 3527 CA LEU A 456 9622 9432 8462 210 -654 -189 C
ATOM 3528 C LEU A 456 -3.906 28.503 38.157 1.00 78.42 C
ANISOU 3528 C LEU A 456 10525 10164 9105 219 -700 -65 C
ATOM 3529 O LEU A 456 -4.514 29.506 38.549 1.00 79.62 O
ANISOU 3529 O LEU A 456 10705 10243 9306 285 -746 -38 O
ATOM 3530 CB LEU A 456 -4.221 26.319 39.355 1.00 79.74 C
ANISOU 3530 CB LEU A 456 10531 10293 9472 164 -513 -184 C
ATOM 3531 CG LEU A 456 -4.605 26.901 40.723 1.00 66.46 C
ANISOU 3531 CG LEU A 456 8867 8554 7831 184 -437 -144 C
ATOM 3532 CD1 LEU A 456 -4.960 25.793 41.697 1.00 67.04 C
ANISOU 3532 CD1 LEU A 456 8860 8603 8011 130 -317 -153 C
ATOM 3533 CD2 LEU A 456 -3.484 27.759 41.301 1.00 68.21 C
ANISOU 3533 CD2 LEU A 456 9226 8753 7938 170 -424 -54 C
ATOM 3534 N GLU A 457 -2.632 28.556 37.762 1.00 79.02 N
ANISOU 3534 N GLU A 457 10682 10292 9048 149 -688 -1 N
ATOM 3535 CA GLU A 457 -1.932 29.836 37.753 1.00 81.00 C
ANISOU 3535 CA GLU A 457 11066 10507 9204 121 -733 127 C
ATOM 3536 C GLU A 457 -2.413 30.734 36.623 1.00 83.67 C
ANISOU 3536 C GLU A 457 11454 10868 9468 146 -884 208 C
ATOM 3537 O GLU A 457 -2.403 31.962 36.766 1.00 84.45 O
ANISOU 3537 O GLU A 457 11656 10856 9577 159 -957 315 O
ATOM 3538 CB GLU A 457 -0.421 29.622 37.656 1.00 77.35 C
ANISOU 3538 CB GLU A 457 10645 10118 8627 21 -669 171 C
ATOM 3539 CG GLU A 457 0.402 30.851 38.041 1.00 88.83 C
ANISOU 3539 CG GLU A 457 12220 11505 10027 -39 -685 293 C
ATOM 3540 CD GLU A 457 0.530 31.047 39.544 1.00 83.21 C
ANISOU 3540 CD GLU A 457 11529 10682 9406 -21 -622 269 C
ATOM 3541 OE1 GLU A 457 -0.488 30.947 40.261 1.00 76.29 O
ANISOU 3541 OE1 GLU A 457 10614 9737 8636 61 -606 201 O
ATOM 3542 OE2 GLU A 457 1.657 31.316 40.011 1.00 84.74 O1-
ANISOU 3542 OE2 GLU A 457 11766 10882 9551 -98 -588 309 O1-
ATOM 3543 N LYS A 458 -2.834 30.154 35.496 1.00 80.32 N
ANISOU 3543 N LYS A 458 10963 10580 8974 150 -946 159 N
ATOM 3544 CA LYS A 458 -3.352 30.983 34.413 1.00 76.62 C
ANISOU 3544 CA LYS A 458 10544 10156 8411 177 -1115 261 C
ATOM 3545 C LYS A 458 -4.677 31.626 34.799 1.00 79.11 C
ANISOU 3545 C LYS A 458 10825 10334 8900 313 -1221 251 C
ATOM 3546 O LYS A 458 -4.925 32.790 34.463 1.00 81.51 O
ANISOU 3546 O LYS A 458 11219 10550 9200 358 -1365 390 O
ATOM 3547 CB LYS A 458 -3.508 30.167 33.132 1.00 85.70 C
ANISOU 3547 CB LYS A 458 11620 11527 9415 149 -1165 183 C
ATOM 3548 CG LYS A 458 -3.467 31.032 31.884 1.00 88.29 C
ANISOU 3548 CG LYS A 458 12044 11974 9530 115 -1321 353 C
ATOM 3549 CD LYS A 458 -4.102 30.356 30.686 1.00 88.94 C
ANISOU 3549 CD LYS A 458 12032 12279 9480 128 -1421 248 C
ATOM 3550 CE LYS A 458 -3.728 31.088 29.410 1.00 99.84 C
ANISOU 3550 CE LYS A 458 13524 13848 10563 49 -1544 442 C
ATOM 3551 NZ LYS A 458 -3.761 32.566 29.599 1.00106.80 N
ANISOU 3551 NZ LYS A 458 14560 14540 11478 63 -1661 719 N
ATOM 3552 N TRP A 459 -5.539 30.886 35.500 1.00 78.52 N
ANISOU 3552 N TRP A 459 10610 10233 8992 377 -1154 91 N
ATOM 3553 CA TRP A 459 -6.774 31.478 36.001 1.00 84.54 C
ANISOU 3553 CA TRP A 459 11300 10885 9934 510 -1223 44 C
ATOM 3554 C TRP A 459 -6.483 32.669 36.904 1.00 86.58 C
ANISOU 3554 C TRP A 459 11669 10962 10264 550 -1214 114 C
ATOM 3555 O TRP A 459 -7.146 33.707 36.808 1.00 85.38 O
ANISOU 3555 O TRP A 459 11535 10694 10210 665 -1354 150 O
ATOM 3556 CB TRP A 459 -7.599 30.435 36.755 1.00 85.25 C
ANISOU 3556 CB TRP A 459 11212 11000 10179 528 -1104 -134 C
ATOM 3557 CG TRP A 459 -8.886 30.984 37.300 1.00 86.21 C
ANISOU 3557 CG TRP A 459 11215 11055 10486 660 -1145 -216 C
ATOM 3558 CD1 TRP A 459 -10.095 31.020 36.668 1.00 92.78 C
ANISOU 3558 CD1 TRP A 459 11902 11940 11409 758 -1284 -288 C
ATOM 3559 CD2 TRP A 459 -9.085 31.596 38.581 1.00 83.46 C
ANISOU 3559 CD2 TRP A 459 10863 10598 10250 718 -1050 -262 C
ATOM 3560 NE1 TRP A 459 -11.036 31.605 37.481 1.00 97.26 N
ANISOU 3560 NE1 TRP A 459 12360 12434 12162 880 -1273 -379 N
ATOM 3561 CE2 TRP A 459 -10.441 31.969 38.660 1.00 88.71 C
ANISOU 3561 CE2 TRP A 459 11364 11256 11085 857 -1122 -375 C
ATOM 3562 CE3 TRP A 459 -8.249 31.860 39.669 1.00 85.70 C
ANISOU 3562 CE3 TRP A 459 11252 10812 10499 667 -916 -240 C
ATOM 3563 CZ2 TRP A 459 -10.979 32.591 39.785 1.00 97.84 C
ANISOU 3563 CZ2 TRP A 459 12454 12344 12376 950 -1044 -484 C
ATOM 3564 CZ3 TRP A 459 -8.785 32.479 40.784 1.00 85.96 C
ANISOU 3564 CZ3 TRP A 459 11236 10782 10644 749 -848 -342 C
ATOM 3565 CH2 TRP A 459 -10.136 32.839 40.833 1.00 95.08 C
ANISOU 3565 CH2 TRP A 459 12223 11936 11965 891 -903 -471 C
ATOM 3566 N ARG A 460 -5.487 32.540 37.783 1.00 90.09 N
ANISOU 3566 N ARG A 460 12183 11372 10674 464 -1067 120 N
ATOM 3567 CA ARG A 460 -5.171 33.624 38.708 1.00 91.00 C
ANISOU 3567 CA ARG A 460 12397 11325 10855 488 -1056 144 C
ATOM 3568 C ARG A 460 -4.498 34.785 37.988 1.00 88.99 C
ANISOU 3568 C ARG A 460 12308 10970 10534 449 -1194 324 C
ATOM 3569 O ARG A 460 -4.846 35.951 38.214 1.00 97.80 O
ANISOU 3569 O ARG A 460 13486 11900 11774 532 -1300 351 O
ATOM 3570 CB ARG A 460 -4.287 33.106 39.841 1.00 89.25 C
ANISOU 3570 CB ARG A 460 12192 11126 10593 398 -879 100 C
ATOM 3571 CG ARG A 460 -5.005 32.177 40.797 1.00 84.30 C
ANISOU 3571 CG ARG A 460 11426 10561 10045 427 -743 -39 C
ATOM 3572 CD ARG A 460 -4.345 32.188 42.158 1.00 80.54 C
ANISOU 3572 CD ARG A 460 10992 10071 9536 377 -613 -67 C
ATOM 3573 NE ARG A 460 -2.993 31.648 42.101 1.00 84.74 N
ANISOU 3573 NE ARG A 460 11594 10656 9946 259 -569 21 N
ATOM 3574 CZ ARG A 460 -2.247 31.390 43.165 1.00 86.29 C
ANISOU 3574 CZ ARG A 460 11819 10879 10090 201 -474 20 C
ATOM 3575 NH1 ARG A 460 -2.689 31.617 44.390 1.00 83.37 N
ANISOU 3575 NH1 ARG A 460 11430 10508 9740 231 -400 -60 N
ATOM 3576 NH2 ARG A 460 -1.024 30.895 42.995 1.00 83.40 N
ANISOU 3576 NH2 ARG A 460 11490 10562 9635 113 -458 94 N
ATOM 3577 N TRP A 461 -3.519 34.485 37.127 1.00 82.91 N
ANISOU 3577 N TRP A 461 11604 10318 9580 315 -1191 446 N
ATOM 3578 CA TRP A 461 -2.876 35.523 36.326 1.00 87.56 C
ANISOU 3578 CA TRP A 461 12345 10847 10078 237 -1312 654 C
ATOM 3579 C TRP A 461 -3.907 36.392 35.622 1.00 96.48 C
ANISOU 3579 C TRP A 461 13503 11866 11288 357 -1527 751 C
ATOM 3580 O TRP A 461 -3.769 37.620 35.569 1.00 99.77 O
ANISOU 3580 O TRP A 461 14052 12080 11778 360 -1650 895 O
ATOM 3581 CB TRP A 461 -1.947 34.888 35.290 1.00 97.52 C
ANISOU 3581 CB TRP A 461 13619 12336 11100 87 -1270 741 C
ATOM 3582 CG TRP A 461 -0.621 34.438 35.815 1.00 87.68 C
ANISOU 3582 CG TRP A 461 12376 11160 9779 -45 -1106 711 C
ATOM 3583 CD1 TRP A 461 -0.056 34.756 37.013 1.00 96.88 C
ANISOU 3583 CD1 TRP A 461 13572 12200 11039 -69 -1027 670 C
ATOM 3584 CD2 TRP A 461 0.311 33.581 35.145 1.00 88.22 C
ANISOU 3584 CD2 TRP A 461 12396 11459 9665 -159 -1013 701 C
ATOM 3585 NE1 TRP A 461 1.171 34.149 37.133 1.00102.68 N
ANISOU 3585 NE1 TRP A 461 14278 13067 11667 -188 -905 655 N
ATOM 3586 CE2 TRP A 461 1.420 33.422 35.998 1.00 94.74 C
ANISOU 3586 CE2 TRP A 461 13218 12275 10505 -239 -888 666 C
ATOM 3587 CE3 TRP A 461 0.315 32.933 33.906 1.00 93.08 C
ANISOU 3587 CE3 TRP A 461 12959 12304 10102 -196 -1027 694 C
ATOM 3588 CZ2 TRP A 461 2.520 32.641 35.652 1.00 97.58 C
ANISOU 3588 CZ2 TRP A 461 13509 12830 10737 -337 -780 626 C
ATOM 3589 CZ3 TRP A 461 1.408 32.160 33.565 1.00 87.36 C
ANISOU 3589 CZ3 TRP A 461 12173 11780 9240 -298 -903 632 C
ATOM 3590 CH2 TRP A 461 2.495 32.020 34.434 1.00 93.23 C
ANISOU 3590 CH2 TRP A 461 12900 12492 10031 -360 -782 600 C
ATOM 3591 N MET A 462 -4.955 35.768 35.083 1.00 94.98 N
ANISOU 3591 N MET A 462 13187 11795 11106 459 -1590 672 N
ATOM 3592 CA MET A 462 -5.981 36.512 34.364 1.00 99.36 C
ANISOU 3592 CA MET A 462 13744 12272 11736 593 -1823 762 C
ATOM 3593 C MET A 462 -6.884 37.273 35.327 1.00101.14 C
ANISOU 3593 C MET A 462 13919 12257 12251 776 -1874 648 C
ATOM 3594 O MET A 462 -7.198 38.448 35.097 1.00109.41 O
ANISOU 3594 O MET A 462 15055 13094 13421 870 -2066 772 O
ATOM 3595 CB MET A 462 -6.796 35.554 33.497 1.00 90.18 C
ANISOU 3595 CB MET A 462 12436 11341 10488 636 -1881 682 C
ATOM 3596 CG MET A 462 -5.991 34.909 32.383 1.00 97.29 C
ANISOU 3596 CG MET A 462 13380 12497 11089 475 -1859 769 C
ATOM 3597 SD MET A 462 -6.881 33.562 31.582 1.00 88.23 S
ANISOU 3597 SD MET A 462 12035 11622 9865 511 -1889 575 S
ATOM 3598 CE MET A 462 -8.250 34.449 30.845 1.00111.80 C
ANISOU 3598 CE MET A 462 14990 14562 12925 688 -2205 679 C
ATOM 3599 N VAL A 463 -7.323 36.613 36.407 1.00 89.76 N
ANISOU 3599 N VAL A 463 12332 10848 10924 831 -1707 409 N
ATOM 3600 CA VAL A 463 -8.143 37.279 37.421 1.00 90.29 C
ANISOU 3600 CA VAL A 463 12324 10738 11243 998 -1712 250 C
ATOM 3601 C VAL A 463 -7.483 38.575 37.868 1.00 92.48 C
ANISOU 3601 C VAL A 463 12778 10752 11608 994 -1769 330 C
ATOM 3602 O VAL A 463 -8.101 39.646 37.863 1.00 99.58 O
ANISOU 3602 O VAL A 463 13696 11428 12712 1151 -1940 333 O
ATOM 3603 CB VAL A 463 -8.395 36.339 38.615 1.00 89.11 C
ANISOU 3603 CB VAL A 463 12022 10706 11129 986 -1473 18 C
ATOM 3604 CG1 VAL A 463 -8.914 37.124 39.807 1.00 89.72 C
ANISOU 3604 CG1 VAL A 463 12050 10632 11406 1119 -1431 -160 C
ATOM 3605 CG2 VAL A 463 -9.398 35.274 38.239 1.00 87.22 C
ANISOU 3605 CG2 VAL A 463 11578 10656 10907 1024 -1456 -88 C
ATOM 3606 N PHE A 464 -6.204 38.496 38.238 1.00 89.73 N
ANISOU 3606 N PHE A 464 12553 10414 11128 816 -1642 388 N
ATOM 3607 CA PHE A 464 -5.470 39.693 38.628 1.00 96.24 C
ANISOU 3607 CA PHE A 464 13544 10989 12036 772 -1697 460 C
ATOM 3608 C PHE A 464 -5.346 40.667 37.463 1.00 98.88 C
ANISOU 3608 C PHE A 464 14029 11158 12381 755 -1934 738 C
ATOM 3609 O PHE A 464 -5.456 41.885 37.647 1.00109.06 O
ANISOU 3609 O PHE A 464 15418 12144 13875 827 -2078 779 O
ATOM 3610 CB PHE A 464 -4.090 39.303 39.155 1.00102.57 C
ANISOU 3610 CB PHE A 464 14417 11879 12674 567 -1522 474 C
ATOM 3611 CG PHE A 464 -4.133 38.393 40.349 1.00 97.85 C
ANISOU 3611 CG PHE A 464 13697 11430 12051 574 -1312 249 C
ATOM 3612 CD1 PHE A 464 -5.130 38.520 41.303 1.00 97.89 C
ANISOU 3612 CD1 PHE A 464 13589 11392 12214 732 -1268 24 C
ATOM 3613 CD2 PHE A 464 -3.183 37.399 40.509 1.00 80.09 C
ANISOU 3613 CD2 PHE A 464 11438 9374 9618 422 -1160 270 C
ATOM 3614 CE1 PHE A 464 -5.169 37.679 42.400 1.00 84.09 C
ANISOU 3614 CE1 PHE A 464 11738 9806 10407 711 -1070 -143 C
ATOM 3615 CE2 PHE A 464 -3.218 36.556 41.600 1.00 76.52 C
ANISOU 3615 CE2 PHE A 464 10890 9046 9140 422 -989 111 C
ATOM 3616 CZ PHE A 464 -4.211 36.696 42.547 1.00 77.63 C
ANISOU 3616 CZ PHE A 464 10934 9156 9404 554 -940 -80 C
ATOM 3617 N LYS A 465 -5.127 40.147 36.252 1.00 97.72 N
ANISOU 3617 N LYS A 465 13904 11207 12016 656 -1982 931 N
ATOM 3618 CA LYS A 465 -4.993 41.002 35.078 1.00102.44 C
ANISOU 3618 CA LYS A 465 14654 11702 12565 611 -2204 1239 C
ATOM 3619 C LYS A 465 -6.258 41.799 34.791 1.00 97.57 C
ANISOU 3619 C LYS A 465 14014 10877 12183 848 -2458 1268 C
ATOM 3620 O LYS A 465 -6.179 42.860 34.163 1.00 99.02 O
ANISOU 3620 O LYS A 465 14354 10838 12431 843 -2676 1528 O
ATOM 3621 CB LYS A 465 -4.624 40.158 33.854 1.00109.26 C
ANISOU 3621 CB LYS A 465 15513 12895 13106 470 -2188 1390 C
ATOM 3622 CG LYS A 465 -3.299 40.526 33.204 1.00121.69 C
ANISOU 3622 CG LYS A 465 17254 14518 14465 216 -2166 1654 C
ATOM 3623 CD LYS A 465 -2.759 39.382 32.357 1.00116.47 C
ANISOU 3623 CD LYS A 465 16530 14251 13473 73 -2044 1664 C
ATOM 3624 CE LYS A 465 -1.449 39.767 31.687 1.00115.43 C
ANISOU 3624 CE LYS A 465 16533 14212 13112 -189 -2002 1914 C
ATOM 3625 NZ LYS A 465 -0.811 38.616 30.992 1.00 87.13 N
ANISOU 3625 NZ LYS A 465 12859 11028 9219 -320 -1845 1854 N
ATOM 3626 N GLY A 466 -7.417 41.319 35.242 1.00114.43 N
ANISOU 3626 N GLY A 466 15948 13072 14460 1051 -2442 1016 N
ATOM 3627 CA GLY A 466 -8.692 41.929 34.928 1.00117.59 C
ANISOU 3627 CA GLY A 466 16269 13324 15086 1300 -2685 1009 C
ATOM 3628 C GLY A 466 -9.439 41.263 33.792 1.00107.75 C
ANISOU 3628 C GLY A 466 14916 12332 13692 1349 -2816 1086 C
ATOM 3629 O GLY A 466 -10.577 41.656 33.504 1.00103.60 O
ANISOU 3629 O GLY A 466 14285 11725 13352 1570 -3032 1064 O
ATOM 3630 N GLU A 467 -8.837 40.255 33.156 1.00101.73 N
ANISOU 3630 N GLU A 467 14160 11881 12611 1157 -2699 1148 N
ATOM 3631 CA GLU A 467 -9.416 39.653 31.963 1.00 96.58 C
ANISOU 3631 CA GLU A 467 13429 11492 11776 1173 -2839 1221 C
ATOM 3632 C GLU A 467 -10.667 38.836 32.257 1.00 96.43 C
ANISOU 3632 C GLU A 467 13135 11611 11894 1336 -2817 930 C
ATOM 3633 O GLU A 467 -11.407 38.508 31.324 1.00113.85 O
ANISOU 3633 O GLU A 467 15244 13995 14020 1399 -2990 957 O
ATOM 3634 CB GLU A 467 -8.382 38.765 31.270 1.00107.95 C
ANISOU 3634 CB GLU A 467 14934 13233 12849 925 -2695 1303 C
ATOM 3635 CG GLU A 467 -7.117 39.486 30.831 1.00116.83 C
ANISOU 3635 CG GLU A 467 16300 14294 13796 724 -2700 1602 C
ATOM 3636 CD GLU A 467 -6.117 38.547 30.181 1.00122.90 C
ANISOU 3636 CD GLU A 467 17085 15402 14209 496 -2532 1625 C
ATOM 3637 OE1 GLU A 467 -6.418 37.339 30.078 1.00118.53 O
ANISOU 3637 OE1 GLU A 467 16370 15096 13571 507 -2427 1401 O
ATOM 3638 OE2 GLU A 467 -5.039 39.015 29.759 1.00126.01 O1-
ANISOU 3638 OE2 GLU A 467 17643 15812 14422 303 -2505 1856 O1-
ATOM 3639 N ILE A 468 -10.920 38.491 33.514 1.00 86.64 N
ANISOU 3639 N ILE A 468 11760 10317 10840 1390 -2610 656 N
ATOM 3640 CA ILE A 468 -12.082 37.699 33.889 1.00 88.87 C
ANISOU 3640 CA ILE A 468 11767 10739 11261 1508 -2553 383 C
ATOM 3641 C ILE A 468 -12.897 38.493 34.903 1.00 96.23 C
ANISOU 3641 C ILE A 468 12586 11449 12528 1724 -2570 208 C
ATOM 3642 O ILE A 468 -12.415 38.765 36.007 1.00100.96 O
ANISOU 3642 O ILE A 468 13236 11918 13206 1697 -2390 107 O
ATOM 3643 CB ILE A 468 -11.693 36.325 34.460 1.00 84.75 C
ANISOU 3643 CB ILE A 468 11154 10420 10627 1345 -2256 204 C
ATOM 3644 CG1 ILE A 468 -10.819 35.561 33.463 1.00 83.99 C
ANISOU 3644 CG1 ILE A 468 11159 10530 10221 1151 -2235 333 C
ATOM 3645 CG2 ILE A 468 -12.938 35.529 34.805 1.00 84.54 C
ANISOU 3645 CG2 ILE A 468 10838 10526 10757 1436 -2203 -51 C
ATOM 3646 CD1 ILE A 468 -10.436 34.170 33.927 1.00 82.88 C
ANISOU 3646 CD1 ILE A 468 10929 10553 10008 1009 -1980 162 C
ATOM 3647 N PRO A 469 -14.121 38.896 34.575 1.00 96.68 N
ANISOU 3647 N PRO A 469 12475 11472 12785 1946 -2786 148 N
ATOM 3648 CA PRO A 469 -14.927 39.672 35.522 1.00100.66 C
ANISOU 3648 CA PRO A 469 12841 11778 13628 2176 -2800 -61 C
ATOM 3649 C PRO A 469 -15.431 38.817 36.676 1.00100.92 C
ANISOU 3649 C PRO A 469 12631 11978 13736 2161 -2503 -391 C
ATOM 3650 O PRO A 469 -15.510 37.588 36.596 1.00 90.89 O
ANISOU 3650 O PRO A 469 11247 10965 12322 2017 -2350 -458 O
ATOM 3651 CB PRO A 469 -16.091 40.186 34.665 1.00112.10 C
ANISOU 3651 CB PRO A 469 14150 13194 15250 2416 -3137 -18 C
ATOM 3652 CG PRO A 469 -15.620 40.052 33.245 1.00109.39 C
ANISOU 3652 CG PRO A 469 13980 12956 14626 2294 -3340 307 C
ATOM 3653 CD PRO A 469 -14.739 38.844 33.242 1.00104.47 C
ANISOU 3653 CD PRO A 469 13414 12584 13694 2013 -3070 293 C
ATOM 3654 N LYS A 470 -15.793 39.511 37.760 1.00108.32 N
ANISOU 3654 N LYS A 470 13487 12761 14910 2310 -2426 -600 N
ATOM 3655 CA LYS A 470 -16.207 38.851 38.996 1.00104.50 C
ANISOU 3655 CA LYS A 470 12791 12441 14473 2282 -2122 -900 C
ATOM 3656 C LYS A 470 -17.368 37.889 38.775 1.00107.21 C
ANISOU 3656 C LYS A 470 12815 13053 14868 2307 -2090 -1053 C
ATOM 3657 O LYS A 470 -17.416 36.812 39.381 1.00102.32 O
ANISOU 3657 O LYS A 470 12076 12646 14154 2145 -1826 -1170 O
ATOM 3658 CB LYS A 470 -16.593 39.901 40.037 1.00100.58 C
ANISOU 3658 CB LYS A 470 12224 11756 14233 2483 -2092 -1135 C
ATOM 3659 CG LYS A 470 -15.473 40.333 40.962 1.00 99.50 C
ANISOU 3659 CG LYS A 470 12312 11482 14012 2372 -1930 -1145 C
ATOM 3660 CD LYS A 470 -15.955 41.449 41.873 1.00114.94 C
ANISOU 3660 CD LYS A 470 14184 13242 16245 2600 -1941 -1420 C
ATOM 3661 CE LYS A 470 -17.309 41.109 42.479 1.00100.67 C
ANISOU 3661 CE LYS A 470 12001 11650 14600 2755 -1816 -1754 C
ATOM 3662 NZ LYS A 470 -17.660 41.997 43.619 1.00117.01 N
ANISOU 3662 NZ LYS A 470 13966 13614 16877 2938 -1728 -2098 N
ATOM 3663 N ASP A 471 -18.321 38.261 37.922 1.00113.93 N
ANISOU 3663 N ASP A 471 13518 13891 15881 2501 -2367 -1046 N
ATOM 3664 CA ASP A 471 -19.500 37.436 37.690 1.00120.84 C
ANISOU 3664 CA ASP A 471 14055 15018 16840 2533 -2365 -1215 C
ATOM 3665 C ASP A 471 -19.225 36.250 36.772 1.00120.88 C
ANISOU 3665 C ASP A 471 14093 15232 16603 2315 -2374 -1080 C
ATOM 3666 O ASP A 471 -20.176 35.599 36.326 1.00104.83 O
ANISOU 3666 O ASP A 471 11798 13393 14638 2331 -2439 -1194 O
ATOM 3667 CB ASP A 471 -20.639 38.287 37.119 1.00132.42 C
ANISOU 3667 CB ASP A 471 15326 16405 18583 2841 -2688 -1275 C
ATOM 3668 CG ASP A 471 -20.335 38.825 35.732 1.00135.21 C
ANISOU 3668 CG ASP A 471 15890 16638 18845 2897 -3058 -955 C
ATOM 3669 OD1 ASP A 471 -19.145 38.889 35.358 1.00129.34 O
ANISOU 3669 OD1 ASP A 471 15476 15808 17858 2726 -3056 -696 O
ATOM 3670 OD2 ASP A 471 -21.292 39.187 35.015 1.00140.41 O1-
ANISOU 3670 OD2 ASP A 471 16374 17308 19668 3108 -3356 -957 O1-
ATOM 3671 N GLN A 472 -17.952 35.960 36.479 1.00122.45 N
ANISOU 3671 N GLN A 472 14590 15400 16537 2114 -2313 -868 N
ATOM 3672 CA GLN A 472 -17.598 34.814 35.651 1.00122.05 C
ANISOU 3672 CA GLN A 472 14572 15542 16258 1911 -2300 -783 C
ATOM 3673 C GLN A 472 -16.346 34.110 36.170 1.00113.34 C
ANISOU 3673 C GLN A 472 13664 14450 14950 1671 -2033 -720 C
ATOM 3674 O GLN A 472 -15.708 33.364 35.416 1.00109.43 O
ANISOU 3674 O GLN A 472 13274 14060 14246 1512 -2039 -618 O
ATOM 3675 CB GLN A 472 -17.407 35.248 34.190 1.00110.62 C
ANISOU 3675 CB GLN A 472 13272 14093 14667 1954 -2626 -550 C
ATOM 3676 CG GLN A 472 -18.705 35.686 33.518 1.00122.21 C
ANISOU 3676 CG GLN A 472 14516 15604 16314 2180 -2928 -602 C
ATOM 3677 CD GLN A 472 -18.516 36.144 32.088 1.00136.73 C
ANISOU 3677 CD GLN A 472 16516 17463 17972 2216 -3266 -336 C
ATOM 3678 OE1 GLN A 472 -17.391 36.318 31.621 1.00135.98 O
ANISOU 3678 OE1 GLN A 472 16713 17327 17627 2079 -3270 -98 O
ATOM 3679 NE2 GLN A 472 -19.623 36.351 31.384 1.00142.43 N
ANISOU 3679 NE2 GLN A 472 17036 18271 18809 2394 -3556 -368 N
ATOM 3680 N TRP A 473 -15.984 34.332 37.437 1.00106.13 N
ANISOU 3680 N TRP A 473 12791 13445 14089 1651 -1809 -795 N
ATOM 3681 CA TRP A 473 -14.837 33.657 38.037 1.00108.67 C
ANISOU 3681 CA TRP A 473 13273 13783 14233 1440 -1570 -739 C
ATOM 3682 C TRP A 473 -14.975 32.142 37.946 1.00104.69 C
ANISOU 3682 C TRP A 473 12643 13466 13669 1265 -1428 -806 C
ATOM 3683 O TRP A 473 -14.091 31.451 37.428 1.00112.44 O
ANISOU 3683 O TRP A 473 13762 14487 14475 1115 -1405 -700 O
ATOM 3684 CB TRP A 473 -14.684 34.087 39.498 1.00105.33 C
ANISOU 3684 CB TRP A 473 12856 13282 13882 1460 -1363 -850 C
ATOM 3685 CG TRP A 473 -13.840 35.303 39.698 1.00 92.43 C
ANISOU 3685 CG TRP A 473 11459 11431 12228 1520 -1435 -747 C
ATOM 3686 CD1 TRP A 473 -13.350 36.134 38.734 1.00 95.39 C
ANISOU 3686 CD1 TRP A 473 12023 11655 12563 1566 -1670 -548 C
ATOM 3687 CD2 TRP A 473 -13.386 35.828 40.949 1.00 90.43 C
ANISOU 3687 CD2 TRP A 473 11277 11090 11991 1520 -1275 -838 C
ATOM 3688 NE1 TRP A 473 -12.615 37.143 39.308 1.00 93.46 N
ANISOU 3688 NE1 TRP A 473 11962 11204 12344 1586 -1666 -508 N
ATOM 3689 CE2 TRP A 473 -12.624 36.979 40.668 1.00 94.01 C
ANISOU 3689 CE2 TRP A 473 11959 11312 12447 1566 -1431 -703 C
ATOM 3690 CE3 TRP A 473 -13.551 35.438 42.282 1.00 93.70 C
ANISOU 3690 CE3 TRP A 473 11584 11615 12404 1471 -1018 -1016 C
ATOM 3691 CZ2 TRP A 473 -12.027 37.741 41.668 1.00 97.18 C
ANISOU 3691 CZ2 TRP A 473 12476 11574 12872 1571 -1346 -775 C
ATOM 3692 CZ3 TRP A 473 -12.958 36.195 43.273 1.00 94.71 C
ANISOU 3692 CZ3 TRP A 473 11830 11640 12515 1484 -933 -1084 C
ATOM 3693 CH2 TRP A 473 -12.205 37.333 42.961 1.00 96.02 C
ANISOU 3693 CH2 TRP A 473 12216 11561 12706 1537 -1101 -981 C
ATOM 3694 N MET A 474 -16.083 31.607 38.458 1.00 98.20 N
ANISOU 3694 N MET A 474 11546 12755 13011 1277 -1329 -993 N
ATOM 3695 CA MET A 474 -16.272 30.163 38.449 1.00101.90 C
ANISOU 3695 CA MET A 474 11888 13360 13471 1093 -1195 -1057 C
ATOM 3696 C MET A 474 -16.643 29.640 37.069 1.00106.75 C
ANISOU 3696 C MET A 474 12429 14070 14061 1079 -1402 -1064 C
ATOM 3697 O MET A 474 -16.296 28.502 36.732 1.00104.16 O
ANISOU 3697 O MET A 474 12110 13801 13665 912 -1341 -1071 O
ATOM 3698 CB MET A 474 -17.337 29.766 39.470 1.00 99.01 C
ANISOU 3698 CB MET A 474 11242 13094 13283 1074 -1005 -1240 C
ATOM 3699 CG MET A 474 -16.943 30.073 40.902 1.00105.10 C
ANISOU 3699 CG MET A 474 12078 13832 14022 1048 -766 -1251 C
ATOM 3700 SD MET A 474 -15.263 29.537 41.286 1.00 99.81 S
ANISOU 3700 SD MET A 474 11729 13078 13118 861 -631 -1053 S
ATOM 3701 CE MET A 474 -15.344 27.793 40.874 1.00 98.72 C
ANISOU 3701 CE MET A 474 11497 13016 12994 642 -560 -1038 C
ATOM 3702 N LYS A 475 -17.341 30.442 36.264 1.00116.78 N
ANISOU 3702 N LYS A 475 13625 15355 15392 1258 -1661 -1071 N
ATOM 3703 CA LYS A 475 -17.653 30.018 34.904 1.00107.75 C
ANISOU 3703 CA LYS A 475 12426 14337 14177 1247 -1887 -1072 C
ATOM 3704 C LYS A 475 -16.386 29.871 34.074 1.00102.10 C
ANISOU 3704 C LYS A 475 11990 13617 13185 1144 -1940 -900 C
ATOM 3705 O LYS A 475 -16.257 28.928 33.285 1.00100.48 O
ANISOU 3705 O LYS A 475 11761 13540 12876 1025 -1975 -952 O
ATOM 3706 CB LYS A 475 -18.610 31.010 34.246 1.00100.46 C
ANISOU 3706 CB LYS A 475 11381 13429 13359 1477 -2182 -1077 C
ATOM 3707 CG LYS A 475 -19.087 30.575 32.873 1.00107.98 C
ANISOU 3707 CG LYS A 475 12241 14559 14227 1473 -2438 -1098 C
ATOM 3708 CD LYS A 475 -19.764 31.716 32.139 1.00121.43 C
ANISOU 3708 CD LYS A 475 13905 16253 15982 1714 -2778 -1016 C
ATOM 3709 CE LYS A 475 -20.320 31.257 30.805 1.00125.12 C
ANISOU 3709 CE LYS A 475 14256 16942 16342 1708 -3048 -1050 C
ATOM 3710 NZ LYS A 475 -20.818 32.405 30.000 1.00141.99 N
ANISOU 3710 NZ LYS A 475 16405 19064 18480 1940 -3418 -899 N
ATOM 3711 N LYS A 476 -15.434 30.790 34.240 1.00101.14 N
ANISOU 3711 N LYS A 476 12120 13359 12949 1180 -1941 -716 N
ATOM 3712 CA LYS A 476 -14.181 30.695 33.505 1.00 99.90 C
ANISOU 3712 CA LYS A 476 12208 13223 12526 1067 -1964 -554 C
ATOM 3713 C LYS A 476 -13.225 29.687 34.127 1.00101.37 C
ANISOU 3713 C LYS A 476 12465 13402 12649 886 -1702 -589 C
ATOM 3714 O LYS A 476 -12.346 29.175 33.427 1.00 95.17 O
ANISOU 3714 O LYS A 476 11794 12694 11670 776 -1699 -543 O
ATOM 3715 CB LYS A 476 -13.509 32.067 33.422 1.00 99.31 C
ANISOU 3715 CB LYS A 476 12365 12998 12369 1147 -2068 -331 C
ATOM 3716 CG LYS A 476 -13.527 32.688 32.030 1.00120.08 C
ANISOU 3716 CG LYS A 476 15092 15702 14830 1199 -2358 -156 C
ATOM 3717 CD LYS A 476 -12.658 31.937 31.035 1.00129.88 C
ANISOU 3717 CD LYS A 476 16438 17138 15772 1028 -2347 -104 C
ATOM 3718 CE LYS A 476 -12.670 32.637 29.679 1.00115.83 C
ANISOU 3718 CE LYS A 476 14767 15469 13774 1064 -2631 100 C
ATOM 3719 NZ LYS A 476 -11.712 32.033 28.711 1.00126.73 N
ANISOU 3719 NZ LYS A 476 16260 17075 14817 890 -2598 147 N
ATOM 3720 N TRP A 477 -13.379 29.392 35.420 1.00101.98 N
ANISOU 3720 N TRP A 477 12467 13401 12880 858 -1489 -670 N
ATOM 3721 CA TRP A 477 -12.550 28.371 36.053 1.00 88.43 C
ANISOU 3721 CA TRP A 477 10806 11668 11126 696 -1267 -683 C
ATOM 3722 C TRP A 477 -12.826 26.997 35.458 1.00 89.97 C
ANISOU 3722 C TRP A 477 10870 11964 11349 583 -1260 -813 C
ATOM 3723 O TRP A 477 -11.899 26.282 35.061 1.00 93.44 O
ANISOU 3723 O TRP A 477 11410 12420 11675 480 -1218 -801 O
ATOM 3724 CB TRP A 477 -12.790 28.356 37.566 1.00 87.22 C
ANISOU 3724 CB TRP A 477 10590 11441 11108 684 -1058 -724 C
ATOM 3725 CG TRP A 477 -12.091 27.226 38.273 1.00 92.26 C
ANISOU 3725 CG TRP A 477 11265 12059 11730 521 -853 -714 C
ATOM 3726 CD1 TRP A 477 -12.625 26.015 38.612 1.00 93.96 C
ANISOU 3726 CD1 TRP A 477 11323 12304 12074 407 -739 -804 C
ATOM 3727 CD2 TRP A 477 -10.732 27.205 38.730 1.00 86.53 C
ANISOU 3727 CD2 TRP A 477 10740 11265 10871 455 -756 -592 C
ATOM 3728 NE1 TRP A 477 -11.683 25.242 39.247 1.00100.96 N
ANISOU 3728 NE1 TRP A 477 12317 13125 12919 286 -590 -727 N
ATOM 3729 CE2 TRP A 477 -10.513 25.950 39.333 1.00 83.88 C
ANISOU 3729 CE2 TRP A 477 10364 10916 10593 322 -601 -607 C
ATOM 3730 CE3 TRP A 477 -9.682 28.126 38.691 1.00 79.85 C
ANISOU 3730 CE3 TRP A 477 10096 10364 9879 487 -794 -468 C
ATOM 3731 CZ2 TRP A 477 -9.287 25.592 39.887 1.00 77.00 C
ANISOU 3731 CZ2 TRP A 477 9639 9986 9633 248 -500 -504 C
ATOM 3732 CZ3 TRP A 477 -8.464 27.768 39.237 1.00 77.67 C
ANISOU 3732 CZ3 TRP A 477 9950 10050 9511 397 -679 -387 C
ATOM 3733 CH2 TRP A 477 -8.277 26.514 39.830 1.00 91.08 C
ANISOU 3733 CH2 TRP A 477 11597 11745 11266 291 -541 -407 C
ATOM 3734 N TRP A 478 -14.101 26.611 35.385 1.00 86.26 N
ANISOU 3734 N TRP A 478 10161 11561 11052 601 -1304 -962 N
ATOM 3735 CA TRP A 478 -14.450 25.280 34.908 1.00 86.60 C
ANISOU 3735 CA TRP A 478 10062 11672 11170 476 -1297 -1114 C
ATOM 3736 C TRP A 478 -14.433 25.165 33.391 1.00 89.92 C
ANISOU 3736 C TRP A 478 10490 12233 11443 492 -1520 -1172 C
ATOM 3737 O TRP A 478 -14.362 24.045 32.874 1.00 95.30 O
ANISOU 3737 O TRP A 478 11110 12960 12139 379 -1516 -1312 O
ATOM 3738 CB TRP A 478 -15.816 24.864 35.455 1.00 87.48 C
ANISOU 3738 CB TRP A 478 9890 11814 11533 454 -1244 -1260 C
ATOM 3739 CG TRP A 478 -15.746 24.470 36.893 1.00 86.10 C
ANISOU 3739 CG TRP A 478 9696 11547 11471 356 -982 -1224 C
ATOM 3740 CD1 TRP A 478 -16.264 25.144 37.958 1.00 88.69 C
ANISOU 3740 CD1 TRP A 478 9948 11874 11877 419 -867 -1210 C
ATOM 3741 CD2 TRP A 478 -15.087 23.316 37.428 1.00 93.26 C
ANISOU 3741 CD2 TRP A 478 10665 12359 12410 181 -809 -1190 C
ATOM 3742 NE1 TRP A 478 -15.982 24.474 39.124 1.00 93.30 N
ANISOU 3742 NE1 TRP A 478 10547 12403 12499 275 -625 -1158 N
ATOM 3743 CE2 TRP A 478 -15.259 23.348 38.825 1.00 98.44 C
ANISOU 3743 CE2 TRP A 478 11289 12979 13135 130 -597 -1124 C
ATOM 3744 CE3 TRP A 478 -14.375 22.256 36.860 1.00104.34 C
ANISOU 3744 CE3 TRP A 478 12143 13704 13796 71 -820 -1219 C
ATOM 3745 CZ2 TRP A 478 -14.744 22.361 39.662 1.00109.19 C
ANISOU 3745 CZ2 TRP A 478 12706 14243 14537 -34 -414 -1039 C
ATOM 3746 CZ3 TRP A 478 -13.864 21.277 37.692 1.00101.03 C
ANISOU 3746 CZ3 TRP A 478 11769 13152 13464 -72 -644 -1156 C
ATOM 3747 CH2 TRP A 478 -14.051 21.336 39.077 1.00105.45 C
ANISOU 3747 CH2 TRP A 478 12311 13673 14081 -127 -452 -1044 C
ATOM 3748 N GLU A 479 -14.497 26.283 32.663 1.00 97.09 N
ANISOU 3748 N GLU A 479 11475 13209 12206 625 -1720 -1069 N
ATOM 3749 CA GLU A 479 -14.225 26.230 31.230 1.00 97.73 C
ANISOU 3749 CA GLU A 479 11617 13459 12058 619 -1916 -1075 C
ATOM 3750 C GLU A 479 -12.785 25.811 30.971 1.00103.58 C
ANISOU 3750 C GLU A 479 12557 14205 12593 510 -1805 -1022 C
ATOM 3751 O GLU A 479 -12.510 25.022 30.059 1.00 96.96 O
ANISOU 3751 O GLU A 479 11702 13507 11631 433 -1851 -1153 O
ATOM 3752 CB GLU A 479 -14.500 27.585 30.580 1.00105.49 C
ANISOU 3752 CB GLU A 479 12673 14493 12915 773 -2156 -907 C
ATOM 3753 CG GLU A 479 -15.953 27.854 30.245 1.00124.39 C
ANISOU 3753 CG GLU A 479 14835 16969 15458 899 -2366 -1002 C
ATOM 3754 CD GLU A 479 -16.138 29.186 29.547 1.00134.19 C
ANISOU 3754 CD GLU A 479 16173 18233 16580 1063 -2638 -800 C
ATOM 3755 OE1 GLU A 479 -15.130 29.754 29.073 1.00114.08 O
ANISOU 3755 OE1 GLU A 479 13877 15683 13787 1036 -2673 -589 O
ATOM 3756 OE2 GLU A 479 -17.289 29.666 29.475 1.00139.00 O1-
ANISOU 3756 OE2 GLU A 479 16600 18858 17354 1216 -2819 -842 O1-
ATOM 3757 N MET A 480 -11.853 26.329 31.770 1.00 91.22 N
ANISOU 3757 N MET A 480 11164 12501 10995 506 -1661 -858 N
ATOM 3758 CA MET A 480 -10.440 26.029 31.583 1.00 80.90 C
ANISOU 3758 CA MET A 480 10024 11207 9507 415 -1556 -804 C
ATOM 3759 C MET A 480 -10.067 24.666 32.150 1.00 78.88 C
ANISOU 3759 C MET A 480 9706 10872 9394 308 -1372 -952 C
ATOM 3760 O MET A 480 -9.143 24.022 31.641 1.00 94.39 O
ANISOU 3760 O MET A 480 11725 12896 11242 241 -1329 -1017 O
ATOM 3761 CB MET A 480 -9.604 27.141 32.215 1.00 79.50 C
ANISOU 3761 CB MET A 480 10038 10913 9256 445 -1495 -577 C
ATOM 3762 CG MET A 480 -9.902 28.504 31.605 1.00 82.65 C
ANISOU 3762 CG MET A 480 10522 11339 9541 544 -1696 -404 C
ATOM 3763 SD MET A 480 -9.302 29.916 32.551 1.00 97.54 S
ANISOU 3763 SD MET A 480 12591 13010 11460 595 -1650 -180 S
ATOM 3764 CE MET A 480 -7.529 29.694 32.427 1.00 87.69 C
ANISOU 3764 CE MET A 480 11521 11807 9992 442 -1505 -86 C
ATOM 3765 N LYS A 481 -10.771 24.206 33.187 1.00 85.22 N
ANISOU 3765 N LYS A 481 10386 11543 10450 292 -1266 -1006 N
ATOM 3766 CA LYS A 481 -10.558 22.848 33.680 1.00 88.90 C
ANISOU 3766 CA LYS A 481 10787 11908 11083 181 -1123 -1120 C
ATOM 3767 C LYS A 481 -10.958 21.819 32.628 1.00 91.56 C
ANISOU 3767 C LYS A 481 10994 12337 11459 124 -1222 -1355 C
ATOM 3768 O LYS A 481 -10.292 20.790 32.467 1.00 93.79 O
ANISOU 3768 O LYS A 481 11286 12565 11783 50 -1159 -1468 O
ATOM 3769 CB LYS A 481 -11.349 22.630 34.971 1.00 85.27 C
ANISOU 3769 CB LYS A 481 10216 11321 10862 149 -993 -1099 C
ATOM 3770 CG LYS A 481 -10.617 23.046 36.239 1.00 85.47 C
ANISOU 3770 CG LYS A 481 10376 11230 10870 150 -831 -921 C
ATOM 3771 CD LYS A 481 -9.778 21.918 36.813 1.00 97.66 C
ANISOU 3771 CD LYS A 481 11969 12649 12490 44 -695 -903 C
ATOM 3772 CE LYS A 481 -9.002 22.391 38.033 1.00 95.70 C
ANISOU 3772 CE LYS A 481 11856 12323 12182 49 -564 -722 C
ATOM 3773 NZ LYS A 481 -8.640 21.264 38.932 1.00 85.11 N
ANISOU 3773 NZ LYS A 481 10514 10848 10976 -55 -433 -672 N
ATOM 3774 N ARG A 482 -12.047 22.087 31.904 1.00 91.85 N
ANISOU 3774 N ARG A 482 10897 12510 11493 166 -1391 -1450 N
ATOM 3775 CA ARG A 482 -12.506 21.189 30.848 1.00 98.06 C
ANISOU 3775 CA ARG A 482 11546 13416 12296 110 -1513 -1702 C
ATOM 3776 C ARG A 482 -11.527 21.167 29.681 1.00 98.25 C
ANISOU 3776 C ARG A 482 11693 13613 12026 114 -1587 -1759 C
ATOM 3777 O ARG A 482 -11.159 20.099 29.178 1.00 95.07 O
ANISOU 3777 O ARG A 482 11248 13225 11648 41 -1570 -1979 O
ATOM 3778 CB ARG A 482 -13.881 21.635 30.357 1.00100.56 C
ANISOU 3778 CB ARG A 482 11685 13871 12651 170 -1703 -1771 C
ATOM 3779 CG ARG A 482 -15.040 21.370 31.295 1.00 98.18 C
ANISOU 3779 CG ARG A 482 11178 13461 12667 137 -1633 -1815 C
ATOM 3780 CD ARG A 482 -16.248 22.150 30.802 1.00 93.33 C
ANISOU 3780 CD ARG A 482 10401 13007 12055 249 -1841 -1845 C
ATOM 3781 NE ARG A 482 -17.398 22.061 31.693 1.00 94.14 N
ANISOU 3781 NE ARG A 482 10273 13050 12447 232 -1767 -1894 N
ATOM 3782 CZ ARG A 482 -18.480 21.334 31.447 1.00116.40 C
ANISOU 3782 CZ ARG A 482 12824 15935 15469 152 -1833 -2107 C
ATOM 3783 NH1 ARG A 482 -18.588 20.605 30.349 1.00123.23 N
ANISOU 3783 NH1 ARG A 482 13621 16912 16289 86 -1989 -2311 N
ATOM 3784 NH2 ARG A 482 -19.482 21.349 32.320 1.00125.02 N
ANISOU 3784 NH2 ARG A 482 13695 16998 16810 130 -1738 -2134 N
ATOM 3785 N GLU A 483 -11.108 22.350 29.229 1.00 94.57 N
ANISOU 3785 N GLU A 483 11371 13280 11281 191 -1669 -1568 N
ATOM 3786 CA GLU A 483 -10.309 22.476 28.016 1.00 91.30 C
ANISOU 3786 CA GLU A 483 11056 13101 10531 178 -1748 -1598 C
ATOM 3787 C GLU A 483 -8.846 22.131 28.262 1.00 93.22 C
ANISOU 3787 C GLU A 483 11428 13290 10702 128 -1566 -1578 C
ATOM 3788 O GLU A 483 -8.240 21.381 27.489 1.00 95.41 O
ANISOU 3788 O GLU A 483 11687 13702 10862 80 -1551 -1781 O
ATOM 3789 CB GLU A 483 -10.429 23.900 27.470 1.00102.67 C
ANISOU 3789 CB GLU A 483 12609 14688 11715 258 -1910 -1353 C
ATOM 3790 CG GLU A 483 -9.572 24.177 26.252 1.00116.24 C
ANISOU 3790 CG GLU A 483 14448 16682 13036 219 -1976 -1318 C
ATOM 3791 CD GLU A 483 -9.517 25.652 25.914 1.00130.52 C
ANISOU 3791 CD GLU A 483 16410 18560 14621 274 -2112 -991 C
ATOM 3792 OE1 GLU A 483 -10.145 26.451 26.641 1.00133.40 O
ANISOU 3792 OE1 GLU A 483 16782 18736 15170 367 -2162 -825 O
ATOM 3793 OE2 GLU A 483 -8.857 26.009 24.917 1.00136.12 O1-
ANISOU 3793 OE2 GLU A 483 17228 19515 14975 222 -2169 -903 O1-
ATOM 3794 N ILE A 484 -8.263 22.675 29.329 1.00 96.01 N
ANISOU 3794 N ILE A 484 11895 13462 11124 145 -1432 -1359 N
ATOM 3795 CA ILE A 484 -6.831 22.526 29.562 1.00 82.46 C
ANISOU 3795 CA ILE A 484 10293 11717 9323 108 -1282 -1312 C
ATOM 3796 C ILE A 484 -6.535 21.208 30.265 1.00 75.87 C
ANISOU 3796 C ILE A 484 9381 10685 8760 70 -1146 -1473 C
ATOM 3797 O ILE A 484 -5.692 20.420 29.821 1.00 73.91 O
ANISOU 3797 O ILE A 484 9119 10484 8481 44 -1093 -1642 O
ATOM 3798 CB ILE A 484 -6.303 23.720 30.376 1.00 74.66 C
ANISOU 3798 CB ILE A 484 9457 10628 8282 136 -1222 -1015 C
ATOM 3799 CG1 ILE A 484 -6.625 25.033 29.658 1.00 84.33 C
ANISOU 3799 CG1 ILE A 484 10767 11995 9279 174 -1382 -833 C
ATOM 3800 CG2 ILE A 484 -4.807 23.580 30.618 1.00 74.26 C
ANISOU 3800 CG2 ILE A 484 9498 10569 8148 92 -1078 -972 C
ATOM 3801 CD1 ILE A 484 -6.186 26.264 30.425 1.00 81.66 C
ANISOU 3801 CD1 ILE A 484 10578 11521 8928 199 -1347 -563 C
ATOM 3802 N VAL A 485 -7.226 20.950 31.376 1.00 74.34 N
ANISOU 3802 N VAL A 485 9132 10270 8844 65 -1089 -1422 N
ATOM 3803 CA VAL A 485 -6.912 19.800 32.214 1.00 77.24 C
ANISOU 3803 CA VAL A 485 9458 10411 9477 18 -964 -1488 C
ATOM 3804 C VAL A 485 -7.719 18.560 31.841 1.00 79.49 C
ANISOU 3804 C VAL A 485 9579 10631 9992 -40 -1012 -1748 C
ATOM 3805 O VAL A 485 -7.358 17.450 32.256 1.00 89.13 O
ANISOU 3805 O VAL A 485 10768 11656 11442 -84 -939 -1837 O
ATOM 3806 CB VAL A 485 -7.136 20.162 33.695 1.00 81.49 C
ANISOU 3806 CB VAL A 485 10036 10764 10161 15 -857 -1267 C
ATOM 3807 CG1 VAL A 485 -6.395 19.197 34.616 1.00 89.74 C
ANISOU 3807 CG1 VAL A 485 11105 11598 11395 -27 -731 -1237 C
ATOM 3808 CG2 VAL A 485 -6.708 21.599 33.958 1.00 71.88 C
ANISOU 3808 CG2 VAL A 485 8959 9622 8732 74 -855 -1046 C
ATOM 3809 N GLY A 486 -8.784 18.708 31.059 1.00 81.64 N
ANISOU 3809 N GLY A 486 9742 11050 10226 -42 -1151 -1873 N
ATOM 3810 CA GLY A 486 -9.641 17.573 30.764 1.00 89.00 C
ANISOU 3810 CA GLY A 486 10500 11912 11404 -118 -1206 -2129 C
ATOM 3811 C GLY A 486 -10.410 17.094 31.976 1.00 95.86 C
ANISOU 3811 C GLY A 486 11283 12534 12604 -194 -1112 -2043 C
ATOM 3812 O GLY A 486 -10.551 15.881 32.181 1.00 95.44 O
ANISOU 3812 O GLY A 486 11146 12286 12831 -289 -1076 -2182 O
ATOM 3813 N VAL A 487 -10.912 18.023 32.784 1.00101.06 N
ANISOU 3813 N VAL A 487 11958 13199 13241 -163 -1067 -1820 N
ATOM 3814 CA VAL A 487 -11.565 17.720 34.051 1.00103.92 C
ANISOU 3814 CA VAL A 487 12247 13383 13854 -243 -941 -1704 C
ATOM 3815 C VAL A 487 -12.890 18.468 34.085 1.00104.37 C
ANISOU 3815 C VAL A 487 12158 13572 13927 -215 -1005 -1700 C
ATOM 3816 O VAL A 487 -12.935 19.666 33.787 1.00107.35 O
ANISOU 3816 O VAL A 487 12592 14101 14096 -92 -1086 -1615 O
ATOM 3817 CB VAL A 487 -10.680 18.124 35.247 1.00 84.48 C
ANISOU 3817 CB VAL A 487 9951 10809 11340 -220 -785 -1442 C
ATOM 3818 CG1 VAL A 487 -11.460 18.058 36.544 1.00 84.46 C
ANISOU 3818 CG1 VAL A 487 9872 10708 11512 -299 -653 -1305 C
ATOM 3819 CG2 VAL A 487 -9.432 17.255 35.307 1.00 80.45 C
ANISOU 3819 CG2 VAL A 487 9546 10148 10874 -241 -732 -1452 C
ATOM 3820 N VAL A 488 -13.964 17.767 34.440 1.00 91.33 N
ANISOU 3820 N VAL A 488 10308 11853 12540 -331 -975 -1790 N
ATOM 3821 CA VAL A 488 -15.300 18.348 34.462 1.00 90.19 C
ANISOU 3821 CA VAL A 488 9967 11846 12456 -308 -1035 -1830 C
ATOM 3822 C VAL A 488 -15.886 18.198 35.860 1.00 97.55 C
ANISOU 3822 C VAL A 488 10805 12679 13580 -407 -838 -1702 C
ATOM 3823 O VAL A 488 -15.742 17.152 36.502 1.00 98.57 O
ANISOU 3823 O VAL A 488 10927 12627 13898 -568 -707 -1666 O
ATOM 3824 CB VAL A 488 -16.220 17.712 33.397 1.00100.83 C
ANISOU 3824 CB VAL A 488 11100 13290 13922 -367 -1208 -2108 C
ATOM 3825 CG1 VAL A 488 -16.391 16.218 33.637 1.00106.78 C
ANISOU 3825 CG1 VAL A 488 11750 13839 14981 -571 -1130 -2235 C
ATOM 3826 CG2 VAL A 488 -17.570 18.420 33.362 1.00 94.45 C
ANISOU 3826 CG2 VAL A 488 10068 12652 13168 -311 -1298 -2151 C
ATOM 3827 N GLU A 489 -16.531 19.259 36.331 1.00 97.51 N
ANISOU 3827 N GLU A 489 10730 12796 13522 -309 -818 -1631 N
ATOM 3828 CA GLU A 489 -17.144 19.240 37.648 1.00 97.70 C
ANISOU 3828 CA GLU A 489 10644 12797 13681 -397 -615 -1535 C
ATOM 3829 C GLU A 489 -18.349 18.300 37.660 1.00 93.44 C
ANISOU 3829 C GLU A 489 9814 12265 13423 -577 -589 -1683 C
ATOM 3830 O GLU A 489 -19.102 18.242 36.683 1.00 97.24 O
ANISOU 3830 O GLU A 489 10118 12854 13976 -554 -767 -1884 O
ATOM 3831 CB GLU A 489 -17.562 20.655 38.057 1.00105.14 C
ANISOU 3831 CB GLU A 489 11558 13880 14511 -222 -613 -1485 C
ATOM 3832 CG GLU A 489 -18.727 21.238 37.261 1.00104.41 C
ANISOU 3832 CG GLU A 489 11234 13957 14480 -106 -800 -1657 C
ATOM 3833 CD GLU A 489 -18.302 21.807 35.916 1.00105.32 C
ANISOU 3833 CD GLU A 489 11471 14133 14412 49 -1062 -1691 C
ATOM 3834 OE1 GLU A 489 -17.249 21.390 35.389 1.00107.49 O
ANISOU 3834 OE1 GLU A 489 11948 14339 14555 14 -1094 -1655 O
ATOM 3835 OE2 GLU A 489 -19.029 22.669 35.379 1.00 98.91 O1-
ANISOU 3835 OE2 GLU A 489 10545 13452 13586 206 -1239 -1752 O1-
ATOM 3836 N PRO A 490 -18.545 17.535 38.741 1.00 89.55 N
ANISOU 3836 N PRO A 490 9266 11668 13091 -774 -378 -1578 N
ATOM 3837 CA PRO A 490 -19.706 16.635 38.803 1.00 93.13 C
ANISOU 3837 CA PRO A 490 9432 12122 13832 -985 -337 -1699 C
ATOM 3838 C PRO A 490 -21.018 17.341 39.083 1.00 94.40 C
ANISOU 3838 C PRO A 490 9299 12517 14053 -950 -302 -1793 C
ATOM 3839 O PRO A 490 -22.075 16.746 38.845 1.00 94.23 O
ANISOU 3839 O PRO A 490 8992 12547 14265 -1097 -322 -1950 O
ATOM 3840 CB PRO A 490 -19.354 15.686 39.952 1.00 95.09 C
ANISOU 3840 CB PRO A 490 9757 12178 14195 -1212 -112 -1488 C
ATOM 3841 CG PRO A 490 -18.445 16.493 40.821 1.00100.11 C
ANISOU 3841 CG PRO A 490 10632 12835 14571 -1086 3 -1265 C
ATOM 3842 CD PRO A 490 -17.662 17.392 39.908 1.00100.67 C
ANISOU 3842 CD PRO A 490 10879 12953 14419 -833 -183 -1329 C
ATOM 3843 N VAL A 491 -20.985 18.574 39.571 1.00101.84 N
ANISOU 3843 N VAL A 491 10286 13594 14814 -759 -258 -1724 N
ATOM 3844 CA VAL A 491 -22.177 19.301 39.976 1.00106.32 C
ANISOU 3844 CA VAL A 491 10566 14379 15451 -696 -204 -1826 C
ATOM 3845 C VAL A 491 -22.047 20.742 39.496 1.00104.56 C
ANISOU 3845 C VAL A 491 10419 14254 15054 -378 -379 -1866 C
ATOM 3846 O VAL A 491 -20.966 21.337 39.604 1.00104.98 O
ANISOU 3846 O VAL A 491 10771 14222 14897 -255 -389 -1724 O
ATOM 3847 CB VAL A 491 -22.377 19.214 41.496 1.00112.01 C
ANISOU 3847 CB VAL A 491 11234 15151 16175 -840 112 -1687 C
ATOM 3848 CG1 VAL A 491 -23.158 20.420 42.036 1.00122.59 C
ANISOU 3848 CG1 VAL A 491 12383 16723 17475 -663 179 -1785 C
ATOM 3849 CG2 VAL A 491 -23.065 17.908 41.890 1.00107.67 C
ANISOU 3849 CG2 VAL A 491 10475 14567 15868 -1172 265 -1680 C
ATOM 3850 N PRO A 492 -23.103 21.342 38.947 1.00101.94 N
ANISOU 3850 N PRO A 492 9823 14088 14820 -239 -534 -2048 N
ATOM 3851 CA PRO A 492 -22.972 22.706 38.412 1.00 95.34 C
ANISOU 3851 CA PRO A 492 9077 13302 13848 68 -740 -2057 C
ATOM 3852 C PRO A 492 -22.676 23.681 39.535 1.00 98.00 C
ANISOU 3852 C PRO A 492 9514 13636 14085 189 -567 -1961 C
ATOM 3853 O PRO A 492 -23.143 23.516 40.669 1.00101.82 O
ANISOU 3853 O PRO A 492 9845 14200 14641 82 -312 -1977 O
ATOM 3854 CB PRO A 492 -24.339 22.966 37.765 1.00 96.51 C
ANISOU 3854 CB PRO A 492 8858 13630 14181 166 -926 -2276 C
ATOM 3855 CG PRO A 492 -25.270 22.003 38.418 1.00107.23 C
ANISOU 3855 CG PRO A 492 9897 15074 15772 -84 -719 -2384 C
ATOM 3856 CD PRO A 492 -24.441 20.775 38.673 1.00107.89 C
ANISOU 3856 CD PRO A 492 10183 14978 15831 -357 -567 -2252 C
ATOM 3857 N HIS A 493 -21.865 24.686 39.234 1.00 87.44 N
ANISOU 3857 N HIS A 493 8439 12216 12569 394 -699 -1862 N
ATOM 3858 CA HIS A 493 -21.416 25.605 40.264 1.00 89.02 C
ANISOU 3858 CA HIS A 493 8775 12382 12667 500 -553 -1785 C
ATOM 3859 C HIS A 493 -21.706 27.043 39.885 1.00 88.84 C
ANISOU 3859 C HIS A 493 8740 12358 12655 802 -758 -1842 C
ATOM 3860 O HIS A 493 -21.408 27.484 38.772 1.00 86.45 O
ANISOU 3860 O HIS A 493 8565 11995 12286 929 -1029 -1788 O
ATOM 3861 CB HIS A 493 -19.928 25.425 40.580 1.00 97.45 C
ANISOU 3861 CB HIS A 493 10212 13295 13521 419 -465 -1577 C
ATOM 3862 CG HIS A 493 -19.678 24.334 41.567 1.00 88.92 C
ANISOU 3862 CG HIS A 493 9142 12204 12441 166 -196 -1495 C
ATOM 3863 ND1 HIS A 493 -18.450 24.105 42.157 1.00 83.06 N
ANISOU 3863 ND1 HIS A 493 8680 11348 11530 84 -81 -1312 N
ATOM 3864 CD2 HIS A 493 -20.520 23.397 42.071 1.00 92.51 C
ANISOU 3864 CD2 HIS A 493 9352 12747 13052 -35 -30 -1552 C
ATOM 3865 CE1 HIS A 493 -18.551 23.083 42.993 1.00 92.54 C
ANISOU 3865 CE1 HIS A 493 9823 12560 12778 -142 131 -1242 C
ATOM 3866 NE2 HIS A 493 -19.793 22.630 42.954 1.00 85.62 N
ANISOU 3866 NE2 HIS A 493 8635 11799 12098 -232 175 -1377 N
ATOM 3867 N ASP A 494 -22.353 27.740 40.810 1.00114.65 N
ANISOU 3867 N ASP A 494 11836 15706 16020 911 -631 -1961 N
ATOM 3868 CA ASP A 494 -22.731 29.141 40.691 1.00108.37 C
ANISOU 3868 CA ASP A 494 10996 14881 15300 1216 -799 -2048 C
ATOM 3869 C ASP A 494 -21.491 30.017 40.844 1.00109.87 C
ANISOU 3869 C ASP A 494 11563 14874 15309 1311 -839 -1884 C
ATOM 3870 O ASP A 494 -20.352 29.537 40.808 1.00119.09 O
ANISOU 3870 O ASP A 494 13011 15952 16285 1158 -781 -1704 O
ATOM 3871 CB ASP A 494 -23.810 29.450 41.719 1.00102.04 C
ANISOU 3871 CB ASP A 494 9856 14245 14669 1279 -607 -2276 C
ATOM 3872 CG ASP A 494 -24.680 30.623 41.329 1.00151.77 C
ANISOU 3872 CG ASP A 494 15952 20546 21168 1607 -838 -2446 C
ATOM 3873 OD1 ASP A 494 -24.402 31.234 40.291 1.00167.58 O
ANISOU 3873 OD1 ASP A 494 18110 22402 23159 1777 -1155 -2344 O
ATOM 3874 OD2 ASP A 494 -25.624 30.950 42.090 1.00172.62 O1-
ANISOU 3874 OD2 ASP A 494 18275 23338 23974 1697 -698 -2678 O1-
ATOM 3875 N GLU A 495 -21.705 31.322 40.998 1.00100.20 N
ANISOU 3875 N GLU A 495 10333 13569 14168 1569 -949 -1957 N
ATOM 3876 CA GLU A 495 -20.642 32.255 41.314 1.00114.22 C
ANISOU 3876 CA GLU A 495 12428 15150 15819 1653 -968 -1840 C
ATOM 3877 C GLU A 495 -20.606 32.583 42.799 1.00115.60 C
ANISOU 3877 C GLU A 495 12568 15372 15984 1648 -687 -1975 C
ATOM 3878 O GLU A 495 -19.871 33.489 43.205 1.00100.54 O
ANISOU 3878 O GLU A 495 10879 13309 14014 1739 -700 -1943 O
ATOM 3879 CB GLU A 495 -20.759 33.536 40.467 1.00111.87 C
ANISOU 3879 CB GLU A 495 12201 14677 15626 1931 -1303 -1806 C
ATOM 3880 CG GLU A 495 -20.634 33.254 38.985 1.00112.74 C
ANISOU 3880 CG GLU A 495 12396 14773 15667 1917 -1583 -1637 C
ATOM 3881 CD GLU A 495 -19.200 33.043 38.553 1.00115.80 C
ANISOU 3881 CD GLU A 495 13154 15056 15790 1760 -1592 -1385 C
ATOM 3882 OE1 GLU A 495 -18.272 33.571 39.200 1.00102.01 O
ANISOU 3882 OE1 GLU A 495 11636 13171 13954 1741 -1489 -1307 O
ATOM 3883 OE2 GLU A 495 -19.011 32.350 37.541 1.00132.86 O1-
ANISOU 3883 OE2 GLU A 495 15358 17289 17834 1655 -1707 -1288 O1-
ATOM 3884 N THR A 496 -21.394 31.869 43.612 1.00125.76 N
ANISOU 3884 N THR A 496 13577 16885 17322 1528 -434 -2128 N
ATOM 3885 CA THR A 496 -21.220 31.869 45.056 1.00120.11 C
ANISOU 3885 CA THR A 496 12854 16282 16501 1438 -121 -2214 C
ATOM 3886 C THR A 496 -20.026 31.039 45.483 1.00120.04 C
ANISOU 3886 C THR A 496 13126 16247 16236 1179 35 -1984 C
ATOM 3887 O THR A 496 -19.484 31.248 46.580 1.00129.40 O
ANISOU 3887 O THR A 496 14425 17473 17267 1125 226 -1992 O
ATOM 3888 CB THR A 496 -22.473 31.351 45.760 1.00117.63 C
ANISOU 3888 CB THR A 496 12139 16254 16303 1366 110 -2428 C
ATOM 3889 OG1 THR A 496 -22.763 30.025 45.297 1.00129.81 O
ANISOU 3889 OG1 THR A 496 13576 17886 17861 1127 148 -2322 O
ATOM 3890 CG2 THR A 496 -23.625 32.229 45.436 1.00112.97 C
ANISOU 3890 CG2 THR A 496 11243 15699 15982 1650 -41 -2686 C
ATOM 3891 N TYR A 497 -19.576 30.141 44.613 1.00105.68 N
ANISOU 3891 N TYR A 497 11423 14361 14371 1035 -64 -1794 N
ATOM 3892 CA TYR A 497 -18.434 29.279 44.858 1.00107.70 C
ANISOU 3892 CA TYR A 497 11928 14564 14427 814 42 -1577 C
ATOM 3893 C TYR A 497 -17.133 30.039 44.620 1.00105.21 C
ANISOU 3893 C TYR A 497 11954 14055 13967 894 -89 -1441 C
ATOM 3894 O TYR A 497 -17.099 31.068 43.942 1.00104.02 O
ANISOU 3894 O TYR A 497 11869 13776 13877 1090 -306 -1463 O
ATOM 3895 CB TYR A 497 -18.494 28.059 43.943 1.00111.13 C
ANISOU 3895 CB TYR A 497 12329 14986 14909 655 -30 -1480 C
ATOM 3896 CG TYR A 497 -19.567 27.048 44.287 1.00113.27 C
ANISOU 3896 CG TYR A 497 12297 15427 15315 485 134 -1567 C
ATOM 3897 CD1 TYR A 497 -20.869 27.198 43.822 1.00100.33 C
ANISOU 3897 CD1 TYR A 497 10333 13902 13886 576 52 -1759 C
ATOM 3898 CD2 TYR A 497 -19.264 25.911 45.022 1.00122.49 C
ANISOU 3898 CD2 TYR A 497 13498 16630 16414 224 352 -1439 C
ATOM 3899 CE1 TYR A 497 -21.852 26.261 44.121 1.00100.08 C
ANISOU 3899 CE1 TYR A 497 10002 14032 13991 391 208 -1841 C
ATOM 3900 CE2 TYR A 497 -20.233 24.971 45.318 1.00114.24 C
ANISOU 3900 CE2 TYR A 497 12182 15720 15506 34 503 -1490 C
ATOM 3901 CZ TYR A 497 -21.523 25.147 44.867 1.00101.89 C
ANISOU 3901 CZ TYR A 497 10283 14282 14149 107 440 -1698 C
ATOM 3902 OH TYR A 497 -22.481 24.204 45.168 1.00103.91 O
ANISOU 3902 OH TYR A 497 10250 14680 14553 -111 599 -1751 O
ATOM 3903 N CYS A 498 -16.054 29.517 45.190 1.00 99.83 N
ANISOU 3903 N CYS A 498 11483 13349 13100 733 36 -1284 N
ATOM 3904 CA CYS A 498 -14.710 30.026 44.942 1.00 97.52 C
ANISOU 3904 CA CYS A 498 11497 12893 12663 758 -71 -1140 C
ATOM 3905 C CYS A 498 -13.751 28.839 45.031 1.00 93.15 C
ANISOU 3905 C CYS A 498 11086 12329 11977 549 14 -952 C
ATOM 3906 O CYS A 498 -12.816 28.810 45.825 1.00101.25 O
ANISOU 3906 O CYS A 498 12276 13346 12849 475 112 -860 O
ATOM 3907 CB CYS A 498 -14.354 31.140 45.925 1.00 96.04 C
ANISOU 3907 CB CYS A 498 11403 12683 12406 854 -8 -1222 C
ATOM 3908 SG CYS A 498 -12.987 32.181 45.384 1.00106.08 S
ANISOU 3908 SG CYS A 498 12996 13722 13590 932 -207 -1094 S
ATOM 3909 N ASP A 499 -14.000 27.837 44.187 1.00 85.81 N
ANISOU 3909 N ASP A 499 10084 11398 11124 462 -42 -912 N
ATOM 3910 CA ASP A 499 -13.280 26.568 44.289 1.00 95.59 C
ANISOU 3910 CA ASP A 499 11409 12606 12303 274 38 -768 C
ATOM 3911 C ASP A 499 -11.766 26.676 44.126 1.00 94.77 C
ANISOU 3911 C ASP A 499 11573 12393 12043 263 -21 -622 C
ATOM 3912 O ASP A 499 -11.054 25.928 44.818 1.00 97.11 O
ANISOU 3912 O ASP A 499 11957 12678 12264 138 91 -504 O
ATOM 3913 CB ASP A 499 -13.858 25.574 43.277 1.00 86.43 C
ANISOU 3913 CB ASP A 499 10112 11439 11287 204 -44 -806 C
ATOM 3914 CG ASP A 499 -15.348 25.401 43.433 1.00101.69 C
ANISOU 3914 CG ASP A 499 11749 13495 13393 191 15 -955 C
ATOM 3915 OD1 ASP A 499 -15.870 25.741 44.515 1.00 92.42 O
ANISOU 3915 OD1 ASP A 499 10471 12430 12214 187 182 -1006 O
ATOM 3916 OD2 ASP A 499 -15.996 24.944 42.468 1.00108.55 O1-
ANISOU 3916 OD2 ASP A 499 12475 14373 14394 182 -105 -1040 O1-
ATOM 3917 N PRO A 500 -11.201 27.552 43.256 1.00 80.42 N
ANISOU 3917 N PRO A 500 9886 10498 10171 379 -196 -608 N
ATOM 3918 CA PRO A 500 -9.740 27.723 43.245 1.00 73.82 C
ANISOU 3918 CA PRO A 500 9277 9587 9183 350 -222 -478 C
ATOM 3919 C PRO A 500 -9.176 28.018 44.625 1.00 84.33 C
ANISOU 3919 C PRO A 500 10696 10938 10407 314 -83 -438 C
ATOM 3920 O PRO A 500 -8.056 27.595 44.914 1.00 89.16 O
ANISOU 3920 O PRO A 500 11438 11524 10914 234 -53 -322 O
ATOM 3921 CB PRO A 500 -9.524 28.901 42.289 1.00 75.38 C
ANISOU 3921 CB PRO A 500 9568 9722 9353 475 -409 -475 C
ATOM 3922 CG PRO A 500 -10.867 29.538 42.164 1.00 75.93 C
ANISOU 3922 CG PRO A 500 9474 9814 9561 603 -471 -604 C
ATOM 3923 CD PRO A 500 -11.832 28.409 42.247 1.00 81.91 C
ANISOU 3923 CD PRO A 500 10020 10670 10431 528 -382 -684 C
ATOM 3924 N ALA A 501 -9.951 28.691 45.478 1.00 93.68 N
ANISOU 3924 N ALA A 501 11791 12188 11614 374 -2 -550 N
ATOM 3925 CA ALA A 501 -9.597 28.937 46.862 1.00 88.77 C
ANISOU 3925 CA ALA A 501 11223 11640 10866 334 143 -552 C
ATOM 3926 C ALA A 501 -9.840 27.738 47.812 1.00 88.46 C
ANISOU 3926 C ALA A 501 11105 11725 10780 174 331 -478 C
ATOM 3927 O ALA A 501 -9.397 27.809 48.973 1.00 95.53 O
ANISOU 3927 O ALA A 501 12068 12712 11518 116 444 -440 O
ATOM 3928 CB ALA A 501 -10.356 30.160 47.401 1.00 93.08 C
ANISOU 3928 CB ALA A 501 11690 12225 11451 470 163 -744 C
ATOM 3929 N SER A 502 -10.482 26.636 47.366 1.00 73.73 N
ANISOU 3929 N SER A 502 9110 9865 9041 87 358 -444 N
ATOM 3930 CA SER A 502 -10.529 25.413 48.153 1.00 74.64 C
ANISOU 3930 CA SER A 502 9188 10039 9131 -92 508 -311 C
ATOM 3931 C SER A 502 -9.169 24.740 48.269 1.00 81.47 C
ANISOU 3931 C SER A 502 10243 10806 9907 -165 469 -117 C
ATOM 3932 O SER A 502 -9.021 23.783 49.044 1.00 84.63 O
ANISOU 3932 O SER A 502 10654 11229 10272 -306 571 38 O
ATOM 3933 CB SER A 502 -11.525 24.385 47.552 1.00 78.78 C
ANISOU 3933 CB SER A 502 9526 10547 9860 -182 524 -331 C
ATOM 3934 OG SER A 502 -11.031 23.832 46.342 1.00112.22 O
ANISOU 3934 OG SER A 502 13819 14625 14194 -172 367 -303 O
ATOM 3935 N LEU A 503 -8.181 25.203 47.525 1.00 97.26 N
ANISOU 3935 N LEU A 503 12380 12700 11873 -78 322 -111 N
ATOM 3936 CA LEU A 503 -6.825 24.718 47.667 1.00 84.06 C
ANISOU 3936 CA LEU A 503 10863 10959 10118 -122 281 40 C
ATOM 3937 C LEU A 503 -6.023 25.681 48.533 1.00 91.57 C
ANISOU 3937 C LEU A 503 11940 11978 10874 -86 290 52 C
ATOM 3938 O LEU A 503 -6.188 26.901 48.457 1.00 91.13 O
ANISOU 3938 O LEU A 503 11900 11941 10783 10 255 -77 O
ATOM 3939 CB LEU A 503 -6.164 24.548 46.294 1.00 83.46 C
ANISOU 3939 CB LEU A 503 10833 10761 10116 -70 131 24 C
ATOM 3940 CG LEU A 503 -4.720 24.046 46.270 1.00 89.27 C
ANISOU 3940 CG LEU A 503 11690 11430 10798 -92 78 141 C
ATOM 3941 CD1 LEU A 503 -4.636 22.636 46.826 1.00 94.93 C
ANISOU 3941 CD1 LEU A 503 12384 12086 11598 -194 134 274 C
ATOM 3942 CD2 LEU A 503 -4.128 24.096 44.835 1.00 85.85 C
ANISOU 3942 CD2 LEU A 503 11280 10937 10403 -35 -49 76 C
ATOM 3943 N PHE A 504 -5.154 25.097 49.374 1.00 85.17 N
ANISOU 3943 N PHE A 504 11217 11192 9952 -164 322 208 N
ATOM 3944 CA PHE A 504 -4.300 25.843 50.303 1.00 85.55 C
ANISOU 3944 CA PHE A 504 11380 11328 9798 -154 321 225 C
ATOM 3945 C PHE A 504 -3.614 27.026 49.609 1.00 87.58 C
ANISOU 3945 C PHE A 504 11718 11514 10044 -56 198 119 C
ATOM 3946 O PHE A 504 -3.796 28.195 49.987 1.00 93.69 O
ANISOU 3946 O PHE A 504 12514 12332 10752 -2 202 -13 O
ATOM 3947 CB PHE A 504 -3.305 24.883 50.959 1.00 86.08 C
ANISOU 3947 CB PHE A 504 11525 11398 9784 -235 308 433 C
ATOM 3948 CG PHE A 504 -2.278 25.573 51.805 1.00 84.26 C
ANISOU 3948 CG PHE A 504 11406 11264 9346 -228 271 449 C
ATOM 3949 CD1 PHE A 504 -2.520 25.824 53.131 1.00 71.31 C
ANISOU 3949 CD1 PHE A 504 9780 9815 7500 -283 368 459 C
ATOM 3950 CD2 PHE A 504 -1.039 25.928 51.271 1.00 87.13 C
ANISOU 3950 CD2 PHE A 504 11845 11551 9710 -181 139 448 C
ATOM 3951 CE1 PHE A 504 -1.586 26.483 53.926 1.00 97.65 C
ANISOU 3951 CE1 PHE A 504 13210 13259 10632 -281 319 444 C
ATOM 3952 CE2 PHE A 504 -0.090 26.579 52.071 1.00 83.00 C
ANISOU 3952 CE2 PHE A 504 11406 11124 9007 -189 94 446 C
ATOM 3953 CZ PHE A 504 -0.367 26.854 53.395 1.00 99.43 C
ANISOU 3953 CZ PHE A 504 13507 13387 10885 -235 174 438 C
ATOM 3954 N HIS A 505 -2.854 26.730 48.560 1.00 75.80 N
ANISOU 3954 N HIS A 505 10262 9910 8628 -40 90 166 N
ATOM 3955 CA HIS A 505 -1.952 27.681 47.920 1.00 75.00 C
ANISOU 3955 CA HIS A 505 10248 9756 8494 5 -20 127 C
ATOM 3956 C HIS A 505 -2.657 28.937 47.390 1.00 87.66 C
ANISOU 3956 C HIS A 505 11847 11314 10145 85 -65 -6 C
ATOM 3957 O HIS A 505 -2.049 30.021 47.323 1.00 94.35 O
ANISOU 3957 O HIS A 505 12782 12117 10948 105 -135 -40 O
ATOM 3958 CB HIS A 505 -1.211 26.971 46.776 1.00 75.88 C
ANISOU 3958 CB HIS A 505 10358 9797 8677 -2 -97 185 C
ATOM 3959 CG HIS A 505 -0.483 25.738 47.222 1.00 79.54 C
ANISOU 3959 CG HIS A 505 10816 10259 9146 -50 -82 305 C
ATOM 3960 ND1 HIS A 505 -1.147 24.557 47.486 1.00 77.84 N
ANISOU 3960 ND1 HIS A 505 10534 10014 9029 -88 -23 366 N
ATOM 3961 CD2 HIS A 505 0.830 25.497 47.476 1.00 81.00 C
ANISOU 3961 CD2 HIS A 505 11046 10456 9276 -64 -132 382 C
ATOM 3962 CE1 HIS A 505 -0.277 23.642 47.881 1.00 81.24 C
ANISOU 3962 CE1 HIS A 505 10984 10411 9472 -113 -48 489 C
ATOM 3963 NE2 HIS A 505 0.928 24.185 47.883 1.00 88.79 N
ANISOU 3963 NE2 HIS A 505 11999 11403 10334 -88 -116 492 N
ATOM 3964 N VAL A 506 -3.928 28.822 46.998 1.00 90.16 N
ANISOU 3964 N VAL A 506 12057 11625 10574 131 -40 -79 N
ATOM 3965 CA VAL A 506 -4.651 29.977 46.472 1.00 91.24 C
ANISOU 3965 CA VAL A 506 12177 11703 10786 234 -112 -195 C
ATOM 3966 C VAL A 506 -5.217 30.829 47.599 1.00 88.29 C
ANISOU 3966 C VAL A 506 11782 11378 10386 284 -40 -330 C
ATOM 3967 O VAL A 506 -5.115 32.058 47.567 1.00 88.11 O
ANISOU 3967 O VAL A 506 11822 11269 10387 358 -117 -416 O
ATOM 3968 CB VAL A 506 -5.750 29.506 45.503 1.00 83.45 C
ANISOU 3968 CB VAL A 506 11062 10707 9938 276 -144 -233 C
ATOM 3969 CG1 VAL A 506 -6.591 30.683 45.047 1.00 74.54 C
ANISOU 3969 CG1 VAL A 506 9900 9519 8905 406 -239 -342 C
ATOM 3970 CG2 VAL A 506 -5.134 28.778 44.314 1.00 79.79 C
ANISOU 3970 CG2 VAL A 506 10626 10212 9481 234 -226 -147 C
ATOM 3971 N SER A 507 -5.823 30.203 48.613 1.00 87.11 N
ANISOU 3971 N SER A 507 11540 11368 10190 239 111 -358 N
ATOM 3972 CA SER A 507 -6.374 30.981 49.719 1.00 88.33 C
ANISOU 3972 CA SER A 507 11653 11620 10288 284 204 -524 C
ATOM 3973 C SER A 507 -5.337 31.324 50.783 1.00 97.04 C
ANISOU 3973 C SER A 507 12882 12793 11198 226 230 -517 C
ATOM 3974 O SER A 507 -5.663 32.054 51.726 1.00 95.60 O
ANISOU 3974 O SER A 507 12679 12705 10942 262 300 -690 O
ATOM 3975 CB SER A 507 -7.546 30.241 50.370 1.00 79.33 C
ANISOU 3975 CB SER A 507 10339 10652 9152 242 376 -569 C
ATOM 3976 OG SER A 507 -7.154 28.957 50.813 1.00 75.95 O
ANISOU 3976 OG SER A 507 9928 10305 8626 92 460 -377 O
ATOM 3977 N ASN A 508 -4.110 30.818 50.661 1.00 88.50 N
ANISOU 3977 N ASN A 508 11911 11682 10033 142 171 -347 N
ATOM 3978 CA ASN A 508 -3.007 31.214 51.529 1.00 81.92 C
ANISOU 3978 CA ASN A 508 11190 10906 9028 91 152 -342 C
ATOM 3979 C ASN A 508 -1.964 32.042 50.786 1.00 84.89 C
ANISOU 3979 C ASN A 508 11678 11121 9455 105 -3 -334 C
ATOM 3980 O ASN A 508 -0.842 32.206 51.276 1.00107.64 O
ANISOU 3980 O ASN A 508 14642 14038 12219 42 -46 -299 O
ATOM 3981 CB ASN A 508 -2.364 29.987 52.175 1.00 87.97 C
ANISOU 3981 CB ASN A 508 11976 11795 9652 -20 200 -148 C
ATOM 3982 CG ASN A 508 -3.250 29.359 53.232 1.00 78.58 C
ANISOU 3982 CG ASN A 508 10704 10800 8351 -75 364 -136 C
ATOM 3983 OD1 ASN A 508 -3.125 29.656 54.420 1.00 81.46 O
ANISOU 3983 OD1 ASN A 508 11094 11345 8509 -113 430 -190 O
ATOM 3984 ND2 ASN A 508 -4.165 28.500 52.803 1.00 77.81 N
ANISOU 3984 ND2 ASN A 508 10500 10686 8377 -96 434 -71 N
ATOM 3985 N ASP A 509 -2.315 32.549 49.602 1.00 77.89 N
ANISOU 3985 N ASP A 509 10788 10074 8733 174 -91 -352 N
ATOM 3986 CA ASP A 509 -1.546 33.578 48.902 1.00 74.28 C
ANISOU 3986 CA ASP A 509 10435 9456 8333 177 -229 -348 C
ATOM 3987 C ASP A 509 -0.117 33.109 48.614 1.00 80.41 C
ANISOU 3987 C ASP A 509 11275 10254 9025 69 -275 -195 C
ATOM 3988 O ASP A 509 0.868 33.693 49.068 1.00100.36 O
ANISOU 3988 O ASP A 509 13873 12774 11483 8 -320 -213 O
ATOM 3989 CB ASP A 509 -1.565 34.887 49.702 1.00 68.78 C
ANISOU 3989 CB ASP A 509 9791 8702 7641 216 -253 -536 C
ATOM 3990 CG ASP A 509 -0.989 36.057 48.930 1.00 85.72 C
ANISOU 3990 CG ASP A 509 12042 10628 9901 213 -405 -525 C
ATOM 3991 OD1 ASP A 509 -1.401 36.268 47.771 1.00 89.69 O
ANISOU 3991 OD1 ASP A 509 12546 11000 10531 262 -487 -447 O
ATOM 3992 OD2 ASP A 509 -0.133 36.775 49.490 1.00107.73 O1-
ANISOU 3992 OD2 ASP A 509 14910 13375 12646 149 -448 -588 O1-
ATOM 3993 N TYR A 510 -0.024 32.030 47.839 1.00 79.30 N
ANISOU 3993 N TYR A 510 11086 10139 8904 49 -266 -70 N
ATOM 3994 CA TYR A 510 1.247 31.460 47.413 1.00 81.14 C
ANISOU 3994 CA TYR A 510 11339 10401 9088 -27 -303 49 C
ATOM 3995 C TYR A 510 1.253 31.354 45.896 1.00 86.67 C
ANISOU 3995 C TYR A 510 12026 11042 9862 -21 -361 105 C
ATOM 3996 O TYR A 510 0.297 30.840 45.306 1.00 94.24 O
ANISOU 3996 O TYR A 510 12923 11992 10892 32 -346 95 O
ATOM 3997 CB TYR A 510 1.470 30.073 48.026 1.00 80.74 C
ANISOU 3997 CB TYR A 510 11233 10457 8987 -52 -237 131 C
ATOM 3998 CG TYR A 510 1.931 30.081 49.466 1.00 97.40 C
ANISOU 3998 CG TYR A 510 13373 12675 10960 -90 -208 132 C
ATOM 3999 CD1 TYR A 510 3.245 30.383 49.797 1.00112.07 C
ANISOU 3999 CD1 TYR A 510 15273 14573 12735 -145 -277 156 C
ATOM 4000 CD2 TYR A 510 1.051 29.771 50.494 1.00 95.09 C
ANISOU 4000 CD2 TYR A 510 13053 12474 10602 -82 -113 108 C
ATOM 4001 CE1 TYR A 510 3.666 30.387 51.116 1.00114.79 C
ANISOU 4001 CE1 TYR A 510 15642 15044 12929 -179 -274 152 C
ATOM 4002 CE2 TYR A 510 1.462 29.771 51.813 1.00 95.68 C
ANISOU 4002 CE2 TYR A 510 13161 12691 10503 -126 -90 117 C
ATOM 4003 CZ TYR A 510 2.770 30.080 52.119 1.00109.85 C
ANISOU 4003 CZ TYR A 510 15006 14521 12211 -169 -182 138 C
ATOM 4004 OH TYR A 510 3.186 30.082 53.430 1.00119.89 O
ANISOU 4004 OH TYR A 510 16307 15959 13285 -213 -182 142 O
ATOM 4005 N SER A 511 2.321 31.839 45.267 1.00 78.21 N
ANISOU 4005 N SER A 511 11004 9955 8758 -89 -424 159 N
ATOM 4006 CA SER A 511 2.469 31.649 43.831 1.00 73.95 C
ANISOU 4006 CA SER A 511 10447 9420 8230 -106 -464 219 C
ATOM 4007 C SER A 511 2.601 30.163 43.524 1.00 79.20 C
ANISOU 4007 C SER A 511 11016 10175 8902 -93 -412 228 C
ATOM 4008 O SER A 511 3.321 29.432 44.209 1.00 87.95 O
ANISOU 4008 O SER A 511 12090 11336 9990 -111 -377 245 O
ATOM 4009 CB SER A 511 3.684 32.415 43.306 1.00 72.74 C
ANISOU 4009 CB SER A 511 10348 9270 8019 -214 -515 284 C
ATOM 4010 OG SER A 511 4.892 31.849 43.780 1.00 85.33 O
ANISOU 4010 OG SER A 511 11896 10966 9558 -274 -483 294 O
ATOM 4011 N PHE A 512 1.886 29.713 42.492 1.00 81.92 N
ANISOU 4011 N PHE A 512 11314 10526 9286 -56 -425 212 N
ATOM 4012 CA PHE A 512 1.775 28.294 42.185 1.00 72.47 C
ANISOU 4012 CA PHE A 512 10021 9374 8141 -34 -385 180 C
ATOM 4013 C PHE A 512 2.565 27.856 40.960 1.00 73.20 C
ANISOU 4013 C PHE A 512 10070 9555 8187 -65 -403 163 C
ATOM 4014 O PHE A 512 2.722 26.648 40.752 1.00 70.71 O
ANISOU 4014 O PHE A 512 9671 9262 7935 -43 -375 107 O
ATOM 4015 CB PHE A 512 0.302 27.910 41.986 1.00 68.07 C
ANISOU 4015 CB PHE A 512 9407 8779 7677 26 -380 123 C
ATOM 4016 CG PHE A 512 0.004 26.473 42.298 1.00 72.90 C
ANISOU 4016 CG PHE A 512 9930 9379 8390 32 -323 96 C
ATOM 4017 CD1 PHE A 512 0.018 26.015 43.603 1.00 74.56 C
ANISOU 4017 CD1 PHE A 512 10141 9563 8626 18 -258 148 C
ATOM 4018 CD2 PHE A 512 -0.287 25.578 41.282 1.00 76.89 C
ANISOU 4018 CD2 PHE A 512 10356 9896 8964 41 -343 22 C
ATOM 4019 CE1 PHE A 512 -0.257 24.688 43.890 1.00 79.21 C
ANISOU 4019 CE1 PHE A 512 10661 10108 9328 5 -217 163 C
ATOM 4020 CE2 PHE A 512 -0.561 24.253 41.561 1.00 78.17 C
ANISOU 4020 CE2 PHE A 512 10440 9998 9262 36 -304 -5 C
ATOM 4021 CZ PHE A 512 -0.546 23.807 42.865 1.00 77.36 C
ANISOU 4021 CZ PHE A 512 10348 9839 9206 14 -242 84 C
ATOM 4022 N ILE A 513 3.065 28.790 40.147 1.00 65.59 N
ANISOU 4022 N ILE A 513 9159 8644 7120 -123 -445 206 N
ATOM 4023 CA ILE A 513 3.762 28.403 38.926 1.00 67.05 C
ANISOU 4023 CA ILE A 513 9288 8969 7218 -166 -440 177 C
ATOM 4024 C ILE A 513 5.082 27.703 39.222 1.00 82.08 C
ANISOU 4024 C ILE A 513 11113 10947 9126 -190 -386 141 C
ATOM 4025 O ILE A 513 5.628 27.027 38.342 1.00 88.26 O
ANISOU 4025 O ILE A 513 11805 11856 9875 -195 -359 57 O
ATOM 4026 CB ILE A 513 3.989 29.630 38.023 1.00 76.27 C
ANISOU 4026 CB ILE A 513 10538 10192 8250 -252 -492 275 C
ATOM 4027 CG1 ILE A 513 4.256 29.195 36.579 1.00 69.67 C
ANISOU 4027 CG1 ILE A 513 9641 9548 7283 -291 -486 232 C
ATOM 4028 CG2 ILE A 513 5.134 30.481 38.550 1.00 78.20 C
ANISOU 4028 CG2 ILE A 513 10832 10429 8453 -353 -480 358 C
ATOM 4029 CD1 ILE A 513 3.143 28.366 35.977 1.00 71.26 C
ANISOU 4029 CD1 ILE A 513 9783 9769 7523 -204 -516 122 C
ATOM 4030 N ARG A 514 5.604 27.834 40.447 1.00 89.16 N
ANISOU 4030 N ARG A 514 12030 11785 10063 -194 -377 186 N
ATOM 4031 CA ARG A 514 6.889 27.224 40.777 1.00 83.38 C
ANISOU 4031 CA ARG A 514 11209 11125 9348 -202 -355 161 C
ATOM 4032 C ARG A 514 6.856 25.715 40.566 1.00 82.46 C
ANISOU 4032 C ARG A 514 10981 11000 9351 -110 -336 63 C
ATOM 4033 O ARG A 514 7.841 25.123 40.111 1.00 90.42 O
ANISOU 4033 O ARG A 514 11876 12104 10375 -97 -319 -17 O
ATOM 4034 CB ARG A 514 7.277 27.555 42.220 1.00 74.94 C
ANISOU 4034 CB ARG A 514 10182 9998 8292 -210 -375 227 C
ATOM 4035 CG ARG A 514 6.475 26.799 43.273 1.00 85.94 C
ANISOU 4035 CG ARG A 514 11592 11288 9772 -131 -372 248 C
ATOM 4036 CD ARG A 514 5.985 27.700 44.383 1.00 90.20 C
ANISOU 4036 CD ARG A 514 12234 11778 10259 -154 -380 296 C
ATOM 4037 NE ARG A 514 7.087 28.254 45.158 1.00 94.85 N
ANISOU 4037 NE ARG A 514 12835 12425 10778 -209 -416 321 N
ATOM 4038 CZ ARG A 514 6.957 29.222 46.054 1.00102.73 C
ANISOU 4038 CZ ARG A 514 13917 13405 11712 -247 -434 320 C
ATOM 4039 NH1 ARG A 514 5.779 29.757 46.328 1.00 84.79 N
ANISOU 4039 NH1 ARG A 514 11717 11059 9442 -220 -412 292 N
ATOM 4040 NH2 ARG A 514 8.036 29.660 46.695 1.00122.28 N
ANISOU 4040 NH2 ARG A 514 16386 15947 14127 -308 -481 322 N
ATOM 4041 N TYR A 515 5.721 25.080 40.870 1.00 71.29 N
ANISOU 4041 N TYR A 515 9582 9464 8039 -49 -339 54 N
ATOM 4042 CA TYR A 515 5.618 23.634 40.729 1.00 72.81 C
ANISOU 4042 CA TYR A 515 9681 9593 8391 25 -335 -33 C
ATOM 4043 C TYR A 515 5.727 23.217 39.270 1.00 80.41 C
ANISOU 4043 C TYR A 515 10557 10659 9335 35 -324 -196 C
ATOM 4044 O TYR A 515 6.223 22.126 38.969 1.00 81.70 O
ANISOU 4044 O TYR A 515 10612 10810 9620 97 -322 -321 O
ATOM 4045 CB TYR A 515 4.300 23.156 41.337 1.00 72.49 C
ANISOU 4045 CB TYR A 515 9675 9407 8462 48 -332 6 C
ATOM 4046 CG TYR A 515 4.139 23.556 42.787 1.00 73.53 C
ANISOU 4046 CG TYR A 515 9885 9485 8568 29 -324 150 C
ATOM 4047 CD1 TYR A 515 4.761 22.843 43.803 1.00 97.21 C
ANISOU 4047 CD1 TYR A 515 12872 12432 11630 51 -339 238 C
ATOM 4048 CD2 TYR A 515 3.384 24.668 43.138 1.00 81.61 C
ANISOU 4048 CD2 TYR A 515 10990 10522 9495 -4 -310 190 C
ATOM 4049 CE1 TYR A 515 4.619 23.215 45.128 1.00 98.53 C
ANISOU 4049 CE1 TYR A 515 13112 12600 11724 22 -332 365 C
ATOM 4050 CE2 TYR A 515 3.238 25.049 44.458 1.00 79.42 C
ANISOU 4050 CE2 TYR A 515 10774 10233 9170 -21 -292 278 C
ATOM 4051 CZ TYR A 515 3.857 24.319 45.449 1.00 82.72 C
ANISOU 4051 CZ TYR A 515 11184 10637 9608 -17 -298 366 C
ATOM 4052 OH TYR A 515 3.715 24.693 46.765 1.00 92.79 O
ANISOU 4052 OH TYR A 515 12521 11946 10789 -44 -280 449 O
ATOM 4053 N TYR A 516 5.278 24.074 38.355 1.00 75.10 N
ANISOU 4053 N TYR A 516 9930 10094 8512 -20 -327 -203 N
ATOM 4054 CA TYR A 516 5.497 23.834 36.934 1.00 75.88 C
ANISOU 4054 CA TYR A 516 9953 10362 8516 -33 -314 -349 C
ATOM 4055 C TYR A 516 6.963 24.033 36.567 1.00 78.13 C
ANISOU 4055 C TYR A 516 10164 10825 8696 -78 -266 -382 C
ATOM 4056 O TYR A 516 7.603 23.140 36.000 1.00 77.67 O
ANISOU 4056 O TYR A 516 9971 10860 8680 -32 -232 -561 O
ATOM 4057 CB TYR A 516 4.597 24.758 36.111 1.00 73.77 C
ANISOU 4057 CB TYR A 516 9768 10171 8092 -86 -354 -298 C
ATOM 4058 CG TYR A 516 4.651 24.525 34.618 1.00 75.63 C
ANISOU 4058 CG TYR A 516 9938 10619 8177 -111 -352 -438 C
ATOM 4059 CD1 TYR A 516 5.585 25.184 33.829 1.00 83.30 C
ANISOU 4059 CD1 TYR A 516 10905 11817 8928 -206 -313 -407 C
ATOM 4060 CD2 TYR A 516 3.771 23.650 33.997 1.00 71.63 C
ANISOU 4060 CD2 TYR A 516 9369 10110 7736 -57 -386 -606 C
ATOM 4061 CE1 TYR A 516 5.640 24.983 32.468 1.00 86.57 C
ANISOU 4061 CE1 TYR A 516 11259 12478 9156 -242 -300 -534 C
ATOM 4062 CE2 TYR A 516 3.818 23.441 32.633 1.00 72.82 C
ANISOU 4062 CE2 TYR A 516 9459 10493 7716 -82 -390 -760 C
ATOM 4063 CZ TYR A 516 4.756 24.111 31.874 1.00 83.44 C
ANISOU 4063 CZ TYR A 516 10806 12090 8807 -173 -343 -720 C
ATOM 4064 OH TYR A 516 4.813 23.910 30.515 1.00 90.97 O
ANISOU 4064 OH TYR A 516 11697 13324 9541 -212 -335 -872 O
ATOM 4065 N THR A 517 7.512 25.207 36.889 1.00 77.33 N
ANISOU 4065 N THR A 517 10135 10774 8473 -171 -261 -230 N
ATOM 4066 CA THR A 517 8.878 25.530 36.488 1.00 81.06 C
ANISOU 4066 CA THR A 517 10522 11444 8834 -251 -206 -250 C
ATOM 4067 C THR A 517 9.880 24.558 37.098 1.00 93.82 C
ANISOU 4067 C THR A 517 11993 13047 10609 -163 -190 -353 C
ATOM 4068 O THR A 517 10.783 24.067 36.411 1.00100.04 O
ANISOU 4068 O THR A 517 12622 14011 11376 -153 -134 -509 O
ATOM 4069 CB THR A 517 9.216 26.966 36.888 1.00 81.60 C
ANISOU 4069 CB THR A 517 10700 11511 8794 -382 -221 -59 C
ATOM 4070 OG1 THR A 517 9.089 27.109 38.309 1.00 80.68 O
ANISOU 4070 OG1 THR A 517 10649 11204 8803 -339 -267 24 O
ATOM 4071 CG2 THR A 517 8.287 27.951 36.191 1.00 86.01 C
ANISOU 4071 CG2 THR A 517 11398 12062 9219 -454 -260 57 C
ATOM 4072 N ARG A 518 9.734 24.268 38.394 1.00 95.42 N
ANISOU 4072 N ARG A 518 12237 13052 10965 -95 -244 -270 N
ATOM 4073 CA ARG A 518 10.662 23.363 39.064 1.00 85.86 C
ANISOU 4073 CA ARG A 518 10902 11806 9916 2 -266 -326 C
ATOM 4074 C ARG A 518 10.642 21.972 38.445 1.00 97.09 C
ANISOU 4074 C ARG A 518 12192 13196 11501 128 -260 -529 C
ATOM 4075 O ARG A 518 11.678 21.298 38.398 1.00100.64 O
ANISOU 4075 O ARG A 518 12479 13701 12059 209 -261 -653 O
ATOM 4076 CB ARG A 518 10.329 23.287 40.554 1.00 84.55 C
ANISOU 4076 CB ARG A 518 10830 11446 9847 41 -337 -167 C
ATOM 4077 CG ARG A 518 11.072 22.204 41.306 1.00 99.96 C
ANISOU 4077 CG ARG A 518 12677 13318 11987 162 -398 -181 C
ATOM 4078 CD ARG A 518 10.128 21.415 42.194 1.00107.15 C
ANISOU 4078 CD ARG A 518 13674 13998 13040 229 -449 -76 C
ATOM 4079 NE ARG A 518 9.404 20.393 41.448 1.00114.45 N
ANISOU 4079 NE ARG A 518 14560 14808 14117 294 -434 -203 N
ATOM 4080 CZ ARG A 518 8.394 19.686 41.935 1.00131.35 C
ANISOU 4080 CZ ARG A 518 16766 16747 16393 318 -457 -132 C
ATOM 4081 NH1 ARG A 518 7.975 19.846 43.180 1.00131.89 N
ANISOU 4081 NH1 ARG A 518 16941 16729 16440 286 -483 74 N
ATOM 4082 NH2 ARG A 518 7.789 18.795 41.154 1.00132.51 N
ANISOU 4082 NH2 ARG A 518 16862 16793 16691 359 -449 -280 N
ATOM 4083 N THR A 519 9.483 21.529 37.955 1.00 83.03 N
ANISOU 4083 N THR A 519 10464 11323 9760 153 -263 -590 N
ATOM 4084 CA THR A 519 9.395 20.203 37.352 1.00 79.71 C
ANISOU 4084 CA THR A 519 9923 10842 9520 264 -268 -815 C
ATOM 4085 C THR A 519 10.195 20.126 36.057 1.00 80.82 C
ANISOU 4085 C THR A 519 9910 11253 9544 258 -194 -1053 C
ATOM 4086 O THR A 519 10.930 19.156 35.834 1.00 82.64 O
ANISOU 4086 O THR A 519 9974 11488 9938 373 -190 -1261 O
ATOM 4087 CB THR A 519 7.933 19.842 37.103 1.00 86.33 C
ANISOU 4087 CB THR A 519 10844 11539 10417 262 -292 -835 C
ATOM 4088 OG1 THR A 519 7.237 19.784 38.355 1.00 77.91 O
ANISOU 4088 OG1 THR A 519 9888 10245 9467 264 -338 -631 O
ATOM 4089 CG2 THR A 519 7.831 18.503 36.405 1.00 84.75 C
ANISOU 4089 CG2 THR A 519 10519 11267 10416 360 -305 -1102 C
ATOM 4090 N LEU A 520 10.062 21.131 35.189 1.00 88.21 N
ANISOU 4090 N LEU A 520 10895 12424 10198 127 -136 -1027 N
ATOM 4091 CA LEU A 520 10.870 21.163 33.976 1.00 93.78 C
ANISOU 4091 CA LEU A 520 11453 13449 10729 87 -44 -1226 C
ATOM 4092 C LEU A 520 12.348 21.335 34.299 1.00 96.73 C
ANISOU 4092 C LEU A 520 11682 13960 11110 80 7 -1237 C
ATOM 4093 O LEU A 520 13.206 20.853 33.551 1.00 96.90 O
ANISOU 4093 O LEU A 520 11504 14202 11111 115 85 -1480 O
ATOM 4094 CB LEU A 520 10.395 22.286 33.051 1.00103.99 C
ANISOU 4094 CB LEU A 520 12855 14961 11697 -77 -8 -1122 C
ATOM 4095 CG LEU A 520 9.326 21.947 32.007 1.00101.49 C
ANISOU 4095 CG LEU A 520 12568 14710 11283 -70 -29 -1259 C
ATOM 4096 CD1 LEU A 520 8.026 21.504 32.666 1.00 93.61 C
ANISOU 4096 CD1 LEU A 520 11676 13394 10498 9 -131 -1205 C
ATOM 4097 CD2 LEU A 520 9.079 23.126 31.078 1.00 89.75 C
ANISOU 4097 CD2 LEU A 520 11179 13474 9447 -235 -10 -1116 C
ATOM 4098 N TYR A 521 12.659 22.010 35.408 1.00 99.61 N
ANISOU 4098 N TYR A 521 12125 14216 11505 36 -38 -1003 N
ATOM 4099 CA TYR A 521 14.050 22.215 35.799 1.00 87.51 C
ANISOU 4099 CA TYR A 521 10443 12815 9991 20 -12 -1008 C
ATOM 4100 C TYR A 521 14.734 20.898 36.145 1.00 84.39 C
ANISOU 4100 C TYR A 521 9854 12331 9879 224 -55 -1202 C
ATOM 4101 O TYR A 521 15.854 20.632 35.695 1.00 93.44 O
ANISOU 4101 O TYR A 521 10772 13691 11040 258 8 -1393 O
ATOM 4102 CB TYR A 521 14.121 23.179 36.985 1.00 80.43 C
ANISOU 4102 CB TYR A 521 9683 11801 9076 -66 -78 -736 C
ATOM 4103 CG TYR A 521 13.848 24.627 36.644 1.00 79.44 C
ANISOU 4103 CG TYR A 521 9704 11775 8705 -273 -40 -559 C
ATOM 4104 CD1 TYR A 521 14.040 25.110 35.356 1.00 80.16 C
ANISOU 4104 CD1 TYR A 521 9754 12130 8572 -406 62 -609 C
ATOM 4105 CD2 TYR A 521 13.389 25.509 37.613 1.00 79.84 C
ANISOU 4105 CD2 TYR A 521 9937 11651 8747 -337 -111 -342 C
ATOM 4106 CE1 TYR A 521 13.793 26.435 35.048 1.00 79.85 C
ANISOU 4106 CE1 TYR A 521 9864 12143 8333 -599 73 -407 C
ATOM 4107 CE2 TYR A 521 13.136 26.832 37.313 1.00 83.68 C
ANISOU 4107 CE2 TYR A 521 10560 12175 9059 -511 -98 -187 C
ATOM 4108 CZ TYR A 521 13.339 27.290 36.030 1.00 78.43 C
ANISOU 4108 CZ TYR A 521 9864 11736 8198 -643 -14 -200 C
ATOM 4109 OH TYR A 521 13.089 28.609 35.727 1.00 77.18 O
ANISOU 4109 OH TYR A 521 9856 11580 7888 -820 -22 -8 O
ATOM 4110 N GLN A 522 14.075 20.054 36.947 1.00 83.34 N
ANISOU 4110 N GLN A 522 9800 11879 9987 361 -164 -1153 N
ATOM 4111 CA GLN A 522 14.762 18.901 37.520 1.00 86.87 C
ANISOU 4111 CA GLN A 522 10094 12176 10738 556 -248 -1257 C
ATOM 4112 C GLN A 522 15.120 17.846 36.481 1.00 86.97 C
ANISOU 4112 C GLN A 522 9897 12259 10889 691 -202 -1617 C
ATOM 4113 O GLN A 522 16.060 17.078 36.704 1.00 92.35 O
ANISOU 4113 O GLN A 522 10381 12908 11800 853 -251 -1761 O
ATOM 4114 CB GLN A 522 13.921 18.257 38.624 1.00 85.83 C
ANISOU 4114 CB GLN A 522 10116 11678 10819 641 -377 -1074 C
ATOM 4115 CG GLN A 522 12.809 17.348 38.133 1.00 84.46 C
ANISOU 4115 CG GLN A 522 9996 11304 10792 699 -386 -1191 C
ATOM 4116 CD GLN A 522 11.996 16.768 39.271 1.00 85.96 C
ANISOU 4116 CD GLN A 522 10332 11152 11179 740 -495 -972 C
ATOM 4117 OE1 GLN A 522 11.463 17.500 40.106 1.00 87.26 O
ANISOU 4117 OE1 GLN A 522 10661 11282 11210 639 -507 -713 O
ATOM 4118 NE2 GLN A 522 11.915 15.444 39.325 1.00 84.84 N
ANISOU 4118 NE2 GLN A 522 10123 10754 11359 883 -573 -1078 N
ATOM 4119 N PHE A 523 14.401 17.780 35.363 1.00 87.48 N
ANISOU 4119 N PHE A 523 9988 12424 10826 640 -122 -1784 N
ATOM 4120 CA PHE A 523 14.767 16.829 34.323 1.00 90.32 C
ANISOU 4120 CA PHE A 523 10138 12894 11286 760 -68 -2178 C
ATOM 4121 C PHE A 523 15.807 17.400 33.371 1.00 93.51 C
ANISOU 4121 C PHE A 523 10347 13750 11432 675 87 -2358 C
ATOM 4122 O PHE A 523 16.637 16.644 32.850 1.00 94.35 O
ANISOU 4122 O PHE A 523 10199 13985 11665 809 134 -2692 O
ATOM 4123 CB PHE A 523 13.520 16.372 33.561 1.00 90.91 C
ANISOU 4123 CB PHE A 523 10310 12884 11346 750 -68 -2315 C
ATOM 4124 CG PHE A 523 12.584 15.538 34.393 1.00 95.68 C
ANISOU 4124 CG PHE A 523 11043 13044 12266 841 -205 -2207 C
ATOM 4125 CD1 PHE A 523 12.865 14.206 34.653 1.00 90.36 C
ANISOU 4125 CD1 PHE A 523 10250 12094 11989 1038 -295 -2389 C
ATOM 4126 CD2 PHE A 523 11.434 16.091 34.930 1.00 89.76 C
ANISOU 4126 CD2 PHE A 523 10523 12149 11431 725 -245 -1918 C
ATOM 4127 CE1 PHE A 523 12.009 13.440 35.428 1.00 85.95 C
ANISOU 4127 CE1 PHE A 523 9816 11120 11723 1089 -418 -2250 C
ATOM 4128 CE2 PHE A 523 10.575 15.329 35.704 1.00 85.45 C
ANISOU 4128 CE2 PHE A 523 10079 11228 11159 778 -348 -1806 C
ATOM 4129 CZ PHE A 523 10.864 14.002 35.952 1.00 86.52 C
ANISOU 4129 CZ PHE A 523 10110 11089 11676 946 -434 -1955 C
ATOM 4130 N GLN A 524 15.792 18.716 33.144 1.00 87.87 N
ANISOU 4130 N GLN A 524 9738 13277 10374 451 168 -2147 N
ATOM 4131 CA GLN A 524 16.928 19.365 32.496 1.00 87.13 C
ANISOU 4131 CA GLN A 524 9457 13599 10048 330 314 -2232 C
ATOM 4132 C GLN A 524 18.207 19.111 33.280 1.00101.07 C
ANISOU 4132 C GLN A 524 11009 15360 12032 437 282 -2269 C
ATOM 4133 O GLN A 524 19.222 18.685 32.715 1.00120.61 O
ANISOU 4133 O GLN A 524 13195 18090 14542 507 375 -2563 O
ATOM 4134 CB GLN A 524 16.680 20.869 32.360 1.00 85.68 C
ANISOU 4134 CB GLN A 524 9457 13575 9521 60 368 -1920 C
ATOM 4135 CG GLN A 524 15.533 21.248 31.444 1.00 84.59 C
ANISOU 4135 CG GLN A 524 9502 13510 9127 -53 394 -1875 C
ATOM 4136 CD GLN A 524 15.410 22.744 31.255 1.00 84.00 C
ANISOU 4136 CD GLN A 524 9593 13580 8742 -309 432 -1561 C
ATOM 4137 OE1 GLN A 524 14.453 23.364 31.717 1.00 82.21 O
ANISOU 4137 OE1 GLN A 524 9608 13127 8499 -359 336 -1303 O
ATOM 4138 NE2 GLN A 524 16.384 23.335 30.574 1.00 85.28 N
ANISOU 4138 NE2 GLN A 524 9616 14116 8671 -476 573 -1583 N
ATOM 4139 N PHE A 525 18.175 19.380 34.589 1.00 94.91 N
ANISOU 4139 N PHE A 525 10354 14314 11392 453 146 -1984 N
ATOM 4140 CA PHE A 525 19.284 19.029 35.470 1.00 94.32 C
ANISOU 4140 CA PHE A 525 10091 14192 11553 584 61 -1998 C
ATOM 4141 C PHE A 525 19.684 17.570 35.292 1.00101.11 C
ANISOU 4141 C PHE A 525 10727 14941 12750 865 9 -2323 C
ATOM 4142 O PHE A 525 20.823 17.259 34.925 1.00107.56 O
ANISOU 4142 O PHE A 525 11236 15986 13645 952 68 -2580 O
ATOM 4143 CB PHE A 525 18.900 19.281 36.931 1.00 89.10 C
ANISOU 4143 CB PHE A 525 9639 13217 10999 593 -109 -1658 C
ATOM 4144 CG PHE A 525 18.806 20.732 37.310 1.00 86.52 C
ANISOU 4144 CG PHE A 525 9480 12987 10408 348 -83 -1378 C
ATOM 4145 CD1 PHE A 525 19.343 21.722 36.506 1.00 86.93 C
ANISOU 4145 CD1 PHE A 525 9456 13376 10196 134 65 -1400 C
ATOM 4146 CD2 PHE A 525 18.190 21.098 38.496 1.00 83.61 C
ANISOU 4146 CD2 PHE A 525 9340 12366 10062 325 -208 -1096 C
ATOM 4147 CE1 PHE A 525 19.255 23.054 36.876 1.00 84.92 C
ANISOU 4147 CE1 PHE A 525 9364 13155 9748 -92 70 -1143 C
ATOM 4148 CE2 PHE A 525 18.100 22.422 38.869 1.00 81.84 C
ANISOU 4148 CE2 PHE A 525 9264 12202 9630 116 -195 -881 C
ATOM 4149 CZ PHE A 525 18.633 23.402 38.059 1.00 81.81 C
ANISOU 4149 CZ PHE A 525 9193 12483 9406 -89 -66 -902 C
ATOM 4150 N GLN A 526 18.738 16.661 35.551 1.00 97.18 N
ANISOU 4150 N GLN A 526 10369 14078 12476 1006 -103 -2323 N
ATOM 4151 CA GLN A 526 19.030 15.230 35.553 1.00 99.48 C
ANISOU 4151 CA GLN A 526 10486 14151 13162 1284 -197 -2593 C
ATOM 4152 C GLN A 526 19.660 14.774 34.244 1.00103.77 C
ANISOU 4152 C GLN A 526 10741 15000 13688 1358 -48 -3061 C
ATOM 4153 O GLN A 526 20.622 13.998 34.246 1.00 99.67 O
ANISOU 4153 O GLN A 526 9942 14484 13444 1572 -85 -3323 O
ATOM 4154 CB GLN A 526 17.748 14.441 35.826 1.00 96.79 C
ANISOU 4154 CB GLN A 526 10365 13391 13021 1354 -308 -2519 C
ATOM 4155 CG GLN A 526 17.944 12.935 35.925 1.00103.53 C
ANISOU 4155 CG GLN A 526 11076 13921 14338 1632 -438 -2754 C
ATOM 4156 CD GLN A 526 18.616 12.504 37.216 1.00127.63 C
ANISOU 4156 CD GLN A 526 14089 16717 17689 1795 -634 -2540 C
ATOM 4157 OE1 GLN A 526 19.037 13.331 38.025 1.00124.04 O
ANISOU 4157 OE1 GLN A 526 13682 16373 17074 1702 -665 -2255 O
ATOM 4158 NE2 GLN A 526 18.724 11.194 37.411 1.00128.71 N
ANISOU 4158 NE2 GLN A 526 14136 16500 18268 2040 -783 -2680 N
ATOM 4159 N GLU A 527 19.133 15.249 33.114 1.00114.16 N
ANISOU 4159 N GLU A 527 12111 16591 14675 1188 115 -3180 N
ATOM 4160 CA GLU A 527 19.659 14.823 31.821 1.00113.86 C
ANISOU 4160 CA GLU A 527 11806 16896 14560 1239 274 -3644 C
ATOM 4161 C GLU A 527 21.085 15.320 31.618 1.00117.07 C
ANISOU 4161 C GLU A 527 11915 17720 14848 1197 404 -3756 C
ATOM 4162 O GLU A 527 21.957 14.565 31.172 1.00128.14 O
ANISOU 4162 O GLU A 527 12991 19267 16429 1381 456 -4157 O
ATOM 4163 CB GLU A 527 18.749 15.318 30.698 1.00104.40 C
ANISOU 4163 CB GLU A 527 10755 15939 12974 1040 404 -3691 C
ATOM 4164 CG GLU A 527 19.086 14.746 29.333 1.00115.87 C
ANISOU 4164 CG GLU A 527 11961 17743 14322 1096 558 -4202 C
ATOM 4165 CD GLU A 527 18.241 15.346 28.230 1.00134.77 C
ANISOU 4165 CD GLU A 527 14505 20435 16268 876 673 -4204 C
ATOM 4166 OE1 GLU A 527 18.439 16.537 27.909 1.00140.77 O
ANISOU 4166 OE1 GLU A 527 15324 21539 16624 625 792 -3970 O
ATOM 4167 OE2 GLU A 527 17.377 14.628 27.687 1.00136.26 O1-
ANISOU 4167 OE2 GLU A 527 14753 20505 16515 949 628 -4432 O1-
ATOM 4168 N ALA A 528 21.343 16.588 31.947 1.00 96.51 N
ANISOU 4168 N ALA A 528 9401 15305 11963 954 457 -3421 N
ATOM 4169 CA ALA A 528 22.683 17.141 31.776 1.00 96.98 C
ANISOU 4169 CA ALA A 528 9172 15770 11906 868 587 -3502 C
ATOM 4170 C ALA A 528 23.705 16.394 32.626 1.00110.73 C
ANISOU 4170 C ALA A 528 10650 17360 14060 1130 451 -3620 C
ATOM 4171 O ALA A 528 24.808 16.089 32.158 1.00100.49 O
ANISOU 4171 O ALA A 528 8982 16369 12830 1220 554 -3952 O
ATOM 4172 CB ALA A 528 22.683 18.629 32.120 1.00 97.91 C
ANISOU 4172 CB ALA A 528 9470 16022 11709 552 628 -3087 C
ATOM 4173 N LEU A 529 23.349 16.080 33.874 1.00117.93 N
ANISOU 4173 N LEU A 529 11741 17819 15250 1260 214 -3352 N
ATOM 4174 CA LEU A 529 24.293 15.424 34.775 1.00116.62 C
ANISOU 4174 CA LEU A 529 11353 17494 15465 1509 42 -3396 C
ATOM 4175 C LEU A 529 24.548 13.981 34.357 1.00119.44 C
ANISOU 4175 C LEU A 529 11472 17702 16208 1843 -10 -3822 C
ATOM 4176 O LEU A 529 25.691 13.509 34.402 1.00115.63 O
ANISOU 4176 O LEU A 529 10634 17337 15964 2038 -37 -4073 O
ATOM 4177 CB LEU A 529 23.767 15.478 36.208 1.00100.50 C
ANISOU 4177 CB LEU A 529 9593 15030 13565 1538 -199 -2967 C
ATOM 4178 CG LEU A 529 23.586 16.875 36.799 1.00 99.63 C
ANISOU 4178 CG LEU A 529 9701 15023 13131 1244 -181 -2575 C
ATOM 4179 CD1 LEU A 529 23.352 16.786 38.298 1.00102.34 C
ANISOU 4179 CD1 LEU A 529 10233 15013 13638 1319 -426 -2228 C
ATOM 4180 CD2 LEU A 529 24.786 17.752 36.481 1.00101.98 C
ANISOU 4180 CD2 LEU A 529 9732 15773 13241 1079 -44 -2653 C
ATOM 4181 N CYS A 530 23.494 13.265 33.955 1.00118.84 N
ANISOU 4181 N CYS A 530 11574 17356 16224 1917 -34 -3925 N
ATOM 4182 CA CYS A 530 23.639 11.888 33.501 1.00116.48 C
ANISOU 4182 CA CYS A 530 11071 16871 16316 2224 -89 -4360 C
ATOM 4183 C CYS A 530 24.402 11.782 32.188 1.00128.84 C
ANISOU 4183 C CYS A 530 12278 18925 17751 2248 147 -4886 C
ATOM 4184 O CYS A 530 25.018 10.743 31.929 1.00135.38 O
ANISOU 4184 O CYS A 530 12810 19686 18942 2542 106 -5306 O
ATOM 4185 CB CYS A 530 22.262 11.240 33.365 1.00110.92 C
ANISOU 4185 CB CYS A 530 10654 15771 15720 2246 -166 -4338 C
ATOM 4186 SG CYS A 530 21.431 11.018 34.946 1.00109.45 S
ANISOU 4186 SG CYS A 530 10823 14980 15781 2276 -448 -3788 S
ATOM 4187 N GLN A 531 24.365 12.823 31.356 1.00145.10 N
ANISOU 4187 N GLN A 531 14356 21472 19303 1946 390 -4874 N
ATOM 4188 CA GLN A 531 25.235 12.863 30.187 1.00155.52 C
ANISOU 4188 CA GLN A 531 15312 23348 20432 1924 641 -5329 C
ATOM 4189 C GLN A 531 26.701 12.876 30.599 1.00158.78 C
ANISOU 4189 C GLN A 531 15335 23964 21032 2045 642 -5444 C
ATOM 4190 O GLN A 531 27.530 12.185 29.994 1.00165.17 O
ANISOU 4190 O GLN A 531 15750 24995 22013 2249 732 -5944 O
ATOM 4191 CB GLN A 531 24.911 14.090 29.335 1.00157.22 C
ANISOU 4191 CB GLN A 531 15658 24036 20040 1536 881 -5180 C
ATOM 4192 CG GLN A 531 25.863 14.297 28.171 1.00169.74 C
ANISOU 4192 CG GLN A 531 16874 26275 21346 1444 1170 -5577 C
ATOM 4193 CD GLN A 531 26.937 15.329 28.465 1.00191.77 C
ANISOU 4193 CD GLN A 531 19483 29424 23955 1235 1279 -5371 C
ATOM 4194 OE1 GLN A 531 26.929 15.976 29.514 1.00192.62 O
ANISOU 4194 OE1 GLN A 531 19769 29301 24118 1142 1135 -4928 O
ATOM 4195 NE2 GLN A 531 27.875 15.481 27.538 1.00179.94 N
ANISOU 4195 NE2 GLN A 531 17616 28513 22239 1150 1541 -5711 N
ATOM 4196 N ALA A 532 27.040 13.668 31.621 1.00131.78 N
ANISOU 4196 N ALA A 532 12000 20487 17582 1923 540 -5012 N
ATOM 4197 CA ALA A 532 28.408 13.686 32.129 1.00126.10 C
ANISOU 4197 CA ALA A 532 10910 19939 17064 2038 500 -5094 C
ATOM 4198 C ALA A 532 28.808 12.325 32.682 1.00129.45 C
ANISOU 4198 C ALA A 532 11135 19969 18081 2482 258 -5331 C
ATOM 4199 O ALA A 532 29.940 11.871 32.478 1.00128.34 O
ANISOU 4199 O ALA A 532 10551 20045 18166 2688 287 -5702 O
ATOM 4200 CB ALA A 532 28.558 14.767 33.200 1.00113.41 C
ANISOU 4200 CB ALA A 532 9476 18292 15321 1820 397 -4576 C
ATOM 4201 N ALA A 533 27.890 11.654 33.384 1.00115.27 N
ANISOU 4201 N ALA A 533 9650 17588 16558 2634 14 -5116 N
ATOM 4202 CA ALA A 533 28.130 10.286 33.824 1.00123.22 C
ANISOU 4202 CA ALA A 533 10513 18154 18151 3050 -231 -5321 C
ATOM 4203 C ALA A 533 28.196 9.300 32.664 1.00126.98 C
ANISOU 4203 C ALA A 533 10739 18694 18813 3265 -111 -5943 C
ATOM 4204 O ALA A 533 28.492 8.122 32.895 1.00124.95 O
ANISOU 4204 O ALA A 533 10314 18075 19088 3634 -305 -6191 O
ATOM 4205 CB ALA A 533 27.042 9.851 34.809 1.00112.47 C
ANISOU 4205 CB ALA A 533 9573 16165 16997 3103 -497 -4903 C
ATOM 4206 N LYS A 534 27.931 9.754 31.436 1.00143.36 N
ANISOU 4206 N LYS A 534 12789 21215 20465 3045 189 -6199 N
ATOM 4207 CA LYS A 534 27.962 8.907 30.244 1.00145.31 C
ANISOU 4207 CA LYS A 534 12800 21606 20804 3212 333 -6832 C
ATOM 4208 C LYS A 534 27.027 7.712 30.396 1.00148.14 C
ANISOU 4208 C LYS A 534 13364 21331 21591 3450 115 -6929 C
ATOM 4209 O LYS A 534 27.362 6.586 30.020 1.00151.63 O
ANISOU 4209 O LYS A 534 13548 21608 22455 3775 58 -7433 O
ATOM 4210 CB LYS A 534 29.386 8.446 29.922 1.00140.00 C
ANISOU 4210 CB LYS A 534 11569 21244 20380 3471 405 -7338 C
ATOM 4211 CG LYS A 534 30.372 9.579 29.703 1.00140.78 C
ANISOU 4211 CG LYS A 534 11413 22003 20075 3217 642 -7285 C
ATOM 4212 CD LYS A 534 31.799 9.057 29.660 1.00163.35 C
ANISOU 4212 CD LYS A 534 13735 25072 23260 3491 644 -7703 C
ATOM 4213 CE LYS A 534 32.807 10.192 29.594 1.00169.98 C
ANISOU 4213 CE LYS A 534 14315 26528 23741 3216 853 -7598 C
ATOM 4214 NZ LYS A 534 32.665 10.996 28.352 1.00182.04 N
ANISOU 4214 NZ LYS A 534 15861 28666 24640 2826 1228 -7706 N
ATOM 4215 N HIS A 535 25.850 7.954 30.967 1.00137.72 N
ANISOU 4215 N HIS A 535 12499 19642 20186 3283 -9 -6452 N
ATOM 4216 CA HIS A 535 24.872 6.886 31.101 1.00137.86 C
ANISOU 4216 CA HIS A 535 12728 19068 20584 3446 -200 -6505 C
ATOM 4217 C HIS A 535 24.447 6.395 29.725 1.00140.55 C
ANISOU 4217 C HIS A 535 12976 19600 20826 3455 -23 -7075 C
ATOM 4218 O HIS A 535 24.196 7.187 28.813 1.00144.25 O
ANISOU 4218 O HIS A 535 13476 20582 20750 3184 229 -7153 O
ATOM 4219 CB HIS A 535 23.644 7.354 31.880 1.00129.80 C
ANISOU 4219 CB HIS A 535 12190 17713 19415 3217 -316 -5902 C
ATOM 4220 CG HIS A 535 22.633 6.272 32.101 1.00138.12 C
ANISOU 4220 CG HIS A 535 13456 18149 20873 3349 -513 -5909 C
ATOM 4221 ND1 HIS A 535 21.485 6.161 31.347 1.00143.00 N
ANISOU 4221 ND1 HIS A 535 14269 18737 21326 3201 -429 -6039 N
ATOM 4222 CD2 HIS A 535 22.602 5.247 32.987 1.00146.66 C
ANISOU 4222 CD2 HIS A 535 14581 18618 22526 3602 -796 -5791 C
ATOM 4223 CE1 HIS A 535 20.790 5.115 31.756 1.00144.20 C
ANISOU 4223 CE1 HIS A 535 14564 18283 21942 3344 -641 -6019 C
ATOM 4224 NE2 HIS A 535 21.444 4.544 32.752 1.00152.38 N
ANISOU 4224 NE2 HIS A 535 15522 18946 23429 3583 -864 -5853 N
ATOM 4225 N GLU A 536 24.377 5.078 29.579 1.00141.07 N
ANISOU 4225 N GLU A 536 12928 19247 21424 3768 -170 -7474 N
ATOM 4226 CA GLU A 536 23.959 4.443 28.337 1.00150.09 C
ANISOU 4226 CA GLU A 536 13973 20503 22550 3816 -43 -8077 C
ATOM 4227 C GLU A 536 22.588 3.825 28.573 1.00143.27 C
ANISOU 4227 C GLU A 536 13471 19051 21915 3784 -228 -7917 C
ATOM 4228 O GLU A 536 22.458 2.862 29.336 1.00155.32 O
ANISOU 4228 O GLU A 536 15054 19926 24035 4017 -496 -7840 O
ATOM 4229 CB GLU A 536 24.974 3.395 27.887 1.00147.14 C
ANISOU 4229 CB GLU A 536 13270 20098 22537 4061 -98 -8556 C
ATOM 4230 CG GLU A 536 26.220 3.987 27.246 1.00149.96 C
ANISOU 4230 CG GLU A 536 13284 21156 22539 3984 140 -8784 C
ATOM 4231 CD GLU A 536 25.932 4.692 25.935 1.00161.40 C
ANISOU 4231 CD GLU A 536 14727 23274 23325 3674 456 -9006 C
ATOM 4232 OE1 GLU A 536 25.287 4.086 25.052 1.00147.92 O
ANISOU 4232 OE1 GLU A 536 13092 21532 21577 3633 466 -9318 O
ATOM 4233 OE2 GLU A 536 26.356 5.858 25.787 1.00175.91 O1-
ANISOU 4233 OE2 GLU A 536 16486 25675 24678 3456 682 -8844 O1-
ATOM 4234 N GLY A 537 21.568 4.389 27.934 1.00113.65 N
ANISOU 4234 N GLY A 537 9957 15526 17696 3487 -93 -7846 N
ATOM 4235 CA GLY A 537 20.225 3.881 28.050 1.00130.11 C
ANISOU 4235 CA GLY A 537 12356 17132 19949 3419 -239 -7725 C
ATOM 4236 C GLY A 537 19.209 4.966 28.320 1.00135.71 C
ANISOU 4236 C GLY A 537 13434 17951 20178 3060 -195 -7157 C
ATOM 4237 O GLY A 537 19.479 6.163 28.171 1.00135.53 O
ANISOU 4237 O GLY A 537 13433 18431 19629 2841 -23 -6924 O
ATOM 4238 N PRO A 538 18.004 4.568 28.712 1.00124.64 N
ANISOU 4238 N PRO A 538 12320 16071 18967 2991 -351 -6933 N
ATOM 4239 CA PRO A 538 16.979 5.560 29.052 1.00106.50 C
ANISOU 4239 CA PRO A 538 10362 13837 16266 2677 -327 -6398 C
ATOM 4240 C PRO A 538 17.362 6.344 30.300 1.00112.58 C
ANISOU 4240 C PRO A 538 11258 14547 16971 2612 -385 -5790 C
ATOM 4241 O PRO A 538 17.947 5.808 31.238 1.00116.28 O
ANISOU 4241 O PRO A 538 11670 14657 17855 2809 -550 -5647 O
ATOM 4242 CB PRO A 538 15.730 4.698 29.297 1.00109.96 C
ANISOU 4242 CB PRO A 538 11011 13707 17061 2671 -504 -6356 C
ATOM 4243 CG PRO A 538 16.014 3.418 28.565 1.00115.41 C
ANISOU 4243 CG PRO A 538 11461 14213 18178 2920 -552 -7015 C
ATOM 4244 CD PRO A 538 17.473 3.203 28.823 1.00123.02 C
ANISOU 4244 CD PRO A 538 12136 15244 19362 3180 -553 -7173 C
ATOM 4245 N LEU A 539 17.013 7.628 30.301 1.00115.28 N
ANISOU 4245 N LEU A 539 11774 15240 16789 2336 -263 -5435 N
ATOM 4246 CA LEU A 539 17.212 8.470 31.465 1.00112.05 C
ANISOU 4246 CA LEU A 539 11516 14783 16274 2238 -315 -4869 C
ATOM 4247 C LEU A 539 16.498 7.960 32.716 1.00117.46 C
ANISOU 4247 C LEU A 539 12437 14872 17318 2275 -536 -4466 C
ATOM 4248 O LEU A 539 16.798 8.429 33.823 1.00116.81 O
ANISOU 4248 O LEU A 539 12450 14701 17231 2251 -616 -4037 O
ATOM 4249 CB LEU A 539 16.779 9.899 31.142 1.00 98.08 C
ANISOU 4249 CB LEU A 539 9915 13440 13912 1930 -157 -4598 C
ATOM 4250 CG LEU A 539 17.543 11.004 31.853 1.00101.24 C
ANISOU 4250 CG LEU A 539 10324 14060 14082 1824 -117 -4227 C
ATOM 4251 CD1 LEU A 539 18.950 11.097 31.282 1.00112.16 C
ANISOU 4251 CD1 LEU A 539 11362 15859 15394 1906 17 -4550 C
ATOM 4252 CD2 LEU A 539 16.813 12.354 31.730 1.00108.87 C
ANISOU 4252 CD2 LEU A 539 11536 15273 14556 1519 -20 -3883 C
ATOM 4253 N HIS A 540 15.573 7.016 32.560 1.00138.42 N
ANISOU 4253 N HIS A 540 15183 17140 20272 2318 -634 -4601 N
ATOM 4254 CA HIS A 540 14.794 6.492 33.682 1.00137.67 C
ANISOU 4254 CA HIS A 540 15313 16490 20503 2314 -825 -4211 C
ATOM 4255 C HIS A 540 15.665 5.793 34.731 1.00119.27 C
ANISOU 4255 C HIS A 540 12904 13797 18617 2546 -1016 -4052 C
ATOM 4256 O HIS A 540 15.387 5.870 35.935 1.00124.93 O
ANISOU 4256 O HIS A 540 13812 14240 19414 2497 -1143 -3561 O
ATOM 4257 CB HIS A 540 13.711 5.533 33.132 1.00132.40 C
ANISOU 4257 CB HIS A 540 14707 15497 20102 2306 -882 -4468 C
ATOM 4258 CG HIS A 540 13.276 4.454 34.088 1.00152.01 C
ANISOU 4258 CG HIS A 540 17304 17324 23130 2395 -1101 -4252 C
ATOM 4259 ND1 HIS A 540 12.593 4.705 35.261 1.00165.17 N
ANISOU 4259 ND1 HIS A 540 19222 18744 24791 2251 -1183 -3685 N
ATOM 4260 CD2 HIS A 540 13.422 3.108 34.026 1.00138.62 C
ANISOU 4260 CD2 HIS A 540 15502 15161 22005 2604 -1254 -4527 C
ATOM 4261 CE1 HIS A 540 12.339 3.561 35.874 1.00154.95 C
ANISOU 4261 CE1 HIS A 540 17978 16877 24019 2348 -1371 -3589 C
ATOM 4262 NE2 HIS A 540 12.832 2.579 35.147 1.00147.83 N
ANISOU 4262 NE2 HIS A 540 16869 15804 23496 2566 -1429 -4086 N
ATOM 4263 N LYS A 541 16.709 5.096 34.294 1.00104.76 N
ANISOU 4263 N LYS A 541 10775 11961 17067 2807 -1045 -4468 N
ATOM 4264 CA LYS A 541 17.557 4.332 35.193 1.00117.88 C
ANISOU 4264 CA LYS A 541 12332 13257 19202 3069 -1260 -4360 C
ATOM 4265 C LYS A 541 18.967 4.894 35.295 1.00127.57 C
ANISOU 4265 C LYS A 541 13306 14871 20293 3185 -1212 -4416 C
ATOM 4266 O LYS A 541 19.934 4.124 35.278 1.00128.95 O
ANISOU 4266 O LYS A 541 13215 14916 20862 3479 -1320 -4692 O
ATOM 4267 CB LYS A 541 17.626 2.866 34.747 1.00120.74 C
ANISOU 4267 CB LYS A 541 12539 13177 20158 3334 -1394 -4804 C
ATOM 4268 CG LYS A 541 17.819 2.704 33.242 1.00119.23 C
ANISOU 4268 CG LYS A 541 12105 13328 19868 3389 -1211 -5493 C
ATOM 4269 CD LYS A 541 17.584 1.273 32.787 1.00117.25 C
ANISOU 4269 CD LYS A 541 11758 12591 20202 3604 -1347 -5944 C
ATOM 4270 CE LYS A 541 16.261 0.726 33.290 1.00131.21 C
ANISOU 4270 CE LYS A 541 13832 13809 22213 3462 -1491 -5642 C
ATOM 4271 NZ LYS A 541 16.071 -0.693 32.896 1.00126.63 N
ANISOU 4271 NZ LYS A 541 13158 12696 22260 3664 -1646 -6074 N
ATOM 4272 N CYS A 542 19.120 6.211 35.407 1.00126.99 N
ANISOU 4272 N CYS A 542 13294 15257 19700 2963 -1063 -4169 N
ATOM 4273 CA CYS A 542 20.455 6.785 35.556 1.00113.57 C
ANISOU 4273 CA CYS A 542 11347 13927 17877 3038 -1020 -4200 C
ATOM 4274 C CYS A 542 20.810 6.986 37.023 1.00125.67 C
ANISOU 4274 C CYS A 542 12986 15260 19503 3068 -1223 -3683 C
ATOM 4275 O CYS A 542 19.960 7.354 37.841 1.00119.15 O
ANISOU 4275 O CYS A 542 12474 14257 18541 2891 -1284 -3221 O
ATOM 4276 CB CYS A 542 20.575 8.122 34.827 1.00121.37 C
ANISOU 4276 CB CYS A 542 12312 15537 18268 2772 -751 -4239 C
ATOM 4277 SG CYS A 542 21.919 9.128 35.490 1.00116.26 S
ANISOU 4277 SG CYS A 542 11488 15269 17416 2739 -733 -4022 S
ATOM 4278 N ASP A 543 22.080 6.752 37.339 1.00147.99 N
ANISOU 4278 N ASP A 543 15532 18149 22548 3294 -1325 -3783 N
ATOM 4279 CA ASP A 543 22.650 7.020 38.653 1.00129.07 C
ANISOU 4279 CA ASP A 543 13173 15671 20195 3336 -1521 -3346 C
ATOM 4280 C ASP A 543 23.885 7.890 38.456 1.00124.07 C
ANISOU 4280 C ASP A 543 12248 15576 19316 3314 -1404 -3483 C
ATOM 4281 O ASP A 543 24.796 7.514 37.710 1.00132.29 O
ANISOU 4281 O ASP A 543 12926 16813 20525 3504 -1340 -3944 O
ATOM 4282 CB ASP A 543 23.013 5.712 39.366 1.00121.57 C
ANISOU 4282 CB ASP A 543 12151 14190 19849 3670 -1835 -3297 C
ATOM 4283 CG ASP A 543 23.335 5.912 40.838 1.00130.47 C
ANISOU 4283 CG ASP A 543 13398 15182 20991 3686 -2076 -2758 C
ATOM 4284 OD1 ASP A 543 23.144 7.037 41.349 1.00132.87 O
ANISOU 4284 OD1 ASP A 543 13872 15768 20846 3426 -1996 -2430 O
ATOM 4285 OD2 ASP A 543 23.788 4.942 41.486 1.00130.94 O1-
ANISOU 4285 OD2 ASP A 543 13383 14853 21516 3964 -2359 -2666 O1-
ATOM 4286 N ILE A 544 23.920 9.051 39.112 1.00104.16 N
ANISOU 4286 N ILE A 544 9867 13300 16408 3076 -1371 -3107 N
ATOM 4287 CA ILE A 544 25.062 9.946 38.954 1.00114.53 C
ANISOU 4287 CA ILE A 544 10911 15118 17486 3008 -1258 -3211 C
ATOM 4288 C ILE A 544 26.133 9.588 39.978 1.00121.19 C
ANISOU 4288 C ILE A 544 11558 15863 18627 3242 -1524 -3082 C
ATOM 4289 O ILE A 544 27.116 10.319 40.145 1.00114.95 O
ANISOU 4289 O ILE A 544 10548 15447 17680 3187 -1493 -3092 O
ATOM 4290 CB ILE A 544 24.660 11.428 39.080 1.00103.97 C
ANISOU 4290 CB ILE A 544 9795 14102 15608 2630 -1095 -2917 C
ATOM 4291 CG1 ILE A 544 24.130 11.733 40.481 1.00113.39 C
ANISOU 4291 CG1 ILE A 544 11305 15035 16743 2544 -1291 -2385 C
ATOM 4292 CG2 ILE A 544 23.622 11.790 38.031 1.00106.64 C
ANISOU 4292 CG2 ILE A 544 10313 14549 15656 2416 -858 -3036 C
ATOM 4293 CD1 ILE A 544 23.862 13.204 40.719 1.00106.62 C
ANISOU 4293 CD1 ILE A 544 10634 14468 15407 2207 -1161 -2125 C
ATOM 4294 N SER A 545 25.951 8.461 40.662 1.00118.05 N
ANISOU 4294 N SER A 545 11231 14958 18666 3498 -1800 -2950 N
ATOM 4295 CA SER A 545 26.908 8.025 41.670 1.00112.40 C
ANISOU 4295 CA SER A 545 10347 14106 18256 3748 -2101 -2790 C
ATOM 4296 C SER A 545 28.255 7.698 41.032 1.00125.13 C
ANISOU 4296 C SER A 545 11451 15974 20118 4004 -2081 -3277 C
ATOM 4297 O SER A 545 28.334 7.287 39.871 1.00130.89 O
ANISOU 4297 O SER A 545 11976 16796 20958 4095 -1900 -3767 O
ATOM 4298 CB SER A 545 26.368 6.804 42.418 1.00119.69 C
ANISOU 4298 CB SER A 545 11463 14396 19617 3966 -2400 -2542 C
ATOM 4299 OG SER A 545 25.168 7.115 43.106 1.00116.05 O
ANISOU 4299 OG SER A 545 11442 13737 18914 3718 -2414 -2076 O
ATOM 4300 N ASN A 546 29.323 7.884 41.811 1.00132.38 N
ANISOU 4300 N ASN A 546 12150 17031 21117 4123 -2272 -3155 N
ATOM 4301 CA ASN A 546 30.698 7.685 41.342 1.00134.96 C
ANISOU 4301 CA ASN A 546 11951 17656 21672 4359 -2264 -3592 C
ATOM 4302 C ASN A 546 30.945 8.448 40.032 1.00141.56 C
ANISOU 4302 C ASN A 546 12571 19051 22165 4143 -1857 -4019 C
ATOM 4303 O ASN A 546 31.377 7.883 39.025 1.00157.22 O
ANISOU 4303 O ASN A 546 14230 21155 24352 4325 -1722 -4545 O
ATOM 4304 CB ASN A 546 31.025 6.186 41.185 1.00135.35 C
ANISOU 4304 CB ASN A 546 11782 17275 22368 4816 -2483 -3884 C
ATOM 4305 CG ASN A 546 31.195 5.449 42.537 1.00152.63 C
ANISOU 4305 CG ASN A 546 14072 18983 24938 5074 -2936 -3457 C
ATOM 4306 OD1 ASN A 546 30.799 5.954 43.587 1.00150.04 O
ANISOU 4306 OD1 ASN A 546 14056 18592 24358 4888 -3071 -2920 O
ATOM 4307 ND2 ASN A 546 31.798 4.240 42.495 1.00167.00 N
ANISOU 4307 ND2 ASN A 546 15618 20466 27367 5510 -3176 -3708 N
ATOM 4308 N SER A 547 30.660 9.768 40.046 1.00131.84 N
ANISOU 4308 N SER A 547 11524 18172 20399 3742 -1658 -3788 N
ATOM 4309 CA SER A 547 30.748 10.574 38.813 1.00133.50 C
ANISOU 4309 CA SER A 547 11601 18895 20228 3479 -1271 -4099 C
ATOM 4310 C SER A 547 31.049 12.034 39.177 1.00136.70 C
ANISOU 4310 C SER A 547 12057 19699 20183 3115 -1166 -3820 C
ATOM 4311 O SER A 547 30.173 12.905 39.171 1.00133.34 O
ANISOU 4311 O SER A 547 11988 19306 19370 2791 -1040 -3545 O
ATOM 4312 CB SER A 547 29.472 10.474 37.977 1.00125.93 C
ANISOU 4312 CB SER A 547 10952 17808 19088 3333 -1078 -4163 C
ATOM 4313 OG SER A 547 29.508 11.371 36.879 1.00128.09 O
ANISOU 4313 OG SER A 547 11146 18594 18927 3042 -728 -4369 O
ATOM 4314 N THR A 548 32.329 12.307 39.454 1.00135.76 N
ANISOU 4314 N THR A 548 11552 19890 20142 3172 -1220 -3924 N
ATOM 4315 CA THR A 548 32.740 13.651 39.855 1.00130.81 C
ANISOU 4315 CA THR A 548 10931 19621 19149 2834 -1150 -3687 C
ATOM 4316 C THR A 548 32.503 14.679 38.755 1.00135.16 C
ANISOU 4316 C THR A 548 11518 20587 19249 2450 -764 -3796 C
ATOM 4317 O THR A 548 32.361 15.873 39.044 1.00134.73 O
ANISOU 4317 O THR A 548 11646 20699 18848 2105 -694 -3512 O
ATOM 4318 CB THR A 548 34.214 13.655 40.260 1.00128.58 C
ANISOU 4318 CB THR A 548 10165 19614 19075 2979 -1279 -3838 C
ATOM 4319 OG1 THR A 548 35.019 13.243 39.148 1.00134.73 O
ANISOU 4319 OG1 THR A 548 10470 20725 19995 3113 -1070 -4374 O
ATOM 4320 CG2 THR A 548 34.450 12.712 41.427 1.00134.12 C
ANISOU 4320 CG2 THR A 548 10857 19906 20198 3351 -1703 -3662 C
ATOM 4321 N GLU A 549 32.474 14.246 37.492 1.00136.87 N
ANISOU 4321 N GLU A 549 11560 20981 19462 2501 -522 -4205 N
ATOM 4322 CA GLU A 549 32.211 15.180 36.401 1.00128.29 C
ANISOU 4322 CA GLU A 549 10525 20301 17919 2133 -166 -4280 C
ATOM 4323 C GLU A 549 30.796 15.736 36.487 1.00108.88 C
ANISOU 4323 C GLU A 549 8614 17593 15161 1891 -141 -3909 C
ATOM 4324 O GLU A 549 30.580 16.935 36.274 1.00107.42 O
ANISOU 4324 O GLU A 549 8589 17641 14583 1522 21 -3700 O
ATOM 4325 CB GLU A 549 32.442 14.497 35.053 1.00123.22 C
ANISOU 4325 CB GLU A 549 9583 19914 17320 2261 73 -4817 C
ATOM 4326 CG GLU A 549 33.799 13.820 34.920 1.00153.99 C
ANISOU 4326 CG GLU A 549 12902 24043 21565 2554 52 -5253 C
ATOM 4327 CD GLU A 549 33.824 12.423 35.513 1.00155.01 C
ANISOU 4327 CD GLU A 549 12963 23670 22262 3041 -265 -5381 C
ATOM 4328 OE1 GLU A 549 33.111 11.537 34.996 1.00165.84 O
ANISOU 4328 OE1 GLU A 549 14456 24767 23790 3224 -260 -5590 O
ATOM 4329 OE2 GLU A 549 34.558 12.212 36.502 1.00138.60 O1-
ANISOU 4329 OE2 GLU A 549 10714 21465 20483 3237 -534 -5264 O1-
ATOM 4330 N ALA A 550 29.822 14.879 36.795 1.00103.84 N
ANISOU 4330 N ALA A 550 8256 16474 14726 2093 -306 -3824 N
ATOM 4331 CA ALA A 550 28.468 15.357 37.043 1.00101.67 C
ANISOU 4331 CA ALA A 550 8479 15939 14213 1892 -316 -3460 C
ATOM 4332 C ALA A 550 28.439 16.292 38.245 1.00102.87 C
ANISOU 4332 C ALA A 550 8844 16016 14226 1710 -462 -3010 C
ATOM 4333 O ALA A 550 27.802 17.351 38.208 1.00102.13 O
ANISOU 4333 O ALA A 550 9028 15991 13786 1401 -357 -2763 O
ATOM 4334 CB ALA A 550 27.526 14.172 37.255 1.00104.85 C
ANISOU 4334 CB ALA A 550 9093 15832 14914 2149 -483 -3458 C
ATOM 4335 N GLY A 551 29.143 15.919 39.316 1.00114.39 N
ANISOU 4335 N GLY A 551 10168 17341 15956 1907 -718 -2914 N
ATOM 4336 CA GLY A 551 29.145 16.741 40.515 1.00104.23 C
ANISOU 4336 CA GLY A 551 9070 15999 14534 1751 -878 -2522 C
ATOM 4337 C GLY A 551 29.695 18.134 40.276 1.00102.31 C
ANISOU 4337 C GLY A 551 8742 16172 13961 1398 -703 -2484 C
ATOM 4338 O GLY A 551 29.156 19.119 40.786 1.00101.09 O
ANISOU 4338 O GLY A 551 8884 15974 13552 1144 -709 -2181 O
ATOM 4339 N GLN A 552 30.772 18.238 39.493 1.00107.65 N
ANISOU 4339 N GLN A 552 9002 17252 14647 1371 -539 -2801 N
ATOM 4340 CA GLN A 552 31.364 19.548 39.240 1.00107.87 C
ANISOU 4340 CA GLN A 552 8924 17676 14386 1007 -367 -2757 C
ATOM 4341 C GLN A 552 30.427 20.432 38.428 1.00107.96 C
ANISOU 4341 C GLN A 552 9247 17753 14020 678 -125 -2632 C
ATOM 4342 O GLN A 552 30.313 21.633 38.697 1.00111.55 O
ANISOU 4342 O GLN A 552 9874 18276 14233 362 -89 -2385 O
ATOM 4343 CB GLN A 552 32.709 19.394 38.531 1.00112.33 C
ANISOU 4343 CB GLN A 552 8945 18688 15047 1042 -221 -3135 C
ATOM 4344 CG GLN A 552 33.477 20.700 38.387 1.00129.88 C
ANISOU 4344 CG GLN A 552 11007 21320 17021 654 -66 -3077 C
ATOM 4345 CD GLN A 552 33.980 21.228 39.719 1.00134.70 C
ANISOU 4345 CD GLN A 552 11618 21856 17708 604 -325 -2841 C
ATOM 4346 OE1 GLN A 552 34.703 20.541 40.440 1.00127.43 O
ANISOU 4346 OE1 GLN A 552 10441 20890 17087 886 -560 -2930 O
ATOM 4347 NE2 GLN A 552 33.592 22.454 40.056 1.00120.90 N
ANISOU 4347 NE2 GLN A 552 10155 20088 15692 252 -301 -2548 N
ATOM 4348 N LYS A 553 29.741 19.857 37.437 1.00120.04 N
ANISOU 4348 N LYS A 553 10851 19251 15508 754 23 -2804 N
ATOM 4349 CA LYS A 553 28.829 20.648 36.615 1.00113.79 C
ANISOU 4349 CA LYS A 553 10347 18532 14356 464 227 -2681 C
ATOM 4350 C LYS A 553 27.666 21.177 37.446 1.00106.34 C
ANISOU 4350 C LYS A 553 9876 17213 13317 369 83 -2288 C
ATOM 4351 O LYS A 553 27.299 22.353 37.342 1.00105.11 O
ANISOU 4351 O LYS A 553 9932 17123 12884 59 169 -2063 O
ATOM 4352 CB LYS A 553 28.319 19.813 35.440 1.00106.88 C
ANISOU 4352 CB LYS A 553 9442 17702 13466 594 379 -2973 C
ATOM 4353 CG LYS A 553 28.022 20.628 34.190 1.00114.82 C
ANISOU 4353 CG LYS A 553 10512 19051 14062 277 660 -2988 C
ATOM 4354 CD LYS A 553 28.058 19.763 32.940 1.00133.63 C
ANISOU 4354 CD LYS A 553 12683 21664 16425 412 839 -3408 C
ATOM 4355 CE LYS A 553 28.539 20.554 31.735 1.00143.54 C
ANISOU 4355 CE LYS A 553 13773 23476 17289 94 1146 -3507 C
ATOM 4356 NZ LYS A 553 27.703 21.761 31.490 1.00139.38 N
ANISOU 4356 NZ LYS A 553 13624 22945 16388 -258 1209 -3122 N
ATOM 4357 N LEU A 554 27.073 20.318 38.278 1.00 99.91 N
ANISOU 4357 N LEU A 554 9225 15998 12738 631 -135 -2201 N
ATOM 4358 CA LEU A 554 26.031 20.773 39.193 1.00 95.75 C
ANISOU 4358 CA LEU A 554 9107 15145 12128 554 -271 -1846 C
ATOM 4359 C LEU A 554 26.569 21.832 40.146 1.00 99.17 C
ANISOU 4359 C LEU A 554 9562 15652 12466 364 -364 -1628 C
ATOM 4360 O LEU A 554 25.926 22.861 40.379 1.00 95.17 O
ANISOU 4360 O LEU A 554 9337 15083 11741 130 -340 -1396 O
ATOM 4361 CB LEU A 554 25.462 19.591 39.977 1.00 95.66 C
ANISOU 4361 CB LEU A 554 9217 14731 12398 858 -488 -1787 C
ATOM 4362 CG LEU A 554 24.384 19.944 41.007 1.00 93.85 C
ANISOU 4362 CG LEU A 554 9383 14190 12086 793 -621 -1434 C
ATOM 4363 CD1 LEU A 554 23.121 20.452 40.326 1.00 94.12 C
ANISOU 4363 CD1 LEU A 554 9710 14162 11891 620 -470 -1357 C
ATOM 4364 CD2 LEU A 554 24.075 18.759 41.910 1.00 93.17 C
ANISOU 4364 CD2 LEU A 554 9365 13748 12287 1073 -848 -1343 C
ATOM 4365 N PHE A 555 27.763 21.598 40.700 1.00109.80 N
ANISOU 4365 N PHE A 555 10598 17131 13990 470 -483 -1719 N
ATOM 4366 CA PHE A 555 28.318 22.526 41.680 1.00104.62 C
ANISOU 4366 CA PHE A 555 9942 16546 13264 302 -604 -1542 C
ATOM 4367 C PHE A 555 28.598 23.894 41.072 1.00 99.83 C
ANISOU 4367 C PHE A 555 9321 16213 12395 -81 -405 -1514 C
ATOM 4368 O PHE A 555 28.496 24.910 41.769 1.00103.70 O
ANISOU 4368 O PHE A 555 9985 16655 12760 -292 -474 -1312 O
ATOM 4369 CB PHE A 555 29.596 21.952 42.287 1.00107.66 C
ANISOU 4369 CB PHE A 555 9950 17056 13901 502 -780 -1676 C
ATOM 4370 CG PHE A 555 30.178 22.803 43.377 1.00111.83 C
ANISOU 4370 CG PHE A 555 10463 17659 14369 351 -944 -1515 C
ATOM 4371 CD1 PHE A 555 29.731 22.682 44.681 1.00107.68 C
ANISOU 4371 CD1 PHE A 555 10176 16876 13861 449 -1199 -1277 C
ATOM 4372 CD2 PHE A 555 31.164 23.734 43.094 1.00116.86 C
ANISOU 4372 CD2 PHE A 555 10842 18640 14918 91 -840 -1608 C
ATOM 4373 CE1 PHE A 555 30.262 23.469 45.685 1.00116.45 C
ANISOU 4373 CE1 PHE A 555 11271 18081 14894 308 -1358 -1162 C
ATOM 4374 CE2 PHE A 555 31.697 24.524 44.091 1.00117.84 C
ANISOU 4374 CE2 PHE A 555 10946 18829 14999 -60 -1003 -1490 C
ATOM 4375 CZ PHE A 555 31.247 24.391 45.389 1.00123.65 C
ANISOU 4375 CZ PHE A 555 11923 19315 15744 57 -1267 -1281 C
ATOM 4376 N ASN A 556 28.959 23.942 39.785 1.00103.97 N
ANISOU 4376 N ASN A 556 9643 17028 12833 -184 -160 -1715 N
ATOM 4377 CA ASN A 556 29.220 25.225 39.137 1.00109.64 C
ANISOU 4377 CA ASN A 556 10356 18005 13297 -574 36 -1648 C
ATOM 4378 C ASN A 556 28.008 26.145 39.209 1.00115.07 C
ANISOU 4378 C ASN A 556 11498 18452 13771 -778 46 -1361 C
ATOM 4379 O ASN A 556 28.159 27.372 39.201 1.00113.76 O
ANISOU 4379 O ASN A 556 11411 18359 13452 -1098 101 -1211 O
ATOM 4380 CB ASN A 556 29.632 25.005 37.680 1.00124.96 C
ANISOU 4380 CB ASN A 556 12040 20307 15133 -641 310 -1894 C
ATOM 4381 CG ASN A 556 30.967 24.295 37.548 1.00131.56 C
ANISOU 4381 CG ASN A 556 12367 21447 16175 -480 332 -2214 C
ATOM 4382 OD1 ASN A 556 31.746 24.228 38.499 1.00131.37 O
ANISOU 4382 OD1 ASN A 556 12154 21414 16344 -393 148 -2220 O
ATOM 4383 ND2 ASN A 556 31.233 23.754 36.364 1.00136.64 N
ANISOU 4383 ND2 ASN A 556 12770 22376 16772 -431 550 -2501 N
ATOM 4384 N MET A 557 26.806 25.574 39.283 1.00109.55 N
ANISOU 4384 N MET A 557 11088 17454 13084 -599 -11 -1290 N
ATOM 4385 CA MET A 557 25.575 26.338 39.435 1.00 95.33 C
ANISOU 4385 CA MET A 557 9699 15402 11119 -737 -25 -1040 C
ATOM 4386 C MET A 557 25.193 26.538 40.895 1.00 99.05 C
ANISOU 4386 C MET A 557 10380 15588 11667 -673 -250 -858 C
ATOM 4387 O MET A 557 24.644 27.588 41.250 1.00 98.87 O
ANISOU 4387 O MET A 557 10611 15438 11517 -866 -271 -672 O
ATOM 4388 CB MET A 557 24.434 25.634 38.701 1.00100.37 C
ANISOU 4388 CB MET A 557 10515 15902 11719 -594 42 -1076 C
ATOM 4389 CG MET A 557 23.055 26.254 38.888 1.00109.91 C
ANISOU 4389 CG MET A 557 12127 16835 12798 -678 8 -842 C
ATOM 4390 SD MET A 557 22.143 25.606 40.309 1.00100.09 S
ANISOU 4390 SD MET A 557 11116 15190 11723 -435 -218 -714 S
ATOM 4391 CE MET A 557 22.027 23.868 39.895 1.00 92.08 C
ANISOU 4391 CE MET A 557 9951 14111 10923 -108 -228 -933 C
ATOM 4392 N LEU A 558 25.462 25.541 41.741 1.00102.84 N
ANISOU 4392 N LEU A 558 10758 15966 12350 -402 -423 -910 N
ATOM 4393 CA LEU A 558 25.062 25.617 43.143 1.00 95.97 C
ANISOU 4393 CA LEU A 558 10090 14862 11514 -332 -635 -731 C
ATOM 4394 C LEU A 558 25.675 26.831 43.829 1.00 93.49 C
ANISOU 4394 C LEU A 558 9765 14648 11108 -573 -699 -652 C
ATOM 4395 O LEU A 558 24.985 27.577 44.532 1.00 86.31 O
ANISOU 4395 O LEU A 558 9131 13571 10092 -678 -766 -495 O
ATOM 4396 CB LEU A 558 25.465 24.331 43.868 1.00 89.15 C
ANISOU 4396 CB LEU A 558 9073 13917 10881 -17 -822 -782 C
ATOM 4397 CG LEU A 558 24.808 23.030 43.403 1.00 89.15 C
ANISOU 4397 CG LEU A 558 9106 13734 11033 241 -807 -854 C
ATOM 4398 CD1 LEU A 558 25.353 21.846 44.183 1.00 90.33 C
ANISOU 4398 CD1 LEU A 558 9094 13780 11447 540 -1024 -875 C
ATOM 4399 CD2 LEU A 558 23.294 23.108 43.535 1.00 95.91 C
ANISOU 4399 CD2 LEU A 558 10341 14317 11784 216 -786 -679 C
ATOM 4400 N ARG A 559 26.975 27.051 43.626 1.00 92.83 N
ANISOU 4400 N ARG A 559 9348 14846 11078 -667 -677 -785 N
ATOM 4401 CA ARG A 559 27.660 28.140 44.312 1.00 93.19 C
ANISOU 4401 CA ARG A 559 9345 14990 11072 -901 -759 -740 C
ATOM 4402 C ARG A 559 27.135 29.510 43.909 1.00 93.24 C
ANISOU 4402 C ARG A 559 9586 14936 10903 -1230 -635 -620 C
ATOM 4403 O ARG A 559 27.299 30.470 44.668 1.00111.60 O
ANISOU 4403 O ARG A 559 11996 17217 13190 -1412 -734 -554 O
ATOM 4404 CB ARG A 559 29.160 28.078 44.033 1.00 95.66 C
ANISOU 4404 CB ARG A 559 9212 15643 11491 -955 -736 -924 C
ATOM 4405 CG ARG A 559 29.505 27.940 42.562 1.00110.30 C
ANISOU 4405 CG ARG A 559 10855 17737 13318 -1036 -474 -1070 C
ATOM 4406 CD ARG A 559 30.974 28.212 42.340 1.00100.60 C
ANISOU 4406 CD ARG A 559 9189 16876 12160 -1181 -424 -1237 C
ATOM 4407 NE ARG A 559 31.325 29.522 42.873 1.00112.32 N
ANISOU 4407 NE ARG A 559 10725 18383 13570 -1513 -473 -1126 N
ATOM 4408 CZ ARG A 559 31.373 30.637 42.158 1.00125.21 C
ANISOU 4408 CZ ARG A 559 12408 20106 15061 -1884 -292 -1050 C
ATOM 4409 NH1 ARG A 559 31.122 30.638 40.858 1.00124.96 N
ANISOU 4409 NH1 ARG A 559 12377 20198 14903 -1984 -41 -1057 N
ATOM 4410 NH2 ARG A 559 31.672 31.783 42.764 1.00135.97 N
ANISOU 4410 NH2 ARG A 559 13828 21428 16405 -2168 -374 -959 N
ATOM 4411 N LEU A 560 26.518 29.625 42.731 1.00 92.69 N
ANISOU 4411 N LEU A 560 9624 14861 10734 -1308 -437 -596 N
ATOM 4412 CA LEU A 560 26.109 30.936 42.239 1.00 96.88 C
ANISOU 4412 CA LEU A 560 10358 15336 11118 -1623 -332 -459 C
ATOM 4413 C LEU A 560 25.060 31.568 43.145 1.00 96.97 C
ANISOU 4413 C LEU A 560 10734 15021 11090 -1630 -461 -308 C
ATOM 4414 O LEU A 560 25.062 32.787 43.352 1.00 90.28 O
ANISOU 4414 O LEU A 560 10009 14093 10200 -1881 -479 -224 O
ATOM 4415 CB LEU A 560 25.586 30.819 40.808 1.00113.99 C
ANISOU 4415 CB LEU A 560 12576 17573 13161 -1671 -122 -446 C
ATOM 4416 CG LEU A 560 26.550 30.226 39.780 1.00110.24 C
ANISOU 4416 CG LEU A 560 11738 17463 12684 -1676 47 -630 C
ATOM 4417 CD1 LEU A 560 25.938 30.264 38.390 1.00 96.02 C
ANISOU 4417 CD1 LEU A 560 10033 15752 10699 -1762 248 -601 C
ATOM 4418 CD2 LEU A 560 27.874 30.973 39.804 1.00101.52 C
ANISOU 4418 CD2 LEU A 560 10352 16623 11596 -1948 90 -672 C
ATOM 4419 N GLY A 561 24.169 30.755 43.709 1.00 94.83 N
ANISOU 4419 N GLY A 561 10626 14559 10844 -1363 -551 -282 N
ATOM 4420 CA GLY A 561 23.078 31.302 44.499 1.00 89.89 C
ANISOU 4420 CA GLY A 561 10329 13658 10164 -1359 -641 -163 C
ATOM 4421 C GLY A 561 22.225 32.218 43.646 1.00107.09 C
ANISOU 4421 C GLY A 561 12734 15707 12247 -1533 -522 -56 C
ATOM 4422 O GLY A 561 21.812 31.866 42.535 1.00113.10 O
ANISOU 4422 O GLY A 561 13507 16508 12960 -1507 -390 -43 O
ATOM 4423 N LYS A 562 21.960 33.416 44.163 1.00 99.58 N
ANISOU 4423 N LYS A 562 11964 14598 11273 -1707 -584 13 N
ATOM 4424 CA LYS A 562 21.274 34.456 43.409 1.00102.57 C
ANISOU 4424 CA LYS A 562 12550 14825 11595 -1890 -508 134 C
ATOM 4425 C LYS A 562 22.230 35.461 42.782 1.00103.60 C
ANISOU 4425 C LYS A 562 12568 15073 11724 -2217 -441 175 C
ATOM 4426 O LYS A 562 21.771 36.429 42.169 1.00104.76 O
ANISOU 4426 O LYS A 562 12890 15077 11837 -2401 -399 311 O
ATOM 4427 CB LYS A 562 20.275 35.198 44.303 1.00 99.27 C
ANISOU 4427 CB LYS A 562 12414 14113 11190 -1868 -617 176 C
ATOM 4428 CG LYS A 562 18.933 34.504 44.455 1.00116.05 C
ANISOU 4428 CG LYS A 562 14717 16088 13288 -1619 -620 200 C
ATOM 4429 CD LYS A 562 17.936 35.398 45.177 1.00121.06 C
ANISOU 4429 CD LYS A 562 15606 16458 13933 -1623 -697 221 C
ATOM 4430 CE LYS A 562 17.842 36.763 44.509 1.00115.27 C
ANISOU 4430 CE LYS A 562 14996 15574 13230 -1856 -680 309 C
ATOM 4431 NZ LYS A 562 16.892 37.676 45.204 1.00 86.47 N
ANISOU 4431 NZ LYS A 562 11577 11643 9634 -1839 -767 291 N
ATOM 4432 N SER A 563 23.543 35.252 42.915 1.00 91.66 N
ANISOU 4432 N SER A 563 10758 13814 10255 -2299 -437 71 N
ATOM 4433 CA SER A 563 24.509 36.227 42.419 1.00 96.74 C
ANISOU 4433 CA SER A 563 11266 14582 10908 -2646 -371 109 C
ATOM 4434 C SER A 563 24.477 36.344 40.901 1.00101.85 C
ANISOU 4434 C SER A 563 11891 15369 11438 -2800 -172 222 C
ATOM 4435 O SER A 563 24.811 37.401 40.355 1.00 94.80 O
ANISOU 4435 O SER A 563 11024 14473 10524 -3124 -111 353 O
ATOM 4436 CB SER A 563 25.914 35.856 42.893 1.00118.92 C
ANISOU 4436 CB SER A 563 13716 17673 13797 -2676 -409 -52 C
ATOM 4437 OG SER A 563 26.295 34.579 42.408 1.00117.79 O
ANISOU 4437 OG SER A 563 13328 17783 13644 -2464 -326 -163 O
ATOM 4438 N GLU A 564 24.085 35.280 40.207 1.00117.49 N
ANISOU 4438 N GLU A 564 13828 17477 13338 -2585 -76 178 N
ATOM 4439 CA GLU A 564 24.003 35.290 38.759 1.00114.16 C
ANISOU 4439 CA GLU A 564 13383 17236 12757 -2709 110 261 C
ATOM 4440 C GLU A 564 22.565 35.032 38.322 1.00115.09 C
ANISOU 4440 C GLU A 564 13785 17155 12790 -2534 103 352 C
ATOM 4441 O GLU A 564 21.816 34.347 39.026 1.00110.57 O
ANISOU 4441 O GLU A 564 13316 16405 12290 -2252 1 281 O
ATOM 4442 CB GLU A 564 24.928 34.229 38.147 1.00112.21 C
ANISOU 4442 CB GLU A 564 12772 17385 12476 -2627 250 66 C
ATOM 4443 CG GLU A 564 26.410 34.412 38.479 1.00119.11 C
ANISOU 4443 CG GLU A 564 13302 18513 13441 -2793 268 -48 C
ATOM 4444 CD GLU A 564 27.065 35.568 37.738 1.00123.75 C
ANISOU 4444 CD GLU A 564 13828 19256 13937 -3226 402 98 C
ATOM 4445 OE1 GLU A 564 26.374 36.274 36.973 1.00133.61 O
ANISOU 4445 OE1 GLU A 564 15323 20396 15045 -3399 466 318 O
ATOM 4446 OE2 GLU A 564 28.285 35.768 37.921 1.00108.15 O1-
ANISOU 4446 OE2 GLU A 564 11546 17513 12034 -3402 436 4 O1-
ATOM 4447 N PRO A 565 22.146 35.580 37.179 1.00110.81 N
ANISOU 4447 N PRO A 565 13369 16646 12090 -2705 202 523 N
ATOM 4448 CA PRO A 565 20.768 35.363 36.719 1.00 95.78 C
ANISOU 4448 CA PRO A 565 11716 14572 10104 -2541 177 606 C
ATOM 4449 C PRO A 565 20.471 33.884 36.532 1.00 95.27 C
ANISOU 4449 C PRO A 565 11535 14640 10025 -2234 218 403 C
ATOM 4450 O PRO A 565 21.339 33.098 36.146 1.00101.15 O
ANISOU 4450 O PRO A 565 11999 15689 10745 -2200 327 230 O
ATOM 4451 CB PRO A 565 20.717 36.117 35.386 1.00 98.53 C
ANISOU 4451 CB PRO A 565 12139 15049 10248 -2811 288 819 C
ATOM 4452 CG PRO A 565 21.798 37.140 35.491 1.00 95.08 C
ANISOU 4452 CG PRO A 565 11608 14669 9850 -3153 318 922 C
ATOM 4453 CD PRO A 565 22.888 36.487 36.287 1.00104.80 C
ANISOU 4453 CD PRO A 565 12533 16074 11211 -3077 328 675 C
ATOM 4454 N TRP A 566 19.217 33.507 36.808 1.00 86.66 N
ANISOU 4454 N TRP A 566 10650 13305 8970 -2010 128 413 N
ATOM 4455 CA TRP A 566 18.857 32.093 36.802 1.00 90.99 C
ANISOU 4455 CA TRP A 566 11109 13903 9560 -1720 138 224 C
ATOM 4456 C TRP A 566 19.034 31.459 35.430 1.00100.60 C
ANISOU 4456 C TRP A 566 12180 15431 10611 -1728 291 124 C
ATOM 4457 O TRP A 566 19.141 30.232 35.338 1.00103.21 O
ANISOU 4457 O TRP A 566 12350 15860 11004 -1516 321 -93 O
ATOM 4458 CB TRP A 566 17.417 31.895 37.291 1.00 93.74 C
ANISOU 4458 CB TRP A 566 11703 13942 9972 -1524 25 270 C
ATOM 4459 CG TRP A 566 16.344 32.366 36.348 1.00100.19 C
ANISOU 4459 CG TRP A 566 12719 14698 10652 -1573 35 408 C
ATOM 4460 CD1 TRP A 566 15.685 33.561 36.385 1.00 99.88 C
ANISOU 4460 CD1 TRP A 566 12910 14444 10595 -1693 -41 611 C
ATOM 4461 CD2 TRP A 566 15.785 31.636 35.246 1.00100.10 C
ANISOU 4461 CD2 TRP A 566 12687 14833 10513 -1488 102 339 C
ATOM 4462 NE1 TRP A 566 14.763 33.626 35.368 1.00 94.54 N
ANISOU 4462 NE1 TRP A 566 12356 13781 9784 -1682 -36 699 N
ATOM 4463 CE2 TRP A 566 14.805 32.456 34.655 1.00 96.11 C
ANISOU 4463 CE2 TRP A 566 12404 14215 9897 -1567 53 531 C
ATOM 4464 CE3 TRP A 566 16.025 30.371 34.699 1.00101.68 C
ANISOU 4464 CE3 TRP A 566 12697 15244 10694 -1347 185 116 C
ATOM 4465 CZ2 TRP A 566 14.067 32.054 33.543 1.00102.20 C
ANISOU 4465 CZ2 TRP A 566 13210 15110 10509 -1519 80 517 C
ATOM 4466 CZ3 TRP A 566 15.291 29.974 33.595 1.00 86.92 C
ANISOU 4466 CZ3 TRP A 566 10864 13487 8674 -1307 225 74 C
ATOM 4467 CH2 TRP A 566 14.324 30.813 33.029 1.00100.46 C
ANISOU 4467 CH2 TRP A 566 12801 15119 10251 -1398 170 278 C
ATOM 4468 N THR A 567 19.068 32.263 34.366 1.00105.45 N
ANISOU 4468 N THR A 567 12850 16202 11016 -1970 382 274 N
ATOM 4469 CA THR A 567 19.362 31.723 33.044 1.00 97.51 C
ANISOU 4469 CA THR A 567 11683 15568 9798 -2012 546 164 C
ATOM 4470 C THR A 567 20.824 31.303 32.945 1.00109.08 C
ANISOU 4470 C THR A 567 12794 17372 11280 -2073 680 -33 C
ATOM 4471 O THR A 567 21.134 30.193 32.496 1.00107.79 O
ANISOU 4471 O THR A 567 12411 17433 11111 -1908 769 -301 O
ATOM 4472 CB THR A 567 19.022 32.756 31.970 1.00 89.07 C
ANISOU 4472 CB THR A 567 10780 14597 8466 -2278 597 424 C
ATOM 4473 OG1 THR A 567 19.696 33.986 32.258 1.00 99.14 O
ANISOU 4473 OG1 THR A 567 12087 15821 9760 -2569 593 639 O
ATOM 4474 CG2 THR A 567 17.522 33.008 31.940 1.00 91.33 C
ANISOU 4474 CG2 THR A 567 11374 14580 8744 -2166 454 575 C
ATOM 4475 N LEU A 568 21.739 32.183 33.362 1.00111.20 N
ANISOU 4475 N LEU A 568 12986 17675 11588 -2306 692 76 N
ATOM 4476 CA LEU A 568 23.151 31.821 33.421 1.00106.62 C
ANISOU 4476 CA LEU A 568 12038 17407 11065 -2356 800 -120 C
ATOM 4477 C LEU A 568 23.405 30.744 34.468 1.00 96.94 C
ANISOU 4477 C LEU A 568 10661 16063 10110 -2033 686 -355 C
ATOM 4478 O LEU A 568 24.350 29.959 34.333 1.00 97.97 O
ANISOU 4478 O LEU A 568 10459 16458 10308 -1939 766 -604 O
ATOM 4479 CB LEU A 568 23.992 33.068 33.705 1.00108.29 C
ANISOU 4479 CB LEU A 568 12213 17647 11284 -2700 813 63 C
ATOM 4480 CG LEU A 568 25.484 32.934 34.018 1.00 99.01 C
ANISOU 4480 CG LEU A 568 10654 16751 10214 -2790 886 -110 C
ATOM 4481 CD1 LEU A 568 26.235 32.278 32.870 1.00 99.19 C
ANISOU 4481 CD1 LEU A 568 10346 17271 10069 -2826 1122 -318 C
ATOM 4482 CD2 LEU A 568 26.069 34.304 34.327 1.00 98.66 C
ANISOU 4482 CD2 LEU A 568 10642 16652 10190 -3161 869 108 C
ATOM 4483 N ALA A 569 22.573 30.689 35.510 1.00 91.84 N
ANISOU 4483 N ALA A 569 10246 15029 9619 -1859 499 -277 N
ATOM 4484 CA ALA A 569 22.662 29.594 36.470 1.00 99.63 C
ANISOU 4484 CA ALA A 569 11131 15886 10836 -1548 378 -451 C
ATOM 4485 C ALA A 569 22.305 28.269 35.811 1.00 96.89 C
ANISOU 4485 C ALA A 569 10691 15615 10509 -1295 434 -668 C
ATOM 4486 O ALA A 569 23.042 27.283 35.924 1.00103.36 O
ANISOU 4486 O ALA A 569 11238 16557 11479 -1112 440 -901 O
ATOM 4487 CB ALA A 569 21.749 29.869 37.664 1.00 92.91 C
ANISOU 4487 CB ALA A 569 10567 14641 10095 -1451 189 -299 C
ATOM 4488 N LEU A 570 21.172 28.233 35.106 1.00101.75 N
ANISOU 4488 N LEU A 570 11521 16149 10990 -1278 463 -608 N
ATOM 4489 CA LEU A 570 20.760 27.025 34.398 1.00102.67 C
ANISOU 4489 CA LEU A 570 11560 16332 11118 -1064 513 -835 C
ATOM 4490 C LEU A 570 21.800 26.613 33.363 1.00108.57 C
ANISOU 4490 C LEU A 570 11977 17511 11763 -1111 698 -1084 C
ATOM 4491 O LEU A 570 22.149 25.432 33.251 1.00110.58 O
ANISOU 4491 O LEU A 570 12012 17832 12171 -878 713 -1375 O
ATOM 4492 CB LEU A 570 19.402 27.260 33.734 1.00 93.38 C
ANISOU 4492 CB LEU A 570 10660 15045 9776 -1091 508 -716 C
ATOM 4493 CG LEU A 570 18.772 26.129 32.921 1.00 91.34 C
ANISOU 4493 CG LEU A 570 10363 14839 9502 -905 546 -945 C
ATOM 4494 CD1 LEU A 570 18.506 24.914 33.794 1.00 88.92 C
ANISOU 4494 CD1 LEU A 570 10023 14253 9511 -605 423 -1092 C
ATOM 4495 CD2 LEU A 570 17.494 26.609 32.256 1.00 91.30 C
ANISOU 4495 CD2 LEU A 570 10623 14765 9301 -981 526 -790 C
ATOM 4496 N GLU A 571 22.312 27.586 32.601 1.00114.95 N
ANISOU 4496 N GLU A 571 12741 18615 12321 -1416 844 -977 N
ATOM 4497 CA GLU A 571 23.269 27.294 31.538 1.00113.26 C
ANISOU 4497 CA GLU A 571 12206 18876 11951 -1503 1057 -1207 C
ATOM 4498 C GLU A 571 24.527 26.619 32.070 1.00122.40 C
ANISOU 4498 C GLU A 571 12989 20166 13350 -1362 1067 -1466 C
ATOM 4499 O GLU A 571 25.173 25.853 31.344 1.00130.80 O
ANISOU 4499 O GLU A 571 13746 21556 14397 -1273 1210 -1786 O
ATOM 4500 CB GLU A 571 23.634 28.584 30.803 1.00103.18 C
ANISOU 4500 CB GLU A 571 10964 17871 10370 -1904 1201 -971 C
ATOM 4501 CG GLU A 571 24.329 28.376 29.470 1.00101.99 C
ANISOU 4501 CG GLU A 571 10543 18264 9946 -2042 1454 -1166 C
ATOM 4502 CD GLU A 571 24.879 29.667 28.898 1.00108.82 C
ANISOU 4502 CD GLU A 571 11410 19399 10538 -2475 1597 -893 C
ATOM 4503 OE1 GLU A 571 25.687 30.326 29.584 1.00121.76 O
ANISOU 4503 OE1 GLU A 571 12951 21002 12310 -2639 1579 -782 O
ATOM 4504 OE2 GLU A 571 24.505 30.023 27.762 1.00119.06 O1-
ANISOU 4504 OE2 GLU A 571 12807 20945 11486 -2663 1718 -782 O1-
ATOM 4505 N ASN A 572 24.897 26.890 33.325 1.00105.28 N
ANISOU 4505 N ASN A 572 10828 17767 11407 -1332 910 -1352 N
ATOM 4506 CA ASN A 572 26.085 26.259 33.891 1.00113.81 C
ANISOU 4506 CA ASN A 572 11548 18964 12731 -1181 879 -1579 C
ATOM 4507 C ASN A 572 25.921 24.750 34.007 1.00120.53 C
ANISOU 4507 C ASN A 572 12280 19690 13827 -785 801 -1865 C
ATOM 4508 O ASN A 572 26.895 24.007 33.842 1.00139.96 O
ANISOU 4508 O ASN A 572 14371 22371 16436 -636 852 -2164 O
ATOM 4509 CB ASN A 572 26.404 26.875 35.255 1.00122.02 C
ANISOU 4509 CB ASN A 572 12654 19775 13935 -1229 692 -1382 C
ATOM 4510 CG ASN A 572 27.128 28.202 35.138 1.00121.29 C
ANISOU 4510 CG ASN A 572 12503 19888 13694 -1616 784 -1217 C
ATOM 4511 OD1 ASN A 572 27.045 28.879 34.113 1.00115.11 O
ANISOU 4511 OD1 ASN A 572 11767 19319 12651 -1885 963 -1124 O
ATOM 4512 ND2 ASN A 572 27.847 28.580 36.189 1.00117.80 N
ANISOU 4512 ND2 ASN A 572 11959 19384 13414 -1658 652 -1171 N
ATOM 4513 N VAL A 573 24.705 24.278 34.276 1.00 94.21 N
ANISOU 4513 N VAL A 573 9240 15999 10558 -613 677 -1788 N
ATOM 4514 CA VAL A 573 24.454 22.839 34.314 1.00 87.65 C
ANISOU 4514 CA VAL A 573 8322 15004 9975 -263 600 -2043 C
ATOM 4515 C VAL A 573 24.205 22.301 32.914 1.00111.39 C
ANISOU 4515 C VAL A 573 11237 18258 12827 -239 780 -2318 C
ATOM 4516 O VAL A 573 24.924 21.423 32.424 1.00108.86 O
ANISOU 4516 O VAL A 573 10592 18140 12628 -71 858 -2679 O
ATOM 4517 CB VAL A 573 23.261 22.516 35.233 1.00 86.40 C
ANISOU 4517 CB VAL A 573 8499 14364 9965 -111 396 -1843 C
ATOM 4518 CG1 VAL A 573 23.270 21.043 35.623 1.00 86.90 C
ANISOU 4518 CG1 VAL A 573 8445 14200 10374 243 267 -2053 C
ATOM 4519 CG2 VAL A 573 23.268 23.391 36.450 1.00 85.53 C
ANISOU 4519 CG2 VAL A 573 8559 14071 9869 -224 257 -1533 C
ATOM 4520 N VAL A 574 23.178 22.830 32.250 1.00122.60 N
ANISOU 4520 N VAL A 574 12932 19674 13976 -401 840 -2168 N
ATOM 4521 CA VAL A 574 22.585 22.167 31.096 1.00104.36 C
ANISOU 4521 CA VAL A 574 10617 17497 11538 -330 941 -2412 C
ATOM 4522 C VAL A 574 23.013 22.755 29.753 1.00101.24 C
ANISOU 4522 C VAL A 574 10092 17625 10748 -586 1186 -2496 C
ATOM 4523 O VAL A 574 22.801 22.107 28.717 1.00107.83 O
ANISOU 4523 O VAL A 574 10834 18681 11457 -518 1295 -2789 O
ATOM 4524 CB VAL A 574 21.047 22.178 31.215 1.00 99.76 C
ANISOU 4524 CB VAL A 574 10409 16566 10927 -300 818 -2220 C
ATOM 4525 CG1 VAL A 574 20.624 21.749 32.614 1.00 95.77 C
ANISOU 4525 CG1 VAL A 574 10047 15579 10763 -105 596 -2075 C
ATOM 4526 CG2 VAL A 574 20.500 23.558 30.895 1.00104.99 C
ANISOU 4526 CG2 VAL A 574 11331 17303 11255 -607 858 -1873 C
ATOM 4527 N GLY A 575 23.598 23.950 29.733 1.00103.60 N
ANISOU 4527 N GLY A 575 10385 18137 10842 -890 1275 -2252 N
ATOM 4528 CA GLY A 575 24.050 24.533 28.485 1.00114.24 C
ANISOU 4528 CA GLY A 575 11610 20000 11798 -1169 1516 -2285 C
ATOM 4529 C GLY A 575 22.988 25.233 27.669 1.00110.54 C
ANISOU 4529 C GLY A 575 11460 19572 10968 -1373 1540 -2037 C
ATOM 4530 O GLY A 575 23.269 25.636 26.534 1.00100.10 O
ANISOU 4530 O GLY A 575 10056 18702 9275 -1604 1736 -2053 O
ATOM 4531 N ALA A 576 21.778 25.380 28.199 1.00118.64 N
ANISOU 4531 N ALA A 576 12834 20163 12082 -1294 1346 -1809 N
ATOM 4532 CA ALA A 576 20.724 26.157 27.565 1.00115.34 C
ANISOU 4532 CA ALA A 576 12730 19729 11365 -1472 1321 -1528 C
ATOM 4533 C ALA A 576 20.296 27.271 28.508 1.00120.21 C
ANISOU 4533 C ALA A 576 13633 19969 12072 -1597 1167 -1105 C
ATOM 4534 O ALA A 576 20.301 27.105 29.732 1.00120.08 O
ANISOU 4534 O ALA A 576 13650 19600 12374 -1447 1026 -1074 O
ATOM 4535 CB ALA A 576 19.519 25.282 27.198 1.00118.49 C
ANISOU 4535 CB ALA A 576 13264 19972 11783 -1249 1228 -1693 C
ATOM 4536 N LYS A 577 19.930 28.413 27.932 1.00114.66 N
ANISOU 4536 N LYS A 577 13136 19347 11084 -1872 1186 -782 N
ATOM 4537 CA LYS A 577 19.585 29.583 28.726 1.00107.95 C
ANISOU 4537 CA LYS A 577 12546 18152 10320 -2011 1049 -401 C
ATOM 4538 C LYS A 577 18.133 29.607 29.179 1.00110.79 C
ANISOU 4538 C LYS A 577 13216 18088 10791 -1846 848 -266 C
ATOM 4539 O LYS A 577 17.725 30.579 29.821 1.00117.11 O
ANISOU 4539 O LYS A 577 14240 18588 11670 -1935 727 20 O
ATOM 4540 CB LYS A 577 19.881 30.872 27.947 1.00 97.91 C
ANISOU 4540 CB LYS A 577 11360 17103 8738 -2392 1140 -81 C
ATOM 4541 CG LYS A 577 21.346 31.107 27.634 1.00105.99 C
ANISOU 4541 CG LYS A 577 12082 18528 9660 -2627 1345 -145 C
ATOM 4542 CD LYS A 577 21.532 32.393 26.843 1.00118.50 C
ANISOU 4542 CD LYS A 577 13785 20304 10934 -3034 1429 224 C
ATOM 4543 CE LYS A 577 22.996 32.641 26.514 1.00138.55 C
ANISOU 4543 CE LYS A 577 16002 23274 13368 -3307 1655 167 C
ATOM 4544 NZ LYS A 577 23.186 33.882 25.713 1.00151.15 N
ANISOU 4544 NZ LYS A 577 17718 25058 14654 -3740 1745 563 N
ATOM 4545 N ASN A 578 17.338 28.582 28.882 1.00106.33 N
ANISOU 4545 N ASN A 578 12659 17488 10253 -1612 809 -482 N
ATOM 4546 CA ASN A 578 15.917 28.690 29.172 1.00 99.51 C
ANISOU 4546 CA ASN A 578 12070 16278 9460 -1496 636 -343 C
ATOM 4547 C ASN A 578 15.299 27.316 29.393 1.00 97.94 C
ANISOU 4547 C ASN A 578 11812 15938 9463 -1197 579 -637 C
ATOM 4548 O ASN A 578 15.937 26.275 29.211 1.00 97.87 O
ANISOU 4548 O ASN A 578 11563 16091 9531 -1072 665 -954 O
ATOM 4549 CB ASN A 578 15.190 29.442 28.050 1.00106.63 C
ANISOU 4549 CB ASN A 578 13155 17330 10031 -1664 625 -128 C
ATOM 4550 CG ASN A 578 13.909 30.094 28.525 1.00129.28 C
ANISOU 4550 CG ASN A 578 16316 19808 12995 -1614 430 125 C
ATOM 4551 OD1 ASN A 578 13.398 29.771 29.598 1.00117.93 O
ANISOU 4551 OD1 ASN A 578 14937 18024 11849 -1429 323 82 O
ATOM 4552 ND2 ASN A 578 13.383 31.020 27.730 1.00136.42 N
ANISOU 4552 ND2 ASN A 578 17400 20780 13653 -1780 381 396 N
ATOM 4553 N MET A 579 14.026 27.348 29.782 1.00 90.85 N
ANISOU 4553 N MET A 579 11130 14723 8667 -1090 429 -529 N
ATOM 4554 CA MET A 579 13.268 26.163 30.154 1.00 85.49 C
ANISOU 4554 CA MET A 579 10435 13829 8217 -838 352 -742 C
ATOM 4555 C MET A 579 12.877 25.353 28.926 1.00106.03 C
ANISOU 4555 C MET A 579 12952 16678 10657 -783 399 -1000 C
ATOM 4556 O MET A 579 12.437 25.902 27.913 1.00126.70 O
ANISOU 4556 O MET A 579 15659 19511 12972 -914 407 -906 O
ATOM 4557 CB MET A 579 12.010 26.596 30.906 1.00 83.90 C
ANISOU 4557 CB MET A 579 10476 13258 8144 -781 195 -531 C
ATOM 4558 CG MET A 579 11.512 25.675 31.992 1.00104.69 C
ANISOU 4558 CG MET A 579 13108 15567 11102 -570 113 -630 C
ATOM 4559 SD MET A 579 9.921 26.279 32.601 1.00109.00 S
ANISOU 4559 SD MET A 579 13909 15784 11723 -536 -34 -408 S
ATOM 4560 CE MET A 579 10.132 28.054 32.430 1.00 83.47 C
ANISOU 4560 CE MET A 579 10834 12598 8282 -758 -48 -89 C
ATOM 4561 N ASN A 580 13.024 24.034 29.022 1.00104.22 N
ANISOU 4561 N ASN A 580 12555 16408 10637 -587 413 -1329 N
ATOM 4562 CA ASN A 580 12.592 23.142 27.956 1.00112.69 C
ANISOU 4562 CA ASN A 580 13540 17667 11610 -510 440 -1637 C
ATOM 4563 C ASN A 580 12.042 21.863 28.562 1.00116.86 C
ANISOU 4563 C ASN A 580 14029 17863 12511 -273 347 -1858 C
ATOM 4564 O ASN A 580 12.594 21.334 29.530 1.00104.61 O
ANISOU 4564 O ASN A 580 12394 16090 11264 -150 328 -1899 O
ATOM 4565 CB ASN A 580 13.730 22.814 26.984 1.00 93.64 C
ANISOU 4565 CB ASN A 580 10875 15708 8995 -563 619 -1917 C
ATOM 4566 CG ASN A 580 13.247 22.048 25.767 1.00110.06 C
ANISOU 4566 CG ASN A 580 12878 18040 10898 -514 649 -2248 C
ATOM 4567 OD1 ASN A 580 12.048 21.969 25.506 1.00127.23 O
ANISOU 4567 OD1 ASN A 580 15207 20097 13037 -487 531 -2215 O
ATOM 4568 ND2 ASN A 580 14.183 21.477 25.015 1.00116.83 N
ANISOU 4568 ND2 ASN A 580 13480 19266 11645 -500 807 -2596 N
ATOM 4569 N VAL A 581 10.952 21.371 27.976 1.00121.29 N
ANISOU 4569 N VAL A 581 14648 18392 13046 -221 277 -1989 N
ATOM 4570 CA VAL A 581 10.291 20.189 28.509 1.00110.63 C
ANISOU 4570 CA VAL A 581 13278 16698 12058 -32 181 -2171 C
ATOM 4571 C VAL A 581 10.823 18.895 27.890 1.00107.42 C
ANISOU 4571 C VAL A 581 12639 16401 11776 105 239 -2633 C
ATOM 4572 O VAL A 581 10.595 17.811 28.448 1.00106.42 O
ANISOU 4572 O VAL A 581 12462 15949 12025 271 165 -2794 O
ATOM 4573 CB VAL A 581 8.766 20.333 28.328 1.00 86.44 C
ANISOU 4573 CB VAL A 581 10385 13497 8960 -51 58 -2073 C
ATOM 4574 CG1 VAL A 581 8.417 20.635 26.871 1.00104.53 C
ANISOU 4574 CG1 VAL A 581 12675 16180 10863 -155 78 -2183 C
ATOM 4575 CG2 VAL A 581 8.031 19.117 28.833 1.00 84.78 C
ANISOU 4575 CG2 VAL A 581 10148 12939 9125 104 -32 -2251 C
ATOM 4576 N ARG A 582 11.548 18.980 26.772 1.00105.03 N
ANISOU 4576 N ARG A 582 12187 16544 11176 36 372 -2851 N
ATOM 4577 CA ARG A 582 12.122 17.794 26.122 1.00107.37 C
ANISOU 4577 CA ARG A 582 12234 16984 11578 176 443 -3348 C
ATOM 4578 C ARG A 582 12.781 16.808 27.079 1.00123.55 C
ANISOU 4578 C ARG A 582 14141 18694 14107 388 407 -3495 C
ATOM 4579 O ARG A 582 12.553 15.599 26.936 1.00113.28 O
ANISOU 4579 O ARG A 582 12739 17210 13093 558 353 -3841 O
ATOM 4580 CB ARG A 582 13.118 18.244 25.043 1.00128.67 C
ANISOU 4580 CB ARG A 582 14766 20253 13869 48 633 -3498 C
ATOM 4581 CG ARG A 582 13.992 17.114 24.520 1.00145.67 C
ANISOU 4581 CG ARG A 582 16611 22582 16154 209 738 -4033 C
ATOM 4582 CD ARG A 582 15.136 17.641 23.653 1.00161.07 C
ANISOU 4582 CD ARG A 582 18366 25120 17714 67 958 -4146 C
ATOM 4583 NE ARG A 582 16.054 18.495 24.404 1.00164.15 N
ANISOU 4583 NE ARG A 582 18738 25517 18114 -33 1018 -3818 N
ATOM 4584 CZ ARG A 582 17.149 18.075 25.022 1.00155.63 C
ANISOU 4584 CZ ARG A 582 17435 24372 17325 98 1063 -3955 C
ATOM 4585 NH1 ARG A 582 17.488 16.795 25.035 1.00154.49 N
ANISOU 4585 NH1 ARG A 582 17070 24106 17523 357 1047 -4398 N
ATOM 4586 NH2 ARG A 582 17.917 18.961 25.647 1.00146.77 N
ANISOU 4586 NH2 ARG A 582 16305 23292 16169 -29 1107 -3644 N
ATOM 4587 N PRO A 583 13.571 17.242 28.059 1.00122.66 N
ANISOU 4587 N PRO A 583 14018 18470 14116 390 414 -3251 N
ATOM 4588 CA PRO A 583 14.145 16.288 29.021 1.00102.30 C
ANISOU 4588 CA PRO A 583 11318 15551 12000 605 340 -3350 C
ATOM 4589 C PRO A 583 13.071 15.512 29.750 1.00107.98 C
ANISOU 4589 C PRO A 583 12184 15774 13070 717 172 -3284 C
ATOM 4590 O PRO A 583 13.165 14.291 29.862 1.00111.35 O
ANISOU 4590 O PRO A 583 12492 15956 13859 906 108 -3556 O
ATOM 4591 CB PRO A 583 14.944 17.184 29.985 1.00101.20 C
ANISOU 4591 CB PRO A 583 11203 15408 11841 531 349 -3005 C
ATOM 4592 CG PRO A 583 15.096 18.511 29.277 1.00110.72 C
ANISOU 4592 CG PRO A 583 12469 17023 12578 277 474 -2830 C
ATOM 4593 CD PRO A 583 14.112 18.605 28.185 1.00105.70 C
ANISOU 4593 CD PRO A 583 11935 16555 11670 189 493 -2915 C
ATOM 4594 N LEU A 584 12.037 16.207 30.228 1.00106.22 N
ANISOU 4594 N LEU A 584 12210 15396 12753 597 103 -2933 N
ATOM 4595 CA LEU A 584 10.908 15.536 30.852 1.00102.01 C
ANISOU 4595 CA LEU A 584 11808 14442 12511 662 -32 -2861 C
ATOM 4596 C LEU A 584 10.321 14.499 29.902 1.00109.49 C
ANISOU 4596 C LEU A 584 12668 15370 13562 733 -54 -3261 C
ATOM 4597 O LEU A 584 10.000 13.369 30.297 1.00106.59 O
ANISOU 4597 O LEU A 584 12272 14637 13592 863 -150 -3394 O
ATOM 4598 CB LEU A 584 9.836 16.543 31.248 1.00 89.62 C
ANISOU 4598 CB LEU A 584 10479 12812 10760 511 -74 -2490 C
ATOM 4599 CG LEU A 584 8.438 16.038 31.624 1.00 87.79 C
ANISOU 4599 CG LEU A 584 10372 12252 10730 521 -183 -2428 C
ATOM 4600 CD1 LEU A 584 8.520 15.168 32.856 1.00 87.81 C
ANISOU 4600 CD1 LEU A 584 10380 11841 11144 638 -265 -2334 C
ATOM 4601 CD2 LEU A 584 7.525 17.205 31.873 1.00 90.86 C
ANISOU 4601 CD2 LEU A 584 10955 12673 10894 381 -203 -2104 C
ATOM 4602 N LEU A 585 10.180 14.872 28.631 1.00104.75 N
ANISOU 4602 N LEU A 585 12029 15168 12605 639 27 -3454 N
ATOM 4603 CA LEU A 585 9.588 13.961 27.662 1.00106.16 C
ANISOU 4603 CA LEU A 585 12125 15379 12834 690 0 -3866 C
ATOM 4604 C LEU A 585 10.503 12.772 27.426 1.00113.14 C
ANISOU 4604 C LEU A 585 12766 16211 14011 882 27 -4311 C
ATOM 4605 O LEU A 585 10.057 11.618 27.431 1.00118.21 O
ANISOU 4605 O LEU A 585 13360 16538 15018 1002 -68 -4576 O
ATOM 4606 CB LEU A 585 9.303 14.707 26.357 1.00119.71 C
ANISOU 4606 CB LEU A 585 13855 17592 14036 536 74 -3950 C
ATOM 4607 CG LEU A 585 8.364 15.911 26.451 1.00108.37 C
ANISOU 4607 CG LEU A 585 12649 16209 12316 365 23 -3530 C
ATOM 4608 CD1 LEU A 585 8.340 16.694 25.153 1.00111.60 C
ANISOU 4608 CD1 LEU A 585 13064 17141 12198 216 91 -3571 C
ATOM 4609 CD2 LEU A 585 6.975 15.417 26.753 1.00101.75 C
ANISOU 4609 CD2 LEU A 585 11914 15034 11712 386 -124 -3510 C
ATOM 4610 N ASN A 586 11.802 13.041 27.246 1.00109.05 N
ANISOU 4610 N ASN A 586 12082 15983 13369 914 151 -4400 N
ATOM 4611 CA ASN A 586 12.785 11.970 27.115 1.00109.51 C
ANISOU 4611 CA ASN A 586 11879 15991 13738 1127 175 -4822 C
ATOM 4612 C ASN A 586 12.703 11.036 28.305 1.00100.21 C
ANISOU 4612 C ASN A 586 10729 14212 13132 1305 11 -4728 C
ATOM 4613 O ASN A 586 12.794 9.811 28.162 1.00 98.89 O
ANISOU 4613 O ASN A 586 10427 13791 13355 1490 -58 -5097 O
ATOM 4614 CB ASN A 586 14.196 12.554 27.015 1.00115.48 C
ANISOU 4614 CB ASN A 586 12452 17126 14299 1119 327 -4832 C
ATOM 4615 CG ASN A 586 15.276 11.483 26.927 1.00140.76 C
ANISOU 4615 CG ASN A 586 15348 20287 17849 1368 348 -5279 C
ATOM 4616 OD1 ASN A 586 15.012 10.352 26.514 1.00145.25 O
ANISOU 4616 OD1 ASN A 586 15817 20671 18700 1527 289 -5696 O
ATOM 4617 ND2 ASN A 586 16.496 11.835 27.313 1.00136.70 N
ANISOU 4617 ND2 ASN A 586 14670 19934 17338 1406 421 -5212 N
ATOM 4618 N TYR A 587 12.533 11.600 29.499 1.00102.28 N
ANISOU 4618 N TYR A 587 11171 14239 13453 1246 -60 -4231 N
ATOM 4619 CA TYR A 587 12.412 10.764 30.684 1.00107.24 C
ANISOU 4619 CA TYR A 587 11851 14320 14574 1386 -220 -4073 C
ATOM 4620 C TYR A 587 11.246 9.794 30.563 1.00103.59 C
ANISOU 4620 C TYR A 587 11467 13491 14402 1409 -332 -4214 C
ATOM 4621 O TYR A 587 11.326 8.656 31.037 1.00102.82 O
ANISOU 4621 O TYR A 587 11316 12965 14785 1570 -454 -4320 O
ATOM 4622 CB TYR A 587 12.263 11.655 31.915 1.00105.24 C
ANISOU 4622 CB TYR A 587 11798 13952 14236 1279 -262 -3518 C
ATOM 4623 CG TYR A 587 12.185 10.921 33.232 1.00100.79 C
ANISOU 4623 CG TYR A 587 11307 12885 14104 1392 -422 -3279 C
ATOM 4624 CD1 TYR A 587 10.964 10.476 33.722 1.00100.18 C
ANISOU 4624 CD1 TYR A 587 11405 12444 14216 1338 -520 -3110 C
ATOM 4625 CD2 TYR A 587 13.321 10.685 33.993 1.00100.52 C
ANISOU 4625 CD2 TYR A 587 11160 12759 14274 1540 -481 -3203 C
ATOM 4626 CE1 TYR A 587 10.876 9.812 34.929 1.00 95.75 C
ANISOU 4626 CE1 TYR A 587 10921 11444 14015 1412 -659 -2850 C
ATOM 4627 CE2 TYR A 587 13.243 10.021 35.205 1.00102.40 C
ANISOU 4627 CE2 TYR A 587 11480 12552 14876 1636 -646 -2942 C
ATOM 4628 CZ TYR A 587 12.016 9.586 35.669 1.00 90.47 C
ANISOU 4628 CZ TYR A 587 10160 10688 13525 1563 -728 -2754 C
ATOM 4629 OH TYR A 587 11.927 8.923 36.874 1.00 91.13 O
ANISOU 4629 OH TYR A 587 10335 10350 13942 1630 -884 -2459 O
ATOM 4630 N PHE A 588 10.161 10.219 29.920 1.00104.27 N
ANISOU 4630 N PHE A 588 11670 13730 14218 1244 -307 -4215 N
ATOM 4631 CA PHE A 588 8.952 9.415 29.818 1.00101.40 C
ANISOU 4631 CA PHE A 588 11377 13045 14104 1224 -413 -4326 C
ATOM 4632 C PHE A 588 8.743 8.771 28.454 1.00106.44 C
ANISOU 4632 C PHE A 588 11869 13866 14707 1257 -391 -4884 C
ATOM 4633 O PHE A 588 7.745 8.066 28.279 1.00110.07 O
ANISOU 4633 O PHE A 588 12365 14069 15387 1230 -488 -5028 O
ATOM 4634 CB PHE A 588 7.719 10.262 30.157 1.00 89.90 C
ANISOU 4634 CB PHE A 588 10143 11591 12425 1026 -433 -3941 C
ATOM 4635 CG PHE A 588 7.544 10.544 31.624 1.00 87.00 C
ANISOU 4635 CG PHE A 588 9933 10916 12207 996 -489 -3446 C
ATOM 4636 CD1 PHE A 588 7.102 9.548 32.478 1.00 88.35 C
ANISOU 4636 CD1 PHE A 588 10147 10592 12832 1046 -605 -3351 C
ATOM 4637 CD2 PHE A 588 7.779 11.804 32.142 1.00 86.44 C
ANISOU 4637 CD2 PHE A 588 9971 11053 11817 902 -428 -3077 C
ATOM 4638 CE1 PHE A 588 6.919 9.796 33.827 1.00 87.81 C
ANISOU 4638 CE1 PHE A 588 10222 10288 12853 1003 -647 -2893 C
ATOM 4639 CE2 PHE A 588 7.595 12.055 33.494 1.00 87.56 C
ANISOU 4639 CE2 PHE A 588 10252 10944 12071 874 -477 -2660 C
ATOM 4640 CZ PHE A 588 7.165 11.053 34.334 1.00 85.89 C
ANISOU 4640 CZ PHE A 588 10079 10289 12268 922 -581 -2566 C
ATOM 4641 N GLU A 589 9.637 8.996 27.489 1.00 99.05 N
ANISOU 4641 N GLU A 589 10760 13383 13491 1298 -264 -5210 N
ATOM 4642 CA GLU A 589 9.420 8.479 26.139 1.00 99.87 C
ANISOU 4642 CA GLU A 589 10727 13745 13476 1310 -230 -5758 C
ATOM 4643 C GLU A 589 9.040 7.002 26.094 1.00119.34 C
ANISOU 4643 C GLU A 589 13107 15753 16485 1453 -362 -6152 C
ATOM 4644 O GLU A 589 8.101 6.663 25.352 1.00134.69 O
ANISOU 4644 O GLU A 589 15064 17729 18384 1377 -413 -6415 O
ATOM 4645 CB GLU A 589 10.656 8.723 25.260 1.00107.00 C
ANISOU 4645 CB GLU A 589 11408 15170 14076 1367 -59 -6090 C
ATOM 4646 CG GLU A 589 10.504 8.100 23.878 1.00136.08 C
ANISOU 4646 CG GLU A 589 14928 19147 17628 1395 -17 -6714 C
ATOM 4647 CD GLU A 589 11.522 8.585 22.872 1.00168.64 C
ANISOU 4647 CD GLU A 589 18858 23928 21290 1376 188 -6993 C
ATOM 4648 OE1 GLU A 589 12.284 9.520 23.192 1.00178.26 O
ANISOU 4648 OE1 GLU A 589 20082 25391 22259 1306 301 -6663 O
ATOM 4649 OE2 GLU A 589 11.567 8.015 21.759 1.00161.91 O1-
ANISOU 4649 OE2 GLU A 589 17837 23359 20322 1421 241 -7558 O1-
ATOM 4650 N PRO A 590 9.690 6.089 26.831 1.00111.33 N
ANISOU 4650 N PRO A 590 12006 14297 15999 1652 -441 -6210 N
ATOM 4651 CA PRO A 590 9.232 4.693 26.799 1.00122.27 C
ANISOU 4651 CA PRO A 590 13335 15180 17941 1767 -588 -6554 C
ATOM 4652 C PRO A 590 7.813 4.509 27.319 1.00117.86 C
ANISOU 4652 C PRO A 590 12982 14238 17562 1606 -717 -6267 C
ATOM 4653 O PRO A 590 7.132 3.564 26.901 1.00103.60 O
ANISOU 4653 O PRO A 590 11137 12164 16064 1610 -816 -6610 O
ATOM 4654 CB PRO A 590 10.252 3.974 27.687 1.00111.38 C
ANISOU 4654 CB PRO A 590 11860 13391 17066 2003 -665 -6511 C
ATOM 4655 CG PRO A 590 11.481 4.787 27.595 1.00106.45 C
ANISOU 4655 CG PRO A 590 11112 13231 16102 2059 -516 -6469 C
ATOM 4656 CD PRO A 590 10.987 6.209 27.526 1.00103.72 C
ANISOU 4656 CD PRO A 590 10945 13312 15152 1801 -405 -6064 C
ATOM 4657 N LEU A 591 7.351 5.361 28.241 1.00109.40 N
ANISOU 4657 N LEU A 591 12113 13125 16327 1461 -716 -5669 N
ATOM 4658 CA LEU A 591 5.942 5.319 28.616 1.00109.16 C
ANISOU 4658 CA LEU A 591 12247 12840 16387 1284 -804 -5425 C
ATOM 4659 C LEU A 591 5.079 5.981 27.556 1.00119.71 C
ANISOU 4659 C LEU A 591 13602 14618 17264 1121 -757 -5576 C
ATOM 4660 O LEU A 591 3.927 5.581 27.357 1.00124.38 O
ANISOU 4660 O LEU A 591 14227 15043 17986 1011 -846 -5661 O
ATOM 4661 CB LEU A 591 5.716 5.980 29.978 1.00104.10 C
ANISOU 4661 CB LEU A 591 11798 12024 15730 1195 -813 -4773 C
ATOM 4662 CG LEU A 591 4.268 5.957 30.495 1.00 99.87 C
ANISOU 4662 CG LEU A 591 11411 11237 15297 1008 -882 -4494 C
ATOM 4663 CD1 LEU A 591 3.778 4.534 30.708 1.00117.26 C
ANISOU 4663 CD1 LEU A 591 13578 12884 18092 1031 -1016 -4669 C
ATOM 4664 CD2 LEU A 591 4.130 6.740 31.787 1.00 95.09 C
ANISOU 4664 CD2 LEU A 591 10979 10561 14591 924 -859 -3890 C
ATOM 4665 N PHE A 592 5.628 6.975 26.851 1.00120.09 N
ANISOU 4665 N PHE A 592 13618 15230 16778 1096 -629 -5608 N
ATOM 4666 CA PHE A 592 4.871 7.653 25.805 1.00120.84 C
ANISOU 4666 CA PHE A 592 13738 15776 16400 946 -604 -5717 C
ATOM 4667 C PHE A 592 4.538 6.707 24.656 1.00106.57 C
ANISOU 4667 C PHE A 592 11779 14034 14678 979 -657 -6340 C
ATOM 4668 O PHE A 592 3.426 6.745 24.118 1.00113.41 O
ANISOU 4668 O PHE A 592 12681 14988 15422 853 -734 -6430 O
ATOM 4669 CB PHE A 592 5.652 8.864 25.292 1.00125.78 C
ANISOU 4669 CB PHE A 592 14362 16975 16452 904 -457 -5600 C
ATOM 4670 CG PHE A 592 4.889 9.699 24.305 1.00121.43 C
ANISOU 4670 CG PHE A 592 13869 16885 15382 744 -452 -5601 C
ATOM 4671 CD1 PHE A 592 3.553 9.996 24.518 1.00110.73 C
ANISOU 4671 CD1 PHE A 592 12649 15402 14021 620 -563 -5364 C
ATOM 4672 CD2 PHE A 592 5.502 10.177 23.159 1.00120.92 C
ANISOU 4672 CD2 PHE A 592 13715 17397 14833 716 -340 -5834 C
ATOM 4673 CE1 PHE A 592 2.843 10.760 23.609 1.00104.64 C
ANISOU 4673 CE1 PHE A 592 11924 15045 12788 493 -591 -5353 C
ATOM 4674 CE2 PHE A 592 4.798 10.942 22.245 1.00117.33 C
ANISOU 4674 CE2 PHE A 592 13327 17368 13885 567 -360 -5797 C
ATOM 4675 CZ PHE A 592 3.467 11.233 22.471 1.00109.26 C
ANISOU 4675 CZ PHE A 592 12442 16189 12882 467 -499 -5555 C
ATOM 4676 N THR A 593 5.484 5.852 24.263 1.00 94.53 N
ANISOU 4676 N THR A 593 10070 12475 13370 1155 -626 -6803 N
ATOM 4677 CA THR A 593 5.211 4.915 23.177 1.00111.52 C
ANISOU 4677 CA THR A 593 12066 14684 15622 1198 -677 -7457 C
ATOM 4678 C THR A 593 4.400 3.713 23.646 1.00118.02 C
ANISOU 4678 C THR A 593 12900 14859 17082 1211 -851 -7583 C
ATOM 4679 O THR A 593 3.641 3.142 22.857 1.00126.13 O
ANISOU 4679 O THR A 593 13862 15899 18162 1154 -936 -8002 O
ATOM 4680 CB THR A 593 6.515 4.449 22.532 1.00102.49 C
ANISOU 4680 CB THR A 593 10697 13767 14479 1391 -569 -7965 C
ATOM 4681 OG1 THR A 593 7.392 3.930 23.539 1.00112.67 O
ANISOU 4681 OG1 THR A 593 11944 14609 16255 1575 -586 -7834 O
ATOM 4682 CG2 THR A 593 7.194 5.606 21.818 1.00101.73 C
ANISOU 4682 CG2 THR A 593 10567 14396 13692 1323 -384 -7909 C
ATOM 4683 N TRP A 594 4.549 3.310 24.911 1.00114.47 N
ANISOU 4683 N TRP A 594 12529 13849 17115 1271 -913 -7226 N
ATOM 4684 CA TRP A 594 3.675 2.276 25.454 1.00117.85 C
ANISOU 4684 CA TRP A 594 12999 13651 18128 1228 -1075 -7228 C
ATOM 4685 C TRP A 594 2.250 2.791 25.595 1.00120.19 C
ANISOU 4685 C TRP A 594 13433 13979 18257 984 -1124 -6921 C
ATOM 4686 O TRP A 594 1.289 2.054 25.342 1.00120.82 O
ANISOU 4686 O TRP A 594 13482 13804 18620 889 -1241 -7153 O
ATOM 4687 CB TRP A 594 4.203 1.783 26.800 1.00123.42 C
ANISOU 4687 CB TRP A 594 13771 13788 19337 1336 -1131 -6854 C
ATOM 4688 CG TRP A 594 3.353 0.710 27.417 1.00120.62 C
ANISOU 4688 CG TRP A 594 13470 12766 19594 1268 -1292 -6796 C
ATOM 4689 CD1 TRP A 594 3.464 -0.636 27.222 1.00118.98 C
ANISOU 4689 CD1 TRP A 594 13152 12079 19976 1382 -1419 -7222 C
ATOM 4690 CD2 TRP A 594 2.263 0.894 28.329 1.00113.48 C
ANISOU 4690 CD2 TRP A 594 12733 11598 18784 1056 -1339 -6281 C
ATOM 4691 NE1 TRP A 594 2.511 -1.301 27.954 1.00111.06 N
ANISOU 4691 NE1 TRP A 594 12251 10514 19433 1234 -1546 -6974 N
ATOM 4692 CE2 TRP A 594 1.762 -0.385 28.644 1.00107.80 C
ANISOU 4692 CE2 TRP A 594 12000 10247 18710 1028 -1488 -6397 C
ATOM 4693 CE3 TRP A 594 1.662 2.016 28.911 1.00105.76 C
ANISOU 4693 CE3 TRP A 594 11906 10857 17420 887 -1266 -5748 C
ATOM 4694 CZ2 TRP A 594 0.690 -0.574 29.514 1.00109.94 C
ANISOU 4694 CZ2 TRP A 594 12397 10153 19222 813 -1548 -5979 C
ATOM 4695 CZ3 TRP A 594 0.598 1.826 29.774 1.00106.52 C
ANISOU 4695 CZ3 TRP A 594 12114 10604 17755 700 -1324 -5372 C
ATOM 4696 CH2 TRP A 594 0.122 0.542 30.066 1.00115.33 C
ANISOU 4696 CH2 TRP A 594 13206 11127 19486 654 -1455 -5479 C
ATOM 4697 N LEU A 595 2.093 4.055 26.002 1.00115.09 N
ANISOU 4697 N LEU A 595 12923 13635 17173 882 -1042 -6418 N
ATOM 4698 CA LEU A 595 0.769 4.667 26.007 1.00112.18 C
ANISOU 4698 CA LEU A 595 12652 13379 16594 676 -1083 -6172 C
ATOM 4699 C LEU A 595 0.206 4.790 24.598 1.00113.16 C
ANISOU 4699 C LEU A 595 12681 13946 16368 608 -1116 -6615 C
ATOM 4700 O LEU A 595 -1.008 4.660 24.407 1.00120.56 O
ANISOU 4700 O LEU A 595 13620 14829 17359 464 -1218 -6653 O
ATOM 4701 CB LEU A 595 0.819 6.042 26.682 1.00107.69 C
ANISOU 4701 CB LEU A 595 12237 13049 15631 612 -992 -5587 C
ATOM 4702 CG LEU A 595 0.890 6.067 28.212 1.00101.79 C
ANISOU 4702 CG LEU A 595 11616 11885 15173 606 -985 -5060 C
ATOM 4703 CD1 LEU A 595 1.080 7.489 28.718 1.00 93.14 C
ANISOU 4703 CD1 LEU A 595 10651 11092 13644 561 -889 -4584 C
ATOM 4704 CD2 LEU A 595 -0.338 5.429 28.843 1.00100.64 C
ANISOU 4704 CD2 LEU A 595 11509 11311 15420 466 -1082 -4922 C
ATOM 4705 N LYS A 596 1.061 5.036 23.602 1.00107.05 N
ANISOU 4705 N LYS A 596 11812 13639 15223 700 -1032 -6954 N
ATOM 4706 CA LYS A 596 0.619 5.089 22.211 1.00117.05 C
ANISOU 4706 CA LYS A 596 12984 15373 16118 640 -1067 -7407 C
ATOM 4707 C LYS A 596 0.412 3.708 21.600 1.00135.94 C
ANISOU 4707 C LYS A 596 15215 17523 18914 691 -1172 -8059 C
ATOM 4708 O LYS A 596 0.205 3.607 20.388 1.00150.99 O
ANISOU 4708 O LYS A 596 17014 19834 20519 665 -1200 -8536 O
ATOM 4709 CB LYS A 596 1.614 5.873 21.345 1.00105.31 C
ANISOU 4709 CB LYS A 596 11451 14525 14039 692 -922 -7524 C
ATOM 4710 CG LYS A 596 1.561 7.380 21.511 1.00 98.92 C
ANISOU 4710 CG LYS A 596 10796 14084 12704 587 -851 -6968 C
ATOM 4711 CD LYS A 596 2.382 8.073 20.434 1.00104.35 C
ANISOU 4711 CD LYS A 596 11426 15442 12781 587 -722 -7132 C
ATOM 4712 CE LYS A 596 3.876 7.909 20.641 1.00117.27 C
ANISOU 4712 CE LYS A 596 12964 17107 14486 732 -560 -7231 C
ATOM 4713 NZ LYS A 596 4.627 8.520 19.508 1.00115.76 N
ANISOU 4713 NZ LYS A 596 12689 17612 13684 699 -416 -7430 N
ATOM 4714 N ASP A 597 0.486 2.646 22.401 1.00132.57 N
ANISOU 4714 N ASP A 597 14769 16445 19155 761 -1238 -8094 N
ATOM 4715 CA ASP A 597 0.167 1.303 21.935 1.00132.00 C
ANISOU 4715 CA ASP A 597 14561 16032 19562 791 -1365 -8682 C
ATOM 4716 C ASP A 597 -0.892 0.679 22.838 1.00132.05 C
ANISOU 4716 C ASP A 597 14639 15411 20122 652 -1500 -8426 C
ATOM 4717 O ASP A 597 -1.266 -0.482 22.644 1.00135.12 O
ANISOU 4717 O ASP A 597 14933 15430 20976 640 -1606 -8714 O
ATOM 4718 CB ASP A 597 1.453 0.457 21.854 1.00125.45 C
ANISOU 4718 CB ASP A 597 13597 15038 19031 1025 -1307 -8949 C
ATOM 4719 CG ASP A 597 1.215 -0.974 21.382 1.00142.76 C
ANISOU 4719 CG ASP A 597 15637 16900 21705 1061 -1415 -9319 C
ATOM 4720 OD1 ASP A 597 0.943 -1.864 22.219 1.00155.26 O
ANISOU 4720 OD1 ASP A 597 17256 17812 23922 1060 -1527 -9192 O
ATOM 4721 OD2 ASP A 597 1.296 -1.205 20.159 1.00149.65 O1-
ANISOU 4721 OD2 ASP A 597 16356 18193 22312 1080 -1390 -9725 O1-
ATOM 4722 N GLN A 598 -1.408 1.449 23.797 1.00129.82 N
ANISOU 4722 N GLN A 598 14513 15063 19750 531 -1473 -7770 N
ATOM 4723 CA GLN A 598 -2.525 1.049 24.638 1.00127.55 C
ANISOU 4723 CA GLN A 598 14287 14299 19877 355 -1569 -7474 C
ATOM 4724 C GLN A 598 -3.812 1.779 24.282 1.00114.95 C
ANISOU 4724 C GLN A 598 12701 13037 17937 153 -1612 -7355 C
ATOM 4725 O GLN A 598 -4.886 1.357 24.721 1.00119.51 O
ANISOU 4725 O GLN A 598 13271 13290 18849 -18 -1699 -7246 O
ATOM 4726 CB GLN A 598 -2.192 1.314 26.114 1.00116.41 C
ANISOU 4726 CB GLN A 598 13029 12549 18652 366 -1503 -6818 C
ATOM 4727 CG GLN A 598 -1.263 0.293 26.760 1.00114.79 C
ANISOU 4727 CG GLN A 598 12817 11796 19000 526 -1532 -6853 C
ATOM 4728 CD GLN A 598 -1.928 -1.034 27.051 1.00120.49 C
ANISOU 4728 CD GLN A 598 13503 11870 20409 433 -1679 -7005 C
ATOM 4729 OE1 GLN A 598 -3.050 -1.081 27.552 1.00123.93 O
ANISOU 4729 OE1 GLN A 598 13988 12111 20990 210 -1720 -6732 O
ATOM 4730 NE2 GLN A 598 -1.228 -2.125 26.758 1.00111.81 N
ANISOU 4730 NE2 GLN A 598 12307 10418 19759 600 -1757 -7442 N
ATOM 4731 N ASN A 599 -3.725 2.858 23.498 1.00110.11 N
ANISOU 4731 N ASN A 599 12097 13064 16678 166 -1559 -7365 N
ATOM 4732 CA ASN A 599 -4.857 3.721 23.181 1.00137.27 C
ANISOU 4732 CA ASN A 599 15554 16857 19748 11 -1614 -7191 C
ATOM 4733 C ASN A 599 -5.177 3.713 21.691 1.00138.58 C
ANISOU 4733 C ASN A 599 15594 17508 19551 -9 -1706 -7728 C
ATOM 4734 O ASN A 599 -5.867 4.617 21.203 1.00124.28 O
ANISOU 4734 O ASN A 599 13798 16130 17292 -91 -1756 -7600 O
ATOM 4735 CB ASN A 599 -4.579 5.150 23.654 1.00127.43 C
ANISOU 4735 CB ASN A 599 14454 15926 18037 30 -1500 -6628 C
ATOM 4736 CG ASN A 599 -4.359 5.238 25.153 1.00119.03 C
ANISOU 4736 CG ASN A 599 13514 14438 17273 33 -1418 -6092 C
ATOM 4737 OD1 ASN A 599 -4.849 4.406 25.916 1.00118.58 O
ANISOU 4737 OD1 ASN A 599 13446 13881 17727 -42 -1463 -6018 O
ATOM 4738 ND2 ASN A 599 -3.604 6.245 25.581 1.00108.00 N
ANISOU 4738 ND2 ASN A 599 12236 13249 15553 107 -1299 -5714 N
ATOM 4739 N LYS A 600 -4.675 2.714 20.959 1.00136.21 N
ANISOU 4739 N LYS A 600 15168 17151 19434 74 -1740 -8337 N
ATOM 4740 CA LYS A 600 -4.898 2.652 19.518 1.00130.46 C
ANISOU 4740 CA LYS A 600 14318 16931 18318 66 -1796 -8785 C
ATOM 4741 C LYS A 600 -6.384 2.666 19.188 1.00131.19 C
ANISOU 4741 C LYS A 600 14355 17092 18400 -115 -1960 -8794 C
ATOM 4742 O LYS A 600 -6.823 3.391 18.288 1.00145.51 O
ANISOU 4742 O LYS A 600 16152 19464 19673 -159 -2012 -8813 O
ATOM 4743 CB LYS A 600 -4.231 1.400 18.945 1.00135.53 C
ANISOU 4743 CB LYS A 600 14819 17412 19262 194 -1763 -9216 C
ATOM 4744 CG LYS A 600 -4.079 1.383 17.430 1.00137.69 C
ANISOU 4744 CG LYS A 600 14968 18286 19062 231 -1746 -9591 C
ATOM 4745 CD LYS A 600 -3.851 2.774 16.857 1.00142.73 C
ANISOU 4745 CD LYS A 600 15686 19617 18927 212 -1677 -9391 C
ATOM 4746 CE LYS A 600 -3.484 2.699 15.385 1.00145.59 C
ANISOU 4746 CE LYS A 600 15925 20563 18828 253 -1629 -9739 C
ATOM 4747 NZ LYS A 600 -3.874 3.935 14.656 1.00148.11 N
ANISOU 4747 NZ LYS A 600 16320 21527 18427 158 -1650 -9518 N
ATOM 4748 N ASN A 601 -7.174 1.876 19.914 1.00123.54 N
ANISOU 4748 N ASN A 601 13351 15561 18028 -228 -2046 -8755 N
ATOM 4749 CA ASN A 601 -8.617 1.801 19.730 1.00119.84 C
ANISOU 4749 CA ASN A 601 12797 15101 17634 -413 -2196 -8760 C
ATOM 4750 C ASN A 601 -9.364 2.564 20.815 1.00117.84 C
ANISOU 4750 C ASN A 601 12620 14695 17458 -548 -2220 -8285 C
ATOM 4751 O ASN A 601 -10.451 2.156 21.240 1.00116.52 O
ANISOU 4751 O ASN A 601 12374 14235 17664 -720 -2310 -8228 O
ATOM 4752 CB ASN A 601 -9.062 0.339 19.674 1.00117.65 C
ANISOU 4752 CB ASN A 601 12396 14348 17957 -473 -2263 -9042 C
ATOM 4753 CG ASN A 601 -8.427 -0.408 18.522 1.00122.29 C
ANISOU 4753 CG ASN A 601 12879 15129 18456 -336 -2245 -9519 C
ATOM 4754 OD1 ASN A 601 -8.237 0.148 17.439 1.00123.22 O
ANISOU 4754 OD1 ASN A 601 12966 15854 17999 -277 -2236 -9690 O
ATOM 4755 ND2 ASN A 601 -8.078 -1.665 18.752 1.00131.50 N
ANISOU 4755 ND2 ASN A 601 13989 15784 20191 -287 -2243 -9720 N
ATOM 4756 N SER A 602 -8.780 3.667 21.273 1.00108.42 N
ANISOU 4756 N SER A 602 11580 13719 15894 -454 -2083 -7790 N
ATOM 4757 CA SER A 602 -9.359 4.530 22.292 1.00114.98 C
ANISOU 4757 CA SER A 602 12506 14482 16700 -521 -2030 -7164 C
ATOM 4758 C SER A 602 -9.221 5.980 21.851 1.00110.71 C
ANISOU 4758 C SER A 602 12055 14520 15491 -452 -2006 -6894 C
ATOM 4759 O SER A 602 -8.287 6.332 21.129 1.00121.69 O
ANISOU 4759 O SER A 602 13491 16267 16479 -338 -1955 -7034 O
ATOM 4760 CB SER A 602 -8.673 4.335 23.649 1.00129.28 C
ANISOU 4760 CB SER A 602 14444 15814 18862 -476 -1876 -6753 C
ATOM 4761 OG SER A 602 -8.739 2.986 24.073 1.00136.83 O
ANISOU 4761 OG SER A 602 15338 16199 20453 -538 -1911 -6957 O
ATOM 4762 N PHE A 603 -10.157 6.821 22.283 1.00 96.11 N
ANISOU 4762 N PHE A 603 10222 12760 13534 -526 -2043 -6506 N
ATOM 4763 CA PHE A 603 -10.174 8.217 21.861 1.00 94.09 C
ANISOU 4763 CA PHE A 603 10050 13004 12695 -467 -2060 -6232 C
ATOM 4764 C PHE A 603 -9.156 8.985 22.687 1.00 95.38 C
ANISOU 4764 C PHE A 603 10401 13110 12727 -366 -1873 -5775 C
ATOM 4765 O PHE A 603 -9.231 8.963 23.916 1.00 98.03 O
ANISOU 4765 O PHE A 603 10795 13074 13380 -389 -1777 -5435 O
ATOM 4766 CB PHE A 603 -11.576 8.815 22.021 1.00 93.64 C
ANISOU 4766 CB PHE A 603 9917 13038 12623 -559 -2188 -6021 C
ATOM 4767 CG PHE A 603 -11.698 10.205 21.448 1.00 96.10 C
ANISOU 4767 CG PHE A 603 10304 13846 12363 -490 -2260 -5776 C
ATOM 4768 CD1 PHE A 603 -11.172 10.498 20.210 1.00107.19 C
ANISOU 4768 CD1 PHE A 603 11734 15719 13273 -434 -2326 -6000 C
ATOM 4769 CD2 PHE A 603 -12.283 11.230 22.183 1.00 94.45 C
ANISOU 4769 CD2 PHE A 603 10146 13626 12113 -479 -2252 -5307 C
ATOM 4770 CE1 PHE A 603 -11.237 11.774 19.687 1.00118.28 C
ANISOU 4770 CE1 PHE A 603 13230 17555 14158 -383 -2401 -5726 C
ATOM 4771 CE2 PHE A 603 -12.351 12.523 21.659 1.00 98.95 C
ANISOU 4771 CE2 PHE A 603 10800 14602 12194 -404 -2336 -5063 C
ATOM 4772 CZ PHE A 603 -11.822 12.787 20.404 1.00116.97 C
ANISOU 4772 CZ PHE A 603 13123 17329 13992 -363 -2417 -5252 C
ATOM 4773 N VAL A 604 -8.177 9.611 22.034 1.00 90.56 N
ANISOU 4773 N VAL A 604 9878 12872 11658 -268 -1816 -5780 N
ATOM 4774 CA VAL A 604 -7.178 10.439 22.697 1.00109.91 C
ANISOU 4774 CA VAL A 604 12494 15326 13939 -185 -1652 -5368 C
ATOM 4775 C VAL A 604 -7.603 11.881 22.508 1.00108.71 C
ANISOU 4775 C VAL A 604 12434 15524 13349 -189 -1705 -4999 C
ATOM 4776 O VAL A 604 -7.529 12.417 21.396 1.00103.65 O
ANISOU 4776 O VAL A 604 11797 15342 12243 -182 -1783 -5104 O
ATOM 4777 CB VAL A 604 -5.766 10.189 22.151 1.00112.96 C
ANISOU 4777 CB VAL A 604 12898 15880 14142 -91 -1539 -5604 C
ATOM 4778 CG1 VAL A 604 -4.792 11.230 22.723 1.00 92.47 C
ANISOU 4778 CG1 VAL A 604 10460 13370 11306 -29 -1388 -5162 C
ATOM 4779 CG2 VAL A 604 -5.302 8.759 22.522 1.00116.37 C
ANISOU 4779 CG2 VAL A 604 13244 15870 15102 -53 -1495 -5933 C
ATOM 4780 N GLY A 605 -8.050 12.501 23.589 1.00106.87 N
ANISOU 4780 N GLY A 605 12272 15073 13262 -200 -1668 -4570 N
ATOM 4781 CA GLY A 605 -8.673 13.808 23.528 1.00 94.40 C
ANISOU 4781 CA GLY A 605 10756 13731 11380 -194 -1749 -4235 C
ATOM 4782 C GLY A 605 -9.848 13.865 24.482 1.00100.34 C
ANISOU 4782 C GLY A 605 11447 14210 12468 -242 -1783 -4037 C
ATOM 4783 O GLY A 605 -10.172 12.902 25.175 1.00116.98 O
ANISOU 4783 O GLY A 605 13470 15963 15012 -307 -1736 -4132 O
ATOM 4784 N TRP A 606 -10.482 15.034 24.509 1.00 90.75 N
ANISOU 4784 N TRP A 606 10269 13169 11045 -213 -1865 -3752 N
ATOM 4785 CA TRP A 606 -11.675 15.231 25.320 1.00100.99 C
ANISOU 4785 CA TRP A 606 11475 14286 12612 -245 -1901 -3587 C
ATOM 4786 C TRP A 606 -12.607 16.210 24.618 1.00112.77 C
ANISOU 4786 C TRP A 606 12916 16093 13839 -202 -2107 -3511 C
ATOM 4787 O TRP A 606 -12.178 17.077 23.856 1.00122.85 O
ANISOU 4787 O TRP A 606 14306 17669 14703 -136 -2183 -3401 O
ATOM 4788 CB TRP A 606 -11.343 15.751 26.733 1.00105.12 C
ANISOU 4788 CB TRP A 606 12115 14543 13284 -218 -1723 -3202 C
ATOM 4789 CG TRP A 606 -10.316 16.845 26.795 1.00107.21 C
ANISOU 4789 CG TRP A 606 12582 14932 13222 -128 -1652 -2919 C
ATOM 4790 CD1 TRP A 606 -10.529 18.168 26.544 1.00103.26 C
ANISOU 4790 CD1 TRP A 606 12161 14638 12435 -60 -1740 -2676 C
ATOM 4791 CD2 TRP A 606 -8.921 16.714 27.109 1.00 99.20 C
ANISOU 4791 CD2 TRP A 606 11702 13834 12154 -105 -1494 -2854 C
ATOM 4792 NE1 TRP A 606 -9.362 18.871 26.713 1.00103.35 N
ANISOU 4792 NE1 TRP A 606 12356 14684 12228 -18 -1635 -2455 N
ATOM 4793 CE2 TRP A 606 -8.360 18.003 27.051 1.00 97.98 C
ANISOU 4793 CE2 TRP A 606 11701 13850 11675 -45 -1481 -2568 C
ATOM 4794 CE3 TRP A 606 -8.092 15.633 27.436 1.00 86.89 C
ANISOU 4794 CE3 TRP A 606 10139 12061 10815 -124 -1375 -3010 C
ATOM 4795 CZ2 TRP A 606 -7.016 18.245 27.306 1.00 94.25 C
ANISOU 4795 CZ2 TRP A 606 11362 13369 11080 -22 -1343 -2445 C
ATOM 4796 CZ3 TRP A 606 -6.750 15.878 27.690 1.00 94.37 C
ANISOU 4796 CZ3 TRP A 606 11214 13005 11637 -74 -1248 -2888 C
ATOM 4797 CH2 TRP A 606 -6.229 17.174 27.623 1.00100.43 C
ANISOU 4797 CH2 TRP A 606 12118 13974 12068 -32 -1228 -2614 C
ATOM 4798 N SER A 607 -13.897 16.062 24.901 1.00101.60 N
ANISOU 4798 N SER A 607 11321 14605 12676 -244 -2200 -3554 N
ATOM 4799 CA SER A 607 -14.938 16.963 24.444 1.00 96.00 C
ANISOU 4799 CA SER A 607 10525 14138 11813 -183 -2408 -3466 C
ATOM 4800 C SER A 607 -15.355 17.861 25.591 1.00103.93 C
ANISOU 4800 C SER A 607 11552 14975 12961 -119 -2327 -3115 C
ATOM 4801 O SER A 607 -15.697 17.371 26.672 1.00103.16 O
ANISOU 4801 O SER A 607 11374 14602 13222 -188 -2178 -3086 O
ATOM 4802 CB SER A 607 -16.138 16.150 23.936 1.00106.91 C
ANISOU 4802 CB SER A 607 11640 15581 13398 -273 -2579 -3810 C
ATOM 4803 OG SER A 607 -17.193 16.998 23.533 1.00108.91 O
ANISOU 4803 OG SER A 607 11778 16067 13534 -198 -2801 -3729 O
ATOM 4804 N THR A 608 -15.327 19.168 25.336 1.00110.93 N
ANISOU 4804 N THR A 608 12548 16035 13565 7 -2429 -2854 N
ATOM 4805 CA THR A 608 -15.589 20.150 26.376 1.00110.15 C
ANISOU 4805 CA THR A 608 12493 15784 13573 94 -2356 -2541 C
ATOM 4806 C THR A 608 -16.998 20.014 26.932 1.00122.57 C
ANISOU 4806 C THR A 608 13808 17286 15476 83 -2400 -2614 C
ATOM 4807 O THR A 608 -17.214 20.182 28.138 1.00135.36 O
ANISOU 4807 O THR A 608 15403 18699 17330 82 -2232 -2475 O
ATOM 4808 CB THR A 608 -15.367 21.563 25.822 1.00117.67 C
ANISOU 4808 CB THR A 608 13602 16924 14183 231 -2507 -2277 C
ATOM 4809 OG1 THR A 608 -16.272 21.806 24.735 1.00126.08 O
ANISOU 4809 OG1 THR A 608 14538 18264 15103 281 -2799 -2377 O
ATOM 4810 CG2 THR A 608 -13.940 21.726 25.325 1.00 97.76 C
ANISOU 4810 CG2 THR A 608 11321 14493 11332 211 -2431 -2186 C
ATOM 4811 N ASP A 609 -17.971 19.689 26.076 1.00121.05 N
ANISOU 4811 N ASP A 609 13406 17288 15301 65 -2620 -2847 N
ATOM 4812 CA ASP A 609 -19.369 19.856 26.465 1.00116.49 C
ANISOU 4812 CA ASP A 609 12559 16714 14990 87 -2705 -2890 C
ATOM 4813 C ASP A 609 -19.844 18.773 27.429 1.00119.68 C
ANISOU 4813 C ASP A 609 12781 16884 15809 -84 -2504 -3031 C
ATOM 4814 O ASP A 609 -20.637 19.066 28.331 1.00140.91 O
ANISOU 4814 O ASP A 609 15314 19493 18732 -74 -2423 -2949 O
ATOM 4815 CB ASP A 609 -20.273 19.911 25.234 1.00137.75 C
ANISOU 4815 CB ASP A 609 15066 19711 17561 126 -3033 -3085 C
ATOM 4816 CG ASP A 609 -19.629 20.632 24.070 1.00146.19 C
ANISOU 4816 CG ASP A 609 16340 21041 18164 230 -3230 -2978 C
ATOM 4817 OD1 ASP A 609 -19.321 21.831 24.227 1.00144.96 O
ANISOU 4817 OD1 ASP A 609 16352 20881 17844 374 -3258 -2660 O
ATOM 4818 OD2 ASP A 609 -19.456 20.016 22.996 1.00149.90 O1-
ANISOU 4818 OD2 ASP A 609 16798 21726 18430 160 -3360 -3214 O1-
ATOM 4819 N TRP A 610 -19.403 17.521 27.257 1.00100.34 N
ANISOU 4819 N TRP A 610 10336 14321 13466 -246 -2424 -3245 N
ATOM 4820 CA TRP A 610 -19.935 16.454 28.104 1.00101.38 C
ANISOU 4820 CA TRP A 610 10291 14216 14015 -435 -2263 -3357 C
ATOM 4821 C TRP A 610 -19.744 16.794 29.572 1.00104.83 C
ANISOU 4821 C TRP A 610 10803 14436 14592 -438 -2000 -3066 C
ATOM 4822 O TRP A 610 -18.654 17.183 30.002 1.00111.12 O
ANISOU 4822 O TRP A 610 11857 15135 15229 -370 -1869 -2852 O
ATOM 4823 CB TRP A 610 -19.288 15.097 27.823 1.00 93.73 C
ANISOU 4823 CB TRP A 610 9369 13075 13170 -591 -2203 -3587 C
ATOM 4824 CG TRP A 610 -19.904 14.030 28.718 1.00 94.50 C
ANISOU 4824 CG TRP A 610 9288 12895 13724 -806 -2053 -3655 C
ATOM 4825 CD1 TRP A 610 -21.076 13.359 28.507 1.00103.36 C
ANISOU 4825 CD1 TRP A 610 10112 14034 15127 -960 -2148 -3900 C
ATOM 4826 CD2 TRP A 610 -19.413 13.580 29.993 1.00103.74 C
ANISOU 4826 CD2 TRP A 610 10563 13746 15110 -905 -1787 -3440 C
ATOM 4827 NE1 TRP A 610 -21.326 12.497 29.549 1.00105.48 N
ANISOU 4827 NE1 TRP A 610 10298 14000 15778 -1166 -1945 -3842 N
ATOM 4828 CE2 TRP A 610 -20.323 12.616 30.475 1.00115.56 C
ANISOU 4828 CE2 TRP A 610 11827 15071 17010 -1131 -1727 -3550 C
ATOM 4829 CE3 TRP A 610 -18.287 13.887 30.763 1.00 97.39 C
ANISOU 4829 CE3 TRP A 610 10021 12793 14190 -835 -1605 -3162 C
ATOM 4830 CZ2 TRP A 610 -20.138 11.955 31.691 1.00115.97 C
ANISOU 4830 CZ2 TRP A 610 11919 14812 17332 -1292 -1491 -3358 C
ATOM 4831 CZ3 TRP A 610 -18.107 13.230 31.970 1.00 98.00 C
ANISOU 4831 CZ3 TRP A 610 10131 12574 14531 -975 -1387 -2993 C
ATOM 4832 CH2 TRP A 610 -19.028 12.277 32.422 1.00 94.19 C
ANISOU 4832 CH2 TRP A 610 9431 11927 14429 -1202 -1331 -3076 C
ATOM 4833 N SER A 611 -20.823 16.650 30.334 1.00 96.42 N
ANISOU 4833 N SER A 611 9495 13325 13813 -526 -1924 -3071 N
ATOM 4834 CA SER A 611 -20.852 16.946 31.743 1.00 91.09 C
ANISOU 4834 CA SER A 611 8840 12506 13263 -549 -1674 -2831 C
ATOM 4835 C SER A 611 -21.737 15.909 32.416 1.00102.29 C
ANISOU 4835 C SER A 611 10005 13800 15062 -792 -1542 -2930 C
ATOM 4836 O SER A 611 -22.794 15.549 31.878 1.00110.90 O
ANISOU 4836 O SER A 611 10811 15006 16318 -870 -1680 -3161 O
ATOM 4837 CB SER A 611 -21.395 18.357 32.010 1.00 88.96 C
ANISOU 4837 CB SER A 611 8516 12405 12879 -347 -1723 -2692 C
ATOM 4838 OG SER A 611 -22.566 18.605 31.249 1.00125.43 O
ANISOU 4838 OG SER A 611 12859 17244 17555 -290 -1956 -2880 O
ATOM 4839 N PRO A 612 -21.331 15.405 33.582 1.00105.37 N
ANISOU 4839 N PRO A 612 10484 13962 15590 -928 -1283 -2749 N
ATOM 4840 CA PRO A 612 -22.156 14.421 34.290 1.00105.15 C
ANISOU 4840 CA PRO A 612 10227 13809 15917 -1194 -1137 -2788 C
ATOM 4841 C PRO A 612 -23.376 15.013 34.976 1.00116.47 C
ANISOU 4841 C PRO A 612 11376 15423 17453 -1208 -1049 -2759 C
ATOM 4842 O PRO A 612 -24.160 14.255 35.558 1.00117.20 O
ANISOU 4842 O PRO A 612 11242 15458 17831 -1451 -916 -2787 O
ATOM 4843 CB PRO A 612 -21.179 13.836 35.320 1.00 95.80 C
ANISOU 4843 CB PRO A 612 9280 12342 14777 -1305 -905 -2541 C
ATOM 4844 CG PRO A 612 -20.212 14.935 35.580 1.00 96.29 C
ANISOU 4844 CG PRO A 612 9610 12467 14507 -1073 -870 -2335 C
ATOM 4845 CD PRO A 612 -20.080 15.709 34.299 1.00 93.75 C
ANISOU 4845 CD PRO A 612 9327 12349 13945 -857 -1122 -2485 C
ATOM 4846 N TYR A 613 -23.577 16.329 34.914 1.00121.41 N
ANISOU 4846 N TYR A 613 11993 16262 17874 -960 -1121 -2712 N
ATOM 4847 CA TYR A 613 -24.630 16.982 35.679 1.00117.58 C
ANISOU 4847 CA TYR A 613 11244 15947 17483 -933 -1013 -2694 C
ATOM 4848 C TYR A 613 -25.840 17.374 34.836 1.00138.92 C
ANISOU 4848 C TYR A 613 13611 18896 20276 -838 -1252 -2939 C
ATOM 4849 O TYR A 613 -26.737 18.053 35.348 1.00153.57 O
ANISOU 4849 O TYR A 613 15220 20921 22211 -760 -1198 -2962 O
ATOM 4850 CB TYR A 613 -24.072 18.208 36.412 1.00112.95 C
ANISOU 4850 CB TYR A 613 10856 15395 16664 -715 -906 -2480 C
ATOM 4851 CG TYR A 613 -23.468 19.306 35.550 1.00114.01 C
ANISOU 4851 CG TYR A 613 11199 15597 16524 -422 -1139 -2452 C
ATOM 4852 CD1 TYR A 613 -24.273 20.174 34.821 1.00122.77 C
ANISOU 4852 CD1 TYR A 613 12126 16906 17616 -219 -1379 -2577 C
ATOM 4853 CD2 TYR A 613 -22.092 19.502 35.506 1.00116.37 C
ANISOU 4853 CD2 TYR A 613 11869 15759 16587 -352 -1120 -2281 C
ATOM 4854 CE1 TYR A 613 -23.724 21.186 34.050 1.00131.35 C
ANISOU 4854 CE1 TYR A 613 13418 18037 18452 28 -1597 -2503 C
ATOM 4855 CE2 TYR A 613 -21.535 20.513 34.740 1.00117.56 C
ANISOU 4855 CE2 TYR A 613 12208 15974 16486 -120 -1317 -2227 C
ATOM 4856 CZ TYR A 613 -22.355 21.350 34.014 1.00124.47 C
ANISOU 4856 CZ TYR A 613 12920 17031 17342 62 -1555 -2323 C
ATOM 4857 OH TYR A 613 -21.801 22.354 33.251 1.00137.93 O
ANISOU 4857 OH TYR A 613 14828 18783 18796 272 -1758 -2225 O
ATOM 4858 N ALA A 614 -25.889 16.959 33.571 1.00131.01 N
ANISOU 4858 N ALA A 614 12580 17934 19262 -837 -1519 -3139 N
ATOM 4859 CA ALA A 614 -27.037 17.215 32.698 1.00122.24 C
ANISOU 4859 CA ALA A 614 11141 17071 18235 -763 -1784 -3383 C
ATOM 4860 C ALA A 614 -27.408 18.697 32.647 1.00119.94 C
ANISOU 4860 C ALA A 614 10798 16976 17797 -443 -1914 -3315 C
ATOM 4861 O ALA A 614 -27.421 19.311 31.580 1.00129.91 O
ANISOU 4861 O ALA A 614 12098 18380 18882 -240 -2220 -3369 O
ATOM 4862 CB ALA A 614 -28.237 16.384 33.145 1.00100.61 C
ANISOU 4862 CB ALA A 614 7994 14367 15865 -1027 -1676 -3549 C
TER 4863 ALA A 614
ATOM 4864 N THR B 333 68.834 30.002 83.576 1.00152.05 N
ANISOU 4864 N THR B 333 14338 22350 21085 6115 -6034 -3002 N
ATOM 4865 CA THR B 333 67.723 29.090 83.821 1.00155.31 C
ANISOU 4865 CA THR B 333 15549 22330 21133 6279 -6010 -2845 C
ATOM 4866 C THR B 333 66.423 29.841 84.086 1.00152.79 C
ANISOU 4866 C THR B 333 15774 21868 20411 5770 -5915 -2852 C
ATOM 4867 O THR B 333 65.456 29.262 84.581 1.00150.83 O
ANISOU 4867 O THR B 333 16133 21370 19806 5805 -5977 -2670 O
ATOM 4868 CB THR B 333 68.009 28.153 85.010 1.00174.10 C
ANISOU 4868 CB THR B 333 18087 24672 23393 6705 -6570 -2612 C
ATOM 4869 OG1 THR B 333 68.169 28.926 86.207 1.00177.60 O
ANISOU 4869 OG1 THR B 333 18434 25429 23616 6469 -7051 -2608 O
ATOM 4870 CG2 THR B 333 69.265 27.340 84.757 1.00154.73 C
ANISOU 4870 CG2 THR B 333 15096 22318 21376 7299 -6699 -2616 C
ATOM 4871 N ASN B 334 66.402 31.132 83.762 1.00151.35 N
ANISOU 4871 N ASN B 334 15348 21847 20310 5301 -5781 -3039 N
ATOM 4872 CA ASN B 334 65.173 31.913 83.835 1.00157.35 C
ANISOU 4872 CA ASN B 334 16577 22453 20756 4870 -5649 -3102 C
ATOM 4873 C ASN B 334 64.373 31.655 82.565 1.00163.94 C
ANISOU 4873 C ASN B 334 17704 22995 21591 4784 -5089 -3084 C
ATOM 4874 O ASN B 334 64.742 32.124 81.483 1.00160.18 O
ANISOU 4874 O ASN B 334 16900 22580 21379 4628 -4756 -3174 O
ATOM 4875 CB ASN B 334 65.475 33.399 84.006 1.00155.16 C
ANISOU 4875 CB ASN B 334 15964 22367 20623 4427 -5817 -3319 C
ATOM 4876 CG ASN B 334 64.220 34.226 84.230 1.00170.70 C
ANISOU 4876 CG ASN B 334 18417 24168 22272 4079 -5762 -3436 C
ATOM 4877 OD1 ASN B 334 63.254 33.756 84.833 1.00173.57 O
ANISOU 4877 OD1 ASN B 334 19299 24446 22202 4188 -5782 -3351 O
ATOM 4878 ND2 ASN B 334 64.226 35.460 83.740 1.00171.15 N
ANISOU 4878 ND2 ASN B 334 18283 24184 22563 3661 -5698 -3605 N
ATOM 4879 N LEU B 335 63.288 30.900 82.693 1.00161.05 N
ANISOU 4879 N LEU B 335 17938 22339 20915 4865 -5004 -2937 N
ATOM 4880 CA LEU B 335 62.501 30.516 81.534 1.00153.54 C
ANISOU 4880 CA LEU B 335 17302 21084 19952 4808 -4556 -2926 C
ATOM 4881 C LEU B 335 61.717 31.710 80.997 1.00151.75 C
ANISOU 4881 C LEU B 335 17158 20843 19657 4325 -4305 -3045 C
ATOM 4882 O LEU B 335 61.457 32.689 81.701 1.00147.67 O
ANISOU 4882 O LEU B 335 16629 20451 19029 4063 -4503 -3127 O
ATOM 4883 CB LEU B 335 61.551 29.374 81.892 1.00157.73 C
ANISOU 4883 CB LEU B 335 18423 21283 20225 4966 -4614 -2693 C
ATOM 4884 CG LEU B 335 62.236 28.049 82.228 1.00153.13 C
ANISOU 4884 CG LEU B 335 17851 20559 19771 5473 -4868 -2534 C
ATOM 4885 CD1 LEU B 335 61.239 27.063 82.821 1.00152.16 C
ANISOU 4885 CD1 LEU B 335 18323 20101 19389 5506 -5025 -2201 C
ATOM 4886 CD2 LEU B 335 62.927 27.462 81.002 1.00145.60 C
ANISOU 4886 CD2 LEU B 335 16689 19477 19154 5800 -4605 -2709 C
ATOM 4887 N CYS B 336 61.347 31.622 79.725 1.00146.82 N
ANISOU 4887 N CYS B 336 16634 20055 19095 4242 -3898 -3076 N
ATOM 4888 CA CYS B 336 60.555 32.706 79.163 1.00138.32 C
ANISOU 4888 CA CYS B 336 15666 18927 17964 3805 -3691 -3140 C
ATOM 4889 C CYS B 336 59.080 32.500 79.502 1.00129.14 C
ANISOU 4889 C CYS B 336 15060 17527 16479 3691 -3688 -3052 C
ATOM 4890 O CYS B 336 58.580 31.373 79.446 1.00123.04 O
ANISOU 4890 O CYS B 336 14624 16540 15584 3879 -3650 -2917 O
ATOM 4891 CB CYS B 336 60.742 32.789 77.651 1.00125.66 C
ANISOU 4891 CB CYS B 336 13933 17318 16495 3732 -3271 -3176 C
ATOM 4892 SG CYS B 336 62.380 33.366 77.123 1.00143.54 S
ANISOU 4892 SG CYS B 336 15413 19999 19126 3723 -3172 -3220 S
ATOM 4893 N PRO B 337 58.367 33.566 79.861 1.00132.48 N
ANISOU 4893 N PRO B 337 15566 17979 16791 3390 -3748 -3125 N
ATOM 4894 CA PRO B 337 56.983 33.434 80.354 1.00123.21 C
ANISOU 4894 CA PRO B 337 14817 16702 15294 3310 -3750 -3041 C
ATOM 4895 C PRO B 337 55.965 33.272 79.229 1.00139.38 C
ANISOU 4895 C PRO B 337 17139 18499 17319 3145 -3435 -2977 C
ATOM 4896 O PRO B 337 55.092 34.117 79.015 1.00149.03 O
ANISOU 4896 O PRO B 337 18458 19681 18487 2904 -3358 -3036 O
ATOM 4897 CB PRO B 337 56.790 34.743 81.130 1.00133.39 C
ANISOU 4897 CB PRO B 337 16012 18155 16514 3134 -3956 -3240 C
ATOM 4898 CG PRO B 337 57.663 35.716 80.422 1.00142.03 C
ANISOU 4898 CG PRO B 337 16742 19243 17979 2942 -3943 -3385 C
ATOM 4899 CD PRO B 337 58.866 34.948 79.961 1.00134.11 C
ANISOU 4899 CD PRO B 337 15442 18322 17192 3134 -3877 -3297 C
ATOM 4900 N PHE B 338 56.072 32.164 78.493 1.00144.63 N
ANISOU 4900 N PHE B 338 17941 18976 18035 3305 -3291 -2881 N
ATOM 4901 CA PHE B 338 55.093 31.896 77.448 1.00129.57 C
ANISOU 4901 CA PHE B 338 16330 16826 16076 3158 -3060 -2839 C
ATOM 4902 C PHE B 338 53.755 31.454 78.021 1.00123.45 C
ANISOU 4902 C PHE B 338 15898 15934 15075 3051 -3129 -2650 C
ATOM 4903 O PHE B 338 52.739 31.529 77.322 1.00114.24 O
ANISOU 4903 O PHE B 338 14930 14617 13860 2847 -2993 -2616 O
ATOM 4904 CB PHE B 338 55.625 30.842 76.479 1.00118.19 C
ANISOU 4904 CB PHE B 338 14959 15207 14740 3396 -2927 -2873 C
ATOM 4905 CG PHE B 338 56.645 31.373 75.518 1.00125.51 C
ANISOU 4905 CG PHE B 338 15538 16326 15824 3428 -2711 -3036 C
ATOM 4906 CD1 PHE B 338 56.427 32.567 74.853 1.00120.63 C
ANISOU 4906 CD1 PHE B 338 14796 15819 15219 3098 -2547 -3066 C
ATOM 4907 CD2 PHE B 338 57.819 30.682 75.277 1.00141.99 C
ANISOU 4907 CD2 PHE B 338 17396 18505 18050 3793 -2673 -3127 C
ATOM 4908 CE1 PHE B 338 57.363 33.064 73.969 1.00120.49 C
ANISOU 4908 CE1 PHE B 338 14428 16031 15322 3068 -2329 -3121 C
ATOM 4909 CE2 PHE B 338 58.756 31.174 74.391 1.00142.08 C
ANISOU 4909 CE2 PHE B 338 17011 18803 18171 3811 -2420 -3236 C
ATOM 4910 CZ PHE B 338 58.528 32.368 73.738 1.00131.75 C
ANISOU 4910 CZ PHE B 338 15578 17635 16846 3416 -2237 -3202 C
ATOM 4911 N GLY B 339 53.735 31.002 79.275 1.00145.70 N
ANISOU 4911 N GLY B 339 18758 18863 17738 3171 -3343 -2492 N
ATOM 4912 CA GLY B 339 52.478 30.615 79.892 1.00130.09 C
ANISOU 4912 CA GLY B 339 17031 16884 15515 3035 -3373 -2242 C
ATOM 4913 C GLY B 339 51.503 31.770 80.012 1.00123.13 C
ANISOU 4913 C GLY B 339 16096 16199 14490 2809 -3271 -2346 C
ATOM 4914 O GLY B 339 50.294 31.590 79.852 1.00126.82 O
ANISOU 4914 O GLY B 339 16719 16615 14851 2630 -3175 -2191 O
ATOM 4915 N GLU B 340 52.013 32.977 80.287 1.00122.86 N
ANISOU 4915 N GLU B 340 15824 16368 14490 2819 -3325 -2618 N
ATOM 4916 CA GLU B 340 51.117 34.119 80.450 1.00124.50 C
ANISOU 4916 CA GLU B 340 15996 16709 14600 2679 -3282 -2774 C
ATOM 4917 C GLU B 340 50.445 34.516 79.141 1.00135.44 C
ANISOU 4917 C GLU B 340 17447 17846 16166 2470 -3095 -2801 C
ATOM 4918 O GLU B 340 49.341 35.069 79.164 1.00147.18 O
ANISOU 4918 O GLU B 340 18969 19386 17567 2370 -3042 -2824 O
ATOM 4919 CB GLU B 340 51.848 35.331 81.033 1.00120.66 C
ANISOU 4919 CB GLU B 340 15285 16391 14168 2736 -3471 -3094 C
ATOM 4920 CG GLU B 340 52.481 35.137 82.401 1.00142.29 C
ANISOU 4920 CG GLU B 340 17955 19438 16670 2947 -3722 -3126 C
ATOM 4921 CD GLU B 340 53.788 35.892 82.544 1.00157.18 C
ANISOU 4921 CD GLU B 340 19577 21347 18798 2979 -3961 -3390 C
ATOM 4922 OE1 GLU B 340 53.840 37.070 82.128 1.00159.98 O
ANISOU 4922 OE1 GLU B 340 19819 21579 19386 2826 -4003 -3638 O
ATOM 4923 OE2 GLU B 340 54.754 35.323 83.094 1.00152.15 O1-
ANISOU 4923 OE2 GLU B 340 18831 20836 18144 3143 -4146 -3326 O1-
ATOM 4924 N VAL B 341 51.083 34.260 78.000 1.00127.05 N
ANISOU 4924 N VAL B 341 16386 16562 15325 2430 -2997 -2805 N
ATOM 4925 CA VAL B 341 50.463 34.613 76.726 1.00118.90 C
ANISOU 4925 CA VAL B 341 15445 15338 14394 2232 -2842 -2806 C
ATOM 4926 C VAL B 341 49.472 33.541 76.291 1.00109.99 C
ANISOU 4926 C VAL B 341 14584 14044 13162 2165 -2775 -2606 C
ATOM 4927 O VAL B 341 48.300 33.829 76.028 1.00113.77 O
ANISOU 4927 O VAL B 341 15137 14498 13592 2001 -2744 -2546 O
ATOM 4928 CB VAL B 341 51.537 34.857 75.649 1.00113.16 C
ANISOU 4928 CB VAL B 341 14591 14538 13865 2208 -2736 -2885 C
ATOM 4929 CG1 VAL B 341 50.881 35.206 74.318 1.00111.35 C
ANISOU 4929 CG1 VAL B 341 14492 14161 13656 2002 -2591 -2846 C
ATOM 4930 CG2 VAL B 341 52.482 35.964 76.085 1.00102.78 C
ANISOU 4930 CG2 VAL B 341 12969 13361 12723 2184 -2852 -3030 C
ATOM 4931 N PHE B 342 49.923 32.287 76.223 1.00 97.00 N
ANISOU 4931 N PHE B 342 13077 12258 11520 2294 -2798 -2506 N
ATOM 4932 CA PHE B 342 49.115 31.228 75.627 1.00 98.13 C
ANISOU 4932 CA PHE B 342 13509 12132 11644 2200 -2800 -2350 C
ATOM 4933 C PHE B 342 47.998 30.741 76.542 1.00108.40 C
ANISOU 4933 C PHE B 342 14888 13487 12811 2074 -2892 -2068 C
ATOM 4934 O PHE B 342 46.921 30.382 76.054 1.00129.49 O
ANISOU 4934 O PHE B 342 17702 16012 15487 1858 -2898 -1930 O
ATOM 4935 CB PHE B 342 50.006 30.051 75.231 1.00 94.71 C
ANISOU 4935 CB PHE B 342 13224 11455 11307 2426 -2845 -2383 C
ATOM 4936 CG PHE B 342 50.848 30.314 74.020 1.00 94.94 C
ANISOU 4936 CG PHE B 342 13195 11468 11409 2529 -2684 -2632 C
ATOM 4937 CD1 PHE B 342 52.044 31.003 74.124 1.00 95.10 C
ANISOU 4937 CD1 PHE B 342 12891 11737 11505 2667 -2601 -2768 C
ATOM 4938 CD2 PHE B 342 50.445 29.867 72.773 1.00115.70 C
ANISOU 4938 CD2 PHE B 342 16076 13879 14006 2474 -2622 -2719 C
ATOM 4939 CE1 PHE B 342 52.821 31.245 73.007 1.00 94.56 C
ANISOU 4939 CE1 PHE B 342 12708 11751 11471 2734 -2403 -2931 C
ATOM 4940 CE2 PHE B 342 51.217 30.104 71.653 1.00125.76 C
ANISOU 4940 CE2 PHE B 342 17287 15245 15251 2587 -2431 -2932 C
ATOM 4941 CZ PHE B 342 52.406 30.793 71.771 1.00105.19 C
ANISOU 4941 CZ PHE B 342 14315 12941 12713 2712 -2292 -3011 C
ATOM 4942 N ASN B 343 48.224 30.703 77.851 1.00 98.33 N
ANISOU 4942 N ASN B 343 13502 12462 11396 2186 -2969 -1954 N
ATOM 4943 CA ASN B 343 47.229 30.206 78.789 1.00 99.55 C
ANISOU 4943 CA ASN B 343 13690 12779 11356 2062 -3013 -1616 C
ATOM 4944 C ASN B 343 46.489 31.330 79.516 1.00101.73 C
ANISOU 4944 C ASN B 343 13735 13505 11413 2030 -2918 -1688 C
ATOM 4945 O ASN B 343 45.817 31.067 80.520 1.00105.07 O
ANISOU 4945 O ASN B 343 14099 14246 11577 1991 -2906 -1428 O
ATOM 4946 CB ASN B 343 47.889 29.235 79.784 1.00114.74 C
ANISOU 4946 CB ASN B 343 15690 14714 13193 2224 -3178 -1366 C
ATOM 4947 CG ASN B 343 48.207 27.865 79.150 1.00122.73 C
ANISOU 4947 CG ASN B 343 16990 15198 14443 2248 -3325 -1218 C
ATOM 4948 OD1 ASN B 343 47.946 27.648 77.968 1.00 98.02 O
ANISOU 4948 OD1 ASN B 343 14011 11734 11498 2152 -3292 -1350 O
ATOM 4949 ND2 ASN B 343 48.774 26.941 79.942 1.00134.36 N
ANISOU 4949 ND2 ASN B 343 18565 16584 15904 2405 -3526 -960 N
ATOM 4950 N ALA B 344 46.578 32.566 79.017 1.00 97.79 N
ANISOU 4950 N ALA B 344 13105 13042 11008 2056 -2855 -2026 N
ATOM 4951 CA ALA B 344 45.835 33.679 79.598 1.00100.30 C
ANISOU 4951 CA ALA B 344 13232 13703 11175 2088 -2803 -2176 C
ATOM 4952 C ALA B 344 44.336 33.405 79.558 1.00112.64 C
ANISOU 4952 C ALA B 344 14755 15398 12645 1906 -2701 -1928 C
ATOM 4953 O ALA B 344 43.825 32.786 78.622 1.00127.11 O
ANISOU 4953 O ALA B 344 16709 16943 14645 1688 -2698 -1751 O
ATOM 4954 CB ALA B 344 46.151 34.975 78.852 1.00106.24 C
ANISOU 4954 CB ALA B 344 13905 14309 12152 2104 -2818 -2528 C
ATOM 4955 N THR B 345 43.626 33.889 80.582 1.00112.22 N
ANISOU 4955 N THR B 345 14505 15823 12312 2008 -2628 -1938 N
ATOM 4956 CA THR B 345 42.215 33.545 80.734 1.00115.88 C
ANISOU 4956 CA THR B 345 14827 16549 12654 1842 -2500 -1636 C
ATOM 4957 C THR B 345 41.360 34.202 79.653 1.00123.52 C
ANISOU 4957 C THR B 345 15712 17340 13880 1732 -2478 -1764 C
ATOM 4958 O THR B 345 40.520 33.542 79.029 1.00127.76 O
ANISOU 4958 O THR B 345 16253 17753 14538 1459 -2474 -1473 O
ATOM 4959 CB THR B 345 41.725 33.934 82.129 1.00128.36 C
ANISOU 4959 CB THR B 345 16169 18804 13798 2046 -2378 -1646 C
ATOM 4960 OG1 THR B 345 42.418 33.154 83.111 1.00123.88 O
ANISOU 4960 OG1 THR B 345 15701 18424 12942 2099 -2427 -1411 O
ATOM 4961 CG2 THR B 345 40.233 33.669 82.258 1.00133.36 C
ANISOU 4961 CG2 THR B 345 16546 19810 14314 1876 -2197 -1320 C
ATOM 4962 N ARG B 346 41.551 35.499 79.419 1.00126.00 N
ANISOU 4962 N ARG B 346 15960 17611 14304 1926 -2517 -2177 N
ATOM 4963 CA ARG B 346 40.902 36.185 78.313 1.00126.96 C
ANISOU 4963 CA ARG B 346 16046 17495 14699 1843 -2557 -2280 C
ATOM 4964 C ARG B 346 41.946 36.777 77.376 1.00122.67 C
ANISOU 4964 C ARG B 346 15692 16503 14415 1837 -2679 -2508 C
ATOM 4965 O ARG B 346 43.012 37.230 77.807 1.00121.07 O
ANISOU 4965 O ARG B 346 15519 16271 14212 1986 -2739 -2731 O
ATOM 4966 CB ARG B 346 39.949 37.296 78.792 1.00134.67 C
ANISOU 4966 CB ARG B 346 16738 18811 15620 2080 -2519 -2511 C
ATOM 4967 CG ARG B 346 38.992 37.770 77.694 1.00147.71 C
ANISOU 4967 CG ARG B 346 18309 20266 17546 1974 -2584 -2486 C
ATOM 4968 CD ARG B 346 38.190 39.007 78.083 1.00144.53 C
ANISOU 4968 CD ARG B 346 17636 20106 17172 2302 -2599 -2792 C
ATOM 4969 NE ARG B 346 37.542 38.879 79.382 1.00173.88 N
ANISOU 4969 NE ARG B 346 21056 24478 20531 2528 -2401 -2804 N
ATOM 4970 CZ ARG B 346 36.271 38.538 79.545 1.00180.85 C
ANISOU 4970 CZ ARG B 346 21600 25793 21322 2485 -2246 -2560 C
ATOM 4971 NH1 ARG B 346 35.485 38.285 78.510 1.00172.75 N
ANISOU 4971 NH1 ARG B 346 20497 24571 20569 2221 -2320 -2308 N
ATOM 4972 NH2 ARG B 346 35.775 38.451 80.775 1.00181.19 N
ANISOU 4972 NH2 ARG B 346 21348 26530 20967 2706 -2017 -2558 N
ATOM 4973 N PHE B 347 41.630 36.756 76.087 1.00112.51 N
ANISOU 4973 N PHE B 347 14511 14907 13331 1640 -2726 -2420 N
ATOM 4974 CA PHE B 347 42.466 37.340 75.051 1.00106.30 C
ANISOU 4974 CA PHE B 347 13873 13771 12746 1588 -2802 -2549 C
ATOM 4975 C PHE B 347 41.902 38.692 74.625 1.00108.54 C
ANISOU 4975 C PHE B 347 14060 13964 13218 1642 -2914 -2696 C
ATOM 4976 O PHE B 347 40.805 39.094 75.020 1.00112.83 O
ANISOU 4976 O PHE B 347 14418 14700 13751 1753 -2931 -2730 O
ATOM 4977 CB PHE B 347 42.566 36.399 73.848 1.00103.63 C
ANISOU 4977 CB PHE B 347 13765 13176 12434 1362 -2794 -2361 C
ATOM 4978 CG PHE B 347 43.696 35.413 73.936 1.00101.30 C
ANISOU 4978 CG PHE B 347 13623 12793 12073 1388 -2741 -2339 C
ATOM 4979 CD1 PHE B 347 43.896 34.665 75.085 1.00111.37 C
ANISOU 4979 CD1 PHE B 347 14862 14236 13219 1485 -2718 -2257 C
ATOM 4980 CD2 PHE B 347 44.551 35.223 72.862 1.00 99.10 C
ANISOU 4980 CD2 PHE B 347 13513 12299 11841 1343 -2714 -2386 C
ATOM 4981 CE1 PHE B 347 44.934 33.754 75.165 1.00110.19 C
ANISOU 4981 CE1 PHE B 347 14848 13967 13052 1556 -2717 -2231 C
ATOM 4982 CE2 PHE B 347 45.590 34.313 72.936 1.00 99.82 C
ANISOU 4982 CE2 PHE B 347 13706 12327 11896 1445 -2666 -2407 C
ATOM 4983 CZ PHE B 347 45.781 33.577 74.089 1.00 99.55 C
ANISOU 4983 CZ PHE B 347 13641 12386 11796 1560 -2692 -2332 C
ATOM 4984 N ALA B 348 42.667 39.392 73.798 1.00101.50 N
ANISOU 4984 N ALA B 348 13273 12785 12508 1570 -2995 -2757 N
ATOM 4985 CA ALA B 348 42.288 40.722 73.353 1.00102.11 C
ANISOU 4985 CA ALA B 348 13304 12672 12820 1604 -3166 -2849 C
ATOM 4986 C ALA B 348 41.436 40.655 72.091 1.00 99.88 C
ANISOU 4986 C ALA B 348 13111 12253 12585 1423 -3226 -2623 C
ATOM 4987 O ALA B 348 41.475 39.684 71.331 1.00 98.10 O
ANISOU 4987 O ALA B 348 13041 12011 12222 1233 -3147 -2439 O
ATOM 4988 CB ALA B 348 43.530 41.577 73.097 1.00113.89 C
ANISOU 4988 CB ALA B 348 14845 13915 14512 1548 -3263 -2939 C
ATOM 4989 N SER B 349 40.646 41.705 71.883 1.00104.54 N
ANISOU 4989 N SER B 349 13614 12732 13375 1515 -3410 -2666 N
ATOM 4990 CA SER B 349 39.971 41.902 70.609 1.00103.10 C
ANISOU 4990 CA SER B 349 13525 12381 13267 1351 -3548 -2442 C
ATOM 4991 C SER B 349 40.984 42.387 69.581 1.00103.59 C
ANISOU 4991 C SER B 349 13798 12169 13394 1147 -3599 -2304 C
ATOM 4992 O SER B 349 41.854 43.207 69.889 1.00107.48 O
ANISOU 4992 O SER B 349 14273 12498 14064 1176 -3655 -2404 O
ATOM 4993 CB SER B 349 38.824 42.901 70.753 1.00104.25 C
ANISOU 4993 CB SER B 349 13483 12489 13640 1567 -3764 -2520 C
ATOM 4994 OG SER B 349 37.793 42.374 71.573 1.00104.90 O
ANISOU 4994 OG SER B 349 13300 12941 13614 1730 -3663 -2584 O
ATOM 4995 N VAL B 350 40.860 41.879 68.351 1.00 88.19 N
ANISOU 4995 N VAL B 350 12033 10196 11281 924 -3592 -2066 N
ATOM 4996 CA VAL B 350 41.953 41.976 67.385 1.00 85.82 C
ANISOU 4996 CA VAL B 350 11916 9808 10883 720 -3514 -1908 C
ATOM 4997 C VAL B 350 42.317 43.426 67.078 1.00 85.45 C
ANISOU 4997 C VAL B 350 11854 9494 11120 656 -3706 -1786 C
ATOM 4998 O VAL B 350 43.476 43.725 66.763 1.00 93.49 O
ANISOU 4998 O VAL B 350 12896 10474 12152 500 -3614 -1679 O
ATOM 4999 CB VAL B 350 41.596 41.192 66.104 1.00 94.24 C
ANISOU 4999 CB VAL B 350 13211 10951 11646 543 -3500 -1723 C
ATOM 5000 CG1 VAL B 350 40.377 41.794 65.423 1.00108.83 C
ANISOU 5000 CG1 VAL B 350 15081 12697 13574 500 -3795 -1548 C
ATOM 5001 CG2 VAL B 350 42.787 41.133 65.153 1.00 96.31 C
ANISOU 5001 CG2 VAL B 350 13633 11268 11693 384 -3329 -1590 C
ATOM 5002 N TYR B 351 41.358 44.351 67.177 1.00 84.93 N
ANISOU 5002 N TYR B 351 11724 9228 11317 775 -3993 -1784 N
ATOM 5003 CA TYR B 351 41.674 45.748 66.894 1.00 87.75 C
ANISOU 5003 CA TYR B 351 12108 9218 12016 710 -4257 -1647 C
ATOM 5004 C TYR B 351 42.547 46.352 67.987 1.00 92.75 C
ANISOU 5004 C TYR B 351 12616 9702 12922 806 -4288 -1912 C
ATOM 5005 O TYR B 351 43.360 47.241 67.709 1.00 93.83 O
ANISOU 5005 O TYR B 351 12785 9553 13311 612 -4433 -1754 O
ATOM 5006 CB TYR B 351 40.390 46.564 66.717 1.00107.19 C
ANISOU 5006 CB TYR B 351 14542 11455 14731 882 -4610 -1608 C
ATOM 5007 CG TYR B 351 39.810 47.099 68.006 1.00 90.97 C
ANISOU 5007 CG TYR B 351 12276 9327 12961 1279 -4746 -2018 C
ATOM 5008 CD1 TYR B 351 39.016 46.300 68.814 1.00 89.59 C
ANISOU 5008 CD1 TYR B 351 11904 9528 12608 1519 -4574 -2266 C
ATOM 5009 CD2 TYR B 351 40.046 48.408 68.409 1.00 94.22 C
ANISOU 5009 CD2 TYR B 351 12687 9304 13809 1416 -5060 -2156 C
ATOM 5010 CE1 TYR B 351 38.487 46.781 69.989 1.00 91.94 C
ANISOU 5010 CE1 TYR B 351 11985 9876 13071 1920 -4645 -2652 C
ATOM 5011 CE2 TYR B 351 39.518 48.899 69.587 1.00100.87 C
ANISOU 5011 CE2 TYR B 351 13359 10113 14855 1852 -5187 -2618 C
ATOM 5012 CZ TYR B 351 38.738 48.081 70.374 1.00 95.53 C
ANISOU 5012 CZ TYR B 351 12464 9921 13913 2122 -4947 -2871 C
ATOM 5013 OH TYR B 351 38.207 48.563 71.549 1.00 96.72 O
ANISOU 5013 OH TYR B 351 12420 10155 14176 2594 -5022 -3342 O
ATOM 5014 N ALA B 352 42.396 45.886 69.226 1.00102.18 N
ANISOU 5014 N ALA B 352 13664 11098 14060 1075 -4180 -2287 N
ATOM 5015 CA ALA B 352 43.244 46.333 70.323 1.00100.02 C
ANISOU 5015 CA ALA B 352 13290 10748 13964 1184 -4231 -2589 C
ATOM 5016 C ALA B 352 44.206 45.219 70.711 1.00104.77 C
ANISOU 5016 C ALA B 352 13847 11684 14277 1113 -3912 -2633 C
ATOM 5017 O ALA B 352 44.309 44.864 71.890 1.00103.04 O
ANISOU 5017 O ALA B 352 13523 11663 13965 1335 -3852 -2934 O
ATOM 5018 CB ALA B 352 42.396 46.757 71.524 1.00 88.39 C
ANISOU 5018 CB ALA B 352 11690 9298 12596 1603 -4382 -3013 C
ATOM 5019 N TRP B 353 44.908 44.667 69.722 1.00112.51 N
ANISOU 5019 N TRP B 353 14905 12752 15090 841 -3714 -2338 N
ATOM 5020 CA TRP B 353 45.731 43.487 69.951 1.00104.57 C
ANISOU 5020 CA TRP B 353 13865 12052 13815 837 -3418 -2380 C
ATOM 5021 C TRP B 353 46.789 43.767 71.012 1.00107.46 C
ANISOU 5021 C TRP B 353 14059 12431 14338 903 -3465 -2604 C
ATOM 5022 O TRP B 353 47.317 44.877 71.122 1.00 95.05 O
ANISOU 5022 O TRP B 353 12413 10604 13095 795 -3691 -2619 O
ATOM 5023 CB TRP B 353 46.385 43.024 68.646 1.00101.72 C
ANISOU 5023 CB TRP B 353 13597 11796 13257 593 -3210 -2082 C
ATOM 5024 CG TRP B 353 47.095 44.095 67.866 1.00 97.98 C
ANISOU 5024 CG TRP B 353 13085 11155 12989 312 -3296 -1801 C
ATOM 5025 CD1 TRP B 353 46.531 45.006 67.021 1.00104.45 C
ANISOU 5025 CD1 TRP B 353 14020 11734 13933 144 -3501 -1524 C
ATOM 5026 CD2 TRP B 353 48.510 44.323 67.814 1.00101.21 C
ANISOU 5026 CD2 TRP B 353 13303 11649 13502 130 -3185 -1697 C
ATOM 5027 NE1 TRP B 353 47.503 45.807 66.470 1.00107.46 N
ANISOU 5027 NE1 TRP B 353 14316 12023 14490 -164 -3526 -1218 N
ATOM 5028 CE2 TRP B 353 48.726 45.406 66.939 1.00102.34 C
ANISOU 5028 CE2 TRP B 353 13450 11595 13837 -190 -3319 -1320 C
ATOM 5029 CE3 TRP B 353 49.612 43.726 68.433 1.00109.82 C
ANISOU 5029 CE3 TRP B 353 14188 12974 14565 201 -3008 -1853 C
ATOM 5030 CZ2 TRP B 353 50.000 45.902 66.666 1.00108.09 C
ANISOU 5030 CZ2 TRP B 353 13951 12384 14732 -487 -3253 -1071 C
ATOM 5031 CZ3 TRP B 353 50.874 44.221 68.162 1.00112.72 C
ANISOU 5031 CZ3 TRP B 353 14308 13414 15107 -49 -2952 -1655 C
ATOM 5032 CH2 TRP B 353 51.058 45.298 67.286 1.00110.57 C
ANISOU 5032 CH2 TRP B 353 14012 12972 15026 -412 -3059 -1256 C
ATOM 5033 N ASN B 354 47.084 42.744 71.807 1.00119.61 N
ANISOU 5033 N ASN B 354 15546 14242 15660 1069 -3302 -2763 N
ATOM 5034 CA ASN B 354 47.904 42.883 73.001 1.00124.12 C
ANISOU 5034 CA ASN B 354 15961 14888 16310 1196 -3392 -3013 C
ATOM 5035 C ASN B 354 49.323 42.411 72.714 1.00124.04 C
ANISOU 5035 C ASN B 354 15822 15008 16298 1065 -3240 -2900 C
ATOM 5036 O ASN B 354 49.520 41.343 72.127 1.00122.53 O
ANISOU 5036 O ASN B 354 15686 14992 15876 1068 -2984 -2763 O
ATOM 5037 CB ASN B 354 47.301 42.086 74.159 1.00106.01 C
ANISOU 5037 CB ASN B 354 13672 12857 13750 1481 -3338 -3212 C
ATOM 5038 CG ASN B 354 47.790 42.560 75.510 1.00124.88 C
ANISOU 5038 CG ASN B 354 15942 15325 16183 1668 -3531 -3534 C
ATOM 5039 OD1 ASN B 354 47.144 43.380 76.162 1.00115.13 O
ANISOU 5039 OD1 ASN B 354 14702 14031 15010 1844 -3727 -3794 O
ATOM 5040 ND2 ASN B 354 48.935 42.044 75.941 1.00143.91 N
ANISOU 5040 ND2 ASN B 354 18251 17884 18544 1669 -3502 -3552 N
ATOM 5041 N ARG B 355 50.305 43.206 73.131 1.00114.45 N
ANISOU 5041 N ARG B 355 14418 13706 15361 968 -3425 -2982 N
ATOM 5042 CA ARG B 355 51.711 42.923 72.882 1.00107.24 C
ANISOU 5042 CA ARG B 355 13273 12959 14515 832 -3303 -2861 C
ATOM 5043 C ARG B 355 52.422 42.718 74.211 1.00108.53 C
ANISOU 5043 C ARG B 355 13268 13268 14703 1016 -3462 -3134 C
ATOM 5044 O ARG B 355 52.339 43.571 75.100 1.00112.78 O
ANISOU 5044 O ARG B 355 13785 13648 15417 1058 -3793 -3388 O
ATOM 5045 CB ARG B 355 52.367 44.063 72.096 1.00115.35 C
ANISOU 5045 CB ARG B 355 14149 13788 15892 455 -3412 -2614 C
ATOM 5046 CG ARG B 355 53.887 44.069 72.135 1.00118.83 C
ANISOU 5046 CG ARG B 355 14218 14423 16510 289 -3370 -2521 C
ATOM 5047 CD ARG B 355 54.464 44.869 70.972 1.00124.95 C
ANISOU 5047 CD ARG B 355 14827 15139 17508 -148 -3312 -2096 C
ATOM 5048 NE ARG B 355 54.244 44.224 69.681 1.00116.04 N
ANISOU 5048 NE ARG B 355 13809 14259 16023 -176 -2906 -1812 N
ATOM 5049 CZ ARG B 355 54.757 44.650 68.534 1.00120.33 C
ANISOU 5049 CZ ARG B 355 14211 14930 16581 -516 -2730 -1388 C
ATOM 5050 NH1 ARG B 355 55.538 45.716 68.479 1.00124.87 N
ANISOU 5050 NH1 ARG B 355 14496 15378 17571 -916 -2919 -1124 N
ATOM 5051 NH2 ARG B 355 54.475 43.992 67.413 1.00124.60 N
ANISOU 5051 NH2 ARG B 355 14905 15742 16694 -471 -2374 -1209 N
ATOM 5052 N LYS B 356 53.112 41.588 74.345 1.00116.80 N
ANISOU 5052 N LYS B 356 14212 14603 15564 1159 -3262 -3106 N
ATOM 5053 CA LYS B 356 53.906 41.277 75.528 1.00123.77 C
ANISOU 5053 CA LYS B 356 14915 15666 16444 1339 -3424 -3303 C
ATOM 5054 C LYS B 356 55.364 41.158 75.109 1.00123.19 C
ANISOU 5054 C LYS B 356 14477 15764 16565 1215 -3343 -3164 C
ATOM 5055 O LYS B 356 55.707 40.309 74.280 1.00110.27 O
ANISOU 5055 O LYS B 356 12796 14301 14800 1267 -3020 -2993 O
ATOM 5056 CB LYS B 356 53.424 39.985 76.195 1.00120.67 C
ANISOU 5056 CB LYS B 356 14698 15465 15685 1660 -3315 -3355 C
ATOM 5057 CG LYS B 356 53.639 39.926 77.706 1.00 99.44 C
ANISOU 5057 CG LYS B 356 11961 12938 12882 1880 -3580 -3586 C
ATOM 5058 CD LYS B 356 55.065 39.517 78.053 1.00133.02 C
ANISOU 5058 CD LYS B 356 15920 17380 17242 1945 -3665 -3581 C
ATOM 5059 CE LYS B 356 55.288 39.477 79.558 1.00146.09 C
ANISOU 5059 CE LYS B 356 17550 19225 18732 2162 -3982 -3800 C
ATOM 5060 NZ LYS B 356 55.756 40.787 80.090 1.00143.55 N
ANISOU 5060 NZ LYS B 356 17064 18814 18663 2023 -4364 -4070 N
ATOM 5061 N ARG B 357 56.216 42.006 75.678 1.00143.26 N
ANISOU 5061 N ARG B 357 16737 18274 19420 1065 -3649 -3261 N
ATOM 5062 CA ARG B 357 57.634 42.012 75.344 1.00134.76 C
ANISOU 5062 CA ARG B 357 15204 17410 18589 905 -3601 -3104 C
ATOM 5063 C ARG B 357 58.368 41.000 76.215 1.00134.51 C
ANISOU 5063 C ARG B 357 15000 17682 18428 1239 -3642 -3239 C
ATOM 5064 O ARG B 357 58.319 41.079 77.447 1.00141.16 O
ANISOU 5064 O ARG B 357 15898 18519 19217 1397 -3982 -3490 O
ATOM 5065 CB ARG B 357 58.235 43.405 75.514 1.00137.67 C
ANISOU 5065 CB ARG B 357 15315 17565 19429 517 -3976 -3100 C
ATOM 5066 CG ARG B 357 59.730 43.443 75.260 1.00152.03 C
ANISOU 5066 CG ARG B 357 16558 19664 21542 303 -3949 -2902 C
ATOM 5067 CD ARG B 357 60.277 44.856 75.291 1.00149.09 C
ANISOU 5067 CD ARG B 357 15929 19015 21704 -193 -4348 -2813 C
ATOM 5068 NE ARG B 357 61.722 44.869 75.106 1.00170.57 N
ANISOU 5068 NE ARG B 357 18009 22071 24730 -431 -4328 -2587 N
ATOM 5069 CZ ARG B 357 62.453 45.968 74.977 1.00188.74 C
ANISOU 5069 CZ ARG B 357 19942 24212 27556 -957 -4631 -2385 C
ATOM 5070 NH1 ARG B 357 61.900 47.169 74.972 1.00186.08 N
ANISOU 5070 NH1 ARG B 357 19865 23310 27528 -1291 -5009 -2387 N
ATOM 5071 NH2 ARG B 357 63.772 45.858 74.845 1.00184.91 N
ANISOU 5071 NH2 ARG B 357 18795 24132 27333 -1153 -4578 -2161 N
ATOM 5072 N ILE B 358 59.046 40.057 75.571 1.00120.50 N
ANISOU 5072 N ILE B 358 13022 16183 16578 1380 -3314 -3082 N
ATOM 5073 CA ILE B 358 59.812 39.018 76.246 1.00129.97 C
ANISOU 5073 CA ILE B 358 14038 17644 17701 1740 -3353 -3164 C
ATOM 5074 C ILE B 358 61.292 39.341 76.097 1.00135.43 C
ANISOU 5074 C ILE B 358 14095 18618 18744 1603 -3396 -3069 C
ATOM 5075 O ILE B 358 61.736 39.792 75.034 1.00128.05 O
ANISOU 5075 O ILE B 358 12880 17799 17976 1325 -3140 -2847 O
ATOM 5076 CB ILE B 358 59.467 37.628 75.679 1.00111.76 C
ANISOU 5076 CB ILE B 358 11978 15397 15090 2084 -3002 -3110 C
ATOM 5077 CG1 ILE B 358 57.966 37.370 75.825 1.00110.16 C
ANISOU 5077 CG1 ILE B 358 12338 14924 14593 2130 -2992 -3151 C
ATOM 5078 CG2 ILE B 358 60.235 36.551 76.394 1.00131.86 C
ANISOU 5078 CG2 ILE B 358 14365 18130 17604 2489 -3102 -3174 C
ATOM 5079 CD1 ILE B 358 57.399 36.441 74.784 1.00130.13 C
ANISOU 5079 CD1 ILE B 358 15152 17387 16903 2251 -2652 -3065 C
ATOM 5080 N SER B 359 62.050 39.122 77.168 1.00159.68 N
ANISOU 5080 N SER B 359 16914 21844 21912 1780 -3729 -3204 N
ATOM 5081 CA SER B 359 63.429 39.584 77.242 1.00170.93 C
ANISOU 5081 CA SER B 359 17676 23534 23736 1599 -3893 -3133 C
ATOM 5082 C SER B 359 64.141 38.870 78.381 1.00166.30 C
ANISOU 5082 C SER B 359 16894 23162 23132 1970 -4218 -3281 C
ATOM 5083 O SER B 359 63.514 38.482 79.371 1.00172.69 O
ANISOU 5083 O SER B 359 18113 23852 23651 2221 -4463 -3453 O
ATOM 5084 CB SER B 359 63.487 41.102 77.450 1.00172.43 C
ANISOU 5084 CB SER B 359 17745 23485 24284 1073 -4265 -3148 C
ATOM 5085 OG SER B 359 63.022 41.449 78.743 1.00178.10 O
ANISOU 5085 OG SER B 359 18768 23990 24911 1161 -4767 -3472 O
ATOM 5086 N ASN B 360 65.454 38.702 78.223 1.00156.58 N
ANISOU 5086 N ASN B 360 15002 22296 22196 2002 -4212 -3177 N
ATOM 5087 CA ASN B 360 66.343 38.200 79.273 1.00163.52 C
ANISOU 5087 CA ASN B 360 15557 23414 23160 2303 -4606 -3281 C
ATOM 5088 C ASN B 360 65.836 36.884 79.866 1.00161.56 C
ANISOU 5088 C ASN B 360 15767 23112 22507 2872 -4610 -3360 C
ATOM 5089 O ASN B 360 65.631 36.756 81.074 1.00156.23 O
ANISOU 5089 O ASN B 360 15328 22389 21645 3024 -5040 -3490 O
ATOM 5090 CB ASN B 360 66.524 39.248 80.377 1.00162.24 C
ANISOU 5090 CB ASN B 360 15325 23141 23178 1999 -5249 -3465 C
ATOM 5091 CG ASN B 360 66.986 40.592 79.847 1.00168.10 C
ANISOU 5091 CG ASN B 360 15660 23813 24398 1372 -5347 -3357 C
ATOM 5092 OD1 ASN B 360 68.169 40.793 79.575 1.00176.71 O
ANISOU 5092 OD1 ASN B 360 16027 25218 25896 1181 -5385 -3186 O
ATOM 5093 ND2 ASN B 360 66.049 41.522 79.701 1.00146.68 N
ANISOU 5093 ND2 ASN B 360 13384 20680 21666 1041 -5408 -3427 N
ATOM 5094 N CYS B 361 65.639 35.891 79.000 1.00154.57 N
ANISOU 5094 N CYS B 361 15020 22236 21474 3181 -4146 -3269 N
ATOM 5095 CA CYS B 361 65.133 34.605 79.461 1.00149.71 C
ANISOU 5095 CA CYS B 361 14865 21473 20545 3671 -4171 -3289 C
ATOM 5096 C CYS B 361 65.556 33.502 78.499 1.00150.50 C
ANISOU 5096 C CYS B 361 14839 21666 20677 4086 -3773 -3247 C
ATOM 5097 O CYS B 361 66.261 33.738 77.514 1.00153.13 O
ANISOU 5097 O CYS B 361 14694 22278 21212 4025 -3438 -3216 O
ATOM 5098 CB CYS B 361 63.610 34.633 79.619 1.00158.59 C
ANISOU 5098 CB CYS B 361 16720 22235 21300 3551 -4120 -3308 C
ATOM 5099 SG CYS B 361 62.709 35.102 78.129 1.00171.02 S
ANISOU 5099 SG CYS B 361 18547 23615 22819 3224 -3599 -3257 S
ATOM 5100 N VAL B 362 65.111 32.285 78.805 1.00157.26 N
ANISOU 5100 N VAL B 362 16136 22292 21324 4516 -3824 -3244 N
ATOM 5101 CA VAL B 362 65.387 31.094 78.010 1.00164.64 C
ANISOU 5101 CA VAL B 362 17093 23186 22276 5004 -3541 -3283 C
ATOM 5102 C VAL B 362 64.057 30.551 77.509 1.00153.52 C
ANISOU 5102 C VAL B 362 16417 21345 20569 4981 -3336 -3282 C
ATOM 5103 O VAL B 362 63.174 30.218 78.310 1.00153.41 O
ANISOU 5103 O VAL B 362 16905 21032 20352 4949 -3586 -3186 O
ATOM 5104 CB VAL B 362 66.143 30.029 78.820 1.00163.25 C
ANISOU 5104 CB VAL B 362 16781 23025 22220 5570 -3893 -3265 C
ATOM 5105 CG1 VAL B 362 66.074 28.680 78.120 1.00156.91 C
ANISOU 5105 CG1 VAL B 362 16250 21966 21401 6112 -3693 -3347 C
ATOM 5106 CG2 VAL B 362 67.588 30.451 79.036 1.00156.33 C
ANISOU 5106 CG2 VAL B 362 15058 22644 21696 5654 -4037 -3285 C
ATOM 5107 N ALA B 363 63.911 30.469 76.189 1.00151.55 N
ANISOU 5107 N ALA B 363 16204 21110 20270 4980 -2891 -3370 N
ATOM 5108 CA ALA B 363 62.690 29.996 75.551 1.00165.82 C
ANISOU 5108 CA ALA B 363 18659 22528 21816 4926 -2711 -3395 C
ATOM 5109 C ALA B 363 62.955 28.664 74.867 1.00168.16 C
ANISOU 5109 C ALA B 363 19110 22669 22116 5487 -2579 -3565 C
ATOM 5110 O ALA B 363 63.895 28.544 74.074 1.00166.83 O
ANISOU 5110 O ALA B 363 18509 22838 22039 5774 -2298 -3723 O
ATOM 5111 CB ALA B 363 62.175 31.014 74.533 1.00150.45 C
ANISOU 5111 CB ALA B 363 16726 20687 19752 4460 -2364 -3384 C
ATOM 5112 N ASP B 364 62.122 27.668 75.169 1.00171.62 N
ANISOU 5112 N ASP B 364 20150 22599 22457 5645 -2788 -3534 N
ATOM 5113 CA ASP B 364 62.249 26.338 74.577 1.00171.79 C
ANISOU 5113 CA ASP B 364 20439 22310 22522 6183 -2770 -3731 C
ATOM 5114 C ASP B 364 61.234 26.237 73.441 1.00175.12 C
ANISOU 5114 C ASP B 364 21341 22493 22703 5990 -2511 -3862 C
ATOM 5115 O ASP B 364 60.154 25.663 73.579 1.00178.68 O
ANISOU 5115 O ASP B 364 22376 22445 23071 5861 -2703 -3777 O
ATOM 5116 CB ASP B 364 62.044 25.259 75.637 1.00170.63 C
ANISOU 5116 CB ASP B 364 20654 21692 22488 6452 -3249 -3562 C
ATOM 5117 CG ASP B 364 62.427 23.876 75.147 1.00185.24 C
ANISOU 5117 CG ASP B 364 22716 23163 24504 7099 -3338 -3790 C
ATOM 5118 OD1 ASP B 364 62.999 23.768 74.042 1.00187.36 O
ANISOU 5118 OD1 ASP B 364 22771 23642 24774 7422 -3002 -4143 O
ATOM 5119 OD2 ASP B 364 62.160 22.895 75.873 1.00191.90 O1-
ANISOU 5119 OD2 ASP B 364 23945 23499 25469 7298 -3757 -3614 O1-
ATOM 5120 N TYR B 365 61.603 26.816 72.292 1.00156.97 N
ANISOU 5120 N TYR B 365 17539 20296 21807 2408 -3982 2193 N
ATOM 5121 CA TYR B 365 60.699 26.873 71.146 1.00157.21 C
ANISOU 5121 CA TYR B 365 17776 20227 21732 2082 -3766 1805 C
ATOM 5122 C TYR B 365 60.255 25.494 70.671 1.00155.97 C
ANISOU 5122 C TYR B 365 17762 19403 22094 2248 -3698 1637 C
ATOM 5123 O TYR B 365 59.213 25.386 70.016 1.00148.93 O
ANISOU 5123 O TYR B 365 17127 18267 21194 1990 -3602 1448 O
ATOM 5124 CB TYR B 365 61.352 27.617 69.978 1.00154.29 C
ANISOU 5124 CB TYR B 365 17196 20315 21113 1944 -3575 1314 C
ATOM 5125 CG TYR B 365 61.651 29.081 70.224 1.00158.47 C
ANISOU 5125 CG TYR B 365 17661 21451 21097 1646 -3717 1444 C
ATOM 5126 CD1 TYR B 365 60.627 30.016 70.308 1.00136.70 C
ANISOU 5126 CD1 TYR B 365 15266 18842 17832 1267 -3834 1504 C
ATOM 5127 CD2 TYR B 365 62.960 29.533 70.338 1.00162.95 C
ANISOU 5127 CD2 TYR B 365 17820 22450 21645 1749 -3794 1491 C
ATOM 5128 CE1 TYR B 365 60.898 31.356 70.520 1.00143.01 C
ANISOU 5128 CE1 TYR B 365 16092 20140 18106 1020 -4093 1606 C
ATOM 5129 CE2 TYR B 365 63.240 30.870 70.548 1.00155.67 C
ANISOU 5129 CE2 TYR B 365 16872 22014 20262 1438 -4031 1645 C
ATOM 5130 CZ TYR B 365 62.206 31.776 70.638 1.00159.86 C
ANISOU 5130 CZ TYR B 365 17838 22621 20280 1083 -4213 1697 C
ATOM 5131 OH TYR B 365 62.485 33.107 70.847 1.00160.66 O
ANISOU 5131 OH TYR B 365 17994 23152 19896 800 -4574 1838 O
ATOM 5132 N SER B 366 61.017 24.443 70.974 1.00155.89 N
ANISOU 5132 N SER B 366 17629 19068 22534 2691 -3808 1677 N
ATOM 5133 CA SER B 366 60.656 23.101 70.533 1.00157.87 C
ANISOU 5133 CA SER B 366 18080 18620 23282 2888 -3886 1518 C
ATOM 5134 C SER B 366 59.519 22.491 71.343 1.00156.07 C
ANISOU 5134 C SER B 366 18170 17861 23270 2681 -4057 2043 C
ATOM 5135 O SER B 366 58.982 21.455 70.938 1.00158.95 O
ANISOU 5135 O SER B 366 18761 17582 24051 2706 -4187 1967 O
ATOM 5136 CB SER B 366 61.878 22.181 70.591 1.00167.12 C
ANISOU 5136 CB SER B 366 19067 19637 24793 3482 -4034 1347 C
ATOM 5137 OG SER B 366 62.728 22.531 71.668 1.00171.88 O
ANISOU 5137 OG SER B 366 19445 20563 25299 3660 -4124 1674 O
ATOM 5138 N VAL B 367 59.144 23.096 72.472 1.00150.65 N
ANISOU 5138 N VAL B 367 17497 17440 22301 2501 -4099 2598 N
ATOM 5139 CA VAL B 367 58.015 22.584 73.243 1.00153.05 C
ANISOU 5139 CA VAL B 367 18032 17386 22734 2284 -4212 3170 C
ATOM 5140 C VAL B 367 56.700 22.929 72.554 1.00175.44 C
ANISOU 5140 C VAL B 367 21032 20231 25397 1808 -4079 3050 C
ATOM 5141 O VAL B 367 55.772 22.112 72.509 1.00180.72 O
ANISOU 5141 O VAL B 367 21876 20390 26401 1602 -4164 3262 O
ATOM 5142 CB VAL B 367 58.066 23.129 74.684 1.00155.12 C
ANISOU 5142 CB VAL B 367 18242 18017 22681 2372 -4305 3802 C
ATOM 5143 CG1 VAL B 367 56.717 22.968 75.373 1.00152.03 C
ANISOU 5143 CG1 VAL B 367 18016 17552 22197 2075 -4331 4412 C
ATOM 5144 CG2 VAL B 367 59.160 22.431 75.478 1.00161.66 C
ANISOU 5144 CG2 VAL B 367 18998 18599 23827 2863 -4489 3984 C
ATOM 5145 N LEU B 368 56.607 24.132 71.986 1.00165.77 N
ANISOU 5145 N LEU B 368 19768 19562 23656 1614 -3908 2698 N
ATOM 5146 CA LEU B 368 55.359 24.584 71.378 1.00156.97 C
ANISOU 5146 CA LEU B 368 18840 18517 22285 1197 -3797 2526 C
ATOM 5147 C LEU B 368 55.077 23.845 70.074 1.00160.64 C
ANISOU 5147 C LEU B 368 19436 18420 23178 1161 -3737 1981 C
ATOM 5148 O LEU B 368 54.036 23.194 69.927 1.00161.88 O
ANISOU 5148 O LEU B 368 19762 18116 23630 936 -3808 2103 O
ATOM 5149 CB LEU B 368 55.421 26.094 71.141 1.00148.80 C
ANISOU 5149 CB LEU B 368 17805 18197 20536 1040 -3711 2262 C
ATOM 5150 CG LEU B 368 55.923 26.916 72.329 1.00132.98 C
ANISOU 5150 CG LEU B 368 15694 16734 18098 1190 -3883 2708 C
ATOM 5151 CD1 LEU B 368 56.133 28.368 71.933 1.00119.69 C
ANISOU 5151 CD1 LEU B 368 14060 15656 15758 1033 -3916 2381 C
ATOM 5152 CD2 LEU B 368 54.953 26.810 73.496 1.00138.37 C
ANISOU 5152 CD2 LEU B 368 16463 17502 18609 1156 -4011 3374 C
ATOM 5153 N TYR B 369 56.001 23.941 69.113 1.00168.49 N
ANISOU 5153 N TYR B 369 20341 19469 24208 1410 -3632 1394 N
ATOM 5154 CA TYR B 369 55.790 23.345 67.796 1.00176.11 C
ANISOU 5154 CA TYR B 369 21455 19962 25496 1504 -3596 808 C
ATOM 5155 C TYR B 369 55.620 21.834 67.882 1.00181.26 C
ANISOU 5155 C TYR B 369 22242 19780 26850 1710 -3894 972 C
ATOM 5156 O TYR B 369 54.955 21.234 67.030 1.00177.05 O
ANISOU 5156 O TYR B 369 21937 18687 26648 1689 -4000 663 O
ATOM 5157 CB TYR B 369 56.961 23.705 66.878 1.00182.61 C
ANISOU 5157 CB TYR B 369 22087 21131 26167 1836 -3424 240 C
ATOM 5158 CG TYR B 369 56.858 23.184 65.459 1.00191.45 C
ANISOU 5158 CG TYR B 369 23355 21864 27524 2081 -3381 -415 C
ATOM 5159 CD1 TYR B 369 55.856 23.627 64.604 1.00181.89 C
ANISOU 5159 CD1 TYR B 369 22410 20555 26146 1802 -3254 -790 C
ATOM 5160 CD2 TYR B 369 57.775 22.261 64.969 1.00195.21 C
ANISOU 5160 CD2 TYR B 369 23729 22093 28349 2672 -3503 -698 C
ATOM 5161 CE1 TYR B 369 55.765 23.161 63.305 1.00177.12 C
ANISOU 5161 CE1 TYR B 369 21975 19567 25757 2111 -3242 -1410 C
ATOM 5162 CE2 TYR B 369 57.691 21.789 63.670 1.00199.69 C
ANISOU 5162 CE2 TYR B 369 24456 22330 29089 3021 -3517 -1308 C
ATOM 5163 CZ TYR B 369 56.684 22.242 62.844 1.00193.77 C
ANISOU 5163 CZ TYR B 369 23979 21440 28206 2742 -3382 -1653 C
ATOM 5164 OH TYR B 369 56.596 21.776 61.552 1.00192.33 O
ANISOU 5164 OH TYR B 369 23989 20893 28196 3168 -3422 -2278 O
ATOM 5165 N ASN B 370 56.196 21.207 68.906 1.00181.99 N
ANISOU 5165 N ASN B 370 22242 19730 27176 1920 -4093 1450 N
ATOM 5166 CA ASN B 370 56.094 19.770 69.110 1.00188.28 C
ANISOU 5166 CA ASN B 370 23226 19705 28607 2100 -4471 1666 C
ATOM 5167 C ASN B 370 55.158 19.420 70.267 1.00194.68 C
ANISOU 5167 C ASN B 370 24127 20286 29557 1704 -4616 2479 C
ATOM 5168 O ASN B 370 55.399 18.457 70.999 1.00199.25 O
ANISOU 5168 O ASN B 370 24792 20401 30513 1852 -4916 2902 O
ATOM 5169 CB ASN B 370 57.485 19.173 69.331 1.00189.98 C
ANISOU 5169 CB ASN B 370 23326 19867 28992 2698 -4642 1546 C
ATOM 5170 CG ASN B 370 57.530 17.685 69.065 1.00198.81 C
ANISOU 5170 CG ASN B 370 24732 20089 30718 3027 -5124 1465 C
ATOM 5171 OD1 ASN B 370 56.625 17.121 68.450 1.00197.43 O
ANISOU 5171 OD1 ASN B 370 24831 19306 30877 2850 -5337 1377 O
ATOM 5172 ND2 ASN B 370 58.595 17.039 69.523 1.00200.88 N
ANISOU 5172 ND2 ASN B 370 24964 20241 31122 3535 -5364 1470 N
ATOM 5173 N SER B 371 54.087 20.200 70.445 1.00204.78 N
ANISOU 5173 N SER B 371 25388 21929 30488 1222 -4416 2708 N
ATOM 5174 CA SER B 371 53.050 19.893 71.422 1.00213.62 C
ANISOU 5174 CA SER B 371 26533 22947 31685 830 -4512 3492 C
ATOM 5175 C SER B 371 51.757 19.401 70.790 1.00219.28 C
ANISOU 5175 C SER B 371 27411 23172 32734 404 -4625 3490 C
ATOM 5176 O SER B 371 50.927 18.819 71.497 1.00222.43 O
ANISOU 5176 O SER B 371 27811 23333 33369 63 -4780 4190 O
ATOM 5177 CB SER B 371 52.738 21.124 72.288 1.00203.05 C
ANISOU 5177 CB SER B 371 25020 22499 29632 667 -4264 3856 C
ATOM 5178 OG SER B 371 51.575 20.929 73.076 1.00210.41 O
ANISOU 5178 OG SER B 371 25927 23488 30530 296 -4300 4575 O
ATOM 5179 N ALA B 372 51.569 19.632 69.489 1.00202.66 N
ANISOU 5179 N ALA B 372 25427 20924 30650 419 -4557 2744 N
ATOM 5180 CA ALA B 372 50.417 19.138 68.734 1.00200.72 C
ANISOU 5180 CA ALA B 372 25365 20112 30789 91 -4718 2609 C
ATOM 5181 C ALA B 372 49.098 19.653 69.300 1.00192.65 C
ANISOU 5181 C ALA B 372 24224 19514 29461 -475 -4570 3110 C
ATOM 5182 O ALA B 372 48.068 18.979 69.213 1.00187.80 O
ANISOU 5182 O ALA B 372 23664 18417 29275 -856 -4784 3406 O
ATOM 5183 CB ALA B 372 50.412 17.608 68.666 1.00197.64 C
ANISOU 5183 CB ALA B 372 25180 18690 31224 168 -5244 2835 C
ATOM 5184 N SER B 373 49.114 20.853 69.878 1.00178.05 N
ANISOU 5184 N SER B 373 22207 18592 26850 -512 -4255 3212 N
ATOM 5185 CA SER B 373 47.903 21.471 70.400 1.00180.64 C
ANISOU 5185 CA SER B 373 22414 19498 26722 -925 -4122 3609 C
ATOM 5186 C SER B 373 47.319 22.524 69.472 1.00170.24 C
ANISOU 5186 C SER B 373 21218 18575 24890 -1044 -3920 2884 C
ATOM 5187 O SER B 373 46.150 22.890 69.635 1.00163.46 O
ANISOU 5187 O SER B 373 20303 18079 23726 -1384 -3866 3060 O
ATOM 5188 CB SER B 373 48.179 22.110 71.768 1.00175.97 C
ANISOU 5188 CB SER B 373 21617 19704 25540 -807 -4016 4244 C
ATOM 5189 OG SER B 373 46.972 22.442 72.432 1.00182.21 O
ANISOU 5189 OG SER B 373 22252 21048 25933 -1132 -3953 4791 O
ATOM 5190 N PHE B 374 48.089 23.005 68.501 1.00151.40 N
ANISOU 5190 N PHE B 374 18994 16154 22378 -764 -3814 2082 N
ATOM 5191 CA PHE B 374 47.692 24.131 67.670 1.00129.46 C
ANISOU 5191 CA PHE B 374 16386 13796 19008 -841 -3624 1378 C
ATOM 5192 C PHE B 374 47.250 23.660 66.292 1.00135.11 C
ANISOU 5192 C PHE B 374 17347 13806 20182 -856 -3668 686 C
ATOM 5193 O PHE B 374 47.880 22.786 65.689 1.00135.49 O
ANISOU 5193 O PHE B 374 17470 13168 20841 -572 -3806 452 O
ATOM 5194 CB PHE B 374 48.843 25.127 67.528 1.00131.60 C
ANISOU 5194 CB PHE B 374 16672 14588 18743 -553 -3476 999 C
ATOM 5195 CG PHE B 374 49.532 25.441 68.823 1.00143.44 C
ANISOU 5195 CG PHE B 374 17953 16606 19943 -411 -3519 1630 C
ATOM 5196 CD1 PHE B 374 48.915 26.235 69.775 1.00132.68 C
ANISOU 5196 CD1 PHE B 374 16539 15947 17925 -538 -3549 2060 C
ATOM 5197 CD2 PHE B 374 50.799 24.947 69.088 1.00140.42 C
ANISOU 5197 CD2 PHE B 374 17428 16024 19903 -75 -3565 1762 C
ATOM 5198 CE1 PHE B 374 49.546 26.529 70.966 1.00122.07 C
ANISOU 5198 CE1 PHE B 374 15033 15042 16307 -315 -3639 2622 C
ATOM 5199 CE2 PHE B 374 51.436 25.238 70.278 1.00135.11 C
ANISOU 5199 CE2 PHE B 374 16578 15776 18982 98 -3631 2306 C
ATOM 5200 CZ PHE B 374 50.808 26.030 71.218 1.00133.75 C
ANISOU 5200 CZ PHE B 374 16382 16247 18189 -12 -3675 2743 C
ATOM 5201 N SER B 375 46.163 24.254 65.797 1.00144.60 N
ANISOU 5201 N SER B 375 18700 15193 21050 -1120 -3592 322 N
ATOM 5202 CA SER B 375 45.701 23.985 64.442 1.00138.25 C
ANISOU 5202 CA SER B 375 18180 13758 20592 -1082 -3630 -434 C
ATOM 5203 C SER B 375 46.510 24.731 63.389 1.00139.96 C
ANISOU 5203 C SER B 375 18628 14099 20453 -744 -3429 -1285 C
ATOM 5204 O SER B 375 46.462 24.357 62.212 1.00142.31 O
ANISOU 5204 O SER B 375 19166 13794 21112 -524 -3467 -1928 O
ATOM 5205 CB SER B 375 44.221 24.352 64.311 1.00124.43 C
ANISOU 5205 CB SER B 375 16506 12171 18602 -1474 -3629 -542 C
ATOM 5206 OG SER B 375 44.022 25.738 64.524 1.00113.80 O
ANISOU 5206 OG SER B 375 15234 11742 16265 -1541 -3436 -771 O
ATOM 5207 N THR B 376 47.246 25.769 63.779 1.00131.74 N
ANISOU 5207 N THR B 376 16354 15841 17859 1335 -1817 -2688 N
ATOM 5208 CA THR B 376 48.066 26.532 62.847 1.00129.08 C
ANISOU 5208 CA THR B 376 15890 15926 17228 1301 -1669 -2939 C
ATOM 5209 C THR B 376 49.399 26.862 63.501 1.00133.33 C
ANISOU 5209 C THR B 376 16170 16712 17776 1471 -1639 -2844 C
ATOM 5210 O THR B 376 49.435 27.366 64.628 1.00125.69 O
ANISOU 5210 O THR B 376 15161 15810 16786 1449 -1744 -2534 O
ATOM 5211 CB THR B 376 47.362 27.821 62.403 1.00117.98 C
ANISOU 5211 CB THR B 376 14585 14804 15439 990 -1625 -2863 C
ATOM 5212 OG1 THR B 376 46.137 27.493 61.736 1.00115.51 O
ANISOU 5212 OG1 THR B 376 14466 14320 15100 854 -1679 -2983 O
ATOM 5213 CG2 THR B 376 48.250 28.618 61.457 1.00120.14 C
ANISOU 5213 CG2 THR B 376 14724 15494 15431 962 -1422 -3055 C
ATOM 5214 N PHE B 377 50.488 26.569 62.789 1.00135.19 N
ANISOU 5214 N PHE B 377 16217 17114 18036 1655 -1502 -3134 N
ATOM 5215 CA PHE B 377 51.838 26.881 63.264 1.00125.17 C
ANISOU 5215 CA PHE B 377 14628 16138 16792 1811 -1464 -3098 C
ATOM 5216 C PHE B 377 52.720 26.993 62.014 1.00127.49 C
ANISOU 5216 C PHE B 377 14745 16728 16969 1870 -1223 -3438 C
ATOM 5217 O PHE B 377 53.370 26.026 61.616 1.00136.14 O
ANISOU 5217 O PHE B 377 15738 17744 18245 2174 -1156 -3678 O
ATOM 5218 CB PHE B 377 52.357 25.829 64.229 1.00136.04 C
ANISOU 5218 CB PHE B 377 15905 17287 18499 2171 -1596 -2985 C
ATOM 5219 CG PHE B 377 53.451 26.318 65.149 1.00147.62 C
ANISOU 5219 CG PHE B 377 17052 19079 19957 2293 -1669 -2838 C
ATOM 5220 CD1 PHE B 377 54.556 26.995 64.653 1.00150.14 C
ANISOU 5220 CD1 PHE B 377 17050 19825 20172 2256 -1530 -3020 C
ATOM 5221 CD2 PHE B 377 53.374 26.093 66.514 1.00141.07 C
ANISOU 5221 CD2 PHE B 377 16224 18154 19224 2453 -1879 -2518 C
ATOM 5222 CE1 PHE B 377 55.557 27.436 65.500 1.00127.36 C
ANISOU 5222 CE1 PHE B 377 13825 17253 17315 2342 -1629 -2931 C
ATOM 5223 CE2 PHE B 377 54.372 26.534 67.365 1.00124.59 C
ANISOU 5223 CE2 PHE B 377 13826 16415 17100 2584 -1992 -2430 C
ATOM 5224 CZ PHE B 377 55.465 27.205 66.856 1.00124.49 C
ANISOU 5224 CZ PHE B 377 13467 16814 17020 2512 -1884 -2659 C
ATOM 5225 N LYS B 378 52.711 28.176 61.403 1.00131.29 N
ANISOU 5225 N LYS B 378 15201 17537 17147 1597 -1070 -3437 N
ATOM 5226 CA LYS B 378 53.507 28.470 60.219 1.00145.87 C
ANISOU 5226 CA LYS B 378 16877 19724 18825 1626 -788 -3682 C
ATOM 5227 C LYS B 378 54.512 29.560 60.559 1.00136.39 C
ANISOU 5227 C LYS B 378 15345 18887 17589 1486 -676 -3546 C
ATOM 5228 O LYS B 378 54.129 30.626 61.052 1.00132.56 O
ANISOU 5228 O LYS B 378 14913 18456 16997 1193 -726 -3314 O
ATOM 5229 CB LYS B 378 52.628 28.922 59.047 1.00151.06 C
ANISOU 5229 CB LYS B 378 17788 20465 19142 1440 -654 -3781 C
ATOM 5230 CG LYS B 378 51.431 28.032 58.745 1.00148.70 C
ANISOU 5230 CG LYS B 378 17810 19819 18871 1480 -814 -3927 C
ATOM 5231 CD LYS B 378 50.672 28.561 57.531 1.00147.21 C
ANISOU 5231 CD LYS B 378 17819 19829 18285 1331 -697 -4049 C
ATOM 5232 CE LYS B 378 49.376 27.802 57.290 1.00139.94 C
ANISOU 5232 CE LYS B 378 17177 18592 17401 1307 -903 -4204 C
ATOM 5233 NZ LYS B 378 49.355 27.137 55.956 1.00135.23 N
ANISOU 5233 NZ LYS B 378 16654 18092 16634 1485 -818 -4667 N
ATOM 5234 N CYS B 379 55.788 29.299 60.293 1.00140.63 N
ANISOU 5234 N CYS B 379 15526 19665 18241 1693 -522 -3708 N
ATOM 5235 CA CYS B 379 56.851 30.260 60.546 1.00140.27 C
ANISOU 5235 CA CYS B 379 15088 19977 18231 1547 -402 -3626 C
ATOM 5236 C CYS B 379 57.452 30.735 59.230 1.00146.97 C
ANISOU 5236 C CYS B 379 15777 21167 18900 1494 -3 -3762 C
ATOM 5237 O CYS B 379 57.617 29.951 58.290 1.00161.40 O
ANISOU 5237 O CYS B 379 17635 23036 20654 1757 161 -4005 O
ATOM 5238 CB CYS B 379 57.942 29.661 61.440 1.00142.58 C
ANISOU 5238 CB CYS B 379 15001 20346 18826 1830 -550 -3658 C
ATOM 5239 SG CYS B 379 57.374 29.149 63.081 1.00153.74 S
ANISOU 5239 SG CYS B 379 16569 21437 20409 1955 -990 -3428 S
ATOM 5240 N TYR B 380 57.778 32.024 59.174 1.00150.90 N
ANISOU 5240 N TYR B 380 16108 21897 19330 1161 167 -3603 N
ATOM 5241 CA TYR B 380 58.253 32.677 57.960 1.00158.37 C
ANISOU 5241 CA TYR B 380 16924 23163 20086 1058 595 -3625 C
ATOM 5242 C TYR B 380 59.674 33.168 58.201 1.00163.53 C
ANISOU 5242 C TYR B 380 17011 24130 20992 987 761 -3618 C
ATOM 5243 O TYR B 380 59.906 33.973 59.108 1.00161.31 O
ANISOU 5243 O TYR B 380 16553 23841 20896 712 623 -3478 O
ATOM 5244 CB TYR B 380 57.334 33.841 57.576 1.00149.49 C
ANISOU 5244 CB TYR B 380 16108 22000 18691 704 710 -3393 C
ATOM 5245 CG TYR B 380 55.874 33.464 57.420 1.00150.96 C
ANISOU 5245 CG TYR B 380 16804 21912 18643 739 512 -3386 C
ATOM 5246 CD1 TYR B 380 55.046 33.339 58.530 1.00147.63 C
ANISOU 5246 CD1 TYR B 380 16590 21166 18335 666 141 -3272 C
ATOM 5247 CD2 TYR B 380 55.321 33.243 56.165 1.00153.36 C
ANISOU 5247 CD2 TYR B 380 17355 22315 18600 852 696 -3496 C
ATOM 5248 CE1 TYR B 380 53.714 32.997 58.396 1.00143.93 C
ANISOU 5248 CE1 TYR B 380 16530 20461 17695 675 -27 -3257 C
ATOM 5249 CE2 TYR B 380 53.987 32.902 56.021 1.00153.04 C
ANISOU 5249 CE2 TYR B 380 17725 22052 18372 864 487 -3521 C
ATOM 5250 CZ TYR B 380 53.190 32.780 57.140 1.00149.46 C
ANISOU 5250 CZ TYR B 380 17439 21259 18091 760 134 -3394 C
ATOM 5251 OH TYR B 380 51.863 32.441 57.005 1.00142.27 O
ANISOU 5251 OH TYR B 380 16883 20138 17034 752 -61 -3410 O
ATOM 5252 N GLY B 381 60.620 32.682 57.398 1.00179.03 N
ANISOU 5252 N GLY B 381 18672 26381 22970 1239 1052 -3795 N
ATOM 5253 CA GLY B 381 62.010 33.072 57.549 1.00189.25 C
ANISOU 5253 CA GLY B 381 19362 28014 24532 1188 1235 -3803 C
ATOM 5254 C GLY B 381 62.786 32.120 58.432 1.00185.33 C
ANISOU 5254 C GLY B 381 18530 27540 24347 1521 957 -3962 C
ATOM 5255 O GLY B 381 63.607 31.337 57.949 1.00185.90 O
ANISOU 5255 O GLY B 381 18326 27821 24488 1883 1125 -4152 O
ATOM 5256 N VAL B 382 62.534 32.182 59.740 1.00182.94 N
ANISOU 5256 N VAL B 382 18254 27043 24212 1440 537 -3876 N
ATOM 5257 CA VAL B 382 63.116 31.205 60.650 1.00181.00 C
ANISOU 5257 CA VAL B 382 17766 26796 24209 1820 231 -3978 C
ATOM 5258 C VAL B 382 62.454 29.848 60.421 1.00184.77 C
ANISOU 5258 C VAL B 382 18645 26952 24609 2241 129 -4086 C
ATOM 5259 O VAL B 382 61.402 29.742 59.781 1.00186.53 O
ANISOU 5259 O VAL B 382 19347 26930 24597 2174 194 -4089 O
ATOM 5260 CB VAL B 382 62.957 31.688 62.103 1.00180.88 C
ANISOU 5260 CB VAL B 382 17707 26697 24322 1640 -186 -3840 C
ATOM 5261 CG1 VAL B 382 61.471 31.909 62.430 1.00174.41 C
ANISOU 5261 CG1 VAL B 382 17501 25478 23290 1453 -377 -3671 C
ATOM 5262 CG2 VAL B 382 63.637 30.740 63.112 1.00168.66 C
ANISOU 5262 CG2 VAL B 382 15871 25219 22993 2072 -511 -3900 C
ATOM 5263 N SER B 383 63.110 28.789 60.899 1.00166.28 N
ANISOU 5263 N SER B 383 16081 24612 22485 2691 -22 -4191 N
ATOM 5264 CA SER B 383 62.546 27.452 60.823 1.00170.44 C
ANISOU 5264 CA SER B 383 16967 24755 23037 3096 -135 -4291 C
ATOM 5265 C SER B 383 62.113 26.985 62.201 1.00169.54 C
ANISOU 5265 C SER B 383 17001 24344 23073 3227 -558 -4099 C
ATOM 5266 O SER B 383 62.920 27.013 63.140 1.00162.59 O
ANISOU 5266 O SER B 383 15737 23678 22363 3368 -751 -4022 O
ATOM 5267 CB SER B 383 63.569 26.477 60.238 1.00173.10 C
ANISOU 5267 CB SER B 383 17001 25254 23517 3591 62 -4540 C
ATOM 5268 OG SER B 383 63.985 26.908 58.954 1.00162.64 O
ANISOU 5268 OG SER B 383 15532 24253 22012 3504 489 -4698 O
ATOM 5269 N PRO B 384 60.864 26.545 62.373 1.00193.58 N
ANISOU 5269 N PRO B 384 20570 26927 26054 3200 -711 -4008 N
ATOM 5270 CA PRO B 384 60.465 25.997 63.675 1.00188.25 C
ANISOU 5270 CA PRO B 384 20036 25968 25522 3380 -1064 -3779 C
ATOM 5271 C PRO B 384 61.250 24.758 64.021 1.00187.90 C
ANISOU 5271 C PRO B 384 19794 25852 25748 3950 -1131 -3832 C
ATOM 5272 O PRO B 384 61.210 24.315 65.173 1.00183.97 O
ANISOU 5272 O PRO B 384 19309 25220 25372 4182 -1404 -3603 O
ATOM 5273 CB PRO B 384 58.973 25.688 63.491 1.00199.75 C
ANISOU 5273 CB PRO B 384 22068 26938 26890 3231 -1117 -3708 C
ATOM 5274 CG PRO B 384 58.835 25.488 62.022 1.00195.18 C
ANISOU 5274 CG PRO B 384 21615 26346 26199 3207 -824 -4010 C
ATOM 5275 CD PRO B 384 59.763 26.486 61.402 1.00196.12 C
ANISOU 5275 CD PRO B 384 21354 26989 26174 3028 -572 -4104 C
ATOM 5276 N THR B 385 61.993 24.205 63.064 1.00203.43 N
ANISOU 5276 N THR B 385 21570 27930 27792 4221 -876 -4112 N
ATOM 5277 CA THR B 385 62.722 22.950 63.246 1.00206.92 C
ANISOU 5277 CA THR B 385 21855 28258 28508 4818 -896 -4192 C
ATOM 5278 C THR B 385 63.974 23.175 64.094 1.00191.99 C
ANISOU 5278 C THR B 385 19381 26834 26732 5038 -1032 -4092 C
ATOM 5279 O THR B 385 65.099 23.236 63.596 1.00190.03 O
ANISOU 5279 O THR B 385 18663 26996 26543 5202 -842 -4282 O
ATOM 5280 CB THR B 385 63.101 22.373 61.890 1.00202.27 C
ANISOU 5280 CB THR B 385 21249 27676 27926 5040 -560 -4567 C
ATOM 5281 OG1 THR B 385 63.902 23.326 61.182 1.00200.90 O
ANISOU 5281 OG1 THR B 385 20673 28074 27586 4826 -297 -4694 O
ATOM 5282 CG2 THR B 385 61.862 22.057 61.083 1.00190.77 C
ANISOU 5282 CG2 THR B 385 20353 25776 26354 4864 -484 -4719 C
ATOM 5283 N LYS B 386 63.764 23.284 65.404 1.00176.37 N
ANISOU 5283 N LYS B 386 17419 24821 24772 5060 -1370 -3795 N
ATOM 5284 CA LYS B 386 64.864 23.416 66.363 1.00195.22 C
ANISOU 5284 CA LYS B 386 19271 27658 27245 5316 -1587 -3700 C
ATOM 5285 C LYS B 386 65.799 24.580 66.027 1.00199.72 C
ANISOU 5285 C LYS B 386 19286 28840 27757 4981 -1472 -3873 C
ATOM 5286 O LYS B 386 67.010 24.495 66.253 1.00200.22 O
ANISOU 5286 O LYS B 386 18773 29340 27962 5255 -1507 -3955 O
ATOM 5287 CB LYS B 386 65.678 22.115 66.478 1.00200.91 C
ANISOU 5287 CB LYS B 386 19792 28323 28223 6024 -1585 -3729 C
ATOM 5288 CG LYS B 386 65.133 21.128 67.498 1.00194.34 C
ANISOU 5288 CG LYS B 386 19295 27042 27502 6431 -1836 -3407 C
ATOM 5289 CD LYS B 386 65.528 21.512 68.913 1.00187.93 C
ANISOU 5289 CD LYS B 386 18200 26605 26601 6556 -2209 -3132 C
ATOM 5290 CE LYS B 386 65.123 20.447 69.918 1.00179.34 C
ANISOU 5290 CE LYS B 386 17408 25121 25614 7067 -2410 -2756 C
ATOM 5291 NZ LYS B 386 65.419 20.868 71.316 1.00178.05 N
ANISOU 5291 NZ LYS B 386 17009 25374 25268 7206 -2790 -2482 N
ATOM 5292 N LEU B 387 65.261 25.675 65.485 1.00179.45 N
ANISOU 5292 N LEU B 387 16865 26309 25011 4392 -1325 -3917 N
ATOM 5293 CA LEU B 387 66.080 26.875 65.325 1.00182.07 C
ANISOU 5293 CA LEU B 387 16682 27156 25339 4013 -1227 -4022 C
ATOM 5294 C LEU B 387 66.020 27.735 66.564 1.00185.19 C
ANISOU 5294 C LEU B 387 16954 27723 25687 3754 -1595 -3883 C
ATOM 5295 O LEU B 387 66.336 28.931 66.518 1.00177.94 O
ANISOU 5295 O LEU B 387 15757 27088 24763 3286 -1548 -3953 O
ATOM 5296 CB LEU B 387 65.659 27.674 64.092 1.00175.84 C
ANISOU 5296 CB LEU B 387 16071 26344 24398 3542 -844 -4117 C
ATOM 5297 CG LEU B 387 66.693 27.659 62.960 1.00168.28 C
ANISOU 5297 CG LEU B 387 14677 25744 23519 3632 -431 -4331 C
ATOM 5298 CD1 LEU B 387 66.810 26.269 62.363 1.00164.66 C
ANISOU 5298 CD1 LEU B 387 14354 25095 23113 4206 -294 -4480 C
ATOM 5299 CD2 LEU B 387 66.335 28.666 61.883 1.00180.35 C
ANISOU 5299 CD2 LEU B 387 16336 27329 24860 3137 -59 -4349 C
ATOM 5300 N ASN B 388 65.599 27.125 67.673 1.00194.89 N
ANISOU 5300 N ASN B 388 18404 28764 26883 4066 -1948 -3685 N
ATOM 5301 CA ASN B 388 65.784 27.728 68.976 1.00182.95 C
ANISOU 5301 CA ASN B 388 16686 27522 25306 3997 -2345 -3592 C
ATOM 5302 C ASN B 388 67.256 27.972 69.246 1.00182.41 C
ANISOU 5302 C ASN B 388 15841 28054 25411 4123 -2444 -3778 C
ATOM 5303 O ASN B 388 67.600 28.678 70.200 1.00180.49 O
ANISOU 5303 O ASN B 388 15304 28146 25130 3985 -2770 -3808 O
ATOM 5304 CB ASN B 388 65.200 26.815 70.061 1.00175.13 C
ANISOU 5304 CB ASN B 388 16034 26270 24236 4451 -2658 -3309 C
ATOM 5305 CG ASN B 388 65.528 25.350 69.833 1.00186.27 C
ANISOU 5305 CG ASN B 388 17464 27481 25829 5083 -2572 -3255 C
ATOM 5306 OD1 ASN B 388 66.441 25.023 69.077 1.00192.60 O
ANISOU 5306 OD1 ASN B 388 17896 28478 26807 5267 -2356 -3463 O
ATOM 5307 ND2 ASN B 388 64.807 24.466 70.512 1.00176.58 N
ANISOU 5307 ND2 ASN B 388 16655 25860 24579 5433 -2723 -2963 N
ATOM 5308 N ASP B 389 68.135 27.391 68.420 1.00185.11 N
ANISOU 5308 N ASP B 389 15830 28559 25946 4395 -2176 -3928 N
ATOM 5309 CA ASP B 389 69.574 27.585 68.565 1.00195.28 C
ANISOU 5309 CA ASP B 389 16312 30450 27436 4522 -2227 -4111 C
ATOM 5310 C ASP B 389 69.955 29.057 68.540 1.00196.89 C
ANISOU 5310 C ASP B 389 16124 30992 27694 3866 -2209 -4273 C
ATOM 5311 O ASP B 389 70.936 29.451 69.175 1.00201.14 O
ANISOU 5311 O ASP B 389 16020 32030 28375 3864 -2450 -4411 O
ATOM 5312 CB ASP B 389 70.306 26.852 67.440 1.00190.05 C
ANISOU 5312 CB ASP B 389 15394 29867 26949 4842 -1828 -4253 C
ATOM 5313 CG ASP B 389 69.992 25.378 67.409 1.00194.05 C
ANISOU 5313 CG ASP B 389 16277 29984 27469 5494 -1824 -4140 C
ATOM 5314 OD1 ASP B 389 69.531 24.841 68.437 1.00200.45 O
ANISOU 5314 OD1 ASP B 389 17362 30588 28212 5797 -2168 -3918 O
ATOM 5315 OD2 ASP B 389 70.177 24.765 66.337 1.00198.52 O1-
ANISOU 5315 OD2 ASP B 389 16885 30429 28115 5702 -1456 -4272 O1-
ATOM 5316 N LEU B 390 69.191 29.883 67.829 1.00188.00 N
ANISOU 5316 N LEU B 390 15364 29592 26474 3310 -1937 -4262 N
ATOM 5317 CA LEU B 390 69.573 31.263 67.562 1.00183.90 C
ANISOU 5317 CA LEU B 390 14494 29306 26073 2672 -1797 -4398 C
ATOM 5318 C LEU B 390 69.192 32.198 68.711 1.00178.36 C
ANISOU 5318 C LEU B 390 13858 28618 25294 2325 -2210 -4403 C
ATOM 5319 O LEU B 390 68.251 31.946 69.469 1.00180.17 O
ANISOU 5319 O LEU B 390 14605 28569 25283 2464 -2494 -4244 O
ATOM 5320 CB LEU B 390 68.935 31.741 66.259 1.00179.08 C
ANISOU 5320 CB LEU B 390 14260 28403 25378 2281 -1297 -4348 C
ATOM 5321 CG LEU B 390 69.114 30.785 65.077 1.00178.44 C
ANISOU 5321 CG LEU B 390 14243 28272 25285 2649 -892 -4372 C
ATOM 5322 CD1 LEU B 390 68.354 31.301 63.864 1.00165.46 C
ANISOU 5322 CD1 LEU B 390 13030 26371 23464 2285 -453 -4314 C
ATOM 5323 CD2 LEU B 390 70.593 30.573 64.758 1.00177.42 C
ANISOU 5323 CD2 LEU B 390 13320 28662 25429 2866 -720 -4540 C
ATOM 5324 N CYS B 391 69.946 33.292 68.823 1.00176.12 N
ANISOU 5324 N CYS B 391 13026 28660 25232 1868 -2223 -4600 N
ATOM 5325 CA CYS B 391 69.726 34.341 69.808 1.00176.79 C
ANISOU 5325 CA CYS B 391 13097 28781 25294 1471 -2583 -4702 C
ATOM 5326 C CYS B 391 69.060 35.548 69.157 1.00184.32 C
ANISOU 5326 C CYS B 391 14367 29399 26266 799 -2264 -4670 C
ATOM 5327 O CYS B 391 69.266 35.830 67.974 1.00193.39 O
ANISOU 5327 O CYS B 391 15430 30496 27554 551 -1765 -4636 O
ATOM 5328 CB CYS B 391 71.047 34.771 70.457 1.00185.82 C
ANISOU 5328 CB CYS B 391 13374 30501 26729 1396 -2866 -4999 C
ATOM 5329 SG CYS B 391 71.826 33.486 71.458 1.00199.04 S
ANISOU 5329 SG CYS B 391 14648 32642 28335 2226 -3344 -5023 S
ATOM 5330 N PHE B 392 68.264 36.269 69.946 1.00181.10 N
ANISOU 5330 N PHE B 392 14331 28778 25699 540 -2541 -4666 N
ATOM 5331 CA PHE B 392 67.513 37.406 69.437 1.00178.39 C
ANISOU 5331 CA PHE B 392 14362 28067 25352 -41 -2271 -4605 C
ATOM 5332 C PHE B 392 67.457 38.499 70.491 1.00177.41 C
ANISOU 5332 C PHE B 392 14162 27965 25280 -408 -2641 -4810 C
ATOM 5333 O PHE B 392 67.383 38.215 71.690 1.00173.09 O
ANISOU 5333 O PHE B 392 13628 27582 24556 -121 -3142 -4898 O
ATOM 5334 CB PHE B 392 66.096 36.990 69.018 1.00150.96 C
ANISOU 5334 CB PHE B 392 11714 24118 21526 92 -2116 -4309 C
ATOM 5335 CG PHE B 392 66.063 36.137 67.783 1.00151.13 C
ANISOU 5335 CG PHE B 392 11855 24058 21508 335 -1696 -4170 C
ATOM 5336 CD1 PHE B 392 66.226 36.706 66.531 1.00152.83 C
ANISOU 5336 CD1 PHE B 392 12007 24230 21831 0 -1182 -4134 C
ATOM 5337 CD2 PHE B 392 65.895 34.766 67.875 1.00151.03 C
ANISOU 5337 CD2 PHE B 392 12017 24015 21353 917 -1804 -4081 C
ATOM 5338 CE1 PHE B 392 66.208 35.926 65.392 1.00158.48 C
ANISOU 5338 CE1 PHE B 392 12836 24921 22458 258 -808 -4050 C
ATOM 5339 CE2 PHE B 392 65.878 33.980 66.739 1.00161.29 C
ANISOU 5339 CE2 PHE B 392 13432 25229 22624 1148 -1436 -4023 C
ATOM 5340 CZ PHE B 392 66.034 34.561 65.496 1.00163.35 C
ANISOU 5340 CZ PHE B 392 13629 25497 22938 827 -949 -4027 C
ATOM 5341 N THR B 393 67.501 39.750 70.029 1.00180.51 N
ANISOU 5341 N THR B 393 14481 28190 25913 -1026 -2379 -4887 N
ATOM 5342 CA THR B 393 67.438 40.890 70.937 1.00167.44 C
ANISOU 5342 CA THR B 393 12774 26484 24362 -1430 -2691 -5133 C
ATOM 5343 C THR B 393 66.139 40.887 71.732 1.00165.61 C
ANISOU 5343 C THR B 393 13261 25959 23703 -1265 -2982 -5014 C
ATOM 5344 O THR B 393 66.145 40.768 72.962 1.00161.78 O
ANISOU 5344 O THR B 393 12738 25683 23049 -1037 -3495 -5184 O
ATOM 5345 CB THR B 393 67.586 42.191 70.148 1.00169.95 C
ANISOU 5345 CB THR B 393 12983 26546 25043 -2116 -2262 -5162 C
ATOM 5346 OG1 THR B 393 68.710 42.094 69.263 1.00175.99 O
ANISOU 5346 OG1 THR B 393 13115 27577 26176 -2234 -1891 -5185 O
ATOM 5347 CG2 THR B 393 67.770 43.365 71.089 1.00162.57 C
ANISOU 5347 CG2 THR B 393 11861 25575 24334 -2557 -2597 -5514 C
ATOM 5348 N ASN B 394 65.010 41.021 71.041 1.00161.08 N
ANISOU 5348 N ASN B 394 13333 24939 22932 -1355 -2655 -4716 N
ATOM 5349 CA ASN B 394 63.705 41.041 71.682 1.00143.18 C
ANISOU 5349 CA ASN B 394 11743 22381 20278 -1216 -2861 -4564 C
ATOM 5350 C ASN B 394 62.744 40.124 70.944 1.00143.81 C
ANISOU 5350 C ASN B 394 12358 22207 20075 -908 -2604 -4194 C
ATOM 5351 O ASN B 394 62.703 40.110 69.710 1.00141.52 O
ANISOU 5351 O ASN B 394 12128 21779 19865 -1042 -2153 -4048 O
ATOM 5352 CB ASN B 394 63.126 42.459 71.737 1.00137.32 C
ANISOU 5352 CB ASN B 394 11275 21291 19608 -1737 -2774 -4629 C
ATOM 5353 CG ASN B 394 63.813 43.327 72.769 1.00157.90 C
ANISOU 5353 CG ASN B 394 13478 24088 22429 -1997 -3157 -5054 C
ATOM 5354 OD1 ASN B 394 63.666 43.114 73.972 1.00167.36 O
ANISOU 5354 OD1 ASN B 394 14729 25480 23380 -1716 -3644 -5207 O
ATOM 5355 ND2 ASN B 394 64.569 44.315 72.303 1.00169.33 N
ANISOU 5355 ND2 ASN B 394 14513 25484 24339 -2534 -2935 -5254 N
ATOM 5356 N VAL B 395 61.976 39.361 71.714 1.00145.87 N
ANISOU 5356 N VAL B 395 12997 22422 20006 -491 -2894 -4049 N
ATOM 5357 CA VAL B 395 60.886 38.543 71.199 1.00130.56 C
ANISOU 5357 CA VAL B 395 11606 20188 17814 -235 -2718 -3723 C
ATOM 5358 C VAL B 395 59.583 39.169 71.672 1.00130.75 C
ANISOU 5358 C VAL B 395 12197 19901 17581 -366 -2798 -3585 C
ATOM 5359 O VAL B 395 59.372 39.342 72.879 1.00140.87 O
ANISOU 5359 O VAL B 395 13548 21273 18702 -244 -3168 -3650 O
ATOM 5360 CB VAL B 395 60.999 37.084 71.666 1.00133.01 C
ANISOU 5360 CB VAL B 395 11893 20639 18007 357 -2932 -3613 C
ATOM 5361 CG1 VAL B 395 59.784 36.287 71.214 1.00111.74 C
ANISOU 5361 CG1 VAL B 395 9774 17580 15104 563 -2774 -3307 C
ATOM 5362 CG2 VAL B 395 62.280 36.457 71.139 1.00145.21 C
ANISOU 5362 CG2 VAL B 395 12878 22488 19809 528 -2825 -3750 C
ATOM 5363 N TYR B 396 58.719 39.522 70.727 1.00119.65 N
ANISOU 5363 N TYR B 396 11185 18167 16110 -584 -2453 -3399 N
ATOM 5364 CA TYR B 396 57.410 40.074 71.033 1.00107.80 C
ANISOU 5364 CA TYR B 396 10225 16368 14368 -680 -2480 -3235 C
ATOM 5365 C TYR B 396 56.346 39.014 70.782 1.00107.80 C
ANISOU 5365 C TYR B 396 10650 16179 14131 -357 -2432 -2944 C
ATOM 5366 O TYR B 396 56.481 38.176 69.887 1.00121.48 O
ANISOU 5366 O TYR B 396 12347 17897 15914 -217 -2229 -2878 O
ATOM 5367 CB TYR B 396 57.123 41.323 70.192 1.00103.41 C
ANISOU 5367 CB TYR B 396 9812 15572 13909 -1150 -2138 -3214 C
ATOM 5368 CG TYR B 396 58.112 42.451 70.406 1.00126.03 C
ANISOU 5368 CG TYR B 396 12269 18530 17088 -1541 -2147 -3497 C
ATOM 5369 CD1 TYR B 396 58.019 43.288 71.513 1.00123.00 C
ANISOU 5369 CD1 TYR B 396 11916 18121 16699 -1675 -2449 -3697 C
ATOM 5370 CD2 TYR B 396 59.135 42.683 69.496 1.00131.34 C
ANISOU 5370 CD2 TYR B 396 12515 19312 18076 -1782 -1840 -3581 C
ATOM 5371 CE1 TYR B 396 58.923 44.320 71.708 1.00116.71 C
ANISOU 5371 CE1 TYR B 396 10729 17370 16247 -2070 -2474 -4008 C
ATOM 5372 CE2 TYR B 396 60.041 43.712 69.682 1.00134.07 C
ANISOU 5372 CE2 TYR B 396 12449 19712 18781 -2186 -1829 -3838 C
ATOM 5373 CZ TYR B 396 59.931 44.527 70.788 1.00130.47 C
ANISOU 5373 CZ TYR B 396 12025 19192 18355 -2345 -2159 -4068 C
ATOM 5374 OH TYR B 396 60.833 45.550 70.974 1.00131.63 O
ANISOU 5374 OH TYR B 396 11745 19355 18913 -2782 -2165 -4374 O
ATOM 5375 N ALA B 397 55.287 39.051 71.589 1.00116.87 N
ANISOU 5375 N ALA B 397 12185 17186 15034 -240 -2619 -2789 N
ATOM 5376 CA ALA B 397 54.205 38.070 71.519 1.00113.17 C
ANISOU 5376 CA ALA B 397 12096 16522 14382 39 -2603 -2506 C
ATOM 5377 C ALA B 397 52.877 38.817 71.429 1.00112.19 C
ANISOU 5377 C ALA B 397 12427 16134 14065 -148 -2502 -2334 C
ATOM 5378 O ALA B 397 52.389 39.356 72.427 1.00115.68 O
ANISOU 5378 O ALA B 397 13033 16573 14348 -130 -2697 -2308 O
ATOM 5379 CB ALA B 397 54.233 37.132 72.721 1.00111.35 C
ANISOU 5379 CB ALA B 397 11841 16421 14046 471 -2929 -2415 C
ATOM 5380 N ASP B 398 52.297 38.841 70.234 1.00110.96 N
ANISOU 5380 N ASP B 398 12469 15792 13899 -291 -2204 -2224 N
ATOM 5381 CA ASP B 398 51.026 39.505 69.981 1.00108.93 C
ANISOU 5381 CA ASP B 398 12618 15309 13462 -441 -2086 -2042 C
ATOM 5382 C ASP B 398 49.902 38.482 70.072 1.00 97.78 C
ANISOU 5382 C ASP B 398 11489 13753 11908 -188 -2141 -1806 C
ATOM 5383 O ASP B 398 49.998 37.400 69.486 1.00 95.74 O
ANISOU 5383 O ASP B 398 11178 13468 11731 -33 -2083 -1794 O
ATOM 5384 CB ASP B 398 51.032 40.172 68.606 1.00103.44 C
ANISOU 5384 CB ASP B 398 11958 14538 12808 -721 -1734 -2043 C
ATOM 5385 CG ASP B 398 52.123 41.216 68.473 1.00111.68 C
ANISOU 5385 CG ASP B 398 12706 15671 14055 -1016 -1622 -2236 C
ATOM 5386 OD1 ASP B 398 52.541 41.776 69.507 1.00107.50 O
ANISOU 5386 OD1 ASP B 398 12046 15200 13598 -1079 -1841 -2385 O
ATOM 5387 OD2 ASP B 398 52.562 41.479 67.333 1.00113.14 O1-
ANISOU 5387 OD2 ASP B 398 12780 15877 14333 -1184 -1310 -2244 O1-
ATOM 5388 N SER B 399 48.840 38.824 70.800 1.00 97.11 N
ANISOU 5388 N SER B 399 11692 13565 11639 -152 -2242 -1631 N
ATOM 5389 CA SER B 399 47.748 37.889 71.043 1.00 99.81 C
ANISOU 5389 CA SER B 399 12263 13772 11889 66 -2296 -1381 C
ATOM 5390 C SER B 399 46.408 38.581 70.850 1.00105.74 C
ANISOU 5390 C SER B 399 13342 14374 12460 -59 -2194 -1199 C
ATOM 5391 O SER B 399 46.194 39.686 71.356 1.00108.42 O
ANISOU 5391 O SER B 399 13788 14725 12681 -164 -2217 -1207 O
ATOM 5392 CB SER B 399 47.836 37.292 72.454 1.00110.73 C
ANISOU 5392 CB SER B 399 13608 15248 13218 373 -2556 -1280 C
ATOM 5393 OG SER B 399 47.803 38.304 73.445 1.00122.83 O
ANISOU 5393 OG SER B 399 15193 16896 14580 344 -2697 -1325 O
ATOM 5394 N PHE B 400 45.512 37.918 70.125 1.00100.90 N
ANISOU 5394 N PHE B 400 12874 13623 11841 -36 -2094 -1059 N
ATOM 5395 CA PHE B 400 44.165 38.415 69.873 1.00 90.84 C
ANISOU 5395 CA PHE B 400 11870 12241 10404 -116 -2011 -870 C
ATOM 5396 C PHE B 400 43.283 37.224 69.518 1.00 83.40 C
ANISOU 5396 C PHE B 400 10996 11169 9525 -10 -2015 -733 C
ATOM 5397 O PHE B 400 43.750 36.084 69.442 1.00 87.10 O
ANISOU 5397 O PHE B 400 11332 11587 10174 117 -2063 -794 O
ATOM 5398 CB PHE B 400 44.161 39.471 68.764 1.00 97.97 C
ANISOU 5398 CB PHE B 400 12837 13151 11235 -357 -1798 -943 C
ATOM 5399 CG PHE B 400 44.967 39.087 67.554 1.00 94.19 C
ANISOU 5399 CG PHE B 400 12192 12734 10862 -429 -1650 -1120 C
ATOM 5400 CD1 PHE B 400 44.427 38.271 66.572 1.00 94.98 C
ANISOU 5400 CD1 PHE B 400 12342 12800 10944 -384 -1583 -1119 C
ATOM 5401 CD2 PHE B 400 46.264 39.546 67.396 1.00 97.18 C
ANISOU 5401 CD2 PHE B 400 12345 13220 11358 -538 -1574 -1309 C
ATOM 5402 CE1 PHE B 400 45.166 37.918 65.458 1.00 99.11 C
ANISOU 5402 CE1 PHE B 400 12726 13414 11516 -407 -1438 -1306 C
ATOM 5403 CE2 PHE B 400 47.008 39.197 66.284 1.00104.90 C
ANISOU 5403 CE2 PHE B 400 13157 14288 12412 -575 -1401 -1453 C
ATOM 5404 CZ PHE B 400 46.459 38.382 65.314 1.00108.26 C
ANISOU 5404 CZ PHE B 400 13668 14697 12770 -490 -1329 -1452 C
ATOM 5405 N VAL B 401 41.999 37.497 69.296 1.00 81.49 N
ANISOU 5405 N VAL B 401 10947 10858 9160 -62 -1964 -558 N
ATOM 5406 CA VAL B 401 41.033 36.476 68.907 1.00 85.77 C
ANISOU 5406 CA VAL B 401 11530 11268 9792 -20 -1973 -452 C
ATOM 5407 C VAL B 401 40.320 36.926 67.640 1.00 90.10 C
ANISOU 5407 C VAL B 401 12169 11850 10214 -173 -1854 -498 C
ATOM 5408 O VAL B 401 39.890 38.081 67.537 1.00 86.69 O
ANISOU 5408 O VAL B 401 11864 11492 9581 -251 -1777 -412 O
ATOM 5409 CB VAL B 401 40.014 36.184 70.026 1.00 74.82 C
ANISOU 5409 CB VAL B 401 10234 9805 8391 108 -2054 -148 C
ATOM 5410 CG1 VAL B 401 38.755 35.551 69.458 1.00 80.42 C
ANISOU 5410 CG1 VAL B 401 10983 10390 9182 53 -2027 -36 C
ATOM 5411 CG2 VAL B 401 40.625 35.272 71.065 1.00100.67 C
ANISOU 5411 CG2 VAL B 401 13407 13030 11813 322 -2164 -70 C
ATOM 5412 N ILE B 402 40.203 36.012 66.679 1.00 84.33 N
ANISOU 5412 N ILE B 402 11381 11068 9594 -189 -1844 -643 N
ATOM 5413 CA ILE B 402 39.478 36.216 65.436 1.00 82.87 C
ANISOU 5413 CA ILE B 402 11262 10963 9264 -285 -1775 -714 C
ATOM 5414 C ILE B 402 38.673 34.952 65.151 1.00 91.96 C
ANISOU 5414 C ILE B 402 12370 11967 10605 -268 -1879 -764 C
ATOM 5415 O ILE B 402 38.670 34.005 65.941 1.00 92.77 O
ANISOU 5415 O ILE B 402 12412 11868 10970 -191 -1965 -692 O
ATOM 5416 CB ILE B 402 40.421 36.546 64.261 1.00 80.24 C
ANISOU 5416 CB ILE B 402 10880 10784 8823 -336 -1631 -954 C
ATOM 5417 CG1 ILE B 402 41.559 35.522 64.199 1.00 90.93 C
ANISOU 5417 CG1 ILE B 402 12063 12081 10407 -252 -1651 -1187 C
ATOM 5418 CG2 ILE B 402 40.966 37.959 64.392 1.00 80.68 C
ANISOU 5418 CG2 ILE B 402 10987 10949 8719 -416 -1492 -871 C
ATOM 5419 CD1 ILE B 402 42.565 35.786 63.102 1.00 96.35 C
ANISOU 5419 CD1 ILE B 402 12666 12949 10996 -275 -1478 -1412 C
ATOM 5420 N ARG B 403 37.986 34.935 64.013 1.00 96.10 N
ANISOU 5420 N ARG B 403 12919 12589 11006 -336 -1872 -889 N
ATOM 5421 CA ARG B 403 37.238 33.745 63.637 1.00 90.24 C
ANISOU 5421 CA ARG B 403 12109 11700 10479 -360 -1992 -1018 C
ATOM 5422 C ARG B 403 38.066 32.861 62.709 1.00 85.24 C
ANISOU 5422 C ARG B 403 11402 11032 9955 -322 -1990 -1405 C
ATOM 5423 O ARG B 403 39.038 33.302 62.090 1.00 85.32 O
ANISOU 5423 O ARG B 403 11409 11220 9787 -283 -1872 -1560 O
ATOM 5424 CB ARG B 403 35.913 34.109 62.968 1.00 98.48 C
ANISOU 5424 CB ARG B 403 13183 12896 11337 -438 -2042 -983 C
ATOM 5425 CG ARG B 403 35.989 35.328 62.087 1.00102.55 C
ANISOU 5425 CG ARG B 403 13801 13727 11438 -428 -1929 -990 C
ATOM 5426 CD ARG B 403 34.669 35.599 61.394 1.00108.15 C
ANISOU 5426 CD ARG B 403 14517 14628 11947 -453 -2008 -958 C
ATOM 5427 NE ARG B 403 34.421 34.617 60.347 1.00105.50 N
ANISOU 5427 NE ARG B 403 14084 14338 11661 -477 -2137 -1324 N
ATOM 5428 CZ ARG B 403 33.457 34.705 59.442 1.00108.14 C
ANISOU 5428 CZ ARG B 403 14386 14916 11785 -480 -2244 -1429 C
ATOM 5429 NH1 ARG B 403 32.614 35.725 59.426 1.00118.24 N
ANISOU 5429 NH1 ARG B 403 15720 16414 12790 -441 -2223 -1156 N
ATOM 5430 NH2 ARG B 403 33.340 33.749 58.526 1.00112.65 N
ANISOU 5430 NH2 ARG B 403 14865 15522 12414 -500 -2388 -1839 N
ATOM 5431 N GLY B 404 37.648 31.596 62.610 1.00 87.17 N
ANISOU 5431 N GLY B 404 11576 11028 10516 -334 -2106 -1561 N
ATOM 5432 CA GLY B 404 38.455 30.599 61.923 1.00 94.46 C
ANISOU 5432 CA GLY B 404 12439 11839 11614 -258 -2110 -1942 C
ATOM 5433 C GLY B 404 38.730 30.934 60.469 1.00102.33 C
ANISOU 5433 C GLY B 404 13458 13149 12275 -241 -2053 -2279 C
ATOM 5434 O GLY B 404 39.826 30.679 59.963 1.00104.76 O
ANISOU 5434 O GLY B 404 13729 13516 12561 -128 -1958 -2522 O
ATOM 5435 N ASP B 405 37.741 31.501 59.773 1.00108.69 N
ANISOU 5435 N ASP B 405 14312 14190 12793 -321 -2100 -2283 N
ATOM 5436 CA ASP B 405 37.944 31.873 58.376 1.00 96.76 C
ANISOU 5436 CA ASP B 405 12839 13038 10888 -259 -2036 -2558 C
ATOM 5437 C ASP B 405 38.955 33.001 58.212 1.00100.09 C
ANISOU 5437 C ASP B 405 13311 13716 11004 -195 -1794 -2403 C
ATOM 5438 O ASP B 405 39.466 33.199 57.105 1.00 95.64 O
ANISOU 5438 O ASP B 405 12763 13432 10145 -103 -1670 -2612 O
ATOM 5439 CB ASP B 405 36.618 32.281 57.727 1.00114.32 C
ANISOU 5439 CB ASP B 405 15094 15502 12843 -319 -2158 -2551 C
ATOM 5440 CG ASP B 405 35.769 31.088 57.325 1.00128.86 C
ANISOU 5440 CG ASP B 405 16839 17190 14932 -389 -2400 -2900 C
ATOM 5441 OD1 ASP B 405 36.339 30.003 57.091 1.00148.42 O
ANISOU 5441 OD1 ASP B 405 19273 19444 17676 -350 -2438 -3257 O
ATOM 5442 OD2 ASP B 405 34.533 31.241 57.225 1.00117.90 O1-
ANISOU 5442 OD2 ASP B 405 15406 15899 13492 -482 -2552 -2836 O1-
ATOM 5443 N GLU B 406 39.261 33.737 59.279 1.00105.07 N
ANISOU 5443 N GLU B 406 13958 14260 11704 -241 -1715 -2056 N
ATOM 5444 CA GLU B 406 40.103 34.922 59.184 1.00110.43 C
ANISOU 5444 CA GLU B 406 14669 15136 12151 -239 -1490 -1898 C
ATOM 5445 C GLU B 406 41.557 34.672 59.559 1.00106.54 C
ANISOU 5445 C GLU B 406 14048 14573 11859 -191 -1383 -1989 C
ATOM 5446 O GLU B 406 42.368 35.599 59.469 1.00 98.32 O
ANISOU 5446 O GLU B 406 12984 13681 10694 -222 -1186 -1891 O
ATOM 5447 CB GLU B 406 39.540 36.044 60.063 1.00102.62 C
ANISOU 5447 CB GLU B 406 13779 14119 11095 -323 -1474 -1509 C
ATOM 5448 CG GLU B 406 38.247 36.649 59.549 1.00105.87 C
ANISOU 5448 CG GLU B 406 14307 14694 11224 -334 -1511 -1368 C
ATOM 5449 CD GLU B 406 37.673 37.684 60.497 1.00114.80 C
ANISOU 5449 CD GLU B 406 15539 15758 12320 -379 -1492 -1000 C
ATOM 5450 OE1 GLU B 406 38.091 37.711 61.674 1.00107.88 O
ANISOU 5450 OE1 GLU B 406 14639 14686 11664 -407 -1511 -888 O
ATOM 5451 OE2 GLU B 406 36.797 38.462 60.067 1.00125.74 O1-
ANISOU 5451 OE2 GLU B 406 17029 17306 13440 -354 -1464 -834 O1-
ATOM 5452 N VAL B 407 41.913 33.452 59.973 1.00103.91 N
ANISOU 5452 N VAL B 407 13614 14010 11857 -113 -1500 -2166 N
ATOM 5453 CA VAL B 407 43.290 33.182 60.381 1.00103.71 C
ANISOU 5453 CA VAL B 407 13434 13946 12026 -26 -1420 -2242 C
ATOM 5454 C VAL B 407 44.246 33.329 59.203 1.00107.59 C
ANISOU 5454 C VAL B 407 13845 14709 12327 47 -1204 -2481 C
ATOM 5455 O VAL B 407 45.418 33.685 59.382 1.00114.24 O
ANISOU 5455 O VAL B 407 14534 15650 13222 66 -1057 -2469 O
ATOM 5456 CB VAL B 407 43.388 31.784 61.026 1.00 98.36 C
ANISOU 5456 CB VAL B 407 12686 12943 11742 94 -1581 -2349 C
ATOM 5457 CG1 VAL B 407 44.822 31.472 61.437 1.00104.45 C
ANISOU 5457 CG1 VAL B 407 13273 13714 12700 237 -1514 -2424 C
ATOM 5458 CG2 VAL B 407 42.460 31.690 62.226 1.00 98.14 C
ANISOU 5458 CG2 VAL B 407 12730 12678 11883 35 -1742 -2044 C
ATOM 5459 N ARG B 408 43.762 33.083 57.982 1.00107.94 N
ANISOU 5459 N ARG B 408 13969 14912 12131 96 -1177 -2703 N
ATOM 5460 CA ARG B 408 44.611 33.200 56.800 1.00107.39 C
ANISOU 5460 CA ARG B 408 13838 15149 11817 209 -943 -2918 C
ATOM 5461 C ARG B 408 45.105 34.623 56.575 1.00102.90 C
ANISOU 5461 C ARG B 408 13260 14839 10997 114 -672 -2646 C
ATOM 5462 O ARG B 408 46.112 34.816 55.886 1.00105.27 O
ANISOU 5462 O ARG B 408 13441 15370 11185 188 -415 -2735 O
ATOM 5463 CB ARG B 408 43.855 32.705 55.563 1.00113.90 C
ANISOU 5463 CB ARG B 408 14776 16138 12364 306 -1003 -3216 C
ATOM 5464 CG ARG B 408 42.616 33.518 55.205 1.00129.25 C
ANISOU 5464 CG ARG B 408 16886 18248 13975 212 -1062 -3019 C
ATOM 5465 CD ARG B 408 42.190 33.259 53.765 1.00141.36 C
ANISOU 5465 CD ARG B 408 18494 20113 15103 358 -1065 -3331 C
ATOM 5466 NE ARG B 408 41.225 34.240 53.281 1.00152.88 N
ANISOU 5466 NE ARG B 408 20090 21843 16154 330 -1060 -3094 N
ATOM 5467 CZ ARG B 408 41.545 35.410 52.744 1.00154.43 C
ANISOU 5467 CZ ARG B 408 20352 22345 15980 371 -778 -2817 C
ATOM 5468 NH1 ARG B 408 42.806 35.785 52.603 1.00146.37 N
ANISOU 5468 NH1 ARG B 408 19248 21410 14957 402 -466 -2746 N
ATOM 5469 NH2 ARG B 408 40.574 36.222 52.335 1.00154.31 N
ANISOU 5469 NH2 ARG B 408 20473 22548 15610 387 -797 -2587 N
ATOM 5470 N GLN B 409 44.425 35.622 57.140 1.00 92.11 N
ANISOU 5470 N GLN B 409 12012 13420 9565 -44 -699 -2311 N
ATOM 5471 CA GLN B 409 44.847 37.010 57.006 1.00 94.89 C
ANISOU 5471 CA GLN B 409 12376 13924 9753 -158 -436 -2038 C
ATOM 5472 C GLN B 409 46.018 37.363 57.914 1.00112.31 C
ANISOU 5472 C GLN B 409 14381 16027 12265 -260 -356 -1969 C
ATOM 5473 O GLN B 409 46.639 38.413 57.714 1.00119.80 O
ANISOU 5473 O GLN B 409 15275 17081 13161 -376 -99 -1809 O
ATOM 5474 CB GLN B 409 43.673 37.945 57.292 1.00105.16 C
ANISOU 5474 CB GLN B 409 13888 15173 10894 -259 -497 -1731 C
ATOM 5475 CG GLN B 409 42.487 37.713 56.380 1.00109.95 C
ANISOU 5475 CG GLN B 409 14654 15946 11177 -156 -593 -1787 C
ATOM 5476 CD GLN B 409 41.434 38.790 56.506 1.00 91.07 C
ANISOU 5476 CD GLN B 409 12449 13572 8583 -211 -593 -1450 C
ATOM 5477 OE1 GLN B 409 41.730 39.925 56.880 1.00 90.48 O
ANISOU 5477 OE1 GLN B 409 12424 13437 8517 -310 -414 -1172 O
ATOM 5478 NE2 GLN B 409 40.194 38.441 56.192 1.00 94.47 N
ANISOU 5478 NE2 GLN B 409 12967 14075 8852 -145 -799 -1490 N
ATOM 5479 N ILE B 410 46.330 36.523 58.897 1.00100.42 N
ANISOU 5479 N ILE B 410 12752 14319 11083 -217 -570 -2079 N
ATOM 5480 CA ILE B 410 47.528 36.701 59.701 1.00 87.31 C
ANISOU 5480 CA ILE B 410 10849 12632 9693 -264 -538 -2079 C
ATOM 5481 C ILE B 410 48.694 36.055 58.966 1.00100.43 C
ANISOU 5481 C ILE B 410 12272 14473 11413 -122 -368 -2334 C
ATOM 5482 O ILE B 410 49.153 34.969 59.340 1.00103.42 O
ANISOU 5482 O ILE B 410 12514 14763 12019 46 -506 -2522 O
ATOM 5483 CB ILE B 410 47.349 36.111 61.113 1.00 90.42 C
ANISOU 5483 CB ILE B 410 11218 12782 10356 -220 -840 -2044 C
ATOM 5484 CG1 ILE B 410 45.993 36.520 61.680 1.00 82.95 C
ANISOU 5484 CG1 ILE B 410 10527 11683 9309 -300 -994 -1815 C
ATOM 5485 CG2 ILE B 410 48.462 36.591 62.020 1.00105.88 C
ANISOU 5485 CG2 ILE B 410 12936 14772 12521 -286 -844 -2020 C
ATOM 5486 CD1 ILE B 410 45.805 38.010 61.777 1.00 84.05 C
ANISOU 5486 CD1 ILE B 410 10767 11870 9298 -487 -864 -1597 C
ATOM 5487 N ALA B 411 49.159 36.714 57.911 1.00107.17 N
ANISOU 5487 N ALA B 411 13080 15581 12057 -161 -46 -2315 N
ATOM 5488 CA ALA B 411 50.208 36.225 57.025 1.00114.72 C
ANISOU 5488 CA ALA B 411 13818 16777 12991 -6 188 -2534 C
ATOM 5489 C ALA B 411 50.704 37.390 56.176 1.00121.00 C
ANISOU 5489 C ALA B 411 14557 17829 13587 -132 590 -2351 C
ATOM 5490 O ALA B 411 49.955 38.349 55.947 1.00117.57 O
ANISOU 5490 O ALA B 411 14347 17384 12940 -266 673 -2095 O
ATOM 5491 CB ALA B 411 49.695 35.089 56.134 1.00132.37 C
ANISOU 5491 CB ALA B 411 16189 19064 15041 244 118 -2819 C
ATOM 5492 N PRO B 412 51.951 37.357 55.709 1.00122.63 N
ANISOU 5492 N PRO B 412 14460 18260 13873 -83 870 -2442 N
ATOM 5493 CA PRO B 412 52.456 38.463 54.888 1.00122.06 C
ANISOU 5493 CA PRO B 412 14313 18417 13646 -213 1311 -2217 C
ATOM 5494 C PRO B 412 51.676 38.597 53.589 1.00134.45 C
ANISOU 5494 C PRO B 412 16174 20207 14704 -62 1495 -2147 C
ATOM 5495 O PRO B 412 51.332 37.604 52.944 1.00128.41 O
ANISOU 5495 O PRO B 412 15511 19571 13709 208 1396 -2419 O
ATOM 5496 CB PRO B 412 53.914 38.070 54.629 1.00126.97 C
ANISOU 5496 CB PRO B 412 14512 19267 14462 -123 1546 -2386 C
ATOM 5497 CG PRO B 412 54.259 37.176 55.784 1.00135.17 C
ANISOU 5497 CG PRO B 412 15372 20115 15872 -54 1177 -2609 C
ATOM 5498 CD PRO B 412 53.010 36.385 56.027 1.00129.22 C
ANISOU 5498 CD PRO B 412 14972 19134 14993 85 814 -2709 C
ATOM 5499 N GLY B 413 51.386 39.841 53.220 1.00137.69 N
ANISOU 5499 N GLY B 413 16721 20653 14941 -224 1753 -1788 N
ATOM 5500 CA GLY B 413 50.765 40.123 51.936 1.00132.60 C
ANISOU 5500 CA GLY B 413 16326 20290 13765 -49 1978 -1655 C
ATOM 5501 C GLY B 413 49.422 39.460 51.721 1.00125.01 C
ANISOU 5501 C GLY B 413 15677 19324 12496 136 1625 -1816 C
ATOM 5502 O GLY B 413 49.167 38.915 50.640 1.00144.95 O
ANISOU 5502 O GLY B 413 18301 22164 14610 408 1678 -1998 O
ATOM 5503 N GLN B 414 48.559 39.481 52.732 1.00102.48 N
ANISOU 5503 N GLN B 414 12963 16142 9834 0 1262 -1775 N
ATOM 5504 CA GLN B 414 47.193 39.001 52.611 1.00 97.46 C
ANISOU 5504 CA GLN B 414 12589 15480 8963 117 935 -1873 C
ATOM 5505 C GLN B 414 46.254 40.153 52.934 1.00104.11 C
ANISOU 5505 C GLN B 414 13657 16193 9710 -27 921 -1482 C
ATOM 5506 O GLN B 414 46.552 40.979 53.800 1.00103.64 O
ANISOU 5506 O GLN B 414 13554 15885 9942 -255 981 -1251 O
ATOM 5507 CB GLN B 414 46.937 37.810 53.542 1.00 98.12 C
ANISOU 5507 CB GLN B 414 12616 15280 9386 125 520 -2178 C
ATOM 5508 CG GLN B 414 47.828 36.609 53.251 1.00101.78 C
ANISOU 5508 CG GLN B 414 12877 15818 9976 309 523 -2574 C
ATOM 5509 CD GLN B 414 47.109 35.490 52.524 1.00122.91 C
ANISOU 5509 CD GLN B 414 15682 18576 12442 533 313 -2949 C
ATOM 5510 OE1 GLN B 414 45.999 35.668 52.022 1.00125.75 O
ANISOU 5510 OE1 GLN B 414 16253 19041 12485 563 197 -2919 O
ATOM 5511 NE2 GLN B 414 47.742 34.323 52.467 1.00135.42 N
ANISOU 5511 NE2 GLN B 414 17125 20107 14220 700 251 -3326 N
ATOM 5512 N THR B 415 45.135 40.223 52.216 1.00116.66 N
ANISOU 5512 N THR B 415 15477 17966 10884 124 837 -1431 N
ATOM 5513 CA THR B 415 44.185 41.318 52.347 1.00101.73 C
ANISOU 5513 CA THR B 415 13810 16007 8837 63 850 -1045 C
ATOM 5514 C THR B 415 42.920 40.842 53.056 1.00 93.81 C
ANISOU 5514 C THR B 415 12912 14820 7910 50 415 -1133 C
ATOM 5515 O THR B 415 42.664 39.641 53.179 1.00 98.43 O
ANISOU 5515 O THR B 415 13427 15377 8595 110 124 -1487 O
ATOM 5516 CB THR B 415 43.826 41.909 50.976 1.00103.52 C
ANISOU 5516 CB THR B 415 14202 16637 8493 284 1112 -838 C
ATOM 5517 OG1 THR B 415 43.482 40.858 50.064 1.00124.19 O
ANISOU 5517 OG1 THR B 415 16826 19598 10762 541 945 -1211 O
ATOM 5518 CG2 THR B 415 45.008 42.677 50.404 1.00112.12 C
ANISOU 5518 CG2 THR B 415 15201 17852 9548 255 1626 -594 C
ATOM 5519 N GLY B 416 42.135 41.799 53.524 1.00 88.33 N
ANISOU 5519 N GLY B 416 12382 13983 7198 -25 395 -797 N
ATOM 5520 CA GLY B 416 40.870 41.510 54.163 1.00 99.13 C
ANISOU 5520 CA GLY B 416 13837 15218 8611 -26 39 -807 C
ATOM 5521 C GLY B 416 40.523 42.598 55.158 1.00 97.29 C
ANISOU 5521 C GLY B 416 13716 14695 8555 -167 69 -462 C
ATOM 5522 O GLY B 416 41.102 43.676 55.155 1.00 97.61 O
ANISOU 5522 O GLY B 416 13809 14652 8628 -252 368 -204 O
ATOM 5523 N LYS B 417 39.549 42.293 56.018 1.00 97.70 N
ANISOU 5523 N LYS B 417 13799 14582 8741 -191 -234 -467 N
ATOM 5524 CA LYS B 417 39.192 43.235 57.077 1.00103.78 C
ANISOU 5524 CA LYS B 417 14677 15077 9678 -292 -231 -191 C
ATOM 5525 C LYS B 417 40.228 43.226 58.194 1.00102.61 C
ANISOU 5525 C LYS B 417 14407 14645 9937 -478 -224 -277 C
ATOM 5526 O LYS B 417 40.628 44.286 58.688 1.00101.33 O
ANISOU 5526 O LYS B 417 14307 14297 9897 -594 -59 -97 O
ATOM 5527 CB LYS B 417 37.808 42.906 57.630 1.00 92.34 C
ANISOU 5527 CB LYS B 417 13278 13592 8216 -230 -528 -150 C
ATOM 5528 CG LYS B 417 36.673 43.134 56.650 1.00 84.21 C
ANISOU 5528 CG LYS B 417 12350 12861 6784 -42 -562 -30 C
ATOM 5529 CD LYS B 417 36.404 44.617 56.449 1.00103.19 C
ANISOU 5529 CD LYS B 417 14964 15260 8985 36 -311 371 C
ATOM 5530 CE LYS B 417 35.417 44.854 55.314 1.00123.14 C
ANISOU 5530 CE LYS B 417 17578 18164 11047 284 -324 507 C
ATOM 5531 NZ LYS B 417 34.894 46.251 55.309 1.00124.92 N
ANISOU 5531 NZ LYS B 417 18020 18332 11112 406 -123 945 N
ATOM 5532 N ILE B 418 40.670 42.038 58.607 1.00 90.34 N
ANISOU 5532 N ILE B 418 12674 13049 8604 -496 -414 -562 N
ATOM 5533 CA ILE B 418 41.657 41.941 59.677 1.00 97.42 C
ANISOU 5533 CA ILE B 418 13425 13739 9853 -623 -448 -655 C
ATOM 5534 C ILE B 418 42.994 42.512 59.224 1.00 97.59 C
ANISOU 5534 C ILE B 418 13325 13812 9942 -727 -153 -676 C
ATOM 5535 O ILE B 418 43.577 43.376 59.888 1.00108.57 O
ANISOU 5535 O ILE B 418 14687 15037 11526 -883 -57 -591 O
ATOM 5536 CB ILE B 418 41.798 40.481 60.142 1.00 93.37 C
ANISOU 5536 CB ILE B 418 12754 13175 9548 -564 -701 -915 C
ATOM 5537 CG1 ILE B 418 40.441 39.931 60.581 1.00 82.99 C
ANISOU 5537 CG1 ILE B 418 11531 11786 8217 -497 -954 -857 C
ATOM 5538 CG2 ILE B 418 42.826 40.369 61.257 1.00 91.09 C
ANISOU 5538 CG2 ILE B 418 12302 12731 9577 -640 -758 -992 C
ATOM 5539 CD1 ILE B 418 39.765 40.771 61.643 1.00 93.70 C
ANISOU 5539 CD1 ILE B 418 13015 12994 9594 -534 -1009 -598 C
ATOM 5540 N ALA B 419 43.494 42.044 58.080 1.00 92.31 N
ANISOU 5540 N ALA B 419 12570 13380 9125 -644 2 -806 N
ATOM 5541 CA ALA B 419 44.827 42.431 57.640 1.00 96.61 C
ANISOU 5541 CA ALA B 419 12939 14006 9764 -734 307 -830 C
ATOM 5542 C ALA B 419 44.900 43.880 57.178 1.00100.54 C
ANISOU 5542 C ALA B 419 13562 14484 10156 -838 651 -504 C
ATOM 5543 O ALA B 419 45.992 44.456 57.169 1.00110.40 O
ANISOU 5543 O ALA B 419 14647 15688 11611 -1002 906 -469 O
ATOM 5544 CB ALA B 419 45.296 41.501 56.525 1.00101.00 C
ANISOU 5544 CB ALA B 419 13376 14849 10149 -568 401 -1058 C
ATOM 5545 N ASP B 420 43.777 44.484 56.794 1.00 99.47 N
ANISOU 5545 N ASP B 420 13695 14369 9732 -745 674 -255 N
ATOM 5546 CA ASP B 420 43.781 45.893 56.419 1.00106.56 C
ANISOU 5546 CA ASP B 420 14747 15181 10558 -816 1012 102 C
ATOM 5547 C ASP B 420 43.350 46.822 57.544 1.00104.14 C
ANISOU 5547 C ASP B 420 14582 14511 10477 -956 928 254 C
ATOM 5548 O ASP B 420 43.791 47.975 57.572 1.00112.06 O
ANISOU 5548 O ASP B 420 15636 15306 11635 -1113 1210 460 O
ATOM 5549 CB ASP B 420 42.874 46.142 55.205 1.00122.96 C
ANISOU 5549 CB ASP B 420 17046 17534 12141 -572 1141 334 C
ATOM 5550 CG ASP B 420 43.246 45.289 54.001 1.00123.73 C
ANISOU 5550 CG ASP B 420 17037 18038 11935 -390 1232 159 C
ATOM 5551 OD1 ASP B 420 44.449 45.030 53.796 1.00134.23 O
ANISOU 5551 OD1 ASP B 420 18148 19428 13425 -473 1425 24 O
ATOM 5552 OD2 ASP B 420 42.328 44.883 53.255 1.00103.22 O1-
ANISOU 5552 OD2 ASP B 420 14562 15724 8932 -151 1103 136 O1-
ATOM 5553 N TYR B 421 42.507 46.363 58.473 1.00 91.58 N
ANISOU 5553 N TYR B 421 13053 12822 8921 -901 569 156 N
ATOM 5554 CA TYR B 421 41.914 47.247 59.470 1.00 98.90 C
ANISOU 5554 CA TYR B 421 14155 13454 9970 -959 492 302 C
ATOM 5555 C TYR B 421 42.187 46.862 60.922 1.00 96.06 C
ANISOU 5555 C TYR B 421 13675 12912 9910 -1060 204 74 C
ATOM 5556 O TYR B 421 41.725 47.575 61.820 1.00 95.08 O
ANISOU 5556 O TYR B 421 13697 12564 9866 -1086 130 152 O
ATOM 5557 CB TYR B 421 40.390 47.333 59.281 1.00104.83 C
ANISOU 5557 CB TYR B 421 15136 14285 10407 -737 370 501 C
ATOM 5558 CG TYR B 421 39.902 47.977 57.998 1.00102.28 C
ANISOU 5558 CG TYR B 421 14988 14141 9731 -578 631 798 C
ATOM 5559 CD1 TYR B 421 40.728 48.788 57.231 1.00107.21 C
ANISOU 5559 CD1 TYR B 421 15634 14740 10359 -653 1028 981 C
ATOM 5560 CD2 TYR B 421 38.593 47.788 57.570 1.00111.70 C
ANISOU 5560 CD2 TYR B 421 16307 15546 10587 -337 486 920 C
ATOM 5561 CE1 TYR B 421 40.267 49.379 56.065 1.00116.30 C
ANISOU 5561 CE1 TYR B 421 16963 16080 11146 -455 1284 1307 C
ATOM 5562 CE2 TYR B 421 38.124 48.373 56.409 1.00123.89 C
ANISOU 5562 CE2 TYR B 421 18006 17309 11759 -138 697 1203 C
ATOM 5563 CZ TYR B 421 38.964 49.168 55.661 1.00120.70 C
ANISOU 5563 CZ TYR B 421 17656 16881 11323 -179 1102 1412 C
ATOM 5564 OH TYR B 421 38.497 49.751 54.505 1.00101.75 O
ANISOU 5564 OH TYR B 421 15426 14723 8513 67 1332 1745 O
ATOM 5565 N ASN B 422 42.904 45.770 61.194 1.00 94.62 N
ANISOU 5565 N ASN B 422 13245 12831 9874 -1080 41 -200 N
ATOM 5566 CA ASN B 422 43.067 45.353 62.586 1.00 98.00 C
ANISOU 5566 CA ASN B 422 13578 13134 10523 -1108 -248 -372 C
ATOM 5567 C ASN B 422 44.496 44.956 62.945 1.00 97.99 C
ANISOU 5567 C ASN B 422 13268 13159 10804 -1231 -270 -625 C
ATOM 5568 O ASN B 422 45.050 45.454 63.931 1.00 93.83 O
ANISOU 5568 O ASN B 422 12662 12495 10494 -1355 -352 -724 O
ATOM 5569 CB ASN B 422 42.118 44.198 62.907 1.00 92.13 C
ANISOU 5569 CB ASN B 422 12862 12472 9671 -921 -531 -405 C
ATOM 5570 CG ASN B 422 40.663 44.593 62.783 1.00 92.46 C
ANISOU 5570 CG ASN B 422 13150 12506 9475 -802 -558 -170 C
ATOM 5571 OD1 ASN B 422 40.033 44.997 63.760 1.00 84.48 O
ANISOU 5571 OD1 ASN B 422 12256 11362 8480 -766 -672 -74 O
ATOM 5572 ND2 ASN B 422 40.119 44.477 61.579 1.00 96.46 N
ANISOU 5572 ND2 ASN B 422 13722 13192 9735 -712 -457 -85 N
ATOM 5573 N TYR B 423 45.099 44.063 62.165 1.00 93.87 N
ANISOU 5573 N TYR B 423 12561 12833 10274 -1177 -211 -756 N
ATOM 5574 CA TYR B 423 46.431 43.553 62.479 1.00 90.04 C
ANISOU 5574 CA TYR B 423 11746 12415 10051 -1240 -243 -996 C
ATOM 5575 C TYR B 423 47.136 43.211 61.175 1.00 97.54 C
ANISOU 5575 C TYR B 423 12543 13577 10939 -1219 25 -1050 C
ATOM 5576 O TYR B 423 46.821 42.196 60.546 1.00105.08 O
ANISOU 5576 O TYR B 423 13513 14678 11734 -1032 -28 -1134 O
ATOM 5577 CB TYR B 423 46.350 42.332 63.393 1.00 92.62 C
ANISOU 5577 CB TYR B 423 11980 12750 10462 -1076 -585 -1152 C
ATOM 5578 CG TYR B 423 47.696 41.802 63.827 1.00 99.92 C
ANISOU 5578 CG TYR B 423 12557 13762 11646 -1085 -654 -1383 C
ATOM 5579 CD1 TYR B 423 48.376 42.361 64.900 1.00105.20 C
ANISOU 5579 CD1 TYR B 423 13073 14380 12518 -1202 -775 -1475 C
ATOM 5580 CD2 TYR B 423 48.286 40.735 63.161 1.00104.54 C
ANISOU 5580 CD2 TYR B 423 12953 14500 12265 -952 -612 -1536 C
ATOM 5581 CE1 TYR B 423 49.609 41.871 65.297 1.00109.95 C
ANISOU 5581 CE1 TYR B 423 13315 15114 13346 -1186 -864 -1691 C
ATOM 5582 CE2 TYR B 423 49.514 40.239 63.549 1.00107.42 C
ANISOU 5582 CE2 TYR B 423 12979 14968 12868 -918 -671 -1733 C
ATOM 5583 CZ TYR B 423 50.171 40.810 64.617 1.00106.80 C
ANISOU 5583 CZ TYR B 423 12724 14869 12984 -1035 -803 -1799 C
ATOM 5584 OH TYR B 423 51.396 40.320 65.007 1.00102.47 O
ANISOU 5584 OH TYR B 423 11799 14473 12662 -980 -888 -1999 O
ATOM 5585 N LYS B 424 48.089 44.046 60.778 1.00101.67 N
ANISOU 5585 N LYS B 424 12912 14116 11602 -1409 322 -1014 N
ATOM 5586 CA LYS B 424 48.807 43.875 59.521 1.00107.92 C
ANISOU 5586 CA LYS B 424 13551 15141 12315 -1383 649 -1018 C
ATOM 5587 C LYS B 424 50.232 43.415 59.802 1.00109.19 C
ANISOU 5587 C LYS B 424 13289 15411 12789 -1447 660 -1260 C
ATOM 5588 O LYS B 424 50.996 44.120 60.471 1.00113.19 O
ANISOU 5588 O LYS B 424 13592 15809 13608 -1681 683 -1298 O
ATOM 5589 CB LYS B 424 48.810 45.174 58.712 1.00109.34 C
ANISOU 5589 CB LYS B 424 13852 15277 12413 -1531 1058 -720 C
ATOM 5590 CG LYS B 424 49.590 45.078 57.407 1.00107.21 C
ANISOU 5590 CG LYS B 424 13420 15286 12030 -1486 1455 -672 C
ATOM 5591 CD LYS B 424 49.037 43.981 56.508 1.00109.81 C
ANISOU 5591 CD LYS B 424 13857 15903 11963 -1165 1388 -773 C
ATOM 5592 CE LYS B 424 49.784 43.913 55.187 1.00113.01 C
ANISOU 5592 CE LYS B 424 14125 16634 12182 -1069 1800 -731 C
ATOM 5593 NZ LYS B 424 49.256 42.826 54.315 1.00114.17 N
ANISOU 5593 NZ LYS B 424 14382 17071 11928 -741 1702 -910 N
ATOM 5594 N LEU B 425 50.583 42.234 59.296 1.00104.20 N
ANISOU 5594 N LEU B 425 12513 14995 12085 -1232 633 -1446 N
ATOM 5595 CA LEU B 425 51.965 41.787 59.298 1.00100.15 C
ANISOU 5595 CA LEU B 425 11578 14649 11826 -1237 717 -1650 C
ATOM 5596 C LEU B 425 52.709 42.387 58.106 1.00114.28 C
ANISOU 5596 C LEU B 425 13215 16636 13570 -1328 1206 -1531 C
ATOM 5597 O LEU B 425 52.123 42.592 57.039 1.00138.15 O
ANISOU 5597 O LEU B 425 16479 19761 16251 -1234 1442 -1358 O
ATOM 5598 CB LEU B 425 52.034 40.265 59.232 1.00101.61 C
ANISOU 5598 CB LEU B 425 11687 14951 11968 -929 514 -1896 C
ATOM 5599 CG LEU B 425 51.693 39.488 60.502 1.00101.23 C
ANISOU 5599 CG LEU B 425 11665 14733 12067 -816 74 -2010 C
ATOM 5600 CD1 LEU B 425 51.710 37.996 60.219 1.00101.41 C
ANISOU 5600 CD1 LEU B 425 11654 14812 12066 -507 -51 -2219 C
ATOM 5601 CD2 LEU B 425 52.674 39.838 61.610 1.00117.39 C
ANISOU 5601 CD2 LEU B 425 13388 16768 14444 -950 -56 -2091 C
ATOM 5602 N PRO B 426 54.003 42.678 58.257 1.00127.30 N
ANISOU 5602 N PRO B 426 14446 18371 15551 -1497 1374 -1608 N
ATOM 5603 CA PRO B 426 54.763 43.223 57.124 1.00136.75 C
ANISOU 5603 CA PRO B 426 15458 19769 16732 -1586 1892 -1456 C
ATOM 5604 C PRO B 426 55.038 42.171 56.061 1.00142.21 C
ANISOU 5604 C PRO B 426 16077 20805 17150 -1252 2053 -1583 C
ATOM 5605 O PRO B 426 54.724 40.988 56.238 1.00142.05 O
ANISOU 5605 O PRO B 426 16124 20825 17024 -976 1748 -1826 O
ATOM 5606 CB PRO B 426 56.055 43.725 57.780 1.00141.55 C
ANISOU 5606 CB PRO B 426 15576 20363 17845 -1879 1954 -1555 C
ATOM 5607 CG PRO B 426 56.229 42.840 58.959 1.00145.25 C
ANISOU 5607 CG PRO B 426 15891 20813 18484 -1756 1458 -1863 C
ATOM 5608 CD PRO B 426 54.836 42.537 59.463 1.00134.30 C
ANISOU 5608 CD PRO B 426 14982 19212 16836 -1607 1103 -1826 C
ATOM 5609 N ASP B 427 55.631 42.596 54.947 1.00148.49 N
ANISOU 5609 N ASP B 427 16741 21840 17840 -1264 2553 -1418 N
ATOM 5610 CA ASP B 427 55.889 41.674 53.849 1.00149.42 C
ANISOU 5610 CA ASP B 427 16811 22324 17637 -915 2746 -1551 C
ATOM 5611 C ASP B 427 57.137 40.835 54.093 1.00148.45 C
ANISOU 5611 C ASP B 427 16202 22393 17811 -809 2730 -1850 C
ATOM 5612 O ASP B 427 57.199 39.681 53.655 1.00131.64 O
ANISOU 5612 O ASP B 427 14069 20455 15493 -455 2657 -2111 O
ATOM 5613 CB ASP B 427 56.015 42.458 52.541 1.00138.00 C
ANISOU 5613 CB ASP B 427 15426 21112 15895 -914 3318 -1220 C
ATOM 5614 CG ASP B 427 54.703 43.085 52.115 1.00145.29 C
ANISOU 5614 CG ASP B 427 16858 21928 16418 -884 3324 -934 C
ATOM 5615 OD1 ASP B 427 53.665 42.760 52.729 1.00133.50 O
ANISOU 5615 OD1 ASP B 427 15657 20221 14848 -835 2880 -1042 O
ATOM 5616 OD2 ASP B 427 54.711 43.915 51.181 1.00165.47 O1-
ANISOU 5616 OD2 ASP B 427 19508 24620 18743 -899 3785 -576 O1-
ATOM 5617 N ASP B 428 58.124 41.390 54.793 1.00158.00 N
ANISOU 5617 N ASP B 428 16989 23549 19494 -1100 2781 -1840 N
ATOM 5618 CA ASP B 428 59.353 40.685 55.155 1.00151.28 C
ANISOU 5618 CA ASP B 428 15613 22898 18968 -1009 2734 -2109 C
ATOM 5619 C ASP B 428 59.294 40.141 56.577 1.00140.57 C
ANISOU 5619 C ASP B 428 14190 21336 17886 -996 2166 -2346 C
ATOM 5620 O ASP B 428 60.295 40.150 57.298 1.00134.94 O
ANISOU 5620 O ASP B 428 13007 20697 17567 -1102 2067 -2483 O
ATOM 5621 CB ASP B 428 60.558 41.604 54.982 1.00136.89 C
ANISOU 5621 CB ASP B 428 13286 21215 17509 -1330 3155 -1966 C
ATOM 5622 CG ASP B 428 60.441 42.880 55.798 1.00139.59 C
ANISOU 5622 CG ASP B 428 13626 21219 18193 -1811 3084 -1800 C
ATOM 5623 OD1 ASP B 428 59.361 43.124 56.378 1.00139.50 O
ANISOU 5623 OD1 ASP B 428 14051 20894 18058 -1862 2764 -1753 O
ATOM 5624 OD2 ASP B 428 61.431 43.639 55.862 1.00141.61 O1-
ANISOU 5624 OD2 ASP B 428 13431 21516 18860 -2141 3355 -1732 O1-
ATOM 5625 N PHE B 429 58.126 39.663 57.001 1.00138.32 N
ANISOU 5625 N PHE B 429 14350 20818 17389 -854 1790 -2384 N
ATOM 5626 CA PHE B 429 57.954 39.193 58.368 1.00137.53 C
ANISOU 5626 CA PHE B 429 14239 20519 17498 -819 1280 -2537 C
ATOM 5627 C PHE B 429 58.808 37.959 58.631 1.00143.70 C
ANISOU 5627 C PHE B 429 14680 21478 18444 -494 1128 -2811 C
ATOM 5628 O PHE B 429 58.749 36.975 57.888 1.00148.83 O
ANISOU 5628 O PHE B 429 15410 22234 18905 -160 1209 -2942 O
ATOM 5629 CB PHE B 429 56.480 38.882 58.630 1.00134.97 C
ANISOU 5629 CB PHE B 429 14455 19927 16901 -714 982 -2478 C
ATOM 5630 CG PHE B 429 56.226 38.193 59.940 1.00132.23 C
ANISOU 5630 CG PHE B 429 14133 19401 16707 -592 498 -2598 C
ATOM 5631 CD1 PHE B 429 56.460 38.844 61.139 1.00130.54 C
ANISOU 5631 CD1 PHE B 429 13781 19088 16732 -805 269 -2579 C
ATOM 5632 CD2 PHE B 429 55.744 36.894 59.971 1.00134.72 C
ANISOU 5632 CD2 PHE B 429 14618 19642 16926 -255 279 -2731 C
ATOM 5633 CE1 PHE B 429 56.223 38.212 62.345 1.00134.31 C
ANISOU 5633 CE1 PHE B 429 14292 19450 17288 -644 -159 -2654 C
ATOM 5634 CE2 PHE B 429 55.505 36.257 61.173 1.00126.50 C
ANISOU 5634 CE2 PHE B 429 13609 18429 16027 -122 -121 -2773 C
ATOM 5635 CZ PHE B 429 55.742 36.918 62.362 1.00122.83 C
ANISOU 5635 CZ PHE B 429 13011 17922 15738 -298 -335 -2716 C
ATOM 5636 N THR B 430 59.609 38.020 59.692 1.00144.13 N
ANISOU 5636 N THR B 430 14348 21569 18847 -572 899 -2915 N
ATOM 5637 CA THR B 430 60.415 36.892 60.154 1.00142.94 C
ANISOU 5637 CA THR B 430 13860 21574 18877 -234 697 -3144 C
ATOM 5638 C THR B 430 59.905 36.502 61.538 1.00148.64 C
ANISOU 5638 C THR B 430 14735 22079 19664 -139 178 -3170 C
ATOM 5639 O THR B 430 60.216 37.162 62.534 1.00151.91 O
ANISOU 5639 O THR B 430 14951 22496 20270 -351 -36 -3174 O
ATOM 5640 CB THR B 430 61.904 37.234 60.180 1.00150.04 C
ANISOU 5640 CB THR B 430 14096 22800 20112 -343 878 -3240 C
ATOM 5641 OG1 THR B 430 62.241 37.825 61.441 1.00160.57 O
ANISOU 5641 OG1 THR B 430 15186 24100 21723 -576 552 -3283 O
ATOM 5642 CG2 THR B 430 62.257 38.199 59.055 1.00147.34 C
ANISOU 5642 CG2 THR B 430 13630 22604 19750 -631 1422 -3086 C
ATOM 5643 N GLY B 431 59.118 35.433 61.592 1.00150.59 N
ANISOU 5643 N GLY B 431 15329 22139 19750 180 -13 -3193 N
ATOM 5644 CA GLY B 431 58.526 34.997 62.842 1.00143.27 C
ANISOU 5644 CA GLY B 431 14590 20996 18851 304 -450 -3151 C
ATOM 5645 C GLY B 431 57.510 33.903 62.581 1.00141.23 C
ANISOU 5645 C GLY B 431 14756 20476 18430 583 -544 -3139 C
ATOM 5646 O GLY B 431 57.516 33.280 61.519 1.00149.44 O
ANISOU 5646 O GLY B 431 15858 21543 19380 753 -326 -3255 O
ATOM 5647 N CYS B 432 56.631 33.688 63.557 1.00116.43 N
ANISOU 5647 N CYS B 432 11896 17084 15258 623 -862 -3011 N
ATOM 5648 CA CYS B 432 55.657 32.610 63.475 1.00129.06 C
ANISOU 5648 CA CYS B 432 13856 18390 16790 857 -976 -2986 C
ATOM 5649 C CYS B 432 54.250 33.122 63.749 1.00119.06 C
ANISOU 5649 C CYS B 432 13014 16887 15336 648 -1082 -2784 C
ATOM 5650 O CYS B 432 54.046 34.160 64.385 1.00109.23 O
ANISOU 5650 O CYS B 432 11798 15669 14038 406 -1157 -2650 O
ATOM 5651 CB CYS B 432 55.994 31.471 64.447 1.00119.21 C
ANISOU 5651 CB CYS B 432 12502 17044 15749 1228 -1244 -2988 C
ATOM 5652 SG CYS B 432 57.654 30.791 64.247 1.00132.12 S
ANISOU 5652 SG CYS B 432 13606 18972 17621 1555 -1154 -3211 S
ATOM 5653 N VAL B 433 53.281 32.364 63.242 1.00133.83 N
ANISOU 5653 N VAL B 433 15200 18525 17126 750 -1088 -2793 N
ATOM 5654 CA VAL B 433 51.861 32.583 63.488 1.00117.80 C
ANISOU 5654 CA VAL B 433 13546 16262 14950 613 -1206 -2608 C
ATOM 5655 C VAL B 433 51.300 31.304 64.092 1.00112.63 C
ANISOU 5655 C VAL B 433 13031 15301 14462 862 -1418 -2564 C
ATOM 5656 O VAL B 433 51.437 30.222 63.506 1.00112.43 O
ANISOU 5656 O VAL B 433 13005 15153 14560 1074 -1376 -2748 O
ATOM 5657 CB VAL B 433 51.105 32.960 62.205 1.00124.96 C
ANISOU 5657 CB VAL B 433 14680 17195 15605 460 -1003 -2654 C
ATOM 5658 CG1 VAL B 433 49.617 33.119 62.489 1.00120.28 C
ANISOU 5658 CG1 VAL B 433 14429 16385 14887 346 -1145 -2467 C
ATOM 5659 CG2 VAL B 433 51.677 34.235 61.612 1.00125.94 C
ANISOU 5659 CG2 VAL B 433 14676 17591 15586 230 -742 -2627 C
ATOM 5660 N ILE B 434 50.680 31.425 65.262 1.00107.37 N
ANISOU 5660 N ILE B 434 12488 14497 13809 848 -1626 -2317 N
ATOM 5661 CA ILE B 434 50.105 30.294 65.976 1.00108.72 C
ANISOU 5661 CA ILE B 434 12792 14360 14157 1070 -1798 -2181 C
ATOM 5662 C ILE B 434 48.633 30.588 66.224 1.00108.19 C
ANISOU 5662 C ILE B 434 13032 14107 13969 893 -1861 -1962 C
ATOM 5663 O ILE B 434 48.243 31.742 66.426 1.00106.48 O
ANISOU 5663 O ILE B 434 12891 14027 13539 675 -1854 -1846 O
ATOM 5664 CB ILE B 434 50.847 30.028 67.306 1.00115.55 C
ANISOU 5664 CB ILE B 434 13470 15289 15146 1313 -1982 -2036 C
ATOM 5665 CG1 ILE B 434 52.359 30.018 67.082 1.00124.03 C
ANISOU 5665 CG1 ILE B 434 14167 16646 16312 1449 -1925 -2256 C
ATOM 5666 CG2 ILE B 434 50.413 28.707 67.910 1.00127.25 C
ANISOU 5666 CG2 ILE B 434 15072 16428 16850 1601 -2093 -1868 C
ATOM 5667 CD1 ILE B 434 53.166 29.937 68.359 1.00133.28 C
ANISOU 5667 CD1 ILE B 434 15101 17989 17551 1683 -2137 -2146 C
ATOM 5668 N ALA B 435 47.812 29.540 66.203 1.00111.46 N
ANISOU 5668 N ALA B 435 13607 14191 14551 986 -1913 -1911 N
ATOM 5669 CA ALA B 435 46.385 29.712 66.442 1.00 99.06 C
ANISOU 5669 CA ALA B 435 12277 12451 12911 826 -1967 -1696 C
ATOM 5670 C ALA B 435 45.760 28.373 66.803 1.00107.33 C
ANISOU 5670 C ALA B 435 13415 13094 14273 975 -2040 -1587 C
ATOM 5671 O ALA B 435 46.209 27.320 66.343 1.00116.04 O
ANISOU 5671 O ALA B 435 14463 14000 15628 1139 -2013 -1788 O
ATOM 5672 CB ALA B 435 45.676 30.316 65.224 1.00 97.59 C
ANISOU 5672 CB ALA B 435 12213 12358 12511 580 -1859 -1851 C
ATOM 5673 N TRP B 436 44.712 28.427 67.626 1.00110.85 N
ANISOU 5673 N TRP B 436 13997 13399 14721 918 -2110 -1260 N
ATOM 5674 CA TRP B 436 43.990 27.225 68.020 1.00120.49 C
ANISOU 5674 CA TRP B 436 15299 14201 16280 1011 -2142 -1088 C
ATOM 5675 C TRP B 436 42.528 27.572 68.273 1.00113.42 C
ANISOU 5675 C TRP B 436 14547 13229 15318 801 -2156 -841 C
ATOM 5676 O TRP B 436 42.180 28.724 68.536 1.00110.68 O
ANISOU 5676 O TRP B 436 14247 13155 14652 678 -2161 -716 O
ATOM 5677 CB TRP B 436 44.615 26.576 69.265 1.00124.65 C
ANISOU 5677 CB TRP B 436 15761 14623 16975 1338 -2198 -802 C
ATOM 5678 CG TRP B 436 44.570 27.414 70.511 1.00112.79 C
ANISOU 5678 CG TRP B 436 14270 13385 15201 1402 -2272 -466 C
ATOM 5679 CD1 TRP B 436 43.662 27.320 71.528 1.00111.77 C
ANISOU 5679 CD1 TRP B 436 14257 13148 15064 1449 -2289 -51 C
ATOM 5680 CD2 TRP B 436 45.475 28.462 70.878 1.00112.05 C
ANISOU 5680 CD2 TRP B 436 14056 13710 14806 1432 -2336 -541 C
ATOM 5681 NE1 TRP B 436 43.944 28.247 72.501 1.00109.22 N
ANISOU 5681 NE1 TRP B 436 13919 13174 14407 1540 -2371 113 N
ATOM 5682 CE2 TRP B 436 45.051 28.961 72.127 1.00115.70 C
ANISOU 5682 CE2 TRP B 436 14592 14303 15064 1512 -2417 -203 C
ATOM 5683 CE3 TRP B 436 46.599 29.029 70.272 1.00111.86 C
ANISOU 5683 CE3 TRP B 436 13854 13965 14682 1390 -2322 -868 C
ATOM 5684 CZ2 TRP B 436 45.712 29.999 72.779 1.00111.72 C
ANISOU 5684 CZ2 TRP B 436 14002 14180 14268 1545 -2520 -240 C
ATOM 5685 CZ3 TRP B 436 47.254 30.061 70.922 1.00106.02 C
ANISOU 5685 CZ3 TRP B 436 13001 13582 13702 1388 -2407 -870 C
ATOM 5686 CH2 TRP B 436 46.809 30.535 72.162 1.00104.99 C
ANISOU 5686 CH2 TRP B 436 12959 13556 13378 1461 -2523 -586 C
ATOM 5687 N ASN B 437 41.674 26.550 68.217 1.00105.71 N
ANISOU 5687 N ASN B 437 13624 11858 14682 764 -2153 -772 N
ATOM 5688 CA ASN B 437 40.237 26.751 68.386 1.00114.52 C
ANISOU 5688 CA ASN B 437 14819 12893 15799 555 -2156 -550 C
ATOM 5689 C ASN B 437 39.900 27.055 69.840 1.00117.50 C
ANISOU 5689 C ASN B 437 15235 13324 16086 678 -2149 -44 C
ATOM 5690 O ASN B 437 40.343 26.350 70.749 1.00123.46 O
ANISOU 5690 O ASN B 437 15973 13911 17023 929 -2140 208 O
ATOM 5691 CB ASN B 437 39.476 25.513 67.919 1.00123.37 C
ANISOU 5691 CB ASN B 437 15939 13553 17382 454 -2154 -648 C
ATOM 5692 CG ASN B 437 37.974 25.663 68.055 1.00121.10 C
ANISOU 5692 CG ASN B 437 15668 13195 17148 217 -2158 -432 C
ATOM 5693 OD1 ASN B 437 37.381 25.201 69.029 1.00127.14 O
ANISOU 5693 OD1 ASN B 437 16433 13727 18146 256 -2106 -18 O
ATOM 5694 ND2 ASN B 437 37.351 26.315 67.081 1.00112.45 N
ANISOU 5694 ND2 ASN B 437 14572 12329 15826 -7 -2206 -687 N
ATOM 5695 N SER B 438 39.094 28.097 70.057 1.00107.42 N
ANISOU 5695 N SER B 438 14017 12292 14507 536 -2146 114 N
ATOM 5696 CA SER B 438 38.709 28.521 71.397 1.00 98.76 C
ANISOU 5696 CA SER B 438 12971 11309 13245 668 -2130 559 C
ATOM 5697 C SER B 438 37.211 28.385 71.648 1.00104.95 C
ANISOU 5697 C SER B 438 13780 11956 14139 528 -2066 856 C
ATOM 5698 O SER B 438 36.676 29.072 72.525 1.00105.45 O
ANISOU 5698 O SER B 438 13898 12214 13953 592 -2033 1172 O
ATOM 5699 CB SER B 438 39.144 29.961 71.648 1.00 95.08 C
ANISOU 5699 CB SER B 438 12547 11264 12315 677 -2167 505 C
ATOM 5700 OG SER B 438 38.720 30.806 70.594 1.00104.69 O
ANISOU 5700 OG SER B 438 13797 12627 13353 429 -2150 264 O
ATOM 5701 N ASN B 439 36.523 27.508 70.898 1.00 96.23 N
ANISOU 5701 N ASN B 439 12618 10531 13414 341 -2050 738 N
ATOM 5702 CA ASN B 439 35.073 27.360 71.043 1.00106.72 C
ANISOU 5702 CA ASN B 439 13905 11741 14902 164 -1995 988 C
ATOM 5703 C ASN B 439 34.703 26.962 72.458 1.00109.37 C
ANISOU 5703 C ASN B 439 14250 11957 15348 352 -1876 1554 C
ATOM 5704 O ASN B 439 33.641 27.340 72.966 1.00111.07 O
ANISOU 5704 O ASN B 439 14446 12274 15484 296 -1798 1874 O
ATOM 5705 CB ASN B 439 34.533 26.312 70.067 1.00115.27 C
ANISOU 5705 CB ASN B 439 14889 12450 16459 -69 -2024 718 C
ATOM 5706 CG ASN B 439 33.220 26.726 69.427 1.00102.86 C
ANISOU 5706 CG ASN B 439 13231 10998 14853 -350 -2062 643 C
ATOM 5707 OD1 ASN B 439 33.044 27.884 69.053 1.00 98.02 O
ANISOU 5707 OD1 ASN B 439 12659 10785 13800 -388 -2103 551 O
ATOM 5708 ND2 ASN B 439 32.303 25.778 69.275 1.00101.66 N
ANISOU 5708 ND2 ASN B 439 12945 10492 15190 -547 -2049 676 N
ATOM 5709 N ASN B 440 35.563 26.182 73.108 1.00115.00 N
ANISOU 5709 N ASN B 440 14986 12474 16234 610 -1847 1708 N
ATOM 5710 CA ASN B 440 35.270 25.764 74.470 1.00108.78 C
ANISOU 5710 CA ASN B 440 14221 11599 15509 847 -1714 2293 C
ATOM 5711 C ASN B 440 35.174 26.965 75.397 1.00105.39 C
ANISOU 5711 C ASN B 440 13873 11656 14517 1019 -1714 2530 C
ATOM 5712 O ASN B 440 34.340 26.990 76.308 1.00102.79 O
ANISOU 5712 O ASN B 440 13551 11369 14135 1109 -1580 2997 O
ATOM 5713 CB ASN B 440 36.345 24.797 74.960 1.00113.14 C
ANISOU 5713 CB ASN B 440 14795 11914 16277 1159 -1702 2404 C
ATOM 5714 CG ASN B 440 37.722 25.157 74.449 1.00122.92 C
ANISOU 5714 CG ASN B 440 16040 13368 17297 1270 -1858 1958 C
ATOM 5715 OD1 ASN B 440 37.975 26.298 74.065 1.00127.84 O
ANISOU 5715 OD1 ASN B 440 16674 14382 17516 1174 -1956 1674 O
ATOM 5716 ND2 ASN B 440 38.629 24.190 74.466 1.00125.80 N
ANISOU 5716 ND2 ASN B 440 16385 13469 17946 1488 -1862 1919 N
ATOM 5717 N LEU B 441 36.000 27.984 75.166 1.00103.91 N
ANISOU 5717 N LEU B 441 13738 11827 13916 1061 -1850 2204 N
ATOM 5718 CA LEU B 441 36.150 29.082 76.115 1.00107.45 C
ANISOU 5718 CA LEU B 441 14275 12700 13851 1261 -1881 2353 C
ATOM 5719 C LEU B 441 35.409 30.338 75.674 1.00101.29 C
ANISOU 5719 C LEU B 441 13541 12173 12773 1050 -1887 2205 C
ATOM 5720 O LEU B 441 34.577 30.870 76.416 1.00104.83 O
ANISOU 5720 O LEU B 441 14042 12792 12998 1129 -1805 2506 O
ATOM 5721 CB LEU B 441 37.639 29.390 76.313 1.00116.86 C
ANISOU 5721 CB LEU B 441 15473 14107 14824 1465 -2031 2103 C
ATOM 5722 CG LEU B 441 38.543 28.184 76.572 1.00112.93 C
ANISOU 5722 CG LEU B 441 14912 13382 14614 1707 -2048 2180 C
ATOM 5723 CD1 LEU B 441 39.989 28.513 76.262 1.00107.01 C
ANISOU 5723 CD1 LEU B 441 14091 12837 13731 1792 -2207 1781 C
ATOM 5724 CD2 LEU B 441 38.413 27.713 78.001 1.00108.94 C
ANISOU 5724 CD2 LEU B 441 14453 12918 14023 2081 -1980 2722 C
ATOM 5725 N ASP B 442 35.706 30.825 74.473 1.00 96.90 N
ANISOU 5725 N ASP B 442 12970 11653 12194 816 -1965 1765 N
ATOM 5726 CA ASP B 442 35.220 32.118 74.007 1.00107.44 C
ANISOU 5726 CA ASP B 442 14370 13237 13214 664 -1972 1614 C
ATOM 5727 C ASP B 442 33.888 32.031 73.276 1.00 96.40 C
ANISOU 5727 C ASP B 442 12914 11749 11965 430 -1911 1656 C
ATOM 5728 O ASP B 442 33.522 32.973 72.565 1.00 92.50 O
ANISOU 5728 O ASP B 442 12458 11430 11258 294 -1926 1482 O
ATOM 5729 CB ASP B 442 36.276 32.768 73.109 1.00109.83 C
ANISOU 5729 CB ASP B 442 14687 13661 13383 562 -2058 1169 C
ATOM 5730 CG ASP B 442 37.627 32.874 73.790 1.00110.20 C
ANISOU 5730 CG ASP B 442 14728 13828 13315 767 -2142 1085 C
ATOM 5731 OD1 ASP B 442 37.663 32.953 75.038 1.00111.25 O
ANISOU 5731 OD1 ASP B 442 14904 14078 13288 1008 -2160 1345 O
ATOM 5732 OD2 ASP B 442 38.653 32.872 73.080 1.00111.65 O1-
ANISOU 5732 OD2 ASP B 442 14845 14025 13553 705 -2191 755 O1-
ATOM 5733 N SER B 443 33.151 30.938 73.443 1.00 95.04 N
ANISOU 5733 N SER B 443 12635 11310 12168 384 -1842 1893 N
ATOM 5734 CA SER B 443 31.834 30.776 72.845 1.00 92.31 C
ANISOU 5734 CA SER B 443 12171 10892 12011 152 -1803 1935 C
ATOM 5735 C SER B 443 30.823 30.518 73.946 1.00 92.58 C
ANISOU 5735 C SER B 443 12145 10900 12130 248 -1648 2458 C
ATOM 5736 O SER B 443 31.032 29.638 74.785 1.00102.88 O
ANISOU 5736 O SER B 443 13435 11997 13657 396 -1558 2762 O
ATOM 5737 CB SER B 443 31.813 29.613 71.861 1.00 96.59 C
ANISOU 5737 CB SER B 443 12583 11091 13024 -64 -1860 1670 C
ATOM 5738 OG SER B 443 32.717 29.846 70.806 1.00112.57 O
ANISOU 5738 OG SER B 443 14657 13182 14933 -123 -1976 1194 O
ATOM 5739 N LYS B 444 29.723 31.261 73.927 1.00 98.80 N
ANISOU 5739 N LYS B 444 12888 11905 12745 186 -1595 2587 N
ATOM 5740 CA LYS B 444 28.683 31.117 74.933 1.00105.39 C
ANISOU 5740 CA LYS B 444 13639 12774 13631 284 -1414 3095 C
ATOM 5741 C LYS B 444 27.330 30.988 74.253 1.00101.04 C
ANISOU 5741 C LYS B 444 12856 12206 13328 16 -1390 3112 C
ATOM 5742 O LYS B 444 27.056 31.680 73.269 1.00100.96 O
ANISOU 5742 O LYS B 444 12828 12375 13157 -122 -1510 2797 O
ATOM 5743 CB LYS B 444 28.676 32.312 75.892 1.00109.00 C
ANISOU 5743 CB LYS B 444 14266 13603 13546 575 -1350 3288 C
ATOM 5744 CG LYS B 444 27.711 32.185 77.062 1.00115.16 C
ANISOU 5744 CG LYS B 444 14980 14477 14299 759 -1128 3841 C
ATOM 5745 CD LYS B 444 27.694 33.449 77.917 1.00126.96 C
ANISOU 5745 CD LYS B 444 16663 16359 15214 1066 -1085 3938 C
ATOM 5746 CE LYS B 444 27.049 34.624 77.192 1.00100.84 C
ANISOU 5746 CE LYS B 444 13372 13266 11678 966 -1129 3720 C
ATOM 5747 NZ LYS B 444 26.945 35.815 78.085 1.00 94.97 N
ANISOU 5747 NZ LYS B 444 12822 12842 10421 1280 -1063 3817 N
ATOM 5748 N VAL B 445 26.492 30.093 74.783 1.00 80.73 N
ANISOU 5748 N VAL B 445 10086 9428 11158 -49 -1229 3497 N
ATOM 5749 CA VAL B 445 25.127 29.956 74.292 1.00 82.64 C
ANISOU 5749 CA VAL B 445 10043 9686 11673 -305 -1199 3554 C
ATOM 5750 C VAL B 445 24.430 31.302 74.380 1.00 82.47 C
ANISOU 5750 C VAL B 445 10044 10125 11165 -176 -1176 3627 C
ATOM 5751 O VAL B 445 24.482 31.979 75.412 1.00 93.90 O
ANISOU 5751 O VAL B 445 11645 11798 12233 128 -1038 3929 O
ATOM 5752 CB VAL B 445 24.384 28.872 75.093 1.00 87.24 C
ANISOU 5752 CB VAL B 445 10406 9982 12760 -366 -964 4055 C
ATOM 5753 CG1 VAL B 445 22.962 28.707 74.583 1.00 89.82 C
ANISOU 5753 CG1 VAL B 445 10367 10333 13426 -668 -942 4094 C
ATOM 5754 CG2 VAL B 445 25.139 27.560 75.012 1.00 89.67 C
ANISOU 5754 CG2 VAL B 445 10730 9774 13566 -457 -973 3989 C
ATOM 5755 N GLY B 446 23.787 31.708 73.288 1.00108.37 N
ANISOU 5755 N GLY B 446 13183 13559 14435 -376 -1318 3334 N
ATOM 5756 CA GLY B 446 23.240 33.036 73.176 1.00101.80 C
ANISOU 5756 CA GLY B 446 12403 13139 13136 -231 -1320 3345 C
ATOM 5757 C GLY B 446 24.206 34.029 72.563 1.00 99.34 C
ANISOU 5757 C GLY B 446 12388 12975 12382 -131 -1466 2970 C
ATOM 5758 O GLY B 446 23.773 35.014 71.955 1.00 98.44 O
ANISOU 5758 O GLY B 446 12297 13133 11973 -95 -1523 2851 O
ATOM 5759 N GLY B 447 25.506 33.794 72.717 1.00103.87 N
ANISOU 5759 N GLY B 447 13172 13374 12919 -74 -1511 2808 N
ATOM 5760 CA GLY B 447 26.516 34.606 72.035 1.00106.39 C
ANISOU 5760 CA GLY B 447 13723 13789 12910 -38 -1634 2433 C
ATOM 5761 C GLY B 447 27.434 35.341 72.993 1.00 93.42 C
ANISOU 5761 C GLY B 447 12346 12225 10924 223 -1575 2509 C
ATOM 5762 O GLY B 447 27.010 35.970 73.958 1.00103.51 O
ANISOU 5762 O GLY B 447 13699 13668 11962 440 -1456 2791 O
ATOM 5763 N ASN B 448 28.737 35.258 72.703 1.00 92.00 N
ANISOU 5763 N ASN B 448 12295 11942 10718 207 -1668 2218 N
ATOM 5764 CA ASN B 448 29.763 36.031 73.404 1.00100.48 C
ANISOU 5764 CA ASN B 448 13590 13110 11479 404 -1669 2167 C
ATOM 5765 C ASN B 448 30.135 37.209 72.512 1.00100.02 C
ANISOU 5765 C ASN B 448 13666 13182 11155 342 -1717 1866 C
ATOM 5766 O ASN B 448 30.851 37.051 71.523 1.00 95.26 O
ANISOU 5766 O ASN B 448 13055 12513 10626 193 -1793 1559 O
ATOM 5767 CB ASN B 448 30.980 35.176 73.737 1.00 98.40 C
ANISOU 5767 CB ASN B 448 13334 12670 11384 445 -1730 2074 C
ATOM 5768 CG ASN B 448 32.064 35.961 74.446 1.00105.48 C
ANISOU 5768 CG ASN B 448 14403 13701 11973 631 -1772 1972 C
ATOM 5769 OD1 ASN B 448 31.789 36.966 75.100 1.00114.02 O
ANISOU 5769 OD1 ASN B 448 15613 14970 12740 782 -1730 2065 O
ATOM 5770 ND2 ASN B 448 33.304 35.501 74.327 1.00116.42 N
ANISOU 5770 ND2 ASN B 448 15777 14996 13461 629 -1863 1756 N
ATOM 5771 N TYR B 449 29.637 38.393 72.868 1.00100.21 N
ANISOU 5771 N TYR B 449 13820 13381 10873 477 -1646 1974 N
ATOM 5772 CA TYR B 449 29.824 39.600 72.078 1.00 91.75 C
ANISOU 5772 CA TYR B 449 12894 12397 9568 441 -1643 1772 C
ATOM 5773 C TYR B 449 30.939 40.488 72.619 1.00100.55 C
ANISOU 5773 C TYR B 449 14213 13506 10487 529 -1646 1613 C
ATOM 5774 O TYR B 449 30.957 41.690 72.335 1.00107.96 O
ANISOU 5774 O TYR B 449 15311 14484 11224 551 -1592 1533 O
ATOM 5775 CB TYR B 449 28.511 40.382 72.010 1.00 76.30 C
ANISOU 5775 CB TYR B 449 10947 10602 7441 539 -1556 1979 C
ATOM 5776 CG TYR B 449 27.406 39.645 71.291 1.00 86.25 C
ANISOU 5776 CG TYR B 449 11959 11914 8898 415 -1586 2072 C
ATOM 5777 CD1 TYR B 449 27.263 39.739 69.912 1.00 97.30 C
ANISOU 5777 CD1 TYR B 449 13302 13377 10290 272 -1661 1870 C
ATOM 5778 CD2 TYR B 449 26.510 38.846 71.989 1.00 94.74 C
ANISOU 5778 CD2 TYR B 449 12837 12990 10168 442 -1537 2358 C
ATOM 5779 CE1 TYR B 449 26.253 39.065 69.251 1.00 93.06 C
ANISOU 5779 CE1 TYR B 449 12510 12920 9928 154 -1733 1892 C
ATOM 5780 CE2 TYR B 449 25.499 38.167 71.337 1.00102.45 C
ANISOU 5780 CE2 TYR B 449 13540 14002 11384 286 -1580 2406 C
ATOM 5781 CZ TYR B 449 25.375 38.279 69.969 1.00 90.40 C
ANISOU 5781 CZ TYR B 449 11953 12555 9841 139 -1701 2143 C
ATOM 5782 OH TYR B 449 24.368 37.602 69.321 1.00 91.88 O
ANISOU 5782 OH TYR B 449 11842 12809 10260 -19 -1787 2133 O
ATOM 5783 N ASN B 450 31.867 39.923 73.391 1.00 96.54 N
ANISOU 5783 N ASN B 450 13692 12940 10051 585 -1710 1563 N
ATOM 5784 CA ASN B 450 32.941 40.708 73.986 1.00 88.45 C
ANISOU 5784 CA ASN B 450 12808 11938 8862 659 -1753 1371 C
ATOM 5785 C ASN B 450 34.129 40.896 73.055 1.00 98.47 C
ANISOU 5785 C ASN B 450 14060 13131 10224 460 -1797 1039 C
ATOM 5786 O ASN B 450 34.882 41.863 73.221 1.00 94.65 O
ANISOU 5786 O ASN B 450 13683 12650 9630 444 -1802 848 O
ATOM 5787 CB ASN B 450 33.408 40.058 75.291 1.00 94.62 C
ANISOU 5787 CB ASN B 450 13559 12765 9628 858 -1824 1473 C
ATOM 5788 CG ASN B 450 32.348 40.102 76.373 1.00109.03 C
ANISOU 5788 CG ASN B 450 15432 14713 11280 1107 -1740 1815 C
ATOM 5789 OD1 ASN B 450 31.334 40.788 76.236 1.00103.99 O
ANISOU 5789 OD1 ASN B 450 14858 14134 10518 1140 -1636 1936 O
ATOM 5790 ND2 ASN B 450 32.574 39.367 77.455 1.00110.60 N
ANISOU 5790 ND2 ASN B 450 15594 14976 11455 1314 -1767 1996 N
ATOM 5791 N TYR B 451 34.317 40.005 72.086 1.00110.85 N
ANISOU 5791 N TYR B 451 15486 14628 12003 308 -1817 953 N
ATOM 5792 CA TYR B 451 35.367 40.171 71.094 1.00104.45 C
ANISOU 5792 CA TYR B 451 14646 13784 11257 141 -1816 662 C
ATOM 5793 C TYR B 451 34.846 41.011 69.937 1.00 82.43 C
ANISOU 5793 C TYR B 451 11942 11034 8344 34 -1709 640 C
ATOM 5794 O TYR B 451 33.720 40.815 69.469 1.00 88.93 O
ANISOU 5794 O TYR B 451 12744 11905 9142 41 -1691 783 O
ATOM 5795 CB TYR B 451 35.862 38.815 70.592 1.00 94.01 C
ANISOU 5795 CB TYR B 451 13148 12381 10190 78 -1879 551 C
ATOM 5796 CG TYR B 451 36.538 37.992 71.666 1.00 98.79 C
ANISOU 5796 CG TYR B 451 13673 12942 10920 220 -1973 591 C
ATOM 5797 CD1 TYR B 451 37.891 38.145 71.935 1.00107.05 C
ANISOU 5797 CD1 TYR B 451 14669 14028 11978 240 -2033 382 C
ATOM 5798 CD2 TYR B 451 35.825 37.057 72.404 1.00107.19 C
ANISOU 5798 CD2 TYR B 451 14690 13937 12099 346 -1992 860 C
ATOM 5799 CE1 TYR B 451 38.514 37.396 72.919 1.00115.83 C
ANISOU 5799 CE1 TYR B 451 15696 15145 13168 421 -2138 433 C
ATOM 5800 CE2 TYR B 451 36.440 36.300 73.387 1.00116.80 C
ANISOU 5800 CE2 TYR B 451 15850 15124 13405 525 -2060 952 C
ATOM 5801 CZ TYR B 451 37.785 36.473 73.638 1.00111.93 C
ANISOU 5801 CZ TYR B 451 15193 14580 12753 581 -2146 733 C
ATOM 5802 OH TYR B 451 38.402 35.724 74.614 1.00111.73 O
ANISOU 5802 OH TYR B 451 15100 14570 12782 808 -2232 837 O
ATOM 5803 N ARG B 452 35.667 41.957 69.487 1.00 75.52 N
ANISOU 5803 N ARG B 452 11146 10147 7400 -56 -1632 474 N
ATOM 5804 CA ARG B 452 35.279 42.923 68.469 1.00 73.99 C
ANISOU 5804 CA ARG B 452 11071 9982 7060 -114 -1493 505 C
ATOM 5805 C ARG B 452 36.300 42.928 67.338 1.00 94.01 C
ANISOU 5805 C ARG B 452 13545 12527 9648 -267 -1411 302 C
ATOM 5806 O ARG B 452 37.315 42.224 67.374 1.00 97.21 O
ANISOU 5806 O ARG B 452 13805 12916 10214 -328 -1466 115 O
ATOM 5807 CB ARG B 452 35.164 44.336 69.049 1.00 72.26 C
ANISOU 5807 CB ARG B 452 11056 9694 6705 -55 -1402 572 C
ATOM 5808 CG ARG B 452 34.011 44.589 69.990 1.00 70.52 C
ANISOU 5808 CG ARG B 452 10933 9504 6359 141 -1425 792 C
ATOM 5809 CD ARG B 452 34.320 45.867 70.741 1.00 93.33 C
ANISOU 5809 CD ARG B 452 14018 12281 9163 196 -1367 731 C
ATOM 5810 NE ARG B 452 33.152 46.680 71.049 1.00 95.17 N
ANISOU 5810 NE ARG B 452 14423 12519 9218 385 -1282 937 N
ATOM 5811 CZ ARG B 452 33.223 47.886 71.594 1.00110.98 C
ANISOU 5811 CZ ARG B 452 16637 14387 11144 461 -1210 881 C
ATOM 5812 NH1 ARG B 452 34.387 48.439 71.897 1.00105.95 N
ANISOU 5812 NH1 ARG B 452 16048 13596 10611 328 -1226 613 N
ATOM 5813 NH2 ARG B 452 32.101 48.559 71.832 1.00120.86 N
ANISOU 5813 NH2 ARG B 452 18039 15650 12233 675 -1121 1078 N
ATOM 5814 N TYR B 453 36.023 43.757 66.334 1.00 97.80 N
ANISOU 5814 N TYR B 453 14135 13051 9975 -296 -1258 365 N
ATOM 5815 CA TYR B 453 36.927 43.966 65.212 1.00 94.45 C
ANISOU 5815 CA TYR B 453 13678 12666 9545 -413 -1114 234 C
ATOM 5816 C TYR B 453 36.606 45.309 64.572 1.00100.82 C
ANISOU 5816 C TYR B 453 14680 13455 10171 -400 -902 408 C
ATOM 5817 O TYR B 453 35.507 45.847 64.732 1.00 97.10 O
ANISOU 5817 O TYR B 453 14348 12990 9554 -271 -897 616 O
ATOM 5818 CB TYR B 453 36.848 42.802 64.206 1.00 92.02 C
ANISOU 5818 CB TYR B 453 13225 12510 9228 -414 -1175 112 C
ATOM 5819 CG TYR B 453 35.522 42.586 63.474 1.00 99.19 C
ANISOU 5819 CG TYR B 453 14160 13577 9949 -320 -1226 226 C
ATOM 5820 CD1 TYR B 453 34.891 43.605 62.769 1.00 98.05 C
ANISOU 5820 CD1 TYR B 453 14166 13541 9547 -244 -1094 413 C
ATOM 5821 CD2 TYR B 453 34.902 41.344 63.502 1.00103.32 C
ANISOU 5821 CD2 TYR B 453 14540 14136 10580 -304 -1415 147 C
ATOM 5822 CE1 TYR B 453 33.692 43.389 62.115 1.00102.95 C
ANISOU 5822 CE1 TYR B 453 14769 14364 9984 -136 -1177 498 C
ATOM 5823 CE2 TYR B 453 33.707 41.119 62.852 1.00108.13 C
ANISOU 5823 CE2 TYR B 453 15119 14909 11055 -245 -1495 204 C
ATOM 5824 CZ TYR B 453 33.104 42.144 62.161 1.00110.34 C
ANISOU 5824 CZ TYR B 453 15525 15358 11040 -153 -1392 370 C
ATOM 5825 OH TYR B 453 31.911 41.920 61.515 1.00123.32 O
ANISOU 5825 OH TYR B 453 17102 17222 12533 -73 -1505 412 O
ATOM 5826 N ARG B 454 37.587 45.850 63.853 1.00 97.82 N
ANISOU 5826 N ARG B 454 14301 13049 9816 -519 -705 348 N
ATOM 5827 CA ARG B 454 37.374 47.062 63.073 1.00 91.09 C
ANISOU 5827 CA ARG B 454 13637 12163 8810 -498 -452 557 C
ATOM 5828 C ARG B 454 36.785 46.700 61.717 1.00101.41 C
ANISOU 5828 C ARG B 454 14943 13745 9844 -379 -404 649 C
ATOM 5829 O ARG B 454 37.391 45.947 60.948 1.00101.16 O
ANISOU 5829 O ARG B 454 14768 13876 9793 -421 -392 484 O
ATOM 5830 CB ARG B 454 38.675 47.838 62.898 1.00 91.73 C
ANISOU 5830 CB ARG B 454 13703 12080 9068 -692 -221 492 C
ATOM 5831 CG ARG B 454 38.451 49.313 62.625 1.00 92.60 C
ANISOU 5831 CG ARG B 454 14055 11993 9136 -687 45 741 C
ATOM 5832 CD ARG B 454 39.730 50.107 62.757 1.00104.20 C
ANISOU 5832 CD ARG B 454 15480 13212 10897 -937 253 650 C
ATOM 5833 NE ARG B 454 39.970 50.446 64.152 1.00109.34 N
ANISOU 5833 NE ARG B 454 16138 13627 11780 -1027 90 461 N
ATOM 5834 CZ ARG B 454 39.589 51.582 64.718 1.00105.93 C
ANISOU 5834 CZ ARG B 454 15932 12904 11411 -1014 162 542 C
ATOM 5835 NH1 ARG B 454 38.962 52.521 64.028 1.00110.05 N
ANISOU 5835 NH1 ARG B 454 16698 13298 11818 -914 414 849 N
ATOM 5836 NH2 ARG B 454 39.834 51.776 66.008 1.00106.60 N
ANISOU 5836 NH2 ARG B 454 16007 12832 11662 -1070 -26 304 N
ATOM 5837 N LEU B 455 35.605 47.242 61.423 1.00103.31 N
ANISOU 5837 N LEU B 455 15336 14063 9854 -202 -384 894 N
ATOM 5838 CA LEU B 455 34.942 46.977 60.156 1.00 95.11 C
ANISOU 5838 CA LEU B 455 14291 13342 8503 -50 -377 976 C
ATOM 5839 C LEU B 455 35.176 48.070 59.122 1.00 90.13 C
ANISOU 5839 C LEU B 455 13832 12753 7658 27 -59 1221 C
ATOM 5840 O LEU B 455 35.077 47.795 57.922 1.00106.57 O
ANISOU 5840 O LEU B 455 15889 15146 9456 141 -10 1237 O
ATOM 5841 CB LEU B 455 33.435 46.787 60.383 1.00 97.24 C
ANISOU 5841 CB LEU B 455 14564 13752 8633 128 -578 1102 C
ATOM 5842 CG LEU B 455 32.561 46.436 59.177 1.00 90.52 C
ANISOU 5842 CG LEU B 455 13658 13284 7450 302 -660 1140 C
ATOM 5843 CD1 LEU B 455 33.039 45.147 58.527 1.00 85.39 C
ANISOU 5843 CD1 LEU B 455 12811 12819 6814 213 -800 802 C
ATOM 5844 CD2 LEU B 455 31.103 46.315 59.593 1.00 92.89 C
ANISOU 5844 CD2 LEU B 455 13904 13700 7691 446 -860 1264 C
ATOM 5845 N PHE B 456 35.513 49.285 59.551 1.00 92.02 N
ANISOU 5845 N PHE B 456 14249 12683 8031 -25 166 1405 N
ATOM 5846 CA PHE B 456 35.717 50.399 58.637 1.00106.40 C
ANISOU 5846 CA PHE B 456 16256 14468 9704 48 517 1706 C
ATOM 5847 C PHE B 456 36.895 51.253 59.095 1.00107.15 C
ANISOU 5847 C PHE B 456 16401 14162 10150 -201 773 1700 C
ATOM 5848 O PHE B 456 37.085 51.468 60.296 1.00113.68 O
ANISOU 5848 O PHE B 456 17231 14694 11268 -337 665 1553 O
ATOM 5849 CB PHE B 456 34.457 51.267 58.533 1.00111.99 C
ANISOU 5849 CB PHE B 456 17186 15181 10185 327 559 2051 C
ATOM 5850 CG PHE B 456 33.244 50.543 58.023 1.00112.74 C
ANISOU 5850 CG PHE B 456 17193 15702 9940 571 307 2068 C
ATOM 5851 CD1 PHE B 456 33.233 49.986 56.756 1.00104.29 C
ANISOU 5851 CD1 PHE B 456 16036 15045 8544 682 300 2040 C
ATOM 5852 CD2 PHE B 456 32.097 50.460 58.796 1.00104.89 C
ANISOU 5852 CD2 PHE B 456 16190 14717 8948 698 84 2105 C
ATOM 5853 CE1 PHE B 456 32.113 49.333 56.281 1.00 97.28 C
ANISOU 5853 CE1 PHE B 456 15038 14559 7363 887 32 1999 C
ATOM 5854 CE2 PHE B 456 30.972 49.811 58.326 1.00 96.69 C
ANISOU 5854 CE2 PHE B 456 15018 14074 7647 890 -152 2108 C
ATOM 5855 CZ PHE B 456 30.980 49.247 57.066 1.00102.27 C
ANISOU 5855 CZ PHE B 456 15626 15179 8055 972 -197 2036 C
ATOM 5856 N ARG B 457 37.673 51.748 58.128 1.0 |
