HEADER MEMBRANE PROTEIN 16-DEC-19 6TQ6
TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH COMPOUND 14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OREXIN RECEPTOR TYPE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OX1R,HYPOCRETIN RECEPTOR TYPE 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: COMPOUND 14 BOUND IN THE ORTHOSTERIC SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HCRTR1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS 7TM, GPCR, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE,
AUTHOR 2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI,
AUTHOR 3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR,
AUTHOR 4 J.A.CHRISTOPHER
REVDAT 4 29-JUL-20 6TQ6 1 COMPND REMARK HETNAM SITE
REVDAT 3 11-MAR-20 6TQ6 1 JRNL
REVDAT 2 29-JAN-20 6TQ6 1 JRNL
REVDAT 1 01-JAN-20 6TQ6 0
JRNL AUTH M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,
JRNL AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,
JRNL AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,
JRNL AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER
JRNL TITL COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES
JRNL TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.
JRNL REF J.MED.CHEM. V. 63 1528 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 31860301
JRNL DOI 10.1021/ACS.JMEDCHEM.9B01787
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.7
REMARK 3 NUMBER OF REFLECTIONS : 29926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1482
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 34.0640 - 5.6535 1.00 3321 188 0.2452 0.2928
REMARK 3 2 5.6535 - 4.4906 1.00 3258 213 0.2004 0.2279
REMARK 3 3 4.4906 - 3.9239 1.00 3315 141 0.1883 0.2684
REMARK 3 4 3.9239 - 3.5656 1.00 3298 145 0.1889 0.2117
REMARK 3 5 3.5656 - 3.3102 1.00 3285 176 0.2161 0.2558
REMARK 3 6 3.3102 - 3.1152 0.95 3118 136 0.2431 0.2470
REMARK 3 7 3.1152 - 2.9593 0.82 2707 163 0.2390 0.2693
REMARK 3 8 2.9593 - 2.8305 0.73 2375 110 0.2607 0.2718
REMARK 3 9 2.8305 - 2.7216 0.58 1915 96 0.2765 0.3433
REMARK 3 10 2.7216 - 2.6277 0.44 1428 95 0.2936 0.3302
REMARK 3 11 2.6277 - 2.5460 0.13 424 19 0.7013 0.5807
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.77
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5274 64.8489 124.9920
REMARK 3 T TENSOR
REMARK 3 T11: 1.0089 T22: 0.5811
REMARK 3 T33: 0.8856 T12: -0.0393
REMARK 3 T13: 0.0513 T23: 0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 8.6546 L22: 2.3970
REMARK 3 L33: 9.1248 L12: -1.8887
REMARK 3 L13: -0.8843 L23: 4.3901
REMARK 3 S TENSOR
REMARK 3 S11: 0.5007 S12: -0.9964 S13: -0.6047
REMARK 3 S21: 0.4921 S22: -0.3174 S23: 0.8743
REMARK 3 S31: 0.1288 S32: -0.5831 S33: -0.2581
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2499 50.0635 98.6240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.5792
REMARK 3 T33: 1.1226 T12: -0.0363
REMARK 3 T13: 0.0422 T23: -0.2878
REMARK 3 L TENSOR
REMARK 3 L11: 0.6682 L22: 3.3178
REMARK 3 L33: 2.9778 L12: 0.4535
REMARK 3 L13: -0.3671 L23: 1.6240
REMARK 3 S TENSOR
REMARK 3 S11: 0.3638 S12: -0.1944 S13: 0.3046
REMARK 3 S21: -0.3036 S22: 0.6446 S23: -1.8145
REMARK 3 S31: -0.6633 S32: 0.8597 S33: -0.3151
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5783 34.9378 86.5176
REMARK 3 T TENSOR
REMARK 3 T11: 0.5049 T22: 0.7786
REMARK 3 T33: 1.3014 T12: 0.0669
REMARK 3 T13: 0.1238 T23: -0.2428
REMARK 3 L TENSOR
REMARK 3 L11: 0.1297 L22: 5.1260
REMARK 3 L33: 1.1991 L12: -0.7516
REMARK 3 L13: 0.1627 L23: -0.3010
REMARK 3 S TENSOR
REMARK 3 S11: 0.3590 S12: 0.2166 S13: -0.3388
REMARK 3 S21: -0.7449 S22: 0.4275 S23: -1.9005
REMARK 3 S31: 0.4787 S32: 0.9317 S33: -0.6603
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8260 53.6466 87.7583
REMARK 3 T TENSOR
REMARK 3 T11: 0.5362 T22: 0.5670
REMARK 3 T33: 0.7400 T12: 0.1169
REMARK 3 T13: -0.0055 T23: 0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 1.2845 L22: 2.8654
REMARK 3 L33: 7.3460 L12: 0.2118
REMARK 3 L13: -0.7178 L23: 4.2888
REMARK 3 S TENSOR
REMARK 3 S11: 0.4483 S12: -0.2660 S13: 0.5033
REMARK 3 S21: -1.2801 S22: -0.3782 S23: 1.1382
REMARK 3 S31: -0.7976 S32: -0.7541 S33: -0.0558
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5803 33.9839 100.2424
REMARK 3 T TENSOR
REMARK 3 T11: 0.3335 T22: 0.4808
REMARK 3 T33: 0.5973 T12: 0.1397
REMARK 3 T13: -0.1453 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 2.5286 L22: 4.5977
REMARK 3 L33: 3.7074 L12: 0.5009
REMARK 3 L13: -0.9022 L23: 2.2347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1028 S12: -0.4037 S13: 0.1108
REMARK 3 S21: 0.8341 S22: 0.4009 S23: -1.0955
REMARK 3 S31: 0.4283 S32: 0.7979 S33: -0.0680
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 323 THROUGH 361 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1612 48.0877 105.5165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3607 T22: 0.3754
REMARK 3 T33: 0.5750 T12: 0.0431
REMARK 3 T13: -0.0340 T23: -0.0468
REMARK 3 L TENSOR
REMARK 3 L11: 0.3654 L22: 6.4392
REMARK 3 L33: 5.6801 L12: 0.5398
REMARK 3 L13: -0.0500 L23: 1.7810
REMARK 3 S TENSOR
REMARK 3 S11: 0.4951 S12: -0.1360 S13: 0.0008
REMARK 3 S21: 0.5353 S22: -0.0020 S23: 0.3101
REMARK 3 S31: -0.1495 S32: 0.0480 S33: -0.1115
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 362 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2153 48.3761 108.2752
REMARK 3 T TENSOR
REMARK 3 T11: 0.6128 T22: 1.7747
REMARK 3 T33: 1.8738 T12: 0.0527
REMARK 3 T13: -0.5774 T23: -0.4617
REMARK 3 L TENSOR
REMARK 3 L11: 1.9388 L22: 2.5051
REMARK 3 L33: 3.6679 L12: 2.1946
REMARK 3 L13: -1.3535 L23: -1.3390
REMARK 3 S TENSOR
REMARK 3 S11: -0.2265 S12: -0.0609 S13: -0.1260
REMARK 3 S21: 0.2560 S22: -1.3611 S23: -0.5359
REMARK 3 S31: -0.6700 S32: 1.4422 S33: 0.1655
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4479 13.4503 65.6115
REMARK 3 T TENSOR
REMARK 3 T11: 1.3318 T22: 0.4954
REMARK 3 T33: 0.1373 T12: 0.1543
REMARK 3 T13: 0.1925 T23: -0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 3.2142 L22: 4.2681
REMARK 3 L33: 5.2597 L12: -0.7255
REMARK 3 L13: -1.8580 L23: 1.8396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0816 S12: 0.5271 S13: 0.0559
REMARK 3 S21: -0.8537 S22: 0.0513 S23: -0.5451
REMARK 3 S31: 0.3459 S32: -0.1049 S33: -0.1418
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3096 17.3479 73.2102
REMARK 3 T TENSOR
REMARK 3 T11: 0.8010 T22: 0.3630
REMARK 3 T33: 0.5483 T12: 0.1481
REMARK 3 T13: 0.4107 T23: -0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 2.5279 L22: 4.3316
REMARK 3 L33: 3.9924 L12: -0.4699
REMARK 3 L13: 0.2429 L23: -0.4275
REMARK 3 S TENSOR
REMARK 3 S11: 0.1112 S12: 0.4979 S13: -0.0931
REMARK 3 S21: -1.3893 S22: 0.3701 S23: -0.7615
REMARK 3 S31: 0.3980 S32: 0.2245 S33: 0.0824
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8778 29.9302 79.1182
REMARK 3 T TENSOR
REMARK 3 T11: 0.4813 T22: 0.3002
REMARK 3 T33: 0.5973 T12: 0.0712
REMARK 3 T13: 0.3936 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 3.2295 L22: 4.0479
REMARK 3 L33: 2.7864 L12: -1.3775
REMARK 3 L13: 0.1409 L23: 0.8918
REMARK 3 S TENSOR
REMARK 3 S11: 0.0534 S12: 0.1561 S13: 0.3717
REMARK 3 S21: -0.9919 S22: 0.5857 S23: -1.4554
REMARK 3 S31: -0.1299 S32: 0.2155 S33: -0.2125
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 176 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8528 12.5155 93.2940
REMARK 3 T TENSOR
REMARK 3 T11: 0.7625 T22: 0.3982
REMARK 3 T33: 0.4789 T12: 0.0737
REMARK 3 T13: 0.2258 T23: 0.1295
REMARK 3 L TENSOR
REMARK 3 L11: 0.7244 L22: 4.1320
REMARK 3 L33: 0.8815 L12: -0.3844
REMARK 3 L13: 0.1369 L23: 1.8079
REMARK 3 S TENSOR
REMARK 3 S11: -0.2874 S12: -0.1945 S13: -0.4830
REMARK 3 S21: 1.4724 S22: 0.1912 S23: 0.5868
REMARK 3 S31: 0.6232 S32: 0.0096 S33: 0.1302
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5114 45.4597 68.7710
REMARK 3 T TENSOR
REMARK 3 T11: 1.5701 T22: 0.5348
REMARK 3 T33: 0.7042 T12: 0.0303
REMARK 3 T13: 0.3082 T23: 0.3087
REMARK 3 L TENSOR
REMARK 3 L11: 2.3543 L22: 3.6443
REMARK 3 L33: 2.3502 L12: 0.8497
REMARK 3 L13: -0.9078 L23: -0.9324
REMARK 3 S TENSOR
REMARK 3 S11: 0.3867 S12: 0.9023 S13: 1.1558
REMARK 3 S21: -2.3466 S22: 0.2925 S23: -0.3065
REMARK 3 S31: -1.1340 S32: -0.1372 S33: -0.1035
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 252 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3610 32.7423 69.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.9627 T22: 0.3634
REMARK 3 T33: 0.2036 T12: 0.0337
REMARK 3 T13: 0.1918 T23: 0.0963
REMARK 3 L TENSOR
REMARK 3 L11: 5.4503 L22: 5.3712
REMARK 3 L33: 4.1410 L12: 2.1959
REMARK 3 L13: -2.4990 L23: -1.8229
REMARK 3 S TENSOR
REMARK 3 S11: 0.2111 S12: 0.5651 S13: 0.3152
REMARK 3 S21: -1.3568 S22: -0.1726 S23: -0.2467
REMARK 3 S31: -0.6399 S32: 0.3722 S33: -0.1355
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 323 THROUGH 332 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.5985 15.9999 90.2459
REMARK 3 T TENSOR
REMARK 3 T11: 0.9013 T22: 1.1536
REMARK 3 T33: 1.0950 T12: -0.1866
REMARK 3 T13: 0.1681 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 3.0085 L22: 4.4886
REMARK 3 L33: 6.4866 L12: 3.6225
REMARK 3 L13: -0.2410 L23: -1.1056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: -0.2593 S13: -0.2878
REMARK 3 S21: 0.7646 S22: 0.1077 S23: 2.0696
REMARK 3 S31: 1.4922 S32: -2.4541 S33: 0.6705
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 333 THROUGH 361 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7896 17.4039 71.9515
REMARK 3 T TENSOR
REMARK 3 T11: 0.7161 T22: 0.3162
REMARK 3 T33: 0.3572 T12: -0.0305
REMARK 3 T13: -0.0625 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 4.6568 L22: 4.2479
REMARK 3 L33: 4.9606 L12: -2.2786
REMARK 3 L13: 0.4459 L23: 2.3285
REMARK 3 S TENSOR
REMARK 3 S11: 0.2260 S12: -0.0841 S13: -0.0528
REMARK 3 S21: -1.0575 S22: -0.1674 S23: 0.2529
REMARK 3 S31: 0.1679 S32: 0.5099 S33: -0.0092
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 362 THROUGH 377 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6101 20.7302 53.6489
REMARK 3 T TENSOR
REMARK 3 T11: 3.0178 T22: 0.9635
REMARK 3 T33: 0.9489 T12: 0.1345
REMARK 3 T13: 0.6887 T23: 0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 1.1424 L22: 1.0042
REMARK 3 L33: 5.7282 L12: -0.5192
REMARK 3 L13: 1.8885 L23: 0.5573
REMARK 3 S TENSOR
REMARK 3 S11: 0.4945 S12: 0.6453 S13: -0.1456
REMARK 3 S21: -1.3388 S22: -0.1646 S23: -0.4404
REMARK 3 S31: 1.8509 S32: 0.5827 S33: 0.6934
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 45 THROUGH 375 OR
REMARK 3 RESID 401))
REMARK 3 SELECTION : (CHAIN B AND (RESID 45 THROUGH 187 OR
REMARK 3 RESID 199 THROUGH 244 OR RESID 289
REMARK 3 THROUGH 375 OR RESID 401))
REMARK 3 ATOM PAIRS NUMBER : 2544
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6TQ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105892.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.0-6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96863
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29926
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 34.064
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.7
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 6TO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM
REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 5.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 284K
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 73.53600
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 25
REMARK 465 ALA A 26
REMARK 465 SER A 27
REMARK 465 VAL A 188
REMARK 465 LEU A 189
REMARK 465 PRO A 190
REMARK 465 GLU A 191
REMARK 465 LEU A 192
REMARK 465 ALA A 193
REMARK 465 ALA A 194
REMARK 465 ARG A 195
REMARK 465 THR A 196
REMARK 465 ARG A 197
REMARK 465 ALA A 198
REMARK 465 ARG A 245
REMARK 465 GLN A 246
REMARK 465 ILE A 247
REMARK 465 PRO A 248
REMARK 465 GLY A 249
REMARK 465 THR A 250
REMARK 465 THR A 251
REMARK 465 SER A 252
REMARK 465 ALA A 253
REMARK 465 LEU A 254
REMARK 465 VAL A 255
REMARK 465 ARG A 256
REMARK 465 ASN A 257
REMARK 465 TRP A 258
REMARK 465 LYS A 259
REMARK 465 ARG A 260
REMARK 465 PRO A 261
REMARK 465 SER A 262
REMARK 465 ASP A 263
REMARK 465 GLN A 264
REMARK 465 LEU A 265
REMARK 465 GLY A 266
REMARK 465 ASP A 267
REMARK 465 LEU A 268
REMARK 465 GLU A 269
REMARK 465 GLN A 270
REMARK 465 GLY A 271
REMARK 465 LEU A 272
REMARK 465 SER A 273
REMARK 465 GLY A 274
REMARK 465 GLU A 275
REMARK 465 PRO A 276
REMARK 465 GLN A 277
REMARK 465 PRO A 278
REMARK 465 ARG A 279
REMARK 465 ALA A 280
REMARK 465 ARG A 281
REMARK 465 ALA A 282
REMARK 465 PHE A 283
REMARK 465 LEU A 284
REMARK 465 ALA A 285
REMARK 465 GLU A 286
REMARK 465 VAL A 287
REMARK 465 LYS A 288
REMARK 465 TRP A 376
REMARK 465 LEU A 377
REMARK 465 PRO A 378
REMARK 465 GLY A 379
REMARK 465 LEU A 380
REMARK 465 ALA A 381
REMARK 465 ALA A 382
REMARK 465 ALA A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 SER B 27
REMARK 465 GLU B 28
REMARK 465 ASP B 29
REMARK 465 GLU B 30
REMARK 465 PHE B 31
REMARK 465 LEU B 32
REMARK 465 ARG B 33
REMARK 465 TYR B 34
REMARK 465 LEU B 35
REMARK 465 TRP B 36
REMARK 465 ARG B 37
REMARK 465 ASP B 38
REMARK 465 TYR B 39
REMARK 465 LEU B 40
REMARK 465 TYR B 41
REMARK 465 PRO B 42
REMARK 465 LYS B 43
REMARK 465 GLN B 44
REMARK 465 ALA B 253
REMARK 465 LEU B 254
REMARK 465 VAL B 255
REMARK 465 ARG B 256
REMARK 465 ASN B 257
REMARK 465 TRP B 258
REMARK 465 LYS B 259
REMARK 465 ARG B 260
REMARK 465 PRO B 261
REMARK 465 SER B 262
REMARK 465 ASP B 263
REMARK 465 GLN B 264
REMARK 465 LEU B 265
REMARK 465 GLY B 266
REMARK 465 ASP B 267
REMARK 465 LEU B 268
REMARK 465 GLU B 269
REMARK 465 GLN B 270
REMARK 465 GLY B 271
REMARK 465 LEU B 272
REMARK 465 SER B 273
REMARK 465 GLY B 274
REMARK 465 GLU B 275
REMARK 465 PRO B 276
REMARK 465 GLN B 277
REMARK 465 PRO B 278
REMARK 465 ARG B 279
REMARK 465 ALA B 280
REMARK 465 ARG B 281
REMARK 465 ALA B 282
REMARK 465 PHE B 283
REMARK 465 LEU B 284
REMARK 465 PRO B 378
REMARK 465 GLY B 379
REMARK 465 LEU B 380
REMARK 465 ALA B 381
REMARK 465 ALA B 382
REMARK 465 ALA B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
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 TYR A 39 -57.73 -141.53
REMARK 500 TYR A 224 -67.72 -136.32
REMARK 500 ALA B 194 0.31 -69.35
REMARK 500 TYR B 224 -67.66 -136.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NVH A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6TO7 RELATED DB: PDB
REMARK 900 RELATED ID: 6TOD RELATED DB: PDB
REMARK 900 RELATED ID: 6TOS RELATED DB: PDB
REMARK 900 RELATED ID: 6TOT RELATED DB: PDB
REMARK 900 RELATED ID: 6TP6 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP3 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP4 RELATED DB: PDB
REMARK 900 RELATED ID: 6TQ4 RELATED DB: PDB
DBREF 6TQ6 A 28 380 UNP O43613 OX1R_HUMAN 28 380
DBREF 6TQ6 B 28 380 UNP O43613 OX1R_HUMAN 28 380
SEQADV 6TQ6 ALA A 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA A 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 SER A 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ6 LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ6 LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ6 VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ6 TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ6 TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ6 ALA A 381 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA A 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA A 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS A 392 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA B 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA B 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 SER B 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ6 LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ6 LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ6 VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ6 TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ6 TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ6 ALA B 381 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA B 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 ALA B 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ6 HIS B 392 UNP O43613 EXPRESSION TAG
SEQRES 1 A 368 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 A 368 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 A 368 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 A 368 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 A 368 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 A 368 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 A 368 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 A 368 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 A 368 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 A 368 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 A 368 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 A 368 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 A 368 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 A 368 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 A 368 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 A 368 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 A 368 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 A 368 GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP
SEQRES 19 A 368 LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY
SEQRES 20 A 368 LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU
SEQRES 21 A 368 ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA
SEQRES 22 A 368 LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS
SEQRES 23 A 368 TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL
SEQRES 24 A 368 PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL
SEQRES 25 A 368 TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA
SEQRES 26 A 368 ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER
SEQRES 27 A 368 GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP
SEQRES 28 A 368 TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 29 A 368 HIS HIS HIS HIS
SEQRES 1 B 368 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 B 368 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 B 368 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 B 368 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 B 368 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 B 368 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 B 368 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 B 368 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 B 368 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 B 368 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 B 368 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 B 368 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 B 368 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 B 368 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 B 368 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 B 368 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 B 368 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 B 368 GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP
SEQRES 19 B 368 LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY
SEQRES 20 B 368 LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU
SEQRES 21 B 368 ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA
SEQRES 22 B 368 LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS
SEQRES 23 B 368 TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL
SEQRES 24 B 368 PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL
SEQRES 25 B 368 TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA
SEQRES 26 B 368 ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER
SEQRES 27 B 368 GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP
SEQRES 28 B 368 TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 29 B 368 HIS HIS HIS HIS
HET NVH A 401 33
HET SO4 A 402 5
HET SO4 A 403 5
HET PGW A 404 51
HET SOG A 405 20
HET SOG A 406 20
HET SOG A 407 20
HET SOG A 408 20
HET PG4 A 409 13
HET NVH B 401 33
HET SO4 B 402 5
HET SO4 B 403 5
HET PGW B 404 51
HET SOG B 405 20
HET SOG B 406 20
HET SOG B 407 20
HET SOG B 408 20
HET SOG B 409 20
HET SOG B 410 20
HET PG4 B 411 13
HETNAM NVH 2-(5-METHYLSULFONYLPYRIDIN-3-YL)-1,1-
HETNAM 2 NVH BIS(OXIDANYLIDENE)-4-[[2,4,6-TRIS(FLUORANYL)
HETNAM 3 NVH PHENYL]METHYL]PYRIDO[2,3-E][1,2,4]THIADIAZIN-3-ONE
HETNAM SO4 SULFATE ION
HETNAM PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM 2 PGW PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)-
HETNAM 3 PGW OCTADEC-9-ENOATE
HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1-
HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL
HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE
FORMUL 3 NVH 2(C19 H13 F3 N4 O5 S2)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 PGW 2(C40 H77 O10 P)
FORMUL 7 SOG 10(C14 H28 O5 S)
FORMUL 11 PG4 2(C8 H18 O5)
FORMUL 23 HOH *26(H2 O)
HELIX 1 AA1 GLU A 28 TYR A 39 1 12
HELIX 2 AA2 TYR A 39 ASN A 74 1 36
HELIX 3 AA3 THR A 79 ILE A 98 1 20
HELIX 4 AA4 ILE A 98 GLU A 110 1 13
HELIX 5 AA5 PHE A 114 CYS A 149 1 36
HELIX 6 AA6 THR A 157 MET A 176 1 20
HELIX 7 AA7 MET A 176 VAL A 182 1 7
HELIX 8 AA8 ASP A 209 TYR A 224 1 16
HELIX 9 AA9 TYR A 224 GLY A 244 1 21
HELIX 10 AB1 MET A 290 VAL A 323 1 34
HELIX 11 AB2 GLN A 329 SER A 331 5 3
HELIX 12 AB3 ASP A 332 SER A 362 1 31
HELIX 13 AB4 SER A 362 TRP A 375 1 14
HELIX 14 AB5 ALA B 46 ASN B 74 1 29
HELIX 15 AB6 THR B 79 ILE B 98 1 20
HELIX 16 AB7 ILE B 98 GLU B 110 1 13
HELIX 17 AB8 PHE B 114 CYS B 149 1 36
HELIX 18 AB9 THR B 157 MET B 176 1 20
HELIX 19 AC1 MET B 176 VAL B 182 1 7
HELIX 20 AC2 LEU B 189 ARG B 195 5 7
HELIX 21 AC3 ASP B 209 TYR B 224 1 16
HELIX 22 AC4 TYR B 224 GLY B 244 1 21
HELIX 23 AC5 THR B 251 VAL B 323 1 41
HELIX 24 AC6 ASP B 332 SER B 362 1 31
HELIX 25 AC7 SER B 362 LEU B 377 1 16
SHEET 1 AA1 2 MET A 183 SER A 186 0
SHEET 2 AA1 2 VAL A 201 GLU A 204 -1 O ASP A 203 N GLU A 184
SHEET 1 AA2 2 MET B 183 SER B 187 0
SHEET 2 AA2 2 SER B 200 GLU B 204 -1 O ASP B 203 N GLU B 184
SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.04
SSBOND 2 CYS B 119 CYS B 202 1555 1555 2.04
CRYST1 59.834 147.072 72.260 90.00 111.56 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 0.016713 0.000000 0.006603 0.00000
SCALE2 0.000000 0.006799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014880 0.00000
ATOM 1 N GLU A 28 -51.550 67.621 133.136 1.00116.56 N
ANISOU 1 N GLU A 28 15342 15368 13575 -1172 2413 516 N
ATOM 2 CA GLU A 28 -50.098 67.503 133.240 1.00116.62 C
ANISOU 2 CA GLU A 28 15665 15237 13407 -1120 2266 649 C
ATOM 3 C GLU A 28 -49.567 66.300 132.433 1.00119.09 C
ANISOU 3 C GLU A 28 16223 15055 13971 -1185 2012 1066 C
ATOM 4 O GLU A 28 -48.618 66.454 131.663 1.00116.14 O
ANISOU 4 O GLU A 28 16083 14330 13716 -1028 1791 974 O
ATOM 5 CB GLU A 28 -49.677 67.423 134.724 1.00117.73 C
ANISOU 5 CB GLU A 28 15725 16021 12988 -1218 2443 768 C
ATOM 6 CG GLU A 28 -49.693 68.801 135.426 1.00117.49 C
ANISOU 6 CG GLU A 28 15504 16433 12704 -1078 2618 192 C
ATOM 7 CD GLU A 28 -49.656 68.768 136.959 1.00122.14 C
ANISOU 7 CD GLU A 28 15863 17847 12696 -1162 2836 229 C
ATOM 8 OE1 GLU A 28 -49.334 67.720 137.561 1.00124.60 O
ANISOU 8 OE1 GLU A 28 16250 18397 12696 -1284 2840 760 O
ATOM 9 OE2 GLU A 28 -49.952 69.823 137.562 1.00123.88 O
ANISOU 9 OE2 GLU A 28 15838 18485 12746 -1068 3002 -289 O
ATOM 10 N ASP A 29 -50.206 65.124 132.592 1.00124.72 N
ANISOU 10 N ASP A 29 16872 15734 14783 -1436 2063 1485 N
ATOM 11 CA ASP A 29 -49.814 63.878 131.930 1.00122.79 C
ANISOU 11 CA ASP A 29 16851 14987 14816 -1513 1839 1866 C
ATOM 12 C ASP A 29 -50.239 63.843 130.454 1.00118.40 C
ANISOU 12 C ASP A 29 16246 13954 14788 -1424 1638 1638 C
ATOM 13 O ASP A 29 -49.482 63.362 129.604 1.00116.07 O
ANISOU 13 O ASP A 29 16161 13244 14698 -1308 1358 1699 O
ATOM 14 CB ASP A 29 -50.400 62.682 132.709 1.00130.54 C
ANISOU 14 CB ASP A 29 17814 16049 15735 -1862 2033 2391 C
ATOM 15 CG ASP A 29 -50.361 61.350 131.940 1.00134.29 C
ANISOU 15 CG ASP A 29 18481 15892 16653 -2001 1849 2721 C
ATOM 16 OD1 ASP A 29 -49.272 60.921 131.499 1.00133.31 O
ANISOU 16 OD1 ASP A 29 18656 15420 16576 -1791 1550 2835 O
ATOM 17 OD2 ASP A 29 -51.429 60.705 131.822 1.00138.19 O
ANISOU 17 OD2 ASP A 29 18797 16264 17445 -2339 2016 2828 O
ATOM 18 N GLU A 30 -51.440 64.363 130.148 1.00112.91 N
ANISOU 18 N GLU A 30 15240 13394 14268 -1430 1766 1335 N
ATOM 19 CA GLU A 30 -51.951 64.406 128.774 1.00107.59 C
ANISOU 19 CA GLU A 30 14459 12404 14016 -1269 1576 1072 C
ATOM 20 C GLU A 30 -51.102 65.319 127.884 1.00 99.26 C
ANISOU 20 C GLU A 30 13638 11106 12969 -886 1363 823 C
ATOM 21 O GLU A 30 -50.889 65.021 126.703 1.00 96.67 O
ANISOU 21 O GLU A 30 13378 10439 12911 -740 1116 773 O
ATOM 22 CB GLU A 30 -53.417 64.875 128.767 1.00112.08 C
ANISOU 22 CB GLU A 30 14606 13311 14668 -1273 1758 744 C
ATOM 23 CG GLU A 30 -54.181 64.514 127.480 1.00115.41 C
ANISOU 23 CG GLU A 30 14804 13537 15511 -1178 1580 510 C
ATOM 24 CD GLU A 30 -55.512 65.246 127.281 1.00121.69 C
ANISOU 24 CD GLU A 30 15172 14733 16331 -988 1682 49 C
ATOM 25 OE1 GLU A 30 -56.287 65.404 128.250 1.00126.89 O
ANISOU 25 OE1 GLU A 30 15541 15866 16804 -1189 1963 -29 O
ATOM 26 OE2 GLU A 30 -55.784 65.645 126.127 1.00120.88 O
ANISOU 26 OE2 GLU A 30 15006 14520 16402 -597 1468 -250 O
ATOM 27 N PHE A 31 -50.624 66.439 128.441 1.00 93.79 N
ANISOU 27 N PHE A 31 13057 10600 11981 -746 1483 642 N
ATOM 28 CA PHE A 31 -49.795 67.382 127.690 1.00 88.08 C
ANISOU 28 CA PHE A 31 12592 9617 11258 -470 1368 419 C
ATOM 29 C PHE A 31 -48.467 66.746 127.271 1.00 89.92 C
ANISOU 29 C PHE A 31 13078 9605 11483 -508 1145 606 C
ATOM 30 O PHE A 31 -48.033 66.894 126.123 1.00 92.92 O
ANISOU 30 O PHE A 31 13597 9687 12021 -336 962 519 O
ATOM 31 CB PHE A 31 -49.553 68.650 128.525 1.00 84.22 C
ANISOU 31 CB PHE A 31 12156 9354 10491 -403 1591 143 C
ATOM 32 CG PHE A 31 -48.666 69.681 127.854 1.00 81.15 C
ANISOU 32 CG PHE A 31 12073 8644 10116 -216 1558 -88 C
ATOM 33 CD1 PHE A 31 -49.169 70.515 126.865 1.00 82.83 C
ANISOU 33 CD1 PHE A 31 12395 8552 10524 88 1540 -274 C
ATOM 34 CD2 PHE A 31 -47.334 69.819 128.219 1.00 79.03 C
ANISOU 34 CD2 PHE A 31 11984 8404 9641 -346 1565 -123 C
ATOM 35 CE1 PHE A 31 -48.357 71.458 126.245 1.00 82.79 C
ANISOU 35 CE1 PHE A 31 12734 8193 10530 207 1569 -418 C
ATOM 36 CE2 PHE A 31 -46.518 70.760 127.603 1.00 77.84 C
ANISOU 36 CE2 PHE A 31 12101 7957 9519 -275 1596 -355 C
ATOM 37 CZ PHE A 31 -47.031 71.579 126.616 1.00 80.21 C
ANISOU 37 CZ PHE A 31 12568 7872 10035 -25 1620 -467 C
ATOM 38 N LEU A 32 -47.813 66.031 128.199 1.00 91.04 N
ANISOU 38 N LEU A 32 13270 9924 11398 -691 1152 857 N
ATOM 39 CA LEU A 32 -46.533 65.369 127.941 1.00 90.89 C
ANISOU 39 CA LEU A 32 13456 9761 11317 -668 917 998 C
ATOM 40 C LEU A 32 -46.658 64.208 126.960 1.00 89.40 C
ANISOU 40 C LEU A 32 13280 9202 11487 -656 651 1180 C
ATOM 41 O LEU A 32 -45.653 63.777 126.385 1.00 87.34 O
ANISOU 41 O LEU A 32 13164 8778 11244 -553 403 1186 O
ATOM 42 CB LEU A 32 -45.928 64.874 129.262 1.00 95.59 C
ANISOU 42 CB LEU A 32 14094 10702 11524 -770 981 1233 C
ATOM 43 CG LEU A 32 -45.509 65.956 130.266 1.00 99.61 C
ANISOU 43 CG LEU A 32 14555 11667 11623 -764 1199 961 C
ATOM 44 CD1 LEU A 32 -45.268 65.366 131.650 1.00104.74 C
ANISOU 44 CD1 LEU A 32 15173 12783 11839 -826 1284 1243 C
ATOM 45 CD2 LEU A 32 -44.274 66.713 129.781 1.00 95.66 C
ANISOU 45 CD2 LEU A 32 14182 11126 11037 -667 1112 600 C
ATOM 46 N ARG A 33 -47.879 63.692 126.777 1.00 88.69 N
ANISOU 46 N ARG A 33 12997 9021 11682 -770 703 1262 N
ATOM 47 CA ARG A 33 -48.151 62.665 125.780 1.00 85.05 C
ANISOU 47 CA ARG A 33 12479 8210 11625 -778 471 1313 C
ATOM 48 C ARG A 33 -48.238 63.272 124.381 1.00 82.18 C
ANISOU 48 C ARG A 33 12057 7725 11443 -508 306 981 C
ATOM 49 O ARG A 33 -47.650 62.732 123.435 1.00 82.87 O
ANISOU 49 O ARG A 33 12202 7591 11693 -389 29 938 O
ATOM 50 CB ARG A 33 -49.437 61.916 126.155 1.00 85.32 C
ANISOU 50 CB ARG A 33 12279 8247 11894 -1069 638 1452 C
ATOM 51 CG ARG A 33 -49.274 60.996 127.373 1.00 89.27 C
ANISOU 51 CG ARG A 33 12920 8756 12243 -1350 780 1913 C
ATOM 52 CD ARG A 33 -50.557 60.252 127.722 1.00 97.02 C
ANISOU 52 CD ARG A 33 13677 9719 13470 -1740 1017 2061 C
ATOM 53 NE ARG A 33 -50.305 59.068 128.544 1.00103.43 N
ANISOU 53 NE ARG A 33 14735 10311 14252 -2002 1099 2593 N
ATOM 54 CZ ARG A 33 -50.014 57.866 128.055 1.00106.97 C
ANISOU 54 CZ ARG A 33 15371 10207 15066 -2070 903 2783 C
ATOM 55 NH1 ARG A 33 -49.928 57.683 126.744 1.00103.07 N
ANISOU 55 NH1 ARG A 33 14779 9409 14976 -1910 603 2433 N
ATOM 56 NH2 ARG A 33 -49.805 56.844 128.875 1.00113.82 N
ANISOU 56 NH2 ARG A 33 16542 10823 15881 -2268 1006 3326 N
ATOM 57 N TYR A 34 -48.922 64.419 124.243 1.00 79.65 N
ANISOU 57 N TYR A 34 11638 7567 11056 -362 467 747 N
ATOM 58 CA TYR A 34 -48.995 65.114 122.960 1.00 77.80 C
ANISOU 58 CA TYR A 34 11420 7233 10906 -33 337 500 C
ATOM 59 C TYR A 34 -47.700 65.857 122.631 1.00 76.24 C
ANISOU 59 C TYR A 34 11538 6942 10488 91 299 458 C
ATOM 60 O TYR A 34 -47.371 66.011 121.452 1.00 78.91 O
ANISOU 60 O TYR A 34 11947 7155 10880 305 132 364 O
ATOM 61 CB TYR A 34 -50.226 66.045 122.926 1.00 79.78 C
ANISOU 61 CB TYR A 34 11493 7662 11156 158 507 281 C
ATOM 62 CG TYR A 34 -51.497 65.217 122.885 1.00 88.89 C
ANISOU 62 CG TYR A 34 12244 8962 12568 36 501 212 C
ATOM 63 CD1 TYR A 34 -52.321 65.103 123.997 1.00 95.04 C
ANISOU 63 CD1 TYR A 34 12801 10010 13299 -229 754 239 C
ATOM 64 CD2 TYR A 34 -51.815 64.464 121.758 1.00 93.49 C
ANISOU 64 CD2 TYR A 34 12631 9454 13436 129 256 88 C
ATOM 65 CE1 TYR A 34 -53.453 64.296 123.974 1.00101.35 C
ANISOU 65 CE1 TYR A 34 13202 10961 14346 -443 798 148 C
ATOM 66 CE2 TYR A 34 -52.943 63.653 121.726 1.00 99.30 C
ANISOU 66 CE2 TYR A 34 12954 10328 14446 -63 276 -52 C
ATOM 67 CZ TYR A 34 -53.759 63.574 122.837 1.00103.36 C
ANISOU 67 CZ TYR A 34 13262 11084 14925 -377 564 -16 C
ATOM 68 OH TYR A 34 -54.882 62.773 122.814 1.00108.32 O
ANISOU 68 OH TYR A 34 13450 11874 15831 -654 638 -191 O
ATOM 69 N LEU A 35 -46.936 66.281 123.653 1.00 73.01 N
ANISOU 69 N LEU A 35 11286 6647 9809 -62 463 497 N
ATOM 70 CA LEU A 35 -45.606 66.854 123.421 1.00 69.89 C
ANISOU 70 CA LEU A 35 11131 6213 9211 -46 450 397 C
ATOM 71 C LEU A 35 -44.667 65.813 122.824 1.00 70.82 C
ANISOU 71 C LEU A 35 11267 6270 9373 -48 148 470 C
ATOM 72 O LEU A 35 -43.860 66.122 121.936 1.00 69.06 O
ANISOU 72 O LEU A 35 11154 5991 9093 40 55 342 O
ATOM 73 CB LEU A 35 -45.030 67.394 124.736 1.00 68.89 C
ANISOU 73 CB LEU A 35 11068 6324 8785 -225 674 335 C
ATOM 74 CG LEU A 35 -43.622 68.009 124.750 1.00 66.82 C
ANISOU 74 CG LEU A 35 10977 6125 8287 -303 721 130 C
ATOM 75 CD1 LEU A 35 -43.639 69.435 124.236 1.00 64.98 C
ANISOU 75 CD1 LEU A 35 10938 5679 8074 -254 948 -103 C
ATOM 76 CD2 LEU A 35 -43.021 67.973 126.142 1.00 68.54 C
ANISOU 76 CD2 LEU A 35 11131 6721 8189 -462 831 75 C
ATOM 77 N TRP A 36 -44.772 64.575 123.314 1.00 72.33 N
ANISOU 77 N TRP A 36 11360 6463 9658 -146 9 676 N
ATOM 78 CA TRP A 36 -43.996 63.446 122.815 1.00 67.33 C
ANISOU 78 CA TRP A 36 10743 5723 9118 -92 -312 733 C
ATOM 79 C TRP A 36 -44.407 63.085 121.384 1.00 67.05 C
ANISOU 79 C TRP A 36 10585 5499 9391 73 -536 606 C
ATOM 80 O TRP A 36 -43.571 63.056 120.472 1.00 70.53 O
ANISOU 80 O TRP A 36 11058 5954 9787 212 -733 452 O
ATOM 81 CB TRP A 36 -44.192 62.252 123.767 1.00 64.29 C
ANISOU 81 CB TRP A 36 10356 5280 8793 -222 -356 1040 C
ATOM 82 CG TRP A 36 -43.572 61.000 123.259 1.00 65.18 C
ANISOU 82 CG TRP A 36 10511 5172 9082 -118 -702 1100 C
ATOM 83 CD1 TRP A 36 -44.212 59.923 122.714 1.00 64.46 C
ANISOU 83 CD1 TRP A 36 10331 4745 9416 -142 -870 1164 C
ATOM 84 CD2 TRP A 36 -42.173 60.713 123.193 1.00 68.17 C
ANISOU 84 CD2 TRP A 36 11003 5662 9237 48 -937 1016 C
ATOM 85 NE1 TRP A 36 -43.292 58.978 122.324 1.00 64.98 N
ANISOU 85 NE1 TRP A 36 10486 4646 9556 24 -1206 1143 N
ATOM 86 CE2 TRP A 36 -42.034 59.440 122.607 1.00 63.65 C
ANISOU 86 CE2 TRP A 36 10432 4782 8971 169 -1265 1055 C
ATOM 87 CE3 TRP A 36 -41.023 61.409 123.579 1.00 69.28 C
ANISOU 87 CE3 TRP A 36 11205 6166 8951 102 -900 846 C
ATOM 88 CZ2 TRP A 36 -40.788 58.849 122.396 1.00 66.41 C
ANISOU 88 CZ2 TRP A 36 10854 5190 9189 405 -1584 944 C
ATOM 89 CZ3 TRP A 36 -39.789 60.821 123.370 1.00 68.41 C
ANISOU 89 CZ3 TRP A 36 11126 6177 8690 298 -1199 719 C
ATOM 90 CH2 TRP A 36 -39.681 59.554 122.784 1.00 66.63 C
ANISOU 90 CH2 TRP A 36 10911 5654 8751 479 -1551 777 C
ATOM 91 N ARG A 37 -45.707 62.849 121.187 1.00 64.22 N
ANISOU 91 N ARG A 37 10038 5053 9310 59 -494 619 N
ATOM 92 CA ARG A 37 -46.285 62.472 119.899 1.00 65.65 C
ANISOU 92 CA ARG A 37 10015 5151 9776 234 -702 435 C
ATOM 93 C ARG A 37 -46.012 63.519 118.805 1.00 73.38 C
ANISOU 93 C ARG A 37 11061 6239 10581 518 -721 251 C
ATOM 94 O ARG A 37 -45.554 63.172 117.709 1.00 77.07 O
ANISOU 94 O ARG A 37 11470 6723 11090 692 -970 112 O
ATOM 95 CB ARG A 37 -47.791 62.254 120.108 1.00 67.25 C
ANISOU 95 CB ARG A 37 9952 5367 10233 135 -574 411 C
ATOM 96 CG ARG A 37 -48.644 62.010 118.880 1.00 70.14 C
ANISOU 96 CG ARG A 37 10009 5779 10864 337 -748 126 C
ATOM 97 CD ARG A 37 -50.121 61.882 119.262 1.00 79.79 C
ANISOU 97 CD ARG A 37 10910 7121 12286 193 -572 32 C
ATOM 98 NE ARG A 37 -50.504 60.491 119.491 1.00 90.85 N
ANISOU 98 NE ARG A 37 12126 8314 14077 -150 -624 54 N
ATOM 99 CZ ARG A 37 -51.728 60.090 119.823 1.00101.13 C
ANISOU 99 CZ ARG A 37 13103 9701 15620 -412 -455 -54 C
ATOM 100 NH1 ARG A 37 -52.705 60.973 119.976 1.00104.54 N
ANISOU 100 NH1 ARG A 37 13314 10500 15908 -306 -263 -225 N
ATOM 101 NH2 ARG A 37 -51.974 58.799 120.002 1.00105.95 N
ANISOU 101 NH2 ARG A 37 13611 10021 16624 -786 -466 -13 N
ATOM 102 N ASP A 38 -46.275 64.805 119.100 1.00 73.53 N
ANISOU 102 N ASP A 38 11224 6324 10392 573 -447 256 N
ATOM 103 CA ASP A 38 -46.251 65.903 118.126 1.00 70.51 C
ANISOU 103 CA ASP A 38 10983 5956 9852 859 -392 163 C
ATOM 104 C ASP A 38 -44.892 66.599 117.948 1.00 64.19 C
ANISOU 104 C ASP A 38 10484 5133 8774 792 -303 166 C
ATOM 105 O ASP A 38 -44.726 67.338 116.972 1.00 57.36 O
ANISOU 105 O ASP A 38 9775 4244 7776 998 -265 144 O
ATOM 106 CB ASP A 38 -47.281 66.981 118.515 1.00 70.29 C
ANISOU 106 CB ASP A 38 11003 5928 9778 997 -131 148 C
ATOM 107 CG ASP A 38 -48.719 66.471 118.517 1.00 70.45 C
ANISOU 107 CG ASP A 38 10658 6081 10028 1096 -193 51 C
ATOM 108 OD1 ASP A 38 -48.973 65.361 118.003 1.00 67.46 O
ANISOU 108 OD1 ASP A 38 10002 5751 9879 1071 -430 -25 O
ATOM 109 OD2 ASP A 38 -49.597 67.195 119.040 1.00 69.78 O
ANISOU 109 OD2 ASP A 38 10537 6072 9903 1190 3 -6 O
ATOM 110 N TYR A 39 -43.924 66.405 118.871 1.00 59.03 N
ANISOU 110 N TYR A 39 9908 4523 7996 510 -247 183 N
ATOM 111 CA TYR A 39 -42.632 67.104 118.825 1.00 61.46 C
ANISOU 111 CA TYR A 39 10431 4887 8033 372 -117 87 C
ATOM 112 C TYR A 39 -41.422 66.237 119.235 1.00 70.63 C
ANISOU 112 C TYR A 39 11508 6247 9081 214 -303 11 C
ATOM 113 O TYR A 39 -40.492 66.074 118.435 1.00 73.65 O
ANISOU 113 O TYR A 39 11877 6758 9350 238 -443 -123 O
ATOM 114 CB TYR A 39 -42.680 68.382 119.692 1.00 62.56 C
ANISOU 114 CB TYR A 39 10783 4947 8039 224 268 46 C
ATOM 115 CG TYR A 39 -41.321 69.041 119.835 1.00 60.51 C
ANISOU 115 CG TYR A 39 10689 4767 7534 -31 447 -134 C
ATOM 116 CD1 TYR A 39 -40.770 69.779 118.793 1.00 63.48 C
ANISOU 116 CD1 TYR A 39 11275 5035 7810 -37 568 -182 C
ATOM 117 CD2 TYR A 39 -40.570 68.887 120.994 1.00 57.46 C
ANISOU 117 CD2 TYR A 39 10223 4621 6987 -273 503 -273 C
ATOM 118 CE1 TYR A 39 -39.512 70.352 118.905 1.00 65.86 C
ANISOU 118 CE1 TYR A 39 11683 5441 7902 -359 773 -400 C
ATOM 119 CE2 TYR A 39 -39.312 69.457 121.115 1.00 58.29 C
ANISOU 119 CE2 TYR A 39 10394 4891 6864 -530 665 -543 C
ATOM 120 CZ TYR A 39 -38.788 70.188 120.068 1.00 65.82 C
ANISOU 120 CZ TYR A 39 11535 5708 7767 -613 815 -624 C
ATOM 121 OH TYR A 39 -37.540 70.758 120.182 1.00 70.66 O
ANISOU 121 OH TYR A 39 12174 6507 8166 -954 1024 -943 O
ATOM 122 N LEU A 40 -41.419 65.667 120.454 1.00 66.66 N
ANISOU 122 N LEU A 40 9372 7532 8423 189 -278 -1792 N
ATOM 123 CA LEU A 40 -40.238 64.970 120.986 1.00 68.99 C
ANISOU 123 CA LEU A 40 9541 7878 8794 -42 -596 -1918 C
ATOM 124 C LEU A 40 -39.900 63.696 120.201 1.00 67.34 C
ANISOU 124 C LEU A 40 9089 7846 8652 19 -809 -1793 C
ATOM 125 O LEU A 40 -38.723 63.442 119.904 1.00 67.60 O
ANISOU 125 O LEU A 40 8954 7846 8884 -99 -941 -1871 O
ATOM 126 CB LEU A 40 -40.434 64.644 122.475 1.00 65.30 C
ANISOU 126 CB LEU A 40 9208 7490 8114 -192 -814 -2041 C
ATOM 127 CG LEU A 40 -40.255 65.786 123.488 1.00 61.32 C
ANISOU 127 CG LEU A 40 8924 6796 7577 -357 -701 -2240 C
ATOM 128 CD1 LEU A 40 -40.661 65.356 124.891 1.00 65.64 C
ANISOU 128 CD1 LEU A 40 9642 7438 7860 -480 -899 -2329 C
ATOM 129 CD2 LEU A 40 -38.827 66.325 123.498 1.00 55.20 C
ANISOU 129 CD2 LEU A 40 8076 5859 7039 -566 -751 -2421 C
ATOM 130 N TYR A 41 -40.917 62.859 119.882 1.00 65.98 N
ANISOU 130 N TYR A 41 8885 7866 8317 195 -848 -1615 N
ATOM 131 CA TYR A 41 -40.684 61.639 119.097 1.00 59.81 C
ANISOU 131 CA TYR A 41 7896 7246 7582 262 -1031 -1487 C
ATOM 132 C TYR A 41 -40.312 61.937 117.641 1.00 61.14 C
ANISOU 132 C TYR A 41 7944 7326 7961 373 -834 -1389 C
ATOM 133 O TYR A 41 -39.287 61.414 117.171 1.00 59.85 O
ANISOU 133 O TYR A 41 7600 7166 7973 296 -965 -1419 O
ATOM 134 CB TYR A 41 -41.888 60.690 119.198 1.00 47.49 C
ANISOU 134 CB TYR A 41 6353 5911 5781 389 -1110 -1344 C
ATOM 135 CG TYR A 41 -41.840 59.534 118.199 1.00 47.27 C
ANISOU 135 CG TYR A 41 6136 6037 5790 493 -1234 -1186 C
ATOM 136 CD1 TYR A 41 -41.086 58.388 118.451 1.00 42.74 C
ANISOU 136 CD1 TYR A 41 5456 5556 5228 388 -1558 -1212 C
ATOM 137 CD2 TYR A 41 -42.518 59.608 116.987 1.00 48.85 C
ANISOU 137 CD2 TYR A 41 6276 6274 6012 703 -1034 -1018 C
ATOM 138 CE1 TYR A 41 -41.018 57.349 117.522 1.00 43.09 C
ANISOU 138 CE1 TYR A 41 5339 5723 5311 481 -1655 -1075 C
ATOM 139 CE2 TYR A 41 -42.454 58.578 116.056 1.00 46.72 C
ANISOU 139 CE2 TYR A 41 5846 6133 5770 785 -1136 -880 C
ATOM 140 CZ TYR A 41 -41.705 57.451 116.328 1.00 50.55 C
ANISOU 140 CZ TYR A 41 6227 6706 6272 669 -1435 -911 C
ATOM 141 OH TYR A 41 -41.644 56.427 115.404 1.00 57.22 O
ANISOU 141 OH TYR A 41 6927 7670 7145 751 -1525 -780 O
ATOM 142 N PRO A 42 -41.070 62.743 116.868 1.00 61.58 N
ANISOU 142 N PRO A 42 8098 7293 8008 555 -528 -1279 N
ATOM 143 CA PRO A 42 -40.630 63.067 115.494 1.00 62.40 C
ANISOU 143 CA PRO A 42 8142 7277 8291 636 -337 -1192 C
ATOM 144 C PRO A 42 -39.218 63.586 115.264 1.00 62.93 C
ANISOU 144 C PRO A 42 8165 7144 8601 425 -279 -1360 C
ATOM 145 O PRO A 42 -38.591 63.252 114.251 1.00 64.98 O
ANISOU 145 O PRO A 42 8291 7368 9030 407 -237 -1331 O
ATOM 146 CB PRO A 42 -41.656 64.097 114.999 1.00 61.16 C
ANISOU 146 CB PRO A 42 8182 7002 8056 852 -30 -1091 C
ATOM 147 CG PRO A 42 -42.766 64.062 115.929 1.00 60.15 C
ANISOU 147 CG PRO A 42 8141 6996 7718 924 -72 -1099 C
ATOM 148 CD PRO A 42 -42.336 63.420 117.218 1.00 61.14 C
ANISOU 148 CD PRO A 42 8225 7228 7779 700 -343 -1242 C
ATOM 149 N LYS A 43 -38.728 64.448 116.162 1.00 59.40 N
ANISOU 149 N LYS A 43 7833 6561 8175 256 -249 -1547 N
ATOM 150 CA LYS A 43 -37.354 64.943 116.064 1.00 61.15 C
ANISOU 150 CA LYS A 43 7997 6604 8632 23 -197 -1745 C
ATOM 151 C LYS A 43 -36.287 63.911 116.474 1.00 64.28 C
ANISOU 151 C LYS A 43 8119 7143 9161 -126 -531 -1852 C
ATOM 152 O LYS A 43 -35.247 63.753 115.823 1.00 68.56 O
ANISOU 152 O LYS A 43 8485 7632 9933 -208 -489 -1909 O
ATOM 153 CB LYS A 43 -37.176 66.150 116.997 1.00 65.43 C
ANISOU 153 CB LYS A 43 8735 6986 9138 -127 -114 -1928 C
ATOM 154 CG LYS A 43 -38.048 67.363 116.660 1.00 69.38 C
ANISOU 154 CG LYS A 43 9484 7213 9665 -75 291 -1917 C
ATOM 155 CD LYS A 43 -37.733 68.519 117.604 1.00 81.24 C
ANISOU 155 CD LYS A 43 11036 8496 11336 -359 392 -2170 C
ATOM 156 CE LYS A 43 -36.367 69.138 117.332 1.00 91.96 C
ANISOU 156 CE LYS A 43 12541 9569 12832 -373 785 -2163 C
ATOM 157 NZ LYS A 43 -36.313 69.849 116.027 1.00 99.81 N
ANISOU 157 NZ LYS A 43 13882 10355 13684 -233 1076 -2105 N
ATOM 158 N GLN A 44 -36.606 63.153 117.526 1.00 68.38 N
ANISOU 158 N GLN A 44 8614 7838 9530 -153 -860 -1882 N
ATOM 159 CA GLN A 44 -35.786 62.041 118.006 1.00 69.02 C
ANISOU 159 CA GLN A 44 8470 8061 9693 -249 -1235 -1970 C
ATOM 160 C GLN A 44 -35.648 61.065 116.833 1.00 65.04 C
ANISOU 160 C GLN A 44 7763 7669 9281 -122 -1272 -1822 C
ATOM 161 O GLN A 44 -34.541 60.607 116.527 1.00 65.57 O
ANISOU 161 O GLN A 44 7596 7747 9571 -211 -1407 -1932 O
ATOM 162 CB GLN A 44 -36.368 61.342 119.237 1.00 77.84 C
ANISOU 162 CB GLN A 44 9700 9328 10548 -253 -1537 -1967 C
ATOM 163 CG GLN A 44 -35.468 60.442 120.045 1.00 88.72 C
ANISOU 163 CG GLN A 44 10956 10799 11955 -379 -1967 -2110 C
ATOM 164 CD GLN A 44 -36.186 59.954 121.289 1.00 95.17 C
ANISOU 164 CD GLN A 44 11989 11715 12459 -395 -2197 -2097 C
ATOM 165 OE1 GLN A 44 -36.240 60.653 122.302 1.00 99.03 O
ANISOU 165 OE1 GLN A 44 12660 12118 12847 -521 -2196 -2230 O
ATOM 166 NE2 GLN A 44 -36.778 58.769 121.206 1.00 94.81 N
ANISOU 166 NE2 GLN A 44 11946 11837 12240 -280 -2369 -1939 N
ATOM 167 N TYR A 45 -36.775 60.731 116.185 1.00 58.72 N
ANISOU 167 N TYR A 45 7041 6958 8314 87 -1158 -1587 N
ATOM 168 CA TYR A 45 -36.806 59.843 115.019 1.00 54.43 C
ANISOU 168 CA TYR A 45 6343 6517 7820 218 -1164 -1427 C
ATOM 169 C TYR A 45 -35.914 60.371 113.897 1.00 55.92 C
ANISOU 169 C TYR A 45 6423 6547 8277 168 -922 -1472 C
ATOM 170 O TYR A 45 -35.013 59.671 113.417 1.00 58.40 O
ANISOU 170 O TYR A 45 6511 6904 8774 115 -1038 -1527 O
ATOM 171 CB TYR A 45 -38.261 59.706 114.532 1.00 54.86 C
ANISOU 171 CB TYR A 45 6533 6666 7645 443 -1029 -1191 C
ATOM 172 CG TYR A 45 -38.531 58.830 113.302 1.00 57.13 C
ANISOU 172 CG TYR A 45 6706 7067 7932 597 -1017 -1002 C
ATOM 173 CD1 TYR A 45 -39.337 57.697 113.393 1.00 52.97 C
ANISOU 173 CD1 TYR A 45 6158 6759 7209 701 -1207 -869 C
ATOM 174 CD2 TYR A 45 -38.022 59.161 112.048 1.00 65.79 C
ANISOU 174 CD2 TYR A 45 7746 8044 9207 625 -796 -961 C
ATOM 175 CE1 TYR A 45 -39.603 56.906 112.276 1.00 55.75 C
ANISOU 175 CE1 TYR A 45 6418 7214 7551 832 -1195 -704 C
ATOM 176 CE2 TYR A 45 -38.279 58.374 110.932 1.00 67.64 C
ANISOU 176 CE2 TYR A 45 7900 8376 9423 758 -782 -793 C
ATOM 177 CZ TYR A 45 -39.070 57.252 111.050 1.00 65.06 C
ANISOU 177 CZ TYR A 45 7539 8273 8907 865 -988 -665 C
ATOM 178 OH TYR A 45 -39.321 56.483 109.933 1.00 71.32 O
ANISOU 178 OH TYR A 45 8261 9159 9678 986 -972 -506 O
ATOM 179 N ALA A 46 -36.165 61.612 113.472 1.00 57.10 N
ANISOU 179 N ALA A 46 6749 6501 8446 182 -573 -1457 N
ATOM 180 CA ALA A 46 -35.413 62.238 112.390 1.00 58.38 C
ANISOU 180 CA ALA A 46 6882 6474 8824 117 -284 -1495 C
ATOM 181 C ALA A 46 -33.932 62.392 112.727 1.00 62.92 C
ANISOU 181 C ALA A 46 7257 6972 9678 -147 -348 -1771 C
ATOM 182 O ALA A 46 -33.086 62.310 111.832 1.00 66.71 O
ANISOU 182 O ALA A 46 7584 7388 10374 -225 -221 -1829 O
ATOM 183 CB ALA A 46 -36.020 63.605 112.062 1.00 58.79 C
ANISOU 183 CB ALA A 46 7230 6302 8805 181 83 -1435 C
ATOM 184 N TRP A 47 -33.599 62.636 114.004 1.00 63.74 N
ANISOU 184 N TRP A 47 7357 7080 9782 -294 -537 -1960 N
ATOM 185 CA TRP A 47 -32.192 62.718 114.396 1.00 65.04 C
ANISOU 185 CA TRP A 47 7295 7202 10217 -539 -652 -2249 C
ATOM 186 C TRP A 47 -31.488 61.380 114.175 1.00 72.24 C
ANISOU 186 C TRP A 47 7887 8296 11265 -522 -962 -2285 C
ATOM 187 O TRP A 47 -30.463 61.313 113.486 1.00 75.34 O
ANISOU 187 O TRP A 47 8049 8644 11934 -629 -877 -2420 O
ATOM 188 CB TRP A 47 -32.054 63.154 115.863 1.00 63.54 C
ANISOU 188 CB TRP A 47 7182 6998 9961 -682 -846 -2435 C
ATOM 189 CG TRP A 47 -30.620 63.504 116.226 1.00 74.09 C
ANISOU 189 CG TRP A 47 8299 8261 11589 -949 -916 -2761 C
ATOM 190 CD1 TRP A 47 -30.051 64.747 116.204 1.00 79.98 C
ANISOU 190 CD1 TRP A 47 9108 8791 12488 -1156 -626 -2948 C
ATOM 191 CD2 TRP A 47 -29.576 62.595 116.617 1.00 79.16 C
ANISOU 191 CD2 TRP A 47 8615 9047 12415 -1032 -1299 -2950 C
ATOM 192 NE1 TRP A 47 -28.727 64.671 116.567 1.00 83.36 N
ANISOU 192 NE1 TRP A 47 9245 9236 13190 -1380 -799 -3255 N
ATOM 193 CE2 TRP A 47 -28.409 63.363 116.824 1.00 83.52 C
ANISOU 193 CE2 TRP A 47 9018 9482 13235 -1289 -1221 -3256 C
ATOM 194 CE3 TRP A 47 -29.515 61.212 116.819 1.00 77.97 C
ANISOU 194 CE3 TRP A 47 8298 9108 12219 -904 -1698 -2889 C
ATOM 195 CZ2 TRP A 47 -27.198 62.792 117.222 1.00 86.01 C
ANISOU 195 CZ2 TRP A 47 9094 9964 13623 -1301 -1444 -3303 C
ATOM 196 CZ3 TRP A 47 -28.310 60.647 117.214 1.00 79.78 C
ANISOU 196 CZ3 TRP A 47 8342 9461 12508 -911 -1876 -2916 C
ATOM 197 CH2 TRP A 47 -27.169 61.437 117.411 1.00 83.03 C
ANISOU 197 CH2 TRP A 47 8630 9796 13123 -1101 -1766 -3135 C
ATOM 198 N VAL A 48 -32.057 60.305 114.748 1.00 73.38 N
ANISOU 198 N VAL A 48 8029 8639 11214 -389 -1305 -2171 N
ATOM 199 CA VAL A 48 -31.521 58.941 114.661 1.00 68.78 C
ANISOU 199 CA VAL A 48 7194 8228 10713 -339 -1642 -2185 C
ATOM 200 C VAL A 48 -31.411 58.486 113.205 1.00 65.90 C
ANISOU 200 C VAL A 48 6699 7871 10468 -243 -1447 -2059 C
ATOM 201 O VAL A 48 -30.419 57.860 112.808 1.00 66.23 O
ANISOU 201 O VAL A 48 6461 7953 10749 -289 -1559 -2184 O
ATOM 202 CB VAL A 48 -32.403 57.980 115.496 1.00 59.03 C
ANISOU 202 CB VAL A 48 6088 7167 9174 -209 -1976 -2043 C
ATOM 203 CG1 VAL A 48 -32.005 56.508 115.308 1.00 55.05 C
ANISOU 203 CG1 VAL A 48 5461 6815 8640 -99 -2193 -1924 C
ATOM 204 CG2 VAL A 48 -32.358 58.337 116.986 1.00 58.35 C
ANISOU 204 CG2 VAL A 48 6133 7066 8970 -329 -2199 -2196 C
ATOM 205 N LEU A 49 -32.429 58.804 112.389 1.00 58.81 N
ANISOU 205 N LEU A 49 6006 6933 9406 -104 -1156 -1821 N
ATOM 206 CA LEU A 49 -32.447 58.445 110.971 1.00 53.16 C
ANISOU 206 CA LEU A 49 5230 6211 8757 -9 -951 -1680 C
ATOM 207 C LEU A 49 -31.283 59.080 110.201 1.00 55.94 C
ANISOU 207 C LEU A 49 5440 6392 9424 -183 -675 -1863 C
ATOM 208 O LEU A 49 -30.569 58.388 109.466 1.00 61.53 O
ANISOU 208 O LEU A 49 5920 7141 10318 -199 -688 -1910 O
ATOM 209 CB LEU A 49 -33.794 58.849 110.352 1.00 52.42 C
ANISOU 209 CB LEU A 49 5416 6089 8412 175 -705 -1412 C
ATOM 210 CG LEU A 49 -34.014 58.630 108.847 1.00 53.53 C
ANISOU 210 CG LEU A 49 5577 6202 8560 292 -468 -1235 C
ATOM 211 CD1 LEU A 49 -33.920 57.158 108.485 1.00 55.63 C
ANISOU 211 CD1 LEU A 49 5647 6664 8824 376 -714 -1159 C
ATOM 212 CD2 LEU A 49 -35.354 59.193 108.383 1.00 52.92 C
ANISOU 212 CD2 LEU A 49 5790 6087 8231 484 -260 -1000 C
ATOM 213 N ILE A 50 -31.091 60.402 110.349 1.00 56.61 N
ANISOU 213 N ILE A 50 5667 6274 9568 -325 -402 -1976 N
ATOM 214 CA ILE A 50 -30.002 61.103 109.659 1.00 60.08 C
ANISOU 214 CA ILE A 50 6005 6529 10294 -532 -94 -2171 C
ATOM 215 C ILE A 50 -28.637 60.662 110.212 1.00 67.28 C
ANISOU 215 C ILE A 50 6536 7515 11511 -721 -340 -2489 C
ATOM 216 O ILE A 50 -27.705 60.393 109.445 1.00 77.49 O
ANISOU 216 O ILE A 50 7588 8790 13066 -818 -229 -2623 O
ATOM 217 CB ILE A 50 -30.200 62.642 109.731 1.00 55.38 C
ANISOU 217 CB ILE A 50 5702 5681 9658 -642 263 -2209 C
ATOM 218 CG1 ILE A 50 -31.543 63.068 109.098 1.00 53.65 C
ANISOU 218 CG1 ILE A 50 5849 5382 9152 -414 490 -1899 C
ATOM 219 CG2 ILE A 50 -29.059 63.394 109.013 1.00 53.59 C
ANISOU 219 CG2 ILE A 50 5400 5244 9719 -896 619 -2426 C
ATOM 220 CD1 ILE A 50 -32.065 64.482 109.486 1.00 52.96 C
ANISOU 220 CD1 ILE A 50 6105 5074 8945 -439 741 -1897 C
ATOM 221 N ALA A 51 -28.514 60.548 111.545 1.00 62.94 N
ANISOU 221 N ALA A 51 5930 7058 10928 -764 -688 -2622 N
ATOM 222 CA ALA A 51 -27.263 60.109 112.177 1.00 66.80 C
ANISOU 222 CA ALA A 51 6061 7630 11690 -911 -992 -2932 C
ATOM 223 C ALA A 51 -26.833 58.719 111.701 1.00 70.56 C
ANISOU 223 C ALA A 51 6362 8290 12156 -720 -1171 -2805 C
ATOM 224 O ALA A 51 -25.649 58.489 111.427 1.00 73.38 O
ANISOU 224 O ALA A 51 6527 8669 12687 -754 -1125 -2928 O
ATOM 225 CB ALA A 51 -27.414 60.118 113.701 1.00 69.00 C
ANISOU 225 CB ALA A 51 6473 8002 11743 -881 -1315 -2932 C
ATOM 226 N ALA A 52 -27.787 57.780 111.620 1.00 63.50 N
ANISOU 226 N ALA A 52 5568 7519 11039 -513 -1361 -2563 N
ATOM 227 CA ALA A 52 -27.499 56.426 111.144 1.00 58.45 C
ANISOU 227 CA ALA A 52 4867 7011 10331 -332 -1483 -2411 C
ATOM 228 C ALA A 52 -27.062 56.430 109.682 1.00 61.62 C
ANISOU 228 C ALA A 52 5093 7340 10980 -378 -1182 -2457 C
ATOM 229 O ALA A 52 -26.123 55.717 109.306 1.00 65.46 O
ANISOU 229 O ALA A 52 5457 7863 11551 -337 -1194 -2500 O
ATOM 230 CB ALA A 52 -28.732 55.535 111.326 1.00 49.75 C
ANISOU 230 CB ALA A 52 3975 6032 8894 -133 -1670 -2123 C
ATOM 231 N TYR A 53 -27.736 57.233 108.846 1.00 59.43 N
ANISOU 231 N TYR A 53 4882 6934 10765 -449 -859 -2414 N
ATOM 232 CA TYR A 53 -27.381 57.332 107.433 1.00 60.56 C
ANISOU 232 CA TYR A 53 4982 6975 11054 -492 -480 -2394 C
ATOM 233 C TYR A 53 -26.020 58.000 107.231 1.00 68.03 C
ANISOU 233 C TYR A 53 5683 7791 12375 -763 -258 -2738 C
ATOM 234 O TYR A 53 -25.235 57.561 106.382 1.00 73.07 O
ANISOU 234 O TYR A 53 6173 8430 13161 -775 -116 -2799 O
ATOM 235 CB TYR A 53 -28.469 58.085 106.655 1.00 62.18 C
ANISOU 235 CB TYR A 53 5580 7043 11001 -408 -111 -2119 C
ATOM 236 CG TYR A 53 -29.480 57.180 105.972 1.00 63.44 C
ANISOU 236 CG TYR A 53 5868 7324 10914 -162 -173 -1805 C
ATOM 237 CD1 TYR A 53 -29.144 56.494 104.811 1.00 66.06 C
ANISOU 237 CD1 TYR A 53 6088 7669 11342 -132 -50 -1762 C
ATOM 238 CD2 TYR A 53 -30.779 57.054 106.451 1.00 60.98 C
ANISOU 238 CD2 TYR A 53 5792 7106 10273 24 -325 -1567 C
ATOM 239 CE1 TYR A 53 -30.055 55.669 104.175 1.00 64.80 C
ANISOU 239 CE1 TYR A 53 6047 7620 10953 77 -108 -1487 C
ATOM 240 CE2 TYR A 53 -31.701 56.236 105.814 1.00 57.75 C
ANISOU 240 CE2 TYR A 53 5480 6816 9646 230 -376 -1304 C
ATOM 241 CZ TYR A 53 -31.334 55.548 104.677 1.00 61.45 C
ANISOU 241 CZ TYR A 53 5839 7298 10210 255 -274 -1261 C
ATOM 242 OH TYR A 53 -32.249 54.737 104.044 1.00 61.82 O
ANISOU 242 OH TYR A 53 5988 7467 10035 446 -330 -1009 O
ATOM 243 N VAL A 54 -25.722 59.066 107.993 1.00 67.94 N
ANISOU 243 N VAL A 54 5721 7669 12425 -945 -192 -2921 N
ATOM 244 CA VAL A 54 -24.440 59.761 107.863 1.00 66.16 C
ANISOU 244 CA VAL A 54 5371 7349 12419 -1149 53 -3180 C
ATOM 245 C VAL A 54 -23.293 58.875 108.352 1.00 72.29 C
ANISOU 245 C VAL A 54 5918 8309 13238 -1037 -247 -3285 C
ATOM 246 O VAL A 54 -22.253 58.764 107.682 1.00 75.56 O
ANISOU 246 O VAL A 54 6159 8705 13847 -1099 -68 -3438 O
ATOM 247 CB VAL A 54 -24.480 61.125 108.600 1.00 60.64 C
ANISOU 247 CB VAL A 54 4834 6489 11717 -1353 199 -3316 C
ATOM 248 CG1 VAL A 54 -23.087 61.768 108.683 1.00 61.03 C
ANISOU 248 CG1 VAL A 54 4726 6506 11958 -1541 378 -3584 C
ATOM 249 CG2 VAL A 54 -25.443 62.093 107.906 1.00 59.17 C
ANISOU 249 CG2 VAL A 54 5046 6057 11378 -1385 619 -3134 C
ATOM 250 N ALA A 55 -23.466 58.210 109.502 1.00 73.15 N
ANISOU 250 N ALA A 55 6063 8572 13156 -874 -683 -3202 N
ATOM 251 CA ALA A 55 -22.459 57.290 110.034 1.00 73.14 C
ANISOU 251 CA ALA A 55 5921 8702 13168 -756 -970 -3267 C
ATOM 252 C ALA A 55 -22.130 56.182 109.035 1.00 76.39 C
ANISOU 252 C ALA A 55 6241 9154 13629 -625 -945 -3202 C
ATOM 253 O ALA A 55 -20.955 55.871 108.799 1.00 79.85 O
ANISOU 253 O ALA A 55 6483 9602 14253 -638 -923 -3381 O
ATOM 254 CB ALA A 55 -22.943 56.679 111.353 1.00 67.96 C
ANISOU 254 CB ALA A 55 5424 8164 12234 -604 -1388 -3115 C
ATOM 255 N VAL A 56 -23.164 55.561 108.459 1.00 74.95 N
ANISOU 255 N VAL A 56 6204 8996 13276 -497 -956 -2953 N
ATOM 256 CA VAL A 56 -22.967 54.510 107.462 1.00 69.00 C
ANISOU 256 CA VAL A 56 5410 8273 12534 -386 -918 -2868 C
ATOM 257 C VAL A 56 -22.288 55.080 106.210 1.00 69.26 C
ANISOU 257 C VAL A 56 5283 8181 12850 -551 -499 -3048 C
ATOM 258 O VAL A 56 -21.336 54.489 105.689 1.00 72.77 O
ANISOU 258 O VAL A 56 5584 8633 13433 -535 -461 -3165 O
ATOM 259 CB VAL A 56 -24.313 53.813 107.156 1.00 65.04 C
ANISOU 259 CB VAL A 56 5120 7833 11757 -230 -1007 -2551 C
ATOM 260 CG1 VAL A 56 -24.334 53.183 105.767 1.00 66.04 C
ANISOU 260 CG1 VAL A 56 5221 7943 11927 -191 -815 -2466 C
ATOM 261 CG2 VAL A 56 -24.614 52.737 108.214 1.00 62.84 C
ANISOU 261 CG2 VAL A 56 5012 7681 11184 -58 -1390 -2380 C
ATOM 262 N PHE A 57 -22.722 56.268 105.756 1.00 68.36 N
ANISOU 262 N PHE A 57 5217 7930 12825 -733 -153 -3085 N
ATOM 263 CA PHE A 57 -22.138 56.928 104.584 1.00 67.50 C
ANISOU 263 CA PHE A 57 5043 7664 12941 -930 324 -3236 C
ATOM 264 C PHE A 57 -20.626 57.155 104.746 1.00 72.03 C
ANISOU 264 C PHE A 57 5399 8229 13741 -1044 389 -3552 C
ATOM 265 O PHE A 57 -19.844 56.799 103.856 1.00 77.53 O
ANISOU 265 O PHE A 57 5979 8895 14584 -1075 575 -3667 O
ATOM 266 CB PHE A 57 -22.883 58.250 104.312 1.00 66.00 C
ANISOU 266 CB PHE A 57 5036 7282 12758 -1127 695 -3204 C
ATOM 267 CG PHE A 57 -22.378 59.055 103.114 1.00 68.75 C
ANISOU 267 CG PHE A 57 5446 7414 13262 -1355 1260 -3317 C
ATOM 268 CD1 PHE A 57 -22.824 58.790 101.823 1.00 64.55 C
ANISOU 268 CD1 PHE A 57 5036 6788 12702 -1346 1552 -3153 C
ATOM 269 CD2 PHE A 57 -21.505 60.119 103.298 1.00 75.26 C
ANISOU 269 CD2 PHE A 57 6255 8122 14220 -1580 1516 -3566 C
ATOM 270 CE1 PHE A 57 -22.375 59.546 100.740 1.00 68.49 C
ANISOU 270 CE1 PHE A 57 5681 7064 13278 -1554 2088 -3233 C
ATOM 271 CE2 PHE A 57 -21.053 60.874 102.221 1.00 76.27 C
ANISOU 271 CE2 PHE A 57 6506 8043 14431 -1787 2050 -3657 C
ATOM 272 CZ PHE A 57 -21.489 60.587 100.943 1.00 74.87 C
ANISOU 272 CZ PHE A 57 6493 7755 14198 -1772 2336 -3486 C
ATOM 273 N VAL A 58 -20.190 57.733 105.879 1.00 69.07 N
ANISOU 273 N VAL A 58 4962 7886 13395 -1109 235 -3703 N
ATOM 274 CA VAL A 58 -18.760 57.997 106.074 1.00 71.80 C
ANISOU 274 CA VAL A 58 5074 8238 13969 -1219 292 -4015 C
ATOM 275 C VAL A 58 -17.984 56.684 106.288 1.00 69.84 C
ANISOU 275 C VAL A 58 4650 8126 13759 -1020 -43 -4059 C
ATOM 276 O VAL A 58 -16.977 56.441 105.613 1.00 71.86 O
ANISOU 276 O VAL A 58 4720 8360 14222 -1065 115 -4258 O
ATOM 277 CB VAL A 58 -18.512 59.013 107.215 1.00 76.89 C
ANISOU 277 CB VAL A 58 5708 8876 14629 -1356 228 -4160 C
ATOM 278 CG1 VAL A 58 -17.006 59.191 107.475 1.00 82.68 C
ANISOU 278 CG1 VAL A 58 6166 9645 15605 -1453 243 -4491 C
ATOM 279 CG2 VAL A 58 -19.119 60.393 106.891 1.00 78.33 C
ANISOU 279 CG2 VAL A 58 6097 8873 14792 -1590 637 -4151 C
ATOM 280 N VAL A 59 -18.462 55.799 107.189 1.00 65.79 N
ANISOU 280 N VAL A 59 4226 7737 13035 -806 -483 -3871 N
ATOM 281 CA VAL A 59 -17.781 54.522 107.469 1.00 67.90 C
ANISOU 281 CA VAL A 59 4391 8103 13305 -617 -796 -3887 C
ATOM 282 C VAL A 59 -17.637 53.673 106.194 1.00 72.19 C
ANISOU 282 C VAL A 59 4901 8620 13907 -556 -643 -3847 C
ATOM 283 O VAL A 59 -16.571 53.098 105.939 1.00 73.96 O
ANISOU 283 O VAL A 59 4932 8858 14312 -525 -667 -4034 O
ATOM 284 CB VAL A 59 -18.495 53.744 108.605 1.00 65.92 C
ANISOU 284 CB VAL A 59 4335 7954 12756 -422 -1226 -3645 C
ATOM 285 CG1 VAL A 59 -18.012 52.279 108.708 1.00 64.73 C
ANISOU 285 CG1 VAL A 59 4164 7872 12560 -224 -1496 -3597 C
ATOM 286 CG2 VAL A 59 -18.289 54.428 109.966 1.00 66.25 C
ANISOU 286 CG2 VAL A 59 4370 8029 12772 -482 -1420 -3740 C
ATOM 287 N ALA A 60 -18.694 53.592 105.370 1.00 72.11 N
ANISOU 287 N ALA A 60 5075 8571 13753 -542 -483 -3616 N
ATOM 288 CA ALA A 60 -18.623 52.818 104.125 1.00 66.51 C
ANISOU 288 CA ALA A 60 4360 7834 13078 -501 -326 -3562 C
ATOM 289 C ALA A 60 -17.676 53.449 103.096 1.00 76.92 C
ANISOU 289 C ALA A 60 5504 9034 14688 -701 99 -3835 C
ATOM 290 O ALA A 60 -16.994 52.729 102.360 1.00 80.85 O
ANISOU 290 O ALA A 60 5893 9523 15303 -674 162 -3929 O
ATOM 291 CB ALA A 60 -20.018 52.645 103.518 1.00 57.66 C
ANISOU 291 CB ALA A 60 3477 6705 11725 -445 -256 -3245 C
ATOM 292 N LEU A 61 -17.634 54.790 103.013 1.00 82.64 N
ANISOU 292 N LEU A 61 6228 9654 15519 -917 419 -3965 N
ATOM 293 CA LEU A 61 -16.758 55.446 102.038 1.00 84.48 C
ANISOU 293 CA LEU A 61 6353 9756 15991 -1134 876 -4221 C
ATOM 294 C LEU A 61 -15.287 55.299 102.419 1.00 91.02 C
ANISOU 294 C LEU A 61 6884 10633 17067 -1162 795 -4563 C
ATOM 295 O LEU A 61 -14.448 54.966 101.574 1.00 94.54 O
ANISOU 295 O LEU A 61 7194 11035 17692 -1214 990 -4746 O
ATOM 296 CB LEU A 61 -17.118 56.932 101.880 1.00 82.01 C
ANISOU 296 CB LEU A 61 6180 9295 15684 -1372 1271 -4256 C
ATOM 297 CG LEU A 61 -18.311 57.318 100.992 1.00 85.28 C
ANISOU 297 CG LEU A 61 6889 9577 15938 -1425 1574 -3995 C
ATOM 298 CD1 LEU A 61 -18.331 58.813 100.701 1.00 91.00 C
ANISOU 298 CD1 LEU A 61 7778 10103 16695 -1694 2051 -4086 C
ATOM 299 CD2 LEU A 61 -18.339 56.534 99.685 1.00 86.42 C
ANISOU 299 CD2 LEU A 61 7085 9677 16074 -1381 1749 -3905 C
ATOM 300 N VAL A 62 -14.958 55.562 103.693 1.00 93.96 N
ANISOU 300 N VAL A 62 7153 11093 17456 -1134 511 -4660 N
ATOM 301 CA VAL A 62 -13.584 55.412 104.188 1.00 96.09 C
ANISOU 301 CA VAL A 62 7125 11423 17963 -1142 386 -4983 C
ATOM 302 C VAL A 62 -13.169 53.946 104.125 1.00 98.85 C
ANISOU 302 C VAL A 62 7375 11855 18329 -917 83 -4961 C
ATOM 303 O VAL A 62 -12.138 53.594 103.531 1.00103.67 O
ANISOU 303 O VAL A 62 7771 12446 19172 -948 204 -5209 O
ATOM 304 CB VAL A 62 -13.468 55.980 105.619 1.00 93.75 C
ANISOU 304 CB VAL A 62 6781 11202 17636 -1151 117 -5045 C
ATOM 305 CG1 VAL A 62 -12.111 55.658 106.260 1.00 98.86 C
ANISOU 305 CG1 VAL A 62 7120 11934 18511 -1113 -100 -5351 C
ATOM 306 CG2 VAL A 62 -13.704 57.490 105.635 1.00 94.98 C
ANISOU 306 CG2 VAL A 62 7021 11259 17809 -1410 460 -5117 C
ATOM 307 N GLY A 63 -14.001 53.066 104.691 1.00 92.55 N
ANISOU 307 N GLY A 63 6755 11137 17273 -698 -287 -4663 N
ATOM 308 CA GLY A 63 -13.694 51.641 104.735 1.00 89.69 C
ANISOU 308 CA GLY A 63 6355 10841 16881 -484 -585 -4610 C
ATOM 309 C GLY A 63 -13.484 51.013 103.367 1.00 89.07 C
ANISOU 309 C GLY A 63 6246 10704 16893 -493 -348 -4631 C
ATOM 310 O GLY A 63 -12.513 50.282 103.156 1.00 92.36 O
ANISOU 310 O GLY A 63 6465 11134 17492 -433 -415 -4825 O
ATOM 311 N ASN A 64 -14.400 51.271 102.424 1.00 88.85 N
ANISOU 311 N ASN A 64 6413 10606 16739 -567 -73 -4432 N
ATOM 312 CA ASN A 64 -14.311 50.634 101.109 1.00 86.71 C
ANISOU 312 CA ASN A 64 6151 10278 16515 -577 146 -4414 C
ATOM 313 C ASN A 64 -13.193 51.217 100.248 1.00 88.75 C
ANISOU 313 C ASN A 64 6198 10433 17089 -785 549 -4767 C
ATOM 314 O ASN A 64 -12.691 50.531 99.351 1.00 92.45 O
ANISOU 314 O ASN A 64 6590 10868 17669 -783 668 -4854 O
ATOM 315 CB ASN A 64 -15.647 50.728 100.375 1.00 83.71 C
ANISOU 315 CB ASN A 64 6055 9857 15896 -590 310 -4088 C
ATOM 316 CG ASN A 64 -16.657 49.721 100.887 1.00 85.68 C
ANISOU 316 CG ASN A 64 6505 10216 15835 -367 -65 -3747 C
ATOM 317 OD1 ASN A 64 -16.461 48.512 100.762 1.00 89.44 O
ANISOU 317 OD1 ASN A 64 6976 10746 16263 -224 -260 -3689 O
ATOM 318 ND2 ASN A 64 -17.738 50.212 101.478 1.00 87.39 N
ANISOU 318 ND2 ASN A 64 6908 10461 15835 -345 -154 -3529 N
ATOM 319 N THR A 65 -12.794 52.474 100.485 1.00 91.10 N
ANISOU 319 N THR A 65 6414 10675 17525 -981 784 -4978 N
ATOM 320 CA THR A 65 -11.642 53.013 99.761 1.00 95.73 C
ANISOU 320 CA THR A 65 6799 11167 18405 -1191 1171 -5345 C
ATOM 321 C THR A 65 -10.347 52.393 100.288 1.00 96.10 C
ANISOU 321 C THR A 65 6513 11300 18699 -1106 928 -5653 C
ATOM 322 O THR A 65 -9.451 52.059 99.505 1.00 96.60 O
ANISOU 322 O THR A 65 6402 11318 18984 -1170 1120 -5899 O
ATOM 323 CB THR A 65 -11.621 54.549 99.840 1.00 98.13 C
ANISOU 323 CB THR A 65 7148 11378 18758 -1442 1524 -5474 C
ATOM 324 OG1 THR A 65 -11.936 54.987 101.168 1.00102.53 O
ANISOU 324 OG1 THR A 65 7705 12026 19224 -1385 1224 -5411 O
ATOM 325 CG2 THR A 65 -12.632 55.166 98.851 1.00 91.88 C
ANISOU 325 CG2 THR A 65 6683 10438 17791 -1574 1922 -5247 C
ATOM 326 N LEU A 66 -10.273 52.174 101.608 1.00 93.96 N
ANISOU 326 N LEU A 66 6166 11150 18385 -953 495 -5634 N
ATOM 327 CA LEU A 66 -9.133 51.514 102.241 1.00 94.06 C
ANISOU 327 CA LEU A 66 5886 11248 18606 -834 201 -5894 C
ATOM 328 C LEU A 66 -8.996 50.045 101.834 1.00 92.25 C
ANISOU 328 C LEU A 66 5641 11045 18365 -633 -5 -5819 C
ATOM 329 O LEU A 66 -7.888 49.504 101.911 1.00 95.07 O
ANISOU 329 O LEU A 66 5724 11431 18967 -577 -114 -6103 O
ATOM 330 CB LEU A 66 -9.238 51.629 103.770 1.00 93.57 C
ANISOU 330 CB LEU A 66 5817 11291 18443 -715 -217 -5837 C
ATOM 331 CG LEU A 66 -9.025 53.010 104.410 1.00 99.37 C
ANISOU 331 CG LEU A 66 6478 12024 19252 -909 -87 -6002 C
ATOM 332 CD1 LEU A 66 -9.007 52.912 105.929 1.00103.56 C
ANISOU 332 CD1 LEU A 66 6990 12664 19693 -771 -549 -5960 C
ATOM 333 CD2 LEU A 66 -7.746 53.670 103.907 1.00104.65 C
ANISOU 333 CD2 LEU A 66 6839 12649 20274 -1123 252 -6446 C
ATOM 334 N VAL A 67 -10.090 49.395 101.408 1.00 89.43 N
ANISOU 334 N VAL A 67 5566 10680 17735 -529 -57 -5455 N
ATOM 335 CA VAL A 67 -10.012 48.032 100.872 1.00 92.23 C
ANISOU 335 CA VAL A 67 5932 11047 18065 -371 -193 -5375 C
ATOM 336 C VAL A 67 -9.279 48.039 99.527 1.00 97.62 C
ANISOU 336 C VAL A 67 6461 11635 18996 -527 208 -5619 C
ATOM 337 O VAL A 67 -8.305 47.298 99.332 1.00 97.29 O
ANISOU 337 O VAL A 67 6188 11604 19174 -467 138 -5856 O
ATOM 338 CB VAL A 67 -11.427 47.411 100.766 1.00 86.65 C
ANISOU 338 CB VAL A 67 5574 10364 16984 -245 -328 -4922 C
ATOM 339 CG1 VAL A 67 -11.429 46.088 99.982 1.00 84.56 C
ANISOU 339 CG1 VAL A 67 5348 10099 16683 -127 -379 -4827 C
ATOM 340 CG2 VAL A 67 -12.045 47.176 102.157 1.00 82.94 C
ANISOU 340 CG2 VAL A 67 5259 9987 16269 -76 -751 -4704 C
ATOM 341 N CYS A 68 -9.705 48.920 98.607 1.00103.99 N
ANISOU 341 N CYS A 68 7398 12336 19776 -740 648 -5582 N
ATOM 342 CA CYS A 68 -9.094 49.053 97.280 1.00108.55 C
ANISOU 342 CA CYS A 68 7894 12797 20554 -926 1092 -5797 C
ATOM 343 C CYS A 68 -7.627 49.479 97.354 1.00116.54 C
ANISOU 343 C CYS A 68 8552 13791 21936 -1057 1239 -6283 C
ATOM 344 O CYS A 68 -6.788 48.975 96.597 1.00119.93 O
ANISOU 344 O CYS A 68 8805 14179 22585 -1101 1392 -6523 O
ATOM 345 CB CYS A 68 -9.883 50.068 96.445 1.00108.26 C
ANISOU 345 CB CYS A 68 8119 12632 20382 -1137 1535 -5652 C
ATOM 346 SG CYS A 68 -11.643 49.699 96.242 1.00106.65 S
ANISOU 346 SG CYS A 68 8311 12447 19763 -1006 1415 -5107 S
ATOM 347 N LEU A 69 -7.314 50.437 98.240 1.00117.81 N
ANISOU 347 N LEU A 69 8604 13985 22174 -1134 1213 -6441 N
ATOM 348 CA LEU A 69 -5.942 50.917 98.417 1.00117.39 C
ANISOU 348 CA LEU A 69 8200 13935 22469 -1265 1339 -6912 C
ATOM 349 C LEU A 69 -5.033 49.821 98.963 1.00113.69 C
ANISOU 349 C LEU A 69 7435 13571 22192 -1055 945 -7106 C
ATOM 350 O LEU A 69 -3.865 49.717 98.570 1.00116.27 O
ANISOU 350 O LEU A 69 7461 13879 22836 -1136 1093 -7497 O
ATOM 351 CB LEU A 69 -5.928 52.126 99.358 1.00115.56 C
ANISOU 351 CB LEU A 69 7938 13734 22236 -1376 1345 -6993 C
ATOM 352 CG LEU A 69 -6.270 53.496 98.765 1.00112.15 C
ANISOU 352 CG LEU A 69 7688 13170 21754 -1669 1861 -7007 C
ATOM 353 CD1 LEU A 69 -6.676 54.480 99.854 1.00108.00 C
ANISOU 353 CD1 LEU A 69 7225 12694 21117 -1712 1749 -6934 C
ATOM 354 CD2 LEU A 69 -5.101 54.047 97.953 1.00116.88 C
ANISOU 354 CD2 LEU A 69 8082 13672 22653 -1931 2329 -7447 C
ATOM 355 N ALA A 70 -5.567 48.993 99.867 1.00106.35 N
ANISOU 355 N ALA A 70 6601 12741 21065 -788 451 -6841 N
ATOM 356 CA ALA A 70 -4.791 47.924 100.485 1.00107.55 C
ANISOU 356 CA ALA A 70 6524 12979 21359 -564 42 -6989 C
ATOM 357 C ALA A 70 -4.293 46.909 99.451 1.00113.84 C
ANISOU 357 C ALA A 70 7216 13732 22306 -525 142 -7102 C
ATOM 358 O ALA A 70 -3.181 46.390 99.582 1.00124.80 O
ANISOU 358 O ALA A 70 8286 15152 23979 -456 16 -7432 O
ATOM 359 CB ALA A 70 -5.628 47.236 101.567 1.00102.79 C
ANISOU 359 CB ALA A 70 6143 12461 20451 -306 -454 -6630 C
ATOM 360 N VAL A 71 -5.125 46.560 98.461 1.00107.26 N
ANISOU 360 N VAL A 71 6643 12829 21280 -554 338 -6827 N
ATOM 361 CA VAL A 71 -4.660 45.645 97.412 1.00109.60 C
ANISOU 361 CA VAL A 71 6847 13078 21720 -544 468 -6936 C
ATOM 362 C VAL A 71 -3.832 46.363 96.338 1.00110.05 C
ANISOU 362 C VAL A 71 6725 13025 22063 -829 998 -7301 C
ATOM 363 O VAL A 71 -3.149 45.697 95.554 1.00112.00 O
ANISOU 363 O VAL A 71 6811 13233 22512 -846 1120 -7504 O
ATOM 364 CB VAL A 71 -5.799 44.820 96.764 1.00107.46 C
ANISOU 364 CB VAL A 71 6907 12787 21138 -449 441 -6512 C
ATOM 365 CG1 VAL A 71 -6.641 44.100 97.827 1.00 96.43 C
ANISOU 365 CG1 VAL A 71 5713 11489 19435 -187 -53 -6159 C
ATOM 366 CG2 VAL A 71 -6.667 45.643 95.822 1.00103.07 C
ANISOU 366 CG2 VAL A 71 6619 12130 20411 -660 869 -6315 C
ATOM 367 N TRP A 72 -3.939 47.699 96.235 1.00109.76 N
ANISOU 367 N TRP A 72 6752 12926 22028 -1066 1341 -7372 N
ATOM 368 CA TRP A 72 -3.088 48.477 95.329 1.00117.02 C
ANISOU 368 CA TRP A 72 7522 13730 23211 -1361 1865 -7750 C
ATOM 369 C TRP A 72 -1.682 48.679 95.904 1.00124.93 C
ANISOU 369 C TRP A 72 8087 14795 24588 -1394 1803 -8248 C
ATOM 370 O TRP A 72 -0.695 48.619 95.163 1.00130.32 O
ANISOU 370 O TRP A 72 8536 15418 25562 -1536 2088 -8621 O
ATOM 371 CB TRP A 72 -3.739 49.833 95.014 1.00117.22 C
ANISOU 371 CB TRP A 72 7813 13650 23075 -1606 2270 -7638 C
ATOM 372 CG TRP A 72 -2.804 50.803 94.320 1.00123.83 C
ANISOU 372 CG TRP A 72 8516 14368 24167 -1928 2806 -8057 C
ATOM 373 CD1 TRP A 72 -2.076 51.799 94.907 1.00128.50 C
ANISOU 373 CD1 TRP A 72 8902 14980 24941 -2080 2921 -8380 C
ATOM 374 CD2 TRP A 72 -2.479 50.845 92.920 1.00125.18 C
ANISOU 374 CD2 TRP A 72 8758 14377 24427 -2147 3305 -8206 C
ATOM 375 NE1 TRP A 72 -1.325 52.459 93.963 1.00131.96 N
ANISOU 375 NE1 TRP A 72 9285 15280 25572 -2383 3470 -8726 N
ATOM 376 CE2 TRP A 72 -1.554 51.894 92.737 1.00130.42 C
ANISOU 376 CE2 TRP A 72 9268 14965 25321 -2430 3716 -8627 C
ATOM 377 CE3 TRP A 72 -2.883 50.101 91.806 1.00122.69 C
ANISOU 377 CE3 TRP A 72 8636 13971 24009 -2140 3451 -8025 C
ATOM 378 CZ2 TRP A 72 -1.026 52.217 91.485 1.00133.07 C
ANISOU 378 CZ2 TRP A 72 9658 15125 25777 -2707 4273 -8873 C
ATOM 379 CZ3 TRP A 72 -2.357 50.424 90.564 1.00125.23 C
ANISOU 379 CZ3 TRP A 72 9005 14119 24455 -2411 3993 -8263 C
ATOM 380 CH2 TRP A 72 -1.439 51.471 90.415 1.00129.76 C
ANISOU 380 CH2 TRP A 72 9445 14609 25250 -2692 4400 -8684 C
ATOM 381 N ARG A 73 -1.591 48.964 97.207 1.00128.69 N
ANISOU 381 N ARG A 73 8452 15387 25058 -1277 1450 -8265 N
ATOM 382 CA ARG A 73 -0.295 49.134 97.868 1.00134.99 C
ANISOU 382 CA ARG A 73 8825 16264 26202 -1284 1335 -8724 C
ATOM 383 C ARG A 73 0.402 47.783 98.091 1.00138.33 C
ANISOU 383 C ARG A 73 8992 16764 26804 -1028 949 -8863 C
ATOM 384 O ARG A 73 1.573 47.620 97.733 1.00146.75 O
ANISOU 384 O ARG A 73 9708 17827 28225 -1095 1075 -9300 O
ATOM 385 CB ARG A 73 -0.473 49.914 99.179 1.00135.81 C
ANISOU 385 CB ARG A 73 8920 16461 26220 -1253 1088 -8678 C
ATOM 386 CG ARG A 73 -0.957 51.375 99.000 1.00139.11 C
ANISOU 386 CG ARG A 73 9534 16801 26520 -1535 1502 -8629 C
ATOM 387 CD ARG A 73 0.172 52.380 98.739 1.00149.25 C
ANISOU 387 CD ARG A 73 10537 18050 28124 -1827 1911 -9128 C
ATOM 388 NE ARG A 73 -0.291 53.760 98.906 1.00152.74 N
ANISOU 388 NE ARG A 73 11168 18439 28428 -2058 2203 -9065 N
ATOM 389 CZ ARG A 73 -0.640 54.569 97.909 1.00154.14 C
ANISOU 389 CZ ARG A 73 11592 18458 28516 -2325 2748 -9034 C
ATOM 390 NH1 ARG A 73 -0.578 54.147 96.653 1.00156.91 N
ANISOU 390 NH1 ARG A 73 12032 18686 28900 -2404 3066 -9061 N
ATOM 391 NH2 ARG A 73 -1.054 55.803 98.167 1.00151.52 N
ANISOU 391 NH2 ARG A 73 11438 18081 28053 -2516 2978 -8974 N
ATOM 392 N ASN A 74 -0.285 46.832 98.738 1.00133.68 N
ANISOU 392 N ASN A 74 8574 16242 25977 -737 476 -8513 N
ATOM 393 CA ASN A 74 0.224 45.487 99.029 1.00127.53 C
ANISOU 393 CA ASN A 74 7624 15524 25307 -467 73 -8582 C
ATOM 394 C ASN A 74 0.065 44.550 97.819 1.00138.50 C
ANISOU 394 C ASN A 74 9101 16838 26685 -454 242 -8492 C
ATOM 395 O ASN A 74 -0.952 44.584 97.129 1.00136.10 O
ANISOU 395 O ASN A 74 9134 16467 26112 -523 443 -8149 O
ATOM 396 CB ASN A 74 -0.514 44.934 100.257 1.00124.08 C
ANISOU 396 CB ASN A 74 7395 15172 24576 -187 -469 -8227 C
ATOM 397 CG ASN A 74 0.144 43.699 100.886 1.00126.96 C
ANISOU 397 CG ASN A 74 7570 15604 25067 103 -942 -8346 C
ATOM 398 OD1 ASN A 74 0.622 42.790 100.203 1.00128.78 O
ANISOU 398 OD1 ASN A 74 7669 15807 25454 172 -924 -8476 O
ATOM 399 ND2 ASN A 74 0.136 43.660 102.215 1.00127.43 N
ANISOU 399 ND2 ASN A 74 7633 15742 25041 277 -1372 -8290 N
ATOM 400 N HIS A 75 1.136 43.811 97.497 1.00130.98 N
ANISOU 400 N HIS A 75 7820 15893 26055 -395 204 -8842 N
ATOM 401 CA HIS A 75 1.164 42.868 96.376 1.00134.19 C
ANISOU 401 CA HIS A 75 8250 16233 26502 -383 354 -8819 C
ATOM 402 C HIS A 75 0.983 41.398 96.802 1.00133.44 C
ANISOU 402 C HIS A 75 8202 16197 26302 -51 -132 -8625 C
ATOM 403 O HIS A 75 0.735 40.549 95.933 1.00127.84 O
ANISOU 403 O HIS A 75 7594 15441 25540 -19 -46 -8498 O
ATOM 404 CB HIS A 75 2.480 43.067 95.610 1.00137.16 C
ANISOU 404 CB HIS A 75 8232 16563 27320 -573 703 -9362 C
ATOM 405 CG HIS A 75 2.660 44.465 95.076 1.00138.65 C
ANISOU 405 CG HIS A 75 8416 16670 27596 -926 1237 -9559 C
ATOM 406 ND1 HIS A 75 2.296 44.840 93.800 1.00137.83 N
ANISOU 406 ND1 HIS A 75 8523 16426 27419 -1179 1755 -9491 N
ATOM 407 CD2 HIS A 75 3.077 45.597 95.692 1.00141.82 C
ANISOU 407 CD2 HIS A 75 8672 17103 28111 -1066 1326 -9790 C
ATOM 408 CE1 HIS A 75 2.548 46.125 93.630 1.00139.47 C
ANISOU 408 CE1 HIS A 75 8713 16572 27706 -1462 2154 -9697 C
ATOM 409 NE2 HIS A 75 3.013 46.614 94.768 1.00142.19 N
ANISOU 409 NE2 HIS A 75 8837 17025 28164 -1403 1907 -9879 N
ATOM 410 N HIS A 76 1.117 41.094 98.098 1.00138.88 N
ANISOU 410 N HIS A 76 8832 16978 26957 184 -621 -8608 N
ATOM 411 CA HIS A 76 0.845 39.755 98.632 1.00142.41 C
ANISOU 411 CA HIS A 76 9393 17465 27250 500 -1094 -8390 C
ATOM 412 C HIS A 76 -0.643 39.470 98.677 1.00142.72 C
ANISOU 412 C HIS A 76 9919 17493 26816 565 -1177 -7827 C
ATOM 413 O HIS A 76 -1.070 38.315 98.550 1.00140.83 O
ANISOU 413 O HIS A 76 9847 17251 26411 744 -1379 -7598 O
ATOM 414 CB HIS A 76 1.420 39.625 100.048 1.00144.49 C
ANISOU 414 CB HIS A 76 9483 17813 27602 713 -1574 -8543 C
ATOM 415 CG HIS A 76 2.916 39.566 100.101 1.00151.87 C
ANISOU 415 CG HIS A 76 9914 18779 29009 730 -1610 -9100 C
ATOM 416 ND1 HIS A 76 3.607 38.384 99.962 1.00143.07 N
ANISOU 416 ND1 HIS A 76 8596 17669 28093 931 -1833 -9286 N
ATOM 417 CD2 HIS A 76 3.848 40.531 100.268 1.00144.53 C
ANISOU 417 CD2 HIS A 76 8636 17881 28397 570 -1447 -9522 C
ATOM 418 CE1 HIS A 76 4.900 38.618 100.046 1.00149.86 C
ANISOU 418 CE1 HIS A 76 8992 18566 29380 904 -1818 -9804 C
ATOM 419 NE2 HIS A 76 5.078 39.918 100.232 1.00150.91 N
ANISOU 419 NE2 HIS A 76 9026 18719 29594 679 -1580 -9961 N
ATOM 420 N MET A 77 -1.428 40.525 98.867 1.00145.55 N
ANISOU 420 N MET A 77 10496 17847 26960 416 -1017 -7617 N
ATOM 421 CA MET A 77 -2.872 40.528 98.978 1.00141.23 C
ANISOU 421 CA MET A 77 10390 17297 25973 443 -1060 -7111 C
ATOM 422 C MET A 77 -3.603 40.404 97.645 1.00139.48 C
ANISOU 422 C MET A 77 10382 17004 25608 307 -695 -6892 C
ATOM 423 O MET A 77 -4.822 40.224 97.643 1.00136.28 O
ANISOU 423 O MET A 77 10334 16605 24840 351 -748 -6470 O
ATOM 424 CB MET A 77 -3.277 41.819 99.686 1.00136.73 C
ANISOU 424 CB MET A 77 9909 16749 25293 323 -1009 -7045 C
ATOM 425 CG MET A 77 -2.909 41.818 101.156 1.00138.84 C
ANISOU 425 CG MET A 77 10082 17095 25577 492 -1444 -7123 C
ATOM 426 SD MET A 77 -4.196 42.533 102.179 1.00133.54 S
ANISOU 426 SD MET A 77 9783 16460 24497 498 -1595 -6712 S
ATOM 427 CE MET A 77 -3.802 44.263 101.976 1.00135.77 C
ANISOU 427 CE MET A 77 9881 16724 24983 192 -1182 -6979 C
ATOM 428 N ARG A 78 -2.890 40.460 96.511 1.00137.69 N
ANISOU 428 N ARG A 78 9948 16711 25655 145 -329 -7172 N
ATOM 429 CA ARG A 78 -3.511 40.411 95.185 1.00134.60 C
ANISOU 429 CA ARG A 78 9757 16238 25145 -7 52 -6990 C
ATOM 430 C ARG A 78 -3.803 38.956 94.780 1.00106.51 C
ANISOU 430 C ARG A 78 6300 12694 21474 180 -132 -6798 C
ATOM 431 O ARG A 78 -3.189 38.391 93.869 1.00109.07 O
ANISOU 431 O ARG A 78 6462 12973 22008 139 47 -6993 O
ATOM 432 CB ARG A 78 -2.627 41.121 94.168 1.00112.30 C
ANISOU 432 CB ARG A 78 6701 13321 22647 -282 548 -7376 C
ATOM 433 CG ARG A 78 -2.424 42.609 94.449 1.00115.75 C
ANISOU 433 CG ARG A 78 7082 13730 23168 -499 795 -7550 C
ATOM 434 CD ARG A 78 -1.581 43.258 93.368 1.00121.74 C
ANISOU 434 CD ARG A 78 7659 14376 24221 -792 1328 -7929 C
ATOM 435 NE ARG A 78 -1.296 44.662 93.647 1.00124.54 N
ANISOU 435 NE ARG A 78 7951 14700 24669 -1009 1581 -8132 N
ATOM 436 CZ ARG A 78 -0.860 45.523 92.735 1.00129.57 C
ANISOU 436 CZ ARG A 78 8558 15213 25460 -1315 2116 -8383 C
ATOM 437 NH1 ARG A 78 -0.669 45.124 91.485 1.00133.26 N
ANISOU 437 NH1 ARG A 78 9057 15573 26004 -1440 2449 -8454 N
ATOM 438 NH2 ARG A 78 -0.624 46.785 93.067 1.00124.48 N
ANISOU 438 NH2 ARG A 78 7872 14545 24879 -1505 2332 -8560 N
ATOM 439 N THR A 79 -4.773 38.363 95.481 1.00102.25 N
ANISOU 439 N THR A 79 6044 12217 20590 376 -480 -6413 N
ATOM 440 CA THR A 79 -5.316 37.029 95.230 1.00 99.74 C
ANISOU 440 CA THR A 79 5906 11917 20072 555 -671 -6150 C
ATOM 441 C THR A 79 -6.667 37.135 94.507 1.00 94.22 C
ANISOU 441 C THR A 79 5575 11202 19023 469 -464 -5734 C
ATOM 442 O THR A 79 -7.235 38.224 94.384 1.00 95.66 O
ANISOU 442 O THR A 79 5889 11362 19095 306 -238 -5626 O
ATOM 443 CB THR A 79 -5.485 36.246 96.548 1.00 99.21 C
ANISOU 443 CB THR A 79 5931 11921 19844 827 -1196 -6014 C
ATOM 444 OG1 THR A 79 -6.511 36.850 97.347 1.00 95.12 O
ANISOU 444 OG1 THR A 79 5701 11440 19001 829 -1310 -5702 O
ATOM 445 CG2 THR A 79 -4.187 36.213 97.363 1.00105.01 C
ANISOU 445 CG2 THR A 79 6309 12675 20913 929 -1435 -6419 C
ATOM 446 N VAL A 80 -7.187 35.988 94.036 1.00 91.78 N
ANISOU 446 N VAL A 80 5427 10905 18541 588 -548 -5507 N
ATOM 447 CA VAL A 80 -8.474 35.955 93.324 1.00 88.88 C
ANISOU 447 CA VAL A 80 5394 10536 17840 529 -376 -5116 C
ATOM 448 C VAL A 80 -9.601 36.483 94.217 1.00 86.87 C
ANISOU 448 C VAL A 80 5427 10339 17242 567 -549 -4787 C
ATOM 449 O VAL A 80 -10.359 37.382 93.822 1.00 86.14 O
ANISOU 449 O VAL A 80 5497 10227 17004 418 -304 -4622 O
ATOM 450 CB VAL A 80 -8.771 34.529 92.795 1.00 85.36 C
ANISOU 450 CB VAL A 80 5052 10106 17275 673 -480 -4952 C
ATOM 451 CG1 VAL A 80 -10.171 34.426 92.172 1.00 80.01 C
ANISOU 451 CG1 VAL A 80 4725 9447 16228 639 -350 -4535 C
ATOM 452 CG2 VAL A 80 -7.728 34.089 91.758 1.00 89.48 C
ANISOU 452 CG2 VAL A 80 5299 10563 18136 607 -244 -5270 C
ATOM 453 N THR A 81 -9.717 35.948 95.445 1.00 85.54 N
ANISOU 453 N THR A 81 5328 10232 16941 762 -965 -4698 N
ATOM 454 CA THR A 81 -10.735 36.374 96.412 1.00 81.16 C
ANISOU 454 CA THR A 81 5041 9731 16063 802 -1148 -4406 C
ATOM 455 C THR A 81 -10.686 37.886 96.658 1.00 84.09 C
ANISOU 455 C THR A 81 5347 10085 16519 634 -965 -4507 C
ATOM 456 O THR A 81 -11.720 38.565 96.643 1.00 82.21 O
ANISOU 456 O THR A 81 5336 9861 16041 557 -859 -4253 O
ATOM 457 CB THR A 81 -10.552 35.598 97.733 1.00 81.97 C
ANISOU 457 CB THR A 81 5161 9845 16138 1022 -1611 -4447 C
ATOM 458 OG1 THR A 81 -10.777 34.201 97.510 1.00 85.18 O
ANISOU 458 OG1 THR A 81 5677 10243 16447 1175 -1778 -4342 O
ATOM 459 CG2 THR A 81 -11.507 36.073 98.841 1.00 81.31 C
ANISOU 459 CG2 THR A 81 5336 9795 15764 1054 -1800 -4207 C
ATOM 460 N ASN A 82 -9.478 38.424 96.866 1.00 87.45 N
ANISOU 460 N ASN A 82 5453 10478 17294 574 -918 -4895 N
ATOM 461 CA ASN A 82 -9.309 39.843 97.175 1.00 88.05 C
ANISOU 461 CA ASN A 82 5443 10535 17475 413 -750 -5035 C
ATOM 462 C ASN A 82 -9.557 40.746 95.964 1.00 91.04 C
ANISOU 462 C ASN A 82 5853 10836 17902 170 -265 -5046 C
ATOM 463 O ASN A 82 -9.991 41.890 96.136 1.00 94.46 O
ANISOU 463 O ASN A 82 6371 11251 18269 41 -110 -4994 O
ATOM 464 CB ASN A 82 -7.912 40.087 97.755 1.00 89.96 C
ANISOU 464 CB ASN A 82 5322 10776 18082 421 -844 -5466 C
ATOM 465 CG ASN A 82 -7.762 39.543 99.169 1.00 91.75 C
ANISOU 465 CG ASN A 82 5555 11069 18235 642 -1322 -5443 C
ATOM 466 OD1 ASN A 82 -8.728 39.070 99.770 1.00 87.10 O
ANISOU 466 OD1 ASN A 82 5264 10520 17310 767 -1560 -5102 O
ATOM 467 ND2 ASN A 82 -6.551 39.624 99.712 1.00 99.44 N
ANISOU 467 ND2 ASN A 82 6208 12053 19522 683 -1455 -5813 N
ATOM 468 N TYR A 83 -9.274 40.266 94.739 1.00 88.23 N
ANISOU 468 N TYR A 83 5441 10422 17661 100 -10 -5121 N
ATOM 469 CA TYR A 83 -9.639 41.027 93.541 1.00 86.50 C
ANISOU 469 CA TYR A 83 5325 10110 17432 -127 457 -5082 C
ATOM 470 C TYR A 83 -11.157 41.135 93.416 1.00 86.24 C
ANISOU 470 C TYR A 83 5654 10107 17009 -103 454 -4636 C
ATOM 471 O TYR A 83 -11.681 42.178 93.003 1.00 91.06 O
ANISOU 471 O TYR A 83 6395 10656 17549 -268 745 -4559 O
ATOM 472 CB TYR A 83 -9.041 40.382 92.280 1.00 89.82 C
ANISOU 472 CB TYR A 83 5633 10460 18037 -199 718 -5241 C
ATOM 473 CG TYR A 83 -7.640 40.862 91.927 1.00102.93 C
ANISOU 473 CG TYR A 83 6961 12039 20108 -364 978 -5721 C
ATOM 474 CD1 TYR A 83 -6.877 41.563 92.849 1.00107.44 C
ANISOU 474 CD1 TYR A 83 7309 12633 20881 -384 879 -6000 C
ATOM 475 CD2 TYR A 83 -7.087 40.627 90.668 1.00104.37 C
ANISOU 475 CD2 TYR A 83 7058 12124 20475 -509 1337 -5903 C
ATOM 476 CE1 TYR A 83 -5.603 42.010 92.541 1.00113.27 C
ANISOU 476 CE1 TYR A 83 7731 13309 21997 -540 1124 -6458 C
ATOM 477 CE2 TYR A 83 -5.808 41.075 90.349 1.00108.53 C
ANISOU 477 CE2 TYR A 83 7283 12576 21378 -675 1595 -6362 C
ATOM 478 CZ TYR A 83 -5.072 41.765 91.293 1.00113.90 C
ANISOU 478 CZ TYR A 83 7730 13290 22256 -689 1485 -6642 C
ATOM 479 OH TYR A 83 -3.804 42.215 90.997 1.00120.19 O
ANISOU 479 OH TYR A 83 8213 14024 23429 -859 1746 -7117 O
ATOM 480 N PHE A 84 -11.866 40.063 93.785 1.00 79.66 N
ANISOU 480 N PHE A 84 4986 9362 15917 100 132 -4353 N
ATOM 481 CA PHE A 84 -13.325 40.083 93.836 1.00 75.20 C
ANISOU 481 CA PHE A 84 4749 8850 14972 147 74 -3939 C
ATOM 482 C PHE A 84 -13.831 40.943 95.005 1.00 74.62 C
ANISOU 482 C PHE A 84 4766 8822 14764 162 -95 -3843 C
ATOM 483 O PHE A 84 -14.828 41.658 94.858 1.00 73.26 O
ANISOU 483 O PHE A 84 4791 8649 14395 94 33 -3623 O
ATOM 484 CB PHE A 84 -13.880 38.648 93.943 1.00 73.21 C
ANISOU 484 CB PHE A 84 4650 8679 14487 347 -209 -3694 C
ATOM 485 CG PHE A 84 -13.934 37.859 92.623 1.00 77.18 C
ANISOU 485 CG PHE A 84 5177 9150 14996 327 -2 -3648 C
ATOM 486 CD1 PHE A 84 -14.609 38.344 91.507 1.00 76.87 C
ANISOU 486 CD1 PHE A 84 5282 9064 14861 191 344 -3504 C
ATOM 487 CD2 PHE A 84 -13.379 36.583 92.545 1.00 79.48 C
ANISOU 487 CD2 PHE A 84 5373 9458 15368 460 -172 -3729 C
ATOM 488 CE1 PHE A 84 -14.677 37.594 90.328 1.00 76.74 C
ANISOU 488 CE1 PHE A 84 5305 9018 14836 178 529 -3456 C
ATOM 489 CE2 PHE A 84 -13.447 35.832 91.373 1.00 76.58 C
ANISOU 489 CE2 PHE A 84 5032 9065 15002 447 11 -3685 C
ATOM 490 CZ PHE A 84 -14.095 36.339 90.266 1.00 75.20 C
ANISOU 490 CZ PHE A 84 4997 8844 14731 304 363 -3547 C
ATOM 491 N LEU A 85 -13.159 40.896 96.170 1.00 72.53 N
ANISOU 491 N LEU A 85 4359 8594 14607 253 -379 -4010 N
ATOM 492 CA LEU A 85 -13.601 41.699 97.317 1.00 71.91 C
ANISOU 492 CA LEU A 85 4365 8555 14404 264 -539 -3929 C
ATOM 493 C LEU A 85 -13.488 43.200 97.039 1.00 76.44 C
ANISOU 493 C LEU A 85 4866 9057 15120 52 -208 -4073 C
ATOM 494 O LEU A 85 -14.255 43.994 97.596 1.00 80.20 O
ANISOU 494 O LEU A 85 5487 9552 15433 23 -230 -3918 O
ATOM 495 CB LEU A 85 -12.814 41.317 98.584 1.00 74.32 C
ANISOU 495 CB LEU A 85 4527 8903 14808 402 -900 -4099 C
ATOM 496 CG LEU A 85 -13.153 39.964 99.238 1.00 75.05 C
ANISOU 496 CG LEU A 85 4780 9057 14679 619 -1272 -3901 C
ATOM 497 CD1 LEU A 85 -12.367 39.740 100.525 1.00 74.07 C
ANISOU 497 CD1 LEU A 85 4524 8947 14674 745 -1612 -4095 C
ATOM 498 CD2 LEU A 85 -14.652 39.816 99.502 1.00 72.84 C
ANISOU 498 CD2 LEU A 85 4862 8832 13982 662 -1352 -3486 C
ATOM 499 N VAL A 86 -12.542 43.591 96.170 1.00 80.12 N
ANISOU 499 N VAL A 86 5120 9431 15889 -108 119 -4377 N
ATOM 500 CA VAL A 86 -12.403 44.974 95.701 1.00 81.51 C
ANISOU 500 CA VAL A 86 5262 9508 16198 -344 517 -4525 C
ATOM 501 C VAL A 86 -13.552 45.340 94.762 1.00 75.40 C
ANISOU 501 C VAL A 86 4767 8679 15204 -435 796 -4238 C
ATOM 502 O VAL A 86 -14.022 46.485 94.752 1.00 72.37 O
ANISOU 502 O VAL A 86 4489 8237 14771 -568 1010 -4194 O
ATOM 503 CB VAL A 86 -11.029 45.155 95.021 1.00 84.99 C
ANISOU 503 CB VAL A 86 5420 9860 17012 -496 803 -4944 C
ATOM 504 CG1 VAL A 86 -10.906 46.512 94.320 1.00 86.94 C
ANISOU 504 CG1 VAL A 86 5693 9973 17368 -772 1297 -5091 C
ATOM 505 CG2 VAL A 86 -9.899 44.981 96.026 1.00 85.76 C
ANISOU 505 CG2 VAL A 86 5219 10018 17348 -410 532 -5253 C
ATOM 506 N ASN A 87 -14.012 44.375 93.956 1.00 73.38 N
ANISOU 506 N ASN A 87 4632 8437 14812 -363 802 -4044 N
ATOM 507 CA ASN A 87 -15.159 44.599 93.081 1.00 71.33 C
ANISOU 507 CA ASN A 87 4641 8140 14320 -418 1029 -3749 C
ATOM 508 C ASN A 87 -16.444 44.750 93.890 1.00 71.21 C
ANISOU 508 C ASN A 87 4840 8224 13993 -297 777 -3417 C
ATOM 509 O ASN A 87 -17.322 45.535 93.511 1.00 73.32 O
ANISOU 509 O ASN A 87 5288 8446 14124 -378 988 -3245 O
ATOM 510 CB ASN A 87 -15.291 43.452 92.071 1.00 72.94 C
ANISOU 510 CB ASN A 87 4905 8352 14457 -358 1074 -3635 C
ATOM 511 CG ASN A 87 -16.263 43.766 90.941 1.00 74.59 C
ANISOU 511 CG ASN A 87 5368 8494 14478 -447 1394 -3394 C
ATOM 512 OD1 ASN A 87 -16.161 44.808 90.293 1.00 71.78 O
ANISOU 512 OD1 ASN A 87 5074 7997 14202 -648 1790 -3483 O
ATOM 513 ND2 ASN A 87 -17.221 42.874 90.713 1.00 79.44 N
ANISOU 513 ND2 ASN A 87 6155 9204 14826 -297 1232 -3085 N
ATOM 514 N LEU A 88 -16.557 44.014 95.004 1.00 69.81 N
ANISOU 514 N LEU A 88 4658 8169 13697 -108 346 -3333 N
ATOM 515 CA LEU A 88 -17.671 44.201 95.934 1.00 66.39 C
ANISOU 515 CA LEU A 88 4421 7826 12978 -9 103 -3061 C
ATOM 516 C LEU A 88 -17.673 45.629 96.494 1.00 71.11 C
ANISOU 516 C LEU A 88 4983 8372 13663 -133 220 -3168 C
ATOM 517 O LEU A 88 -18.726 46.276 96.537 1.00 71.56 O
ANISOU 517 O LEU A 88 5217 8434 13541 -156 285 -2960 O
ATOM 518 CB LEU A 88 -17.605 43.141 97.051 1.00 64.55 C
ANISOU 518 CB LEU A 88 4211 7700 12615 186 -337 -2995 C
ATOM 519 CG LEU A 88 -18.684 43.049 98.153 1.00 60.72 C
ANISOU 519 CG LEU A 88 3956 7312 11804 300 -625 -2719 C
ATOM 520 CD1 LEU A 88 -20.089 42.880 97.588 1.00 55.17 C
ANISOU 520 CD1 LEU A 88 3508 6660 10794 327 -557 -2379 C
ATOM 521 CD2 LEU A 88 -18.401 41.931 99.160 1.00 58.98 C
ANISOU 521 CD2 LEU A 88 3768 7155 11487 463 -992 -2698 C
ATOM 522 N SER A 89 -16.486 46.149 96.851 1.00 77.28 N
ANISOU 522 N SER A 89 5528 9101 14733 -222 274 -3507 N
ATOM 523 CA SER A 89 -16.323 47.526 97.338 1.00 76.23 C
ANISOU 523 CA SER A 89 5336 8911 14715 -365 422 -3657 C
ATOM 524 C SER A 89 -16.683 48.579 96.282 1.00 77.12 C
ANISOU 524 C SER A 89 5554 8887 14863 -573 900 -3649 C
ATOM 525 O SER A 89 -17.186 49.655 96.625 1.00 78.50 O
ANISOU 525 O SER A 89 5815 9020 14992 -661 1014 -3608 O
ATOM 526 CB SER A 89 -14.878 47.759 97.800 1.00 80.86 C
ANISOU 526 CB SER A 89 5628 9477 15618 -423 408 -4049 C
ATOM 527 OG SER A 89 -14.553 47.063 98.992 1.00 83.47 O
ANISOU 527 OG SER A 89 5882 9916 15919 -243 -27 -4068 O
ATOM 528 N LEU A 90 -16.355 48.322 95.005 1.00 78.01 N
ANISOU 528 N LEU A 90 5669 8907 15062 -667 1209 -3707 N
ATOM 529 CA LEU A 90 -16.719 49.255 93.934 1.00 77.58 C
ANISOU 529 CA LEU A 90 5787 8694 14997 -865 1692 -3672 C
ATOM 530 C LEU A 90 -18.234 49.369 93.812 1.00 77.51 C
ANISOU 530 C LEU A 90 6053 8713 14685 -787 1669 -3286 C
ATOM 531 O LEU A 90 -18.781 50.473 93.681 1.00 80.66 O
ANISOU 531 O LEU A 90 6609 9007 15030 -906 1931 -3222 O
ATOM 532 CB LEU A 90 -16.109 48.809 92.596 1.00 75.01 C
ANISOU 532 CB LEU A 90 5450 8265 14784 -967 2005 -3786 C
ATOM 533 CG LEU A 90 -14.594 48.911 92.363 1.00 74.60 C
ANISOU 533 CG LEU A 90 5144 8137 15063 -1106 2186 -4207 C
ATOM 534 CD1 LEU A 90 -14.230 48.548 90.929 1.00 73.22 C
ANISOU 534 CD1 LEU A 90 5032 7839 14949 -1225 2543 -4271 C
ATOM 535 CD2 LEU A 90 -14.069 50.300 92.698 1.00 74.61 C
ANISOU 535 CD2 LEU A 90 5095 8035 15217 -1307 2447 -4456 C
ATOM 536 N ALA A 91 -18.915 48.218 93.862 1.00 74.06 N
ANISOU 536 N ALA A 91 5683 8413 14042 -585 1364 -3035 N
ATOM 537 CA ALA A 91 -20.374 48.144 93.877 1.00 68.37 C
ANISOU 537 CA ALA A 91 5191 7765 13021 -468 1269 -2672 C
ATOM 538 C ALA A 91 -20.960 48.814 95.118 1.00 73.24 C
ANISOU 538 C ALA A 91 5833 8444 13552 -419 1051 -2605 C
ATOM 539 O ALA A 91 -22.001 49.479 95.037 1.00 75.35 O
ANISOU 539 O ALA A 91 6269 8687 13673 -422 1168 -2408 O
ATOM 540 CB ALA A 91 -20.802 46.676 93.821 1.00 62.33 C
ANISOU 540 CB ALA A 91 4472 7149 12059 -265 957 -2469 C
ATOM 541 N ASP A 92 -20.313 48.609 96.277 1.00 75.24 N
ANISOU 541 N ASP A 92 5930 8774 13885 -360 734 -2761 N
ATOM 542 CA ASP A 92 -20.748 49.217 97.539 1.00 75.83 C
ANISOU 542 CA ASP A 92 6026 8903 13883 -322 514 -2726 C
ATOM 543 C ASP A 92 -20.563 50.739 97.526 1.00 73.69 C
ANISOU 543 C ASP A 92 5727 8491 13781 -528 849 -2892 C
ATOM 544 O ASP A 92 -21.357 51.466 98.132 1.00 69.72 O
ANISOU 544 O ASP A 92 5321 7993 13178 -529 814 -2782 O
ATOM 545 CB ASP A 92 -20.001 48.592 98.737 1.00 81.54 C
ANISOU 545 CB ASP A 92 6618 9722 14640 -214 124 -2857 C
ATOM 546 CG ASP A 92 -20.505 47.173 99.132 1.00 85.66 C
ANISOU 546 CG ASP A 92 7272 10380 14897 -3 -243 -2623 C
ATOM 547 OD1 ASP A 92 -21.578 46.727 98.667 1.00 81.51 O
ANISOU 547 OD1 ASP A 92 6938 9907 14127 70 -248 -2343 O
ATOM 548 OD2 ASP A 92 -19.825 46.516 99.961 1.00 90.40 O
ANISOU 548 OD2 ASP A 92 7795 11031 15525 87 -517 -2722 O
ATOM 549 N VAL A 93 -19.496 51.237 96.870 1.00 76.81 N
ANISOU 549 N VAL A 93 6004 8752 14427 -713 1188 -3170 N
ATOM 550 CA VAL A 93 -19.248 52.682 96.751 1.00 74.83 C
ANISOU 550 CA VAL A 93 5778 8342 14313 -942 1574 -3337 C
ATOM 551 C VAL A 93 -20.270 53.331 95.811 1.00 74.41 C
ANISOU 551 C VAL A 93 6009 8150 14113 -1026 1953 -3110 C
ATOM 552 O VAL A 93 -20.780 54.424 96.092 1.00 75.01 O
ANISOU 552 O VAL A 93 6215 8132 14152 -1124 2130 -3069 O
ATOM 553 CB VAL A 93 -17.788 52.940 96.302 1.00 75.58 C
ANISOU 553 CB VAL A 93 5690 8340 14688 -1114 1836 -3706 C
ATOM 554 CG1 VAL A 93 -17.598 54.339 95.695 1.00 73.30 C
ANISOU 554 CG1 VAL A 93 5536 7839 14478 -1383 2372 -3839 C
ATOM 555 CG2 VAL A 93 -16.824 52.765 97.476 1.00 79.20 C
ANISOU 555 CG2 VAL A 93 5874 8911 15306 -1056 1511 -3953 C
ATOM 556 N LEU A 94 -20.595 52.660 94.694 1.00 75.02 N
ANISOU 556 N LEU A 94 6210 8204 14089 -983 2086 -2947 N
ATOM 557 CA LEU A 94 -21.632 53.129 93.771 1.00 73.49 C
ANISOU 557 CA LEU A 94 6329 7887 13705 -1014 2422 -2683 C
ATOM 558 C LEU A 94 -22.937 53.410 94.514 1.00 71.71 C
ANISOU 558 C LEU A 94 6210 7747 13289 -871 2233 -2420 C
ATOM 559 O LEU A 94 -23.547 54.474 94.351 1.00 78.20 O
ANISOU 559 O LEU A 94 7255 8421 14036 -955 2545 -2321 O
ATOM 560 CB LEU A 94 -21.860 52.086 92.664 1.00 72.60 C
ANISOU 560 CB LEU A 94 6309 7805 13473 -923 2459 -2519 C
ATOM 561 CG LEU A 94 -23.000 52.304 91.652 1.00 72.80 C
ANISOU 561 CG LEU A 94 6687 7736 13238 -885 2749 -2200 C
ATOM 562 CD1 LEU A 94 -22.747 53.531 90.779 1.00 76.52 C
ANISOU 562 CD1 LEU A 94 7454 7911 13708 -1124 3313 -2266 C
ATOM 563 CD2 LEU A 94 -23.253 51.067 90.783 1.00 70.26 C
ANISOU 563 CD2 LEU A 94 6408 7504 12782 -753 2667 -2039 C
ATOM 564 N ALA A 95 -23.352 52.456 95.350 1.00 64.61 N
ANISOU 564 N ALA A 95 5187 7074 12288 -650 1733 -2308 N
ATOM 565 CA ALA A 95 -24.578 52.564 96.134 1.00 60.57 C
ANISOU 565 CA ALA A 95 4757 6674 11583 -484 1495 -2075 C
ATOM 566 C ALA A 95 -24.465 53.603 97.249 1.00 60.19 C
ANISOU 566 C ALA A 95 4638 6586 11644 -583 1453 -2223 C
ATOM 567 O ALA A 95 -25.430 54.320 97.531 1.00 62.36 O
ANISOU 567 O ALA A 95 5061 6829 11804 -543 1530 -2068 O
ATOM 568 CB ALA A 95 -24.923 51.197 96.725 1.00 56.39 C
ANISOU 568 CB ALA A 95 4180 6376 10871 -253 976 -1934 C
ATOM 569 N THR A 96 -23.303 53.680 97.910 1.00 63.84 N
ANISOU 569 N THR A 96 4905 7053 12297 -685 1324 -2515 N
ATOM 570 CA THR A 96 -23.149 54.592 99.045 1.00 69.57 C
ANISOU 570 CA THR A 96 5568 7761 13105 -773 1242 -2663 C
ATOM 571 C THR A 96 -23.051 56.051 98.579 1.00 72.63 C
ANISOU 571 C THR A 96 6086 7907 13603 -1032 1764 -2764 C
ATOM 572 O THR A 96 -23.694 56.929 99.163 1.00 69.86 O
ANISOU 572 O THR A 96 5840 7493 13212 -1090 1814 -2710 O
ATOM 573 CB THR A 96 -21.942 54.158 99.896 1.00 72.51 C
ANISOU 573 CB THR A 96 5717 8227 13607 -757 942 -2919 C
ATOM 574 OG1 THR A 96 -22.251 52.910 100.531 1.00 74.03 O
ANISOU 574 OG1 THR A 96 5910 8606 13613 -519 467 -2763 O
ATOM 575 CG2 THR A 96 -21.590 55.176 100.992 1.00 71.88 C
ANISOU 575 CG2 THR A 96 5569 8120 13623 -873 902 -3109 C
ATOM 576 N ALA A 97 -22.315 56.309 97.489 1.00 77.00 N
ANISOU 576 N ALA A 97 6697 8301 14259 -1194 2173 -2889 N
ATOM 577 CA ALA A 97 -22.143 57.677 96.987 1.00 72.88 C
ANISOU 577 CA ALA A 97 6403 7515 13772 -1449 2696 -2974 C
ATOM 578 C ALA A 97 -23.421 58.235 96.337 1.00 71.64 C
ANISOU 578 C ALA A 97 6635 7190 13395 -1446 3009 -2648 C
ATOM 579 O ALA A 97 -23.807 59.379 96.616 1.00 70.30 O
ANISOU 579 O ALA A 97 6776 6845 13090 -1516 3174 -2592 O
ATOM 580 CB ALA A 97 -20.972 57.726 96.002 1.00 69.31 C
ANISOU 580 CB ALA A 97 5938 6945 13453 -1606 3032 -3205 C
ATOM 581 N ILE A 98 -24.074 57.471 95.464 1.00 68.70 N
ANISOU 581 N ILE A 98 6425 6864 12812 -1254 3004 -2381 N
ATOM 582 CA ILE A 98 -25.200 57.972 94.647 1.00 65.62 C
ANISOU 582 CA ILE A 98 6603 6312 12016 -1120 3211 -2021 C
ATOM 583 C ILE A 98 -26.566 57.630 95.262 1.00 67.66 C
ANISOU 583 C ILE A 98 7019 6745 11943 -782 2790 -1695 C
ATOM 584 O ILE A 98 -27.425 58.495 95.410 1.00 73.83 O
ANISOU 584 O ILE A 98 8173 7411 12469 -692 2842 -1506 O
ATOM 585 CB ILE A 98 -25.096 57.437 93.193 1.00 64.25 C
ANISOU 585 CB ILE A 98 6568 6061 11782 -1135 3502 -1932 C
ATOM 586 CG1 ILE A 98 -23.778 57.850 92.485 1.00 61.50 C
ANISOU 586 CG1 ILE A 98 6143 5515 11707 -1474 3955 -2255 C
ATOM 587 CG2 ILE A 98 -26.342 57.812 92.362 1.00 64.24 C
ANISOU 587 CG2 ILE A 98 7150 5925 11334 -944 3628 -1541 C
ATOM 588 CD1 ILE A 98 -23.312 59.334 92.567 1.00 63.58 C
ANISOU 588 CD1 ILE A 98 6656 5506 11997 -1723 4321 -2423 C
ATOM 589 N CYS A 99 -26.786 56.354 95.622 1.00 64.05 N
ANISOU 589 N CYS A 99 6286 6563 11489 -594 2378 -1636 N
ATOM 590 CA CYS A 99 -28.105 55.889 96.058 1.00 59.30 C
ANISOU 590 CA CYS A 99 5833 6135 10562 -293 2016 -1330 C
ATOM 591 C CYS A 99 -28.417 56.233 97.519 1.00 57.52 C
ANISOU 591 C CYS A 99 5524 6008 10322 -244 1698 -1372 C
ATOM 592 O CYS A 99 -29.568 56.532 97.847 1.00 57.73 O
ANISOU 592 O CYS A 99 5812 6066 10058 -62 1577 -1139 O
ATOM 593 CB CYS A 99 -28.237 54.385 95.812 1.00 61.68 C
ANISOU 593 CB CYS A 99 5924 6665 10847 -135 1736 -1248 C
ATOM 594 SG CYS A 99 -27.835 53.889 94.115 1.00 63.66 S
ANISOU 594 SG CYS A 99 6263 6807 11116 -201 2102 -1218 S
ATOM 595 N LEU A 100 -27.420 56.169 98.424 1.00 55.88 N
ANISOU 595 N LEU A 100 4949 5861 10423 -397 1547 -1676 N
ATOM 596 CA LEU A 100 -27.680 56.442 99.840 1.00 57.24 C
ANISOU 596 CA LEU A 100 5055 6126 10566 -361 1228 -1725 C
ATOM 597 C LEU A 100 -28.289 57.823 100.093 1.00 67.04 C
ANISOU 597 C LEU A 100 6657 7182 11634 -390 1436 -1641 C
ATOM 598 O LEU A 100 -29.269 57.909 100.845 1.00 67.57 O
ANISOU 598 O LEU A 100 6870 7337 11468 -222 1203 -1476 O
ATOM 599 CB LEU A 100 -26.407 56.224 100.673 1.00 58.62 C
ANISOU 599 CB LEU A 100 4787 6372 11113 -535 1047 -2091 C
ATOM 600 CG LEU A 100 -26.488 56.362 102.209 1.00 58.06 C
ANISOU 600 CG LEU A 100 4611 6411 11039 -517 667 -2186 C
ATOM 601 CD1 LEU A 100 -25.455 55.492 102.916 1.00 60.02 C
ANISOU 601 CD1 LEU A 100 4472 6815 11519 -536 310 -2434 C
ATOM 602 CD2 LEU A 100 -26.312 57.807 102.653 1.00 56.96 C
ANISOU 602 CD2 LEU A 100 4626 6079 10938 -710 905 -2316 C
ATOM 603 N PRO A 101 -27.781 58.933 99.516 1.00 66.28 N
ANISOU 603 N PRO A 101 6735 6819 11629 -599 1876 -1750 N
ATOM 604 CA PRO A 101 -28.424 60.233 99.794 1.00 57.80 C
ANISOU 604 CA PRO A 101 6041 5553 10367 -598 2054 -1657 C
ATOM 605 C PRO A 101 -29.841 60.343 99.242 1.00 59.03 C
ANISOU 605 C PRO A 101 6604 5685 10140 -319 2074 -1287 C
ATOM 606 O PRO A 101 -30.712 60.930 99.895 1.00 63.29 O
ANISOU 606 O PRO A 101 7351 6213 10485 -188 1978 -1168 O
ATOM 607 CB PRO A 101 -27.478 61.253 99.129 1.00 59.37 C
ANISOU 607 CB PRO A 101 6350 5456 10753 -901 2549 -1861 C
ATOM 608 CG PRO A 101 -26.200 60.510 98.863 1.00 66.46 C
ANISOU 608 CG PRO A 101 6809 6438 12004 -1094 2569 -2143 C
ATOM 609 CD PRO A 101 -26.608 59.080 98.638 1.00 67.69 C
ANISOU 609 CD PRO A 101 6788 6849 12082 -854 2243 -1978 C
ATOM 610 N ALA A 102 -30.083 59.790 98.042 1.00 58.79 N
ANISOU 610 N ALA A 102 6686 5649 10002 -224 2195 -1118 N
ATOM 611 CA ALA A 102 -31.421 59.777 97.449 1.00 56.42 C
ANISOU 611 CA ALA A 102 6737 5357 9344 56 2174 -778 C
ATOM 612 C ALA A 102 -32.399 59.008 98.328 1.00 59.25 C
ANISOU 612 C ALA A 102 6967 6005 9540 297 1726 -636 C
ATOM 613 O ALA A 102 -33.561 59.408 98.483 1.00 65.07 O
ANISOU 613 O ALA A 102 7956 6751 10016 506 1662 -434 O
ATOM 614 CB ALA A 102 -31.361 59.157 96.049 1.00 54.03 C
ANISOU 614 CB ALA A 102 6523 5024 8980 86 2345 -659 C
ATOM 615 N SER A 103 -31.924 57.908 98.917 1.00 55.57 N
ANISOU 615 N SER A 103 6114 5770 9232 266 1420 -756 N
ATOM 616 CA SER A 103 -32.706 57.088 99.837 1.00 52.40 C
ANISOU 616 CA SER A 103 5583 5636 8691 445 997 -658 C
ATOM 617 C SER A 103 -32.995 57.819 101.156 1.00 59.15 C
ANISOU 617 C SER A 103 6469 6490 9516 432 865 -731 C
ATOM 618 O SER A 103 -34.114 57.737 101.672 1.00 61.04 O
ANISOU 618 O SER A 103 6822 6851 9518 617 679 -570 O
ATOM 619 CB SER A 103 -31.955 55.773 100.080 1.00 45.20 C
ANISOU 619 CB SER A 103 4289 4918 7969 396 730 -790 C
ATOM 620 OG SER A 103 -32.638 54.902 100.963 1.00 48.54 O
ANISOU 620 OG SER A 103 4614 5580 8249 544 328 -704 O
ATOM 621 N LEU A 104 -32.003 58.542 101.706 1.00 62.74 N
ANISOU 621 N LEU A 104 6821 6810 10207 204 970 -989 N
ATOM 622 CA LEU A 104 -32.206 59.284 102.958 1.00 59.18 C
ANISOU 622 CA LEU A 104 6417 6341 9730 167 862 -1078 C
ATOM 623 C LEU A 104 -33.267 60.374 102.794 1.00 57.27 C
ANISOU 623 C LEU A 104 6575 5944 9242 301 1067 -896 C
ATOM 624 O LEU A 104 -34.116 60.555 103.674 1.00 54.91 O
ANISOU 624 O LEU A 104 6359 5728 8776 423 892 -827 O
ATOM 625 CB LEU A 104 -30.880 59.897 103.452 1.00 59.45 C
ANISOU 625 CB LEU A 104 6268 6245 10074 -124 965 -1406 C
ATOM 626 CG LEU A 104 -30.861 61.008 104.532 1.00 57.85 C
ANISOU 626 CG LEU A 104 6172 5930 9880 -236 987 -1543 C
ATOM 627 CD1 LEU A 104 -31.358 60.537 105.897 1.00 55.56 C
ANISOU 627 CD1 LEU A 104 5787 5846 9478 -144 570 -1543 C
ATOM 628 CD2 LEU A 104 -29.477 61.637 104.688 1.00 58.04 C
ANISOU 628 CD2 LEU A 104 6021 5803 10228 -553 1166 -1876 C
ATOM 629 N LEU A 105 -33.231 61.097 101.670 1.00 58.27 N
ANISOU 629 N LEU A 105 6966 5836 9339 285 1439 -822 N
ATOM 630 CA LEU A 105 -34.184 62.179 101.427 1.00 60.74 C
ANISOU 630 CA LEU A 105 7688 5965 9424 436 1637 -653 C
ATOM 631 C LEU A 105 -35.599 61.654 101.172 1.00 65.49 C
ANISOU 631 C LEU A 105 8408 6742 9734 762 1452 -371 C
ATOM 632 O LEU A 105 -36.577 62.277 101.596 1.00 65.27 O
ANISOU 632 O LEU A 105 8584 6692 9525 933 1428 -270 O
ATOM 633 CB LEU A 105 -33.710 63.035 100.248 1.00 60.77 C
ANISOU 633 CB LEU A 105 7981 5649 9458 326 2076 -650 C
ATOM 634 CG LEU A 105 -32.908 64.292 100.597 1.00 63.24 C
ANISOU 634 CG LEU A 105 8420 5681 9929 68 2367 -870 C
ATOM 635 CD1 LEU A 105 -32.215 64.851 99.368 1.00 66.75 C
ANISOU 635 CD1 LEU A 105 9093 5832 10436 -104 2805 -904 C
ATOM 636 CD2 LEU A 105 -33.805 65.352 101.222 1.00 68.65 C
ANISOU 636 CD2 LEU A 105 9415 6240 10427 209 2394 -787 C
ATOM 637 N VAL A 106 -35.720 60.502 100.493 1.00 67.56 N
ANISOU 637 N VAL A 106 8532 7182 9956 846 1323 -260 N
ATOM 638 CA VAL A 106 -37.038 59.918 100.220 1.00 58.71 C
ANISOU 638 CA VAL A 106 7489 6250 8569 1133 1141 -15 C
ATOM 639 C VAL A 106 -37.657 59.356 101.508 1.00 59.09 C
ANISOU 639 C VAL A 106 7345 6558 8548 1205 792 -32 C
ATOM 640 O VAL A 106 -38.872 59.455 101.710 1.00 63.64 O
ANISOU 640 O VAL A 106 8039 7232 8907 1420 697 112 O
ATOM 641 CB VAL A 106 -36.949 58.850 99.102 1.00 44.26 C
ANISOU 641 CB VAL A 106 5583 4522 6712 1176 1120 96 C
ATOM 642 CG1 VAL A 106 -38.309 58.197 98.848 1.00 40.37 C
ANISOU 642 CG1 VAL A 106 5143 4246 5948 1452 914 329 C
ATOM 643 CG2 VAL A 106 -36.439 59.450 97.789 1.00 44.45 C
ANISOU 643 CG2 VAL A 106 5859 4271 6758 1105 1491 127 C
ATOM 644 N ASP A 107 -36.824 58.766 102.395 1.00 56.94 N
ANISOU 644 N ASP A 107 6782 6394 8458 1026 597 -221 N
ATOM 645 CA ASP A 107 -37.264 58.219 103.691 1.00 53.65 C
ANISOU 645 CA ASP A 107 6217 6195 7972 1053 269 -260 C
ATOM 646 C ASP A 107 -37.691 59.311 104.682 1.00 56.23 C
ANISOU 646 C ASP A 107 6697 6429 8239 1053 311 -322 C
ATOM 647 O ASP A 107 -38.343 58.997 105.686 1.00 55.90 O
ANISOU 647 O ASP A 107 6613 6553 8074 1109 86 -320 O
ATOM 648 CB ASP A 107 -36.156 57.348 104.353 1.00 57.08 C
ANISOU 648 CB ASP A 107 6337 6734 8618 868 36 -456 C
ATOM 649 CG ASP A 107 -35.950 55.948 103.694 1.00 67.96 C
ANISOU 649 CG ASP A 107 7530 8276 10016 908 -118 -390 C
ATOM 650 OD1 ASP A 107 -36.821 55.469 102.935 1.00 70.21 O
ANISOU 650 OD1 ASP A 107 7910 8654 10113 1077 -111 -183 O
ATOM 651 OD2 ASP A 107 -34.902 55.309 103.975 1.00 70.87 O
ANISOU 651 OD2 ASP A 107 7650 8685 10594 773 -262 -559 O
ATOM 652 N ILE A 108 -37.263 60.570 104.464 1.00 62.50 N
ANISOU 652 N ILE A 108 7676 6950 9121 967 607 -398 N
ATOM 653 CA ILE A 108 -37.655 61.743 105.255 1.00 64.26 C
ANISOU 653 CA ILE A 108 8094 7036 9286 973 704 -454 C
ATOM 654 C ILE A 108 -38.942 62.364 104.694 1.00 65.47 C
ANISOU 654 C ILE A 108 8541 7126 9208 1248 841 -243 C
ATOM 655 O ILE A 108 -39.961 62.441 105.390 1.00 64.84 O
ANISOU 655 O ILE A 108 8504 7164 8969 1401 718 -191 O
ATOM 656 CB ILE A 108 -36.523 62.804 105.301 1.00 61.12 C
ANISOU 656 CB ILE A 108 7766 6355 9100 727 965 -657 C
ATOM 657 CG1 ILE A 108 -35.277 62.314 106.068 1.00 64.81 C
ANISOU 657 CG1 ILE A 108 7915 6898 9813 461 792 -912 C
ATOM 658 CG2 ILE A 108 -37.022 64.117 105.918 1.00 57.29 C
ANISOU 658 CG2 ILE A 108 7553 5684 8528 758 1119 -686 C
ATOM 659 CD1 ILE A 108 -34.016 63.237 105.941 1.00 65.02 C
ANISOU 659 CD1 ILE A 108 7947 6666 10091 180 1066 -1146 C
ATOM 660 N THR A 109 -38.897 62.803 103.426 1.00 65.62 N
ANISOU 660 N THR A 109 8768 6957 9206 1316 1094 -132 N
ATOM 661 CA THR A 109 -39.971 63.559 102.782 1.00 65.22 C
ANISOU 661 CA THR A 109 9041 6787 8953 1586 1241 53 C
ATOM 662 C THR A 109 -41.078 62.695 102.176 1.00 68.41 C
ANISOU 662 C THR A 109 9406 7427 9160 1855 1064 265 C
ATOM 663 O THR A 109 -42.202 63.182 101.999 1.00 71.76 O
ANISOU 663 O THR A 109 10018 7843 9405 2120 1077 394 O
ATOM 664 CB THR A 109 -39.385 64.464 101.679 1.00 65.15 C
ANISOU 664 CB THR A 109 9335 6433 8985 1527 1596 76 C
ATOM 665 OG1 THR A 109 -38.873 63.654 100.613 1.00 59.56 O
ANISOU 665 OG1 THR A 109 8544 5765 8321 1470 1626 136 O
ATOM 666 CG2 THR A 109 -38.258 65.350 102.223 1.00 71.66 C
ANISOU 666 CG2 THR A 109 10199 7015 10014 1228 1803 -156 C
ATOM 667 N GLU A 110 -40.775 61.421 101.867 1.00 67.49 N
ANISOU 667 N GLU A 110 9040 7521 9080 1792 894 288 N
ATOM 668 CA GLU A 110 -41.641 60.463 101.154 1.00 59.84 C
ANISOU 668 CA GLU A 110 8017 6777 7945 1994 739 473 C
ATOM 669 C GLU A 110 -42.055 60.992 99.765 1.00 61.11 C
ANISOU 669 C GLU A 110 8482 6762 7975 2182 936 649 C
ATOM 670 O GLU A 110 -43.113 60.631 99.234 1.00 63.67 O
ANISOU 670 O GLU A 110 8831 7260 8100 2359 808 792 O
ATOM 671 CB GLU A 110 -42.865 60.051 101.994 1.00 53.97 C
ANISOU 671 CB GLU A 110 7161 6302 7043 2161 495 515 C
ATOM 672 CG GLU A 110 -42.570 59.466 103.426 1.00 62.30 C
ANISOU 672 CG GLU A 110 7967 7531 8172 1982 278 354 C
ATOM 673 CD GLU A 110 -41.814 58.124 103.521 1.00 72.76 C
ANISOU 673 CD GLU A 110 9028 9025 9593 1812 80 303 C
ATOM 674 OE1 GLU A 110 -41.378 57.804 104.652 1.00 77.79 O
ANISOU 674 OE1 GLU A 110 9518 9737 10303 1656 -83 158 O
ATOM 675 OE2 GLU A 110 -41.666 57.388 102.519 1.00 73.11 O
ANISOU 675 OE2 GLU A 110 9026 9122 9630 1840 74 399 O
ATOM 676 N SER A 111 -41.187 61.820 99.164 1.00 65.00 N
ANISOU 676 N SER A 111 9194 6938 8564 2054 1228 605 N
ATOM 677 CA SER A 111 -41.376 62.411 97.838 1.00 64.82 C
ANISOU 677 CA SER A 111 9532 6683 8415 2187 1451 757 C
ATOM 678 C SER A 111 -40.052 62.437 97.071 1.00 62.70 C
ANISOU 678 C SER A 111 9320 6199 8302 1919 1709 676 C
ATOM 679 O SER A 111 -38.968 62.347 97.659 1.00 66.42 O
ANISOU 679 O SER A 111 9581 6647 9007 1637 1756 473 O
ATOM 680 CB SER A 111 -41.942 63.837 97.931 1.00 66.60 C
ANISOU 680 CB SER A 111 10108 6668 8530 2332 1605 791 C
ATOM 681 OG SER A 111 -40.968 64.751 98.409 1.00 71.90 O
ANISOU 681 OG SER A 111 10891 7053 9376 2107 1851 621 O
ATOM 682 N TRP A 112 -40.148 62.570 95.742 1.00 55.69 N
ANISOU 682 N TRP A 112 8724 5153 7283 2006 1877 824 N
ATOM 683 CA TRP A 112 -38.986 62.609 94.854 1.00 56.56 C
ANISOU 683 CA TRP A 112 8937 5044 7510 1758 2168 758 C
ATOM 684 C TRP A 112 -38.665 64.056 94.481 1.00 74.28 C
ANISOU 684 C TRP A 112 11628 6869 9725 1696 2530 739 C
ATOM 685 O TRP A 112 -39.528 64.776 93.963 1.00 86.08 O
ANISOU 685 O TRP A 112 13466 8275 10965 1909 2547 899 O
ATOM 686 CB TRP A 112 -39.225 61.757 93.601 1.00 47.39 C
ANISOU 686 CB TRP A 112 7839 3961 6204 1855 2141 923 C
ATOM 687 CG TRP A 112 -37.975 61.528 92.796 1.00 48.64 C
ANISOU 687 CG TRP A 112 8007 3959 6514 1568 2416 820 C
ATOM 688 CD1 TRP A 112 -37.633 62.129 91.620 1.00 51.67 C
ANISOU 688 CD1 TRP A 112 8801 4027 6805 1508 2753 881 C
ATOM 689 CD2 TRP A 112 -36.881 60.663 93.137 1.00 51.70 C
ANISOU 689 CD2 TRP A 112 7981 4484 7179 1299 2389 619 C
ATOM 690 NE1 TRP A 112 -36.403 61.681 91.199 1.00 57.44 N
ANISOU 690 NE1 TRP A 112 9380 4700 7745 1201 2962 719 N
ATOM 691 CE2 TRP A 112 -35.919 60.783 92.113 1.00 57.52 C
ANISOU 691 CE2 TRP A 112 8869 4990 7997 1081 2734 552 C
ATOM 692 CE3 TRP A 112 -36.626 59.794 94.203 1.00 53.65 C
ANISOU 692 CE3 TRP A 112 7761 5018 7607 1229 2102 483 C
ATOM 693 CZ2 TRP A 112 -34.722 60.067 92.124 1.00 60.78 C
ANISOU 693 CZ2 TRP A 112 8938 5467 8691 809 2800 341 C
ATOM 694 CZ3 TRP A 112 -35.436 59.084 94.213 1.00 58.68 C
ANISOU 694 CZ3 TRP A 112 8083 5706 8508 979 2140 289 C
ATOM 695 CH2 TRP A 112 -34.500 59.225 93.179 1.00 63.03 C
ANISOU 695 CH2 TRP A 112 8750 6040 9161 777 2487 211 C
ATOM 696 N LEU A 113 -37.425 64.482 94.748 1.00 73.22 N
ANISOU 696 N LEU A 113 11440 6552 9828 1358 2777 517 N
ATOM 697 CA LEU A 113 -37.011 65.863 94.531 1.00 69.90 C
ANISOU 697 CA LEU A 113 11432 5723 9403 1238 3145 460 C
ATOM 698 C LEU A 113 -35.872 66.014 93.504 1.00 72.71 C
ANISOU 698 C LEU A 113 11958 5816 9854 941 3533 370 C
ATOM 699 O LEU A 113 -35.337 67.119 93.363 1.00 80.53 O
ANISOU 699 O LEU A 113 13232 6513 10852 751 3851 280 O
ATOM 700 CB LEU A 113 -36.630 66.500 95.883 1.00 66.80 C
ANISOU 700 CB LEU A 113 10879 5307 9195 1080 3136 246 C
ATOM 701 CG LEU A 113 -37.675 66.449 97.024 1.00 64.93 C
ANISOU 701 CG LEU A 113 10489 5304 8878 1327 2799 294 C
ATOM 702 CD1 LEU A 113 -37.066 66.805 98.381 1.00 68.99 C
ANISOU 702 CD1 LEU A 113 10769 5839 9605 1101 2767 46 C
ATOM 703 CD2 LEU A 113 -38.899 67.334 96.756 1.00 61.78 C
ANISOU 703 CD2 LEU A 113 10504 4770 8200 1663 2807 497 C
ATOM 704 N PHE A 114 -35.525 64.953 92.753 1.00 67.90 N
ANISOU 704 N PHE A 114 11167 5352 9279 881 3505 393 N
ATOM 705 CA PHE A 114 -34.402 64.950 91.804 1.00 68.56 C
ANISOU 705 CA PHE A 114 11351 5224 9477 577 3878 278 C
ATOM 706 C PHE A 114 -34.815 64.949 90.325 1.00 73.59 C
ANISOU 706 C PHE A 114 12408 5743 9811 698 4018 501 C
ATOM 707 O PHE A 114 -33.948 64.812 89.454 1.00 75.04 O
ANISOU 707 O PHE A 114 12654 5810 10049 453 4308 411 O
ATOM 708 CB PHE A 114 -33.488 63.739 92.046 1.00 74.28 C
ANISOU 708 CB PHE A 114 11511 6221 10492 365 3762 82 C
ATOM 709 CG PHE A 114 -32.996 63.609 93.460 1.00 81.99 C
ANISOU 709 CG PHE A 114 12025 7384 11744 232 3559 -152 C
ATOM 710 CD1 PHE A 114 -31.955 64.397 93.925 1.00 85.96 C
ANISOU 710 CD1 PHE A 114 12476 7694 12489 -88 3816 -425 C
ATOM 711 CD2 PHE A 114 -33.566 62.686 94.321 1.00 83.53 C
ANISOU 711 CD2 PHE A 114 11852 7941 11943 414 3112 -109 C
ATOM 712 CE1 PHE A 114 -31.499 64.273 95.227 1.00 86.43 C
ANISOU 712 CE1 PHE A 114 12122 7927 12789 -205 3602 -646 C
ATOM 713 CE2 PHE A 114 -33.117 62.560 95.624 1.00 84.80 C
ANISOU 713 CE2 PHE A 114 11634 8259 12328 296 2910 -319 C
ATOM 714 CZ PHE A 114 -32.082 63.356 96.077 1.00 84.35 C
ANISOU 714 CZ PHE A 114 11525 8015 12510 -5 3142 -586 C
ATOM 715 N GLY A 115 -36.110 65.070 90.015 1.00 76.60 N
ANISOU 715 N GLY A 115 12996 6260 9849 1051 3768 748 N
ATOM 716 CA GLY A 115 -36.566 65.104 88.631 1.00 80.60 C
ANISOU 716 CA GLY A 115 13834 6768 10024 1172 3808 906 C
ATOM 717 C GLY A 115 -36.788 63.735 88.001 1.00 76.07 C
ANISOU 717 C GLY A 115 13071 6417 9415 1263 3627 1006 C
ATOM 718 O GLY A 115 -36.542 62.679 88.598 1.00 73.33 O
ANISOU 718 O GLY A 115 12336 6220 9308 1233 3483 969 O
ATOM 719 N HIS A 116 -37.225 63.769 86.728 1.00 77.33 N
ANISOU 719 N HIS A 116 13524 6584 9275 1372 3637 1110 N
ATOM 720 CA HIS A 116 -37.664 62.576 85.992 1.00 76.01 C
ANISOU 720 CA HIS A 116 13231 6652 8999 1495 3425 1212 C
ATOM 721 C HIS A 116 -36.492 61.666 85.592 1.00 76.33 C
ANISOU 721 C HIS A 116 13106 6629 9267 1217 3655 1110 C
ATOM 722 O HIS A 116 -36.612 60.437 85.647 1.00 81.91 O
ANISOU 722 O HIS A 116 13519 7555 10047 1267 3458 1164 O
ATOM 723 CB HIS A 116 -38.450 63.011 84.748 1.00 81.32 C
ANISOU 723 CB HIS A 116 14275 7309 9315 1675 3367 1298 C
ATOM 724 CG HIS A 116 -39.624 63.896 85.056 1.00 90.50 C
ANISOU 724 CG HIS A 116 15576 8531 10279 1943 3147 1374 C
ATOM 725 ND1 HIS A 116 -40.855 63.418 85.447 1.00 91.02 N
ANISOU 725 ND1 HIS A 116 15393 8924 10265 2197 2737 1455 N
ATOM 726 CD2 HIS A 116 -39.728 65.245 85.052 1.00 95.93 C
ANISOU 726 CD2 HIS A 116 16612 8990 10847 1975 3297 1357 C
ATOM 727 CE1 HIS A 116 -41.670 64.430 85.664 1.00 91.70 C
ANISOU 727 CE1 HIS A 116 15653 8978 10209 2376 2649 1480 C
ATOM 728 NE2 HIS A 116 -41.013 65.557 85.432 1.00 95.04 N
ANISOU 728 NE2 HIS A 116 16455 9059 10596 2263 2977 1436 N
ATOM 729 N ALA A 117 -35.363 62.255 85.153 1.00 72.44 N
ANISOU 729 N ALA A 117 12788 5854 8884 915 4075 939 N
ATOM 730 CA ALA A 117 -34.205 61.482 84.689 1.00 67.57 C
ANISOU 730 CA ALA A 117 11992 5182 8499 621 4327 785 C
ATOM 731 C ALA A 117 -33.572 60.651 85.813 1.00 74.33 C
ANISOU 731 C ALA A 117 12332 6131 9780 465 4274 673 C
ATOM 732 O ALA A 117 -33.339 59.447 85.649 1.00 82.09 O
ANISOU 732 O ALA A 117 12991 7327 10873 437 4152 647 O
ATOM 733 CB ALA A 117 -33.162 62.419 84.070 1.00 64.69 C
ANISOU 733 CB ALA A 117 11889 4525 8165 326 4779 571 C
ATOM 734 N LEU A 118 -33.254 61.291 86.949 1.00 72.69 N
ANISOU 734 N LEU A 118 11948 5879 9790 369 4275 520 N
ATOM 735 CA LEU A 118 -32.650 60.617 88.101 1.00 69.03 C
ANISOU 735 CA LEU A 118 10853 5700 9675 250 4053 288 C
ATOM 736 C LEU A 118 -33.618 59.664 88.799 1.00 65.37 C
ANISOU 736 C LEU A 118 10077 5626 9135 546 3534 427 C
ATOM 737 O LEU A 118 -33.184 58.842 89.613 1.00 62.24 O
ANISOU 737 O LEU A 118 9181 5487 8981 479 3305 271 O
ATOM 738 CB LEU A 118 -32.104 61.658 89.097 1.00 69.66 C
ANISOU 738 CB LEU A 118 10871 5637 9961 70 4177 80 C
ATOM 739 CG LEU A 118 -30.948 62.540 88.585 1.00 68.37 C
ANISOU 739 CG LEU A 118 10920 5111 9948 -302 4709 -136 C
ATOM 740 CD1 LEU A 118 -30.525 63.600 89.608 1.00 65.76 C
ANISOU 740 CD1 LEU A 118 10549 4644 9792 -468 4809 -333 C
ATOM 741 CD2 LEU A 118 -29.745 61.697 88.138 1.00 62.38 C
ANISOU 741 CD2 LEU A 118 9804 4419 9478 -590 4889 -377 C
ATOM 742 N CYS A 119 -34.915 59.750 88.481 1.00 64.99 N
ANISOU 742 N CYS A 119 10321 5621 8751 869 3347 707 N
ATOM 743 CA CYS A 119 -35.880 58.755 88.927 1.00 63.27 C
ANISOU 743 CA CYS A 119 9839 5771 8431 1129 2898 842 C
ATOM 744 C CYS A 119 -35.701 57.425 88.195 1.00 64.70 C
ANISOU 744 C CYS A 119 9842 6131 8608 1107 2822 873 C
ATOM 745 O CYS A 119 -36.097 56.383 88.723 1.00 63.93 O
ANISOU 745 O CYS A 119 9403 6354 8532 1214 2477 895 O
ATOM 746 CB CYS A 119 -37.302 59.304 88.746 1.00 63.24 C
ANISOU 746 CB CYS A 119 10188 5754 8086 1474 2744 1102 C
ATOM 747 SG CYS A 119 -38.674 58.159 89.103 1.00 64.80 S
ANISOU 747 SG CYS A 119 10124 6392 8104 1798 2234 1279 S
ATOM 748 N LYS A 120 -35.085 57.444 87.014 1.00 64.78 N
ANISOU 748 N LYS A 120 10092 5929 8593 953 3154 863 N
ATOM 749 CA LYS A 120 -34.723 56.210 86.324 1.00 63.94 C
ANISOU 749 CA LYS A 120 9806 5962 8526 886 3136 848 C
ATOM 750 C LYS A 120 -33.303 55.775 86.682 1.00 67.13 C
ANISOU 750 C LYS A 120 9796 6380 9329 580 3282 539 C
ATOM 751 O LYS A 120 -33.084 54.608 87.032 1.00 72.01 O
ANISOU 751 O LYS A 120 10007 7259 10097 583 3044 465 O
ATOM 752 CB LYS A 120 -34.887 56.387 84.808 1.00 66.94 C
ANISOU 752 CB LYS A 120 10684 6115 8636 897 3406 1006 C
ATOM 753 CG LYS A 120 -36.340 56.481 84.356 1.00 67.01 C
ANISOU 753 CG LYS A 120 11000 6213 8246 1238 3146 1283 C
ATOM 754 CD LYS A 120 -36.462 56.310 82.854 1.00 70.38 C
ANISOU 754 CD LYS A 120 11697 6611 8434 1237 3208 1287 C
ATOM 755 CE LYS A 120 -37.912 56.343 82.406 1.00 75.57 C
ANISOU 755 CE LYS A 120 12468 7482 8763 1528 2834 1411 C
ATOM 756 NZ LYS A 120 -38.584 55.026 82.576 1.00 76.65 N
ANISOU 756 NZ LYS A 120 12274 7976 8871 1647 2474 1478 N
ATOM 757 N VAL A 121 -32.354 56.724 86.669 1.00 65.68 N
ANISOU 757 N VAL A 121 9704 5921 9328 321 3653 346 N
ATOM 758 CA VAL A 121 -30.932 56.449 86.871 1.00 63.34 C
ANISOU 758 CA VAL A 121 9031 5606 9428 9 3849 18 C
ATOM 759 C VAL A 121 -30.652 55.899 88.280 1.00 59.73 C
ANISOU 759 C VAL A 121 8016 5428 9250 22 3484 -154 C
ATOM 760 O VAL A 121 -30.008 54.857 88.431 1.00 60.61 O
ANISOU 760 O VAL A 121 7718 5718 9592 -44 3362 -308 O
ATOM 761 CB VAL A 121 -30.084 57.704 86.582 1.00 65.36 C
ANISOU 761 CB VAL A 121 9538 5500 9794 -280 4339 -156 C
ATOM 762 CG1 VAL A 121 -28.589 57.432 86.783 1.00 62.98 C
ANISOU 762 CG1 VAL A 121 8801 5196 9932 -616 4551 -535 C
ATOM 763 CG2 VAL A 121 -30.325 58.221 85.166 1.00 70.19 C
ANISOU 763 CG2 VAL A 121 10758 5807 10103 -304 4708 15 C
ATOM 764 N ILE A 122 -31.081 56.601 89.331 1.00 60.21 N
ANISOU 764 N ILE A 122 8069 5512 9297 102 3311 -142 N
ATOM 765 CA ILE A 122 -30.719 56.212 90.699 1.00 60.13 C
ANISOU 765 CA ILE A 122 7580 5724 9544 79 2994 -327 C
ATOM 766 C ILE A 122 -31.334 54.854 91.076 1.00 59.04 C
ANISOU 766 C ILE A 122 7177 5923 9334 296 2545 -210 C
ATOM 767 O ILE A 122 -30.591 53.981 91.536 1.00 56.37 O
ANISOU 767 O ILE A 122 6423 5742 9253 218 2382 -397 O
ATOM 768 CB ILE A 122 -30.995 57.347 91.699 1.00 59.98 C
ANISOU 768 CB ILE A 122 7655 5620 9514 85 2958 -355 C
ATOM 769 CG1 ILE A 122 -30.138 58.575 91.309 1.00 60.16 C
ANISOU 769 CG1 ILE A 122 7900 5297 9662 -195 3438 -529 C
ATOM 770 CG2 ILE A 122 -30.629 56.920 93.139 1.00 61.49 C
ANISOU 770 CG2 ILE A 122 7379 6040 9945 59 2609 -545 C
ATOM 771 CD1 ILE A 122 -30.437 59.893 92.033 1.00 61.35 C
ANISOU 771 CD1 ILE A 122 8278 5277 9754 -203 3504 -534 C
ATOM 772 N PRO A 123 -32.649 54.582 90.919 1.00 57.78 N
ANISOU 772 N PRO A 123 7224 5887 8842 565 2325 77 N
ATOM 773 CA PRO A 123 -33.129 53.214 91.198 1.00 50.87 C
ANISOU 773 CA PRO A 123 6099 5319 7911 721 1944 161 C
ATOM 774 C PRO A 123 -32.431 52.143 90.357 1.00 52.87 C
ANISOU 774 C PRO A 123 6199 5610 8280 632 2024 90 C
ATOM 775 O PRO A 123 -32.246 51.013 90.832 1.00 52.89 O
ANISOU 775 O PRO A 123 5875 5828 8394 666 1744 27 O
ATOM 776 CB PRO A 123 -34.631 53.282 90.890 1.00 48.64 C
ANISOU 776 CB PRO A 123 6122 5116 7245 989 1798 465 C
ATOM 777 CG PRO A 123 -34.983 54.710 91.063 1.00 48.79 C
ANISOU 777 CG PRO A 123 6440 4928 7169 1017 1964 508 C
ATOM 778 CD PRO A 123 -33.775 55.448 90.506 1.00 54.90 C
ANISOU 778 CD PRO A 123 7314 5402 8143 749 2391 326 C
ATOM 779 N TYR A 124 -32.061 52.481 89.106 1.00 51.32 N
ANISOU 779 N TYR A 124 6263 5192 8043 522 2409 102 N
ATOM 780 CA TYR A 124 -31.329 51.571 88.222 1.00 53.05 C
ANISOU 780 CA TYR A 124 6364 5410 8381 412 2555 13 C
ATOM 781 C TYR A 124 -29.943 51.247 88.779 1.00 57.64 C
ANISOU 781 C TYR A 124 6491 6011 9397 204 2590 -330 C
ATOM 782 O TYR A 124 -29.523 50.081 88.771 1.00 62.62 O
ANISOU 782 O TYR A 124 6823 6796 10174 216 2436 -419 O
ATOM 783 CB TYR A 124 -31.211 52.186 86.812 1.00 55.13 C
ANISOU 783 CB TYR A 124 7060 5394 8493 309 3003 84 C
ATOM 784 CG TYR A 124 -30.173 51.534 85.892 1.00 54.43 C
ANISOU 784 CG TYR A 124 6861 5229 8589 112 3285 -86 C
ATOM 785 CD1 TYR A 124 -30.470 50.376 85.179 1.00 54.09 C
ANISOU 785 CD1 TYR A 124 6816 5316 8418 208 3183 27 C
ATOM 786 CD2 TYR A 124 -28.900 52.083 85.736 1.00 53.99 C
ANISOU 786 CD2 TYR A 124 6701 4972 8841 -182 3670 -375 C
ATOM 787 CE1 TYR A 124 -29.526 49.774 84.350 1.00 54.17 C
ANISOU 787 CE1 TYR A 124 6726 5254 8603 32 3454 -140 C
ATOM 788 CE2 TYR A 124 -27.950 51.485 84.907 1.00 54.36 C
ANISOU 788 CE2 TYR A 124 6627 4957 9072 -366 3939 -556 C
ATOM 789 CZ TYR A 124 -28.271 50.333 84.218 1.00 54.39 C
ANISOU 789 CZ TYR A 124 6641 5087 8939 -250 3815 -432 C
ATOM 790 OH TYR A 124 -27.339 49.735 83.396 1.00 57.09 O
ANISOU 790 OH TYR A 124 6916 5358 9416 -418 3941 -604 O
ATOM 791 N LEU A 125 -29.226 52.266 89.264 1.00 57.33 N
ANISOU 791 N LEU A 125 6395 5815 9572 20 2785 -534 N
ATOM 792 CA LEU A 125 -27.893 52.067 89.830 1.00 58.99 C
ANISOU 792 CA LEU A 125 6151 6048 10214 -180 2810 -891 C
ATOM 793 C LEU A 125 -27.938 51.276 91.138 1.00 62.16 C
ANISOU 793 C LEU A 125 6158 6720 10741 -47 2306 -955 C
ATOM 794 O LEU A 125 -26.969 50.588 91.474 1.00 70.58 O
ANISOU 794 O LEU A 125 6831 7875 12111 -124 2188 -1201 O
ATOM 795 CB LEU A 125 -27.202 53.418 90.048 1.00 58.06 C
ANISOU 795 CB LEU A 125 6096 5697 10269 -422 3140 -1093 C
ATOM 796 CG LEU A 125 -26.760 54.196 88.800 1.00 60.40 C
ANISOU 796 CG LEU A 125 6735 5682 10531 -642 3707 -1131 C
ATOM 797 CD1 LEU A 125 -26.092 55.508 89.180 1.00 61.57 C
ANISOU 797 CD1 LEU A 125 6930 5610 10854 -894 4005 -1347 C
ATOM 798 CD2 LEU A 125 -25.834 53.365 87.922 1.00 62.80 C
ANISOU 798 CD2 LEU A 125 6876 5977 11008 -780 3853 -1298 C
ATOM 799 N GLN A 126 -29.044 51.381 91.892 1.00 57.06 N
ANISOU 799 N GLN A 126 5641 6196 9844 151 1992 -742 N
ATOM 800 CA GLN A 126 -29.221 50.580 93.107 1.00 57.07 C
ANISOU 800 CA GLN A 126 5346 6443 9896 281 1513 -769 C
ATOM 801 C GLN A 126 -29.348 49.104 92.760 1.00 55.95 C
ANISOU 801 C GLN A 126 5066 6477 9713 406 1295 -697 C
ATOM 802 O GLN A 126 -28.713 48.247 93.392 1.00 55.08 O
ANISOU 802 O GLN A 126 4714 6498 9715 389 990 -835 O
ATOM 803 CB GLN A 126 -30.454 51.066 93.883 1.00 56.23 C
ANISOU 803 CB GLN A 126 5452 6412 9502 446 1289 -554 C
ATOM 804 CG GLN A 126 -30.768 50.310 95.188 1.00 58.16 C
ANISOU 804 CG GLN A 126 5467 6893 9739 567 810 -561 C
ATOM 805 CD GLN A 126 -29.613 50.351 96.169 1.00 70.86 C
ANISOU 805 CD GLN A 126 6718 8509 11695 427 684 -873 C
ATOM 806 OE1 GLN A 126 -29.279 51.406 96.706 1.00 81.60 O
ANISOU 806 OE1 GLN A 126 8085 9756 13163 306 793 -1004 O
ATOM 807 NE2 GLN A 126 -29.027 49.189 96.447 1.00 69.91 N
ANISOU 807 NE2 GLN A 126 6456 8522 11585 420 398 -945 N
ATOM 808 N ALA A 127 -30.159 48.810 91.741 1.00 50.68 N
ANISOU 808 N ALA A 127 4689 5806 8760 508 1395 -451 N
ATOM 809 CA ALA A 127 -30.348 47.458 91.229 1.00 37.34 C
ANISOU 809 CA ALA A 127 2936 4258 6996 611 1244 -365 C
ATOM 810 C ALA A 127 -29.043 46.888 90.677 1.00 40.21 C
ANISOU 810 C ALA A 127 3093 4561 7624 450 1387 -602 C
ATOM 811 O ALA A 127 -28.688 45.737 90.962 1.00 49.06 O
ANISOU 811 O ALA A 127 4082 5827 8734 477 1083 -650 O
ATOM 812 CB ALA A 127 -31.428 47.475 90.147 1.00 34.80 C
ANISOU 812 CB ALA A 127 3008 3912 6301 719 1369 -72 C
ATOM 813 N VAL A 128 -28.337 47.677 89.854 1.00 38.11 N
ANISOU 813 N VAL A 128 2899 4072 7511 263 1841 -732 N
ATOM 814 CA VAL A 128 -27.039 47.270 89.303 1.00 46.55 C
ANISOU 814 CA VAL A 128 3826 5063 8796 77 1974 -970 C
ATOM 815 C VAL A 128 -26.058 46.962 90.432 1.00 49.11 C
ANISOU 815 C VAL A 128 3837 5477 9347 25 1651 -1216 C
ATOM 816 O VAL A 128 -25.330 45.962 90.388 1.00 52.15 O
ANISOU 816 O VAL A 128 4075 5926 9814 26 1486 -1330 O
ATOM 817 CB VAL A 128 -26.496 48.354 88.343 1.00 48.20 C
ANISOU 817 CB VAL A 128 4231 4996 9087 -149 2517 -1071 C
ATOM 818 CG1 VAL A 128 -25.000 48.165 88.048 1.00 49.43 C
ANISOU 818 CG1 VAL A 128 4191 5058 9533 -365 2634 -1390 C
ATOM 819 CG2 VAL A 128 -27.274 48.359 87.026 1.00 48.87 C
ANISOU 819 CG2 VAL A 128 4707 4978 8884 -100 2819 -826 C
ATOM 820 N SER A 129 -26.057 47.798 91.475 1.00 53.95 N
ANISOU 820 N SER A 129 4375 6086 10039 -1 1555 -1289 N
ATOM 821 CA SER A 129 -25.181 47.613 92.628 1.00 60.75 C
ANISOU 821 CA SER A 129 4996 7016 11071 -36 1247 -1509 C
ATOM 822 C SER A 129 -25.438 46.282 93.340 1.00 58.09 C
ANISOU 822 C SER A 129 4630 6887 10553 145 770 -1401 C
ATOM 823 O SER A 129 -24.491 45.591 93.743 1.00 58.16 O
ANISOU 823 O SER A 129 4496 6927 10676 136 585 -1568 O
ATOM 824 CB SER A 129 -25.371 48.792 93.586 1.00 65.69 C
ANISOU 824 CB SER A 129 5600 7599 11759 -84 1243 -1565 C
ATOM 825 OG SER A 129 -24.596 48.649 94.759 1.00 75.08 O
ANISOU 825 OG SER A 129 6599 8853 13076 -101 936 -1763 O
ATOM 826 N VAL A 130 -26.715 45.914 93.505 1.00 52.59 N
ANISOU 826 N VAL A 130 4105 6323 9555 310 590 -1122 N
ATOM 827 CA VAL A 130 -27.112 44.671 94.176 1.00 48.16 C
ANISOU 827 CA VAL A 130 3610 5945 8742 450 194 -985 C
ATOM 828 C VAL A 130 -26.700 43.455 93.343 1.00 51.32 C
ANISOU 828 C VAL A 130 3999 6368 9132 473 205 -986 C
ATOM 829 O VAL A 130 -26.149 42.475 93.867 1.00 52.74 O
ANISOU 829 O VAL A 130 4136 6605 9296 507 -26 -1044 O
ATOM 830 CB VAL A 130 -28.633 44.709 94.453 1.00 44.97 C
ANISOU 830 CB VAL A 130 3417 5667 8003 587 66 -703 C
ATOM 831 CG1 VAL A 130 -29.186 43.359 94.893 1.00 39.82 C
ANISOU 831 CG1 VAL A 130 2910 5192 7029 687 -226 -533 C
ATOM 832 CG2 VAL A 130 -28.965 45.772 95.519 1.00 48.31 C
ANISOU 832 CG2 VAL A 130 3842 6079 8436 575 -8 -722 C
ATOM 833 N SER A 131 -26.957 43.517 92.032 1.00 49.88 N
ANISOU 833 N SER A 131 3874 6119 8959 457 500 -923 N
ATOM 834 CA SER A 131 -26.571 42.480 91.077 1.00 47.34 C
ANISOU 834 CA SER A 131 3542 5794 8653 463 573 -939 C
ATOM 835 C SER A 131 -25.056 42.237 91.076 1.00 48.86 C
ANISOU 835 C SER A 131 3523 5894 9148 352 616 -1231 C
ATOM 836 O SER A 131 -24.604 41.088 91.162 1.00 46.86 O
ANISOU 836 O SER A 131 3218 5698 8889 411 434 -1269 O
ATOM 837 CB SER A 131 -27.065 42.885 89.682 1.00 48.64 C
ANISOU 837 CB SER A 131 3842 5855 8784 434 958 -838 C
ATOM 838 OG SER A 131 -26.811 41.907 88.690 1.00 52.47 O
ANISOU 838 OG SER A 131 4345 6332 9259 438 1052 -838 O
ATOM 839 N VAL A 132 -24.256 43.306 90.957 1.00 52.86 N
ANISOU 839 N VAL A 132 3915 6248 9921 188 874 -1449 N
ATOM 840 CA VAL A 132 -22.801 43.151 90.998 1.00 54.09 C
ANISOU 840 CA VAL A 132 3854 6322 10377 83 913 -1758 C
ATOM 841 C VAL A 132 -22.372 42.507 92.317 1.00 54.27 C
ANISOU 841 C VAL A 132 3769 6450 10401 188 495 -1829 C
ATOM 842 O VAL A 132 -21.572 41.561 92.326 1.00 55.40 O
ANISOU 842 O VAL A 132 3801 6605 10643 228 375 -1954 O
ATOM 843 CB VAL A 132 -22.089 44.508 90.748 1.00 58.78 C
ANISOU 843 CB VAL A 132 4373 6734 11227 -129 1272 -1988 C
ATOM 844 CG1 VAL A 132 -20.569 44.390 90.936 1.00 64.71 C
ANISOU 844 CG1 VAL A 132 4873 7418 12295 -226 1281 -2341 C
ATOM 845 CG2 VAL A 132 -22.370 45.028 89.335 1.00 59.79 C
ANISOU 845 CG2 VAL A 132 4683 6710 11324 -254 1743 -1922 C
ATOM 846 N ALA A 133 -22.939 42.964 93.444 1.00 55.07 N
ANISOU 846 N ALA A 133 3932 6620 10371 242 277 -1737 N
ATOM 847 CA ALA A 133 -22.585 42.436 94.763 1.00 51.24 C
ANISOU 847 CA ALA A 133 3408 6212 9848 330 -87 -1787 C
ATOM 848 C ALA A 133 -22.876 40.936 94.882 1.00 53.19 C
ANISOU 848 C ALA A 133 3770 6563 9877 471 -329 -1629 C
ATOM 849 O ALA A 133 -22.006 40.160 95.295 1.00 55.30 O
ANISOU 849 O ALA A 133 3937 6824 10249 517 -490 -1771 O
ATOM 850 CB ALA A 133 -23.327 43.208 95.859 1.00 42.15 C
ANISOU 850 CB ALA A 133 2356 5109 8547 350 -235 -1681 C
ATOM 851 N VAL A 134 -24.104 40.513 94.541 1.00 50.35 N
ANISOU 851 N VAL A 134 3622 6296 9214 543 -347 -1345 N
ATOM 852 CA VAL A 134 -24.469 39.102 94.698 1.00 47.14 C
ANISOU 852 CA VAL A 134 3353 5983 8578 654 -546 -1190 C
ATOM 853 C VAL A 134 -23.747 38.222 93.655 1.00 47.33 C
ANISOU 853 C VAL A 134 3270 5958 8757 661 -439 -1296 C
ATOM 854 O VAL A 134 -23.349 37.102 93.978 1.00 54.73 O
ANISOU 854 O VAL A 134 4207 6914 9674 734 -615 -1322 O
ATOM 855 CB VAL A 134 -26.013 38.909 94.709 1.00 44.55 C
ANISOU 855 CB VAL A 134 3280 5777 7870 714 -588 -874 C
ATOM 856 CG1 VAL A 134 -26.658 38.988 93.323 1.00 39.11 C
ANISOU 856 CG1 VAL A 134 2640 5096 7126 721 -360 -759 C
ATOM 857 CG2 VAL A 134 -26.411 37.597 95.415 1.00 47.29 C
ANISOU 857 CG2 VAL A 134 3773 6171 8024 792 -836 -784 C
ATOM 858 N LEU A 135 -23.503 38.731 92.433 1.00 44.33 N
ANISOU 858 N LEU A 135 2798 5495 8550 576 -130 -1379 N
ATOM 859 CA LEU A 135 -22.735 37.951 91.448 1.00 49.61 C
ANISOU 859 CA LEU A 135 3357 6104 9390 562 3 -1510 C
ATOM 860 C LEU A 135 -21.259 37.815 91.844 1.00 51.56 C
ANISOU 860 C LEU A 135 3362 6272 9956 528 -51 -1825 C
ATOM 861 O LEU A 135 -20.637 36.782 91.580 1.00 52.36 O
ANISOU 861 O LEU A 135 3384 6363 10146 582 -111 -1918 O
ATOM 862 CB LEU A 135 -22.841 38.570 90.046 1.00 55.79 C
ANISOU 862 CB LEU A 135 4142 6793 10261 452 402 -1523 C
ATOM 863 CG LEU A 135 -24.099 38.343 89.193 1.00 54.22 C
ANISOU 863 CG LEU A 135 4158 6652 9793 509 508 -1252 C
ATOM 864 CD1 LEU A 135 -24.009 39.086 87.870 1.00 55.84 C
ANISOU 864 CD1 LEU A 135 4393 6715 10109 375 953 -1299 C
ATOM 865 CD2 LEU A 135 -24.341 36.870 88.927 1.00 53.70 C
ANISOU 865 CD2 LEU A 135 4160 6669 9575 628 351 -1147 C
ATOM 866 N THR A 136 -20.686 38.862 92.456 1.00 52.99 N
ANISOU 866 N THR A 136 3415 6396 10322 442 -24 -2005 N
ATOM 867 CA THR A 136 -19.295 38.828 92.919 1.00 58.31 C
ANISOU 867 CA THR A 136 3843 7007 11304 418 -90 -2326 C
ATOM 868 C THR A 136 -19.104 37.772 94.010 1.00 57.02 C
ANISOU 868 C THR A 136 3702 6915 11048 577 -474 -2305 C
ATOM 869 O THR A 136 -18.169 36.962 93.953 1.00 58.27 O
ANISOU 869 O THR A 136 3711 7044 11385 629 -553 -2487 O
ATOM 870 CB THR A 136 -18.891 40.228 93.421 1.00 60.71 C
ANISOU 870 CB THR A 136 4035 7247 11786 294 15 -2502 C
ATOM 871 OG1 THR A 136 -18.972 41.175 92.346 1.00 57.99 O
ANISOU 871 OG1 THR A 136 3691 6800 11541 126 421 -2543 O
ATOM 872 CG2 THR A 136 -17.472 40.262 94.006 1.00 63.41 C
ANISOU 872 CG2 THR A 136 4110 7539 12444 277 -72 -2851 C
ATOM 873 N LEU A 137 -20.003 37.768 95.005 1.00 52.14 N
ANISOU 873 N LEU A 137 3284 6379 10147 650 -697 -2086 N
ATOM 874 CA LEU A 137 -19.964 36.795 96.099 1.00 54.12 C
ANISOU 874 CA LEU A 137 3607 6656 10300 783 -1037 -2070 C
ATOM 875 C LEU A 137 -20.128 35.367 95.586 1.00 57.09 C
ANISOU 875 C LEU A 137 4060 7040 10594 880 -1111 -1995 C
ATOM 876 O LEU A 137 -19.487 34.438 96.098 1.00 62.09 O
ANISOU 876 O LEU A 137 4632 7631 11327 982 -1331 -2135 O
ATOM 877 CB LEU A 137 -21.062 37.120 97.120 1.00 47.69 C
ANISOU 877 CB LEU A 137 3017 5893 9209 809 -1197 -1867 C
ATOM 878 CG LEU A 137 -20.942 38.415 97.932 1.00 49.31 C
ANISOU 878 CG LEU A 137 3169 6092 9474 740 -1196 -1939 C
ATOM 879 CD1 LEU A 137 -22.230 38.707 98.662 1.00 46.12 C
ANISOU 879 CD1 LEU A 137 3010 5749 8765 755 -1289 -1699 C
ATOM 880 CD2 LEU A 137 -19.806 38.333 98.930 1.00 55.35 C
ANISOU 880 CD2 LEU A 137 3764 6799 10467 788 -1406 -2210 C
ATOM 881 N SER A 138 -21.007 35.182 94.587 1.00 52.13 N
ANISOU 881 N SER A 138 3569 6462 9776 857 -934 -1774 N
ATOM 882 CA SER A 138 -21.227 33.884 93.944 1.00 50.46 C
ANISOU 882 CA SER A 138 3433 6263 9477 935 -960 -1691 C
ATOM 883 C SER A 138 -19.950 33.353 93.304 1.00 51.77 C
ANISOU 883 C SER A 138 3363 6360 9947 945 -888 -1940 C
ATOM 884 O SER A 138 -19.637 32.161 93.424 1.00 56.19 O
ANISOU 884 O SER A 138 3917 6897 10535 1051 -1057 -1995 O
ATOM 885 CB SER A 138 -22.313 34.003 92.866 1.00 49.25 C
ANISOU 885 CB SER A 138 3437 6179 9096 899 -738 -1436 C
ATOM 886 OG SER A 138 -23.569 34.412 93.380 1.00 46.85 O
ANISOU 886 OG SER A 138 3345 5951 8507 898 -800 -1206 O
ATOM 887 N PHE A 139 -19.222 34.225 92.596 1.00 53.34 N
ANISOU 887 N PHE A 139 3368 6507 10393 828 -625 -2118 N
ATOM 888 CA PHE A 139 -17.993 33.831 91.907 1.00 58.14 C
ANISOU 888 CA PHE A 139 3727 7032 11332 808 -508 -2402 C
ATOM 889 C PHE A 139 -16.848 33.577 92.886 1.00 62.74 C
ANISOU 889 C PHE A 139 4115 7586 12138 878 -746 -2660 C
ATOM 890 O PHE A 139 -15.922 32.825 92.562 1.00 71.79 O
ANISOU 890 O PHE A 139 5083 8689 13505 928 -764 -2864 O
ATOM 891 CB PHE A 139 -17.582 34.905 90.881 1.00 63.72 C
ANISOU 891 CB PHE A 139 4295 7652 12265 625 -118 -2563 C
ATOM 892 CG PHE A 139 -18.416 34.928 89.604 1.00 70.61 C
ANISOU 892 CG PHE A 139 5322 8517 12991 562 167 -2375 C
ATOM 893 CD1 PHE A 139 -19.736 34.503 89.594 1.00 71.82 C
ANISOU 893 CD1 PHE A 139 5733 8766 12789 651 67 -2046 C
ATOM 894 CD2 PHE A 139 -17.866 35.391 88.412 1.00 78.96 C
ANISOU 894 CD2 PHE A 139 6277 9463 14262 405 555 -2542 C
ATOM 895 CE1 PHE A 139 -20.490 34.537 88.423 1.00 72.82 C
ANISOU 895 CE1 PHE A 139 5995 8887 12786 609 323 -1889 C
ATOM 896 CE2 PHE A 139 -18.615 35.425 87.240 1.00 80.36 C
ANISOU 896 CE2 PHE A 139 6624 9616 14293 347 832 -2373 C
ATOM 897 CZ PHE A 139 -19.927 34.998 87.247 1.00 76.94 C
ANISOU 897 CZ PHE A 139 6430 9288 13515 461 705 -2047 C
ATOM 898 N ILE A 140 -16.875 34.209 94.075 1.00 63.31 N
ANISOU 898 N ILE A 140 4201 7668 12185 889 -931 -2685 N
ATOM 899 CA ILE A 140 -15.909 33.892 95.130 1.00 69.19 C
ANISOU 899 CA ILE A 140 4783 8373 13133 987 -1213 -2938 C
ATOM 900 C ILE A 140 -16.156 32.476 95.650 1.00 74.28 C
ANISOU 900 C ILE A 140 5564 9015 13643 1164 -1521 -2861 C
ATOM 901 O ILE A 140 -15.223 31.668 95.774 1.00 81.63 O
ANISOU 901 O ILE A 140 6334 9901 14781 1268 -1672 -3078 O
ATOM 902 CB ILE A 140 -15.970 34.937 96.270 1.00 68.27 C
ANISOU 902 CB ILE A 140 4676 8264 13000 956 -1326 -2969 C
ATOM 903 CG1 ILE A 140 -15.490 36.325 95.805 1.00 67.86 C
ANISOU 903 CG1 ILE A 140 4451 8194 13137 778 -1023 -3111 C
ATOM 904 CG2 ILE A 140 -15.121 34.505 97.473 1.00 74.41 C
ANISOU 904 CG2 ILE A 140 5332 9004 13934 1089 -1664 -3196 C
ATOM 905 CD1 ILE A 140 -15.941 37.509 96.689 1.00 69.31 C
ANISOU 905 CD1 ILE A 140 4712 8402 13221 718 -1056 -3045 C
ATOM 906 N ALA A 141 -17.429 32.152 95.921 1.00 69.42 N
ANISOU 906 N ALA A 141 5250 8446 12679 1196 -1605 -2560 N
ATOM 907 CA ALA A 141 -17.843 30.823 96.374 1.00 63.30 C
ANISOU 907 CA ALA A 141 4661 7661 11730 1338 -1860 -2456 C
ATOM 908 C ALA A 141 -17.479 29.747 95.357 1.00 69.93 C
ANISOU 908 C ALA A 141 5429 8484 12657 1391 -1788 -2497 C
ATOM 909 O ALA A 141 -16.992 28.669 95.721 1.00 75.38 O
ANISOU 909 O ALA A 141 6101 9126 13413 1528 -2014 -2603 O
ATOM 910 CB ALA A 141 -19.354 30.816 96.626 1.00 52.28 C
ANISOU 910 CB ALA A 141 3590 6323 9949 1315 -1871 -2129 C
ATOM 911 N LEU A 142 -17.718 30.041 94.076 1.00 68.04 N
ANISOU 911 N LEU A 142 5158 8278 12415 1290 -1470 -2413 N
ATOM 912 CA LEU A 142 -17.426 29.130 92.974 1.00 64.83 C
ANISOU 912 CA LEU A 142 4687 7858 12087 1323 -1343 -2439 C
ATOM 913 C LEU A 142 -15.928 28.855 92.851 1.00 68.37 C
ANISOU 913 C LEU A 142 4819 8239 12919 1364 -1363 -2787 C
ATOM 914 O LEU A 142 -15.514 27.727 92.556 1.00 69.61 O
ANISOU 914 O LEU A 142 4927 8366 13156 1474 -1445 -2862 O
ATOM 915 CB LEU A 142 -17.965 29.750 91.686 1.00 59.17 C
ANISOU 915 CB LEU A 142 4008 7183 11294 1191 -972 -2293 C
ATOM 916 CG LEU A 142 -18.059 28.881 90.443 1.00 59.29 C
ANISOU 916 CG LEU A 142 4042 7198 11286 1213 -793 -2230 C
ATOM 917 CD1 LEU A 142 -19.160 27.844 90.612 1.00 59.86 C
ANISOU 917 CD1 LEU A 142 4387 7317 11039 1316 -960 -1971 C
ATOM 918 CD2 LEU A 142 -18.305 29.747 89.224 1.00 57.75 C
ANISOU 918 CD2 LEU A 142 3820 6981 11140 1063 -416 -2218 C
ATOM 919 N ASP A 143 -15.114 29.898 93.053 1.00 68.33 N
ANISOU 919 N ASP A 143 4592 8209 13160 1275 -1278 -3012 N
ATOM 920 CA ASP A 143 -13.656 29.810 93.019 1.00 68.35 C
ANISOU 920 CA ASP A 143 4264 8154 13553 1296 -1290 -3381 C
ATOM 921 C ASP A 143 -13.123 28.989 94.192 1.00 73.85 C
ANISOU 921 C ASP A 143 4918 8819 14322 1488 -1703 -3526 C
ATOM 922 O ASP A 143 -12.234 28.145 94.017 1.00 81.32 O
ANISOU 922 O ASP A 143 5682 9726 15490 1594 -1795 -3739 O
ATOM 923 CB ASP A 143 -13.089 31.237 93.031 1.00 69.83 C
ANISOU 923 CB ASP A 143 4263 8328 13941 1134 -1089 -3563 C
ATOM 924 CG ASP A 143 -11.588 31.300 93.262 1.00 85.90 C
ANISOU 924 CG ASP A 143 5941 10313 16384 1152 -1139 -3977 C
ATOM 925 OD1 ASP A 143 -11.170 31.627 94.394 1.00 93.90 O
ANISOU 925 OD1 ASP A 143 6873 11322 17483 1213 -1384 -4119 O
ATOM 926 OD2 ASP A 143 -10.825 31.028 92.312 1.00 91.94 O
ANISOU 926 OD2 ASP A 143 6503 11042 17389 1104 -929 -4172 O
ATOM 927 N ARG A 144 -13.670 29.231 95.391 1.00 73.17 N
ANISOU 927 N ARG A 144 5013 8744 14046 1538 -1950 -3413 N
ATOM 928 CA ARG A 144 -13.292 28.489 96.594 1.00 75.76 C
ANISOU 928 CA ARG A 144 5365 9027 14392 1722 -2351 -3521 C
ATOM 929 C ARG A 144 -13.778 27.044 96.526 1.00 77.06 C
ANISOU 929 C ARG A 144 5738 9172 14369 1863 -2519 -3370 C
ATOM 930 O ARG A 144 -13.084 26.125 96.978 1.00 76.37 O
ANISOU 930 O ARG A 144 5582 9029 14408 2031 -2783 -3539 O
ATOM 931 CB ARG A 144 -13.869 29.178 97.840 1.00 72.41 C
ANISOU 931 CB ARG A 144 5119 8613 13782 1715 -2525 -3414 C
ATOM 932 CG ARG A 144 -13.354 30.595 98.152 1.00 75.15 C
ANISOU 932 CG ARG A 144 5271 8973 14311 1599 -2416 -3577 C
ATOM 933 CD ARG A 144 -11.855 30.624 98.421 1.00 79.15 C
ANISOU 933 CD ARG A 144 5423 9439 15212 1664 -2527 -3975 C
ATOM 934 NE ARG A 144 -11.094 30.676 97.178 1.00 83.85 N
ANISOU 934 NE ARG A 144 5749 10032 16080 1575 -2238 -4161 N
ATOM 935 CZ ARG A 144 -9.926 30.072 96.987 1.00 89.29 C
ANISOU 935 CZ ARG A 144 6158 10686 17084 1666 -2314 -4468 C
ATOM 936 NH1 ARG A 144 -9.380 29.354 97.958 1.00 89.83 N
ANISOU 936 NH1 ARG A 144 6181 10718 17232 1866 -2695 -4619 N
ATOM 937 NH2 ARG A 144 -9.310 30.175 95.817 1.00 85.28 N
ANISOU 937 NH2 ARG A 144 5420 10171 16810 1559 -2007 -4629 N
ATOM 938 N TRP A 145 -14.978 26.837 95.964 1.00 73.07 N
ANISOU 938 N TRP A 145 5492 8712 13560 1800 -2371 -3058 N
ATOM 939 CA TRP A 145 -15.541 25.498 95.817 1.00 70.33 C
ANISOU 939 CA TRP A 145 5360 8350 13014 1911 -2491 -2900 C
ATOM 940 C TRP A 145 -14.677 24.634 94.894 1.00 76.01 C
ANISOU 940 C TRP A 145 5871 9039 13970 1988 -2426 -3069 C
ATOM 941 O TRP A 145 -14.394 23.474 95.216 1.00 80.79 O
ANISOU 941 O TRP A 145 6522 9590 14586 2153 -2667 -3128 O
ATOM 942 CB TRP A 145 -16.985 25.599 95.303 1.00 63.11 C
ANISOU 942 CB TRP A 145 4726 7504 11750 1809 -2307 -2554 C
ATOM 943 CG TRP A 145 -17.761 24.310 95.391 1.00 62.72 C
ANISOU 943 CG TRP A 145 4951 7440 11442 1905 -2451 -2370 C
ATOM 944 CD1 TRP A 145 -18.277 23.738 96.519 1.00 62.62 C
ANISOU 944 CD1 TRP A 145 5191 7383 11219 1985 -2729 -2290 C
ATOM 945 CD2 TRP A 145 -18.106 23.438 94.305 1.00 65.33 C
ANISOU 945 CD2 TRP A 145 5340 7788 11696 1922 -2308 -2253 C
ATOM 946 NE1 TRP A 145 -18.913 22.560 96.203 1.00 65.69 N
ANISOU 946 NE1 TRP A 145 5791 7759 11409 2044 -2767 -2139 N
ATOM 947 CE2 TRP A 145 -18.823 22.354 94.852 1.00 67.49 C
ANISOU 947 CE2 TRP A 145 5900 8030 11715 2012 -2518 -2110 C
ATOM 948 CE3 TRP A 145 -17.874 23.468 92.926 1.00 65.39 C
ANISOU 948 CE3 TRP A 145 5196 7826 11824 1869 -2010 -2262 C
ATOM 949 CZ2 TRP A 145 -19.313 21.309 94.064 1.00 66.19 C
ANISOU 949 CZ2 TRP A 145 5864 7869 11417 2052 -2450 -1975 C
ATOM 950 CZ3 TRP A 145 -18.359 22.428 92.147 1.00 65.04 C
ANISOU 950 CZ3 TRP A 145 5280 7785 11645 1920 -1943 -2123 C
ATOM 951 CH2 TRP A 145 -19.070 21.364 92.718 1.00 64.64 C
ANISOU 951 CH2 TRP A 145 5505 7710 11345 2012 -2167 -1980 C
ATOM 952 N TYR A 146 -14.221 25.188 93.768 1.00 75.19 N
ANISOU 952 N TYR A 146 5544 8959 14065 1870 -2098 -3163 N
ATOM 953 CA TYR A 146 -13.312 24.435 92.905 1.00 75.77 C
ANISOU 953 CA TYR A 146 5394 8998 14397 1934 -2009 -3358 C
ATOM 954 C TYR A 146 -11.871 24.414 93.436 1.00 82.28 C
ANISOU 954 C TYR A 146 5893 9770 15601 2026 -2187 -3742 C
ATOM 955 O TYR A 146 -11.150 23.448 93.187 1.00 84.45 O
ANISOU 955 O TYR A 146 6029 10004 16056 2161 -2279 -3908 O
ATOM 956 CB TYR A 146 -13.346 24.980 91.470 1.00 70.87 C
ANISOU 956 CB TYR A 146 4673 8405 13847 1766 -1568 -3331 C
ATOM 957 CG TYR A 146 -14.536 24.522 90.632 1.00 66.69 C
ANISOU 957 CG TYR A 146 4417 7919 13006 1738 -1399 -3005 C
ATOM 958 CD1 TYR A 146 -14.603 23.229 90.117 1.00 66.94 C
ANISOU 958 CD1 TYR A 146 4514 7929 12992 1861 -1431 -2954 C
ATOM 959 CD2 TYR A 146 -15.580 25.391 90.341 1.00 64.86 C
ANISOU 959 CD2 TYR A 146 4367 7746 12529 1599 -1205 -2758 C
ATOM 960 CE1 TYR A 146 -15.688 22.815 89.348 1.00 63.28 C
ANISOU 960 CE1 TYR A 146 4296 7505 12244 1840 -1274 -2668 C
ATOM 961 CE2 TYR A 146 -16.665 24.987 89.574 1.00 60.58 C
ANISOU 961 CE2 TYR A 146 4061 7249 11707 1585 -1060 -2476 C
ATOM 962 CZ TYR A 146 -16.715 23.702 89.081 1.00 62.05 C
ANISOU 962 CZ TYR A 146 4306 7410 11861 1702 -1096 -2445 C
ATOM 963 OH TYR A 146 -17.798 23.314 88.321 1.00 61.29 O
ANISOU 963 OH TYR A 146 4430 7344 11512 1690 -962 -2202 O
ATOM 964 N ALA A 147 -11.439 25.451 94.173 1.00 84.46 N
ANISOU 964 N ALA A 147 6039 10047 16004 1967 -2242 -3894 N
ATOM 965 CA ALA A 147 -10.079 25.456 94.721 1.00 89.72 C
ANISOU 965 CA ALA A 147 6385 10671 17032 2062 -2426 -4276 C
ATOM 966 C ALA A 147 -9.882 24.382 95.789 1.00 95.77 C
ANISOU 966 C ALA A 147 7247 11386 17756 2307 -2877 -4325 C
ATOM 967 O ALA A 147 -8.794 23.807 95.897 1.00105.66 O
ANISOU 967 O ALA A 147 8252 12598 19296 2450 -3041 -4616 O
ATOM 968 CB ALA A 147 -9.742 26.833 95.300 1.00 85.02 C
ANISOU 968 CB ALA A 147 5653 10092 16558 1942 -2381 -4413 C
ATOM 969 N ILE A 148 -10.940 24.088 96.559 1.00 93.30 N
ANISOU 969 N ILE A 148 7299 11067 17083 2356 -3073 -4047 N
ATOM 970 CA ILE A 148 -10.885 23.227 97.732 1.00 94.17 C
ANISOU 970 CA ILE A 148 7570 11109 17100 2564 -3499 -4070 C
ATOM 971 C ILE A 148 -11.563 21.870 97.480 1.00 94.78 C
ANISOU 971 C ILE A 148 7924 11153 16935 2675 -3592 -3863 C
ATOM 972 O ILE A 148 -10.968 20.819 97.720 1.00103.23 O
ANISOU 972 O ILE A 148 8962 12156 18106 2872 -3844 -4003 O
ATOM 973 CB ILE A 148 -11.501 23.947 98.961 1.00 83.30 C
ANISOU 973 CB ILE A 148 6411 9730 15511 2531 -3660 -3950 C
ATOM 974 CG1 ILE A 148 -10.677 25.204 99.290 1.00 85.68 C
ANISOU 974 CG1 ILE A 148 6416 10055 16084 2452 -3608 -4195 C
ATOM 975 CG2 ILE A 148 -11.631 23.020 100.177 1.00 87.54 C
ANISOU 975 CG2 ILE A 148 7196 10177 15888 2732 -4081 -3929 C
ATOM 976 CD1 ILE A 148 -11.388 26.235 100.144 1.00 83.10 C
ANISOU 976 CD1 ILE A 148 6267 9751 15555 2352 -3617 -4044 C
ATOM 977 N CYS A 149 -12.806 21.871 96.965 1.00 90.40 N
ANISOU 977 N CYS A 149 8625 9263 16460 2702 -4092 -2492 N
ATOM 978 CA CYS A 149 -13.559 20.620 96.830 1.00 91.77 C
ANISOU 978 CA CYS A 149 9141 9328 16400 2775 -4239 -2378 C
ATOM 979 C CYS A 149 -13.250 19.840 95.543 1.00 95.04 C
ANISOU 979 C CYS A 149 9448 9709 16954 2934 -4091 -2551 C
ATOM 980 O CYS A 149 -13.272 18.607 95.563 1.00 98.75 O
ANISOU 980 O CYS A 149 10103 10066 17349 3051 -4271 -2574 O
ATOM 981 CB CYS A 149 -15.065 20.889 96.924 1.00 86.52 C
ANISOU 981 CB CYS A 149 8821 8669 15384 2621 -4219 -2047 C
ATOM 982 SG CYS A 149 -15.596 21.499 98.548 1.00 83.02 S
ANISOU 982 SG CYS A 149 8627 8216 14700 2467 -4388 -1808 S
ATOM 983 N HIS A 150 -12.969 20.525 94.424 1.00 93.30 N
ANISOU 983 N HIS A 150 8956 9570 16922 2945 -3743 -2678 N
ATOM 984 CA HIS A 150 -12.653 19.868 93.147 1.00 89.53 C
ANISOU 984 CA HIS A 150 8411 9035 16569 3113 -3530 -2858 C
ATOM 985 C HIS A 150 -11.404 20.540 92.579 1.00 91.13 C
ANISOU 985 C HIS A 150 8152 9322 17150 3151 -3185 -3128 C
ATOM 986 O HIS A 150 -11.476 21.380 91.671 1.00 88.47 O
ANISOU 986 O HIS A 150 7677 9055 16884 3097 -2794 -3179 O
ATOM 987 CB HIS A 150 -13.872 19.901 92.220 1.00 82.65 C
ANISOU 987 CB HIS A 150 7823 8117 15463 3082 -3396 -2700 C
ATOM 988 CG HIS A 150 -15.109 19.382 92.891 1.00 77.94 C
ANISOU 988 CG HIS A 150 7652 7448 14515 2984 -3714 -2392 C
ATOM 989 ND1 HIS A 150 -15.397 18.039 92.985 1.00 77.37 N
ANISOU 989 ND1 HIS A 150 7869 7241 14289 3072 -3955 -2348 N
ATOM 990 CD2 HIS A 150 -16.075 20.024 93.586 1.00 75.39 C
ANISOU 990 CD2 HIS A 150 7503 7171 13969 2787 -3802 -2111 C
ATOM 991 CE1 HIS A 150 -16.509 17.875 93.671 1.00 74.80 C
ANISOU 991 CE1 HIS A 150 7869 6882 13669 2919 -4147 -2055 C
ATOM 992 NE2 HIS A 150 -16.947 19.066 94.052 1.00 73.70 N
ANISOU 992 NE2 HIS A 150 7673 6848 13480 2748 -4050 -1901 N
ATOM 993 N PRO A 151 -10.219 20.145 93.083 1.00 91.86 N
ANISOU 993 N PRO A 151 8010 9394 17499 3239 -3305 -3308 N
ATOM 994 CA PRO A 151 -8.996 20.949 92.904 1.00 91.34 C
ANISOU 994 CA PRO A 151 7485 9407 17812 3210 -3038 -3515 C
ATOM 995 C PRO A 151 -8.405 21.086 91.498 1.00 95.39 C
ANISOU 995 C PRO A 151 7763 9937 18545 3288 -2519 -3709 C
ATOM 996 O PRO A 151 -7.719 22.082 91.275 1.00102.09 O
ANISOU 996 O PRO A 151 8279 10875 19635 3183 -2213 -3807 O
ATOM 997 CB PRO A 151 -7.993 20.234 93.818 1.00 94.70 C
ANISOU 997 CB PRO A 151 7795 9751 18435 3310 -3372 -3638 C
ATOM 998 CG PRO A 151 -8.814 19.749 94.916 1.00 92.34 C
ANISOU 998 CG PRO A 151 7882 9388 17814 3276 -3808 -3439 C
ATOM 999 CD PRO A 151 -10.066 19.228 94.230 1.00 92.55 C
ANISOU 999 CD PRO A 151 8267 9387 17510 3296 -3755 -3272 C
ATOM 1000 N LEU A 152 -8.526 20.131 90.571 1.00 94.77 N
ANISOU 1000 N LEU A 152 7851 9758 18400 3467 -2385 -3779 N
ATOM 1001 CA LEU A 152 -7.780 20.336 89.325 1.00 97.71 C
ANISOU 1001 CA LEU A 152 8009 10129 18988 3538 -1836 -3977 C
ATOM 1002 C LEU A 152 -8.671 20.340 88.079 1.00 97.21 C
ANISOU 1002 C LEU A 152 8266 10005 18665 3569 -1493 -3949 C
ATOM 1003 O LEU A 152 -8.209 20.039 86.974 1.00103.69 O
ANISOU 1003 O LEU A 152 9100 10751 19548 3693 -1082 -4104 O
ATOM 1004 CB LEU A 152 -6.640 19.322 89.199 1.00106.68 C
ANISOU 1004 CB LEU A 152 8977 11172 20385 3745 -1846 -4165 C
ATOM 1005 CG LEU A 152 -5.617 19.401 90.348 1.00107.86 C
ANISOU 1005 CG LEU A 152 8792 11347 20844 3714 -2152 -4232 C
ATOM 1006 CD1 LEU A 152 -4.892 18.073 90.538 1.00108.42 C
ANISOU 1006 CD1 LEU A 152 8844 11295 21057 3937 -2380 -4352 C
ATOM 1007 CD2 LEU A 152 -4.616 20.558 90.184 1.00107.24 C
ANISOU 1007 CD2 LEU A 152 8262 11357 21127 3583 -1801 -4346 C
ATOM 1008 N LEU A 153 -9.923 20.774 88.243 1.00 92.92 N
ANISOU 1008 N LEU A 153 7994 9479 17830 3445 -1631 -3751 N
ATOM 1009 CA LEU A 153 -10.870 20.920 87.138 1.00 92.01 C
ANISOU 1009 CA LEU A 153 8224 9278 17458 3443 -1352 -3717 C
ATOM 1010 C LEU A 153 -10.692 22.257 86.403 1.00 90.97 C
ANISOU 1010 C LEU A 153 7953 9280 17331 3235 -785 -3748 C
ATOM 1011 O LEU A 153 -10.422 22.276 85.198 1.00 91.64 O
ANISOU 1011 O LEU A 153 8151 9307 17361 3269 -299 -3870 O
ATOM 1012 CB LEU A 153 -12.303 20.784 87.666 1.00 93.06 C
ANISOU 1012 CB LEU A 153 8789 9408 17162 3285 -1750 -3388 C
ATOM 1013 CG LEU A 153 -12.886 19.396 87.976 1.00 96.07 C
ANISOU 1013 CG LEU A 153 9518 9613 17372 3443 -2215 -3295 C
ATOM 1014 CD1 LEU A 153 -12.002 18.521 88.884 1.00100.46 C
ANISOU 1014 CD1 LEU A 153 9869 10154 18150 3598 -2545 -3393 C
ATOM 1015 CD2 LEU A 153 -14.299 19.544 88.547 1.00 91.55 C
ANISOU 1015 CD2 LEU A 153 9299 9058 16428 3229 -2527 -2941 C
ATOM 1016 N PHE A 154 -10.850 23.376 87.116 1.00 87.47 N
ANISOU 1016 N PHE A 154 7306 9002 16927 3020 -833 -3631 N
ATOM 1017 CA PHE A 154 -10.748 24.713 86.531 1.00 89.02 C
ANISOU 1017 CA PHE A 154 7384 9334 17105 2795 -329 -3632 C
ATOM 1018 C PHE A 154 -9.637 25.528 87.194 1.00 91.91 C
ANISOU 1018 C PHE A 154 7182 9816 17924 2748 -266 -3765 C
ATOM 1019 O PHE A 154 -9.480 25.508 88.424 1.00 91.52 O
ANISOU 1019 O PHE A 154 7000 9816 17959 2713 -722 -3683 O
ATOM 1020 CB PHE A 154 -12.106 25.451 86.613 1.00 86.50 C
ANISOU 1020 CB PHE A 154 7445 9114 16309 2504 -394 -3311 C
ATOM 1021 CG PHE A 154 -13.202 24.772 85.825 1.00 84.82 C
ANISOU 1021 CG PHE A 154 7816 8785 15627 2485 -425 -3151 C
ATOM 1022 CD1 PHE A 154 -13.308 24.956 84.454 1.00 86.05 C
ANISOU 1022 CD1 PHE A 154 8243 8887 15565 2442 48 -3204 C
ATOM 1023 CD2 PHE A 154 -14.090 23.908 86.446 1.00 84.38 C
ANISOU 1023 CD2 PHE A 154 8051 8646 15365 2523 -936 -2956 C
ATOM 1024 CE1 PHE A 154 -14.295 24.308 83.722 1.00 86.55 C
ANISOU 1024 CE1 PHE A 154 8861 8813 15211 2432 -32 -3067 C
ATOM 1025 CE2 PHE A 154 -15.078 23.258 85.720 1.00 85.84 C
ANISOU 1025 CE2 PHE A 154 8750 8701 15165 2501 -998 -2813 C
ATOM 1026 CZ PHE A 154 -15.179 23.458 84.357 1.00 86.63 C
ANISOU 1026 CZ PHE A 154 9119 8746 15053 2456 -567 -2872 C
ATOM 1027 N LYS A 155 -8.867 26.240 86.364 1.00 96.29 N
ANISOU 1027 N LYS A 155 7539 10422 18624 2662 296 -3893 N
ATOM 1028 CA LYS A 155 -7.743 27.082 86.780 1.00102.55 C
ANISOU 1028 CA LYS A 155 7905 11324 19736 2518 417 -3954 C
ATOM 1029 C LYS A 155 -8.221 28.492 87.135 1.00106.21 C
ANISOU 1029 C LYS A 155 8315 11938 20103 2244 492 -3817 C
ATOM 1030 O LYS A 155 -9.013 29.081 86.394 1.00107.00 O
ANISOU 1030 O LYS A 155 8630 12073 19950 2137 827 -3751 O
ATOM 1031 CB LYS A 155 -6.707 27.151 85.653 1.00106.84 C
ANISOU 1031 CB LYS A 155 8307 11825 20462 2552 1003 -4123 C
ATOM 1032 CG LYS A 155 -5.271 27.384 86.099 1.00116.08 C
ANISOU 1032 CG LYS A 155 9023 13010 22072 2525 1005 -4234 C
ATOM 1033 CD LYS A 155 -4.322 27.400 84.907 1.00125.35 C
ANISOU 1033 CD LYS A 155 10094 14122 23411 2572 1612 -4370 C
ATOM 1034 CE LYS A 155 -2.980 28.013 85.269 1.00131.73 C
ANISOU 1034 CE LYS A 155 10435 14945 24670 2474 1689 -4454 C
ATOM 1035 NZ LYS A 155 -2.007 27.879 84.151 1.00138.20 N
ANISOU 1035 NZ LYS A 155 11149 15679 25680 2553 2253 -4574 N
ATOM 1036 N SER A 156 -7.736 29.042 88.260 1.00110.49 N
ANISOU 1036 N SER A 156 8606 12550 20826 2131 183 -3779 N
ATOM 1037 CA SER A 156 -8.147 30.369 88.728 1.00108.74 C
ANISOU 1037 CA SER A 156 8352 12459 20503 1879 203 -3641 C
ATOM 1038 C SER A 156 -6.952 31.302 88.943 1.00110.80 C
ANISOU 1038 C SER A 156 8268 12757 21072 1731 368 -3729 C
ATOM 1039 O SER A 156 -6.092 31.031 89.789 1.00113.57 O
ANISOU 1039 O SER A 156 8405 13047 21698 1793 35 -3806 O
ATOM 1040 CB SER A 156 -8.972 30.270 90.018 1.00110.19 C
ANISOU 1040 CB SER A 156 8694 12661 20512 1869 -385 -3455 C
ATOM 1041 OG SER A 156 -8.163 30.108 91.173 1.00114.59 O
ANISOU 1041 OG SER A 156 9086 13171 21282 1903 -801 -3496 O
ATOM 1042 N THR A 157 -6.904 32.402 88.187 1.00109.00 N
ANISOU 1042 N THR A 157 8015 12608 20791 1535 867 -3715 N
ATOM 1043 CA THR A 157 -5.873 33.432 88.319 1.00110.12 C
ANISOU 1043 CA THR A 157 7872 12771 21198 1372 1046 -3773 C
ATOM 1044 C THR A 157 -6.463 34.833 88.383 1.00108.65 C
ANISOU 1044 C THR A 157 7790 12710 20784 1109 1207 -3623 C
ATOM 1045 O THR A 157 -7.663 35.052 88.164 1.00107.05 O
ANISOU 1045 O THR A 157 7870 12587 20220 1039 1265 -3476 O
ATOM 1046 CB THR A 157 -4.831 33.390 87.194 1.00114.48 C
ANISOU 1046 CB THR A 157 8258 13255 21985 1401 1572 -3930 C
ATOM 1047 OG1 THR A 157 -5.487 33.275 85.925 1.00113.38 O
ANISOU 1047 OG1 THR A 157 8416 13123 21541 1409 2040 -3904 O
ATOM 1048 CG2 THR A 157 -3.784 32.305 87.422 1.00118.40 C
ANISOU 1048 CG2 THR A 157 8505 13625 22857 1621 1376 -4096 C
ATOM 1049 N ALA A 158 -5.591 35.778 88.754 1.00109.85 N
ANISOU 1049 N ALA A 158 7706 12864 21168 972 1246 -3659 N
ATOM 1050 CA ALA A 158 -5.944 37.193 88.847 1.00106.47 C
ANISOU 1050 CA ALA A 158 7357 12539 20558 724 1401 -3530 C
ATOM 1051 C ALA A 158 -6.352 37.771 87.492 1.00114.17 C
ANISOU 1051 C ALA A 158 8540 13568 21270 593 2007 -3483 C
ATOM 1052 O ALA A 158 -7.239 38.634 87.416 1.00119.03 O
ANISOU 1052 O ALA A 158 9389 14288 21549 419 2113 -3323 O
ATOM 1053 CB ALA A 158 -4.756 37.970 89.417 1.00104.16 C
ANISOU 1053 CB ALA A 158 6756 12194 20626 642 1331 -3614 C
ATOM 1054 N ARG A 159 -5.701 37.307 86.421 1.00119.30 N
ANISOU 1054 N ARG A 159 9141 14135 22054 678 2406 -3614 N
ATOM 1055 CA ARG A 159 -6.006 37.714 85.049 1.00122.37 C
ANISOU 1055 CA ARG A 159 9792 14531 22172 588 2988 -3581 C
ATOM 1056 C ARG A 159 -7.407 37.278 84.624 1.00118.76 C
ANISOU 1056 C ARG A 159 9728 14118 21279 620 3012 -3473 C
ATOM 1057 O ARG A 159 -8.138 38.046 83.984 1.00114.80 O
ANISOU 1057 O ARG A 159 9525 13672 20421 457 3309 -3353 O
ATOM 1058 CB ARG A 159 -4.930 37.123 84.130 1.00131.94 C
ANISOU 1058 CB ARG A 159 10869 15614 23649 721 3349 -3748 C
ATOM 1059 CG ARG A 159 -4.878 37.638 82.710 1.00137.62 C
ANISOU 1059 CG ARG A 159 11839 16296 24156 632 3976 -3732 C
ATOM 1060 CD ARG A 159 -4.187 36.605 81.825 1.00147.38 C
ANISOU 1060 CD ARG A 159 13055 17394 25548 845 4263 -3875 C
ATOM 1061 NE ARG A 159 -4.358 36.877 80.404 1.00153.84 N
ANISOU 1061 NE ARG A 159 14241 18154 26058 804 4834 -3844 N
ATOM 1062 CZ ARG A 159 -5.322 36.334 79.666 1.00154.28 C
ANISOU 1062 CZ ARG A 159 14743 18181 25695 887 4965 -3801 C
ATOM 1063 NH1 ARG A 159 -6.150 35.444 80.203 1.00149.25 N
ANISOU 1063 NH1 ARG A 159 14197 17565 24946 1024 4583 -3796 N
ATOM 1064 NH2 ARG A 159 -5.429 36.635 78.381 1.00158.23 N
ANISOU 1064 NH2 ARG A 159 15620 18605 25896 847 5461 -3769 N
ATOM 1065 N ARG A 160 -7.779 36.039 84.962 1.00122.19 N
ANISOU 1065 N ARG A 160 10179 14505 21742 837 2689 -3515 N
ATOM 1066 CA ARG A 160 -9.109 35.506 84.680 1.00118.15 C
ANISOU 1066 CA ARG A 160 10012 13999 20879 901 2637 -3427 C
ATOM 1067 C ARG A 160 -10.157 36.119 85.603 1.00109.43 C
ANISOU 1067 C ARG A 160 8983 13018 19578 758 2306 -3232 C
ATOM 1068 O ARG A 160 -11.340 36.194 85.246 1.00106.27 O
ANISOU 1068 O ARG A 160 8881 12646 18851 708 2388 -3113 O
ATOM 1069 CB ARG A 160 -9.073 33.981 84.819 1.00124.04 C
ANISOU 1069 CB ARG A 160 10746 14627 21754 1198 2346 -3537 C
ATOM 1070 CG ARG A 160 -8.121 33.281 83.827 1.00133.21 C
ANISOU 1070 CG ARG A 160 11886 15658 23069 1361 2701 -3715 C
ATOM 1071 CD ARG A 160 -8.580 33.367 82.371 1.00136.14 C
ANISOU 1071 CD ARG A 160 12674 15962 23093 1344 3252 -3715 C
ATOM 1072 NE ARG A 160 -7.624 32.751 81.444 1.00141.44 N
ANISOU 1072 NE ARG A 160 13347 16501 23892 1501 3605 -3864 N
ATOM 1073 CZ ARG A 160 -7.565 31.452 81.138 1.00142.28 C
ANISOU 1073 CZ ARG A 160 13578 16469 24015 1770 3526 -3970 C
ATOM 1074 NH1 ARG A 160 -6.645 31.026 80.282 1.00143.71 N
ANISOU 1074 NH1 ARG A 160 13758 16539 24306 1896 3893 -4087 N
ATOM 1075 NH2 ARG A 160 -8.398 30.577 81.688 1.00140.60 N
ANISOU 1075 NH2 ARG A 160 13500 16210 23710 1920 3074 -3954 N
ATOM 1076 N ALA A 161 -9.725 36.567 86.792 1.00105.93 N
ANISOU 1076 N ALA A 161 8294 12627 19327 694 1936 -3194 N
ATOM 1077 CA ALA A 161 -10.600 37.251 87.743 1.00 97.45 C
ANISOU 1077 CA ALA A 161 7304 11660 18062 551 1629 -2991 C
ATOM 1078 C ALA A 161 -11.049 38.611 87.211 1.00 94.77 C
ANISOU 1078 C ALA A 161 7149 11425 17436 283 2017 -2860 C
ATOM 1079 O ALA A 161 -12.214 38.992 87.387 1.00 97.46 O
ANISOU 1079 O ALA A 161 7709 11847 17475 169 1957 -2667 O
ATOM 1080 CB ALA A 161 -9.883 37.408 89.087 1.00 96.69 C
ANISOU 1080 CB ALA A 161 6965 11552 18221 570 1169 -3005 C
ATOM 1081 N LEU A 162 -10.141 39.354 86.563 1.00 91.36 N
ANISOU 1081 N LEU A 162 6644 10978 17090 181 2401 -2944 N
ATOM 1082 CA LEU A 162 -10.493 40.636 85.949 1.00 89.88 C
ANISOU 1082 CA LEU A 162 6686 10863 16601 -54 2766 -2821 C
ATOM 1083 C LEU A 162 -11.491 40.454 84.809 1.00 87.34 C
ANISOU 1083 C LEU A 162 6750 10535 15899 -82 3102 -2750 C
ATOM 1084 O LEU A 162 -12.348 41.322 84.591 1.00 87.15 O
ANISOU 1084 O LEU A 162 7007 10587 15517 -265 3223 -2573 O
ATOM 1085 CB LEU A 162 -9.231 41.345 85.438 1.00 94.35 C
ANISOU 1085 CB LEU A 162 7095 11377 17378 -122 3086 -2936 C
ATOM 1086 CG LEU A 162 -9.390 42.714 84.755 1.00 97.11 C
ANISOU 1086 CG LEU A 162 7683 11771 17442 -341 3447 -2824 C
ATOM 1087 CD1 LEU A 162 -9.499 43.848 85.771 1.00 98.63 C
ANISOU 1087 CD1 LEU A 162 7826 12059 17589 -491 3198 -2698 C
ATOM 1088 CD2 LEU A 162 -8.265 42.988 83.758 1.00100.06 C
ANISOU 1088 CD2 LEU A 162 7979 12042 17999 -347 3878 -2957 C
ATOM 1089 N GLY A 163 -11.388 39.345 84.074 1.00 84.40 N
ANISOU 1089 N GLY A 163 6430 10056 15584 107 3244 -2886 N
ATOM 1090 CA GLY A 163 -12.344 39.062 83.015 1.00 83.64 C
ANISOU 1090 CA GLY A 163 6748 9911 15119 113 3533 -2841 C
ATOM 1091 C GLY A 163 -13.702 38.663 83.551 1.00 83.10 C
ANISOU 1091 C GLY A 163 6938 9877 14761 106 3137 -2636 C
ATOM 1092 O GLY A 163 -14.730 38.979 82.940 1.00 85.00 O
ANISOU 1092 O GLY A 163 7639 10115 14543 -20 3230 -2451 O
ATOM 1093 N SER A 164 -13.720 37.967 84.693 1.00 80.39 N
ANISOU 1093 N SER A 164 6422 9539 14583 223 2591 -2596 N
ATOM 1094 CA SER A 164 -14.961 37.660 85.400 1.00 76.41 C
ANISOU 1094 CA SER A 164 6233 9054 13747 186 2101 -2311 C
ATOM 1095 C SER A 164 -15.619 38.940 85.903 1.00 75.23 C
ANISOU 1095 C SER A 164 6143 9042 13399 -62 2099 -2095 C
ATOM 1096 O SER A 164 -16.817 39.162 85.690 1.00 70.17 O
ANISOU 1096 O SER A 164 5903 8413 12347 -182 2045 -1846 O
ATOM 1097 CB SER A 164 -14.669 36.713 86.571 1.00 78.35 C
ANISOU 1097 CB SER A 164 6257 9260 14253 374 1562 -2339 C
ATOM 1098 OG SER A 164 -14.086 35.490 86.145 1.00 86.35 O
ANISOU 1098 OG SER A 164 7221 10141 15446 615 1539 -2533 O
ATOM 1099 N ILE A 165 -14.820 39.801 86.547 1.00 80.11 N
ANISOU 1099 N ILE A 165 6359 9750 14328 -137 2158 -2192 N
ATOM 1100 CA ILE A 165 -15.277 41.072 87.108 1.00 75.26 C
ANISOU 1100 CA ILE A 165 5764 9261 13573 -361 2161 -2016 C
ATOM 1101 C ILE A 165 -15.930 41.952 86.038 1.00 76.04 C
ANISOU 1101 C ILE A 165 6188 9399 13303 -557 2606 -1908 C
ATOM 1102 O ILE A 165 -16.992 42.543 86.273 1.00 75.90 O
ANISOU 1102 O ILE A 165 6452 9442 12945 -706 2509 -1648 O
ATOM 1103 CB ILE A 165 -14.091 41.773 87.818 1.00 71.46 C
ANISOU 1103 CB ILE A 165 4916 8812 13422 -383 2110 -2146 C
ATOM 1104 CG1 ILE A 165 -13.874 41.169 89.217 1.00 69.52 C
ANISOU 1104 CG1 ILE A 165 4439 8540 13433 -243 1553 -2154 C
ATOM 1105 CG2 ILE A 165 -14.279 43.290 87.910 1.00 68.62 C
ANISOU 1105 CG2 ILE A 165 4731 8545 12796 -608 2248 -1984 C
ATOM 1106 CD1 ILE A 165 -12.496 41.406 89.822 1.00 69.81 C
ANISOU 1106 CD1 ILE A 165 4187 8532 13806 -186 1414 -2319 C
ATOM 1107 N LEU A 166 -15.322 42.045 84.845 1.00 77.01 N
ANISOU 1107 N LEU A 166 6347 9466 13448 -547 3069 -2083 N
ATOM 1108 CA LEU A 166 -15.907 42.831 83.755 1.00 74.49 C
ANISOU 1108 CA LEU A 166 6451 9144 12708 -703 3425 -1968 C
ATOM 1109 C LEU A 166 -17.206 42.209 83.254 1.00 72.55 C
ANISOU 1109 C LEU A 166 6636 8837 12091 -697 3344 -1803 C
ATOM 1110 O LEU A 166 -18.143 42.923 82.874 1.00 67.81 O
ANISOU 1110 O LEU A 166 6375 8267 11125 -863 3438 -1607 O
ATOM 1111 CB LEU A 166 -14.911 42.962 82.600 1.00 77.31 C
ANISOU 1111 CB LEU A 166 6866 9401 13106 -659 3823 -2147 C
ATOM 1112 CG LEU A 166 -13.860 44.059 82.770 1.00 81.28 C
ANISOU 1112 CG LEU A 166 7198 9935 13751 -743 3887 -2181 C
ATOM 1113 CD1 LEU A 166 -12.654 43.795 81.895 1.00 85.55 C
ANISOU 1113 CD1 LEU A 166 7632 10354 14520 -651 4214 -2389 C
ATOM 1114 CD2 LEU A 166 -14.451 45.421 82.450 1.00 78.78 C
ANISOU 1114 CD2 LEU A 166 7209 9676 13047 -931 3974 -1986 C
ATOM 1115 N GLY A 167 -17.259 40.875 83.235 1.00 73.97 N
ANISOU 1115 N GLY A 167 6891 8905 12308 -494 3070 -1844 N
ATOM 1116 CA GLY A 167 -18.473 40.179 82.847 1.00 69.48 C
ANISOU 1116 CA GLY A 167 6799 8240 11362 -470 2823 -1643 C
ATOM 1117 C GLY A 167 -19.603 40.351 83.841 1.00 65.91 C
ANISOU 1117 C GLY A 167 6449 7853 10739 -567 2389 -1333 C
ATOM 1118 O GLY A 167 -20.772 40.387 83.447 1.00 65.62 O
ANISOU 1118 O GLY A 167 6803 7771 10359 -652 2299 -1110 O
ATOM 1119 N ILE A 168 -19.269 40.451 85.139 1.00 65.98 N
ANISOU 1119 N ILE A 168 6122 7949 10998 -547 2113 -1312 N
ATOM 1120 CA ILE A 168 -20.258 40.718 86.186 1.00 66.00 C
ANISOU 1120 CA ILE A 168 6215 8007 10856 -632 1754 -1016 C
ATOM 1121 C ILE A 168 -20.921 42.075 85.949 1.00 62.50 C
ANISOU 1121 C ILE A 168 5936 7659 10153 -867 1998 -841 C
ATOM 1122 O ILE A 168 -22.151 42.206 86.043 1.00 60.02 O
ANISOU 1122 O ILE A 168 5913 7330 9560 -955 1840 -559 O
ATOM 1123 CB ILE A 168 -19.591 40.626 87.585 1.00 66.12 C
ANISOU 1123 CB ILE A 168 5864 8069 11187 -547 1449 -1069 C
ATOM 1124 CG1 ILE A 168 -19.255 39.163 87.945 1.00 64.29 C
ANISOU 1124 CG1 ILE A 168 5557 7722 11147 -306 1101 -1170 C
ATOM 1125 CG2 ILE A 168 -20.458 41.279 88.687 1.00 63.39 C
ANISOU 1125 CG2 ILE A 168 5609 7789 10688 -662 1204 -778 C
ATOM 1126 CD1 ILE A 168 -18.319 38.961 89.156 1.00 66.11 C
ANISOU 1126 CD1 ILE A 168 5409 7965 11744 -181 817 -1304 C
ATOM 1127 N TRP A 169 -20.121 43.088 85.587 1.00 60.02 N
ANISOU 1127 N TRP A 169 5437 7428 9939 -972 2401 -1004 N
ATOM 1128 CA TRP A 169 -20.624 44.438 85.327 1.00 57.61 C
ANISOU 1128 CA TRP A 169 5277 7212 9399 -1194 2668 -866 C
ATOM 1129 C TRP A 169 -21.467 44.499 84.058 1.00 62.84 C
ANISOU 1129 C TRP A 169 6382 7797 9696 -1263 2874 -771 C
ATOM 1130 O TRP A 169 -22.508 45.166 84.030 1.00 67.40 O
ANISOU 1130 O TRP A 169 7213 8403 9991 -1407 2850 -526 O
ATOM 1131 CB TRP A 169 -19.454 45.425 85.240 1.00 56.06 C
ANISOU 1131 CB TRP A 169 4895 7084 9322 -1210 2884 -1040 C
ATOM 1132 CG TRP A 169 -19.027 45.852 86.592 1.00 54.63 C
ANISOU 1132 CG TRP A 169 4453 6983 9320 -1200 2598 -1006 C
ATOM 1133 CD1 TRP A 169 -18.009 45.332 87.333 1.00 58.09 C
ANISOU 1133 CD1 TRP A 169 4494 7406 10172 -1087 2445 -1200 C
ATOM 1134 CD2 TRP A 169 -19.656 46.846 87.412 1.00 55.15 C
ANISOU 1134 CD2 TRP A 169 4665 7140 9151 -1288 2398 -760 C
ATOM 1135 NE1 TRP A 169 -17.949 45.955 88.556 1.00 62.52 N
ANISOU 1135 NE1 TRP A 169 4961 8030 10763 -1119 2171 -1096 N
ATOM 1136 CE2 TRP A 169 -18.949 46.889 88.629 1.00 61.02 C
ANISOU 1136 CE2 TRP A 169 5100 7908 10175 -1244 2166 -827 C
ATOM 1137 CE3 TRP A 169 -20.739 47.713 87.229 1.00 53.61 C
ANISOU 1137 CE3 TRP A 169 4832 6996 8540 -1375 2369 -494 C
ATOM 1138 CZ2 TRP A 169 -19.290 47.766 89.660 1.00 59.27 C
ANISOU 1138 CZ2 TRP A 169 4945 7758 9818 -1307 1967 -642 C
ATOM 1139 CZ3 TRP A 169 -21.077 48.583 88.255 1.00 51.99 C
ANISOU 1139 CZ3 TRP A 169 4668 6877 8209 -1411 2156 -305 C
ATOM 1140 CH2 TRP A 169 -20.354 48.602 89.454 1.00 55.76 C
ANISOU 1140 CH2 TRP A 169 4859 7372 8955 -1391 1988 -381 C
ATOM 1141 N ALA A 170 -21.017 43.818 82.998 1.00 61.55 N
ANISOU 1141 N ALA A 170 6330 7519 9536 -1154 3075 -967 N
ATOM 1142 CA ALA A 170 -21.754 43.765 81.738 1.00 58.10 C
ANISOU 1142 CA ALA A 170 6368 6965 8743 -1192 3236 -903 C
ATOM 1143 C ALA A 170 -23.140 43.152 81.928 1.00 60.82 C
ANISOU 1143 C ALA A 170 7021 7231 8858 -1186 2793 -618 C
ATOM 1144 O ALA A 170 -24.140 43.681 81.427 1.00 59.50 O
ANISOU 1144 O ALA A 170 7188 7032 8387 -1314 2812 -424 O
ATOM 1145 CB ALA A 170 -20.948 42.967 80.710 1.00 57.24 C
ANISOU 1145 CB ALA A 170 6332 6717 8702 -1031 3486 -1173 C
ATOM 1146 N VAL A 171 -23.208 42.026 82.648 1.00 65.82 N
ANISOU 1146 N VAL A 171 7538 7817 9654 -1037 2389 -588 N
ATOM 1147 CA VAL A 171 -24.474 41.344 82.913 1.00 65.43 C
ANISOU 1147 CA VAL A 171 7733 7675 9454 -1025 1962 -317 C
ATOM 1148 C VAL A 171 -25.384 42.219 83.781 1.00 64.62 C
ANISOU 1148 C VAL A 171 7613 7675 9264 -1183 1827 -17 C
ATOM 1149 O VAL A 171 -26.556 42.438 83.453 1.00 66.89 O
ANISOU 1149 O VAL A 171 8191 7903 9321 -1283 1731 224 O
ATOM 1150 CB VAL A 171 -24.209 39.965 83.555 1.00 60.19 C
ANISOU 1150 CB VAL A 171 6923 6935 9010 -825 1594 -372 C
ATOM 1151 CG1 VAL A 171 -25.486 39.334 84.107 1.00 57.51 C
ANISOU 1151 CG1 VAL A 171 6760 6510 8582 -827 1147 -64 C
ATOM 1152 CG2 VAL A 171 -23.551 39.014 82.551 1.00 63.36 C
ANISOU 1152 CG2 VAL A 171 7439 7196 9439 -662 1709 -627 C
ATOM 1153 N SER A 172 -24.841 42.759 84.880 1.00 59.50 N
ANISOU 1153 N SER A 172 6634 7167 8808 -1202 1821 -32 N
ATOM 1154 CA SER A 172 -25.612 43.584 85.808 1.00 54.14 C
ANISOU 1154 CA SER A 172 5944 6575 8052 -1328 1710 243 C
ATOM 1155 C SER A 172 -26.188 44.833 85.131 1.00 52.12 C
ANISOU 1155 C SER A 172 5896 6371 7538 -1524 2004 359 C
ATOM 1156 O SER A 172 -27.353 45.184 85.348 1.00 49.24 O
ANISOU 1156 O SER A 172 5719 6006 6986 -1583 1825 647 O
ATOM 1157 CB SER A 172 -24.730 43.980 86.993 1.00 52.98 C
ANISOU 1157 CB SER A 172 5439 6545 8147 -1301 1678 151 C
ATOM 1158 OG SER A 172 -24.331 42.829 87.716 1.00 56.48 O
ANISOU 1158 OG SER A 172 5726 6924 8809 -1115 1351 79 O
ATOM 1159 N LEU A 173 -25.371 45.524 84.324 1.00 48.25 N
ANISOU 1159 N LEU A 173 5388 5937 7009 -1556 2365 134 N
ATOM 1160 CA LEU A 173 -25.825 46.727 83.625 1.00 50.79 C
ANISOU 1160 CA LEU A 173 5966 6330 7004 -1545 2363 214 C
ATOM 1161 C LEU A 173 -26.965 46.422 82.651 1.00 56.75 C
ANISOU 1161 C LEU A 173 7094 6949 7519 -1587 2314 356 C
ATOM 1162 O LEU A 173 -27.872 47.241 82.477 1.00 63.65 O
ANISOU 1162 O LEU A 173 8111 7881 8192 -1555 2116 533 O
ATOM 1163 CB LEU A 173 -24.644 47.391 82.899 1.00 51.48 C
ANISOU 1163 CB LEU A 173 5998 6446 7118 -1513 2670 -58 C
ATOM 1164 CG LEU A 173 -23.573 48.126 83.730 1.00 55.20 C
ANISOU 1164 CG LEU A 173 6159 7043 7770 -1475 2662 -162 C
ATOM 1165 CD1 LEU A 173 -22.370 48.519 82.877 1.00 51.06 C
ANISOU 1165 CD1 LEU A 173 5583 6483 7333 -1453 2977 -426 C
ATOM 1166 CD2 LEU A 173 -24.138 49.361 84.440 1.00 53.21 C
ANISOU 1166 CD2 LEU A 173 5951 6921 7346 -1461 2401 63 C
ATOM 1167 N ALA A 174 -26.939 45.230 82.031 1.00 54.59 N
ANISOU 1167 N ALA A 174 6969 6476 7298 -1648 2472 282 N
ATOM 1168 CA ALA A 174 -27.957 44.805 81.070 1.00 56.80 C
ANISOU 1168 CA ALA A 174 7671 6575 7335 -1662 2336 410 C
ATOM 1169 C ALA A 174 -29.256 44.355 81.752 1.00 61.37 C
ANISOU 1169 C ALA A 174 8304 7093 7923 -1675 1887 742 C
ATOM 1170 O ALA A 174 -30.330 44.888 81.457 1.00 68.95 O
ANISOU 1170 O ALA A 174 9417 8065 8715 -1671 1688 935 O
ATOM 1171 CB ALA A 174 -27.398 43.682 80.188 1.00 55.68 C
ANISOU 1171 CB ALA A 174 7679 6274 7202 -1500 2344 175 C
ATOM 1172 N ILE A 175 -29.175 43.368 82.658 1.00 58.23 N
ANISOU 1172 N ILE A 175 7697 6680 7746 -1552 1579 773 N
ATOM 1173 CA ILE A 175 -30.356 42.780 83.297 1.00 54.16 C
ANISOU 1173 CA ILE A 175 7228 6074 7277 -1546 1171 1081 C
ATOM 1174 C ILE A 175 -31.149 43.767 84.167 1.00 57.68 C
ANISOU 1174 C ILE A 175 7545 6657 7716 -1593 1099 1353 C
ATOM 1175 O ILE A 175 -32.293 43.475 84.520 1.00 61.11 O
ANISOU 1175 O ILE A 175 8099 6976 8145 -1469 903 1436 O
ATOM 1176 CB ILE A 175 -29.997 41.506 84.131 1.00 50.12 C
ANISOU 1176 CB ILE A 175 6520 5517 7005 -1374 871 1035 C
ATOM 1177 CG1 ILE A 175 -29.207 41.827 85.413 1.00 47.62 C
ANISOU 1177 CG1 ILE A 175 5849 5364 6880 -1334 914 978 C
ATOM 1178 CG2 ILE A 175 -29.282 40.433 83.273 1.00 49.13 C
ANISOU 1178 CG2 ILE A 175 6491 5272 6903 -1225 856 759 C
ATOM 1179 CD1 ILE A 175 -29.011 40.618 86.358 1.00 43.50 C
ANISOU 1179 CD1 ILE A 175 5174 4779 6574 -1165 576 980 C
ATOM 1180 N MET A 176 -30.588 44.935 84.506 1.00 57.07 N
ANISOU 1180 N MET A 176 8172 7849 5663 571 246 229 N
ATOM 1181 CA MET A 176 -31.317 45.909 85.320 1.00 50.88 C
ANISOU 1181 CA MET A 176 7165 7028 5138 479 413 288 C
ATOM 1182 C MET A 176 -31.942 47.042 84.494 1.00 53.16 C
ANISOU 1182 C MET A 176 7634 6997 5567 380 446 391 C
ATOM 1183 O MET A 176 -32.487 47.990 85.070 1.00 51.80 O
ANISOU 1183 O MET A 176 7313 6774 5593 328 595 407 O
ATOM 1184 CB MET A 176 -30.409 46.465 86.429 1.00 45.72 C
ANISOU 1184 CB MET A 176 6226 6747 4397 440 762 -1 C
ATOM 1185 CG MET A 176 -29.999 45.409 87.472 1.00 49.00 C
ANISOU 1185 CG MET A 176 6472 7463 4684 610 692 -77 C
ATOM 1186 SD MET A 176 -31.388 44.443 88.108 1.00 53.91 S
ANISOU 1186 SD MET A 176 7094 7878 5512 658 410 265 S
ATOM 1187 CE MET A 176 -30.532 43.277 89.166 1.00 50.35 C
ANISOU 1187 CE MET A 176 6632 7740 4758 888 367 127 C
ATOM 1188 N VAL A 177 -31.936 46.924 83.162 1.00 49.27 N
ANISOU 1188 N VAL A 177 7489 6268 4963 383 280 470 N
ATOM 1189 CA VAL A 177 -32.574 47.895 82.269 1.00 52.59 C
ANISOU 1189 CA VAL A 177 8190 6334 5457 354 242 594 C
ATOM 1190 C VAL A 177 -34.101 47.832 82.400 1.00 56.99 C
ANISOU 1190 C VAL A 177 8629 6704 6319 479 -51 831 C
ATOM 1191 O VAL A 177 -34.722 48.903 82.449 1.00 62.71 O
ANISOU 1191 O VAL A 177 9380 7255 7191 509 3 865 O
ATOM 1192 CB VAL A 177 -32.065 47.729 80.814 1.00 51.43 C
ANISOU 1192 CB VAL A 177 8478 6009 5055 319 151 592 C
ATOM 1193 CG1 VAL A 177 -32.825 48.625 79.827 1.00 49.00 C
ANISOU 1193 CG1 VAL A 177 8555 5285 4780 350 40 758 C
ATOM 1194 CG2 VAL A 177 -30.555 48.073 80.712 1.00 47.08 C
ANISOU 1194 CG2 VAL A 177 8006 5683 4200 133 525 262 C
ATOM 1195 N PRO A 178 -34.780 46.665 82.528 1.00 53.51 N
ANISOU 1195 N PRO A 178 8049 6304 5980 545 -342 960 N
ATOM 1196 CA PRO A 178 -36.248 46.705 82.730 1.00 52.14 C
ANISOU 1196 CA PRO A 178 7685 6028 6096 611 -569 1093 C
ATOM 1197 C PRO A 178 -36.675 47.462 83.986 1.00 53.19 C
ANISOU 1197 C PRO A 178 7462 6293 6455 581 -361 1020 C
ATOM 1198 O PRO A 178 -37.786 48.004 84.042 1.00 54.36 O
ANISOU 1198 O PRO A 178 7471 6348 6834 659 -485 1056 O
ATOM 1199 CB PRO A 178 -36.652 45.223 82.822 1.00 52.30 C
ANISOU 1199 CB PRO A 178 7627 6122 6122 587 -806 1175 C
ATOM 1200 CG PRO A 178 -35.531 44.466 82.213 1.00 47.46 C
ANISOU 1200 CG PRO A 178 7287 5531 5215 590 -814 1144 C
ATOM 1201 CD PRO A 178 -34.282 45.273 82.494 1.00 47.24 C
ANISOU 1201 CD PRO A 178 7282 5643 5025 556 -470 959 C
ATOM 1202 N GLN A 179 -35.798 47.483 84.998 1.00 54.07 N
ANISOU 1202 N GLN A 179 7405 6650 6490 488 -60 887 N
ATOM 1203 CA GLN A 179 -36.022 48.251 86.221 1.00 53.69 C
ANISOU 1203 CA GLN A 179 7029 6750 6622 437 186 793 C
ATOM 1204 C GLN A 179 -36.055 49.749 85.920 1.00 59.20 C
ANISOU 1204 C GLN A 179 7853 7264 7375 464 353 737 C
ATOM 1205 O GLN A 179 -36.956 50.469 86.372 1.00 64.37 O
ANISOU 1205 O GLN A 179 8323 7865 8272 520 352 739 O
ATOM 1206 CB GLN A 179 -34.914 47.938 87.230 1.00 52.21 C
ANISOU 1206 CB GLN A 179 6687 6880 6272 360 458 636 C
ATOM 1207 CG GLN A 179 -35.143 48.558 88.586 1.00 54.26 C
ANISOU 1207 CG GLN A 179 6587 7329 6702 291 704 539 C
ATOM 1208 CD GLN A 179 -36.434 48.097 89.217 1.00 62.90 C
ANISOU 1208 CD GLN A 179 7431 8426 8043 266 540 647 C
ATOM 1209 OE1 GLN A 179 -36.711 46.898 89.281 1.00 72.30 O
ANISOU 1209 OE1 GLN A 179 8655 9637 9178 244 354 739 O
ATOM 1210 NE2 GLN A 179 -37.273 49.047 89.608 1.00 60.61 N
ANISOU 1210 NE2 GLN A 179 6920 8096 8013 258 607 615 N
ATOM 1211 N ALA A 180 -35.040 50.234 85.198 1.00 54.89 N
ANISOU 1211 N ALA A 180 7646 6626 6583 412 524 657 N
ATOM 1212 CA ALA A 180 -34.984 51.625 84.761 1.00 49.76 C
ANISOU 1212 CA ALA A 180 7285 5718 5904 405 706 612 C
ATOM 1213 C ALA A 180 -36.201 51.986 83.906 1.00 52.97 C
ANISOU 1213 C ALA A 180 7914 5771 6442 625 364 791 C
ATOM 1214 O ALA A 180 -36.750 53.088 84.027 1.00 60.37 O
ANISOU 1214 O ALA A 180 8927 6514 7495 729 418 781 O
ATOM 1215 CB ALA A 180 -33.689 51.863 83.982 1.00 42.18 C
ANISOU 1215 CB ALA A 180 6710 4717 4600 245 942 478 C
ATOM 1216 N ALA A 181 -36.638 51.041 83.067 1.00 52.30 N
ANISOU 1216 N ALA A 181 7926 5618 6328 724 -5 932 N
ATOM 1217 CA ALA A 181 -37.747 51.237 82.133 1.00 53.86 C
ANISOU 1217 CA ALA A 181 8323 5536 6604 965 -386 1067 C
ATOM 1218 C ALA A 181 -39.096 51.466 82.833 1.00 51.23 C
ANISOU 1218 C ALA A 181 7577 5280 6608 1131 -564 1051 C
ATOM 1219 O ALA A 181 -39.929 52.222 82.326 1.00 51.54 O
ANISOU 1219 O ALA A 181 7771 5094 6717 1391 -775 1072 O
ATOM 1220 CB ALA A 181 -37.839 50.027 81.201 1.00 53.34 C
ANISOU 1220 CB ALA A 181 8375 5462 6431 985 -711 1178 C
ATOM 1221 N VAL A 182 -39.349 50.785 83.963 1.00 49.63 N
ANISOU 1221 N VAL A 182 6868 5399 6590 998 -500 991 N
ATOM 1222 CA VAL A 182 -40.643 50.932 84.648 1.00 48.22 C
ANISOU 1222 CA VAL A 182 6250 5347 6723 1095 -642 921 C
ATOM 1223 C VAL A 182 -40.682 52.147 85.592 1.00 48.86 C
ANISOU 1223 C VAL A 182 6165 5450 6951 1120 -359 799 C
ATOM 1224 O VAL A 182 -41.772 52.622 85.928 1.00 52.14 O
ANISOU 1224 O VAL A 182 6302 5901 7606 1284 -495 709 O
ATOM 1225 CB VAL A 182 -41.064 49.647 85.406 1.00 49.86 C
ANISOU 1225 CB VAL A 182 6041 5857 7047 896 -697 900 C
ATOM 1226 CG1 VAL A 182 -41.278 48.468 84.443 1.00 50.55 C
ANISOU 1226 CG1 VAL A 182 6288 5897 7022 884 -1011 1000 C
ATOM 1227 CG2 VAL A 182 -40.080 49.253 86.513 1.00 42.65 C
ANISOU 1227 CG2 VAL A 182 4998 5159 6047 657 -345 867 C
ATOM 1228 N MET A 183 -39.518 52.684 85.986 1.00 51.54 N
ANISOU 1228 N MET A 183 6661 5782 7139 967 31 756 N
ATOM 1229 CA MET A 183 -39.455 53.846 86.876 1.00 50.65 C
ANISOU 1229 CA MET A 183 6423 5681 7140 954 342 626 C
ATOM 1230 C MET A 183 -40.072 55.076 86.223 1.00 56.04 C
ANISOU 1230 C MET A 183 7438 6000 7855 1246 221 629 C
ATOM 1231 O MET A 183 -39.646 55.491 85.138 1.00 60.50 O
ANISOU 1231 O MET A 183 8579 6230 8177 1328 185 711 O
ATOM 1232 CB MET A 183 -38.001 54.145 87.259 1.00 50.24 C
ANISOU 1232 CB MET A 183 6512 5709 6868 707 788 536 C
ATOM 1233 CG MET A 183 -37.324 53.080 88.101 1.00 47.64 C
ANISOU 1233 CG MET A 183 5853 5765 6482 496 922 486 C
ATOM 1234 SD MET A 183 -38.416 52.380 89.354 1.00 49.19 S
ANISOU 1234 SD MET A 183 5451 6258 6980 468 808 476 S
ATOM 1235 CE MET A 183 -38.627 53.760 90.478 1.00 43.71 C
ANISOU 1235 CE MET A 183 4488 5628 6491 446 1140 303 C
ATOM 1236 N GLU A 184 -41.059 55.676 86.893 1.00 58.80 N
ANISOU 1236 N GLU A 184 7462 6404 8475 1414 162 524 N
ATOM 1237 CA GLU A 184 -41.682 56.908 86.427 1.00 63.52 C
ANISOU 1237 CA GLU A 184 8376 6658 9101 1765 36 494 C
ATOM 1238 C GLU A 184 -41.829 57.882 87.583 1.00 64.99 C
ANISOU 1238 C GLU A 184 8301 6914 9476 1754 332 327 C
ATOM 1239 O GLU A 184 -42.099 57.489 88.728 1.00 62.56 O
ANISOU 1239 O GLU A 184 7390 6985 9394 1584 448 213 O
ATOM 1240 CB GLU A 184 -43.061 56.655 85.772 1.00 71.88 C
ANISOU 1240 CB GLU A 184 9309 7699 10302 2149 -507 487 C
ATOM 1241 CG GLU A 184 -43.051 55.827 84.469 1.00 83.35 C
ANISOU 1241 CG GLU A 184 11080 9032 11558 2222 -849 644 C
ATOM 1242 CD GLU A 184 -42.116 56.348 83.368 1.00 92.86 C
ANISOU 1242 CD GLU A 184 13092 9795 12395 2246 -760 798 C
ATOM 1243 OE1 GLU A 184 -41.982 57.580 83.184 1.00 97.88 O
ANISOU 1243 OE1 GLU A 184 14202 10073 12916 2417 -634 788 O
ATOM 1244 OE2 GLU A 184 -41.526 55.498 82.666 1.00 94.06 O
ANISOU 1244 OE2 GLU A 184 13437 9948 12354 2077 -810 916 O
ATOM 1245 N CYS A 185 -41.675 59.164 87.260 1.00 71.93 N
ANISOU 1245 N CYS A 185 9690 7399 10242 1932 455 309 N
ATOM 1246 CA CYS A 185 -41.788 60.276 88.192 1.00 74.93 C
ANISOU 1246 CA CYS A 185 9965 7741 10762 1961 741 150 C
ATOM 1247 C CYS A 185 -43.083 60.994 87.844 1.00 81.47 C
ANISOU 1247 C CYS A 185 10869 8351 11736 2502 345 86 C
ATOM 1248 O CYS A 185 -43.165 61.657 86.803 1.00 88.54 O
ANISOU 1248 O CYS A 185 12454 8774 12412 2820 165 176 O
ATOM 1249 CB CYS A 185 -40.580 61.205 88.060 1.00 80.36 C
ANISOU 1249 CB CYS A 185 11257 8112 11164 1736 1214 145 C
ATOM 1250 SG CYS A 185 -40.409 62.440 89.362 1.00 88.58 S
ANISOU 1250 SG CYS A 185 12139 9171 12347 1616 1697 -75 S
ATOM 1251 N SER A 186 -44.044 60.971 88.763 1.00 82.12 N
ANISOU 1251 N SER A 186 10282 8764 12155 2614 241 -101 N
ATOM 1252 CA SER A 186 -45.380 61.492 88.515 1.00 89.73 C
ANISOU 1252 CA SER A 186 11147 9659 13289 3162 -191 -246 C
ATOM 1253 C SER A 186 -45.729 62.526 89.575 1.00 91.03 C
ANISOU 1253 C SER A 186 11063 9858 13667 3264 29 -468 C
ATOM 1254 O SER A 186 -45.380 62.360 90.751 1.00 90.11 O
ANISOU 1254 O SER A 186 10462 10069 13706 2870 405 -560 O
ATOM 1255 CB SER A 186 -46.433 60.360 88.516 1.00 94.97 C
ANISOU 1255 CB SER A 186 11135 10776 14173 3219 -598 -353 C
ATOM 1256 OG SER A 186 -46.281 59.494 89.634 1.00 96.77 O
ANISOU 1256 OG SER A 186 10705 11481 14582 2736 -334 -421 O
ATOM 1257 N SER A 187 -46.459 63.564 89.175 1.00 95.64 N
ANISOU 1257 N SER A 187 11976 10114 14249 3825 -230 -568 N
ATOM 1258 CA SER A 187 -46.837 64.625 90.111 1.00 99.86 C
ANISOU 1258 CA SER A 187 12332 10633 14976 3989 -49 -797 C
ATOM 1259 C SER A 187 -48.139 64.267 90.820 1.00 97.19 C
ANISOU 1259 C SER A 187 11078 10830 15021 4174 -336 -1110 C
ATOM 1260 O SER A 187 -49.085 63.778 90.205 1.00 99.90 O
ANISOU 1260 O SER A 187 11195 11336 15425 4515 -839 -1207 O
ATOM 1261 CB SER A 187 -46.995 65.983 89.400 1.00108.82 C
ANISOU 1261 CB SER A 187 14329 11119 15898 4545 -181 -784 C
ATOM 1262 OG SER A 187 -47.918 65.925 88.322 1.00117.82 O
ANISOU 1262 OG SER A 187 15695 12113 16959 5165 -806 -793 O
ATOM 1263 N PHE A 199 -46.244 68.046 94.452 1.00 85.88 N
ANISOU 1263 N PHE A 199 9910 8954 13766 3511 1533 -1501 N
ATOM 1264 CA PHE A 199 -45.029 67.297 94.774 1.00 82.86 C
ANISOU 1264 CA PHE A 199 9432 8795 13254 2843 1952 -1345 C
ATOM 1265 C PHE A 199 -44.926 66.011 93.931 1.00 79.22 C
ANISOU 1265 C PHE A 199 8945 8478 12675 2753 1648 -1131 C
ATOM 1266 O PHE A 199 -45.945 65.444 93.541 1.00 85.10 O
ANISOU 1266 O PHE A 199 9382 9392 13561 3066 1162 -1170 O
ATOM 1267 CB PHE A 199 -44.974 66.992 96.286 1.00 80.34 C
ANISOU 1267 CB PHE A 199 8281 9046 13200 2427 2292 -1533 C
ATOM 1268 CG PHE A 199 -45.860 65.848 96.741 1.00 77.08 C
ANISOU 1268 CG PHE A 199 7033 9202 13050 2377 2002 -1625 C
ATOM 1269 CD1 PHE A 199 -45.350 64.562 96.846 1.00 73.81 C
ANISOU 1269 CD1 PHE A 199 6357 9124 12564 1957 2052 -1476 C
ATOM 1270 CD2 PHE A 199 -47.177 66.068 97.118 1.00 76.51 C
ANISOU 1270 CD2 PHE A 199 6449 9342 13279 2721 1714 -1897 C
ATOM 1271 CE1 PHE A 199 -46.144 63.512 97.284 1.00 72.31 C
ANISOU 1271 CE1 PHE A 199 5527 9412 12538 1833 1825 -1550 C
ATOM 1272 CE2 PHE A 199 -47.976 65.018 97.556 1.00 77.42 C
ANISOU 1272 CE2 PHE A 199 5939 10006 13470 2515 1471 -1950 C
ATOM 1273 CZ PHE A 199 -47.457 63.740 97.638 1.00 73.70 C
ANISOU 1273 CZ PHE A 199 5363 9800 12838 2040 1523 -1740 C
ATOM 1274 N SER A 200 -43.709 65.572 93.622 1.00 73.36 N
ANISOU 1274 N SER A 200 8525 7682 11667 2338 1928 -943 N
ATOM 1275 CA SER A 200 -43.496 64.410 92.764 1.00 73.82 C
ANISOU 1275 CA SER A 200 8648 7820 11578 2255 1666 -737 C
ATOM 1276 C SER A 200 -43.203 63.129 93.549 1.00 77.76 C
ANISOU 1276 C SER A 200 8470 8893 12183 1819 1777 -734 C
ATOM 1277 O SER A 200 -42.727 63.153 94.688 1.00 78.83 O
ANISOU 1277 O SER A 200 8229 9325 12396 1481 2163 -847 O
ATOM 1278 CB SER A 200 -42.366 64.668 91.759 1.00 74.11 C
ANISOU 1278 CB SER A 200 9525 7419 11213 2115 1852 -552 C
ATOM 1279 OG SER A 200 -42.858 65.303 90.588 1.00 80.04 O
ANISOU 1279 OG SER A 200 10978 7633 11801 2592 1518 -459 O
ATOM 1280 N VAL A 201 -43.501 61.992 92.910 1.00 79.16 N
ANISOU 1280 N VAL A 201 8538 9205 12334 1846 1422 -605 N
ATOM 1281 CA VAL A 201 -43.303 60.668 93.489 1.00 70.64 C
ANISOU 1281 CA VAL A 201 6951 8587 11302 1484 1461 -572 C
ATOM 1282 C VAL A 201 -42.677 59.761 92.425 1.00 68.35 C
ANISOU 1282 C VAL A 201 7036 8186 10747 1407 1302 -347 C
ATOM 1283 O VAL A 201 -43.157 59.702 91.288 1.00 72.62 O
ANISOU 1283 O VAL A 201 7900 8473 11220 1706 927 -250 O
ATOM 1284 CB VAL A 201 -44.618 60.079 94.049 1.00 67.43 C
ANISOU 1284 CB VAL A 201 5866 8550 11202 1555 1188 -728 C
ATOM 1285 CG1 VAL A 201 -44.599 58.549 94.080 1.00 67.45 C
ANISOU 1285 CG1 VAL A 201 5602 8861 11165 1269 1073 -630 C
ATOM 1286 CG2 VAL A 201 -44.865 60.628 95.458 1.00 63.13 C
ANISOU 1286 CG2 VAL A 201 4823 8275 10887 1413 1496 -959 C
ATOM 1287 N CYS A 202 -41.581 59.100 92.792 1.00 65.13 N
ANISOU 1287 N CYS A 202 6599 7976 10174 1036 1583 -287 N
ATOM 1288 CA CYS A 202 -40.871 58.159 91.937 1.00 66.95 C
ANISOU 1288 CA CYS A 202 7122 8167 10151 930 1475 -113 C
ATOM 1289 C CYS A 202 -41.286 56.745 92.327 1.00 67.81 C
ANISOU 1289 C CYS A 202 6789 8629 10347 793 1284 -72 C
ATOM 1290 O CYS A 202 -41.137 56.352 93.489 1.00 70.49 O
ANISOU 1290 O CYS A 202 6725 9302 10757 557 1498 -155 O
ATOM 1291 CB CYS A 202 -39.358 58.342 92.068 1.00 65.07 C
ANISOU 1291 CB CYS A 202 7140 7945 9638 645 1898 -136 C
ATOM 1292 SG CYS A 202 -38.335 57.351 90.943 1.00 66.99 S
ANISOU 1292 SG CYS A 202 7785 8134 9534 534 1803 15 S
ATOM 1293 N ASP A 203 -41.839 55.987 91.373 1.00 63.85 N
ANISOU 1293 N ASP A 203 6397 8042 9821 930 889 45 N
ATOM 1294 CA ASP A 203 -42.257 54.623 91.627 1.00 63.50 C
ANISOU 1294 CA ASP A 203 6032 8271 9823 769 719 79 C
ATOM 1295 C ASP A 203 -42.337 53.879 90.295 1.00 59.28 C
ANISOU 1295 C ASP A 203 5828 7557 9139 885 366 238 C
ATOM 1296 O ASP A 203 -42.304 54.484 89.223 1.00 60.65 O
ANISOU 1296 O ASP A 203 6415 7414 9215 1130 208 305 O
ATOM 1297 CB ASP A 203 -43.615 54.598 92.349 1.00 71.47 C
ANISOU 1297 CB ASP A 203 6497 9516 11143 788 598 -99 C
ATOM 1298 CG ASP A 203 -43.828 53.342 93.166 1.00 79.91 C
ANISOU 1298 CG ASP A 203 7218 10911 12233 457 646 -118 C
ATOM 1299 OD1 ASP A 203 -42.849 52.778 93.695 1.00 80.52 O
ANISOU 1299 OD1 ASP A 203 7386 11084 12124 230 880 -30 O
ATOM 1300 OD2 ASP A 203 -44.980 52.864 93.192 1.00 85.00 O
ANISOU 1300 OD2 ASP A 203 7542 11710 13045 432 430 -235 O
ATOM 1301 N GLU A 204 -42.436 52.535 90.379 1.00 57.03 N
ANISOU 1301 N GLU A 204 5401 7457 8810 695 253 298 N
ATOM 1302 CA GLU A 204 -42.598 51.671 89.207 1.00 57.37 C
ANISOU 1302 CA GLU A 204 5695 7374 8728 763 -82 427 C
ATOM 1303 C GLU A 204 -43.995 51.824 88.616 1.00 57.28 C
ANISOU 1303 C GLU A 204 5513 7340 8910 997 -460 333 C
ATOM 1304 O GLU A 204 -44.985 51.811 89.351 1.00 54.13 O
ANISOU 1304 O GLU A 204 4636 7183 8749 946 -485 146 O
ATOM 1305 CB GLU A 204 -42.383 50.195 89.579 1.00 58.75 C
ANISOU 1305 CB GLU A 204 5785 7738 8800 485 -74 491 C
ATOM 1306 CG GLU A 204 -40.982 49.829 90.027 1.00 54.75 C
ANISOU 1306 CG GLU A 204 5468 7288 8047 334 206 561 C
ATOM 1307 CD GLU A 204 -40.861 48.395 90.529 1.00 57.34 C
ANISOU 1307 CD GLU A 204 5763 7772 8253 119 197 615 C
ATOM 1308 OE1 GLU A 204 -41.731 47.551 90.217 1.00 59.80 O
ANISOU 1308 OE1 GLU A 204 6023 8078 8619 44 -35 637 O
ATOM 1309 OE2 GLU A 204 -39.911 48.135 91.295 1.00 59.36 O
ANISOU 1309 OE2 GLU A 204 6052 8161 8342 26 434 609 O
ATOM 1310 N ARG A 205 -44.086 51.947 87.291 1.00 60.70 N
ANISOU 1310 N ARG A 205 6320 7517 9227 1253 -758 426 N
ATOM 1311 CA ARG A 205 -45.374 52.032 86.606 1.00 64.83 C
ANISOU 1311 CA ARG A 205 6697 8049 9887 1537 -1176 309 C
ATOM 1312 C ARG A 205 -45.631 50.707 85.894 1.00 64.06 C
ANISOU 1312 C ARG A 205 6615 8025 9699 1409 -1435 370 C
ATOM 1313 O ARG A 205 -44.835 50.290 85.046 1.00 62.86 O
ANISOU 1313 O ARG A 205 6909 7668 9307 1393 -1478 567 O
ATOM 1314 CB ARG A 205 -45.404 53.179 85.595 1.00 68.30 C
ANISOU 1314 CB ARG A 205 7595 8126 10227 1976 -1371 355 C
ATOM 1315 CG ARG A 205 -46.800 53.505 85.053 1.00 78.40 C
ANISOU 1315 CG ARG A 205 8675 9458 11656 2387 -1824 164 C
ATOM 1316 CD ARG A 205 -46.757 54.785 84.229 1.00 92.31 C
ANISOU 1316 CD ARG A 205 10993 10802 13278 2868 -1980 219 C
ATOM 1317 NE ARG A 205 -48.009 55.535 84.238 1.00106.35 N
ANISOU 1317 NE ARG A 205 12511 12657 15239 3338 -2304 -40 N
ATOM 1318 CZ ARG A 205 -48.082 56.812 84.610 1.00109.58 C
ANISOU 1318 CZ ARG A 205 13068 12871 15695 3626 -2207 -118 C
ATOM 1319 NH1 ARG A 205 -46.980 57.462 84.970 1.00104.80 N
ANISOU 1319 NH1 ARG A 205 12872 11985 14963 3437 -1773 43 N
ATOM 1320 NH2 ARG A 205 -49.246 57.446 84.616 1.00113.72 N
ANISOU 1320 NH2 ARG A 205 13336 13493 16379 4110 -2541 -390 N
ATOM 1321 N TRP A 206 -46.736 50.048 86.244 1.00 59.14 N
ANISOU 1321 N TRP A 206 5507 7705 9260 1286 -1580 171 N
ATOM 1322 CA TRP A 206 -47.112 48.767 85.664 1.00 57.58 C
ANISOU 1322 CA TRP A 206 5287 7600 8990 1107 -1794 177 C
ATOM 1323 C TRP A 206 -48.464 48.884 84.973 1.00 68.70 C
ANISOU 1323 C TRP A 206 6411 9157 10535 1368 -2212 -71 C
ATOM 1324 O TRP A 206 -49.431 49.382 85.566 1.00 73.84 O
ANISOU 1324 O TRP A 206 6571 10066 11419 1451 -2251 -366 O
ATOM 1325 CB TRP A 206 -47.143 47.664 86.728 1.00 55.92 C
ANISOU 1325 CB TRP A 206 4806 7634 8807 616 -1539 128 C
ATOM 1326 CG TRP A 206 -45.795 47.394 87.337 1.00 53.09 C
ANISOU 1326 CG TRP A 206 4745 7163 8264 420 -1194 350 C
ATOM 1327 CD1 TRP A 206 -45.330 47.855 88.533 1.00 52.39 C
ANISOU 1327 CD1 TRP A 206 4514 7166 8224 302 -848 329 C
ATOM 1328 CD2 TRP A 206 -44.732 46.609 86.769 1.00 58.17 C
ANISOU 1328 CD2 TRP A 206 5852 7620 8632 354 -1182 582 C
ATOM 1329 NE1 TRP A 206 -44.049 47.403 88.751 1.00 53.65 N
ANISOU 1329 NE1 TRP A 206 5005 7233 8146 187 -637 516 N
ATOM 1330 CE2 TRP A 206 -43.659 46.638 87.683 1.00 55.93 C
ANISOU 1330 CE2 TRP A 206 5663 7353 8235 226 -839 665 C
ATOM 1331 CE3 TRP A 206 -44.588 45.884 85.581 1.00 58.92 C
ANISOU 1331 CE3 TRP A 206 6270 7558 8557 405 -1436 700 C
ATOM 1332 CZ2 TRP A 206 -42.456 45.969 87.446 1.00 49.38 C
ANISOU 1332 CZ2 TRP A 206 5220 6415 7128 180 -760 830 C
ATOM 1333 CZ3 TRP A 206 -43.390 45.221 85.347 1.00 55.47 C
ANISOU 1333 CZ3 TRP A 206 6235 6984 7856 332 -1338 886 C
ATOM 1334 CH2 TRP A 206 -42.341 45.269 86.275 1.00 50.81 C
ANISOU 1334 CH2 TRP A 206 5710 6438 7157 237 -1011 936 C
ATOM 1335 N ALA A 207 -48.520 48.428 83.717 1.00 69.27 N
ANISOU 1335 N ALA A 207 6772 9097 10451 1512 -2532 16 N
ATOM 1336 CA ALA A 207 -49.758 48.436 82.948 1.00 74.40 C
ANISOU 1336 CA ALA A 207 7162 9923 11185 1785 -2972 -243 C
ATOM 1337 C ALA A 207 -50.772 47.412 83.466 1.00 81.65 C
ANISOU 1337 C ALA A 207 7493 11274 12256 1396 -2974 -557 C
ATOM 1338 O ALA A 207 -51.979 47.629 83.321 1.00 91.17 O
ANISOU 1338 O ALA A 207 8233 12790 13618 1581 -3248 -927 O
ATOM 1339 CB ALA A 207 -49.456 48.185 81.468 1.00 77.21 C
ANISOU 1339 CB ALA A 207 8022 10016 11298 2013 -3290 -54 C
ATOM 1340 N ASP A 208 -50.313 46.306 84.073 1.00 80.67 N
ANISOU 1340 N ASP A 208 7404 11185 12063 862 -2671 -450 N
ATOM 1341 CA ASP A 208 -51.218 45.270 84.575 1.00 80.80 C
ANISOU 1341 CA ASP A 208 6978 11555 12167 398 -2606 -741 C
ATOM 1342 C ASP A 208 -50.771 44.731 85.942 1.00 79.33 C
ANISOU 1342 C ASP A 208 6756 11410 11975 -107 -2137 -675 C
ATOM 1343 O ASP A 208 -49.670 45.031 86.425 1.00 77.20 O
ANISOU 1343 O ASP A 208 6808 10912 11615 -83 -1890 -389 O
ATOM 1344 CB ASP A 208 -51.377 44.123 83.553 1.00 83.54 C
ANISOU 1344 CB ASP A 208 7521 11872 12349 242 -2824 -718 C
ATOM 1345 CG ASP A 208 -50.103 43.320 83.349 1.00 87.16 C
ANISOU 1345 CG ASP A 208 8593 11976 12548 50 -2654 -310 C
ATOM 1346 OD1 ASP A 208 -50.044 42.172 83.841 1.00 90.97 O
ANISOU 1346 OD1 ASP A 208 9133 12490 12942 -430 -2439 -304 O
ATOM 1347 OD2 ASP A 208 -49.174 43.824 82.682 1.00 87.10 O
ANISOU 1347 OD2 ASP A 208 9031 11659 12404 378 -2733 -22 O
ATOM 1348 N ASP A 209 -51.662 43.935 86.565 1.00 58.28 N
ANISOU 1348 N ASP A 209 5210 8080 8855 2176 -1286 235 N
ATOM 1349 CA ASP A 209 -51.466 43.356 87.903 1.00 61.21 C
ANISOU 1349 CA ASP A 209 5488 8440 9328 1957 -975 36 C
ATOM 1350 C ASP A 209 -50.499 42.167 87.910 1.00 60.89 C
ANISOU 1350 C ASP A 209 5589 8469 9076 1649 -768 87 C
ATOM 1351 O ASP A 209 -49.875 41.895 88.944 1.00 63.02 O
ANISOU 1351 O ASP A 209 5930 8642 9371 1484 -537 42 O
ATOM 1352 CB ASP A 209 -52.801 42.870 88.508 1.00 66.75 C
ANISOU 1352 CB ASP A 209 5881 9322 10159 1909 -886 -290 C
ATOM 1353 CG ASP A 209 -53.889 43.951 88.588 1.00 80.65 C
ANISOU 1353 CG ASP A 209 7539 11016 12086 2128 -1009 -351 C
ATOM 1354 OD1 ASP A 209 -53.672 45.005 89.224 1.00 85.21 O
ANISOU 1354 OD1 ASP A 209 8221 11366 12789 2240 -968 -300 O
ATOM 1355 OD2 ASP A 209 -54.992 43.711 88.042 1.00 90.57 O
ANISOU 1355 OD2 ASP A 209 8598 12456 13359 2180 -1141 -481 O
ATOM 1356 N LEU A 210 -50.382 41.433 86.786 1.00 57.45 N
ANISOU 1356 N LEU A 210 5197 8202 8429 1579 -854 167 N
ATOM 1357 CA LEU A 210 -49.591 40.201 86.724 1.00 56.67 C
ANISOU 1357 CA LEU A 210 5199 8181 8153 1308 -659 178 C
ATOM 1358 C LEU A 210 -48.095 40.467 86.519 1.00 58.02 C
ANISOU 1358 C LEU A 210 5674 8163 8208 1222 -581 438 C
ATOM 1359 O LEU A 210 -47.262 39.823 87.164 1.00 60.37 O
ANISOU 1359 O LEU A 210 6046 8410 8483 1042 -376 422 O
ATOM 1360 CB LEU A 210 -50.128 39.275 85.618 1.00 61.13 C
ANISOU 1360 CB LEU A 210 5667 9007 8551 1252 -761 108 C
ATOM 1361 CG LEU A 210 -49.562 37.842 85.523 1.00 58.31 C
ANISOU 1361 CG LEU A 210 5369 8747 8037 977 -549 55 C
ATOM 1362 CD1 LEU A 210 -49.660 37.095 86.855 1.00 61.43 C
ANISOU 1362 CD1 LEU A 210 5683 9112 8546 817 -280 -145 C
ATOM 1363 CD2 LEU A 210 -50.229 37.029 84.410 1.00 52.27 C
ANISOU 1363 CD2 LEU A 210 4493 8246 7123 925 -661 -53 C
ATOM 1364 N ALA A 211 -47.734 41.410 85.633 1.00 52.57 N
ANISOU 1364 N ALA A 211 5167 7360 7449 1348 -739 669 N
ATOM 1365 CA ALA A 211 -46.332 41.735 85.357 1.00 46.98 C
ANISOU 1365 CA ALA A 211 4730 6472 6648 1242 -638 890 C
ATOM 1366 C ALA A 211 -45.496 42.044 86.604 1.00 54.40 C
ANISOU 1366 C ALA A 211 5707 7221 7740 1158 -457 864 C
ATOM 1367 O ALA A 211 -44.437 41.426 86.770 1.00 55.52 O
ANISOU 1367 O ALA A 211 5924 7349 7822 978 -298 885 O
ATOM 1368 CB ALA A 211 -46.262 42.882 84.341 1.00 46.53 C
ANISOU 1368 CB ALA A 211 4889 6280 6512 1400 -818 1130 C
ATOM 1369 N PRO A 212 -45.891 42.967 87.505 1.00 57.16 N
ANISOU 1369 N PRO A 212 6003 7426 8288 1283 -479 801 N
ATOM 1370 CA PRO A 212 -45.074 43.175 88.719 1.00 54.08 C
ANISOU 1370 CA PRO A 212 5655 6883 8009 1180 -315 748 C
ATOM 1371 C PRO A 212 -44.930 41.933 89.586 1.00 49.83 C
ANISOU 1371 C PRO A 212 5025 6472 7435 1019 -160 581 C
ATOM 1372 O PRO A 212 -43.904 41.772 90.256 1.00 49.06 O
ANISOU 1372 O PRO A 212 5011 6291 7339 902 -49 585 O
ATOM 1373 CB PRO A 212 -45.823 44.290 89.471 1.00 54.08 C
ANISOU 1373 CB PRO A 212 5590 6741 8218 1355 -371 662 C
ATOM 1374 CG PRO A 212 -47.206 44.256 88.939 1.00 51.48 C
ANISOU 1374 CG PRO A 212 5086 6557 7916 1535 -533 584 C
ATOM 1375 CD PRO A 212 -47.059 43.864 87.485 1.00 53.39 C
ANISOU 1375 CD PRO A 212 5423 6914 7949 1530 -656 756 C
ATOM 1376 N LYS A 213 -45.943 41.053 89.590 1.00 47.43 N
ANISOU 1376 N LYS A 213 4560 6360 7100 1012 -154 425 N
ATOM 1377 CA LYS A 213 -45.871 39.812 90.354 1.00 48.86 C
ANISOU 1377 CA LYS A 213 4708 6632 7224 851 13 281 C
ATOM 1378 C LYS A 213 -44.817 38.861 89.781 1.00 47.80 C
ANISOU 1378 C LYS A 213 4690 6536 6935 711 79 385 C
ATOM 1379 O LYS A 213 -44.022 38.284 90.531 1.00 43.85 O
ANISOU 1379 O LYS A 213 4270 5982 6409 611 194 364 O
ATOM 1380 CB LYS A 213 -47.246 39.136 90.389 1.00 49.54 C
ANISOU 1380 CB LYS A 213 4594 6901 7327 848 34 72 C
ATOM 1381 CG LYS A 213 -48.320 39.885 91.176 1.00 51.00 C
ANISOU 1381 CG LYS A 213 4618 7062 7699 965 27 -104 C
ATOM 1382 CD LYS A 213 -49.645 39.150 91.076 1.00 47.62 C
ANISOU 1382 CD LYS A 213 3948 6841 7304 934 62 -343 C
ATOM 1383 CE LYS A 213 -50.788 39.955 91.659 1.00 57.06 C
ANISOU 1383 CE LYS A 213 4926 8034 8720 1077 42 -545 C
ATOM 1384 NZ LYS A 213 -51.014 39.633 93.092 1.00 62.33 N
ANISOU 1384 NZ LYS A 213 5595 8651 9436 936 303 -749 N
ATOM 1385 N ILE A 214 -44.796 38.682 88.453 1.00 45.90 N
ANISOU 1385 N ILE A 214 4468 6389 6585 713 -1 486 N
ATOM 1386 CA ILE A 214 -43.800 37.801 87.844 1.00 45.25 C
ANISOU 1386 CA ILE A 214 4485 6340 6370 579 85 560 C
ATOM 1387 C ILE A 214 -42.402 38.419 87.950 1.00 45.73 C
ANISOU 1387 C ILE A 214 4676 6231 6468 552 121 697 C
ATOM 1388 O ILE A 214 -41.447 37.741 88.345 1.00 47.89 O
ANISOU 1388 O ILE A 214 4987 6476 6735 458 227 679 O
ATOM 1389 CB ILE A 214 -44.182 37.455 86.387 1.00 48.34 C
ANISOU 1389 CB ILE A 214 4875 6884 6608 569 5 609 C
ATOM 1390 CG1 ILE A 214 -45.466 36.615 86.367 1.00 47.14 C
ANISOU 1390 CG1 ILE A 214 4553 6924 6433 551 -6 413 C
ATOM 1391 CG2 ILE A 214 -43.048 36.681 85.684 1.00 48.20 C
ANISOU 1391 CG2 ILE A 214 4972 6877 6464 429 120 681 C
ATOM 1392 CD1 ILE A 214 -46.232 36.671 85.072 1.00 50.94 C
ANISOU 1392 CD1 ILE A 214 4983 7576 6794 607 -177 423 C
ATOM 1393 N TYR A 215 -42.276 39.724 87.655 1.00 44.72 N
ANISOU 1393 N TYR A 215 4614 5978 6399 637 34 819 N
ATOM 1394 CA TYR A 215 -40.984 40.412 87.721 1.00 40.74 C
ANISOU 1394 CA TYR A 215 4220 5307 5953 580 92 920 C
ATOM 1395 C TYR A 215 -40.369 40.363 89.125 1.00 43.93 C
ANISOU 1395 C TYR A 215 4586 5628 6476 544 156 812 C
ATOM 1396 O TYR A 215 -39.179 40.069 89.278 1.00 41.84 O
ANISOU 1396 O TYR A 215 4339 5328 6229 450 229 812 O
ATOM 1397 CB TYR A 215 -41.104 41.873 87.256 1.00 38.73 C
ANISOU 1397 CB TYR A 215 4075 4891 5748 673 7 1059 C
ATOM 1398 CG TYR A 215 -39.782 42.617 87.397 1.00 44.29 C
ANISOU 1398 CG TYR A 215 4883 5409 6537 573 104 1127 C
ATOM 1399 CD1 TYR A 215 -38.725 42.355 86.534 1.00 45.76 C
ANISOU 1399 CD1 TYR A 215 5151 5595 6641 428 215 1207 C
ATOM 1400 CD2 TYR A 215 -39.571 43.531 88.426 1.00 50.03 C
ANISOU 1400 CD2 TYR A 215 5606 5968 7436 600 107 1072 C
ATOM 1401 CE1 TYR A 215 -37.501 42.998 86.673 1.00 47.07 C
ANISOU 1401 CE1 TYR A 215 5368 5603 6912 308 330 1223 C
ATOM 1402 CE2 TYR A 215 -38.346 44.181 88.573 1.00 48.72 C
ANISOU 1402 CE2 TYR A 215 5505 5644 7364 480 203 1092 C
ATOM 1403 CZ TYR A 215 -37.317 43.909 87.693 1.00 46.52 C
ANISOU 1403 CZ TYR A 215 5282 5375 7020 332 316 1163 C
ATOM 1404 OH TYR A 215 -36.101 44.545 87.827 1.00 48.65 O
ANISOU 1404 OH TYR A 215 5577 5500 7408 188 434 1144 O
ATOM 1405 N HIS A 216 -41.149 40.681 90.166 1.00 42.57 N
ANISOU 1405 N HIS A 216 4358 5427 6388 621 123 704 N
ATOM 1406 CA HIS A 216 -40.585 40.727 91.508 1.00 42.06 C
ANISOU 1406 CA HIS A 216 4301 5285 6397 588 165 604 C
ATOM 1407 C HIS A 216 -40.344 39.348 92.103 1.00 43.27 C
ANISOU 1407 C HIS A 216 4450 5532 6457 521 231 516 C
ATOM 1408 O HIS A 216 -39.507 39.202 92.998 1.00 49.61 O
ANISOU 1408 O HIS A 216 5291 6281 7276 490 238 468 O
ATOM 1409 CB HIS A 216 -41.446 41.606 92.411 1.00 41.23 C
ANISOU 1409 CB HIS A 216 4170 5099 6398 678 135 509 C
ATOM 1410 CG HIS A 216 -41.229 43.059 92.148 1.00 42.43 C
ANISOU 1410 CG HIS A 216 4376 5073 6674 737 85 592 C
ATOM 1411 ND1 HIS A 216 -40.165 43.752 92.678 1.00 44.71 N
ANISOU 1411 ND1 HIS A 216 4724 5215 7047 670 111 586 N
ATOM 1412 CD2 HIS A 216 -41.865 43.913 91.317 1.00 45.53 C
ANISOU 1412 CD2 HIS A 216 4791 5399 7110 852 9 692 C
ATOM 1413 CE1 HIS A 216 -40.178 44.989 92.219 1.00 45.02 C
ANISOU 1413 CE1 HIS A 216 4834 5083 7187 720 87 674 C
ATOM 1414 NE2 HIS A 216 -41.203 45.116 91.392 1.00 45.96 N
ANISOU 1414 NE2 HIS A 216 4951 5237 7277 846 17 755 N
ATOM 1415 N SER A 217 -41.033 38.326 91.588 1.00 40.55 N
ANISOU 1415 N SER A 217 4075 5322 6012 500 269 492 N
ATOM 1416 CA SER A 217 -40.705 36.953 91.957 1.00 39.99 C
ANISOU 1416 CA SER A 217 4046 5303 5847 432 351 436 C
ATOM 1417 C SER A 217 -39.341 36.556 91.391 1.00 45.27 C
ANISOU 1417 C SER A 217 4740 5954 6509 389 363 513 C
ATOM 1418 O SER A 217 -38.466 36.085 92.130 1.00 48.38 O
ANISOU 1418 O SER A 217 5174 6298 6909 388 366 481 O
ATOM 1419 CB SER A 217 -41.814 36.016 91.477 1.00 31.81 C
ANISOU 1419 CB SER A 217 2965 4397 4723 395 413 368 C
ATOM 1420 OG SER A 217 -43.039 36.318 92.132 1.00 37.86 O
ANISOU 1420 OG SER A 217 3671 5187 5528 423 428 248 O
ATOM 1421 N CYS A 218 -39.140 36.778 90.084 1.00 44.06 N
ANISOU 1421 N CYS A 218 4563 5840 6338 361 365 604 N
ATOM 1422 CA CYS A 218 -37.851 36.524 89.437 1.00 39.36 C
ANISOU 1422 CA CYS A 218 3970 5228 5756 300 416 653 C
ATOM 1423 C CYS A 218 -36.727 37.330 90.083 1.00 42.10 C
ANISOU 1423 C CYS A 218 4296 5459 6239 300 385 647 C
ATOM 1424 O CYS A 218 -35.644 36.795 90.345 1.00 35.72 O
ANISOU 1424 O CYS A 218 3450 4641 5481 283 404 597 O
ATOM 1425 CB CYS A 218 -37.946 36.836 87.939 1.00 40.65 C
ANISOU 1425 CB CYS A 218 4155 5441 5847 252 441 753 C
ATOM 1426 SG CYS A 218 -39.108 35.794 87.019 1.00 50.20 S
ANISOU 1426 SG CYS A 218 5365 6824 6884 229 459 724 S
ATOM 1427 N PHE A 219 -36.978 38.626 90.356 1.00 44.63 N
ANISOU 1427 N PHE A 219 4631 5689 6635 326 330 676 N
ATOM 1428 CA PHE A 219 -35.987 39.492 91.002 1.00 38.54 C
ANISOU 1428 CA PHE A 219 3837 4805 6004 301 307 639 C
ATOM 1429 C PHE A 219 -35.515 38.891 92.331 1.00 39.53 C
ANISOU 1429 C PHE A 219 3936 4938 6144 338 246 518 C
ATOM 1430 O PHE A 219 -34.309 38.783 92.575 1.00 42.83 O
ANISOU 1430 O PHE A 219 4285 5344 6646 310 227 459 O
ATOM 1431 CB PHE A 219 -36.572 40.903 91.235 1.00 37.63 C
ANISOU 1431 CB PHE A 219 3769 4568 5963 336 265 670 C
ATOM 1432 CG PHE A 219 -35.523 41.957 91.574 1.00 35.12 C
ANISOU 1432 CG PHE A 219 3438 4111 5796 264 276 636 C
ATOM 1433 CD1 PHE A 219 -35.037 42.103 92.866 1.00 29.52 C
ANISOU 1433 CD1 PHE A 219 2684 3371 5160 267 214 497 C
ATOM 1434 CD2 PHE A 219 -35.012 42.788 90.582 1.00 41.28 C
ANISOU 1434 CD2 PHE A 219 4267 4789 6629 175 359 731 C
ATOM 1435 CE1 PHE A 219 -34.060 43.053 93.160 1.00 34.55 C
ANISOU 1435 CE1 PHE A 219 3283 3896 5948 179 224 428 C
ATOM 1436 CE2 PHE A 219 -34.036 43.739 90.871 1.00 40.55 C
ANISOU 1436 CE2 PHE A 219 4157 4559 6692 71 405 672 C
ATOM 1437 CZ PHE A 219 -33.560 43.868 92.162 1.00 38.07 C
ANISOU 1437 CZ PHE A 219 3755 4234 6476 71 332 507 C
ATOM 1438 N PHE A 220 -36.462 38.466 93.179 1.00 38.86 N
ANISOU 1438 N PHE A 220 3913 4879 5973 399 217 470 N
ATOM 1439 CA PHE A 220 -36.135 37.917 94.497 1.00 36.70 C
ANISOU 1439 CA PHE A 220 3692 4597 5656 440 154 376 C
ATOM 1440 C PHE A 220 -35.318 36.625 94.387 1.00 37.93 C
ANISOU 1440 C PHE A 220 3846 4798 5768 460 151 370 C
ATOM 1441 O PHE A 220 -34.318 36.450 95.095 1.00 43.48 O
ANISOU 1441 O PHE A 220 4534 5480 6507 504 52 310 O
ATOM 1442 CB PHE A 220 -37.430 37.686 95.300 1.00 38.72 C
ANISOU 1442 CB PHE A 220 4047 4861 5803 468 183 327 C
ATOM 1443 CG PHE A 220 -37.231 36.954 96.613 1.00 37.77 C
ANISOU 1443 CG PHE A 220 4063 4723 5566 498 144 253 C
ATOM 1444 CD1 PHE A 220 -36.466 37.509 97.627 1.00 36.54 C
ANISOU 1444 CD1 PHE A 220 3938 4515 5430 522 27 186 C
ATOM 1445 CD2 PHE A 220 -37.821 35.716 96.833 1.00 36.78 C
ANISOU 1445 CD2 PHE A 220 4059 4623 5292 495 225 249 C
ATOM 1446 CE1 PHE A 220 -36.279 36.837 98.829 1.00 34.81 C
ANISOU 1446 CE1 PHE A 220 3891 4279 5058 564 -37 134 C
ATOM 1447 CE2 PHE A 220 -37.637 35.041 98.034 1.00 33.39 C
ANISOU 1447 CE2 PHE A 220 3823 4146 4718 526 193 209 C
ATOM 1448 CZ PHE A 220 -36.864 35.602 99.030 1.00 31.44 C
ANISOU 1448 CZ PHE A 220 3626 3856 4464 572 48 160 C
ATOM 1449 N ILE A 221 -35.728 35.714 93.492 1.00 41.58 N
ANISOU 1449 N ILE A 221 4318 5320 6161 440 246 419 N
ATOM 1450 CA ILE A 221 -35.047 34.430 93.305 1.00 43.60 C
ANISOU 1450 CA ILE A 221 4584 5593 6387 470 269 408 C
ATOM 1451 C ILE A 221 -33.642 34.623 92.722 1.00 45.47 C
ANISOU 1451 C ILE A 221 4672 5832 6773 458 254 389 C
ATOM 1452 O ILE A 221 -32.673 34.019 93.200 1.00 46.23 O
ANISOU 1452 O ILE A 221 4733 5912 6921 537 179 329 O
ATOM 1453 CB ILE A 221 -35.929 33.503 92.426 1.00 48.66 C
ANISOU 1453 CB ILE A 221 5270 6294 6923 421 400 437 C
ATOM 1454 CG1 ILE A 221 -37.259 33.197 93.144 1.00 51.81 C
ANISOU 1454 CG1 ILE A 221 5789 6693 7202 413 438 405 C
ATOM 1455 CG2 ILE A 221 -35.169 32.249 91.955 1.00 50.30 C
ANISOU 1455 CG2 ILE A 221 5480 6500 7131 440 458 421 C
ATOM 1456 CD1 ILE A 221 -37.958 31.914 92.735 1.00 56.83 C
ANISOU 1456 CD1 ILE A 221 6499 7361 7731 361 568 380 C
ATOM 1457 N VAL A 222 -33.513 35.493 91.710 1.00 47.11 N
ANISOU 1457 N VAL A 222 4795 6052 7052 364 326 432 N
ATOM 1458 CA VAL A 222 -32.276 35.706 90.951 1.00 44.71 C
ANISOU 1458 CA VAL A 222 4349 5751 6885 298 387 400 C
ATOM 1459 C VAL A 222 -31.251 36.567 91.730 1.00 47.23 C
ANISOU 1459 C VAL A 222 4551 6022 7372 297 289 304 C
ATOM 1460 O VAL A 222 -30.055 36.281 91.697 1.00 46.04 O
ANISOU 1460 O VAL A 222 4245 5890 7359 301 280 200 O
ATOM 1461 CB VAL A 222 -32.627 36.309 89.570 1.00 46.16 C
ANISOU 1461 CB VAL A 222 4558 5949 7031 175 525 496 C
ATOM 1462 CG1 VAL A 222 -31.445 37.044 88.917 1.00 47.04 C
ANISOU 1462 CG1 VAL A 222 4562 6023 7288 54 625 464 C
ATOM 1463 CG2 VAL A 222 -33.165 35.221 88.624 1.00 43.64 C
ANISOU 1463 CG2 VAL A 222 4297 5713 6573 157 625 532 C
ATOM 1464 N THR A 223 -31.700 37.622 92.430 1.00 49.47 N
ANISOU 1464 N THR A 223 4888 6248 7662 288 216 308 N
ATOM 1465 CA THR A 223 -30.763 38.467 93.185 1.00 45.99 C
ANISOU 1465 CA THR A 223 4337 5763 7375 263 124 189 C
ATOM 1466 C THR A 223 -30.598 38.057 94.656 1.00 48.56 C
ANISOU 1466 C THR A 223 4691 6105 7655 391 -76 92 C
ATOM 1467 O THR A 223 -29.700 38.586 95.320 1.00 57.81 O
ANISOU 1467 O THR A 223 5747 7272 8947 382 -190 -41 O
ATOM 1468 CB THR A 223 -31.173 39.960 93.128 1.00 45.45 C
ANISOU 1468 CB THR A 223 4319 5592 7360 168 169 222 C
ATOM 1469 OG1 THR A 223 -32.436 40.156 93.774 1.00 46.98 O
ANISOU 1469 OG1 THR A 223 4663 5758 7431 243 114 272 O
ATOM 1470 CG2 THR A 223 -31.253 40.481 91.688 1.00 49.16 C
ANISOU 1470 CG2 THR A 223 4816 6016 7846 47 349 338 C
ATOM 1471 N TYR A 224 -31.412 37.122 95.179 1.00 42.00 N
ANISOU 1471 N TYR A 224 4025 5292 6643 496 -117 145 N
ATOM 1472 CA TYR A 224 -31.326 36.753 96.596 1.00 37.94 C
ANISOU 1472 CA TYR A 224 3617 4772 6027 610 -296 78 C
ATOM 1473 C TYR A 224 -31.391 35.238 96.880 1.00 37.84 C
ANISOU 1473 C TYR A 224 3738 4767 5872 740 -336 116 C
ATOM 1474 O TYR A 224 -30.392 34.659 97.318 1.00 43.55 O
ANISOU 1474 O TYR A 224 4411 5503 6633 858 -491 51 O
ATOM 1475 CB TYR A 224 -32.413 37.487 97.404 1.00 35.81 C
ANISOU 1475 CB TYR A 224 3506 4455 5645 582 -294 82 C
ATOM 1476 CG TYR A 224 -32.226 37.338 98.905 1.00 42.66 C
ANISOU 1476 CG TYR A 224 4509 5314 6386 665 -471 -4 C
ATOM 1477 CD1 TYR A 224 -31.434 38.227 99.630 1.00 43.26 C
ANISOU 1477 CD1 TYR A 224 4501 5390 6547 649 -621 -138 C
ATOM 1478 CD2 TYR A 224 -32.809 36.279 99.589 1.00 41.02 C
ANISOU 1478 CD2 TYR A 224 4536 5094 5956 747 -485 40 C
ATOM 1479 CE1 TYR A 224 -31.243 38.067 101.000 1.00 44.89 C
ANISOU 1479 CE1 TYR A 224 4857 5604 6596 728 -809 -222 C
ATOM 1480 CE2 TYR A 224 -32.623 36.111 100.950 1.00 43.85 C
ANISOU 1480 CE2 TYR A 224 5078 5435 6147 822 -649 -21 C
ATOM 1481 CZ TYR A 224 -31.841 37.004 101.651 1.00 48.80 C
ANISOU 1481 CZ TYR A 224 5621 6083 6839 821 -826 -151 C
ATOM 1482 OH TYR A 224 -31.667 36.825 103.006 1.00 54.66 O
ANISOU 1482 OH TYR A 224 6573 6821 7373 898 -1011 -215 O
ATOM 1483 N LEU A 225 -32.541 34.581 96.644 1.00 35.50 N
ANISOU 1483 N LEU A 225 3609 4456 5424 724 -204 208 N
ATOM 1484 CA LEU A 225 -32.736 33.203 97.112 1.00 39.22 C
ANISOU 1484 CA LEU A 225 4278 4888 5736 826 -216 242 C
ATOM 1485 C LEU A 225 -31.796 32.202 96.421 1.00 43.42 C
ANISOU 1485 C LEU A 225 4713 5423 6363 909 -220 239 C
ATOM 1486 O LEU A 225 -31.066 31.470 97.099 1.00 52.16 O
ANISOU 1486 O LEU A 225 5887 6486 7446 1067 -376 214 O
ATOM 1487 CB LEU A 225 -34.205 32.776 96.954 1.00 38.11 C
ANISOU 1487 CB LEU A 225 4306 4732 5441 745 -34 302 C
ATOM 1488 CG LEU A 225 -34.640 31.531 97.752 1.00 40.29 C
ANISOU 1488 CG LEU A 225 4870 4925 5513 804 -8 328 C
ATOM 1489 CD1 LEU A 225 -34.548 31.750 99.254 1.00 40.40 C
ANISOU 1489 CD1 LEU A 225 5087 4884 5379 871 -152 299 C
ATOM 1490 CD2 LEU A 225 -36.046 31.104 97.389 1.00 47.12 C
ANISOU 1490 CD2 LEU A 225 5831 5793 6278 681 215 342 C
ATOM 1491 N ALA A 226 -31.794 32.134 95.076 1.00 36.46 N
ANISOU 1491 N ALA A 226 3686 4585 5581 818 -57 259 N
ATOM 1492 CA ALA A 226 -30.944 31.150 94.400 1.00 33.70 C
ANISOU 1492 CA ALA A 226 3245 4231 5329 888 -23 229 C
ATOM 1493 C ALA A 226 -29.442 31.361 94.640 1.00 43.94 C
ANISOU 1493 C ALA A 226 4318 5549 6827 992 -186 113 C
ATOM 1494 O ALA A 226 -28.768 30.390 95.018 1.00 46.71 O
ANISOU 1494 O ALA A 226 4689 5854 7205 1170 -300 76 O
ATOM 1495 CB ALA A 226 -31.276 31.084 92.902 1.00 28.88 C
ANISOU 1495 CB ALA A 226 2547 3675 4752 745 201 257 C
ATOM 1496 N PRO A 227 -28.851 32.562 94.466 1.00 44.74 N
ANISOU 1496 N PRO A 227 4203 5708 7087 897 -210 38 N
ATOM 1497 CA PRO A 227 -27.402 32.686 94.744 1.00 48.15 C
ANISOU 1497 CA PRO A 227 4381 6177 7735 986 -366 -121 C
ATOM 1498 C PRO A 227 -26.993 32.326 96.175 1.00 46.51 C
ANISOU 1498 C PRO A 227 4260 5949 7463 1199 -672 -170 C
ATOM 1499 O PRO A 227 -26.003 31.606 96.355 1.00 46.16 O
ANISOU 1499 O PRO A 227 4091 5912 7537 1381 -823 -264 O
ATOM 1500 CB PRO A 227 -27.095 34.162 94.431 1.00 52.81 C
ANISOU 1500 CB PRO A 227 4787 6809 8470 795 -305 -190 C
ATOM 1501 CG PRO A 227 -28.168 34.606 93.543 1.00 47.41 C
ANISOU 1501 CG PRO A 227 4230 6104 7680 629 -80 -50 C
ATOM 1502 CD PRO A 227 -29.405 33.831 93.952 1.00 44.52 C
ANISOU 1502 CD PRO A 227 4142 5702 7071 707 -88 78 C
ATOM 1503 N LEU A 228 -27.713 32.822 97.194 1.00 44.52 N
ANISOU 1503 N LEU A 228 4222 5671 7022 1191 -775 -119 N
ATOM 1504 CA LEU A 228 -27.328 32.572 98.589 1.00 44.50 C
ANISOU 1504 CA LEU A 228 4347 5654 6905 1378 -1077 -164 C
ATOM 1505 C LEU A 228 -27.598 31.136 99.021 1.00 46.12 C
ANISOU 1505 C LEU A 228 4847 5759 6918 1574 -1138 -55 C
ATOM 1506 O LEU A 228 -26.870 30.594 99.860 1.00 53.97 O
ANISOU 1506 O LEU A 228 5900 6732 7873 1800 -1414 -95 O
ATOM 1507 CB LEU A 228 -28.057 33.541 99.527 1.00 43.22 C
ANISOU 1507 CB LEU A 228 4356 5488 6579 1284 -1125 -156 C
ATOM 1508 CG LEU A 228 -27.716 35.029 99.401 1.00 44.82 C
ANISOU 1508 CG LEU A 228 4319 5750 6960 1114 -1111 -280 C
ATOM 1509 CD1 LEU A 228 -28.753 35.862 100.118 1.00 45.66 C
ANISOU 1509 CD1 LEU A 228 4636 5815 6896 1011 -1071 -247 C
ATOM 1510 CD2 LEU A 228 -26.328 35.343 99.946 1.00 52.24 C
ANISOU 1510 CD2 LEU A 228 5008 6772 8071 1197 -1379 -483 C
ATOM 1511 N GLY A 229 -28.655 30.511 98.481 1.00 41.84 N
ANISOU 1511 N GLY A 229 4507 5144 6245 1492 -892 78 N
ATOM 1512 CA GLY A 229 -28.898 29.105 98.764 1.00 43.85 C
ANISOU 1512 CA GLY A 229 5053 5269 6340 1646 -894 173 C
ATOM 1513 C GLY A 229 -27.806 28.215 98.202 1.00 52.83 C
ANISOU 1513 C GLY A 229 6016 6381 7676 1828 -958 115 C
ATOM 1514 O GLY A 229 -27.336 27.292 98.875 1.00 60.79 O
ANISOU 1514 O GLY A 229 7197 7284 8615 2074 -1152 140 O
ATOM 1515 N LEU A 230 -27.373 28.501 96.968 1.00 52.50 N
ANISOU 1515 N LEU A 230 5642 6425 7880 1716 -795 32 N
ATOM 1516 CA LEU A 230 -26.243 27.808 96.353 1.00 53.68 C
ANISOU 1516 CA LEU A 230 5550 6573 8273 1866 -823 -77 C
ATOM 1517 C LEU A 230 -24.940 28.095 97.100 1.00 57.16 C
ANISOU 1517 C LEU A 230 5756 7078 8884 2072 -1161 -230 C
ATOM 1518 O LEU A 230 -24.131 27.184 97.316 1.00 58.78 O
ANISOU 1518 O LEU A 230 5957 7233 9142 2284 -1294 -266 O
ATOM 1519 CB LEU A 230 -26.129 28.221 94.882 1.00 50.86 C
ANISOU 1519 CB LEU A 230 4910 6306 8107 1646 -535 -145 C
ATOM 1520 CG LEU A 230 -27.187 27.647 93.930 1.00 47.20 C
ANISOU 1520 CG LEU A 230 4626 5796 7513 1491 -229 -36 C
ATOM 1521 CD1 LEU A 230 -27.230 28.419 92.620 1.00 47.28 C
ANISOU 1521 CD1 LEU A 230 4419 5918 7628 1241 15 -77 C
ATOM 1522 CD2 LEU A 230 -26.944 26.162 93.666 1.00 48.56 C
ANISOU 1522 CD2 LEU A 230 4900 5842 7709 1658 -176 -42 C
ATOM 1523 N MET A 231 -24.730 29.355 97.495 1.00 57.90 N
ANISOU 1523 N MET A 231 5686 7290 9025 1954 -1263 -316 N
ATOM 1524 CA MET A 231 -23.551 29.739 98.270 1.00 59.99 C
ANISOU 1524 CA MET A 231 5781 7648 9366 2034 -1531 -463 C
ATOM 1525 C MET A 231 -23.514 29.031 99.623 1.00 61.31 C
ANISOU 1525 C MET A 231 6268 7737 9291 2286 -1843 -387 C
ATOM 1526 O MET A 231 -22.464 28.534 100.047 1.00 62.76 O
ANISOU 1526 O MET A 231 6376 7941 9530 2450 -2042 -469 O
ATOM 1527 CB MET A 231 -23.528 31.258 98.462 1.00 58.16 C
ANISOU 1527 CB MET A 231 5369 7525 9202 1827 -1546 -568 C
ATOM 1528 CG MET A 231 -22.967 32.033 97.282 1.00 55.80 C
ANISOU 1528 CG MET A 231 4723 7310 9167 1582 -1291 -696 C
ATOM 1529 SD MET A 231 -22.743 33.782 97.663 1.00 58.27 S
ANISOU 1529 SD MET A 231 4853 7706 9580 1355 -1329 -842 S
ATOM 1530 CE MET A 231 -24.181 34.496 96.872 1.00 54.35 C
ANISOU 1530 CE MET A 231 4493 7140 9019 1127 -1020 -669 C
ATOM 1531 N ALA A 232 -24.653 29.002 100.327 1.00 58.42 N
ANISOU 1531 N ALA A 232 6280 7276 8641 2313 -1884 -236 N
ATOM 1532 CA ALA A 232 -24.740 28.291 101.601 1.00 56.03 C
ANISOU 1532 CA ALA A 232 6380 6869 8039 2519 -2131 -133 C
ATOM 1533 C ALA A 232 -24.288 26.841 101.442 1.00 60.96 C
ANISOU 1533 C ALA A 232 7129 7363 8671 2720 -2137 -63 C
ATOM 1534 O ALA A 232 -23.456 26.350 102.215 1.00 68.37 O
ANISOU 1534 O ALA A 232 8127 8289 9560 2909 -2396 -90 O
ATOM 1535 CB ALA A 232 -26.169 28.359 102.150 1.00 48.13 C
ANISOU 1535 CB ALA A 232 5822 5762 6702 2434 -2025 35 C
ATOM 1536 N MET A 233 -24.806 26.160 100.417 1.00 60.98 N
ANISOU 1536 N MET A 233 7158 7263 8748 2686 -1858 10 N
ATOM 1537 CA MET A 233 -24.456 24.765 100.159 1.00 59.25 C
ANISOU 1537 CA MET A 233 7061 6889 8561 2864 -1822 68 C
ATOM 1538 C MET A 233 -22.984 24.596 99.772 1.00 58.12 C
ANISOU 1538 C MET A 233 6514 6850 8720 2964 -1922 -103 C
ATOM 1539 O MET A 233 -22.380 23.568 100.097 1.00 61.54 O
ANISOU 1539 O MET A 233 7054 7175 9154 3187 -2053 -78 O
ATOM 1540 CB MET A 233 -25.377 24.201 99.074 1.00 57.32 C
ANISOU 1540 CB MET A 233 6913 6523 8342 2776 -1479 141 C
ATOM 1541 CG MET A 233 -26.815 24.041 99.558 1.00 62.09 C
ANISOU 1541 CG MET A 233 7997 6996 8599 2659 -1331 320 C
ATOM 1542 SD MET A 233 -27.940 23.220 98.415 1.00 64.47 S
ANISOU 1542 SD MET A 233 8451 7183 8861 2426 -859 395 S
ATOM 1543 CE MET A 233 -28.229 24.530 97.231 1.00 58.37 C
ANISOU 1543 CE MET A 233 7236 6668 8272 2091 -633 289 C
ATOM 1544 N ALA A 234 -22.403 25.589 99.084 1.00 51.06 N
ANISOU 1544 N ALA A 234 5175 6150 8076 2795 -1845 -281 N
ATOM 1545 CA ALA A 234 -20.986 25.552 98.711 1.00 53.17 C
ANISOU 1545 CA ALA A 234 5051 6527 8623 2852 -1909 -478 C
ATOM 1546 C ALA A 234 -20.083 25.652 99.938 1.00 61.62 C
ANISOU 1546 C ALA A 234 6110 7655 9646 3031 -2297 -557 C
ATOM 1547 O ALA A 234 -19.134 24.871 100.087 1.00 69.19 O
ANISOU 1547 O ALA A 234 6988 8589 10714 3247 -2449 -623 O
ATOM 1548 CB ALA A 234 -20.674 26.689 97.734 1.00 51.52 C
ANISOU 1548 CB ALA A 234 4441 6490 8645 2574 -1696 -645 C
ATOM 1549 N TYR A 235 -20.358 26.625 100.818 1.00 63.51 N
ANISOU 1549 N TYR A 235 6425 7977 9730 2950 -2465 -569 N
ATOM 1550 CA TYR A 235 -19.534 26.819 102.008 1.00 71.14 C
ANISOU 1550 CA TYR A 235 7384 9016 10631 3105 -2843 -669 C
ATOM 1551 C TYR A 235 -19.728 25.702 103.028 1.00 73.90 C
ANISOU 1551 C TYR A 235 8184 9200 10695 3380 -3074 -495 C
ATOM 1552 O TYR A 235 -18.790 25.381 103.764 1.00 80.59 O
ANISOU 1552 O TYR A 235 9001 10075 11544 3593 -3384 -577 O
ATOM 1553 CB TYR A 235 -19.806 28.195 102.641 1.00 67.81 C
ANISOU 1553 CB TYR A 235 6929 8720 10118 2927 -2938 -749 C
ATOM 1554 CG TYR A 235 -19.198 29.327 101.835 1.00 65.04 C
ANISOU 1554 CG TYR A 235 6103 8529 10080 2683 -2782 -972 C
ATOM 1555 CD1 TYR A 235 -17.817 29.485 101.754 1.00 67.65 C
ANISOU 1555 CD1 TYR A 235 6059 8977 10669 2721 -2901 -1215 C
ATOM 1556 CD2 TYR A 235 -19.999 30.214 101.127 1.00 61.82 C
ANISOU 1556 CD2 TYR A 235 5636 8140 9713 2413 -2500 -944 C
ATOM 1557 CE1 TYR A 235 -17.252 30.502 100.996 1.00 69.82 C
ANISOU 1557 CE1 TYR A 235 5940 9371 11220 2470 -2716 -1424 C
ATOM 1558 CE2 TYR A 235 -19.444 31.233 100.367 1.00 66.03 C
ANISOU 1558 CE2 TYR A 235 5790 8785 10514 2172 -2327 -1133 C
ATOM 1559 CZ TYR A 235 -18.070 31.373 100.305 1.00 73.47 C
ANISOU 1559 CZ TYR A 235 6392 9829 11696 2190 -2422 -1372 C
ATOM 1560 OH TYR A 235 -17.515 32.385 99.552 1.00 81.45 O
ANISOU 1560 OH TYR A 235 7065 10924 12958 1927 -2216 -1564 O
ATOM 1561 N PHE A 236 -20.918 25.083 103.079 1.00 67.39 N
ANISOU 1561 N PHE A 236 7793 8192 9621 3377 -2922 -263 N
ATOM 1562 CA PHE A 236 -21.091 23.925 103.956 1.00 70.03 C
ANISOU 1562 CA PHE A 236 8599 8329 9682 3614 -3084 -89 C
ATOM 1563 C PHE A 236 -20.150 22.790 103.544 1.00 76.26 C
ANISOU 1563 C PHE A 236 9258 9035 10681 3847 -3132 -121 C
ATOM 1564 O PHE A 236 -19.560 22.126 104.405 1.00 86.77 O
ANISOU 1564 O PHE A 236 10769 10297 11904 4101 -3421 -93 O
ATOM 1565 CB PHE A 236 -22.554 23.449 103.968 1.00 70.24 C
ANISOU 1565 CB PHE A 236 9112 8154 9422 3523 -2842 143 C
ATOM 1566 CG PHE A 236 -22.785 22.225 104.834 1.00 80.81 C
ANISOU 1566 CG PHE A 236 10988 9255 10461 3721 -2946 327 C
ATOM 1567 CD1 PHE A 236 -22.951 22.345 106.208 1.00 86.22 C
ANISOU 1567 CD1 PHE A 236 12061 9910 10788 3788 -3185 396 C
ATOM 1568 CD2 PHE A 236 -22.798 20.955 104.276 1.00 87.08 C
ANISOU 1568 CD2 PHE A 236 11913 9845 11330 3836 -2795 422 C
ATOM 1569 CE1 PHE A 236 -23.134 21.219 107.006 1.00 90.55 C
ANISOU 1569 CE1 PHE A 236 13131 10227 11045 3957 -3261 566 C
ATOM 1570 CE2 PHE A 236 -22.980 19.827 105.069 1.00 90.09 C
ANISOU 1570 CE2 PHE A 236 12804 9985 11441 4007 -2875 590 C
ATOM 1571 CZ PHE A 236 -23.149 19.960 106.434 1.00 91.58 C
ANISOU 1571 CZ PHE A 236 13389 10145 11261 4064 -3105 667 C
ATOM 1572 N GLN A 237 -19.975 22.590 102.227 1.00 74.03 N
ANISOU 1572 N GLN A 237 8662 8764 10702 3768 -2855 -190 N
ATOM 1573 CA GLN A 237 -19.053 21.582 101.691 1.00 76.13 C
ANISOU 1573 CA GLN A 237 8751 8962 11215 3973 -2858 -255 C
ATOM 1574 C GLN A 237 -17.588 21.957 101.928 1.00 80.21 C
ANISOU 1574 C GLN A 237 8847 9665 11966 4097 -3134 -496 C
ATOM 1575 O GLN A 237 -16.765 21.088 102.242 1.00 86.50 O
ANISOU 1575 O GLN A 237 9640 10390 12836 4379 -3341 -522 O
ATOM 1576 CB GLN A 237 -19.304 21.382 100.190 1.00 73.60 C
ANISOU 1576 CB GLN A 237 8212 8619 11135 3821 -2456 -293 C
ATOM 1577 CG GLN A 237 -20.565 20.596 99.854 1.00 73.83 C
ANISOU 1577 CG GLN A 237 8651 8413 10990 3774 -2191 -83 C
ATOM 1578 CD GLN A 237 -20.475 19.859 98.527 1.00 77.15 C
ANISOU 1578 CD GLN A 237 8909 8747 11658 3762 -1874 -136 C
ATOM 1579 OE1 GLN A 237 -19.819 20.311 97.587 1.00 75.24 O
ANISOU 1579 OE1 GLN A 237 8230 8670 11687 3662 -1738 -326 O
ATOM 1580 NE2 GLN A 237 -21.147 18.717 98.444 1.00 82.14 N
ANISOU 1580 NE2 GLN A 237 9919 9108 12182 3843 -1733 17 N
ATOM 1581 N ILE A 238 -17.247 23.241 101.730 1.00 78.84 N
ANISOU 1581 N ILE A 238 8307 9719 11929 3883 -3121 -687 N
ATOM 1582 CA ILE A 238 -15.914 23.773 102.027 1.00 81.92 C
ANISOU 1582 CA ILE A 238 8297 10296 12533 3949 -3374 -951 C
ATOM 1583 C ILE A 238 -15.604 23.608 103.519 1.00 87.95 C
ANISOU 1583 C ILE A 238 9310 11049 13059 4194 -3819 -919 C
ATOM 1584 O ILE A 238 -14.498 23.197 103.900 1.00 97.95 O
ANISOU 1584 O ILE A 238 10407 12354 14455 4438 -4100 -1054 O
ATOM 1585 CB ILE A 238 -15.832 25.251 101.560 1.00 79.15 C
ANISOU 1585 CB ILE A 238 7594 10149 12332 3618 -3223 -1138 C
ATOM 1586 CG1 ILE A 238 -15.731 25.366 100.022 1.00 78.23 C
ANISOU 1586 CG1 ILE A 238 7163 10064 12498 3406 -2817 -1232 C
ATOM 1587 CG2 ILE A 238 -14.685 26.028 102.227 1.00 81.29 C
ANISOU 1587 CG2 ILE A 238 7548 10605 12734 3647 -3523 -1404 C
ATOM 1588 CD1 ILE A 238 -16.324 26.674 99.419 1.00 73.82 C
ANISOU 1588 CD1 ILE A 238 6480 9606 11962 3036 -2548 -1269 C
ATOM 1589 N PHE A 239 -16.599 23.890 104.375 1.00 84.31 N
ANISOU 1589 N PHE A 239 9272 10529 12234 4138 -3885 -741 N
ATOM 1590 CA PHE A 239 -16.487 23.687 105.821 1.00 91.18 C
ANISOU 1590 CA PHE A 239 10485 11363 12797 4351 -4275 -676 C
ATOM 1591 C PHE A 239 -16.155 22.232 106.157 1.00 95.61 C
ANISOU 1591 C PHE A 239 11318 11726 13284 4693 -4440 -542 C
ATOM 1592 O PHE A 239 -15.249 21.961 106.956 1.00100.72 O
ANISOU 1592 O PHE A 239 11947 12408 13915 4953 -4815 -623 O
ATOM 1593 CB PHE A 239 -17.793 24.112 106.520 1.00 90.49 C
ANISOU 1593 CB PHE A 239 10865 11206 12310 4201 -4219 -486 C
ATOM 1594 CG PHE A 239 -17.889 23.672 107.970 1.00 97.85 C
ANISOU 1594 CG PHE A 239 12289 12042 12848 4412 -4550 -361 C
ATOM 1595 CD1 PHE A 239 -17.245 24.384 108.972 1.00100.53 C
ANISOU 1595 CD1 PHE A 239 12554 12541 13102 4474 -4903 -516 C
ATOM 1596 CD2 PHE A 239 -18.601 22.533 108.326 1.00 99.97 C
ANISOU 1596 CD2 PHE A 239 13108 12050 12826 4539 -4497 -99 C
ATOM 1597 CE1 PHE A 239 -17.310 23.972 110.299 1.00103.09 C
ANISOU 1597 CE1 PHE A 239 13351 12777 13041 4669 -5209 -401 C
ATOM 1598 CE2 PHE A 239 -18.669 22.116 109.653 1.00102.94 C
ANISOU 1598 CE2 PHE A 239 13974 12322 12818 4721 -4779 19 C
ATOM 1599 CZ PHE A 239 -18.022 22.838 110.638 1.00104.16 C
ANISOU 1599 CZ PHE A 239 14055 12647 12874 4791 -5142 -127 C
ATOM 1600 N ARG A 240 -16.899 21.286 105.557 1.00 91.40 N
ANISOU 1600 N ARG A 240 11048 10973 12707 4698 -4163 -339 N
ATOM 1601 CA ARG A 240 -16.680 19.852 105.766 1.00 91.18 C
ANISOU 1601 CA ARG A 240 11308 10712 12626 5003 -4259 -196 C
ATOM 1602 C ARG A 240 -15.302 19.409 105.281 1.00 93.56 C
ANISOU 1602 C ARG A 240 11156 11079 13315 5230 -4395 -395 C
ATOM 1603 O ARG A 240 -14.732 18.453 105.819 1.00100.43 O
ANISOU 1603 O ARG A 240 12190 11819 14152 5559 -4653 -343 O
ATOM 1604 CB ARG A 240 -17.751 19.019 105.035 1.00 86.56 C
ANISOU 1604 CB ARG A 240 11030 9882 11978 4910 -3871 17 C
ATOM 1605 CG ARG A 240 -19.238 19.187 105.451 1.00 86.55 C
ANISOU 1605 CG ARG A 240 11541 9758 11587 4699 -3684 231 C
ATOM 1606 CD ARG A 240 -19.668 18.563 106.797 1.00 95.77 C
ANISOU 1606 CD ARG A 240 13349 10730 12307 4849 -3886 433 C
ATOM 1607 NE ARG A 240 -19.404 17.128 106.927 1.00107.52 N
ANISOU 1607 NE ARG A 240 15133 11953 13768 5120 -3939 565 N
ATOM 1608 CZ ARG A 240 -20.330 16.170 106.895 1.00110.38 C
ANISOU 1608 CZ ARG A 240 15990 12024 13926 5086 -3695 776 C
ATOM 1609 NH1 ARG A 240 -21.612 16.469 106.730 1.00103.66 N
ANISOU 1609 NH1 ARG A 240 15392 11119 12875 4789 -3373 872 N
ATOM 1610 NH2 ARG A 240 -19.967 14.901 107.036 1.00116.93 N
ANISOU 1610 NH2 ARG A 240 17065 12607 14757 5348 -3767 880 N
ATOM 1611 N LYS A 241 -14.772 20.059 104.235 1.00 90.18 N
ANISOU 1611 N LYS A 241 10173 10837 13253 5056 -4205 -625 N
ATOM 1612 CA LYS A 241 -13.461 19.707 103.696 1.00 94.73 C
ANISOU 1612 CA LYS A 241 10285 11490 14217 5234 -4286 -854 C
ATOM 1613 C LYS A 241 -12.332 20.216 104.603 1.00100.66 C
ANISOU 1613 C LYS A 241 10792 12431 15023 5400 -4732 -1073 C
ATOM 1614 O LYS A 241 -11.481 19.430 105.030 1.00105.49 O
ANISOU 1614 O LYS A 241 11381 12989 15712 5743 -5029 -1118 O
ATOM 1615 CB LYS A 241 -13.325 20.249 102.262 1.00 93.19 C
ANISOU 1615 CB LYS A 241 9627 11421 14360 4954 -3891 -1034 C
ATOM 1616 CG LYS A 241 -12.253 19.573 101.396 1.00102.65 C
ANISOU 1616 CG LYS A 241 10433 12621 15949 5109 -3818 -1226 C
ATOM 1617 CD LYS A 241 -12.786 18.339 100.667 1.00106.53 C
ANISOU 1617 CD LYS A 241 11162 12856 16460 5202 -3538 -1045 C
ATOM 1618 CE LYS A 241 -11.727 17.750 99.746 1.00112.90 C
ANISOU 1618 CE LYS A 241 11556 13674 17665 5333 -3430 -1265 C
ATOM 1619 NZ LYS A 241 -12.126 16.399 99.260 1.00115.34 N
ANISOU 1619 NZ LYS A 241 12139 13699 17987 5504 -3229 -1093 N
ATOM 1620 N LEU A 242 -12.352 21.512 104.945 1.00101.84 N
ANISOU 1620 N LEU A 242 10780 12789 15125 5170 -4791 -1209 N
ATOM 1621 CA LEU A 242 -11.287 22.123 105.746 1.00104.65 C
ANISOU 1621 CA LEU A 242 10862 13344 15556 5284 -5187 -1459 C
ATOM 1622 C LEU A 242 -11.356 21.741 107.234 1.00106.98 C
ANISOU 1622 C LEU A 242 11608 13564 15475 5561 -5626 -1315 C
ATOM 1623 O LEU A 242 -10.323 21.717 107.901 1.00112.96 O
ANISOU 1623 O LEU A 242 12188 14426 16306 5801 -6021 -1492 O
ATOM 1624 CB LEU A 242 -11.335 23.650 105.597 1.00101.05 C
ANISOU 1624 CB LEU A 242 10110 13110 15176 4925 -5070 -1654 C
ATOM 1625 CG LEU A 242 -11.048 24.261 104.215 1.00 97.92 C
ANISOU 1625 CG LEU A 242 9228 12823 15156 4628 -4676 -1856 C
ATOM 1626 CD1 LEU A 242 -11.499 25.711 104.179 1.00 94.21 C
ANISOU 1626 CD1 LEU A 242 8657 12492 14648 4261 -4523 -1939 C
ATOM 1627 CD2 LEU A 242 -9.590 24.168 103.796 1.00101.83 C
ANISOU 1627 CD2 LEU A 242 9187 13444 16060 4739 -4771 -2189 C
ATOM 1628 N TRP A 243 -12.551 21.461 107.781 1.00104.30 N
ANISOU 1628 N TRP A 243 11857 13047 14724 5525 -5564 -1010 N
ATOM 1629 CA TRP A 243 -12.683 21.130 109.202 1.00116.84 C
ANISOU 1629 CA TRP A 243 13936 14551 15907 5754 -5944 -864 C
ATOM 1630 C TRP A 243 -13.116 19.681 109.462 1.00118.98 C
ANISOU 1630 C TRP A 243 14744 14510 15954 6013 -5958 -567 C
ATOM 1631 O TRP A 243 -13.401 19.326 110.610 1.00125.76 O
ANISOU 1631 O TRP A 243 16113 15251 16418 6175 -6211 -399 O
ATOM 1632 CB TRP A 243 -13.652 22.094 109.903 1.00104.78 C
ANISOU 1632 CB TRP A 243 12710 13076 14025 5499 -5906 -782 C
ATOM 1633 CG TRP A 243 -13.066 23.461 110.147 1.00107.54 C
ANISOU 1633 CG TRP A 243 12640 13711 14508 5336 -6051 -1074 C
ATOM 1634 CD1 TRP A 243 -12.319 23.855 111.222 1.00110.37 C
ANISOU 1634 CD1 TRP A 243 12957 14212 14766 5491 -6484 -1228 C
ATOM 1635 CD2 TRP A 243 -13.199 24.616 109.308 1.00103.60 C
ANISOU 1635 CD2 TRP A 243 11726 13378 14259 4981 -5754 -1247 C
ATOM 1636 NE1 TRP A 243 -11.967 25.178 111.095 1.00110.67 N
ANISOU 1636 NE1 TRP A 243 12563 14493 14995 5243 -6462 -1500 N
ATOM 1637 CE2 TRP A 243 -12.496 25.669 109.930 1.00104.53 C
ANISOU 1637 CE2 TRP A 243 11562 13723 14432 4927 -6012 -1511 C
ATOM 1638 CE3 TRP A 243 -13.839 24.861 108.089 1.00 98.21 C
ANISOU 1638 CE3 TRP A 243 10894 12667 13753 4704 -5296 -1206 C
ATOM 1639 CZ2 TRP A 243 -12.417 26.946 109.373 1.00100.58 C
ANISOU 1639 CZ2 TRP A 243 10652 13401 14164 4598 -5807 -1729 C
ATOM 1640 CZ3 TRP A 243 -13.758 26.129 107.537 1.00 91.33 C
ANISOU 1640 CZ3 TRP A 243 9626 11977 13099 4391 -5110 -1411 C
ATOM 1641 CH2 TRP A 243 -13.053 27.155 108.179 1.00 94.05 C
ANISOU 1641 CH2 TRP A 243 9710 12525 13500 4335 -5355 -1668 C
ATOM 1642 N GLY A 244 -13.153 18.844 108.428 1.00115.16 N
ANISOU 1642 N GLY A 244 14168 13879 15706 6050 -5682 -507 N
ATOM 1643 CA GLY A 244 -13.503 17.440 108.586 1.00117.86 C
ANISOU 1643 CA GLY A 244 14992 13904 15886 6290 -5666 -245 C
ATOM 1644 C GLY A 244 -12.364 16.559 109.066 1.00129.19 C
ANISOU 1644 C GLY A 244 16390 15274 17422 6733 -6067 -295 C
ATOM 1645 O GLY A 244 -11.195 16.934 108.985 1.00134.10 O
ANISOU 1645 O GLY A 244 16495 16110 18348 6858 -6307 -572 O
ATOM 1646 N GLN A 289 -1.186 25.509 103.924 1.00139.48 N
ANISOU 1646 N GLN A 289 10793 19239 22966 5282 -5933 -4611 N
ATOM 1647 CA GLN A 289 -2.225 25.879 102.970 1.00131.53 C
ANISOU 1647 CA GLN A 289 9987 18127 21861 4898 -5399 -4395 C
ATOM 1648 C GLN A 289 -3.610 25.812 103.621 1.00128.64 C
ANISOU 1648 C GLN A 289 10244 17630 21004 4903 -5448 -3948 C
ATOM 1649 O GLN A 289 -4.427 26.710 103.414 1.00125.12 O
ANISOU 1649 O GLN A 289 9942 17188 20410 4555 -5178 -3845 O
ATOM 1650 CB GLN A 289 -2.165 24.981 101.724 1.00131.31 C
ANISOU 1650 CB GLN A 289 9866 17970 22054 4913 -5046 -4362 C
ATOM 1651 CG GLN A 289 -3.122 25.393 100.600 1.00127.40 C
ANISOU 1651 CG GLN A 289 9521 17389 21497 4503 -4480 -4190 C
ATOM 1652 CD GLN A 289 -3.109 24.443 99.408 1.00129.50 C
ANISOU 1652 CD GLN A 289 9735 17526 21944 4531 -4143 -4148 C
ATOM 1653 OE1 GLN A 289 -2.942 23.231 99.558 1.00127.53 O
ANISOU 1653 OE1 GLN A 289 9584 17164 21708 4900 -4323 -4046 O
ATOM 1654 NE2 GLN A 289 -3.286 24.997 98.213 1.00131.18 N
ANISOU 1654 NE2 GLN A 289 9811 17744 22289 4139 -3646 -4227 N
ATOM 1655 N MET A 290 -3.857 24.762 104.422 1.00133.37 N
ANISOU 1655 N MET A 290 11216 18104 21354 5299 -5792 -3696 N
ATOM 1656 CA MET A 290 -5.164 24.581 105.055 1.00130.62 C
ANISOU 1656 CA MET A 290 11487 17608 20535 5314 -5826 -3280 C
ATOM 1657 C MET A 290 -5.471 25.692 106.059 1.00132.68 C
ANISOU 1657 C MET A 290 11874 17994 20545 5166 -6024 -3304 C
ATOM 1658 O MET A 290 -6.557 26.282 106.029 1.00130.19 O
ANISOU 1658 O MET A 290 11846 17632 19989 4898 -5794 -3104 O
ATOM 1659 CB MET A 290 -5.264 23.200 105.719 1.00137.25 C
ANISOU 1659 CB MET A 290 12714 18266 21168 5769 -6146 -3026 C
ATOM 1660 CG MET A 290 -6.587 22.996 106.469 1.00141.16 C
ANISOU 1660 CG MET A 290 13881 18598 21157 5780 -6184 -2615 C
ATOM 1661 SD MET A 290 -6.929 21.305 106.989 1.00149.32 S
ANISOU 1661 SD MET A 290 15461 19339 21933 6236 -6401 -2260 S
ATOM 1662 CE MET A 290 -7.492 20.640 105.418 1.00144.03 C
ANISOU 1662 CE MET A 290 14758 18496 21469 6075 -5823 -2129 C
ATOM 1663 N ARG A 291 -4.523 25.985 106.960 1.00139.29 N
ANISOU 1663 N ARG A 291 12491 18993 21439 5344 -6456 -3560 N
ATOM 1664 CA ARG A 291 -4.714 27.001 107.998 1.00140.02 C
ANISOU 1664 CA ARG A 291 12692 19214 21294 5232 -6683 -3613 C
ATOM 1665 C ARG A 291 -4.958 28.396 107.408 1.00124.81 C
ANISOU 1665 C ARG A 291 10524 17396 19503 4748 -6305 -3775 C
ATOM 1666 O ARG A 291 -5.696 29.193 107.995 1.00121.79 O
ANISOU 1666 O ARG A 291 10392 17035 18849 4568 -6309 -3673 O
ATOM 1667 CB ARG A 291 -3.492 27.018 108.920 1.00137.79 C
ANISOU 1667 CB ARG A 291 12132 19106 21116 5517 -7206 -3914 C
ATOM 1668 CG ARG A 291 -3.288 25.754 109.753 1.00143.11 C
ANISOU 1668 CG ARG A 291 13119 19671 21585 6021 -7662 -3734 C
ATOM 1669 CD ARG A 291 -2.413 26.038 110.962 1.00150.65 C
ANISOU 1669 CD ARG A 291 13944 20812 22485 6259 -8226 -3968 C
ATOM 1670 NE ARG A 291 -2.128 24.827 111.725 1.00156.58 N
ANISOU 1670 NE ARG A 291 14984 21454 23055 6762 -8681 -3808 N
ATOM 1671 CZ ARG A 291 -1.206 24.750 112.680 1.00164.66 C
ANISOU 1671 CZ ARG A 291 15873 22619 24071 7078 -9227 -4008 C
ATOM 1672 NH1 ARG A 291 -0.993 23.602 113.307 1.00170.11 N
ANISOU 1672 NH1 ARG A 291 16864 23181 24590 7546 -9623 -3832 N
ATOM 1673 NH2 ARG A 291 -0.468 25.811 112.982 1.00167.71 N
ANISOU 1673 NH2 ARG A 291 15816 23273 24635 6931 -9377 -4395 N
ATOM 1674 N ALA A 292 -4.332 28.695 106.258 1.00124.68 N
ANISOU 1674 N ALA A 292 10037 17436 19900 4539 -5973 -4031 N
ATOM 1675 CA ALA A 292 -4.540 29.959 105.543 1.00120.62 C
ANISOU 1675 CA ALA A 292 9313 16986 19531 4072 -5560 -4173 C
ATOM 1676 C ALA A 292 -5.911 30.003 104.874 1.00113.75 C
ANISOU 1676 C ALA A 292 8816 15952 18453 3841 -5152 -3819 C
ATOM 1677 O ALA A 292 -6.578 31.047 104.869 1.00111.78 O
ANISOU 1677 O ALA A 292 8660 15718 18095 3531 -4958 -3779 O
ATOM 1678 CB ALA A 292 -3.443 30.136 104.491 1.00123.49 C
ANISOU 1678 CB ALA A 292 9110 17432 20379 3931 -5313 -4543 C
ATOM 1679 N ARG A 293 -6.313 28.873 104.280 1.00110.83 N
ANISOU 1679 N ARG A 293 8640 15423 18048 3993 -5016 -3580 N
ATOM 1680 CA ARG A 293 -7.616 28.706 103.642 1.00103.92 C
ANISOU 1680 CA ARG A 293 8126 14388 16973 3827 -4659 -3239 C
ATOM 1681 C ARG A 293 -8.750 28.754 104.652 1.00110.76 C
ANISOU 1681 C ARG A 293 9514 15178 17393 3884 -4833 -2934 C
ATOM 1682 O ARG A 293 -9.866 29.174 104.313 1.00111.83 O
ANISOU 1682 O ARG A 293 9891 15239 17362 3649 -4551 -2730 O
ATOM 1683 CB ARG A 293 -7.648 27.373 102.888 1.00103.83 C
ANISOU 1683 CB ARG A 293 8182 14229 17038 4023 -4525 -3090 C
ATOM 1684 CG ARG A 293 -7.073 27.419 101.484 1.00103.66 C
ANISOU 1684 CG ARG A 293 7763 14231 17394 3826 -4132 -3296 C
ATOM 1685 CD ARG A 293 -6.895 26.023 100.915 1.00105.12 C
ANISOU 1685 CD ARG A 293 7977 14286 17678 4084 -4081 -3204 C
ATOM 1686 NE ARG A 293 -6.787 26.033 99.459 1.00103.11 N
ANISOU 1686 NE ARG A 293 7492 14010 17675 3840 -3610 -3300 N
ATOM 1687 CZ ARG A 293 -6.594 24.946 98.718 1.00104.15 C
ANISOU 1687 CZ ARG A 293 7588 14039 17946 3991 -3468 -3273 C
ATOM 1688 NH1 ARG A 293 -6.481 23.759 99.297 1.00107.23 N
ANISOU 1688 NH1 ARG A 293 8156 14321 18265 4398 -3760 -3143 N
ATOM 1689 NH2 ARG A 293 -6.510 25.047 97.399 1.00102.42 N
ANISOU 1689 NH2 ARG A 293 7174 13811 17930 3737 -3028 -3377 N
ATOM 1690 N ARG A 294 -8.501 28.304 105.895 1.00107.96 N
ANISOU 1690 N ARG A 294 9357 14835 16829 4201 -5296 -2899 N
ATOM 1691 CA ARG A 294 -9.488 28.355 106.951 1.00103.95 C
ANISOU 1691 CA ARG A 294 9363 14258 15877 4256 -5477 -2639 C
ATOM 1692 C ARG A 294 -9.696 29.753 107.485 1.00103.99 C
ANISOU 1692 C ARG A 294 9316 14397 15799 3991 -5499 -2771 C
ATOM 1693 O ARG A 294 -10.778 30.086 107.985 1.00102.75 O
ANISOU 1693 O ARG A 294 9549 14177 15314 3892 -5466 -2561 O
ATOM 1694 CB ARG A 294 -9.111 27.440 108.128 1.00110.01 C
ANISOU 1694 CB ARG A 294 10394 14986 16420 4675 -5967 -2562 C
ATOM 1695 CG ARG A 294 -8.949 25.970 107.794 1.00114.90 C
ANISOU 1695 CG ARG A 294 11142 15437 17079 4987 -5997 -2403 C
ATOM 1696 CD ARG A 294 -8.665 25.153 109.048 1.00122.77 C
ANISOU 1696 CD ARG A 294 12470 16372 17805 5394 -6491 -2298 C
ATOM 1697 NE ARG A 294 -8.499 23.742 108.722 1.00125.90 N
ANISOU 1697 NE ARG A 294 13000 16583 18255 5700 -6511 -2145 N
ATOM 1698 CZ ARG A 294 -8.455 22.759 109.613 1.00130.30 C
ANISOU 1698 CZ ARG A 294 13953 17000 18556 6068 -6857 -1964 C
ATOM 1699 NH1 ARG A 294 -8.579 23.017 110.906 1.00131.09 N
ANISOU 1699 NH1 ARG A 294 14376 17133 18299 6175 -7216 -1907 N
ATOM 1700 NH2 ARG A 294 -8.295 21.509 109.201 1.00133.52 N
ANISOU 1700 NH2 ARG A 294 14454 17222 19057 6327 -6831 -1836 N
ATOM 1701 N LYS A 295 -8.635 30.592 107.462 1.00107.19 N
ANISOU 1701 N LYS A 295 9241 14989 16498 3881 -5570 -3141 N
ATOM 1702 CA LYS A 295 -8.708 31.977 107.940 1.00106.43 C
ANISOU 1702 CA LYS A 295 9047 15022 16369 3615 -5579 -3312 C
ATOM 1703 C LYS A 295 -9.429 32.879 106.957 1.00100.71 C
ANISOU 1703 C LYS A 295 8263 14256 15748 3209 -5091 -3277 C
ATOM 1704 O LYS A 295 -9.872 33.982 107.345 1.00 98.71 O
ANISOU 1704 O LYS A 295 8059 14050 15395 2976 -5046 -3324 O
ATOM 1705 CB LYS A 295 -7.293 32.526 108.182 1.00111.49 C
ANISOU 1705 CB LYS A 295 9179 15865 17317 3624 -5791 -3740 C
ATOM 1706 CG LYS A 295 -7.288 33.790 109.053 1.00114.71 C
ANISOU 1706 CG LYS A 295 9551 16412 17623 3437 -5934 -3918 C
ATOM 1707 CD LYS A 295 -5.909 34.420 109.242 1.00121.43 C
ANISOU 1707 CD LYS A 295 9871 17469 18798 3403 -6106 -4373 C
ATOM 1708 CE LYS A 295 -6.040 35.916 109.553 1.00119.33 C
ANISOU 1708 CE LYS A 295 9497 17303 18540 3050 -6003 -4565 C
ATOM 1709 NZ LYS A 295 -6.725 36.213 110.839 1.00118.26 N
ANISOU 1709 NZ LYS A 295 9761 17191 17982 3108 -6299 -4426 N
ATOM 1710 N THR A 296 -9.471 32.510 105.677 1.00 97.27 N
ANISOU 1710 N THR A 296 7690 13738 15530 3109 -4725 -3230 N
ATOM 1711 CA THR A 296 -10.129 33.201 104.611 1.00 94.31 C
ANISOU 1711 CA THR A 296 7278 13305 15251 2756 -4256 -3171 C
ATOM 1712 C THR A 296 -11.528 32.665 104.321 1.00 90.82 C
ANISOU 1712 C THR A 296 7276 12696 14536 2759 -4071 -2783 C
ATOM 1713 O THR A 296 -12.463 33.440 104.079 1.00 88.10 O
ANISOU 1713 O THR A 296 7070 12310 14095 2508 -3837 -2673 O
ATOM 1714 CB THR A 296 -9.179 33.203 103.369 1.00 99.98 C
ANISOU 1714 CB THR A 296 7549 14056 16383 2622 -3967 -3407 C
ATOM 1715 OG1 THR A 296 -9.648 34.053 102.319 1.00107.72 O
ANISOU 1715 OG1 THR A 296 8464 14991 17473 2246 -3507 -3396 O
ATOM 1716 CG2 THR A 296 -8.851 31.808 102.849 1.00 98.43 C
ANISOU 1716 CG2 THR A 296 7341 13788 16271 2886 -3976 -3325 C
ATOM 1717 N ALA A 297 -11.738 31.333 104.442 1.00 91.31 N
ANISOU 1717 N ALA A 297 7588 12652 14454 3056 -4194 -2571 N
ATOM 1718 CA ALA A 297 -13.072 30.790 104.331 1.00 86.27 C
ANISOU 1718 CA ALA A 297 7392 11853 13533 3074 -4050 -2219 C
ATOM 1719 C ALA A 297 -13.954 31.298 105.456 1.00 87.78 C
ANISOU 1719 C ALA A 297 7951 12033 13367 3059 -4230 -2090 C
ATOM 1720 O ALA A 297 -15.098 31.713 105.236 1.00 87.97 O
ANISOU 1720 O ALA A 297 8195 11987 13242 2877 -4008 -1920 O
ATOM 1721 CB ALA A 297 -13.047 29.251 104.332 1.00 83.20 C
ANISOU 1721 CB ALA A 297 7216 11335 13063 3398 -4155 -2038 C
ATOM 1722 N LYS A 298 -13.408 31.328 106.685 1.00 89.54 N
ANISOU 1722 N LYS A 298 8235 12335 13452 3246 -4639 -2191 N
ATOM 1723 CA LYS A 298 -14.114 31.832 107.848 1.00 90.13 C
ANISOU 1723 CA LYS A 298 8659 12415 13173 3235 -4835 -2107 C
ATOM 1724 C LYS A 298 -14.610 33.246 107.610 1.00 91.13 C
ANISOU 1724 C LYS A 298 8658 12604 13363 2881 -4611 -2207 C
ATOM 1725 O LYS A 298 -15.765 33.585 107.908 1.00 94.65 O
ANISOU 1725 O LYS A 298 9431 12979 13551 2777 -4527 -2037 O
ATOM 1726 CB LYS A 298 -13.197 31.805 109.071 1.00 97.93 C
ANISOU 1726 CB LYS A 298 9624 13517 14067 3456 -5302 -2274 C
ATOM 1727 CG LYS A 298 -13.871 32.020 110.429 1.00100.03 C
ANISOU 1727 CG LYS A 298 10347 13771 13888 3516 -5559 -2157 C
ATOM 1728 CD LYS A 298 -12.814 32.161 111.528 1.00108.96 C
ANISOU 1728 CD LYS A 298 11370 15055 14976 3700 -6015 -2376 C
ATOM 1729 CE LYS A 298 -13.419 32.436 112.899 1.00109.34 C
ANISOU 1729 CE LYS A 298 11876 15106 14560 3736 -6269 -2281 C
ATOM 1730 NZ LYS A 298 -12.356 32.607 113.932 1.00113.00 N
ANISOU 1730 NZ LYS A 298 12213 15738 14984 3908 -6722 -2508 N
ATOM 1731 N MET A 299 -13.728 34.115 107.104 1.00 88.73 N
ANISOU 1731 N MET A 299 7885 12424 13404 2689 -4511 -2501 N
ATOM 1732 CA MET A 299 -14.096 35.482 106.792 1.00 83.48 C
ANISOU 1732 CA MET A 299 7081 11796 12843 2341 -4271 -2612 C
ATOM 1733 C MET A 299 -15.192 35.516 105.749 1.00 81.35 C
ANISOU 1733 C MET A 299 6939 11394 12577 2162 -3869 -2390 C
ATOM 1734 O MET A 299 -16.187 36.244 105.889 1.00 80.53 O
ANISOU 1734 O MET A 299 7018 11246 12332 1991 -3755 -2301 O
ATOM 1735 CB MET A 299 -12.885 36.265 106.308 1.00 82.51 C
ANISOU 1735 CB MET A 299 6448 11795 13108 2164 -4184 -2961 C
ATOM 1736 CG MET A 299 -13.195 37.694 105.942 1.00 80.26 C
ANISOU 1736 CG MET A 299 6030 11515 12948 1789 -3905 -3081 C
ATOM 1737 SD MET A 299 -11.719 38.528 105.356 1.00 85.46 S
ANISOU 1737 SD MET A 299 6126 12291 14056 1571 -3765 -3497 S
ATOM 1738 CE MET A 299 -11.469 37.722 103.784 1.00 84.15 C
ANISOU 1738 CE MET A 299 5802 12039 14131 1555 -3406 -3416 C
ATOM 1739 N LEU A 300 -15.037 34.699 104.696 1.00 78.59 N
ANISOU 1739 N LEU A 300 6496 10981 12385 2209 -3659 -2303 N
ATOM 1740 CA LEU A 300 -15.971 34.669 103.591 1.00 72.12 C
ANISOU 1740 CA LEU A 300 5761 10051 11589 2044 -3274 -2109 C
ATOM 1741 C LEU A 300 -17.369 34.257 104.022 1.00 69.64 C
ANISOU 1741 C LEU A 300 5908 9624 10930 2126 -3292 -1811 C
ATOM 1742 O LEU A 300 -18.364 34.857 103.581 1.00 66.15 O
ANISOU 1742 O LEU A 300 5558 9125 10450 1930 -3053 -1705 O
ATOM 1743 CB LEU A 300 -15.469 33.733 102.481 1.00 73.68 C
ANISOU 1743 CB LEU A 300 5796 10211 11988 2109 -3082 -2087 C
ATOM 1744 CG LEU A 300 -14.330 34.296 101.637 1.00 73.86 C
ANISOU 1744 CG LEU A 300 5367 10318 12380 1923 -2897 -2369 C
ATOM 1745 CD1 LEU A 300 -14.226 33.529 100.332 1.00 77.85 C
ANISOU 1745 CD1 LEU A 300 5783 10760 13038 1907 -2597 -2304 C
ATOM 1746 CD2 LEU A 300 -14.583 35.760 101.389 1.00 68.58 C
ANISOU 1746 CD2 LEU A 300 4593 9668 11797 1582 -2683 -2471 C
ATOM 1747 N MET A 301 -17.483 33.263 104.913 1.00 70.52 N
ANISOU 1747 N MET A 301 6330 9688 10778 2413 -3572 -1678 N
ATOM 1748 CA MET A 301 -18.791 32.825 105.385 1.00 71.82 C
ANISOU 1748 CA MET A 301 6972 9726 10588 2485 -3575 -1406 C
ATOM 1749 C MET A 301 -19.505 33.904 106.184 1.00 74.16 C
ANISOU 1749 C MET A 301 7429 10057 10693 2342 -3648 -1435 C
ATOM 1750 O MET A 301 -20.742 33.952 106.200 1.00 77.27 O
ANISOU 1750 O MET A 301 8120 10358 10883 2284 -3519 -1254 O
ATOM 1751 CB MET A 301 -18.664 31.575 106.257 1.00 75.34 C
ANISOU 1751 CB MET A 301 7760 10094 10773 2807 -3855 -1269 C
ATOM 1752 CG MET A 301 -18.028 30.399 105.555 1.00 83.13 C
ANISOU 1752 CG MET A 301 8631 11021 11933 2981 -3804 -1232 C
ATOM 1753 SD MET A 301 -18.046 28.895 106.542 1.00 91.52 S
ANISOU 1753 SD MET A 301 10167 11932 12673 3352 -4093 -1029 S
ATOM 1754 CE MET A 301 -16.989 27.844 105.554 1.00 93.17 C
ANISOU 1754 CE MET A 301 10056 12116 13228 3519 -4029 -1097 C
ATOM 1755 N VAL A 302 -18.748 34.748 106.909 1.00 75.26 N
ANISOU 1755 N VAL A 302 7387 10326 10882 2294 -3865 -1676 N
ATOM 1756 CA VAL A 302 -19.327 35.853 107.649 1.00 74.66 C
ANISOU 1756 CA VAL A 302 7427 10289 10651 2135 -3927 -1751 C
ATOM 1757 C VAL A 302 -19.844 36.930 106.706 1.00 71.43 C
ANISOU 1757 C VAL A 302 6800 9863 10476 1825 -3587 -1803 C
ATOM 1758 O VAL A 302 -20.952 37.459 106.893 1.00 68.93 O
ANISOU 1758 O VAL A 302 6696 9490 10003 1713 -3505 -1721 O
ATOM 1759 CB VAL A 302 -18.285 36.426 108.649 1.00 76.56 C
ANISOU 1759 CB VAL A 302 7513 10678 10900 2161 -4246 -2018 C
ATOM 1760 CG1 VAL A 302 -18.560 37.893 108.964 1.00 76.12 C
ANISOU 1760 CG1 VAL A 302 7366 10682 10876 1885 -4195 -2204 C
ATOM 1761 CG2 VAL A 302 -18.302 35.628 109.959 1.00 76.84 C
ANISOU 1761 CG2 VAL A 302 7956 10703 10538 2436 -4609 -1914 C
ATOM 1762 N VAL A 303 -19.089 37.231 105.643 1.00 68.71 N
ANISOU 1762 N VAL A 303 6055 9551 10499 1682 -3367 -1930 N
ATOM 1763 CA VAL A 303 -19.510 38.222 104.647 1.00 62.61 C
ANISOU 1763 CA VAL A 303 5100 8735 9953 1380 -3011 -1959 C
ATOM 1764 C VAL A 303 -20.819 37.790 103.982 1.00 58.11 C
ANISOU 1764 C VAL A 303 4766 8041 9273 1379 -2784 -1679 C
ATOM 1765 O VAL A 303 -21.737 38.606 103.813 1.00 59.22 O
ANISOU 1765 O VAL A 303 4965 8123 9412 1204 -2629 -1641 O
ATOM 1766 CB VAL A 303 -18.377 38.462 103.623 1.00 61.18 C
ANISOU 1766 CB VAL A 303 4512 8596 10138 1239 -2803 -2133 C
ATOM 1767 CG1 VAL A 303 -18.850 39.305 102.434 1.00 56.97 C
ANISOU 1767 CG1 VAL A 303 3867 7979 9802 937 -2389 -2101 C
ATOM 1768 CG2 VAL A 303 -17.169 39.143 104.285 1.00 66.83 C
ANISOU 1768 CG2 VAL A 303 4965 9436 10991 1189 -2996 -2451 C
ATOM 1769 N VAL A 304 -20.942 36.504 103.623 1.00 58.00 N
ANISOU 1769 N VAL A 304 4890 7975 9174 1576 -2764 -1492 N
ATOM 1770 CA VAL A 304 -22.162 35.982 103.000 1.00 55.88 C
ANISOU 1770 CA VAL A 304 4848 7590 8794 1587 -2549 -1237 C
ATOM 1771 C VAL A 304 -23.324 35.950 104.006 1.00 61.12 C
ANISOU 1771 C VAL A 304 5929 8192 9103 1667 -2685 -1100 C
ATOM 1772 O VAL A 304 -24.466 36.271 103.655 1.00 65.04 O
ANISOU 1772 O VAL A 304 6634 8589 9489 1492 -2377 -942 O
ATOM 1773 CB VAL A 304 -21.891 34.594 102.369 1.00 53.16 C
ANISOU 1773 CB VAL A 304 4541 7196 8461 1760 -2478 -1108 C
ATOM 1774 CG1 VAL A 304 -23.179 33.911 101.884 1.00 49.68 C
ANISOU 1774 CG1 VAL A 304 4383 6630 7864 1797 -2286 -853 C
ATOM 1775 CG2 VAL A 304 -20.910 34.714 101.201 1.00 58.85 C
ANISOU 1775 CG2 VAL A 304 4878 7968 9515 1630 -2262 -1242 C
ATOM 1776 N LEU A 305 -23.049 35.595 105.273 1.00 61.16 N
ANISOU 1776 N LEU A 305 6156 8229 8853 1853 -3029 -1131 N
ATOM 1777 CA LEU A 305 -24.092 35.579 106.303 1.00 63.78 C
ANISOU 1777 CA LEU A 305 6970 8488 8777 1869 -3082 -1001 C
ATOM 1778 C LEU A 305 -24.632 36.986 106.589 1.00 66.67 C
ANISOU 1778 C LEU A 305 7336 8861 9134 1587 -2927 -1105 C
ATOM 1779 O LEU A 305 -25.847 37.181 106.680 1.00 67.66 O
ANISOU 1779 O LEU A 305 7759 8882 9067 1458 -2672 -964 O
ATOM 1780 CB LEU A 305 -23.567 34.923 107.590 1.00 67.24 C
ANISOU 1780 CB LEU A 305 7663 8959 8927 2130 -3500 -1020 C
ATOM 1781 CG LEU A 305 -24.444 34.975 108.856 1.00 69.55 C
ANISOU 1781 CG LEU A 305 8483 9195 8747 2140 -3604 -935 C
ATOM 1782 CD1 LEU A 305 -25.744 34.176 108.707 1.00 64.80 C
ANISOU 1782 CD1 LEU A 305 8328 8408 7885 2109 -3281 -650 C
ATOM 1783 CD2 LEU A 305 -23.678 34.540 110.108 1.00 72.22 C
ANISOU 1783 CD2 LEU A 305 9028 9580 8832 2341 -3983 -987 C
ATOM 1784 N VAL A 306 -23.735 37.979 106.718 1.00 67.72 N
ANISOU 1784 N VAL A 306 7120 9110 9499 1484 -3066 -1375 N
ATOM 1785 CA VAL A 306 -24.147 39.364 106.961 1.00 66.70 C
ANISOU 1785 CA VAL A 306 6979 8962 9402 1216 -2913 -1499 C
ATOM 1786 C VAL A 306 -24.892 39.933 105.740 1.00 63.73 C
ANISOU 1786 C VAL A 306 6521 8466 9227 992 -2461 -1380 C
ATOM 1787 O VAL A 306 -25.869 40.674 105.895 1.00 66.33 O
ANISOU 1787 O VAL A 306 7041 8698 9463 836 -2252 -1333 O
ATOM 1788 CB VAL A 306 -22.923 40.219 107.378 1.00 63.72 C
ANISOU 1788 CB VAL A 306 6239 8731 9242 1149 -3172 -1844 C
ATOM 1789 CG1 VAL A 306 -23.235 41.722 107.422 1.00 62.81 C
ANISOU 1789 CG1 VAL A 306 6063 8559 9243 840 -2959 -1994 C
ATOM 1790 CG2 VAL A 306 -22.402 39.783 108.758 1.00 64.56 C
ANISOU 1790 CG2 VAL A 306 6508 8961 9062 1372 -3657 -1958 C
ATOM 1791 N PHE A 307 -24.476 39.559 104.518 1.00 56.86 N
ANISOU 1791 N PHE A 307 5389 7597 8619 989 -2311 -1328 N
ATOM 1792 CA PHE A 307 -25.206 39.955 103.307 1.00 49.90 C
ANISOU 1792 CA PHE A 307 4485 6605 7871 809 -1912 -1181 C
ATOM 1793 C PHE A 307 -26.631 39.396 103.325 1.00 54.33 C
ANISOU 1793 C PHE A 307 5425 7065 8154 852 -1744 -926 C
ATOM 1794 O PHE A 307 -27.605 40.131 103.121 1.00 57.26 O
ANISOU 1794 O PHE A 307 5912 7344 8499 707 -1515 -858 O
ATOM 1795 CB PHE A 307 -24.456 39.484 102.046 1.00 46.83 C
ANISOU 1795 CB PHE A 307 3788 6249 7757 810 -1795 -1178 C
ATOM 1796 CG PHE A 307 -25.002 40.043 100.733 1.00 50.93 C
ANISOU 1796 CG PHE A 307 4266 6668 8416 603 -1410 -1058 C
ATOM 1797 CD1 PHE A 307 -26.064 39.434 100.074 1.00 53.56 C
ANISOU 1797 CD1 PHE A 307 4817 6929 8603 632 -1209 -810 C
ATOM 1798 CD2 PHE A 307 -24.430 41.170 100.153 1.00 53.25 C
ANISOU 1798 CD2 PHE A 307 4317 6936 8979 375 -1255 -1200 C
ATOM 1799 CE1 PHE A 307 -26.557 39.953 98.877 1.00 51.19 C
ANISOU 1799 CE1 PHE A 307 4499 6551 8401 465 -905 -698 C
ATOM 1800 CE2 PHE A 307 -24.918 41.690 98.957 1.00 51.64 C
ANISOU 1800 CE2 PHE A 307 4137 6621 8863 200 -921 -1065 C
ATOM 1801 CZ PHE A 307 -25.982 41.082 98.321 1.00 47.78 C
ANISOU 1801 CZ PHE A 307 3869 6079 8205 260 -768 -810 C
ATOM 1802 N ALA A 308 -26.758 38.092 103.599 1.00 49.63 N
ANISOU 1802 N ALA A 308 5021 6478 7359 1056 -1858 -802 N
ATOM 1803 CA ALA A 308 -28.068 37.451 103.697 1.00 45.73 C
ANISOU 1803 CA ALA A 308 4885 5892 6600 1079 -1690 -594 C
ATOM 1804 C ALA A 308 -28.960 38.148 104.729 1.00 51.40 C
ANISOU 1804 C ALA A 308 5870 6566 7095 991 -1664 -625 C
ATOM 1805 O ALA A 308 -30.142 38.392 104.464 1.00 49.44 O
ANISOU 1805 O ALA A 308 5754 6242 6790 885 -1405 -531 O
ATOM 1806 CB ALA A 308 -27.892 35.967 104.034 1.00 39.42 C
ANISOU 1806 CB ALA A 308 4286 5080 5610 1309 -1845 -487 C
ATOM 1807 N LEU A 309 -28.399 38.495 105.897 1.00 55.35 N
ANISOU 1807 N LEU A 309 6433 7121 7476 1034 -1932 -781 N
ATOM 1808 CA LEU A 309 -29.165 39.152 106.961 1.00 54.39 C
ANISOU 1808 CA LEU A 309 6579 6962 7124 943 -1906 -845 C
ATOM 1809 C LEU A 309 -29.566 40.586 106.583 1.00 53.59 C
ANISOU 1809 C LEU A 309 6312 6809 7240 729 -1691 -945 C
ATOM 1810 O LEU A 309 -30.719 40.984 106.779 1.00 60.11 O
ANISOU 1810 O LEU A 309 7321 7551 7967 640 -1475 -909 O
ATOM 1811 CB LEU A 309 -28.358 39.145 108.266 1.00 57.17 C
ANISOU 1811 CB LEU A 309 7043 7402 7275 1045 -2278 -1003 C
ATOM 1812 CG LEU A 309 -28.202 37.802 108.992 1.00 61.11 C
ANISOU 1812 CG LEU A 309 7869 7906 7444 1278 -2512 -884 C
ATOM 1813 CD1 LEU A 309 -26.979 37.804 109.899 1.00 63.15 C
ANISOU 1813 CD1 LEU A 309 8079 8292 7623 1431 -2971 -1058 C
ATOM 1814 CD2 LEU A 309 -29.452 37.449 109.790 1.00 62.10 C
ANISOU 1814 CD2 LEU A 309 8489 7929 7178 1235 -2342 -767 C
ATOM 1815 N CYS A 310 -28.617 41.369 106.042 1.00 51.05 N
ANISOU 1815 N CYS A 310 5646 6522 7226 647 -1735 -1082 N
ATOM 1816 CA CYS A 310 -28.854 42.777 105.697 1.00 56.36 C
ANISOU 1816 CA CYS A 310 6190 7107 8117 446 -1542 -1180 C
ATOM 1817 C CYS A 310 -29.893 42.947 104.592 1.00 58.21 C
ANISOU 1817 C CYS A 310 6439 7225 8452 385 -1217 -990 C
ATOM 1818 O CYS A 310 -30.631 43.938 104.567 1.00 65.11 O
ANISOU 1818 O CYS A 310 7364 7986 9388 277 -1042 -1014 O
ATOM 1819 CB CYS A 310 -27.546 43.435 105.252 1.00 60.69 C
ANISOU 1819 CB CYS A 310 6377 7703 8979 351 -1624 -1362 C
ATOM 1820 SG CYS A 310 -26.439 43.914 106.584 1.00 71.17 S
ANISOU 1820 SG CYS A 310 7617 9156 10267 338 -1983 -1691 S
ATOM 1821 N TYR A 311 -29.912 42.018 103.633 1.00 50.50 N
ANISOU 1821 N TYR A 311 5405 6274 7509 460 -1147 -818 N
ATOM 1822 CA TYR A 311 -30.784 42.079 102.467 1.00 40.28 C
ANISOU 1822 CA TYR A 311 4102 4902 6299 415 -883 -644 C
ATOM 1823 C TYR A 311 -32.090 41.311 102.648 1.00 41.78 C
ANISOU 1823 C TYR A 311 4538 5077 6261 485 -776 -506 C
ATOM 1824 O TYR A 311 -32.981 41.442 101.799 1.00 42.11 O
ANISOU 1824 O TYR A 311 4574 5068 6358 452 -579 -391 O
ATOM 1825 CB TYR A 311 -30.034 41.547 101.233 1.00 34.77 C
ANISOU 1825 CB TYR A 311 3190 4248 5771 422 -843 -567 C
ATOM 1826 CG TYR A 311 -29.051 42.544 100.662 1.00 41.21 C
ANISOU 1826 CG TYR A 311 3753 5038 6868 279 -804 -686 C
ATOM 1827 CD1 TYR A 311 -27.791 42.730 101.224 1.00 44.80 C
ANISOU 1827 CD1 TYR A 311 4018 5571 7434 261 -998 -900 C
ATOM 1828 CD2 TYR A 311 -29.406 43.334 99.578 1.00 45.02 C
ANISOU 1828 CD2 TYR A 311 4199 5409 7497 153 -571 -596 C
ATOM 1829 CE1 TYR A 311 -26.906 43.667 100.700 1.00 42.41 C
ANISOU 1829 CE1 TYR A 311 3473 5235 7407 86 -918 -1041 C
ATOM 1830 CE2 TYR A 311 -28.534 44.268 99.051 1.00 50.73 C
ANISOU 1830 CE2 TYR A 311 4741 6072 8462 -12 -487 -700 C
ATOM 1831 CZ TYR A 311 -27.286 44.432 99.612 1.00 52.73 C
ANISOU 1831 CZ TYR A 311 4787 6403 8846 -62 -640 -933 C
ATOM 1832 OH TYR A 311 -26.424 45.366 99.079 1.00 65.04 O
ANISOU 1832 OH TYR A 311 6154 7894 10662 -266 -514 -1065 O
ATOM 1833 N LEU A 312 -32.243 40.554 103.751 1.00 42.40 N
ANISOU 1833 N LEU A 312 4840 5193 6077 570 -896 -527 N
ATOM 1834 CA LEU A 312 -33.483 39.806 103.955 1.00 44.85 C
ANISOU 1834 CA LEU A 312 5392 5477 6174 596 -748 -423 C
ATOM 1835 C LEU A 312 -34.681 40.726 104.198 1.00 44.40 C
ANISOU 1835 C LEU A 312 5400 5347 6124 502 -557 -478 C
ATOM 1836 O LEU A 312 -35.697 40.556 103.516 1.00 44.38 O
ANISOU 1836 O LEU A 312 5386 5322 6156 486 -366 -390 O
ATOM 1837 CB LEU A 312 -33.323 38.776 105.082 1.00 49.09 C
ANISOU 1837 CB LEU A 312 6211 6038 6404 694 -897 -421 C
ATOM 1838 CG LEU A 312 -34.543 37.864 105.339 1.00 49.52 C
ANISOU 1838 CG LEU A 312 6548 6046 6220 688 -706 -325 C
ATOM 1839 CD1 LEU A 312 -34.773 36.845 104.223 1.00 46.62 C
ANISOU 1839 CD1 LEU A 312 6117 5680 5917 723 -587 -173 C
ATOM 1840 CD2 LEU A 312 -34.428 37.138 106.666 1.00 53.48 C
ANISOU 1840 CD2 LEU A 312 7415 6530 6375 754 -835 -337 C
ATOM 1841 N PRO A 313 -34.628 41.697 105.128 1.00 42.06 N
ANISOU 1841 N PRO A 313 5158 5015 5809 444 -603 -640 N
ATOM 1842 CA PRO A 313 -35.838 42.519 105.356 1.00 38.33 C
ANISOU 1842 CA PRO A 313 4742 4459 5365 376 -400 -709 C
ATOM 1843 C PRO A 313 -36.386 43.198 104.099 1.00 44.34 C
ANISOU 1843 C PRO A 313 5302 5151 6394 362 -246 -629 C
ATOM 1844 O PRO A 313 -37.595 43.108 103.853 1.00 47.04 O
ANISOU 1844 O PRO A 313 5668 5473 6733 374 -77 -597 O
ATOM 1845 CB PRO A 313 -35.374 43.531 106.419 1.00 37.37 C
ANISOU 1845 CB PRO A 313 4671 4302 5226 311 -498 -916 C
ATOM 1846 CG PRO A 313 -34.285 42.841 107.142 1.00 37.78 C
ANISOU 1846 CG PRO A 313 4814 4453 5087 362 -759 -949 C
ATOM 1847 CD PRO A 313 -33.556 42.048 106.074 1.00 40.36 C
ANISOU 1847 CD PRO A 313 4962 4839 5535 442 -840 -794 C
ATOM 1848 N ILE A 314 -35.538 43.857 103.292 1.00 48.61 N
ANISOU 1848 N ILE A 314 5654 5656 7160 336 -301 -602 N
ATOM 1849 CA ILE A 314 -36.027 44.586 102.113 1.00 45.97 C
ANISOU 1849 CA ILE A 314 5194 5229 7043 330 -169 -506 C
ATOM 1850 C ILE A 314 -36.545 43.619 101.040 1.00 45.57 C
ANISOU 1850 C ILE A 314 5104 5253 6959 389 -102 -326 C
ATOM 1851 O ILE A 314 -37.582 43.871 100.416 1.00 49.43 O
ANISOU 1851 O ILE A 314 5568 5705 7508 424 10 -262 O
ATOM 1852 CB ILE A 314 -34.949 45.559 101.573 1.00 43.26 C
ANISOU 1852 CB ILE A 314 4714 4802 6923 250 -206 -530 C
ATOM 1853 CG1 ILE A 314 -35.570 46.577 100.595 1.00 40.57 C
ANISOU 1853 CG1 ILE A 314 4340 4302 6773 247 -66 -439 C
ATOM 1854 CG2 ILE A 314 -33.754 44.807 100.911 1.00 36.01 C
ANISOU 1854 CG2 ILE A 314 3665 3985 6031 236 -296 -464 C
ATOM 1855 CD1 ILE A 314 -36.813 47.344 101.151 1.00 51.79 C
ANISOU 1855 CD1 ILE A 314 5850 5609 8220 297 27 -519 C
ATOM 1856 N SER A 315 -35.842 42.492 100.832 1.00 45.52 N
ANISOU 1856 N SER A 315 5087 5351 6858 410 -180 -259 N
ATOM 1857 CA SER A 315 -36.248 41.476 99.851 1.00 47.72 C
ANISOU 1857 CA SER A 315 5340 5701 7091 448 -111 -113 C
ATOM 1858 C SER A 315 -37.621 40.892 100.176 1.00 52.20 C
ANISOU 1858 C SER A 315 6020 6296 7518 471 4 -118 C
ATOM 1859 O SER A 315 -38.466 40.723 99.288 1.00 49.35 O
ANISOU 1859 O SER A 315 5596 5961 7195 484 101 -45 O
ATOM 1860 CB SER A 315 -35.195 40.368 99.757 1.00 43.54 C
ANISOU 1860 CB SER A 315 4794 5252 6496 479 -214 -77 C
ATOM 1861 OG SER A 315 -33.961 40.863 99.264 1.00 45.98 O
ANISOU 1861 OG SER A 315 4939 5555 6977 441 -284 -97 O
ATOM 1862 N VAL A 316 -37.838 40.542 101.451 1.00 54.19 N
ANISOU 1862 N VAL A 316 6445 6550 7593 466 -3 -217 N
ATOM 1863 CA VAL A 316 -39.140 40.049 101.908 1.00 48.77 C
ANISOU 1863 CA VAL A 316 5876 5878 6776 446 155 -265 C
ATOM 1864 C VAL A 316 -40.200 41.149 101.786 1.00 51.81 C
ANISOU 1864 C VAL A 316 6158 6212 7315 442 267 -348 C
ATOM 1865 O VAL A 316 -41.294 40.910 101.258 1.00 52.87 O
ANISOU 1865 O VAL A 316 6216 6384 7487 450 389 -347 O
ATOM 1866 CB VAL A 316 -39.032 39.492 103.343 1.00 41.01 C
ANISOU 1866 CB VAL A 316 5157 4887 5536 422 138 -350 C
ATOM 1867 CG1 VAL A 316 -40.410 39.154 103.929 1.00 41.27 C
ANISOU 1867 CG1 VAL A 316 5323 4915 5442 355 362 -442 C
ATOM 1868 CG2 VAL A 316 -38.141 38.242 103.383 1.00 37.57 C
ANISOU 1868 CG2 VAL A 316 4842 4485 4947 473 19 -247 C
ATOM 1869 N LEU A 317 -39.887 42.375 102.242 1.00 50.90 N
ANISOU 1869 N LEU A 317 6023 6006 7310 437 220 -438 N
ATOM 1870 CA LEU A 317 -40.853 43.475 102.172 1.00 48.46 C
ANISOU 1870 CA LEU A 317 5628 5613 7173 464 319 -526 C
ATOM 1871 C LEU A 317 -41.286 43.772 100.738 1.00 47.77 C
ANISOU 1871 C LEU A 317 5367 5518 7266 540 320 -394 C
ATOM 1872 O LEU A 317 -42.447 44.122 100.504 1.00 53.15 O
ANISOU 1872 O LEU A 317 5962 6187 8047 603 402 -446 O
ATOM 1873 CB LEU A 317 -40.298 44.748 102.835 1.00 50.53 C
ANISOU 1873 CB LEU A 317 5917 5747 7535 439 269 -643 C
ATOM 1874 CG LEU A 317 -40.321 44.867 104.372 1.00 52.53 C
ANISOU 1874 CG LEU A 317 6347 5987 7624 370 300 -841 C
ATOM 1875 CD1 LEU A 317 -39.785 46.212 104.829 1.00 54.56 C
ANISOU 1875 CD1 LEU A 317 6599 6112 8020 335 255 -970 C
ATOM 1876 CD2 LEU A 317 -41.711 44.647 104.957 1.00 50.68 C
ANISOU 1876 CD2 LEU A 317 6169 5767 7319 360 502 -971 C
ATOM 1877 N ASN A 318 -40.382 43.636 99.748 1.00 46.76 N
ANISOU 1877 N ASN A 318 5187 5403 7178 541 226 -234 N
ATOM 1878 CA ASN A 318 -40.786 43.904 98.379 1.00 46.57 C
ANISOU 1878 CA ASN A 318 5052 5371 7270 607 222 -97 C
ATOM 1879 C ASN A 318 -41.575 42.770 97.754 1.00 41.92 C
ANISOU 1879 C ASN A 318 4412 4932 6583 626 265 -48 C
ATOM 1880 O ASN A 318 -42.427 43.012 96.889 1.00 42.01 O
ANISOU 1880 O ASN A 318 4326 4964 6671 704 263 -4 O
ATOM 1881 CB ASN A 318 -39.580 44.270 97.496 1.00 50.39 C
ANISOU 1881 CB ASN A 318 5520 5800 7827 571 153 40 C
ATOM 1882 CG ASN A 318 -39.423 45.776 97.335 1.00 72.08 C
ANISOU 1882 CG ASN A 318 8278 8352 10758 585 151 43 C
ATOM 1883 OD1 ASN A 318 -39.807 46.342 96.307 1.00 81.96 O
ANISOU 1883 OD1 ASN A 318 9520 9526 12093 652 150 168 O
ATOM 1884 ND2 ASN A 318 -38.917 46.435 98.368 1.00 74.87 N
ANISOU 1884 ND2 ASN A 318 8676 8611 11162 527 147 -98 N
ATOM 1885 N VAL A 319 -41.341 41.519 98.184 1.00 32.98 N
ANISOU 1885 N VAL A 319 3353 3899 5280 562 296 -66 N
ATOM 1886 CA VAL A 319 -42.175 40.400 97.762 1.00 31.17 C
ANISOU 1886 CA VAL A 319 3093 3793 4958 547 376 -64 C
ATOM 1887 C VAL A 319 -43.578 40.528 98.368 1.00 40.85 C
ANISOU 1887 C VAL A 319 4275 5039 6206 552 499 -233 C
ATOM 1888 O VAL A 319 -44.589 40.403 97.661 1.00 44.79 O
ANISOU 1888 O VAL A 319 4629 5619 6768 587 531 -260 O
ATOM 1889 CB VAL A 319 -41.489 39.063 98.117 1.00 27.41 C
ANISOU 1889 CB VAL A 319 2749 3365 4301 482 392 -35 C
ATOM 1890 CG1 VAL A 319 -42.468 37.891 98.137 1.00 25.08 C
ANISOU 1890 CG1 VAL A 319 2485 3155 3891 425 534 -93 C
ATOM 1891 CG2 VAL A 319 -40.341 38.769 97.135 1.00 25.91 C
ANISOU 1891 CG2 VAL A 319 2518 3193 4132 490 301 110 C
ATOM 1892 N LEU A 320 -43.663 40.826 99.672 1.00 42.03 N
ANISOU 1892 N LEU A 320 4534 5123 6311 514 567 -371 N
ATOM 1893 CA LEU A 320 -44.953 41.019 100.329 1.00 41.06 C
ANISOU 1893 CA LEU A 320 4364 5011 6227 499 724 -569 C
ATOM 1894 C LEU A 320 -45.755 42.129 99.652 1.00 46.63 C
ANISOU 1894 C LEU A 320 4851 5688 7179 631 682 -606 C
ATOM 1895 O LEU A 320 -46.966 42.002 99.442 1.00 51.26 O
ANISOU 1895 O LEU A 320 5274 6353 7850 660 767 -731 O
ATOM 1896 CB LEU A 320 -44.755 41.322 101.818 1.00 43.43 C
ANISOU 1896 CB LEU A 320 4850 5228 6422 431 801 -709 C
ATOM 1897 CG LEU A 320 -44.138 40.211 102.684 1.00 43.64 C
ANISOU 1897 CG LEU A 320 5146 5270 6166 324 835 -688 C
ATOM 1898 CD1 LEU A 320 -44.003 40.652 104.138 1.00 41.89 C
ANISOU 1898 CD1 LEU A 320 5130 4973 5814 264 888 -834 C
ATOM 1899 CD2 LEU A 320 -44.943 38.912 102.587 1.00 39.54 C
ANISOU 1899 CD2 LEU A 320 4669 4832 5521 233 1011 -717 C
ATOM 1900 N LYS A 321 -45.084 43.217 99.272 1.00 43.20 N
ANISOU 1900 N LYS A 321 4412 5133 6870 718 547 -503 N
ATOM 1901 CA LYS A 321 -45.737 44.340 98.633 1.00 44.52 C
ANISOU 1901 CA LYS A 321 4435 5222 7261 874 484 -502 C
ATOM 1902 C LYS A 321 -46.108 44.079 97.188 1.00 52.91 C
ANISOU 1902 C LYS A 321 5370 6377 8356 966 374 -359 C
ATOM 1903 O LYS A 321 -47.259 44.269 96.774 1.00 61.68 O
ANISOU 1903 O LYS A 321 6305 7545 9585 1084 355 -441 O
ATOM 1904 CB LYS A 321 -44.867 45.582 98.759 1.00 39.20 C
ANISOU 1904 CB LYS A 321 3852 4347 6695 908 408 -441 C
ATOM 1905 CG LYS A 321 -45.185 46.673 97.772 1.00 36.76 C
ANISOU 1905 CG LYS A 321 3474 3911 6582 1078 304 -336 C
ATOM 1906 CD LYS A 321 -44.543 47.942 98.257 1.00 38.86 C
ANISOU 1906 CD LYS A 321 3848 3941 6974 1080 304 -357 C
ATOM 1907 CE LYS A 321 -44.560 49.038 97.226 1.00 55.18 C
ANISOU 1907 CE LYS A 321 5938 5821 9206 1228 206 -197 C
ATOM 1908 NZ LYS A 321 -44.187 50.324 97.873 1.00 67.85 N
ANISOU 1908 NZ LYS A 321 7646 7166 10970 1228 252 -279 N
ATOM 1909 N ARG A 322 -45.129 43.655 96.360 1.00 54.21 N
ANISOU 1909 N ARG A 322 5613 6568 8416 919 289 -157 N
ATOM 1910 CA ARG A 322 -45.331 43.536 94.917 1.00 48.47 C
ANISOU 1910 CA ARG A 322 4817 5914 7686 996 176 -3 C
ATOM 1911 C ARG A 322 -45.998 42.224 94.499 1.00 44.23 C
ANISOU 1911 C ARG A 322 4180 5592 7034 939 216 -56 C
ATOM 1912 O ARG A 322 -46.697 42.206 93.475 1.00 50.91 O
ANISOU 1912 O ARG A 322 4908 6533 7901 1031 118 -22 O
ATOM 1913 CB ARG A 322 -43.999 43.676 94.177 1.00 42.13 C
ANISOU 1913 CB ARG A 322 4145 5041 6823 943 113 209 C
ATOM 1914 CG ARG A 322 -43.279 44.997 94.401 1.00 38.17 C
ANISOU 1914 CG ARG A 322 3743 4314 6446 967 88 262 C
ATOM 1915 CD ARG A 322 -44.014 46.160 93.754 1.00 35.84 C
ANISOU 1915 CD ARG A 322 3436 3887 6295 1148 -2 326 C
ATOM 1916 NE ARG A 322 -43.390 47.442 94.074 1.00 46.68 N
ANISOU 1916 NE ARG A 322 4929 5005 7802 1155 11 354 N
ATOM 1917 CZ ARG A 322 -43.703 48.592 93.485 1.00 53.94 C
ANISOU 1917 CZ ARG A 322 5920 5728 8846 1303 -57 455 C
ATOM 1918 NH1 ARG A 322 -44.631 48.622 92.539 1.00 53.80 N
ANISOU 1918 NH1 ARG A 322 5856 5762 8822 1482 -182 545 N
ATOM 1919 NH2 ARG A 322 -43.087 49.712 93.839 1.00 57.53 N
ANISOU 1919 NH2 ARG A 322 6504 5928 9428 1276 -11 462 N
ATOM 1920 N VAL A 323 -45.778 41.131 95.219 1.00 55.38 N
ANISOU 1920 N VAL A 323 4562 6435 10044 678 -2562 55 N
ATOM 1921 CA VAL A 323 -46.342 39.829 94.858 1.00 57.68 C
ANISOU 1921 CA VAL A 323 4810 6711 10396 457 -2800 58 C
ATOM 1922 C VAL A 323 -47.607 39.516 95.660 1.00 61.61 C
ANISOU 1922 C VAL A 323 4830 7352 11226 240 -2717 12 C
ATOM 1923 O VAL A 323 -48.562 38.964 95.112 1.00 60.79 O
ANISOU 1923 O VAL A 323 4566 7297 11235 120 -2908 -19 O
ATOM 1924 CB VAL A 323 -45.277 38.712 95.004 1.00 54.53 C
ANISOU 1924 CB VAL A 323 4729 6186 9805 322 -2879 96 C
ATOM 1925 CG1 VAL A 323 -45.826 37.345 94.583 1.00 50.09 C
ANISOU 1925 CG1 VAL A 323 4201 5566 9264 76 -3143 104 C
ATOM 1926 CG2 VAL A 323 -44.026 39.036 94.176 1.00 53.09 C
ANISOU 1926 CG2 VAL A 323 4972 5889 9311 527 -2896 104 C
ATOM 1927 N PHE A 324 -47.666 39.897 96.944 1.00 62.11 N
ANISOU 1927 N PHE A 324 4650 7491 11460 170 -2405 -9 N
ATOM 1928 CA PHE A 324 -48.805 39.598 97.807 1.00 64.00 C
ANISOU 1928 CA PHE A 324 4438 7862 12016 -91 -2214 -78 C
ATOM 1929 C PHE A 324 -49.686 40.818 98.094 1.00 69.70 C
ANISOU 1929 C PHE A 324 4806 8734 12941 108 -1985 -151 C
ATOM 1930 O PHE A 324 -50.589 40.744 98.936 1.00 72.82 O
ANISOU 1930 O PHE A 324 4814 9255 13598 -83 -1719 -231 O
ATOM 1931 CB PHE A 324 -48.311 38.943 99.102 1.00 56.79 C
ANISOU 1931 CB PHE A 324 3683 6884 11008 -390 -1912 -59 C
ATOM 1932 CG PHE A 324 -47.692 37.598 98.860 1.00 56.15 C
ANISOU 1932 CG PHE A 324 4027 6652 10655 -602 -2111 -3 C
ATOM 1933 CD1 PHE A 324 -48.487 36.467 98.770 1.00 57.56 C
ANISOU 1933 CD1 PHE A 324 4119 6825 10926 -956 -2214 -30 C
ATOM 1934 CD2 PHE A 324 -46.331 37.474 98.626 1.00 55.23 C
ANISOU 1934 CD2 PHE A 324 4385 6397 10203 -434 -2213 61 C
ATOM 1935 CE1 PHE A 324 -47.930 35.228 98.500 1.00 56.81 C
ANISOU 1935 CE1 PHE A 324 4473 6555 10558 -1128 -2412 21 C
ATOM 1936 CE2 PHE A 324 -45.768 36.237 98.354 1.00 50.40 C
ANISOU 1936 CE2 PHE A 324 4166 5633 9350 -572 -2411 100 C
ATOM 1937 CZ PHE A 324 -46.569 35.113 98.291 1.00 53.21 C
ANISOU 1937 CZ PHE A 324 4499 5952 9768 -909 -2515 88 C
ATOM 1938 N GLY A 325 -49.473 41.925 97.377 1.00 68.62 N
ANISOU 1938 N GLY A 325 4824 8575 12673 471 -2070 -134 N
ATOM 1939 CA GLY A 325 -50.308 43.097 97.458 1.00 66.37 C
ANISOU 1939 CA GLY A 325 4275 8402 12540 707 -1939 -197 C
ATOM 1940 C GLY A 325 -50.544 43.663 98.843 1.00 65.18 C
ANISOU 1940 C GLY A 325 3865 8323 12579 673 -1491 -252 C
ATOM 1941 O GLY A 325 -51.623 44.188 99.128 1.00 70.72 O
ANISOU 1941 O GLY A 325 4201 9165 13505 746 -1342 -341 O
ATOM 1942 N MET A 326 -49.537 43.579 99.720 1.00 60.27 N
ANISOU 1942 N MET A 326 3433 7599 11867 571 -1262 -208 N
ATOM 1943 CA MET A 326 -49.625 44.090 101.075 1.00 60.83 C
ANISOU 1943 CA MET A 326 3339 7693 12083 512 -792 -256 C
ATOM 1944 C MET A 326 -49.268 45.574 101.152 1.00 67.64 C
ANISOU 1944 C MET A 326 4355 8504 12841 869 -649 -253 C
ATOM 1945 O MET A 326 -48.797 46.179 100.184 1.00 73.68 O
ANISOU 1945 O MET A 326 5397 9200 13398 1126 -905 -205 O
ATOM 1946 CB MET A 326 -48.704 43.310 102.007 1.00 60.06 C
ANISOU 1946 CB MET A 326 3611 7487 11723 207 -589 -200 C
ATOM 1947 CG MET A 326 -49.072 41.874 102.171 1.00 67.22 C
ANISOU 1947 CG MET A 326 4500 8400 12642 -192 -636 -203 C
ATOM 1948 SD MET A 326 -48.392 41.265 103.713 1.00 77.88 S
ANISOU 1948 SD MET A 326 6317 9613 13661 -532 -235 -171 S
ATOM 1949 CE MET A 326 -48.734 39.525 103.519 1.00 81.90 C
ANISOU 1949 CE MET A 326 6917 10072 14131 -954 -418 -158 C
ATOM 1950 N PHE A 327 -49.490 46.146 102.348 1.00 68.45 N
ANISOU 1950 N PHE A 327 4321 8618 13069 847 -194 -311 N
ATOM 1951 CA PHE A 327 -49.170 47.535 102.741 1.00 67.61 C
ANISOU 1951 CA PHE A 327 4377 8436 12875 1129 46 -322 C
ATOM 1952 C PHE A 327 -49.877 48.583 101.870 1.00 71.27 C
ANISOU 1952 C PHE A 327 4797 8947 13334 1492 -143 -349 C
ATOM 1953 O PHE A 327 -49.291 49.606 101.505 1.00 68.14 O
ANISOU 1953 O PHE A 327 4710 8435 12744 1756 -192 -312 O
ATOM 1954 CB PHE A 327 -47.656 47.805 102.778 1.00 56.77 C
ANISOU 1954 CB PHE A 327 3558 6905 11107 1145 20 -233 C
ATOM 1955 CG PHE A 327 -46.809 46.609 103.170 1.00 52.58 C
ANISOU 1955 CG PHE A 327 3322 6336 10320 805 -15 -174 C
ATOM 1956 CD1 PHE A 327 -46.903 46.032 104.430 1.00 52.39 C
ANISOU 1956 CD1 PHE A 327 3369 6304 10232 494 311 -191 C
ATOM 1957 CD2 PHE A 327 -45.894 46.084 102.271 1.00 54.99 C
ANISOU 1957 CD2 PHE A 327 3880 6587 10426 817 -374 -109 C
ATOM 1958 CE1 PHE A 327 -46.114 44.932 104.768 1.00 65.21 C
ANISOU 1958 CE1 PHE A 327 5324 7858 11597 229 226 -137 C
ATOM 1959 CE2 PHE A 327 -45.106 44.991 102.603 1.00 58.69 C
ANISOU 1959 CE2 PHE A 327 4622 7010 10669 566 -435 -69 C
ATOM 1960 CZ PHE A 327 -45.216 44.415 103.851 1.00 60.71 C
ANISOU 1960 CZ PHE A 327 4960 7248 10859 286 -160 -79 C
ATOM 1961 N ARG A 328 -51.157 48.356 101.577 1.00 82.58 N
ANISOU 1961 N ARG A 328 5845 10546 14987 1498 -233 -422 N
ATOM 1962 CA ARG A 328 -51.972 49.332 100.859 1.00 90.69 C
ANISOU 1962 CA ARG A 328 6769 11633 16056 1860 -404 -458 C
ATOM 1963 C ARG A 328 -52.870 50.151 101.789 1.00102.42 C
ANISOU 1963 C ARG A 328 7965 13205 17743 1996 -17 -569 C
ATOM 1964 O ARG A 328 -53.217 51.287 101.447 1.00109.42 O
ANISOU 1964 O ARG A 328 8897 14074 18602 2371 -71 -583 O
ATOM 1965 CB ARG A 328 -52.820 48.625 99.789 1.00 93.38 C
ANISOU 1965 CB ARG A 328 6869 12103 16508 1832 -814 -472 C
ATOM 1966 CG ARG A 328 -52.045 48.270 98.518 1.00 93.91 C
ANISOU 1966 CG ARG A 328 7323 12047 16312 1859 -1248 -365 C
ATOM 1967 CD ARG A 328 -52.725 47.148 97.751 1.00105.45 C
ANISOU 1967 CD ARG A 328 8570 13612 17884 1674 -1576 -384 C
ATOM 1968 NE ARG A 328 -51.951 46.733 96.584 1.00109.36 N
ANISOU 1968 NE ARG A 328 9478 13965 18109 1673 -1940 -291 N
ATOM 1969 CZ ARG A 328 -52.251 45.688 95.820 1.00113.38 C
ANISOU 1969 CZ ARG A 328 9949 14499 18632 1498 -2247 -289 C
ATOM 1970 NH1 ARG A 328 -51.488 45.387 94.778 1.00113.16 N
ANISOU 1970 NH1 ARG A 328 10347 14315 18335 1514 -2527 -212 N
ATOM 1971 NH2 ARG A 328 -53.311 44.940 96.097 1.00115.30 N
ANISOU 1971 NH2 ARG A 328 9739 14917 19154 1290 -2249 -374 N
ATOM 1972 N GLN A 329 -53.226 49.601 102.957 1.00107.43 N
ANISOU 1972 N GLN A 329 8351 13913 18555 1697 394 -646 N
ATOM 1973 CA GLN A 329 -54.052 50.283 103.954 1.00114.11 C
ANISOU 1973 CA GLN A 329 8952 14833 19573 1772 841 -766 C
ATOM 1974 C GLN A 329 -53.235 51.319 104.738 1.00112.45 C
ANISOU 1974 C GLN A 329 9134 14427 19164 1917 1183 -742 C
ATOM 1975 O GLN A 329 -52.143 51.020 105.233 1.00107.67 O
ANISOU 1975 O GLN A 329 8857 13670 18384 1714 1330 -672 O
ATOM 1976 CB GLN A 329 -54.666 49.259 104.916 1.00117.75 C
ANISOU 1976 CB GLN A 329 9093 15408 20237 1335 1208 -858 C
ATOM 1977 CG GLN A 329 -55.835 48.431 104.344 1.00126.06 C
ANISOU 1977 CG GLN A 329 9656 16691 21549 1195 981 -936 C
ATOM 1978 CD GLN A 329 -57.092 49.243 104.069 1.00136.26 C
ANISOU 1978 CD GLN A 329 10534 18167 23072 1528 941 -1049 C
ATOM 1979 OE1 GLN A 329 -57.309 49.714 102.952 1.00142.36 O
ANISOU 1979 OE1 GLN A 329 11284 18972 23833 1869 493 -1013 O
ATOM 1980 NE2 GLN A 329 -57.934 49.396 105.086 1.00137.72 N
ANISOU 1980 NE2 GLN A 329 10407 18464 23457 1430 1418 -1188 N
ATOM 1981 N ALA A 330 -53.770 52.533 104.841 1.00121.50 N
ANISOU 1981 N ALA A 330 10255 15575 20335 2276 1297 -804 N
ATOM 1982 CA ALA A 330 -53.143 53.626 105.571 1.00121.72 C
ANISOU 1982 CA ALA A 330 10671 15409 20170 2433 1628 -800 C
ATOM 1983 C ALA A 330 -53.442 53.596 107.086 1.00129.19 C
ANISOU 1983 C ALA A 330 11562 16343 21183 2198 2251 -894 C
ATOM 1984 O ALA A 330 -53.279 54.616 107.771 1.00129.71 O
ANISOU 1984 O ALA A 330 11893 16271 21120 2358 2570 -926 O
ATOM 1985 CB ALA A 330 -53.532 54.970 104.927 1.00120.43 C
ANISOU 1985 CB ALA A 330 10594 15211 19953 2948 1444 -819 C
ATOM 1986 N SER A 331 -53.862 52.416 107.600 1.00134.32 N
ANISOU 1986 N SER A 331 11932 17109 21993 1794 2432 -938 N
ATOM 1987 CA SER A 331 -54.129 52.215 109.025 1.00136.78 C
ANISOU 1987 CA SER A 331 12267 17386 22316 1491 3044 -1022 C
ATOM 1988 C SER A 331 -52.945 52.652 109.875 1.00132.10 C
ANISOU 1988 C SER A 331 12262 16530 21400 1409 3359 -953 C
ATOM 1989 O SER A 331 -53.118 53.319 110.906 1.00134.37 O
ANISOU 1989 O SER A 331 12745 16717 21594 1411 3824 -1018 O
ATOM 1990 CB SER A 331 -54.432 50.736 109.289 1.00138.40 C
ANISOU 1990 CB SER A 331 12248 17694 22643 1007 3126 -1043 C
ATOM 1991 OG SER A 331 -54.478 50.439 110.680 1.00140.26 O
ANISOU 1991 OG SER A 331 12673 17835 22785 648 3725 -1101 O
ATOM 1992 N ASP A 332 -51.742 52.248 109.481 1.00122.31 N
ANISOU 1992 N ASP A 332 11319 15177 19978 1322 3118 -828 N
ATOM 1993 CA ASP A 332 -50.512 52.711 110.102 1.00113.64 C
ANISOU 1993 CA ASP A 332 10777 13843 18557 1284 3331 -763 C
ATOM 1994 C ASP A 332 -49.520 52.933 108.937 1.00 98.80 C
ANISOU 1994 C ASP A 332 9133 11916 16489 1475 2773 -640 C
ATOM 1995 O ASP A 332 -48.674 52.098 108.606 1.00 92.09 O
ANISOU 1995 O ASP A 332 8492 11067 15431 1254 2461 -541 O
ATOM 1996 CB ASP A 332 -50.033 51.763 111.212 1.00115.23 C
ANISOU 1996 CB ASP A 332 11351 13971 18462 782 3578 -725 C
ATOM 1997 CG ASP A 332 -49.243 52.484 112.311 1.00113.15 C
ANISOU 1997 CG ASP A 332 11724 13482 17787 709 3897 -706 C
ATOM 1998 OD1 ASP A 332 -48.999 53.703 112.175 1.00111.51 O
ANISOU 1998 OD1 ASP A 332 11680 13177 17512 1020 3927 -716 O
ATOM 1999 OD2 ASP A 332 -48.934 51.854 113.347 1.00113.40 O
ANISOU 1999 OD2 ASP A 332 12121 13413 17555 335 4131 -691 O
ATOM 2000 N ARG A 333 -49.775 54.059 108.240 1.00 95.85 N
ANISOU 2000 N ARG A 333 8724 11512 16181 1896 2621 -660 N
ATOM 2001 CA ARG A 333 -48.933 54.591 107.168 1.00 92.11 C
ANISOU 2001 CA ARG A 333 8520 10938 15539 2128 2216 -574 C
ATOM 2002 C ARG A 333 -47.490 54.762 107.628 1.00 87.71 C
ANISOU 2002 C ARG A 333 8571 10217 14537 1916 2270 -497 C
ATOM 2003 O ARG A 333 -46.551 54.600 106.841 1.00 85.98 O
ANISOU 2003 O ARG A 333 8576 9969 14124 1887 1917 -418 O
ATOM 2004 CB ARG A 333 -49.514 55.938 106.715 1.00 95.17 C
ANISOU 2004 CB ARG A 333 8971 11285 15903 2546 2139 -618 C
ATOM 2005 CG ARG A 333 -48.757 56.660 105.610 1.00 98.81 C
ANISOU 2005 CG ARG A 333 9792 11601 16151 2791 1778 -546 C
ATOM 2006 CD ARG A 333 -49.430 57.978 105.217 1.00113.17 C
ANISOU 2006 CD ARG A 333 11706 13356 17939 3222 1716 -605 C
ATOM 2007 NE ARG A 333 -48.721 58.615 104.109 1.00117.88 N
ANISOU 2007 NE ARG A 333 12706 13777 18308 3426 1381 -539 N
ATOM 2008 CZ ARG A 333 -49.041 59.794 103.582 1.00121.60 C
ANISOU 2008 CZ ARG A 333 13415 14111 18676 3812 1257 -579 C
ATOM 2009 NH1 ARG A 333 -50.040 60.502 104.089 1.00121.40 N
ANISOU 2009 NH1 ARG A 333 13240 14120 18766 4070 1428 -690 N
ATOM 2010 NH2 ARG A 333 -48.337 60.280 102.569 1.00122.90 N
ANISOU 2010 NH2 ARG A 333 14003 14077 18616 3937 975 -523 N
ATOM 2011 N GLU A 334 -47.325 55.147 108.885 1.00 75.32 N
ANISOU 2011 N GLU A 334 7285 8544 12790 1768 2702 -533 N
ATOM 2012 CA GLU A 334 -46.029 55.399 109.504 1.00 62.43 C
ANISOU 2012 CA GLU A 334 6233 6764 10723 1547 2759 -486 C
ATOM 2013 C GLU A 334 -45.304 54.098 109.918 1.00 59.26 C
ANISOU 2013 C GLU A 334 5950 6421 10143 1146 2623 -430 C
ATOM 2014 O GLU A 334 -44.070 54.079 109.921 1.00 55.30 O
ANISOU 2014 O GLU A 334 5812 5859 9340 1011 2440 -386 O
ATOM 2015 CB GLU A 334 -46.218 56.379 110.659 1.00 66.78 C
ANISOU 2015 CB GLU A 334 7076 7152 11144 1573 3249 -555 C
ATOM 2016 CG GLU A 334 -46.611 57.809 110.185 1.00 75.40 C
ANISOU 2016 CG GLU A 334 8222 8120 12308 2005 3325 -601 C
ATOM 2017 CD GLU A 334 -45.490 58.567 109.461 1.00 80.96 C
ANISOU 2017 CD GLU A 334 9357 8685 12719 2076 3056 -544 C
ATOM 2018 OE1 GLU A 334 -44.299 58.259 109.682 1.00 81.36 O
ANISOU 2018 OE1 GLU A 334 9734 8714 12468 1769 2941 -500 O
ATOM 2019 OE2 GLU A 334 -45.811 59.484 108.670 1.00 84.89 O
ANISOU 2019 OE2 GLU A 334 9876 9089 13290 2442 2963 -557 O
ATOM 2020 N ALA A 335 -46.030 53.053 110.334 1.00 62.47 N
ANISOU 2020 N ALA A 335 6088 6929 10719 948 2730 -445 N
ATOM 2021 CA ALA A 335 -45.379 51.777 110.664 1.00 61.00 C
ANISOU 2021 CA ALA A 335 6071 6760 10346 602 2564 -387 C
ATOM 2022 C ALA A 335 -44.743 51.153 109.416 1.00 63.51 C
ANISOU 2022 C ALA A 335 6291 7168 10674 653 2042 -318 C
ATOM 2023 O ALA A 335 -43.620 50.639 109.469 1.00 61.42 O
ANISOU 2023 O ALA A 335 6319 6868 10148 501 1817 -273 O
ATOM 2024 CB ALA A 335 -46.393 50.810 111.277 1.00 58.06 C
ANISOU 2024 CB ALA A 335 5458 6450 10151 364 2812 -425 C
ATOM 2025 N VAL A 336 -45.448 51.230 108.281 1.00 66.45 N
ANISOU 2025 N VAL A 336 6259 7644 11344 889 1841 -322 N
ATOM 2026 CA VAL A 336 -44.956 50.744 107.013 1.00 62.81 C
ANISOU 2026 CA VAL A 336 5732 7241 10890 964 1376 -265 C
ATOM 2027 C VAL A 336 -43.738 51.543 106.565 1.00 55.06 C
ANISOU 2027 C VAL A 336 5109 6165 9646 1076 1232 -242 C
ATOM 2028 O VAL A 336 -42.749 50.983 106.065 1.00 54.34 O
ANISOU 2028 O VAL A 336 5168 6085 9392 987 952 -207 O
ATOM 2029 CB VAL A 336 -46.093 50.771 105.962 1.00 60.41 C
ANISOU 2029 CB VAL A 336 4954 7045 10956 1206 1195 -287 C
ATOM 2030 CG1 VAL A 336 -45.596 50.439 104.562 1.00 62.07 C
ANISOU 2030 CG1 VAL A 336 5177 7272 11136 1315 719 -228 C
ATOM 2031 CG2 VAL A 336 -47.204 49.820 106.369 1.00 61.39 C
ANISOU 2031 CG2 VAL A 336 4682 7292 11352 1012 1322 -331 C
ATOM 2032 N TYR A 337 -43.783 52.878 106.745 1.00 48.65 N
ANISOU 2032 N TYR A 337 4449 5251 8786 1265 1446 -278 N
ATOM 2033 CA TYR A 337 -42.644 53.744 106.410 1.00 47.09 C
ANISOU 2033 CA TYR A 337 4629 4943 8320 1314 1378 -276 C
ATOM 2034 C TYR A 337 -41.434 53.414 107.276 1.00 50.35 C
ANISOU 2034 C TYR A 337 5365 5331 8436 1017 1414 -284 C
ATOM 2035 O TYR A 337 -40.302 53.370 106.778 1.00 49.10 O
ANISOU 2035 O TYR A 337 5374 5176 8107 953 1204 -287 O
ATOM 2036 CB TYR A 337 -42.997 55.229 106.619 1.00 50.68 C
ANISOU 2036 CB TYR A 337 5252 5253 8750 1541 1646 -319 C
ATOM 2037 CG TYR A 337 -43.900 55.893 105.592 1.00 60.18 C
ANISOU 2037 CG TYR A 337 6265 6425 10174 1924 1532 -323 C
ATOM 2038 CD1 TYR A 337 -43.958 55.428 104.289 1.00 64.96 C
ANISOU 2038 CD1 TYR A 337 6711 7088 10882 2040 1142 -282 C
ATOM 2039 CD2 TYR A 337 -44.678 57.004 105.926 1.00 64.84 C
ANISOU 2039 CD2 TYR A 337 6881 6903 10851 2193 1796 -375 C
ATOM 2040 CE1 TYR A 337 -44.780 56.028 103.347 1.00 70.56 C
ANISOU 2040 CE1 TYR A 337 7295 7746 11770 2408 976 -288 C
ATOM 2041 CE2 TYR A 337 -45.505 57.613 104.987 1.00 71.73 C
ANISOU 2041 CE2 TYR A 337 7599 7731 11925 2595 1635 -388 C
ATOM 2042 CZ TYR A 337 -45.550 57.117 103.698 1.00 78.03 C
ANISOU 2042 CZ TYR A 337 8247 8586 12813 2699 1204 -342 C
ATOM 2043 OH TYR A 337 -46.364 57.708 102.755 1.00 91.73 O
ANISOU 2043 OH TYR A 337 9906 10286 14660 3078 960 -355 O
ATOM 2044 N ALA A 338 -41.657 53.184 108.577 1.00 55.07 N
ANISOU 2044 N ALA A 338 6057 5898 8969 837 1677 -301 N
ATOM 2045 CA ALA A 338 -40.582 52.811 109.497 1.00 49.50 C
ANISOU 2045 CA ALA A 338 5683 5152 7973 570 1661 -312 C
ATOM 2046 C ALA A 338 -39.923 51.489 109.099 1.00 50.27 C
ANISOU 2046 C ALA A 338 5712 5348 8041 446 1299 -280 C
ATOM 2047 O ALA A 338 -38.690 51.376 109.117 1.00 55.55 O
ANISOU 2047 O ALA A 338 6573 6022 8513 355 1105 -307 O
ATOM 2048 CB ALA A 338 -41.128 52.744 110.927 1.00 49.06 C
ANISOU 2048 CB ALA A 338 5790 5008 7842 409 2015 -330 C
ATOM 2049 N ALA A 339 -40.731 50.484 108.737 1.00 48.70 N
ANISOU 2049 N ALA A 339 5231 5227 8045 442 1204 -237 N
ATOM 2050 CA ALA A 339 -40.206 49.182 108.312 1.00 43.92 C
ANISOU 2050 CA ALA A 339 4593 4687 7410 346 865 -205 C
ATOM 2051 C ALA A 339 -39.379 49.307 107.031 1.00 50.48 C
ANISOU 2051 C ALA A 339 5369 5574 8236 488 563 -212 C
ATOM 2052 O ALA A 339 -38.270 48.774 106.941 1.00 56.55 O
ANISOU 2052 O ALA A 339 6265 6364 8855 422 340 -234 O
ATOM 2053 CB ALA A 339 -41.357 48.194 108.104 1.00 43.23 C
ANISOU 2053 CB ALA A 339 4225 4654 7547 294 852 -166 C
ATOM 2054 N PHE A 340 -39.915 50.004 106.019 1.00 49.13 N
ANISOU 2054 N PHE A 340 5022 5417 8227 696 554 -204 N
ATOM 2055 CA PHE A 340 -39.199 50.144 104.764 1.00 46.14 C
ANISOU 2055 CA PHE A 340 4658 5058 7816 809 312 -213 C
ATOM 2056 C PHE A 340 -37.969 51.023 104.907 1.00 50.12 C
ANISOU 2056 C PHE A 340 5427 5518 8099 764 381 -282 C
ATOM 2057 O PHE A 340 -36.952 50.810 104.225 1.00 49.16 O
ANISOU 2057 O PHE A 340 5357 5434 7889 741 203 -324 O
ATOM 2058 CB PHE A 340 -40.127 50.707 103.680 1.00 48.04 C
ANISOU 2058 CB PHE A 340 4729 5281 8245 1049 263 -186 C
ATOM 2059 CG PHE A 340 -40.876 49.648 102.933 1.00 58.58 C
ANISOU 2059 CG PHE A 340 5798 6687 9774 1082 13 -139 C
ATOM 2060 CD1 PHE A 340 -40.304 49.017 101.842 1.00 59.33 C
ANISOU 2060 CD1 PHE A 340 5929 6794 9818 1101 -284 -126 C
ATOM 2061 CD2 PHE A 340 -42.148 49.275 103.322 1.00 62.03 C
ANISOU 2061 CD2 PHE A 340 5950 7175 10443 1071 93 -124 C
ATOM 2062 CE1 PHE A 340 -40.989 48.036 101.154 1.00 60.49 C
ANISOU 2062 CE1 PHE A 340 5877 6986 10119 1112 -529 -85 C
ATOM 2063 CE2 PHE A 340 -42.836 48.296 102.636 1.00 62.32 C
ANISOU 2063 CE2 PHE A 340 5738 7279 10660 1058 -151 -95 C
ATOM 2064 CZ PHE A 340 -42.256 47.677 101.551 1.00 62.34 C
ANISOU 2064 CZ PHE A 340 5823 7276 10586 1080 -478 -69 C
ATOM 2065 N THR A 341 -38.048 52.038 105.771 1.00 53.42 N
ANISOU 2065 N THR A 341 6014 5855 8429 737 658 -311 N
ATOM 2066 CA THR A 341 -36.929 52.933 106.055 1.00 49.35 C
ANISOU 2066 CA THR A 341 5767 5288 7694 639 747 -391 C
ATOM 2067 C THR A 341 -35.756 52.175 106.676 1.00 50.01 C
ANISOU 2067 C THR A 341 5921 5448 7634 437 587 -450 C
ATOM 2068 O THR A 341 -34.616 52.273 106.197 1.00 46.86 O
ANISOU 2068 O THR A 341 5553 5102 7150 378 464 -533 O
ATOM 2069 CB THR A 341 -37.437 54.052 106.972 1.00 49.36 C
ANISOU 2069 CB THR A 341 5961 5163 7629 647 1080 -402 C
ATOM 2070 OG1 THR A 341 -38.316 54.904 106.227 1.00 58.93 O
ANISOU 2070 OG1 THR A 341 7134 6293 8962 893 1181 -373 O
ATOM 2071 CG2 THR A 341 -36.317 54.882 107.574 1.00 47.49 C
ANISOU 2071 CG2 THR A 341 6040 4863 7140 472 1182 -491 C
ATOM 2072 N PHE A 342 -36.020 51.409 107.743 1.00 51.04 N
ANISOU 2072 N PHE A 342 6085 5573 7733 333 588 -421 N
ATOM 2073 CA PHE A 342 -34.978 50.609 108.384 1.00 50.82 C
ANISOU 2073 CA PHE A 342 6160 5589 7559 190 374 -473 C
ATOM 2074 C PHE A 342 -34.404 49.577 107.418 1.00 56.79 C
ANISOU 2074 C PHE A 342 6730 6456 8393 257 54 -487 C
ATOM 2075 O PHE A 342 -33.202 49.283 107.452 1.00 63.59 O
ANISOU 2075 O PHE A 342 7608 7386 9166 211 -145 -583 O
ATOM 2076 CB PHE A 342 -35.522 49.916 109.643 1.00 50.71 C
ANISOU 2076 CB PHE A 342 6304 5497 7467 76 435 -423 C
ATOM 2077 CG PHE A 342 -34.535 48.966 110.283 1.00 57.49 C
ANISOU 2077 CG PHE A 342 7320 6364 8159 -22 144 -466 C
ATOM 2078 CD1 PHE A 342 -33.486 49.451 111.048 1.00 57.51 C
ANISOU 2078 CD1 PHE A 342 7540 6348 7963 -126 76 -564 C
ATOM 2079 CD2 PHE A 342 -34.634 47.594 110.090 1.00 56.14 C
ANISOU 2079 CD2 PHE A 342 7095 6210 8025 1 -94 -419 C
ATOM 2080 CE1 PHE A 342 -32.558 48.589 111.618 1.00 56.31 C
ANISOU 2080 CE1 PHE A 342 7520 6205 7670 -167 -256 -619 C
ATOM 2081 CE2 PHE A 342 -33.708 46.726 110.658 1.00 53.85 C
ANISOU 2081 CE2 PHE A 342 6986 5902 7572 -35 -399 -464 C
ATOM 2082 CZ PHE A 342 -32.670 47.226 111.422 1.00 53.53 C
ANISOU 2082 CZ PHE A 342 7132 5854 7352 -100 -497 -568 C
ATOM 2083 N SER A 343 -35.253 49.029 106.545 1.00 54.26 N
ANISOU 2083 N SER A 343 6221 6153 8243 372 -2 -406 N
ATOM 2084 CA SER A 343 -34.817 48.040 105.564 1.00 48.79 C
ANISOU 2084 CA SER A 343 5394 5534 7611 443 -284 -413 C
ATOM 2085 C SER A 343 -33.894 48.656 104.518 1.00 53.68 C
ANISOU 2085 C SER A 343 5974 6206 8215 500 -316 -504 C
ATOM 2086 O SER A 343 -32.904 48.038 104.115 1.00 57.11 O
ANISOU 2086 O SER A 343 6358 6716 8623 508 -508 -586 O
ATOM 2087 CB SER A 343 -36.036 47.405 104.904 1.00 42.07 C
ANISOU 2087 CB SER A 343 4382 4670 6933 522 -331 -309 C
ATOM 2088 OG SER A 343 -36.715 46.603 105.850 1.00 45.35 O
ANISOU 2088 OG SER A 343 4841 5043 7347 410 -303 -251 O
ATOM 2089 N HIS A 344 -34.210 49.884 104.064 1.00 59.86 N
ANISOU 2089 N HIS A 344 6802 6934 9008 542 -110 -503 N
ATOM 2090 CA HIS A 344 -33.369 50.590 103.121 1.00 56.98 C
ANISOU 2090 CA HIS A 344 6485 6579 8587 544 -73 -595 C
ATOM 2091 C HIS A 344 -32.019 50.929 103.715 1.00 59.20 C
ANISOU 2091 C HIS A 344 6821 6929 8741 376 -46 -745 C
ATOM 2092 O HIS A 344 -30.987 50.892 103.026 1.00 62.38 O
ANISOU 2092 O HIS A 344 7164 7410 9127 334 -95 -867 O
ATOM 2093 CB HIS A 344 -34.045 51.887 102.643 1.00 52.83 C
ANISOU 2093 CB HIS A 344 6095 5926 8050 624 142 -556 C
ATOM 2094 CG HIS A 344 -35.260 51.670 101.807 1.00 53.16 C
ANISOU 2094 CG HIS A 344 6051 5911 8235 821 58 -443 C
ATOM 2095 ND1 HIS A 344 -36.475 52.276 102.081 1.00 53.46 N
ANISOU 2095 ND1 HIS A 344 6082 5867 8365 948 183 -367 N
ATOM 2096 CD2 HIS A 344 -35.452 50.948 100.678 1.00 52.55 C
ANISOU 2096 CD2 HIS A 344 5890 5846 8231 922 -152 -407 C
ATOM 2097 CE1 HIS A 344 -37.356 51.916 101.168 1.00 54.42 C
ANISOU 2097 CE1 HIS A 344 6075 5971 8629 1118 19 -297 C
ATOM 2098 NE2 HIS A 344 -36.765 51.111 100.306 1.00 54.33 N
ANISOU 2098 NE2 HIS A 344 6044 6006 8593 1093 -191 -312 N
ATOM 2099 N TRP A 345 -32.004 51.292 105.005 1.00 56.63 N
ANISOU 2099 N TRP A 345 6610 6578 8329 266 41 -755 N
ATOM 2100 CA TRP A 345 -30.763 51.621 105.696 1.00 55.10 C
ANISOU 2100 CA TRP A 345 6467 6452 8017 92 18 -907 C
ATOM 2101 C TRP A 345 -29.867 50.389 105.832 1.00 55.94 C
ANISOU 2101 C TRP A 345 6405 6694 8155 108 -298 -991 C
ATOM 2102 O TRP A 345 -28.649 50.483 105.635 1.00 55.40 O
ANISOU 2102 O TRP A 345 6220 6748 8083 31 -376 -1163 O
ATOM 2103 CB TRP A 345 -31.076 52.245 107.064 1.00 54.87 C
ANISOU 2103 CB TRP A 345 6666 6325 7858 -20 161 -884 C
ATOM 2104 CG TRP A 345 -29.845 52.476 107.884 1.00 55.45 C
ANISOU 2104 CG TRP A 345 6802 6464 7802 -207 64 -1041 C
ATOM 2105 CD1 TRP A 345 -28.972 53.521 107.780 1.00 56.07 C
ANISOU 2105 CD1 TRP A 345 6934 6567 7802 -381 182 -1187 C
ATOM 2106 CD2 TRP A 345 -29.328 51.622 108.911 1.00 53.52 C
ANISOU 2106 CD2 TRP A 345 6583 6263 7489 -247 -206 -1082 C
ATOM 2107 NE1 TRP A 345 -27.946 53.371 108.683 1.00 57.98 N
ANISOU 2107 NE1 TRP A 345 7173 6895 7960 -531 -14 -1327 N
ATOM 2108 CE2 TRP A 345 -28.142 52.214 109.390 1.00 53.46 C
ANISOU 2108 CE2 TRP A 345 6599 6327 7385 -427 -275 -1262 C
ATOM 2109 CE3 TRP A 345 -29.754 50.415 109.474 1.00 52.81 C
ANISOU 2109 CE3 TRP A 345 6534 6139 7392 -157 -407 -990 C
ATOM 2110 CZ2 TRP A 345 -27.378 51.639 110.406 1.00 48.02 C
ANISOU 2110 CZ2 TRP A 345 5955 5684 6605 -479 -586 -1352 C
ATOM 2111 CZ3 TRP A 345 -28.994 49.846 110.481 1.00 50.55 C
ANISOU 2111 CZ3 TRP A 345 6361 5866 6981 -210 -690 -1067 C
ATOM 2112 CH2 TRP A 345 -27.820 50.458 110.937 1.00 46.18 C
ANISOU 2112 CH2 TRP A 345 5811 5390 6344 -349 -801 -1247 C
ATOM 2113 N LEU A 346 -30.464 49.223 106.116 1.00 57.34 N
ANISOU 2113 N LEU A 346 6567 6848 8373 211 -477 -884 N
ATOM 2114 CA LEU A 346 -29.720 47.975 106.311 1.00 58.23 C
ANISOU 2114 CA LEU A 346 6594 7040 8489 274 -804 -947 C
ATOM 2115 C LEU A 346 -28.911 47.570 105.078 1.00 62.57 C
ANISOU 2115 C LEU A 346 6918 7711 9146 370 -913 -1059 C
ATOM 2116 O LEU A 346 -27.835 46.974 105.204 1.00 71.71 O
ANISOU 2116 O LEU A 346 7952 8979 10317 413 -1139 -1203 O
ATOM 2117 CB LEU A 346 -30.686 46.849 106.680 1.00 56.73 C
ANISOU 2117 CB LEU A 346 6501 6752 8300 344 -921 -793 C
ATOM 2118 CG LEU A 346 -30.736 46.428 108.146 1.00 57.10 C
ANISOU 2118 CG LEU A 346 6799 6707 8188 264 -1019 -766 C
ATOM 2119 CD1 LEU A 346 -31.591 45.193 108.287 1.00 58.60 C
ANISOU 2119 CD1 LEU A 346 7096 6794 8375 303 -1122 -634 C
ATOM 2120 CD2 LEU A 346 -29.342 46.168 108.686 1.00 59.99 C
ANISOU 2120 CD2 LEU A 346 7175 7152 8468 273 -1309 -928 C
ATOM 2121 N VAL A 347 -29.453 47.820 103.879 1.00 56.82 N
ANISOU 2121 N VAL A 347 6148 6951 8491 428 -770 -998 N
ATOM 2122 CA VAL A 347 -28.719 47.561 102.636 1.00 58.86 C
ANISOU 2122 CA VAL A 347 6257 7290 8816 494 -801 -1109 C
ATOM 2123 C VAL A 347 -27.417 48.358 102.629 1.00 65.31 C
ANISOU 2123 C VAL A 347 6965 8231 9617 352 -689 -1330 C
ATOM 2124 O VAL A 347 -26.325 47.802 102.440 1.00 69.60 O
ANISOU 2124 O VAL A 347 7306 8916 10225 388 -826 -1506 O
ATOM 2125 CB VAL A 347 -29.618 47.889 101.424 1.00 56.61 C
ANISOU 2125 CB VAL A 347 6047 6900 8561 556 -659 -995 C
ATOM 2126 CG1 VAL A 347 -28.823 48.107 100.134 1.00 48.78 C
ANISOU 2126 CG1 VAL A 347 5014 5947 7574 553 -563 -1127 C
ATOM 2127 CG2 VAL A 347 -30.672 46.788 101.212 1.00 57.09 C
ANISOU 2127 CG2 VAL A 347 6121 6889 8682 690 -844 -832 C
ATOM 2128 N TYR A 348 -27.509 49.655 102.947 1.00 62.76 N
ANISOU 2128 N TYR A 348 6772 7859 9215 183 -445 -1340 N
ATOM 2129 CA TYR A 348 -26.344 50.533 102.988 1.00 57.50 C
ANISOU 2129 CA TYR A 348 6032 7297 8521 -22 -304 -1556 C
ATOM 2130 C TYR A 348 -25.425 50.172 104.152 1.00 61.91 C
ANISOU 2130 C TYR A 348 6443 7994 9087 -79 -542 -1699 C
ATOM 2131 O TYR A 348 -24.198 50.237 104.026 1.00 65.82 O
ANISOU 2131 O TYR A 348 6695 8662 9650 -172 -578 -1935 O
ATOM 2132 CB TYR A 348 -26.795 52.002 103.048 1.00 51.23 C
ANISOU 2132 CB TYR A 348 5501 6362 7602 -186 12 -1510 C
ATOM 2133 CG TYR A 348 -27.637 52.376 101.842 1.00 49.26 C
ANISOU 2133 CG TYR A 348 5423 5958 7334 -91 190 -1385 C
ATOM 2134 CD1 TYR A 348 -27.103 52.304 100.562 1.00 46.09 C
ANISOU 2134 CD1 TYR A 348 4981 5580 6951 -101 275 -1481 C
ATOM 2135 CD2 TYR A 348 -28.971 52.749 101.973 1.00 49.55 C
ANISOU 2135 CD2 TYR A 348 5665 5823 7338 27 255 -1185 C
ATOM 2136 CE1 TYR A 348 -27.864 52.604 99.444 1.00 47.42 C
ANISOU 2136 CE1 TYR A 348 5372 5577 7067 -1 384 -1366 C
ATOM 2137 CE2 TYR A 348 -29.743 53.052 100.857 1.00 50.72 C
ANISOU 2137 CE2 TYR A 348 5965 5829 7478 155 340 -1081 C
ATOM 2138 CZ TYR A 348 -29.182 52.977 99.595 1.00 54.39 C
ANISOU 2138 CZ TYR A 348 6449 6293 7923 139 384 -1164 C
ATOM 2139 OH TYR A 348 -29.940 53.278 98.484 1.00 61.62 O
ANISOU 2139 OH TYR A 348 7586 7035 8792 271 425 -1060 O
ATOM 2140 N ALA A 349 -26.006 49.767 105.291 1.00 61.65 N
ANISOU 2140 N ALA A 349 6559 7883 8983 -24 -715 -1572 N
ATOM 2141 CA ALA A 349 -25.212 49.320 106.435 1.00 60.45 C
ANISOU 2141 CA ALA A 349 6353 7817 8799 -41 -1013 -1688 C
ATOM 2142 C ALA A 349 -24.267 48.169 106.063 1.00 66.95 C
ANISOU 2142 C ALA A 349 6879 8802 9758 139 -1323 -1840 C
ATOM 2143 O ALA A 349 -23.178 48.058 106.638 1.00 70.71 O
ANISOU 2143 O ALA A 349 7178 9422 10267 117 -1554 -2043 O
ATOM 2144 CB ALA A 349 -26.140 48.917 107.585 1.00 58.35 C
ANISOU 2144 CB ALA A 349 6389 7385 8398 3 -1121 -1500 C
ATOM 2145 N ASN A 350 -24.658 47.335 105.092 1.00 68.10 N
ANISOU 2145 N ASN A 350 6967 8924 9986 327 -1340 -1760 N
ATOM 2146 CA ASN A 350 -23.828 46.213 104.645 1.00 66.97 C
ANISOU 2146 CA ASN A 350 6577 8904 9966 537 -1601 -1902 C
ATOM 2147 C ASN A 350 -22.501 46.683 104.036 1.00 71.58 C
ANISOU 2147 C ASN A 350 6793 9710 10693 452 -1499 -2199 C
ATOM 2148 O ASN A 350 -21.461 46.045 104.235 1.00 73.43 O
ANISOU 2148 O ASN A 350 6750 10107 11043 585 -1765 -2409 O
ATOM 2149 CB ASN A 350 -24.628 45.368 103.645 1.00 62.26 C
ANISOU 2149 CB ASN A 350 6060 8199 9398 712 -1582 -1744 C
ATOM 2150 CG ASN A 350 -23.842 44.197 103.087 1.00 60.62 C
ANISOU 2150 CG ASN A 350 5653 8081 9298 952 -1815 -1883 C
ATOM 2151 OD1 ASN A 350 -23.510 43.255 103.806 1.00 61.21 O
ANISOU 2151 OD1 ASN A 350 5747 8152 9357 1127 -2166 -1913 O
ATOM 2152 ND2 ASN A 350 -23.562 44.241 101.789 1.00 60.85 N
ANISOU 2152 ND2 ASN A 350 5542 8162 9416 976 -1616 -1969 N
ATOM 2153 N SER A 351 -22.533 47.797 103.281 1.00 70.63 N
ANISOU 2153 N SER A 351 6678 9591 10567 233 -1105 -2234 N
ATOM 2154 CA SER A 351 -21.329 48.397 102.695 1.00 72.09 C
ANISOU 2154 CA SER A 351 6552 9971 10868 60 -908 -2527 C
ATOM 2155 C SER A 351 -20.345 48.869 103.763 1.00 70.74 C
ANISOU 2155 C SER A 351 6174 9969 10733 -107 -1060 -2746 C
ATOM 2156 O SER A 351 -19.129 48.849 103.543 1.00 70.59 O
ANISOU 2156 O SER A 351 5749 10185 10887 -162 -1079 -3049 O
ATOM 2157 CB SER A 351 -21.710 49.586 101.802 1.00 69.44 C
ANISOU 2157 CB SER A 351 6417 9526 10441 -180 -447 -2484 C
ATOM 2158 OG SER A 351 -22.543 49.210 100.718 1.00 68.74 O
ANISOU 2158 OG SER A 351 6519 9283 10318 -31 -336 -2310 O
ATOM 2159 N ALA A 352 -20.868 49.330 104.904 1.00 70.71 N
ANISOU 2159 N ALA A 352 6446 9849 10572 -204 -1153 -2610 N
ATOM 2160 CA ALA A 352 -20.055 49.726 106.050 1.00 69.17 C
ANISOU 2160 CA ALA A 352 6145 9772 10365 -357 -1367 -2787 C
ATOM 2161 C ALA A 352 -19.510 48.512 106.801 1.00 71.98 C
ANISOU 2161 C ALA A 352 6337 10220 10793 -75 -1901 -2869 C
ATOM 2162 O ALA A 352 -18.398 48.569 107.342 1.00 77.58 O
ANISOU 2162 O ALA A 352 6829 11087 11560 -110 -2089 -3060 O
ATOM 2163 CB ALA A 352 -20.890 50.610 106.984 1.00 62.09 C
ANISOU 2163 CB ALA A 352 5692 8668 9233 -542 -1259 -2598 C
ATOM 2164 N ALA A 353 -20.269 47.406 106.785 1.00 68.54 N
ANISOU 2164 N ALA A 353 6100 9636 10307 221 -2086 -2658 N
ATOM 2165 CA ALA A 353 -19.931 46.183 107.514 1.00 68.83 C
ANISOU 2165 CA ALA A 353 6208 9638 10305 516 -2524 -2625 C
ATOM 2166 C ALA A 353 -18.746 45.439 106.902 1.00 74.72 C
ANISOU 2166 C ALA A 353 6660 10527 11204 722 -2560 -2774 C
ATOM 2167 O ALA A 353 -17.845 44.994 107.624 1.00 80.60 O
ANISOU 2167 O ALA A 353 7349 11323 11953 845 -2841 -2866 O
ATOM 2168 CB ALA A 353 -21.159 45.267 107.568 1.00 57.68 C
ANISOU 2168 CB ALA A 353 5140 7999 8778 708 -2643 -2364 C
ATOM 2169 N ASN A 354 -18.740 45.251 105.572 1.00 71.50 N
ANISOU 2169 N ASN A 354 6082 10167 10918 774 -2296 -2814 N
ATOM 2170 CA ASN A 354 -17.710 44.423 104.937 1.00 71.40 C
ANISOU 2170 CA ASN A 354 5833 10258 11037 987 -2326 -2971 C
ATOM 2171 C ASN A 354 -16.280 44.825 105.303 1.00 76.11 C
ANISOU 2171 C ASN A 354 6075 11076 11765 911 -2380 -3249 C
ATOM 2172 O ASN A 354 -15.504 43.939 105.690 1.00 74.48 O
ANISOU 2172 O ASN A 354 5800 10895 11602 1160 -2664 -3329 O
ATOM 2173 CB ASN A 354 -17.891 44.378 103.409 1.00 67.94 C
ANISOU 2173 CB ASN A 354 5279 9841 10693 986 -1989 -3010 C
ATOM 2174 CG ASN A 354 -19.237 43.781 102.975 1.00 71.10 C
ANISOU 2174 CG ASN A 354 6012 10020 10981 1108 -1992 -2737 C
ATOM 2175 OD1 ASN A 354 -19.766 42.856 103.598 1.00 72.03 O
ANISOU 2175 OD1 ASN A 354 6423 9972 10974 1291 -2265 -2551 O
ATOM 2176 ND2 ASN A 354 -19.762 44.280 101.861 1.00 73.74 N
ANISOU 2176 ND2 ASN A 354 6309 10345 11362 998 -1680 -2727 N
ATOM 2177 N PRO A 355 -15.852 46.101 105.225 1.00 75.90 N
ANISOU 2177 N PRO A 355 5824 11208 11808 572 -2130 -3415 N
ATOM 2178 CA PRO A 355 -14.463 46.398 105.620 1.00 73.29 C
ANISOU 2178 CA PRO A 355 5142 11092 11612 498 -2213 -3680 C
ATOM 2179 C PRO A 355 -14.194 46.152 107.102 1.00 75.25 C
ANISOU 2179 C PRO A 355 5521 11302 11768 594 -2674 -3632 C
ATOM 2180 O PRO A 355 -13.071 45.778 107.459 1.00 83.80 O
ANISOU 2180 O PRO A 355 6348 12518 12972 724 -2904 -3814 O
ATOM 2181 CB PRO A 355 -14.285 47.881 105.245 1.00 72.91 C
ANISOU 2181 CB PRO A 355 4938 11166 11600 47 -1808 -3828 C
ATOM 2182 CG PRO A 355 -15.389 48.174 104.276 1.00 71.86 C
ANISOU 2182 CG PRO A 355 5002 10901 11400 -49 -1462 -3693 C
ATOM 2183 CD PRO A 355 -16.538 47.321 104.759 1.00 73.81 C
ANISOU 2183 CD PRO A 355 5614 10928 11504 225 -1754 -3394 C
ATOM 2184 N ILE A 356 -15.205 46.340 107.963 1.00 72.33 N
ANISOU 2184 N ILE A 356 5553 10745 11183 534 -2819 -3404 N
ATOM 2185 CA ILE A 356 -15.080 46.033 109.389 1.00 77.61 C
ANISOU 2185 CA ILE A 356 6456 11324 11708 626 -3263 -3336 C
ATOM 2186 C ILE A 356 -14.858 44.525 109.589 1.00 82.06 C
ANISOU 2186 C ILE A 356 7135 11779 12264 1054 -3598 -3283 C
ATOM 2187 O ILE A 356 -14.044 44.113 110.427 1.00 86.12 O
ANISOU 2187 O ILE A 356 7621 12319 12784 1202 -3961 -3376 O
ATOM 2188 CB ILE A 356 -16.313 46.584 110.152 1.00 71.17 C
ANISOU 2188 CB ILE A 356 6093 10306 10642 440 -3277 -3123 C
ATOM 2189 CG1 ILE A 356 -16.360 48.131 110.074 1.00 70.63 C
ANISOU 2189 CG1 ILE A 356 5939 10328 10569 -5 -2967 -3227 C
ATOM 2190 CG2 ILE A 356 -16.346 46.137 111.624 1.00 67.98 C
ANISOU 2190 CG2 ILE A 356 6060 9744 10025 546 -3729 -3026 C
ATOM 2191 CD1 ILE A 356 -17.678 48.807 110.534 1.00 67.39 C
ANISOU 2191 CD1 ILE A 356 5958 9708 9939 -216 -2862 -3068 C
ATOM 2192 N ILE A 357 -15.525 43.686 108.770 1.00 78.34 N
ANISOU 2192 N ILE A 357 6797 11183 11784 1251 -3480 -3155 N
ATOM 2193 CA ILE A 357 -15.317 42.231 108.792 1.00 77.47 C
ANISOU 2193 CA ILE A 357 6826 10951 11660 1630 -3743 -3127 C
ATOM 2194 C ILE A 357 -13.879 41.879 108.394 1.00 78.81 C
ANISOU 2194 C ILE A 357 6551 11331 12062 1795 -3813 -3421 C
ATOM 2195 O ILE A 357 -13.203 41.105 109.083 1.00 78.47 O
ANISOU 2195 O ILE A 357 6542 11254 12021 2049 -4187 -3500 O
ATOM 2196 CB ILE A 357 -16.344 41.509 107.883 1.00 68.25 C
ANISOU 2196 CB ILE A 357 5887 9614 10430 1739 -3562 -2941 C
ATOM 2197 CG1 ILE A 357 -17.794 41.790 108.319 1.00 66.55 C
ANISOU 2197 CG1 ILE A 357 6085 9194 10007 1593 -3518 -2665 C
ATOM 2198 CG2 ILE A 357 -16.098 39.979 107.854 1.00 67.51 C
ANISOU 2198 CG2 ILE A 357 5971 9378 10303 2102 -3818 -2934 C
ATOM 2199 CD1 ILE A 357 -18.868 41.475 107.258 1.00 61.77 C
ANISOU 2199 CD1 ILE A 357 5605 8480 9385 1599 -3263 -2498 C
ATOM 2200 N TYR A 358 -13.390 42.439 107.269 1.00 74.77 N
ANISOU 2200 N TYR A 358 5627 11032 11751 1653 -3453 -3605 N
ATOM 2201 CA TYR A 358 -12.015 42.182 106.831 1.00 80.92 C
ANISOU 2201 CA TYR A 358 5937 12035 12773 1777 -3472 -3918 C
ATOM 2202 C TYR A 358 -10.993 42.647 107.868 1.00 89.16 C
ANISOU 2202 C TYR A 358 6740 13237 13901 1718 -3753 -4100 C
ATOM 2203 O TYR A 358 -9.865 42.141 107.885 1.00 91.37 O
ANISOU 2203 O TYR A 358 6695 13659 14364 1923 -3942 -4340 O
ATOM 2204 CB TYR A 358 -11.690 42.863 105.476 1.00 79.75 C
ANISOU 2204 CB TYR A 358 5415 12081 12805 1558 -2980 -4101 C
ATOM 2205 CG TYR A 358 -12.732 42.767 104.360 1.00 80.49 C
ANISOU 2205 CG TYR A 358 5722 12043 12819 1517 -2647 -3934 C
ATOM 2206 CD1 TYR A 358 -13.588 41.677 104.252 1.00 80.15 C
ANISOU 2206 CD1 TYR A 358 6063 11763 12626 1774 -2795 -3703 C
ATOM 2207 CD2 TYR A 358 -12.844 43.778 103.404 1.00 81.84 C
ANISOU 2207 CD2 TYR A 358 5726 12316 13055 1202 -2184 -4019 C
ATOM 2208 CE1 TYR A 358 -14.542 41.606 103.233 1.00 77.54 C
ANISOU 2208 CE1 TYR A 358 5914 11318 12229 1730 -2523 -3551 C
ATOM 2209 CE2 TYR A 358 -13.790 43.714 102.387 1.00 80.58 C
ANISOU 2209 CE2 TYR A 358 5765 12029 12823 1174 -1912 -3873 C
ATOM 2210 CZ TYR A 358 -14.635 42.630 102.305 1.00 76.58 C
ANISOU 2210 CZ TYR A 358 5607 11305 12185 1446 -2098 -3637 C
ATOM 2211 OH TYR A 358 -15.568 42.581 101.290 1.00 70.68 O
ANISOU 2211 OH TYR A 358 5042 10436 11376 1416 -1856 -3496 O
ATOM 2212 N ASN A 359 -11.371 43.597 108.733 1.00 91.86 N
ANISOU 2212 N ASN A 359 7237 13555 14112 1443 -3799 -3997 N
ATOM 2213 CA ASN A 359 -10.467 44.073 109.777 1.00 96.45 C
ANISOU 2213 CA ASN A 359 7640 14269 14738 1355 -4100 -4148 C
ATOM 2214 C ASN A 359 -10.316 43.041 110.902 1.00 99.76 C
ANISOU 2214 C ASN A 359 8351 14517 15036 1701 -4651 -4079 C
ATOM 2215 O ASN A 359 -9.192 42.714 111.296 1.00110.62 O
ANISOU 2215 O ASN A 359 9446 16024 16562 1874 -4957 -4298 O
ATOM 2216 CB ASN A 359 -10.954 45.421 110.317 1.00 93.70 C
ANISOU 2216 CB ASN A 359 7427 13924 14251 923 -3968 -4061 C
ATOM 2217 CG ASN A 359 -9.973 46.053 111.284 1.00 96.75 C
ANISOU 2217 CG ASN A 359 7607 14468 14684 756 -4244 -4235 C
ATOM 2218 OD1 ASN A 359 -8.880 46.461 110.890 1.00 98.43 O
ANISOU 2218 OD1 ASN A 359 7314 14943 15141 641 -4142 -4514 O
ATOM 2219 ND2 ASN A 359 -10.372 46.179 112.544 1.00 96.41 N
ANISOU 2219 ND2 ASN A 359 7970 14265 14398 711 -4579 -4079 N
ATOM 2220 N PHE A 360 -11.436 42.504 111.413 1.00 93.94 N
ANISOU 2220 N PHE A 360 8187 13477 14028 1807 -4778 -3791 N
ATOM 2221 CA PHE A 360 -11.381 41.531 112.507 1.00 97.67 C
ANISOU 2221 CA PHE A 360 9042 13730 14338 2109 -5274 -3718 C
ATOM 2222 C PHE A 360 -11.137 40.083 112.048 1.00102.67 C
ANISOU 2222 C PHE A 360 9727 14253 15029 2536 -5420 -3765 C
ATOM 2223 O PHE A 360 -10.734 39.257 112.871 1.00111.85 O
ANISOU 2223 O PHE A 360 11108 15273 16118 2823 -5858 -3799 O
ATOM 2224 CB PHE A 360 -12.674 41.557 113.354 1.00 94.56 C
ANISOU 2224 CB PHE A 360 9298 13028 13602 2011 -5347 -3408 C
ATOM 2225 CG PHE A 360 -12.994 42.898 114.011 1.00 96.95 C
ANISOU 2225 CG PHE A 360 9678 13379 13778 1607 -5269 -3354 C
ATOM 2226 CD1 PHE A 360 -14.152 43.585 113.670 1.00 92.45 C
ANISOU 2226 CD1 PHE A 360 9297 12741 13091 1338 -4917 -3178 C
ATOM 2227 CD2 PHE A 360 -12.178 43.437 114.999 1.00101.19 C
ANISOU 2227 CD2 PHE A 360 10142 14010 14294 1499 -5573 -3484 C
ATOM 2228 CE1 PHE A 360 -14.472 44.795 114.271 1.00 90.60 C
ANISOU 2228 CE1 PHE A 360 9185 12521 12716 967 -4842 -3149 C
ATOM 2229 CE2 PHE A 360 -12.496 44.653 115.602 1.00 98.64 C
ANISOU 2229 CE2 PHE A 360 9954 13708 13817 1102 -5497 -3440 C
ATOM 2230 CZ PHE A 360 -13.643 45.328 115.236 1.00 93.11 C
ANISOU 2230 CZ PHE A 360 9459 12924 12992 837 -5122 -3279 C
ATOM 2231 N LEU A 361 -11.357 39.741 110.766 1.00 94.99 N
ANISOU 2231 N LEU A 361 8598 13326 14167 2587 -5081 -3777 N
ATOM 2232 CA LEU A 361 -11.173 38.363 110.309 1.00 93.34 C
ANISOU 2232 CA LEU A 361 8487 12999 13980 2968 -5214 -3821 C
ATOM 2233 C LEU A 361 -10.043 38.180 109.287 1.00 96.65 C
ANISOU 2233 C LEU A 361 8328 13690 14706 3097 -5083 -4130 C
ATOM 2234 O LEU A 361 -9.840 37.061 108.802 1.00 96.53 O
ANISOU 2234 O LEU A 361 8365 13598 14715 3409 -5171 -4190 O
ATOM 2235 CB LEU A 361 -12.495 37.808 109.746 1.00 88.41 C
ANISOU 2235 CB LEU A 361 8301 12127 13164 2966 -5000 -3548 C
ATOM 2236 CG LEU A 361 -13.622 37.566 110.767 1.00 84.02 C
ANISOU 2236 CG LEU A 361 8386 11243 12293 2927 -5177 -3258 C
ATOM 2237 CD1 LEU A 361 -14.885 37.153 110.063 1.00 79.76 C
ANISOU 2237 CD1 LEU A 361 8164 10521 11622 2873 -4915 -3022 C
ATOM 2238 CD2 LEU A 361 -13.257 36.503 111.786 1.00 89.28 C
ANISOU 2238 CD2 LEU A 361 9420 11680 12823 3244 -5665 -3282 C
ATOM 2239 N SER A 362 -9.285 39.242 108.981 1.00104.22 N
ANISOU 2239 N SER A 362 6760 15189 17650 2303 -2221 -6433 N
ATOM 2240 CA SER A 362 -8.126 39.170 108.087 1.00103.74 C
ANISOU 2240 CA SER A 362 6425 15364 17629 2413 -2109 -5874 C
ATOM 2241 C SER A 362 -6.995 40.002 108.681 1.00114.50 C
ANISOU 2241 C SER A 362 7511 16979 19014 2225 -2429 -5300 C
ATOM 2242 O SER A 362 -7.101 41.235 108.774 1.00105.37 O
ANISOU 2242 O SER A 362 6463 15800 17771 2007 -2799 -5353 O
ATOM 2243 CB SER A 362 -8.484 39.643 106.674 1.00103.12 C
ANISOU 2243 CB SER A 362 6473 15235 17474 2470 -2117 -6093 C
ATOM 2244 OG SER A 362 -7.340 39.761 105.842 1.00105.16 O
ANISOU 2244 OG SER A 362 6453 15733 17770 2546 -2054 -5569 O
ATOM 2245 N GLY A 363 -5.917 39.322 109.088 1.00116.37 N
ANISOU 2245 N GLY A 363 7409 17453 19354 2289 -2278 -4712 N
ATOM 2246 CA GLY A 363 -4.757 39.998 109.644 1.00110.19 C
ANISOU 2246 CA GLY A 363 6323 16975 18571 2064 -2586 -4080 C
ATOM 2247 C GLY A 363 -4.014 40.844 108.629 1.00111.41 C
ANISOU 2247 C GLY A 363 6344 17311 18677 2009 -2738 -3747 C
ATOM 2248 O GLY A 363 -3.428 41.871 108.988 1.00112.58 O
ANISOU 2248 O GLY A 363 6416 17630 18731 1701 -3125 -3420 O
ATOM 2249 N LYS A 364 -4.039 40.432 107.357 1.00111.31 N
ANISOU 2249 N LYS A 364 6325 17263 18703 2269 -2437 -3829 N
ATOM 2250 CA LYS A 364 -3.402 41.188 106.281 1.00112.43 C
ANISOU 2250 CA LYS A 364 6343 17571 18805 2233 -2557 -3570 C
ATOM 2251 C LYS A 364 -4.120 42.518 106.022 1.00110.77 C
ANISOU 2251 C LYS A 364 6448 17200 18438 2002 -2954 -3956 C
ATOM 2252 O LYS A 364 -3.463 43.555 105.871 1.00112.03 O
ANISOU 2252 O LYS A 364 6525 17525 18515 1771 -3276 -3619 O
ATOM 2253 CB LYS A 364 -3.347 40.318 105.016 1.00112.84 C
ANISOU 2253 CB LYS A 364 6341 17601 18931 2563 -2092 -3619 C
ATOM 2254 CG LYS A 364 -2.295 39.200 105.088 1.00116.05 C
ANISOU 2254 CG LYS A 364 6386 18203 19505 2803 -1677 -3037 C
ATOM 2255 CD LYS A 364 -2.002 38.562 103.734 1.00116.76 C
ANISOU 2255 CD LYS A 364 6411 18301 19652 3086 -1225 -2980 C
ATOM 2256 CE LYS A 364 -1.124 37.320 103.877 1.00119.57 C
ANISOU 2256 CE LYS A 364 6488 18760 20185 3378 -720 -2451 C
ATOM 2257 NZ LYS A 364 -1.711 36.216 104.670 1.00118.81 N
ANISOU 2257 NZ LYS A 364 6579 18443 20121 3514 -431 -2634 N
ATOM 2258 N PHE A 365 -5.463 42.503 105.987 1.00108.19 N
ANISOU 2258 N PHE A 365 6489 16549 18069 2057 -2926 -4634 N
ATOM 2259 CA PHE A 365 -6.254 43.731 105.837 1.00107.38 C
ANISOU 2259 CA PHE A 365 6706 16246 17847 1885 -3258 -4999 C
ATOM 2260 C PHE A 365 -6.100 44.643 107.058 1.00107.26 C
ANISOU 2260 C PHE A 365 6781 16220 17753 1559 -3617 -4841 C
ATOM 2261 O PHE A 365 -5.915 45.858 106.916 1.00107.88 O
ANISOU 2261 O PHE A 365 6970 16298 17721 1331 -3932 -4707 O
ATOM 2262 CB PHE A 365 -7.744 43.392 105.623 1.00107.51 C
ANISOU 2262 CB PHE A 365 7053 15938 17858 2041 -3111 -5727 C
ATOM 2263 CG PHE A 365 -8.176 43.256 104.164 1.00105.94 C
ANISOU 2263 CG PHE A 365 6917 15701 17635 2211 -2964 -5983 C
ATOM 2264 CD1 PHE A 365 -8.285 44.368 103.338 1.00104.01 C
ANISOU 2264 CD1 PHE A 365 6768 15436 17317 2133 -3217 -6002 C
ATOM 2265 CD2 PHE A 365 -8.539 42.017 103.648 1.00106.08 C
ANISOU 2265 CD2 PHE A 365 6933 15689 17682 2417 -2574 -6208 C
ATOM 2266 CE1 PHE A 365 -8.701 44.239 102.013 1.00103.79 C
ANISOU 2266 CE1 PHE A 365 6778 15398 17258 2266 -3106 -6238 C
ATOM 2267 CE2 PHE A 365 -8.958 41.884 102.326 1.00103.18 C
ANISOU 2267 CE2 PHE A 365 6632 15309 17264 2518 -2450 -6447 C
ATOM 2268 CZ PHE A 365 -9.037 42.996 101.511 1.00103.39 C
ANISOU 2268 CZ PHE A 365 6702 15351 17231 2449 -2728 -6474 C
ATOM 2269 N ARG A 366 -6.200 44.063 108.267 1.00108.98 N
ANISOU 2269 N ARG A 366 6977 16418 18010 1511 -3563 -4862 N
ATOM 2270 CA ARG A 366 -6.037 44.806 109.523 1.00115.97 C
ANISOU 2270 CA ARG A 366 7952 17312 18801 1162 -3873 -4708 C
ATOM 2271 C ARG A 366 -4.738 45.606 109.552 1.00127.53 C
ANISOU 2271 C ARG A 366 9199 19094 20163 858 -4164 -4035 C
ATOM 2272 O ARG A 366 -4.724 46.764 109.988 1.00125.48 O
ANISOU 2272 O ARG A 366 9146 18783 19749 522 -4485 -3977 O
ATOM 2273 CB ARG A 366 -6.123 43.838 110.719 1.00114.90 C
ANISOU 2273 CB ARG A 366 7729 17193 18734 1167 -3737 -4734 C
ATOM 2274 CG ARG A 366 -6.170 44.521 112.100 1.00114.42 C
ANISOU 2274 CG ARG A 366 7826 17099 18549 780 -4028 -4683 C
ATOM 2275 CD ARG A 366 -6.860 43.682 113.187 1.00114.14 C
ANISOU 2275 CD ARG A 366 7871 16927 18572 817 -3876 -5016 C
ATOM 2276 NE ARG A 366 -6.568 42.255 113.134 1.00116.17 N
ANISOU 2276 NE ARG A 366 7829 17319 18993 1096 -3560 -4902 N
ATOM 2277 CZ ARG A 366 -7.326 41.317 113.697 1.00115.96 C
ANISOU 2277 CZ ARG A 366 7879 17134 19048 1241 -3331 -5298 C
ATOM 2278 NH1 ARG A 366 -8.433 41.649 114.352 1.00114.72 N
ANISOU 2278 NH1 ARG A 366 8063 16695 18829 1144 -3383 -5846 N
ATOM 2279 NH2 ARG A 366 -6.980 40.041 113.600 1.00115.98 N
ANISOU 2279 NH2 ARG A 366 7627 17248 19193 1495 -3015 -5125 N
ATOM 2280 N GLU A 367 -3.646 44.994 109.073 1.00143.02 N
ANISOU 2280 N GLU A 367 10750 21382 22208 974 -4029 -3514 N
ATOM 2281 CA GLU A 367 -2.329 45.632 109.026 1.00146.49 C
ANISOU 2281 CA GLU A 367 10910 22187 22562 705 -4276 -2823 C
ATOM 2282 C GLU A 367 -2.345 46.912 108.186 1.00145.47 C
ANISOU 2282 C GLU A 367 10978 22002 22291 538 -4529 -2861 C
ATOM 2283 O GLU A 367 -1.819 47.946 108.609 1.00147.29 O
ANISOU 2283 O GLU A 367 11259 22359 22344 139 -4873 -2558 O
ATOM 2284 CB GLU A 367 -1.296 44.634 108.480 1.00150.08 C
ANISOU 2284 CB GLU A 367 10880 22961 23181 969 -3985 -2311 C
ATOM 2285 CG GLU A 367 -0.732 43.678 109.541 1.00155.00 C
ANISOU 2285 CG GLU A 367 11194 23790 23909 988 -3865 -1923 C
ATOM 2286 CD GLU A 367 0.289 42.676 109.009 1.00159.86 C
ANISOU 2286 CD GLU A 367 11328 24691 24720 1302 -3515 -1372 C
ATOM 2287 OE1 GLU A 367 -0.102 41.755 108.260 1.00159.12 O
ANISOU 2287 OE1 GLU A 367 11254 24432 24771 1708 -3080 -1634 O
ATOM 2288 OE2 GLU A 367 1.483 42.803 109.359 1.00163.58 O
ANISOU 2288 OE2 GLU A 367 11409 25555 25190 1130 -3656 -660 O
ATOM 2289 N GLN A 368 -2.922 46.850 106.979 1.00137.29 N
ANISOU 2289 N GLN A 368 10056 20795 21314 817 -4363 -3215 N
ATOM 2290 CA GLN A 368 -3.063 48.024 106.118 1.00130.29 C
ANISOU 2290 CA GLN A 368 9373 19823 20307 694 -4590 -3292 C
ATOM 2291 C GLN A 368 -4.170 48.981 106.575 1.00124.39 C
ANISOU 2291 C GLN A 368 9102 18703 19459 543 -4791 -3761 C
ATOM 2292 O GLN A 368 -4.271 50.082 106.028 1.00123.33 O
ANISOU 2292 O GLN A 368 9161 18481 19219 403 -5009 -3778 O
ATOM 2293 CB GLN A 368 -3.263 47.619 104.645 1.00126.24 C
ANISOU 2293 CB GLN A 368 8793 19292 19881 1019 -4355 -3473 C
ATOM 2294 CG GLN A 368 -1.950 47.406 103.857 1.00125.81 C
ANISOU 2294 CG GLN A 368 8312 19625 19866 1050 -4285 -2896 C
ATOM 2295 CD GLN A 368 -1.189 46.150 104.220 1.00129.67 C
ANISOU 2295 CD GLN A 368 8398 20354 20518 1243 -3967 -2531 C
ATOM 2296 OE1 GLN A 368 -1.779 45.099 104.452 1.00131.64 O
ANISOU 2296 OE1 GLN A 368 8682 20452 20885 1508 -3646 -2834 O
ATOM 2297 NE2 GLN A 368 0.137 46.251 104.253 1.00131.30 N
ANISOU 2297 NE2 GLN A 368 8214 20941 20735 1113 -4041 -1853 N
ATOM 2298 N PHE A 369 -5.042 48.541 107.495 1.00118.58 N
ANISOU 2298 N PHE A 369 8550 17734 18773 607 -4684 -4154 N
ATOM 2299 CA PHE A 369 -6.021 49.419 108.148 1.00114.64 C
ANISOU 2299 CA PHE A 369 8466 16893 18198 462 -4837 -4538 C
ATOM 2300 C PHE A 369 -5.387 50.179 109.321 1.00112.12 C
ANISOU 2300 C PHE A 369 8204 16683 17712 -2 -5123 -4189 C
ATOM 2301 O PHE A 369 -5.668 51.369 109.519 1.00112.13 O
ANISOU 2301 O PHE A 369 8509 16507 17587 -243 -5342 -4263 O
ATOM 2302 CB PHE A 369 -7.235 48.589 108.611 1.00110.86 C
ANISOU 2302 CB PHE A 369 8142 16140 17842 730 -4572 -5110 C
ATOM 2303 CG PHE A 369 -8.151 48.084 107.482 1.00105.45 C
ANISOU 2303 CG PHE A 369 7516 15285 17265 1118 -4328 -5566 C
ATOM 2304 CD1 PHE A 369 -8.214 48.716 106.245 1.00105.62 C
ANISOU 2304 CD1 PHE A 369 7586 15285 17259 1185 -4407 -5568 C
ATOM 2305 CD2 PHE A 369 -8.921 46.938 107.668 1.00103.75 C
ANISOU 2305 CD2 PHE A 369 7303 14959 17158 1379 -4027 -5979 C
ATOM 2306 CE1 PHE A 369 -9.055 48.232 105.235 1.00104.19 C
ANISOU 2306 CE1 PHE A 369 7458 14984 17147 1489 -4202 -5971 C
ATOM 2307 CE2 PHE A 369 -9.750 46.448 106.662 1.00102.32 C
ANISOU 2307 CE2 PHE A 369 7186 14657 17036 1671 -3815 -6393 C
ATOM 2308 CZ PHE A 369 -9.815 47.095 105.447 1.00102.59 C
ANISOU 2308 CZ PHE A 369 7265 14683 17032 1719 -3907 -6383 C
ATOM 2309 N LYS A 370 -4.525 49.497 110.100 1.00112.91 N
ANISOU 2309 N LYS A 370 8012 17084 17804 -143 -5118 -3794 N
ATOM 2310 CA LYS A 370 -3.731 50.134 111.156 1.00115.31 C
ANISOU 2310 CA LYS A 370 8306 17596 17909 -644 -5407 -3368 C
ATOM 2311 C LYS A 370 -2.746 51.136 110.565 1.00117.57 C
ANISOU 2311 C LYS A 370 8506 18138 18027 -932 -5672 -2904 C
ATOM 2312 O LYS A 370 -2.442 52.161 111.195 1.00119.33 O
ANISOU 2312 O LYS A 370 8916 18408 18017 -1391 -5946 -2742 O
ATOM 2313 CB LYS A 370 -2.965 49.067 111.962 1.00116.55 C
ANISOU 2313 CB LYS A 370 8086 18082 18116 -687 -5334 -2978 C
ATOM 2314 CG LYS A 370 -3.776 48.340 113.039 1.00115.18 C
ANISOU 2314 CG LYS A 370 8051 17703 18010 -626 -5187 -3349 C
ATOM 2315 CD LYS A 370 -2.921 47.358 113.840 1.00117.53 C
ANISOU 2315 CD LYS A 370 7948 18357 18352 -700 -5155 -2882 C
ATOM 2316 CE LYS A 370 -3.739 46.664 114.919 1.00119.84 C
ANISOU 2316 CE LYS A 370 8394 18444 18695 -670 -5025 -3263 C
ATOM 2317 NZ LYS A 370 -2.921 45.685 115.687 1.00123.02 N
ANISOU 2317 NZ LYS A 370 8389 19194 19158 -727 -4998 -2787 N
ATOM 2318 N ALA A 371 -2.230 50.827 109.371 1.00117.75 N
ANISOU 2318 N ALA A 371 8247 18344 18146 -686 -5574 -2697 N
ATOM 2319 CA ALA A 371 -1.322 51.694 108.623 1.00119.79 C
ANISOU 2319 CA ALA A 371 8394 18862 18260 -904 -5788 -2284 C
ATOM 2320 C ALA A 371 -1.996 52.989 108.173 1.00119.29 C
ANISOU 2320 C ALA A 371 8764 18479 18080 -1024 -5967 -2607 C
ATOM 2321 O ALA A 371 -1.377 54.060 108.204 1.00122.48 O
ANISOU 2321 O ALA A 371 9238 19040 18257 -1414 -6236 -2332 O
ATOM 2322 CB ALA A 371 -0.805 50.934 107.401 1.00119.85 C
ANISOU 2322 CB ALA A 371 8027 19075 18436 -545 -5570 -2081 C
ATOM 2323 N ALA A 372 -3.276 52.901 107.795 1.00116.75 N
ANISOU 2323 N ALA A 372 8725 17732 17902 -695 -5808 -3192 N
ATOM 2324 CA ALA A 372 -4.029 54.046 107.293 1.00116.36 C
ANISOU 2324 CA ALA A 372 9055 17355 17801 -719 -5942 -3502 C
ATOM 2325 C ALA A 372 -4.415 55.005 108.412 1.00117.19 C
ANISOU 2325 C ALA A 372 9526 17236 17762 -1067 -6123 -3639 C
ATOM 2326 O ALA A 372 -4.446 56.224 108.206 1.00120.09 O
ANISOU 2326 O ALA A 372 10142 17483 18004 -1289 -6333 -3637 O
ATOM 2327 CB ALA A 372 -5.285 53.560 106.568 1.00113.72 C
ANISOU 2327 CB ALA A 372 8849 16691 17666 -245 -5696 -4051 C
ATOM 2328 N PHE A 373 -4.759 54.465 109.590 1.00116.61 N
ANISOU 2328 N PHE A 373 9509 17087 17709 -1115 -6025 -3786 N
ATOM 2329 CA PHE A 373 -5.117 55.313 110.725 1.00117.65 C
ANISOU 2329 CA PHE A 373 10000 17012 17689 -1473 -6160 -3920 C
ATOM 2330 C PHE A 373 -3.884 55.900 111.409 1.00120.77 C
ANISOU 2330 C PHE A 373 10323 17774 17789 -2059 -6422 -3411 C
ATOM 2331 O PHE A 373 -3.957 56.998 111.974 1.00122.47 O
ANISOU 2331 O PHE A 373 10867 17859 17806 -2444 -6586 -3466 O
ATOM 2332 CB PHE A 373 -5.971 54.537 111.748 1.00116.05 C
ANISOU 2332 CB PHE A 373 9902 16603 17588 -1337 -5948 -4275 C
ATOM 2333 CG PHE A 373 -7.312 54.046 111.213 1.00113.22 C
ANISOU 2333 CG PHE A 373 9643 15897 17479 -803 -5676 -4831 C
ATOM 2334 CD1 PHE A 373 -8.189 54.910 110.572 1.00112.79 C
ANISOU 2334 CD1 PHE A 373 9845 15518 17493 -633 -5693 -5142 C
ATOM 2335 CD2 PHE A 373 -7.736 52.744 111.456 1.00111.29 C
ANISOU 2335 CD2 PHE A 373 9239 15658 17389 -498 -5405 -5045 C
ATOM 2336 CE1 PHE A 373 -9.419 54.459 110.099 1.00110.54 C
ANISOU 2336 CE1 PHE A 373 9607 14972 17420 -164 -5453 -5610 C
ATOM 2337 CE2 PHE A 373 -8.971 52.294 111.000 1.00108.94 C
ANISOU 2337 CE2 PHE A 373 9026 15084 17283 -50 -5152 -5553 C
ATOM 2338 CZ PHE A 373 -9.811 53.153 110.322 1.00108.59 C
ANISOU 2338 CZ PHE A 373 9200 14762 17298 113 -5179 -5819 C
ATOM 2339 N SER A 374 -2.745 55.188 111.357 1.00125.68 N
ANISOU 2339 N SER A 374 10502 18881 18369 -2132 -6440 -2918 N
ATOM 2340 CA SER A 374 -1.485 55.709 111.887 1.00131.09 C
ANISOU 2340 CA SER A 374 11021 20052 18736 -2666 -6660 -2421 C
ATOM 2341 C SER A 374 -0.965 56.865 111.037 1.00132.86 C
ANISOU 2341 C SER A 374 11298 20395 18787 -2842 -6836 -2297 C
ATOM 2342 O SER A 374 -0.439 57.848 111.572 1.00132.87 O
ANISOU 2342 O SER A 374 11419 20570 18497 -3284 -6996 -2261 O
ATOM 2343 CB SER A 374 -0.438 54.591 111.957 1.00126.09 C
ANISOU 2343 CB SER A 374 9820 19959 18129 -2596 -6583 -1941 C
ATOM 2344 OG SER A 374 -0.742 53.639 112.964 1.00125.33 O
ANISOU 2344 OG SER A 374 9670 19817 18131 -2552 -6468 -1995 O
ATOM 2345 N TRP A 375 -1.104 56.753 109.717 1.00136.62 N
ANISOU 2345 N TRP A 375 11681 20783 19445 -2475 -6780 -2311 N
ATOM 2346 CA TRP A 375 -0.683 57.789 108.775 1.00139.83 C
ANISOU 2346 CA TRP A 375 12140 21271 19720 -2592 -6940 -2209 C
ATOM 2347 C TRP A 375 -1.665 58.963 108.766 1.00141.71 C
ANISOU 2347 C TRP A 375 12912 20982 19947 -2666 -7048 -2626 C
ATOM 2348 O TRP A 375 -2.884 58.776 108.726 1.00141.09 O
ANISOU 2348 O TRP A 375 13078 20437 20092 -2340 -6920 -3060 O
ATOM 2349 CB TRP A 375 -0.536 57.203 107.360 1.00141.41 C
ANISOU 2349 CB TRP A 375 12059 21556 20113 -2180 -6825 -2089 C
ATOM 2350 CG TRP A 375 -0.010 58.196 106.357 1.00148.23 C
ANISOU 2350 CG TRP A 375 12938 22555 20826 -2309 -6993 -1946 C
ATOM 2351 CD1 TRP A 375 1.297 58.538 106.161 1.00152.99 C
ANISOU 2351 CD1 TRP A 375 13237 23687 21207 -2527 -7088 -1606 C
ATOM 2352 CD2 TRP A 375 -0.772 58.970 105.421 1.00149.79 C
ANISOU 2352 CD2 TRP A 375 13452 22363 21098 -2167 -7065 -2226 C
ATOM 2353 NE1 TRP A 375 1.397 59.481 105.167 1.00155.13 N
ANISOU 2353 NE1 TRP A 375 13646 23887 21410 -2565 -7230 -1626 N
ATOM 2354 CE2 TRP A 375 0.143 59.763 104.694 1.00152.43 C
ANISOU 2354 CE2 TRP A 375 13683 22999 21233 -2378 -7232 -1954 C
ATOM 2355 CE3 TRP A 375 -2.134 59.074 105.125 1.00149.33 C
ANISOU 2355 CE3 TRP A 375 13722 21767 21249 -1850 -6990 -2715 C
ATOM 2356 CZ2 TRP A 375 -0.263 60.645 103.694 1.00152.45 C
ANISOU 2356 CZ2 TRP A 375 13931 22748 21245 -2324 -7356 -2096 C
ATOM 2357 CZ3 TRP A 375 -2.535 59.951 104.132 1.00150.37 C
ANISOU 2357 CZ3 TRP A 375 14064 21679 21391 -1776 -7109 -2854 C
ATOM 2358 CH2 TRP A 375 -1.603 60.725 103.428 1.00151.70 C
ANISOU 2358 CH2 TRP A 375 14152 22125 21364 -2028 -7303 -2525 C
TER 2359 TRP A 375
ATOM 2360 N TYR B 45 -48.598 3.311 71.532 1.00124.91 N
ANISOU 2360 N TYR B 45 20386 15604 11468 -2517 1123 -2813 N
ATOM 2361 CA TYR B 45 -47.746 4.273 70.842 1.00119.97 C
ANISOU 2361 CA TYR B 45 19637 15118 10827 -2028 861 -2610 C
ATOM 2362 C TYR B 45 -46.230 3.974 70.986 1.00116.55 C
ANISOU 2362 C TYR B 45 19476 14289 10520 -1797 940 -2289 C
ATOM 2363 O TYR B 45 -45.402 4.853 70.742 1.00112.18 O
ANISOU 2363 O TYR B 45 18816 13795 10013 -1435 798 -2083 O
ATOM 2364 CB TYR B 45 -48.085 5.707 71.317 1.00114.24 C
ANISOU 2364 CB TYR B 45 18634 14689 10085 -1768 711 -2523 C
ATOM 2365 CG TYR B 45 -47.876 6.043 72.792 1.00110.73 C
ANISOU 2365 CG TYR B 45 18266 14042 9764 -1740 874 -2314 C
ATOM 2366 CD1 TYR B 45 -46.707 6.662 73.221 1.00106.40 C
ANISOU 2366 CD1 TYR B 45 17769 13317 9340 -1398 841 -1989 C
ATOM 2367 CD2 TYR B 45 -48.868 5.799 73.740 1.00112.25 C
ANISOU 2367 CD2 TYR B 45 18450 14253 9947 -2070 1063 -2465 C
ATOM 2368 CE1 TYR B 45 -46.512 6.995 74.558 1.00103.35 C
ANISOU 2368 CE1 TYR B 45 17444 12773 9052 -1353 955 -1818 C
ATOM 2369 CE2 TYR B 45 -48.680 6.130 75.082 1.00109.75 C
ANISOU 2369 CE2 TYR B 45 18220 13765 9715 -2021 1211 -2274 C
ATOM 2370 CZ TYR B 45 -47.501 6.727 75.483 1.00103.77 C
ANISOU 2370 CZ TYR B 45 17527 12836 9066 -1643 1134 -1949 C
ATOM 2371 OH TYR B 45 -47.311 7.055 76.810 1.00 98.95 O
ANISOU 2371 OH TYR B 45 16993 12076 8527 -1584 1249 -1781 O
ATOM 2372 N ALA B 46 -45.890 2.718 71.333 1.00115.46 N
ANISOU 2372 N ALA B 46 19691 13750 10429 -2028 1180 -2269 N
ATOM 2373 CA ALA B 46 -44.495 2.307 71.524 1.00106.95 C
ANISOU 2373 CA ALA B 46 18900 12289 9447 -1818 1259 -1994 C
ATOM 2374 C ALA B 46 -43.674 2.360 70.231 1.00104.65 C
ANISOU 2374 C ALA B 46 18566 12060 9137 -1594 1116 -1978 C
ATOM 2375 O ALA B 46 -42.475 2.656 70.272 1.00101.77 O
ANISOU 2375 O ALA B 46 18259 11547 8864 -1305 1086 -1742 O
ATOM 2376 CB ALA B 46 -44.437 0.900 72.130 1.00105.52 C
ANISOU 2376 CB ALA B 46 19158 11666 9268 -2109 1564 -1993 C
ATOM 2377 N TRP B 47 -44.283 2.044 69.078 1.00106.81 N
ANISOU 2377 N TRP B 47 18745 12551 9287 -1738 1037 -2247 N
ATOM 2378 CA TRP B 47 -43.561 2.165 67.808 1.00103.91 C
ANISOU 2378 CA TRP B 47 18336 12277 8870 -1522 909 -2243 C
ATOM 2379 C TRP B 47 -43.189 3.623 67.536 1.00100.44 C
ANISOU 2379 C TRP B 47 17609 12117 8438 -1169 709 -2083 C
ATOM 2380 O TRP B 47 -42.020 3.940 67.287 1.00 96.62 O
ANISOU 2380 O TRP B 47 17169 11510 8034 -927 708 -1879 O
ATOM 2381 CB TRP B 47 -44.388 1.599 66.643 1.00107.23 C
ANISOU 2381 CB TRP B 47 18702 12919 9123 -1736 836 -2590 C
ATOM 2382 CG TRP B 47 -43.581 1.486 65.357 1.00112.84 C
ANISOU 2382 CG TRP B 47 19455 13660 9760 -1549 762 -2593 C
ATOM 2383 CD1 TRP B 47 -42.907 0.385 64.907 1.00118.97 C
ANISOU 2383 CD1 TRP B 47 20524 14133 10548 -1629 916 -2622 C
ATOM 2384 CD2 TRP B 47 -43.342 2.523 64.390 1.00114.31 C
ANISOU 2384 CD2 TRP B 47 19411 14184 9838 -1253 552 -2555 C
ATOM 2385 NE1 TRP B 47 -42.273 0.670 63.719 1.00121.14 N
ANISOU 2385 NE1 TRP B 47 20747 14548 10731 -1411 810 -2621 N
ATOM 2386 CE2 TRP B 47 -42.523 1.973 63.381 1.00118.46 C
ANISOU 2386 CE2 TRP B 47 20099 14598 10314 -1189 596 -2572 C
ATOM 2387 CE3 TRP B 47 -43.743 3.859 64.278 1.00113.17 C
ANISOU 2387 CE3 TRP B 47 18967 14414 9617 -1041 356 -2502 C
ATOM 2388 CZ2 TRP B 47 -42.100 2.714 62.274 1.00118.49 C
ANISOU 2388 CZ2 TRP B 47 19977 14852 10190 -945 465 -2535 C
ATOM 2389 CZ3 TRP B 47 -43.320 4.592 63.178 1.00114.26 C
ANISOU 2389 CZ3 TRP B 47 18997 14788 9627 -796 230 -2449 C
ATOM 2390 CH2 TRP B 47 -42.508 4.017 62.192 1.00116.86 C
ANISOU 2390 CH2 TRP B 47 19497 14999 9906 -761 292 -2464 C
ATOM 2391 N VAL B 48 -44.192 4.515 67.591 1.00101.92 N
ANISOU 2391 N VAL B 48 17515 12671 8538 -1152 558 -2186 N
ATOM 2392 CA VAL B 48 -44.025 5.951 67.347 1.00 97.61 C
ANISOU 2392 CA VAL B 48 16716 12401 7972 -846 393 -2048 C
ATOM 2393 C VAL B 48 -43.016 6.556 68.326 1.00 89.37 C
ANISOU 2393 C VAL B 48 15710 11109 7139 -664 473 -1736 C
ATOM 2394 O VAL B 48 -42.174 7.380 67.944 1.00 84.18 O
ANISOU 2394 O VAL B 48 14987 10463 6537 -429 425 -1562 O
ATOM 2395 CB VAL B 48 -45.401 6.659 67.428 1.00 98.10 C
ANISOU 2395 CB VAL B 48 16519 12871 7882 -875 239 -2233 C
ATOM 2396 CG1 VAL B 48 -45.279 8.181 67.314 1.00 92.72 C
ANISOU 2396 CG1 VAL B 48 15618 12440 7171 -568 106 -2065 C
ATOM 2397 CG2 VAL B 48 -46.365 6.134 66.360 1.00103.85 C
ANISOU 2397 CG2 VAL B 48 17185 13889 8383 -1021 99 -2578 C
ATOM 2398 N LEU B 49 -43.080 6.139 69.600 1.00 85.30 N
ANISOU 2398 N LEU B 49 15320 10356 6735 -787 605 -1675 N
ATOM 2399 CA LEU B 49 -42.168 6.615 70.642 1.00 81.76 C
ANISOU 2399 CA LEU B 49 14916 9683 6467 -620 660 -1417 C
ATOM 2400 C LEU B 49 -40.705 6.277 70.323 1.00 84.37 C
ANISOU 2400 C LEU B 49 15421 9738 6899 -464 708 -1257 C
ATOM 2401 O LEU B 49 -39.832 7.149 70.401 1.00 85.54 O
ANISOU 2401 O LEU B 49 15479 9868 7154 -243 662 -1095 O
ATOM 2402 CB LEU B 49 -42.577 6.023 72.000 1.00 81.41 C
ANISOU 2402 CB LEU B 49 15033 9434 6463 -801 805 -1406 C
ATOM 2403 CG LEU B 49 -41.742 6.344 73.250 1.00 84.19 C
ANISOU 2403 CG LEU B 49 15468 9556 6962 -645 855 -1174 C
ATOM 2404 CD1 LEU B 49 -41.779 7.824 73.548 1.00 85.81 C
ANISOU 2404 CD1 LEU B 49 15383 9990 7230 -452 733 -1098 C
ATOM 2405 CD2 LEU B 49 -42.201 5.561 74.472 1.00 86.70 C
ANISOU 2405 CD2 LEU B 49 16026 9654 7263 -847 1028 -1173 C
ATOM 2406 N ILE B 50 -40.419 5.007 69.982 1.00 85.45 N
ANISOU 2406 N ILE B 50 15823 9647 6998 -588 818 -1319 N
ATOM 2407 CA ILE B 50 -39.052 4.586 69.650 1.00 81.42 C
ANISOU 2407 CA ILE B 50 15498 8883 6555 -429 876 -1194 C
ATOM 2408 C ILE B 50 -38.586 5.240 68.340 1.00 80.28 C
ANISOU 2408 C ILE B 50 15200 8928 6374 -280 783 -1207 C
ATOM 2409 O ILE B 50 -37.466 5.757 68.259 1.00 80.22 O
ANISOU 2409 O ILE B 50 15181 8837 6462 -73 784 -1062 O
ATOM 2410 CB ILE B 50 -38.942 3.037 69.595 1.00 80.77 C
ANISOU 2410 CB ILE B 50 15776 8498 6416 -597 1040 -1265 C
ATOM 2411 CG1 ILE B 50 -39.336 2.384 70.937 1.00 75.61 C
ANISOU 2411 CG1 ILE B 50 15355 7599 5775 -746 1179 -1216 C
ATOM 2412 CG2 ILE B 50 -37.513 2.576 69.216 1.00 80.82 C
ANISOU 2412 CG2 ILE B 50 15983 8259 6468 -397 1104 -1150 C
ATOM 2413 CD1 ILE B 50 -39.689 0.868 70.876 1.00 73.23 C
ANISOU 2413 CD1 ILE B 50 15428 7016 5379 -1017 1386 -1333 C
ATOM 2414 N ALA B 51 -39.454 5.256 67.315 1.00 79.19 N
ANISOU 2414 N ALA B 51 14951 9061 6076 -384 706 -1394 N
ATOM 2415 CA ALA B 51 -39.125 5.869 66.024 1.00 75.35 C
ANISOU 2415 CA ALA B 51 14359 8771 5501 -248 627 -1406 C
ATOM 2416 C ALA B 51 -38.773 7.353 66.166 1.00 71.48 C
ANISOU 2416 C ALA B 51 13676 8397 5085 -41 555 -1232 C
ATOM 2417 O ALA B 51 -37.808 7.830 65.556 1.00 68.63 O
ANISOU 2417 O ALA B 51 13341 7978 4755 115 582 -1127 O
ATOM 2418 CB ALA B 51 -40.295 5.688 65.050 1.00 75.51 C
ANISOU 2418 CB ALA B 51 14281 9119 5291 -381 520 -1656 C
ATOM 2419 N ALA B 52 -39.561 8.091 66.962 1.00 67.98 N
ANISOU 2419 N ALA B 52 13063 8101 4664 -50 487 -1214 N
ATOM 2420 CA ALA B 52 -39.306 9.512 67.212 1.00 62.21 C
ANISOU 2420 CA ALA B 52 12182 7443 4010 128 439 -1058 C
ATOM 2421 C ALA B 52 -37.991 9.729 67.960 1.00 65.98 C
ANISOU 2421 C ALA B 52 12741 7626 4701 252 526 -884 C
ATOM 2422 O ALA B 52 -37.235 10.654 67.641 1.00 72.75 O
ANISOU 2422 O ALA B 52 13572 8456 5616 406 537 -774 O
ATOM 2423 CB ALA B 52 -40.471 10.118 68.001 1.00 55.36 C
ANISOU 2423 CB ALA B 52 11141 6780 3112 82 366 -1101 C
ATOM 2424 N TYR B 53 -37.711 8.886 68.965 1.00 63.46 N
ANISOU 2424 N TYR B 53 12545 7089 4478 189 594 -867 N
ATOM 2425 CA TYR B 53 -36.465 8.984 69.729 1.00 62.91 C
ANISOU 2425 CA TYR B 53 12554 6782 4566 326 651 -731 C
ATOM 2426 C TYR B 53 -35.245 8.633 68.871 1.00 67.75 C
ANISOU 2426 C TYR B 53 13298 7260 5184 431 720 -705 C
ATOM 2427 O TYR B 53 -34.212 9.305 68.962 1.00 70.93 O
ANISOU 2427 O TYR B 53 13675 7600 5676 583 745 -618 O
ATOM 2428 CB TYR B 53 -36.541 8.083 70.975 1.00 64.33 C
ANISOU 2428 CB TYR B 53 12883 6772 4786 254 701 -715 C
ATOM 2429 CG TYR B 53 -36.941 8.786 72.274 1.00 69.26 C
ANISOU 2429 CG TYR B 53 13392 7439 5483 266 665 -661 C
ATOM 2430 CD1 TYR B 53 -38.261 8.776 72.711 1.00 72.28 C
ANISOU 2430 CD1 TYR B 53 13704 7961 5799 107 652 -741 C
ATOM 2431 CD2 TYR B 53 -36.012 9.493 73.038 1.00 67.98 C
ANISOU 2431 CD2 TYR B 53 13187 7205 5438 431 649 -556 C
ATOM 2432 CE1 TYR B 53 -38.644 9.425 73.881 1.00 71.63 C
ANISOU 2432 CE1 TYR B 53 13524 7924 5767 118 637 -701 C
ATOM 2433 CE2 TYR B 53 -36.388 10.139 74.221 1.00 65.65 C
ANISOU 2433 CE2 TYR B 53 12793 6957 5193 437 619 -525 C
ATOM 2434 CZ TYR B 53 -37.708 10.103 74.632 1.00 66.91 C
ANISOU 2434 CZ TYR B 53 12895 7239 5290 284 618 -589 C
ATOM 2435 OH TYR B 53 -38.103 10.742 75.792 1.00 62.21 O
ANISOU 2435 OH TYR B 53 12211 6697 4730 291 605 -567 O
ATOM 2436 N VAL B 54 -35.349 7.591 68.026 1.00 67.45 N
ANISOU 2436 N VAL B 54 13406 7185 5038 343 764 -801 N
ATOM 2437 CA VAL B 54 -34.230 7.180 67.168 1.00 69.97 C
ANISOU 2437 CA VAL B 54 13862 7381 5340 441 851 -795 C
ATOM 2438 C VAL B 54 -33.951 8.242 66.101 1.00 72.31 C
ANISOU 2438 C VAL B 54 14047 7833 5594 531 838 -774 C
ATOM 2439 O VAL B 54 -32.795 8.624 65.876 1.00 76.25 O
ANISOU 2439 O VAL B 54 14579 8242 6151 669 917 -707 O
ATOM 2440 CB VAL B 54 -34.502 5.788 66.546 1.00 71.54 C
ANISOU 2440 CB VAL B 54 14267 7494 5422 310 914 -923 C
ATOM 2441 CG1 VAL B 54 -33.475 5.433 65.457 1.00 77.29 C
ANISOU 2441 CG1 VAL B 54 15121 8143 6103 407 1009 -944 C
ATOM 2442 CG2 VAL B 54 -34.497 4.689 67.618 1.00 67.22 C
ANISOU 2442 CG2 VAL B 54 13936 6695 4912 252 984 -904 C
ATOM 2443 N ALA B 55 -35.009 8.755 65.452 1.00 70.17 N
ANISOU 2443 N ALA B 55 13660 7804 5198 463 749 -833 N
ATOM 2444 CA ALA B 55 -34.875 9.820 64.453 1.00 67.88 C
ANISOU 2444 CA ALA B 55 13316 7652 4825 564 740 -788 C
ATOM 2445 C ALA B 55 -34.199 11.061 65.039 1.00 70.87 C
ANISOU 2445 C ALA B 55 13626 7954 5346 701 774 -645 C
ATOM 2446 O ALA B 55 -33.290 11.632 64.425 1.00 76.47 O
ANISOU 2446 O ALA B 55 14400 8596 6057 808 871 -583 O
ATOM 2447 CB ALA B 55 -36.250 10.188 63.889 1.00 63.78 C
ANISOU 2447 CB ALA B 55 12681 7434 4116 499 610 -869 C
ATOM 2448 N VAL B 56 -34.655 11.500 66.219 1.00 64.82 N
ANISOU 2448 N VAL B 56 12742 7199 4686 687 711 -608 N
ATOM 2449 CA VAL B 56 -34.063 12.659 66.885 1.00 61.13 C
ANISOU 2449 CA VAL B 56 12218 6660 4350 799 744 -503 C
ATOM 2450 C VAL B 56 -32.605 12.371 67.265 1.00 66.36 C
ANISOU 2450 C VAL B 56 12961 7126 5126 875 852 -474 C
ATOM 2451 O VAL B 56 -31.719 13.201 67.034 1.00 73.35 O
ANISOU 2451 O VAL B 56 13865 7957 6048 969 947 -424 O
ATOM 2452 CB VAL B 56 -34.931 13.077 68.100 1.00 60.62 C
ANISOU 2452 CB VAL B 56 12017 6663 4352 758 655 -494 C
ATOM 2453 CG1 VAL B 56 -34.124 13.820 69.169 1.00 62.88 C
ANISOU 2453 CG1 VAL B 56 12271 6828 4795 843 695 -425 C
ATOM 2454 CG2 VAL B 56 -36.109 13.960 67.647 1.00 52.34 C
ANISOU 2454 CG2 VAL B 56 10876 5828 3181 769 574 -495 C
ATOM 2455 N PHE B 57 -32.330 11.164 67.784 1.00 69.73 N
ANISOU 2455 N PHE B 57 13462 7450 5583 842 856 -513 N
ATOM 2456 CA PHE B 57 -30.972 10.759 68.159 1.00 67.42 C
ANISOU 2456 CA PHE B 57 13251 7009 5358 950 943 -501 C
ATOM 2457 C PHE B 57 -29.994 10.853 66.973 1.00 72.14 C
ANISOU 2457 C PHE B 57 13925 7580 5904 1021 1079 -516 C
ATOM 2458 O PHE B 57 -28.918 11.449 67.103 1.00 70.85 O
ANISOU 2458 O PHE B 57 13736 7386 5797 1121 1175 -503 O
ATOM 2459 CB PHE B 57 -31.010 9.340 68.760 1.00 61.17 C
ANISOU 2459 CB PHE B 57 12594 6092 4554 925 930 -529 C
ATOM 2460 CG PHE B 57 -29.661 8.777 69.193 1.00 59.38 C
ANISOU 2460 CG PHE B 57 12474 5731 4356 1086 1001 -523 C
ATOM 2461 CD1 PHE B 57 -29.123 9.069 70.443 1.00 57.08 C
ANISOU 2461 CD1 PHE B 57 12136 5422 4130 1198 956 -490 C
ATOM 2462 CD2 PHE B 57 -28.964 7.905 68.366 1.00 55.52 C
ANISOU 2462 CD2 PHE B 57 12136 5154 3806 1141 1106 -569 C
ATOM 2463 CE1 PHE B 57 -27.897 8.534 70.836 1.00 58.74 C
ANISOU 2463 CE1 PHE B 57 12432 5556 4331 1387 1000 -511 C
ATOM 2464 CE2 PHE B 57 -27.741 7.370 68.754 1.00 54.78 C
ANISOU 2464 CE2 PHE B 57 12128 4964 3721 1326 1171 -583 C
ATOM 2465 CZ PHE B 57 -27.209 7.684 69.989 1.00 56.47 C
ANISOU 2465 CZ PHE B 57 12281 5187 3988 1461 1110 -557 C
ATOM 2466 N VAL B 58 -30.352 10.288 65.805 1.00 74.53 N
ANISOU 2466 N VAL B 58 14321 7912 6086 962 1104 -565 N
ATOM 2467 CA VAL B 58 -29.438 10.327 64.659 1.00 76.02 C
ANISOU 2467 CA VAL B 58 14603 8073 6209 1027 1254 -585 C
ATOM 2468 C VAL B 58 -29.339 11.750 64.077 1.00 76.83 C
ANISOU 2468 C VAL B 58 14665 8241 6287 1066 1318 -518 C
ATOM 2469 O VAL B 58 -28.230 12.265 63.888 1.00 76.43 O
ANISOU 2469 O VAL B 58 14637 8129 6274 1142 1481 -504 O
ATOM 2470 CB VAL B 58 -29.788 9.250 63.590 1.00 78.55 C
ANISOU 2470 CB VAL B 58 15058 8402 6384 957 1272 -674 C
ATOM 2471 CG1 VAL B 58 -31.246 9.270 63.113 1.00 83.24 C
ANISOU 2471 CG1 VAL B 58 15613 9166 6850 830 1135 -716 C
ATOM 2472 CG2 VAL B 58 -28.825 9.308 62.386 1.00 73.49 C
ANISOU 2472 CG2 VAL B 58 14524 7736 5662 1027 1449 -698 C
ATOM 2473 N VAL B 59 -30.481 12.429 63.849 1.00 76.43 N
ANISOU 2473 N VAL B 59 14563 8311 6167 1022 1208 -482 N
ATOM 2474 CA VAL B 59 -30.481 13.797 63.297 1.00 70.53 C
ANISOU 2474 CA VAL B 59 13838 7589 5369 1088 1276 -396 C
ATOM 2475 C VAL B 59 -29.681 14.764 64.187 1.00 66.89 C
ANISOU 2475 C VAL B 59 13330 7025 5061 1143 1373 -341 C
ATOM 2476 O VAL B 59 -28.888 15.571 63.685 1.00 70.49 O
ANISOU 2476 O VAL B 59 13872 7404 5508 1195 1562 -299 O
ATOM 2477 CB VAL B 59 -31.930 14.294 63.056 1.00 68.26 C
ANISOU 2477 CB VAL B 59 13498 7473 4965 1070 1116 -373 C
ATOM 2478 CG1 VAL B 59 -31.996 15.813 62.785 1.00 65.31 C
ANISOU 2478 CG1 VAL B 59 13177 7082 4556 1178 1180 -256 C
ATOM 2479 CG2 VAL B 59 -32.581 13.555 61.878 1.00 69.22 C
ANISOU 2479 CG2 VAL B 59 13684 7746 4873 1022 1054 -447 C
ATOM 2480 N ALA B 60 -29.855 14.688 65.517 1.00 65.47 N
ANISOU 2480 N ALA B 60 13024 6843 5009 1122 1268 -354 N
ATOM 2481 CA ALA B 60 -29.114 15.569 66.426 1.00 66.32 C
ANISOU 2481 CA ALA B 60 13072 6888 5237 1162 1346 -337 C
ATOM 2482 C ALA B 60 -27.611 15.258 66.451 1.00 74.87 C
ANISOU 2482 C ALA B 60 14167 7909 6371 1205 1515 -406 C
ATOM 2483 O ALA B 60 -26.792 16.173 66.573 1.00 79.99 O
ANISOU 2483 O ALA B 60 14800 8520 7073 1223 1681 -422 O
ATOM 2484 CB ALA B 60 -29.692 15.491 67.843 1.00 59.20 C
ANISOU 2484 CB ALA B 60 12039 6025 4428 1134 1182 -348 C
ATOM 2485 N LEU B 61 -27.231 13.971 66.357 1.00 75.06 N
ANISOU 2485 N LEU B 61 14214 7926 6380 1223 1496 -470 N
ATOM 2486 CA LEU B 61 -25.810 13.609 66.391 1.00 73.70 C
ANISOU 2486 CA LEU B 61 14025 7725 6251 1302 1654 -567 C
ATOM 2487 C LEU B 61 -25.090 14.043 65.116 1.00 79.09 C
ANISOU 2487 C LEU B 61 14792 8377 6882 1304 1904 -580 C
ATOM 2488 O LEU B 61 -23.997 14.619 65.176 1.00 82.20 O
ANISOU 2488 O LEU B 61 15118 8764 7350 1331 2109 -659 O
ATOM 2489 CB LEU B 61 -25.631 12.099 66.617 1.00 74.46 C
ANISOU 2489 CB LEU B 61 14168 7791 6331 1357 1580 -623 C
ATOM 2490 CG LEU B 61 -25.763 11.546 68.046 1.00 77.80 C
ANISOU 2490 CG LEU B 61 14542 8210 6810 1411 1412 -633 C
ATOM 2491 CD1 LEU B 61 -25.251 10.115 68.143 1.00 76.82 C
ANISOU 2491 CD1 LEU B 61 14529 8005 6653 1521 1415 -686 C
ATOM 2492 CD2 LEU B 61 -25.065 12.425 69.083 1.00 80.67 C
ANISOU 2492 CD2 LEU B 61 14749 8638 7265 1478 1416 -694 C
ATOM 2493 N VAL B 62 -25.684 13.754 63.949 1.00 78.34 N
ANISOU 2493 N VAL B 62 14837 8273 6655 1268 1907 -528 N
ATOM 2494 CA VAL B 62 -25.111 14.159 62.662 1.00 76.97 C
ANISOU 2494 CA VAL B 62 14786 8062 6396 1272 2148 -519 C
ATOM 2495 C VAL B 62 -25.097 15.680 62.551 1.00 78.28 C
ANISOU 2495 C VAL B 62 14987 8181 6575 1253 2287 -431 C
ATOM 2496 O VAL B 62 -24.054 16.296 62.290 1.00 79.27 O
ANISOU 2496 O VAL B 62 15122 8243 6752 1246 2571 -466 O
ATOM 2497 CB VAL B 62 -25.898 13.505 61.502 1.00 78.25 C
ANISOU 2497 CB VAL B 62 15094 8257 6380 1247 2075 -498 C
ATOM 2498 CG1 VAL B 62 -25.479 14.055 60.134 1.00 62.60 C
ANISOU 2498 CG1 VAL B 62 13276 6243 4267 1259 2308 -462 C
ATOM 2499 CG2 VAL B 62 -25.744 11.982 61.519 1.00 60.29 C
ANISOU 2499 CG2 VAL B 62 12834 5979 4095 1253 2015 -601 C
ATOM 2500 N GLY B 63 -26.253 16.304 62.804 1.00 78.12 N
ANISOU 2500 N GLY B 63 14981 8180 6523 1242 2114 -332 N
ATOM 2501 CA GLY B 63 -26.382 17.750 62.695 1.00 71.94 C
ANISOU 2501 CA GLY B 63 14283 7314 5736 1250 2243 -232 C
ATOM 2502 C GLY B 63 -25.429 18.526 63.590 1.00 69.79 C
ANISOU 2502 C GLY B 63 13917 6971 5629 1214 2428 -288 C
ATOM 2503 O GLY B 63 -24.779 19.472 63.141 1.00 74.72 O
ANISOU 2503 O GLY B 63 14645 7473 6271 1185 2727 -264 O
ATOM 2504 N ASN B 64 -25.349 18.155 64.873 1.00 67.91 N
ANISOU 2504 N ASN B 64 13485 6809 5510 1205 2269 -380 N
ATOM 2505 CA ASN B 64 -24.512 18.904 65.811 1.00 69.55 C
ANISOU 2505 CA ASN B 64 13561 6997 5869 1168 2410 -488 C
ATOM 2506 C ASN B 64 -23.016 18.664 65.599 1.00 76.14 C
ANISOU 2506 C ASN B 64 14291 7839 6800 1159 2677 -667 C
ATOM 2507 O ASN B 64 -22.211 19.529 65.958 1.00 80.77 O
ANISOU 2507 O ASN B 64 14779 8383 7526 1094 2909 -789 O
ATOM 2508 CB ASN B 64 -24.916 18.581 67.254 1.00 65.92 C
ANISOU 2508 CB ASN B 64 12927 6638 5482 1186 2136 -549 C
ATOM 2509 CG ASN B 64 -26.191 19.298 67.674 1.00 71.54 C
ANISOU 2509 CG ASN B 64 13688 7331 6164 1174 1977 -422 C
ATOM 2510 OD1 ASN B 64 -26.230 20.527 67.741 1.00 82.94 O
ANISOU 2510 OD1 ASN B 64 15199 8679 7635 1145 2123 -386 O
ATOM 2511 ND2 ASN B 64 -27.242 18.535 67.951 1.00 66.71 N
ANISOU 2511 ND2 ASN B 64 13044 6796 5506 1192 1708 -369 N
ATOM 2512 N THR B 65 -22.629 17.522 65.020 1.00 79.12 N
ANISOU 2512 N THR B 65 14669 8266 7126 1216 2669 -714 N
ATOM 2513 CA THR B 65 -21.224 17.305 64.671 1.00 81.68 C
ANISOU 2513 CA THR B 65 14881 8604 7549 1231 2952 -898 C
ATOM 2514 C THR B 65 -20.841 18.166 63.471 1.00 84.91 C
ANISOU 2514 C THR B 65 15449 8884 7928 1139 3321 -830 C
ATOM 2515 O THR B 65 -19.757 18.766 63.448 1.00 86.64 O
ANISOU 2515 O THR B 65 15545 9069 8307 1068 3652 -980 O
ATOM 2516 CB THR B 65 -20.985 15.809 64.397 1.00 80.46 C
ANISOU 2516 CB THR B 65 14714 8517 7340 1342 2843 -961 C
ATOM 2517 OG1 THR B 65 -21.340 15.047 65.559 1.00 80.31 O
ANISOU 2517 OG1 THR B 65 14595 8571 7347 1427 2535 -999 O
ATOM 2518 CG2 THR B 65 -19.524 15.503 64.038 1.00 82.41 C
ANISOU 2518 CG2 THR B 65 14810 8797 7705 1399 3132 -1179 C
ATOM 2519 N LEU B 66 -21.758 18.292 62.503 1.00 82.38 N
ANISOU 2519 N LEU B 66 15396 8486 7417 1136 3273 -618 N
ATOM 2520 CA LEU B 66 -21.563 19.134 61.327 1.00 78.95 C
ANISOU 2520 CA LEU B 66 15188 7901 6907 1080 3595 -509 C
ATOM 2521 C LEU B 66 -21.504 20.623 61.668 1.00 80.84 C
ANISOU 2521 C LEU B 66 15486 7982 7248 986 3817 -457 C
ATOM 2522 O LEU B 66 -20.914 21.390 60.901 1.00 80.75 O
ANISOU 2522 O LEU B 66 15617 7807 7256 904 4202 -423 O
ATOM 2523 CB LEU B 66 -22.672 18.862 60.294 1.00 74.83 C
ANISOU 2523 CB LEU B 66 14920 7370 6140 1152 3415 -330 C
ATOM 2524 CG LEU B 66 -22.659 17.505 59.567 1.00 73.31 C
ANISOU 2524 CG LEU B 66 14747 7281 5827 1202 3310 -387 C
ATOM 2525 CD1 LEU B 66 -23.711 17.440 58.468 1.00 74.30 C
ANISOU 2525 CD1 LEU B 66 15101 7420 5709 1253 3174 -256 C
ATOM 2526 CD2 LEU B 66 -21.286 17.187 58.992 1.00 70.55 C
ANISOU 2526 CD2 LEU B 66 14359 6910 5535 1176 3658 -518 C
ATOM 2527 N VAL B 67 -22.097 21.043 62.799 1.00 82.93 N
ANISOU 2527 N VAL B 67 15658 8270 7581 987 3608 -454 N
ATOM 2528 CA VAL B 67 -21.970 22.428 63.265 1.00 82.63 C
ANISOU 2528 CA VAL B 67 15660 8067 7669 885 3839 -446 C
ATOM 2529 C VAL B 67 -20.532 22.700 63.721 1.00 85.55 C
ANISOU 2529 C VAL B 67 15767 8436 8301 738 4173 -717 C
ATOM 2530 O VAL B 67 -19.893 23.658 63.264 1.00 87.09 O
ANISOU 2530 O VAL B 67 16046 8435 8608 589 4605 -734 O
ATOM 2531 CB VAL B 67 -23.002 22.722 64.379 1.00 78.85 C
ANISOU 2531 CB VAL B 67 15135 7634 7189 932 3514 -399 C
ATOM 2532 CG1 VAL B 67 -22.746 24.075 65.064 1.00 81.55 C
ANISOU 2532 CG1 VAL B 67 15477 7813 7696 810 3758 -455 C
ATOM 2533 CG2 VAL B 67 -24.440 22.691 63.834 1.00 75.50 C
ANISOU 2533 CG2 VAL B 67 14933 7200 6552 1069 3247 -168 C
ATOM 2534 N CYS B 68 -19.992 21.826 64.586 1.00 87.80 N
ANISOU 2534 N CYS B 68 15724 8935 8702 788 3988 -954 N
ATOM 2535 CA CYS B 68 -18.622 21.950 65.097 1.00 89.73 C
ANISOU 2535 CA CYS B 68 15628 9241 9225 699 4239 -1288 C
ATOM 2536 C CYS B 68 -17.579 21.875 63.978 1.00 90.88 C
ANISOU 2536 C CYS B 68 15762 9330 9437 621 4657 -1357 C
ATOM 2537 O CYS B 68 -16.595 22.622 63.988 1.00 95.34 O
ANISOU 2537 O CYS B 68 16151 9819 10254 438 5057 -1556 O
ATOM 2538 CB CYS B 68 -18.352 20.857 66.137 1.00 86.84 C
ANISOU 2538 CB CYS B 68 14962 9121 8912 865 3894 -1506 C
ATOM 2539 SG CYS B 68 -19.493 20.842 67.542 1.00 88.27 S
ANISOU 2539 SG CYS B 68 15136 9382 9022 945 3412 -1445 S
ATOM 2540 N LEU B 69 -17.771 20.953 63.022 1.00 85.78 N
ANISOU 2540 N LEU B 69 15279 8724 8588 738 4580 -1221 N
ATOM 2541 CA LEU B 69 -16.859 20.804 61.888 1.00 91.10 C
ANISOU 2541 CA LEU B 69 15974 9351 9289 680 4962 -1269 C
ATOM 2542 C LEU B 69 -16.869 22.038 60.984 1.00 92.12 C
ANISOU 2542 C LEU B 69 16398 9204 9400 498 5374 -1095 C
ATOM 2543 O LEU B 69 -15.823 22.434 60.455 1.00 94.23 O
ANISOU 2543 O LEU B 69 16580 9386 9838 341 5829 -1222 O
ATOM 2544 CB LEU B 69 -17.233 19.552 61.083 1.00 93.91 C
ANISOU 2544 CB LEU B 69 16485 9793 9403 847 4751 -1157 C
ATOM 2545 CG LEU B 69 -16.743 18.189 61.587 1.00 92.71 C
ANISOU 2545 CG LEU B 69 16066 9854 9307 1021 4533 -1370 C
ATOM 2546 CD1 LEU B 69 -17.564 17.049 60.999 1.00 88.85 C
ANISOU 2546 CD1 LEU B 69 15802 9397 8561 1149 4241 -1212 C
ATOM 2547 CD2 LEU B 69 -15.269 17.996 61.261 1.00 97.94 C
ANISOU 2547 CD2 LEU B 69 16453 10580 10179 1009 4904 -1641 C
ATOM 2548 N ALA B 70 -18.054 22.636 60.788 1.00 89.65 N
ANISOU 2548 N ALA B 70 16435 8740 8888 534 5223 -809 N
ATOM 2549 CA ALA B 70 -18.215 23.806 59.923 1.00 87.52 C
ANISOU 2549 CA ALA B 70 16526 8167 8559 434 5571 -608 C
ATOM 2550 C ALA B 70 -17.476 25.030 60.458 1.00 90.54 C
ANISOU 2550 C ALA B 70 16797 8355 9249 183 5995 -752 C
ATOM 2551 O ALA B 70 -16.804 25.736 59.695 1.00 96.25 O
ANISOU 2551 O ALA B 70 17657 8847 10066 13 6479 -745 O
ATOM 2552 CB ALA B 70 -19.702 24.130 59.761 1.00 79.81 C
ANISOU 2552 CB ALA B 70 15890 7110 7324 600 5247 -317 C
ATOM 2553 N VAL B 71 -17.570 25.283 61.771 1.00 89.43 N
ANISOU 2553 N VAL B 71 16400 8297 9282 138 5831 -912 N
ATOM 2554 CA VAL B 71 -16.887 26.434 62.357 1.00 95.53 C
ANISOU 2554 CA VAL B 71 17024 8893 10379 -134 6222 -1110 C
ATOM 2555 C VAL B 71 -15.386 26.151 62.440 1.00100.94 C
ANISOU 2555 C VAL B 71 17253 9712 11390 -315 6534 -1490 C
ATOM 2556 O VAL B 71 -14.571 27.061 62.267 1.00105.12 O
ANISOU 2556 O VAL B 71 17709 10038 12192 -608 7037 -1639 O
ATOM 2557 CB VAL B 71 -17.504 26.787 63.739 1.00 94.76 C
ANISOU 2557 CB VAL B 71 16790 8860 10356 -115 5917 -1193 C
ATOM 2558 CG1 VAL B 71 -16.834 28.010 64.385 1.00 98.93 C
ANISOU 2558 CG1 VAL B 71 17153 9194 11243 -427 6315 -1444 C
ATOM 2559 CG2 VAL B 71 -19.014 27.040 63.633 1.00 94.91 C
ANISOU 2559 CG2 VAL B 71 17219 8773 10068 84 5608 -829 C
ATOM 2560 N TRP B 72 -15.008 24.864 62.528 1.00101.68 N
ANISOU 2560 N TRP B 72 17067 10120 11448 -136 6276 -1636 N
ATOM 2561 CA TRP B 72 -13.594 24.481 62.524 1.00104.41 C
ANISOU 2561 CA TRP B 72 16954 10627 12089 -236 6543 -2002 C
ATOM 2562 C TRP B 72 -12.983 24.607 61.125 1.00106.75 C
ANISOU 2562 C TRP B 72 17431 10762 12367 -360 7009 -1909 C
ATOM 2563 O TRP B 72 -11.874 25.125 60.978 1.00112.47 O
ANISOU 2563 O TRP B 72 17888 11430 13415 -622 7472 -2161 O
ATOM 2564 CB TRP B 72 -13.426 23.051 63.061 1.00101.50 C
ANISOU 2564 CB TRP B 72 16284 10610 11670 60 6115 -2169 C
ATOM 2565 CG TRP B 72 -12.046 22.479 62.840 1.00105.35 C
ANISOU 2565 CG TRP B 72 16340 11283 12407 55 6360 -2503 C
ATOM 2566 CD1 TRP B 72 -10.913 22.774 63.543 1.00107.82 C
ANISOU 2566 CD1 TRP B 72 16097 11741 13129 -84 6553 -2938 C
ATOM 2567 CD2 TRP B 72 -11.658 21.524 61.841 1.00108.81 C
ANISOU 2567 CD2 TRP B 72 16832 11797 12715 199 6433 -2454 C
ATOM 2568 NE1 TRP B 72 -9.845 22.066 63.043 1.00113.07 N
ANISOU 2568 NE1 TRP B 72 16451 12577 13933 -15 6740 -3151 N
ATOM 2569 CE2 TRP B 72 -10.276 21.291 61.999 1.00113.38 C
ANISOU 2569 CE2 TRP B 72 16878 12563 13638 163 6682 -2853 C
ATOM 2570 CE3 TRP B 72 -12.345 20.845 60.830 1.00107.42 C
ANISOU 2570 CE3 TRP B 72 17078 11558 12176 351 6306 -2140 C
ATOM 2571 CZ2 TRP B 72 -9.569 20.408 61.180 1.00115.03 C
ANISOU 2571 CZ2 TRP B 72 16994 12883 13828 293 6823 -2922 C
ATOM 2572 CZ3 TRP B 72 -11.642 19.968 60.019 1.00108.52 C
ANISOU 2572 CZ3 TRP B 72 17142 11798 12294 454 6448 -2225 C
ATOM 2573 CH2 TRP B 72 -10.269 19.758 60.200 1.00112.04 C
ANISOU 2573 CH2 TRP B 72 17080 12414 13074 435 6711 -2601 C
ATOM 2574 N ARG B 73 -13.730 24.196 60.088 1.00102.40 N
ANISOU 2574 N ARG B 73 17332 10128 11447 -191 6892 -1564 N
ATOM 2575 CA ARG B 73 -13.230 24.271 58.713 1.00104.33 C
ANISOU 2575 CA ARG B 73 17803 10216 11620 -272 7295 -1463 C
ATOM 2576 C ARG B 73 -13.117 25.719 58.234 1.00110.31 C
ANISOU 2576 C ARG B 73 18855 10579 12480 -542 7788 -1349 C
ATOM 2577 O ARG B 73 -12.019 26.219 57.996 1.00115.46 O
ANISOU 2577 O ARG B 73 19313 11127 13429 -814 8287 -1561 O
ATOM 2578 CB ARG B 73 -14.140 23.457 57.778 1.00102.73 C
ANISOU 2578 CB ARG B 73 18001 10046 10988 -9 6988 -1161 C
ATOM 2579 CG ARG B 73 -13.665 23.384 56.322 1.00111.27 C
ANISOU 2579 CG ARG B 73 19333 11004 11943 -45 7348 -1071 C
ATOM 2580 CD ARG B 73 -14.443 22.358 55.501 1.00111.60 C
ANISOU 2580 CD ARG B 73 19652 11157 11595 214 7001 -879 C
ATOM 2581 NE ARG B 73 -13.972 22.303 54.118 1.00116.61 N
ANISOU 2581 NE ARG B 73 20529 11685 12091 184 7349 -816 N
ATOM 2582 CZ ARG B 73 -14.770 22.201 53.061 1.00118.54 C
ANISOU 2582 CZ ARG B 73 21216 11853 11971 328 7229 -566 C
ATOM 2583 NH1 ARG B 73 -16.085 22.148 53.224 1.00114.24 N
ANISOU 2583 NH1 ARG B 73 20879 11336 11190 505 6770 -369 N
ATOM 2584 NH2 ARG B 73 -14.257 22.160 51.838 1.00124.89 N
ANISOU 2584 NH2 ARG B 73 22231 12571 12650 298 7569 -537 N
ATOM 2585 N ASN B 74 -14.250 26.444 58.186 1.00116.84 N
ANISOU 2585 N ASN B 74 18137 12469 13789 264 8392 -48 N
ATOM 2586 CA ASN B 74 -14.291 27.822 57.696 1.00107.30 C
ANISOU 2586 CA ASN B 74 17093 11153 12522 114 8585 139 C
ATOM 2587 C ASN B 74 -13.773 28.766 58.784 1.00113.27 C
ANISOU 2587 C ASN B 74 17424 11865 13750 -26 8578 157 C
ATOM 2588 O ASN B 74 -14.388 28.869 59.859 1.00108.86 O
ANISOU 2588 O ASN B 74 16723 11265 13375 -20 8234 144 O
ATOM 2589 CB ASN B 74 -15.733 28.172 57.302 1.00105.19 C
ANISOU 2589 CB ASN B 74 17296 10784 11889 135 8322 285 C
ATOM 2590 CG ASN B 74 -15.875 29.426 56.409 1.00108.86 C
ANISOU 2590 CG ASN B 74 18076 11146 12139 25 8538 491 C
ATOM 2591 OD1 ASN B 74 -15.168 30.423 56.567 1.00110.90 O
ANISOU 2591 OD1 ASN B 74 18141 11354 12642 -116 8771 562 O
ATOM 2592 ND2 ASN B 74 -16.861 29.390 55.511 1.00109.70 N
ANISOU 2592 ND2 ASN B 74 18678 11219 11782 85 8426 594 N
ATOM 2593 N HIS B 75 -12.740 29.548 58.466 1.00115.39 N
ANISOU 2593 N HIS B 75 17532 12128 14183 -163 8958 205 N
ATOM 2594 CA HIS B 75 -12.126 30.453 59.429 1.00112.17 C
ANISOU 2594 CA HIS B 75 16721 11672 14228 -319 8988 207 C
ATOM 2595 C HIS B 75 -12.824 31.805 59.481 1.00108.82 C
ANISOU 2595 C HIS B 75 16516 11065 13766 -444 8925 387 C
ATOM 2596 O HIS B 75 -12.612 32.558 60.437 1.00107.27 O
ANISOU 2596 O HIS B 75 16041 10793 13922 -558 8854 381 O
ATOM 2597 CB HIS B 75 -10.628 30.656 59.121 1.00116.77 C
ANISOU 2597 CB HIS B 75 16978 12344 15044 -427 9432 170 C
ATOM 2598 CG HIS B 75 -9.836 29.383 59.124 1.00119.01 C
ANISOU 2598 CG HIS B 75 16996 12821 15400 -283 9514 -13 C
ATOM 2599 ND1 HIS B 75 -9.411 28.794 60.290 1.00116.81 N
ANISOU 2599 ND1 HIS B 75 16263 12635 15483 -226 9300 -176 N
ATOM 2600 CD2 HIS B 75 -9.333 28.634 58.115 1.00123.72 C
ANISOU 2600 CD2 HIS B 75 17708 13539 15762 -176 9802 -60 C
ATOM 2601 CE1 HIS B 75 -8.734 27.697 60.009 1.00118.97 C
ANISOU 2601 CE1 HIS B 75 16389 13077 15736 -75 9427 -314 C
ATOM 2602 NE2 HIS B 75 -8.661 27.580 58.691 1.00123.30 N
ANISOU 2602 NE2 HIS B 75 17273 13644 15930 -41 9745 -254 N
ATOM 2603 N HIS B 76 -13.672 32.108 58.486 1.00110.00 N
ANISOU 2603 N HIS B 76 17166 11142 13486 -413 8934 542 N
ATOM 2604 CA HIS B 76 -14.515 33.302 58.514 1.00116.21 C
ANISOU 2604 CA HIS B 76 18205 11765 14185 -483 8816 720 C
ATOM 2605 C HIS B 76 -15.689 33.117 59.468 1.00110.82 C
ANISOU 2605 C HIS B 76 17534 11049 13525 -373 8346 693 C
ATOM 2606 O HIS B 76 -16.179 34.093 60.051 1.00109.53 O
ANISOU 2606 O HIS B 76 17375 10762 13479 -426 8212 779 O
ATOM 2607 CB HIS B 76 -15.062 33.616 57.117 1.00116.92 C
ANISOU 2607 CB HIS B 76 18828 11815 13781 -464 8949 898 C
ATOM 2608 CG HIS B 76 -14.009 33.962 56.103 1.00120.10 C
ANISOU 2608 CG HIS B 76 19278 12240 14114 -581 9437 968 C
ATOM 2609 ND1 HIS B 76 -13.471 35.222 55.977 1.00123.02 N
ANISOU 2609 ND1 HIS B 76 19609 12502 14633 -776 9702 1111 N
ATOM 2610 CD2 HIS B 76 -13.443 33.209 55.133 1.00123.56 C
ANISOU 2610 CD2 HIS B 76 19825 12798 14323 -527 9714 923 C
ATOM 2611 CE1 HIS B 76 -12.591 35.227 54.994 1.00129.12 C
ANISOU 2611 CE1 HIS B 76 20435 13337 15286 -848 10131 1160 C
ATOM 2612 NE2 HIS B 76 -12.555 34.016 54.458 1.00129.59 N
ANISOU 2612 NE2 HIS B 76 20589 13541 15109 -689 10153 1044 N
ATOM 2613 N MET B 77 -16.139 31.868 59.622 1.00109.77 N
ANISOU 2613 N MET B 77 17408 11025 13273 -219 8109 579 N
ATOM 2614 CA MET B 77 -17.237 31.478 60.496 1.00103.49 C
ANISOU 2614 CA MET B 77 16605 10233 12481 -108 7674 550 C
ATOM 2615 C MET B 77 -16.858 31.496 61.967 1.00 98.92 C
ANISOU 2615 C MET B 77 15563 9662 12361 -138 7523 431 C
ATOM 2616 O MET B 77 -17.726 31.270 62.815 1.00 94.93 O
ANISOU 2616 O MET B 77 15017 9160 11891 -56 7179 416 O
ATOM 2617 CB MET B 77 -17.739 30.085 60.110 1.00105.21 C
ANISOU 2617 CB MET B 77 16987 10566 12421 42 7507 467 C
ATOM 2618 CG MET B 77 -18.594 30.101 58.870 1.00112.67 C
ANISOU 2618 CG MET B 77 18452 11491 12867 95 7498 595 C
ATOM 2619 SD MET B 77 -20.009 29.010 59.031 1.00111.95 S
ANISOU 2619 SD MET B 77 18571 11465 12498 251 7050 563 S
ATOM 2620 CE MET B 77 -19.249 27.485 58.511 1.00114.70 C
ANISOU 2620 CE MET B 77 18908 11924 12750 324 7201 370 C
ATOM 2621 N ARG B 78 -15.587 31.746 62.288 1.00100.93 N
ANISOU 2621 N ARG B 78 15463 9930 12956 -255 7769 347 N
ATOM 2622 CA ARG B 78 -15.119 31.781 63.672 1.00 98.48 C
ANISOU 2622 CA ARG B 78 14703 9634 13081 -296 7630 223 C
ATOM 2623 C ARG B 78 -15.385 33.165 64.283 1.00102.79 C
ANISOU 2623 C ARG B 78 15237 10012 13807 -409 7602 309 C
ATOM 2624 O ARG B 78 -14.472 33.945 64.572 1.00106.62 O
ANISOU 2624 O ARG B 78 15482 10436 14594 -570 7814 286 O
ATOM 2625 CB ARG B 78 -13.647 31.400 63.734 1.00 98.52 C
ANISOU 2625 CB ARG B 78 14318 9748 13368 -363 7888 89 C
ATOM 2626 CG ARG B 78 -13.352 29.983 63.254 1.00 99.37 C
ANISOU 2626 CG ARG B 78 14411 10024 13320 -220 7907 -19 C
ATOM 2627 CD ARG B 78 -11.879 29.667 63.399 1.00107.65 C
ANISOU 2627 CD ARG B 78 15028 11198 14675 -262 8157 -150 C
ATOM 2628 NE ARG B 78 -11.530 28.354 62.866 1.00115.21 N
ANISOU 2628 NE ARG B 78 15986 12313 15476 -104 8219 -256 N
ATOM 2629 CZ ARG B 78 -10.393 27.725 63.140 1.00118.50 C
ANISOU 2629 CZ ARG B 78 16004 12881 16138 -59 8342 -401 C
ATOM 2630 NH1 ARG B 78 -9.504 28.289 63.946 1.00121.18 N
ANISOU 2630 NH1 ARG B 78 15904 13243 16897 -178 8400 -452 N
ATOM 2631 NH2 ARG B 78 -10.145 26.534 62.614 1.00117.76 N
ANISOU 2631 NH2 ARG B 78 15952 12917 15874 111 8403 -500 N
ATOM 2632 N THR B 79 -16.676 33.452 64.479 1.00 98.91 N
ANISOU 2632 N THR B 79 15007 9451 13125 -318 7335 407 N
ATOM 2633 CA THR B 79 -17.185 34.645 65.150 1.00 97.22 C
ANISOU 2633 CA THR B 79 14821 9084 13036 -364 7245 483 C
ATOM 2634 C THR B 79 -17.609 34.297 66.581 1.00 92.09 C
ANISOU 2634 C THR B 79 13916 8464 12609 -285 6918 377 C
ATOM 2635 O THR B 79 -17.688 33.121 66.953 1.00 89.17 O
ANISOU 2635 O THR B 79 13405 8236 12238 -186 6725 278 O
ATOM 2636 CB THR B 79 -18.380 35.249 64.382 1.00 84.97 C
ANISOU 2636 CB THR B 79 13731 7455 11100 -289 7170 682 C
ATOM 2637 OG1 THR B 79 -19.500 34.356 64.440 1.00 81.30 O
ANISOU 2637 OG1 THR B 79 13408 7092 10389 -108 6848 690 O
ATOM 2638 CG2 THR B 79 -18.040 35.520 62.915 1.00 96.01 C
ANISOU 2638 CG2 THR B 79 15424 8834 12220 -357 7471 803 C
ATOM 2639 N VAL B 80 -17.899 35.333 67.383 1.00 87.83 N
ANISOU 2639 N VAL B 80 13336 7788 12247 -326 6859 404 N
ATOM 2640 CA VAL B 80 -18.319 35.141 68.777 1.00 81.69 C
ANISOU 2640 CA VAL B 80 12339 7026 11674 -252 6575 313 C
ATOM 2641 C VAL B 80 -19.602 34.305 68.844 1.00 81.20 C
ANISOU 2641 C VAL B 80 12450 7073 11331 -52 6253 373 C
ATOM 2642 O VAL B 80 -19.667 33.295 69.562 1.00 84.02 O
ANISOU 2642 O VAL B 80 12599 7561 11763 16 6031 278 O
ATOM 2643 CB VAL B 80 -18.474 36.507 69.491 1.00 78.95 C
ANISOU 2643 CB VAL B 80 11988 6493 11519 -323 6612 343 C
ATOM 2644 CG1 VAL B 80 -19.053 36.358 70.902 1.00 73.60 C
ANISOU 2644 CG1 VAL B 80 11138 5825 11003 -224 6330 266 C
ATOM 2645 CG2 VAL B 80 -17.128 37.249 69.572 1.00 80.97 C
ANISOU 2645 CG2 VAL B 80 12004 6653 12108 -558 6908 262 C
ATOM 2646 N THR B 81 -20.635 34.695 68.076 1.00 79.73 N
ANISOU 2646 N THR B 81 12636 6850 10809 37 6210 539 N
ATOM 2647 CA THR B 81 -21.913 33.978 68.026 1.00 77.12 C
ANISOU 2647 CA THR B 81 12474 6631 10197 214 5914 612 C
ATOM 2648 C THR B 81 -21.720 32.497 67.684 1.00 81.26 C
ANISOU 2648 C THR B 81 12944 7318 10612 247 5837 526 C
ATOM 2649 O THR B 81 -22.282 31.614 68.342 1.00 82.94 O
ANISOU 2649 O THR B 81 13051 7646 10818 342 5572 488 O
ATOM 2650 CB THR B 81 -22.851 34.653 67.004 1.00 85.69 C
ANISOU 2650 CB THR B 81 13961 7674 10922 277 5916 804 C
ATOM 2651 OG1 THR B 81 -23.158 35.986 67.432 1.00 95.16 O
ANISOU 2651 OG1 THR B 81 15210 8733 12213 275 5943 891 O
ATOM 2652 CG2 THR B 81 -24.174 33.885 66.809 1.00 80.57 C
ANISOU 2652 CG2 THR B 81 13481 7166 9964 444 5611 882 C
ATOM 2653 N ASN B 82 -20.900 32.217 66.662 1.00 86.04 N
ANISOU 2653 N ASN B 82 13623 7937 11130 170 6085 498 N
ATOM 2654 CA ASN B 82 -20.685 30.847 66.200 1.00 85.13 C
ANISOU 2654 CA ASN B 82 13504 7961 10879 215 6056 413 C
ATOM 2655 C ASN B 82 -19.835 30.022 67.169 1.00 80.14 C
ANISOU 2655 C ASN B 82 12459 7429 10561 198 5992 240 C
ATOM 2656 O ASN B 82 -20.015 28.803 67.252 1.00 79.95 O
ANISOU 2656 O ASN B 82 12396 7531 10449 281 5832 171 O
ATOM 2657 CB ASN B 82 -20.048 30.862 64.806 1.00 90.78 C
ANISOU 2657 CB ASN B 82 14436 8662 11394 155 6371 438 C
ATOM 2658 CG ASN B 82 -21.023 31.295 63.721 1.00 91.48 C
ANISOU 2658 CG ASN B 82 14979 8708 11073 201 6359 607 C
ATOM 2659 OD1 ASN B 82 -22.212 31.483 63.979 1.00 85.09 O
ANISOU 2659 OD1 ASN B 82 14307 7900 10122 291 6097 700 O
ATOM 2660 ND2 ASN B 82 -20.524 31.443 62.499 1.00 99.78 N
ANISOU 2660 ND2 ASN B 82 16255 9737 11919 145 6638 652 N
ATOM 2661 N TYR B 83 -18.901 30.656 67.899 1.00 76.91 N
ANISOU 2661 N TYR B 83 11744 6970 10510 92 6107 165 N
ATOM 2662 CA TYR B 83 -18.168 29.942 68.948 1.00 77.20 C
ANISOU 2662 CA TYR B 83 11371 7122 10840 89 5987 5 C
ATOM 2663 C TYR B 83 -19.114 29.513 70.066 1.00 76.15 C
ANISOU 2663 C TYR B 83 11160 7058 10717 189 5610 8 C
ATOM 2664 O TYR B 83 -18.965 28.421 70.631 1.00 73.85 O
ANISOU 2664 O TYR B 83 10668 6918 10474 254 5419 -90 O
ATOM 2665 CB TYR B 83 -17.034 30.813 69.509 1.00 81.04 C
ANISOU 2665 CB TYR B 83 11551 7535 11705 -57 6177 -77 C
ATOM 2666 CG TYR B 83 -15.709 30.688 68.771 1.00 90.16 C
ANISOU 2666 CG TYR B 83 12567 8729 12960 -145 6508 -150 C
ATOM 2667 CD1 TYR B 83 -15.645 30.088 67.522 1.00 94.77 C
ANISOU 2667 CD1 TYR B 83 13379 9368 13260 -97 6676 -113 C
ATOM 2668 CD2 TYR B 83 -14.522 31.159 69.331 1.00 92.75 C
ANISOU 2668 CD2 TYR B 83 12525 9049 13667 -274 6660 -258 C
ATOM 2669 CE1 TYR B 83 -14.444 29.965 66.842 1.00 98.42 C
ANISOU 2669 CE1 TYR B 83 13709 9882 13802 -161 7003 -172 C
ATOM 2670 CE2 TYR B 83 -13.313 31.038 68.658 1.00 97.67 C
ANISOU 2670 CE2 TYR B 83 12987 9732 14390 -348 6976 -313 C
ATOM 2671 CZ TYR B 83 -13.281 30.441 67.413 1.00101.11 C
ANISOU 2671 CZ TYR B 83 13658 10230 14529 -284 7156 -264 C
ATOM 2672 OH TYR B 83 -12.087 30.318 66.738 1.00107.31 O
ANISOU 2672 OH TYR B 83 14280 11091 15403 -342 7495 -311 O
ATOM 2673 N PHE B 84 -20.096 30.367 70.380 1.00 73.70 N
ANISOU 2673 N PHE B 84 11011 6645 10347 215 5508 127 N
ATOM 2674 CA PHE B 84 -21.142 30.025 71.340 1.00 68.47 C
ANISOU 2674 CA PHE B 84 10310 6057 9647 322 5173 165 C
ATOM 2675 C PHE B 84 -22.110 28.978 70.765 1.00 64.46 C
ANISOU 2675 C PHE B 84 10020 5658 8813 439 5006 226 C
ATOM 2676 O PHE B 84 -22.545 28.077 71.489 1.00 60.73 O
ANISOU 2676 O PHE B 84 9418 5321 8335 510 4749 193 O
ATOM 2677 CB PHE B 84 -21.912 31.291 71.769 1.00 67.78 C
ANISOU 2677 CB PHE B 84 10344 5827 9584 343 5153 279 C
ATOM 2678 CG PHE B 84 -21.217 32.159 72.831 1.00 69.11 C
ANISOU 2678 CG PHE B 84 10255 5898 10106 245 5215 193 C
ATOM 2679 CD1 PHE B 84 -20.819 31.637 74.057 1.00 70.29 C
ANISOU 2679 CD1 PHE B 84 10063 6174 10472 233 5019 69 C
ATOM 2680 CD2 PHE B 84 -21.049 33.526 72.619 1.00 67.33 C
ANISOU 2680 CD2 PHE B 84 10152 5459 9972 174 5452 235 C
ATOM 2681 CE1 PHE B 84 -20.220 32.452 75.024 1.00 69.37 C
ANISOU 2681 CE1 PHE B 84 9725 5966 10668 140 5070 -27 C
ATOM 2682 CE2 PHE B 84 -20.455 34.340 73.581 1.00 66.24 C
ANISOU 2682 CE2 PHE B 84 9801 5204 10164 73 5528 139 C
ATOM 2683 CZ PHE B 84 -20.041 33.802 74.781 1.00 66.02 C
ANISOU 2683 CZ PHE B 84 9428 5294 10362 51 5338 3 C
ATOM 2684 N LEU B 85 -22.453 29.071 69.466 1.00 68.69 N
ANISOU 2684 N LEU B 85 10895 6141 9064 454 5147 310 N
ATOM 2685 CA LEU B 85 -23.369 28.094 68.866 1.00 70.94 C
ANISOU 2685 CA LEU B 85 11412 6514 9029 550 4999 352 C
ATOM 2686 C LEU B 85 -22.770 26.688 68.849 1.00 70.98 C
ANISOU 2686 C LEU B 85 11286 6637 9048 560 4971 209 C
ATOM 2687 O LEU B 85 -23.512 25.694 68.895 1.00 68.20 O
ANISOU 2687 O LEU B 85 11016 6366 8529 638 4777 204 O
ATOM 2688 CB LEU B 85 -23.774 28.533 67.446 1.00 72.54 C
ANISOU 2688 CB LEU B 85 12016 6647 8900 553 5150 460 C
ATOM 2689 CG LEU B 85 -24.750 29.718 67.324 1.00 68.00 C
ANISOU 2689 CG LEU B 85 11643 5998 8197 599 5095 628 C
ATOM 2690 CD1 LEU B 85 -25.131 30.001 65.874 1.00 74.11 C
ANISOU 2690 CD1 LEU B 85 12813 6746 8599 598 5195 737 C
ATOM 2691 CD2 LEU B 85 -26.003 29.505 68.166 1.00 59.68 C
ANISOU 2691 CD2 LEU B 85 10540 5030 7104 720 4779 696 C
ATOM 2692 N VAL B 86 -21.432 26.589 68.794 1.00 72.00 N
ANISOU 2692 N VAL B 86 11206 6773 9377 490 5169 88 N
ATOM 2693 CA VAL B 86 -20.708 25.317 68.913 1.00 74.92 C
ANISOU 2693 CA VAL B 86 11394 7263 9810 528 5147 -65 C
ATOM 2694 C VAL B 86 -20.785 24.799 70.354 1.00 74.45 C
ANISOU 2694 C VAL B 86 11010 7315 9962 572 4854 -133 C
ATOM 2695 O VAL B 86 -20.851 23.578 70.576 1.00 77.02 O
ANISOU 2695 O VAL B 86 11280 7742 10240 655 4704 -216 O
ATOM 2696 CB VAL B 86 -19.244 25.502 68.452 1.00 78.89 C
ANISOU 2696 CB VAL B 86 11739 7757 10477 459 5460 -163 C
ATOM 2697 CG1 VAL B 86 -18.383 24.269 68.751 1.00 81.03 C
ANISOU 2697 CG1 VAL B 86 11757 8165 10868 531 5429 -333 C
ATOM 2698 CG2 VAL B 86 -19.177 25.831 66.968 1.00 79.38 C
ANISOU 2698 CG2 VAL B 86 12145 7736 10279 428 5751 -98 C
ATOM 2699 N ASN B 87 -20.770 25.702 71.333 1.00 71.01 N
ANISOU 2699 N ASN B 87 10380 6857 9745 525 4774 -106 N
ATOM 2700 CA ASN B 87 -20.921 25.310 72.734 1.00 66.67 C
ANISOU 2700 CA ASN B 87 9552 6424 9355 571 4480 -159 C
ATOM 2701 C ASN B 87 -22.335 24.809 73.015 1.00 66.54 C
ANISOU 2701 C ASN B 87 9690 6459 9133 660 4225 -61 C
ATOM 2702 O ASN B 87 -22.513 23.889 73.822 1.00 67.02 O
ANISOU 2702 O ASN B 87 9597 6643 9223 728 3992 -120 O
ATOM 2703 CB ASN B 87 -20.571 26.485 73.659 1.00 66.08 C
ANISOU 2703 CB ASN B 87 9273 6295 9538 495 4481 -162 C
ATOM 2704 CG ASN B 87 -20.410 26.064 75.117 1.00 64.57 C
ANISOU 2704 CG ASN B 87 8769 6246 9518 541 4200 -256 C
ATOM 2705 OD1 ASN B 87 -19.681 25.121 75.425 1.00 64.84 O
ANISOU 2705 OD1 ASN B 87 8604 6397 9635 589 4126 -385 O
ATOM 2706 ND2 ASN B 87 -21.098 26.759 76.016 1.00 62.39 N
ANISOU 2706 ND2 ASN B 87 8466 5962 9278 547 4042 -193 N
ATOM 2707 N LEU B 88 -23.337 25.398 72.351 1.00 64.36 N
ANISOU 2707 N LEU B 88 9717 6090 8648 672 4270 89 N
ATOM 2708 CA LEU B 88 -24.704 24.883 72.423 1.00 58.75 C
ANISOU 2708 CA LEU B 88 9175 5427 7721 764 4069 187 C
ATOM 2709 C LEU B 88 -24.769 23.445 71.890 1.00 61.89 C
ANISOU 2709 C LEU B 88 9686 5879 7951 809 4033 109 C
ATOM 2710 O LEU B 88 -25.387 22.579 72.521 1.00 59.10 O
ANISOU 2710 O LEU B 88 9280 5608 7568 873 3823 99 O
ATOM 2711 CB LEU B 88 -25.657 25.828 71.665 1.00 56.79 C
ANISOU 2711 CB LEU B 88 9242 5074 7264 791 4143 353 C
ATOM 2712 CG LEU B 88 -27.182 25.591 71.618 1.00 56.45 C
ANISOU 2712 CG LEU B 88 9393 5078 6977 900 3960 485 C
ATOM 2713 CD1 LEU B 88 -27.801 25.510 73.002 1.00 59.44 C
ANISOU 2713 CD1 LEU B 88 9530 5559 7494 967 3729 523 C
ATOM 2714 CD2 LEU B 88 -27.911 26.660 70.809 1.00 56.03 C
ANISOU 2714 CD2 LEU B 88 9617 4948 6723 937 4031 633 C
ATOM 2715 N SER B 89 -24.071 23.171 70.773 1.00 65.46 N
ANISOU 2715 N SER B 89 10293 6277 8303 778 4252 41 N
ATOM 2716 CA SER B 89 -23.987 21.825 70.184 1.00 67.19 C
ANISOU 2716 CA SER B 89 10651 6520 8359 826 4257 -61 C
ATOM 2717 C SER B 89 -23.282 20.815 71.099 1.00 68.47 C
ANISOU 2717 C SER B 89 10499 6782 8735 874 4129 -210 C
ATOM 2718 O SER B 89 -23.634 19.630 71.104 1.00 69.80 O
ANISOU 2718 O SER B 89 10757 6968 8797 944 4015 -273 O
ATOM 2719 CB SER B 89 -23.248 21.878 68.839 1.00 71.54 C
ANISOU 2719 CB SER B 89 11410 7000 8771 792 4547 -108 C
ATOM 2720 OG SER B 89 -23.996 22.518 67.819 1.00 73.25 O
ANISOU 2720 OG SER B 89 12001 7132 8699 771 4632 18 O
ATOM 2721 N LEU B 90 -22.237 21.251 71.821 1.00 69.08 N
ANISOU 2721 N LEU B 90 10233 6911 9101 845 4153 -280 N
ATOM 2722 CA LEU B 90 -21.556 20.362 72.766 1.00 67.00 C
ANISOU 2722 CA LEU B 90 9670 6757 9031 914 3998 -419 C
ATOM 2723 C LEU B 90 -22.507 19.931 73.881 1.00 64.24 C
ANISOU 2723 C LEU B 90 9250 6474 8686 967 3688 -374 C
ATOM 2724 O LEU B 90 -22.557 18.751 74.251 1.00 67.35 O
ANISOU 2724 O LEU B 90 9610 6907 9074 1054 3543 -454 O
ATOM 2725 CB LEU B 90 -20.318 21.054 73.359 1.00 63.96 C
ANISOU 2725 CB LEU B 90 8951 6416 8935 871 4070 -494 C
ATOM 2726 CG LEU B 90 -19.083 21.322 72.486 1.00 64.39 C
ANISOU 2726 CG LEU B 90 8965 6434 9067 832 4391 -571 C
ATOM 2727 CD1 LEU B 90 -17.936 21.879 73.314 1.00 60.98 C
ANISOU 2727 CD1 LEU B 90 8162 6053 8953 797 4416 -657 C
ATOM 2728 CD2 LEU B 90 -18.634 20.069 71.766 1.00 70.75 C
ANISOU 2728 CD2 LEU B 90 9853 7264 9765 938 4480 -688 C
ATOM 2729 N ALA B 91 -23.272 20.895 74.408 1.00 58.70 N
ANISOU 2729 N ALA B 91 8538 5771 7993 924 3600 -244 N
ATOM 2730 CA ALA B 91 -24.312 20.646 75.405 1.00 58.40 C
ANISOU 2730 CA ALA B 91 8454 5799 7935 975 3342 -171 C
ATOM 2731 C ALA B 91 -25.421 19.747 74.855 1.00 66.91 C
ANISOU 2731 C ALA B 91 9818 6833 8774 1028 3302 -112 C
ATOM 2732 O ALA B 91 -25.936 18.880 75.573 1.00 72.93 O
ANISOU 2732 O ALA B 91 10534 7638 9539 1092 3117 -120 O
ATOM 2733 CB ALA B 91 -24.895 21.984 75.864 1.00 50.64 C
ANISOU 2733 CB ALA B 91 7445 4811 6986 936 3313 -40 C
ATOM 2734 N ASP B 92 -25.808 19.972 73.589 1.00 68.44 N
ANISOU 2734 N ASP B 92 10334 6925 8744 1002 3478 -54 N
ATOM 2735 CA ASP B 92 -26.826 19.170 72.905 1.00 70.48 C
ANISOU 2735 CA ASP B 92 10936 7122 8721 1043 3457 -18 C
ATOM 2736 C ASP B 92 -26.349 17.731 72.691 1.00 70.75 C
ANISOU 2736 C ASP B 92 11031 7123 8728 1085 3440 -182 C
ATOM 2737 O ASP B 92 -27.139 16.785 72.797 1.00 69.61 O
ANISOU 2737 O ASP B 92 11059 6933 8456 1132 3317 -191 O
ATOM 2738 CB ASP B 92 -27.159 19.793 71.531 1.00 79.24 C
ANISOU 2738 CB ASP B 92 12405 8141 9560 1003 3637 56 C
ATOM 2739 CG ASP B 92 -28.022 21.078 71.597 1.00 86.17 C
ANISOU 2739 CG ASP B 92 13334 9025 10382 1003 3619 242 C
ATOM 2740 OD1 ASP B 92 -28.641 21.384 72.639 1.00 83.59 O
ANISOU 2740 OD1 ASP B 92 12818 8770 10173 1050 3467 329 O
ATOM 2741 OD2 ASP B 92 -28.069 21.790 70.562 1.00 92.16 O
ANISOU 2741 OD2 ASP B 92 14331 9717 10967 970 3760 303 O
ATOM 2742 N VAL B 93 -25.055 17.555 72.380 1.00 70.80 N
ANISOU 2742 N VAL B 93 10910 7136 8854 1082 3571 -315 N
ATOM 2743 CA VAL B 93 -24.485 16.222 72.167 1.00 70.00 C
ANISOU 2743 CA VAL B 93 10850 7002 8747 1156 3566 -482 C
ATOM 2744 C VAL B 93 -24.410 15.455 73.490 1.00 66.13 C
ANISOU 2744 C VAL B 93 10093 6571 8461 1232 3328 -535 C
ATOM 2745 O VAL B 93 -24.743 14.265 73.546 1.00 70.80 O
ANISOU 2745 O VAL B 93 10828 7086 8987 1298 3222 -602 O
ATOM 2746 CB VAL B 93 -23.113 16.333 71.460 1.00 70.81 C
ANISOU 2746 CB VAL B 93 10872 7113 8921 1161 3800 -599 C
ATOM 2747 CG1 VAL B 93 -22.258 15.071 71.638 1.00 72.38 C
ANISOU 2747 CG1 VAL B 93 10960 7318 9222 1282 3767 -784 C
ATOM 2748 CG2 VAL B 93 -23.299 16.602 69.964 1.00 74.70 C
ANISOU 2748 CG2 VAL B 93 11750 7511 9123 1114 4029 -573 C
ATOM 2749 N LEU B 94 -24.018 16.137 74.579 1.00 62.51 N
ANISOU 2749 N LEU B 94 9285 6231 8236 1220 3228 -505 N
ATOM 2750 CA LEU B 94 -24.004 15.536 75.916 1.00 63.45 C
ANISOU 2750 CA LEU B 94 9172 6419 8519 1293 2984 -536 C
ATOM 2751 C LEU B 94 -25.356 14.909 76.252 1.00 61.92 C
ANISOU 2751 C LEU B 94 9163 6161 8203 1316 2834 -440 C
ATOM 2752 O LEU B 94 -25.432 13.752 76.683 1.00 68.48 O
ANISOU 2752 O LEU B 94 10020 6935 9064 1395 2703 -501 O
ATOM 2753 CB LEU B 94 -23.635 16.595 76.968 1.00 67.23 C
ANISOU 2753 CB LEU B 94 9336 7025 9183 1258 2893 -498 C
ATOM 2754 CG LEU B 94 -23.687 16.217 78.460 1.00 67.34 C
ANISOU 2754 CG LEU B 94 9128 7129 9329 1328 2629 -512 C
ATOM 2755 CD1 LEU B 94 -22.644 15.154 78.808 1.00 65.51 C
ANISOU 2755 CD1 LEU B 94 8765 6909 9217 1450 2557 -676 C
ATOM 2756 CD2 LEU B 94 -23.545 17.440 79.377 1.00 69.58 C
ANISOU 2756 CD2 LEU B 94 9195 7520 9721 1279 2550 -468 C
ATOM 2757 N ALA B 95 -26.429 15.673 76.031 1.00 59.96 N
ANISOU 2757 N ALA B 95 9060 5904 7818 1260 2863 -283 N
ATOM 2758 CA ALA B 95 -27.792 15.228 76.307 1.00 54.33 C
ANISOU 2758 CA ALA B 95 8530 5130 6981 1291 2750 -170 C
ATOM 2759 C ALA B 95 -28.256 14.148 75.329 1.00 55.60 C
ANISOU 2759 C ALA B 95 9105 5105 6916 1303 2782 -239 C
ATOM 2760 O ALA B 95 -28.963 13.216 75.724 1.00 57.32 O
ANISOU 2760 O ALA B 95 9462 5207 7109 1341 2632 -226 O
ATOM 2761 CB ALA B 95 -28.739 16.428 76.256 1.00 45.68 C
ANISOU 2761 CB ALA B 95 7476 4087 5794 1264 2790 10 C
ATOM 2762 N THR B 96 -27.892 14.273 74.048 1.00 58.95 N
ANISOU 2762 N THR B 96 9767 5471 7161 1259 2958 -310 N
ATOM 2763 CA THR B 96 -28.368 13.321 73.042 1.00 63.47 C
ANISOU 2763 CA THR B 96 10804 5858 7452 1247 2959 -397 C
ATOM 2764 C THR B 96 -27.661 11.966 73.176 1.00 64.94 C
ANISOU 2764 C THR B 96 10984 5950 7740 1308 2883 -568 C
ATOM 2765 O THR B 96 -28.316 10.921 73.124 1.00 66.54 O
ANISOU 2765 O THR B 96 11482 5970 7830 1305 2727 -613 O
ATOM 2766 CB THR B 96 -28.215 13.935 71.640 1.00 64.22 C
ANISOU 2766 CB THR B 96 11173 5940 7287 1185 3163 -407 C
ATOM 2767 OG1 THR B 96 -29.139 15.025 71.513 1.00 65.45 O
ANISOU 2767 OG1 THR B 96 11423 6152 7293 1145 3181 -234 O
ATOM 2768 CG2 THR B 96 -28.495 12.923 70.514 1.00 62.52 C
ANISOU 2768 CG2 THR B 96 11462 5548 6745 1159 3143 -538 C
ATOM 2769 N ALA B 97 -26.343 11.973 73.428 1.00 68.59 N
ANISOU 2769 N ALA B 97 11116 6516 8427 1367 2961 -664 N
ATOM 2770 CA ALA B 97 -25.576 10.729 73.551 1.00 69.84 C
ANISOU 2770 CA ALA B 97 11249 6597 8691 1468 2902 -831 C
ATOM 2771 C ALA B 97 -25.888 9.965 74.850 1.00 71.27 C
ANISOU 2771 C ALA B 97 11285 6740 9053 1529 2653 -804 C
ATOM 2772 O ALA B 97 -26.103 8.747 74.814 1.00 72.92 O
ANISOU 2772 O ALA B 97 11717 6764 9224 1571 2532 -879 O
ATOM 2773 CB ALA B 97 -24.077 11.029 73.447 1.00 67.08 C
ANISOU 2773 CB ALA B 97 10593 6373 8520 1533 3055 -941 C
ATOM 2774 N ILE B 98 -25.905 10.644 75.998 1.00 72.03 N
ANISOU 2774 N ILE B 98 11040 6992 9337 1532 2564 -695 N
ATOM 2775 CA ILE B 98 -26.026 9.986 77.323 1.00 73.37 C
ANISOU 2775 CA ILE B 98 11039 7153 9686 1604 2339 -661 C
ATOM 2776 C ILE B 98 -27.463 9.968 77.841 1.00 71.58 C
ANISOU 2776 C ILE B 98 10960 6849 9387 1553 2209 -476 C
ATOM 2777 O ILE B 98 -27.970 8.928 78.259 1.00 73.45 O
ANISOU 2777 O ILE B 98 11354 6914 9641 1575 2044 -446 O
ATOM 2778 CB ILE B 98 -25.078 10.648 78.353 1.00 75.97 C
ANISOU 2778 CB ILE B 98 10928 7697 10241 1652 2288 -677 C
ATOM 2779 CG1 ILE B 98 -23.623 10.450 77.946 1.00 83.54 C
ANISOU 2779 CG1 ILE B 98 11748 8696 11297 1734 2383 -863 C
ATOM 2780 CG2 ILE B 98 -25.299 10.109 79.769 1.00 75.35 C
ANISOU 2780 CG2 ILE B 98 10704 7625 10302 1724 2055 -618 C
ATOM 2781 CD1 ILE B 98 -22.937 11.707 77.609 1.00 90.09 C
ANISOU 2781 CD1 ILE B 98 12393 9679 12158 1669 2541 -868 C
ATOM 2782 N CYS B 99 -28.148 11.126 77.840 1.00 61.04 N
ANISOU 2782 N CYS B 99 9580 5625 7986 1489 2274 -333 N
ATOM 2783 CA CYS B 99 -29.446 11.232 78.476 1.00 60.52 C
ANISOU 2783 CA CYS B 99 9576 5518 7900 1478 2153 -132 C
ATOM 2784 C CYS B 99 -30.581 10.686 77.622 1.00 65.23 C
ANISOU 2784 C CYS B 99 10554 5966 8266 1330 2017 -47 C
ATOM 2785 O CYS B 99 -31.495 10.028 78.145 1.00 72.39 O
ANISOU 2785 O CYS B 99 11465 6870 9171 1211 1738 120 O
ATOM 2786 CB CYS B 99 -29.725 12.696 78.841 1.00 56.05 C
ANISOU 2786 CB CYS B 99 8768 5172 7357 1466 2226 0 C
ATOM 2787 SG CYS B 99 -28.362 13.457 79.743 1.00 53.55 S
ANISOU 2787 SG CYS B 99 7991 5104 7251 1471 2208 -92 S
ATOM 2788 N LEU B 100 -30.551 10.910 76.298 1.00 62.04 N
ANISOU 2788 N LEU B 100 10423 5510 7638 1262 2138 -136 N
ATOM 2789 CA LEU B 100 -31.654 10.463 75.440 1.00 64.18 C
ANISOU 2789 CA LEU B 100 11001 5739 7646 1044 1900 -41 C
ATOM 2790 C LEU B 100 -31.942 8.969 75.551 1.00 67.27 C
ANISOU 2790 C LEU B 100 11602 5917 8040 961 1653 -79 C
ATOM 2791 O LEU B 100 -33.113 8.602 75.695 1.00 69.19 O
ANISOU 2791 O LEU B 100 11870 6194 8223 755 1343 115 O
ATOM 2792 CB LEU B 100 -31.396 10.889 73.983 1.00 67.21 C
ANISOU 2792 CB LEU B 100 11696 6082 7758 1019 2089 -163 C
ATOM 2793 CG LEU B 100 -32.478 10.602 72.923 1.00 66.45 C
ANISOU 2793 CG LEU B 100 11950 5961 7338 797 1838 -84 C
ATOM 2794 CD1 LEU B 100 -32.432 11.612 71.789 1.00 65.98 C
ANISOU 2794 CD1 LEU B 100 12070 5982 7017 787 2022 -84 C
ATOM 2795 CD2 LEU B 100 -32.338 9.199 72.352 1.00 65.42 C
ANISOU 2795 CD2 LEU B 100 12207 5559 7089 745 1726 -276 C
ATOM 2796 N PRO B 101 -30.946 8.055 75.508 1.00 64.63 N
ANISOU 2796 N PRO B 101 11417 5350 7790 1109 1768 -314 N
ATOM 2797 CA PRO B 101 -31.289 6.622 75.629 1.00 63.96 C
ANISOU 2797 CA PRO B 101 11572 5020 7710 1020 1511 -336 C
ATOM 2798 C PRO B 101 -31.854 6.238 76.991 1.00 65.91 C
ANISOU 2798 C PRO B 101 11562 5315 8165 970 1277 -113 C
ATOM 2799 O PRO B 101 -32.765 5.404 77.067 1.00 67.26 O
ANISOU 2799 O PRO B 101 11880 5382 8294 757 983 13 O
ATOM 2800 CB PRO B 101 -29.954 5.905 75.349 1.00 58.93 C
ANISOU 2800 CB PRO B 101 11076 4172 7145 1252 1728 -634 C
ATOM 2801 CG PRO B 101 -29.061 6.934 74.726 1.00 63.66 C
ANISOU 2801 CG PRO B 101 11474 5014 7700 1345 2037 -732 C
ATOM 2802 CD PRO B 101 -29.501 8.253 75.306 1.00 64.68 C
ANISOU 2802 CD PRO B 101 11338 5344 7895 1335 2103 -548 C
ATOM 2803 N ALA B 102 -31.316 6.820 78.075 1.00 63.61 N
ANISOU 2803 N ALA B 102 10902 5177 8091 1153 1403 -64 N
ATOM 2804 CA ALA B 102 -31.835 6.576 79.419 1.00 57.65 C
ANISOU 2804 CA ALA B 102 9906 4501 7496 1127 1214 161 C
ATOM 2805 C ALA B 102 -33.288 7.029 79.534 1.00 59.95 C
ANISOU 2805 C ALA B 102 10085 5004 7687 877 1011 453 C
ATOM 2806 O ALA B 102 -34.108 6.359 80.176 1.00 66.35 O
ANISOU 2806 O ALA B 102 10867 5800 8543 726 780 654 O
ATOM 2807 CB ALA B 102 -30.962 7.300 80.449 1.00 53.58 C
ANISOU 2807 CB ALA B 102 9038 4136 7182 1376 1391 134 C
ATOM 2808 N SER B 103 -33.612 8.158 78.897 1.00 57.08 N
ANISOU 2808 N SER B 103 9656 4837 7196 837 1103 487 N
ATOM 2809 CA SER B 103 -34.970 8.693 78.861 1.00 57.82 C
ANISOU 2809 CA SER B 103 9627 5149 7193 636 924 754 C
ATOM 2810 C SER B 103 -35.912 7.804 78.033 1.00 61.23 C
ANISOU 2810 C SER B 103 10340 5456 7470 351 641 812 C
ATOM 2811 O SER B 103 -37.056 7.574 78.437 1.00 63.57 O
ANISOU 2811 O SER B 103 10506 5860 7787 151 403 1062 O
ATOM 2812 CB SER B 103 -34.923 10.129 78.318 1.00 59.75 C
ANISOU 2812 CB SER B 103 9773 5590 7341 708 1107 753 C
ATOM 2813 OG SER B 103 -36.192 10.758 78.270 1.00 67.44 O
ANISOU 2813 OG SER B 103 10603 6787 8232 567 948 1009 O
ATOM 2814 N LEU B 104 -35.442 7.294 76.880 1.00 63.85 N
ANISOU 2814 N LEU B 104 11056 5562 7642 326 666 579 N
ATOM 2815 CA LEU B 104 -36.267 6.411 76.044 1.00 68.78 C
ANISOU 2815 CA LEU B 104 12001 6032 8099 47 372 592 C
ATOM 2816 C LEU B 104 -36.616 5.112 76.769 1.00 65.61 C
ANISOU 2816 C LEU B 104 11648 5436 7846 -94 142 673 C
ATOM 2817 O LEU B 104 -37.757 4.645 76.706 1.00 67.81 O
ANISOU 2817 O LEU B 104 11943 5727 8096 -390 -164 859 O
ATOM 2818 CB LEU B 104 -35.558 6.099 74.714 1.00 72.30 C
ANISOU 2818 CB LEU B 104 12898 6252 8321 91 481 287 C
ATOM 2819 CG LEU B 104 -36.047 4.924 73.833 1.00 74.69 C
ANISOU 2819 CG LEU B 104 13655 6282 8443 -149 198 186 C
ATOM 2820 CD1 LEU B 104 -37.448 5.150 73.263 1.00 75.86 C
ANISOU 2820 CD1 LEU B 104 13816 6586 8419 -464 -140 391 C
ATOM 2821 CD2 LEU B 104 -35.068 4.593 72.701 1.00 76.44 C
ANISOU 2821 CD2 LEU B 104 14328 6260 8454 -9 399 -162 C
ATOM 2822 N LEU B 105 -35.633 4.522 77.464 1.00 61.80 N
ANISOU 2822 N LEU B 105 11180 4769 7531 111 279 546 N
ATOM 2823 CA LEU B 105 -35.834 3.261 78.176 1.00 61.72 C
ANISOU 2823 CA LEU B 105 11260 4528 7663 10 84 623 C
ATOM 2824 C LEU B 105 -36.751 3.429 79.393 1.00 68.89 C
ANISOU 2824 C LEU B 105 11794 5664 8718 -111 -43 975 C
ATOM 2825 O LEU B 105 -37.521 2.514 79.707 1.00 75.36 O
ANISOU 2825 O LEU B 105 12681 6362 9592 -361 -289 1143 O
ATOM 2826 CB LEU B 105 -34.467 2.674 78.573 1.00 54.61 C
ANISOU 2826 CB LEU B 105 10470 3382 6899 316 274 396 C
ATOM 2827 CG LEU B 105 -34.307 1.208 79.011 1.00 64.03 C
ANISOU 2827 CG LEU B 105 11914 4207 8207 290 114 374 C
ATOM 2828 CD1 LEU B 105 -35.087 0.253 78.124 1.00 73.23 C
ANISOU 2828 CD1 LEU B 105 13487 5106 9233 -33 -164 346 C
ATOM 2829 CD2 LEU B 105 -32.839 0.804 79.018 1.00 65.85 C
ANISOU 2829 CD2 LEU B 105 12281 4208 8530 651 337 84 C
ATOM 2830 N VAL B 106 -36.689 4.583 80.081 1.00 67.27 N
ANISOU 2830 N VAL B 106 11207 5780 8573 55 131 1088 N
ATOM 2831 CA VAL B 106 -37.556 4.835 81.240 1.00 64.48 C
ANISOU 2831 CA VAL B 106 10499 5672 8329 -22 56 1413 C
ATOM 2832 C VAL B 106 -39.000 5.095 80.805 1.00 65.34 C
ANISOU 2832 C VAL B 106 10494 5980 8354 -329 -155 1651 C
ATOM 2833 O VAL B 106 -39.944 4.653 81.469 1.00 69.73 O
ANISOU 2833 O VAL B 106 10889 6612 8994 -533 -318 1923 O
ATOM 2834 CB VAL B 106 -37.025 6.006 82.093 1.00 60.08 C
ANISOU 2834 CB VAL B 106 9608 5377 7843 267 303 1430 C
ATOM 2835 CG1 VAL B 106 -37.978 6.306 83.258 1.00 61.50 C
ANISOU 2835 CG1 VAL B 106 9448 5826 8095 206 249 1760 C
ATOM 2836 CG2 VAL B 106 -35.637 5.714 82.634 1.00 57.28 C
ANISOU 2836 CG2 VAL B 106 9309 4853 7603 556 466 1219 C
ATOM 2837 N ASP B 107 -39.199 5.827 79.702 1.00 64.44 N
ANISOU 2837 N ASP B 107 10444 5966 8076 -361 -152 1569 N
ATOM 2838 CA ASP B 107 -40.566 6.094 79.269 1.00 68.29 C
ANISOU 2838 CA ASP B 107 10799 6658 8492 -631 -384 1798 C
ATOM 2839 C ASP B 107 -41.246 4.816 78.731 1.00 72.79 C
ANISOU 2839 C ASP B 107 11630 6994 9033 -992 -717 1827 C
ATOM 2840 O ASP B 107 -42.470 4.694 78.851 1.00 79.58 O
ANISOU 2840 O ASP B 107 12288 8013 9937 -1266 -949 2092 O
ATOM 2841 CB ASP B 107 -40.583 7.258 78.239 1.00 77.02 C
ANISOU 2841 CB ASP B 107 11925 7927 9413 -547 -308 1719 C
ATOM 2842 CG ASP B 107 -40.274 8.665 78.873 1.00 86.25 C
ANISOU 2842 CG ASP B 107 12765 9369 10637 -255 -29 1775 C
ATOM 2843 OD1 ASP B 107 -39.958 9.618 78.113 1.00 90.25 O
ANISOU 2843 OD1 ASP B 107 13337 9943 11012 -132 103 1672 O
ATOM 2844 OD2 ASP B 107 -40.338 8.824 80.114 1.00 86.17 O
ANISOU 2844 OD2 ASP B 107 12464 9491 10787 -151 60 1920 O
ATOM 2845 N ILE B 108 -40.467 3.815 78.282 1.00 71.09 N
ANISOU 2845 N ILE B 108 11835 6397 8779 -993 -738 1572 N
ATOM 2846 CA ILE B 108 -41.023 2.535 77.811 1.00 79.23 C
ANISOU 2846 CA ILE B 108 13175 7140 9791 -1335 -1059 1566 C
ATOM 2847 C ILE B 108 -41.325 1.605 78.983 1.00 82.12 C
ANISOU 2847 C ILE B 108 13430 7392 10379 -1465 -1146 1777 C
ATOM 2848 O ILE B 108 -42.452 1.114 79.134 1.00 86.21 O
ANISOU 2848 O ILE B 108 13841 7947 10968 -1819 -1409 2022 O
ATOM 2849 CB ILE B 108 -40.055 1.828 76.828 1.00 85.13 C
ANISOU 2849 CB ILE B 108 14464 7492 10389 -1254 -1030 1187 C
ATOM 2850 CG1 ILE B 108 -39.883 2.572 75.502 1.00 90.95 C
ANISOU 2850 CG1 ILE B 108 15399 8305 10852 -1195 -980 991 C
ATOM 2851 CG2 ILE B 108 -40.497 0.369 76.562 1.00 89.15 C
ANISOU 2851 CG2 ILE B 108 15335 7625 10914 -1581 -1352 1161 C
ATOM 2852 CD1 ILE B 108 -38.730 1.998 74.653 1.00 96.86 C
ANISOU 2852 CD1 ILE B 108 16653 8699 11450 -1023 -837 601 C
ATOM 2853 N THR B 109 -40.302 1.310 79.800 1.00 79.53 N
ANISOU 2853 N THR B 109 13141 6912 10164 -1189 -934 1687 N
ATOM 2854 CA THR B 109 -40.383 0.329 80.880 1.00 81.62 C
ANISOU 2854 CA THR B 109 13400 7001 10611 -1267 -999 1859 C
ATOM 2855 C THR B 109 -40.993 0.903 82.161 1.00 84.19 C
ANISOU 2855 C THR B 109 13244 7684 11060 -1250 -913 2207 C
ATOM 2856 O THR B 109 -41.519 0.141 82.978 1.00 91.05 O
ANISOU 2856 O THR B 109 14059 8481 12054 -1436 -1017 2453 O
ATOM 2857 CB THR B 109 -38.982 -0.236 81.192 1.00 79.30 C
ANISOU 2857 CB THR B 109 13366 6391 10372 -940 -828 1612 C
ATOM 2858 OG1 THR B 109 -38.165 0.782 81.784 1.00 76.62 O
ANISOU 2858 OG1 THR B 109 12753 6298 10061 -562 -534 1556 O
ATOM 2859 CG2 THR B 109 -38.285 -0.729 79.922 1.00 75.34 C
ANISOU 2859 CG2 THR B 109 13339 5554 9735 -892 -847 1241 C
ATOM 2860 N GLU B 110 -40.949 2.237 82.318 1.00 82.56 N
ANISOU 2860 N GLU B 110 12712 7848 10808 -1032 -716 2231 N
ATOM 2861 CA GLU B 110 -41.353 2.975 83.527 1.00 80.90 C
ANISOU 2861 CA GLU B 110 12068 7992 10680 -919 -572 2500 C
ATOM 2862 C GLU B 110 -40.575 2.546 84.772 1.00 80.52 C
ANISOU 2862 C GLU B 110 12026 7834 10732 -696 -435 2524 C
ATOM 2863 O GLU B 110 -41.039 2.729 85.903 1.00 84.84 O
ANISOU 2863 O GLU B 110 12300 8597 11339 -677 -369 2790 O
ATOM 2864 CB GLU B 110 -42.871 2.903 83.758 1.00 84.88 C
ANISOU 2864 CB GLU B 110 12287 8726 11237 -1262 -747 2862 C
ATOM 2865 CG GLU B 110 -43.698 3.524 82.627 1.00 94.10 C
ANISOU 2865 CG GLU B 110 13367 10080 12307 -1439 -897 2871 C
ATOM 2866 CD GLU B 110 -45.155 3.127 82.685 1.00106.24 C
ANISOU 2866 CD GLU B 110 14669 11765 13931 -1840 -1142 3200 C
ATOM 2867 OE1 GLU B 110 -45.551 2.234 81.908 1.00112.70 O
ANISOU 2867 OE1 GLU B 110 15732 12349 14742 -2178 -1428 3164 O
ATOM 2868 OE2 GLU B 110 -45.897 3.691 83.517 1.00108.64 O
ANISOU 2868 OE2 GLU B 110 14544 12418 14316 -1821 -1045 3489 O
ATOM 2869 N SER B 111 -39.341 2.056 84.565 1.00 77.09 N
ANISOU 2869 N SER B 111 11898 7089 10305 -486 -374 2237 N
ATOM 2870 CA SER B 111 -38.443 1.621 85.627 1.00 72.29 C
ANISOU 2870 CA SER B 111 11333 6347 9788 -232 -275 2218 C
ATOM 2871 C SER B 111 -36.996 2.027 85.315 1.00 65.33 C
ANISOU 2871 C SER B 111 10549 5373 8899 136 -91 1864 C
ATOM 2872 O SER B 111 -36.643 2.289 84.161 1.00 65.18 O
ANISOU 2872 O SER B 111 10679 5283 8803 153 -52 1618 O
ATOM 2873 CB SER B 111 -38.535 0.098 85.836 1.00 79.26 C
ANISOU 2873 CB SER B 111 12526 6839 10749 -418 -465 2299 C
ATOM 2874 OG SER B 111 -37.952 -0.617 84.758 1.00 82.55 O
ANISOU 2874 OG SER B 111 13346 6880 11140 -433 -548 2005 O
ATOM 2875 N TRP B 112 -36.160 2.072 86.359 1.00 62.83 N
ANISOU 2875 N TRP B 112 10144 5067 8661 427 20 1847 N
ATOM 2876 CA TRP B 112 -34.740 2.410 86.233 1.00 57.67 C
ANISOU 2876 CA TRP B 112 9520 4344 8049 780 186 1535 C
ATOM 2877 C TRP B 112 -33.924 1.117 86.226 1.00 59.19 C
ANISOU 2877 C TRP B 112 10038 4123 8330 889 107 1396 C
ATOM 2878 O TRP B 112 -34.014 0.318 87.167 1.00 67.84 O
ANISOU 2878 O TRP B 112 11196 5091 9490 891 -3 1578 O
ATOM 2879 CB TRP B 112 -34.279 3.342 87.362 1.00 56.30 C
ANISOU 2879 CB TRP B 112 9029 4451 7912 1045 327 1578 C
ATOM 2880 CG TRP B 112 -32.904 3.917 87.126 1.00 52.68 C
ANISOU 2880 CG TRP B 112 8520 3980 7513 1360 500 1259 C
ATOM 2881 CD1 TRP B 112 -31.739 3.530 87.725 1.00 53.08 C
ANISOU 2881 CD1 TRP B 112 8573 3915 7677 1632 513 1112 C
ATOM 2882 CD2 TRP B 112 -32.553 4.960 86.206 1.00 53.09 C
ANISOU 2882 CD2 TRP B 112 8487 4158 7526 1408 672 1054 C
ATOM 2883 NE1 TRP B 112 -30.687 4.268 87.236 1.00 54.86 N
ANISOU 2883 NE1 TRP B 112 8646 4255 7942 1791 665 808 N
ATOM 2884 CE2 TRP B 112 -31.159 5.153 86.303 1.00 51.61 C
ANISOU 2884 CE2 TRP B 112 8240 3919 7449 1699 806 793 C
ATOM 2885 CE3 TRP B 112 -33.282 5.751 85.312 1.00 55.36 C
ANISOU 2885 CE3 TRP B 112 8735 4604 7695 1231 719 1077 C
ATOM 2886 CZ2 TRP B 112 -30.481 6.103 85.539 1.00 47.72 C
ANISOU 2886 CZ2 TRP B 112 7625 3560 6947 1760 990 555 C
ATOM 2887 CZ3 TRP B 112 -32.607 6.697 84.557 1.00 50.09 C
ANISOU 2887 CZ3 TRP B 112 8016 4008 7009 1346 916 856 C
ATOM 2888 CH2 TRP B 112 -31.221 6.864 84.674 1.00 50.20 C
ANISOU 2888 CH2 TRP B 112 7978 3953 7143 1615 1075 608 C
ATOM 2889 N LEU B 113 -33.132 0.913 85.168 1.00 55.47 N
ANISOU 2889 N LEU B 113 9788 3438 7852 993 176 1081 N
ATOM 2890 CA LEU B 113 -32.372 -0.319 84.978 1.00 61.49 C
ANISOU 2890 CA LEU B 113 10813 3857 8693 1094 108 899 C
ATOM 2891 C LEU B 113 -30.850 -0.103 84.954 1.00 66.67 C
ANISOU 2891 C LEU B 113 11296 4588 9446 1445 277 587 C
ATOM 2892 O LEU B 113 -30.116 -1.053 84.655 1.00 74.46 O
ANISOU 2892 O LEU B 113 12419 5371 10501 1543 249 401 O
ATOM 2893 CB LEU B 113 -32.837 -1.029 83.692 1.00 60.36 C
ANISOU 2893 CB LEU B 113 11044 3441 8448 848 2 783 C
ATOM 2894 CG LEU B 113 -34.340 -1.340 83.546 1.00 62.07 C
ANISOU 2894 CG LEU B 113 11403 3597 8585 415 -228 1065 C
ATOM 2895 CD1 LEU B 113 -34.705 -1.741 82.120 1.00 65.18 C
ANISOU 2895 CD1 LEU B 113 12143 3782 8840 185 -333 887 C
ATOM 2896 CD2 LEU B 113 -34.799 -2.419 84.519 1.00 62.09 C
ANISOU 2896 CD2 LEU B 113 11413 3482 8696 274 -404 1309 C
ATOM 2897 N PHE B 114 -30.358 1.090 85.316 1.00 63.95 N
ANISOU 2897 N PHE B 114 10623 4553 9123 1616 436 538 N
ATOM 2898 CA PHE B 114 -28.934 1.432 85.240 1.00 69.15 C
ANISOU 2898 CA PHE B 114 11047 5347 9879 1867 571 252 C
ATOM 2899 C PHE B 114 -28.232 1.504 86.606 1.00 67.78 C
ANISOU 2899 C PHE B 114 10583 5332 9837 2054 503 293 C
ATOM 2900 O PHE B 114 -27.059 1.889 86.664 1.00 66.68 O
ANISOU 2900 O PHE B 114 10196 5343 9798 2220 573 79 O
ATOM 2901 CB PHE B 114 -28.740 2.771 84.508 1.00 70.45 C
ANISOU 2901 CB PHE B 114 11043 5755 9970 1871 786 120 C
ATOM 2902 CG PHE B 114 -29.407 2.846 83.149 1.00 76.85 C
ANISOU 2902 CG PHE B 114 12149 6432 10617 1697 857 76 C
ATOM 2903 CD1 PHE B 114 -28.844 2.225 82.042 1.00 79.59 C
ANISOU 2903 CD1 PHE B 114 12710 6611 10918 1711 912 -166 C
ATOM 2904 CD2 PHE B 114 -30.578 3.571 82.975 1.00 75.17 C
ANISOU 2904 CD2 PHE B 114 11996 6278 10286 1523 862 282 C
ATOM 2905 CE1 PHE B 114 -29.455 2.303 80.794 1.00 79.48 C
ANISOU 2905 CE1 PHE B 114 13009 6482 10710 1544 954 -220 C
ATOM 2906 CE2 PHE B 114 -31.190 3.653 81.731 1.00 74.62 C
ANISOU 2906 CE2 PHE B 114 12175 6136 10040 1323 865 240 C
ATOM 2907 CZ PHE B 114 -30.627 3.020 80.640 1.00 77.14 C
ANISOU 2907 CZ PHE B 114 12796 6225 10288 1353 923 -20 C
ATOM 2908 N GLY B 115 -28.920 1.153 87.703 1.00 77.55 N
ANISOU 2908 N GLY B 115 12101 5782 11583 1273 -854 1742 N
ATOM 2909 CA GLY B 115 -28.317 1.164 89.030 1.00 80.22 C
ANISOU 2909 CA GLY B 115 12329 6275 11877 1571 -884 1893 C
ATOM 2910 C GLY B 115 -28.350 2.528 89.717 1.00 77.47 C
ANISOU 2910 C GLY B 115 11769 6356 11311 1685 -848 1973 C
ATOM 2911 O GLY B 115 -28.803 3.531 89.175 1.00 69.18 O
ANISOU 2911 O GLY B 115 10663 5484 10138 1553 -788 1918 O
ATOM 2912 N HIS B 116 -27.800 2.548 90.956 1.00 82.41 N
ANISOU 2912 N HIS B 116 12268 7148 11896 1945 -900 2090 N
ATOM 2913 CA HIS B 116 -27.830 3.722 91.823 1.00 81.07 C
ANISOU 2913 CA HIS B 116 11866 7393 11544 2040 -917 2172 C
ATOM 2914 C HIS B 116 -26.925 4.854 91.353 1.00 78.51 C
ANISOU 2914 C HIS B 116 11385 7209 11236 2191 -890 1774 C
ATOM 2915 O HIS B 116 -27.290 6.034 91.457 1.00 80.99 O
ANISOU 2915 O HIS B 116 11575 7825 11373 2149 -847 1771 O
ATOM 2916 CB HIS B 116 -27.432 3.344 93.256 1.00 86.83 C
ANISOU 2916 CB HIS B 116 12511 8231 12252 2236 -1043 2356 C
ATOM 2917 CG HIS B 116 -28.452 2.530 93.970 1.00100.44 C
ANISOU 2917 CG HIS B 116 14322 9943 13896 2059 -1053 2769 C
ATOM 2918 ND1 HIS B 116 -28.950 1.339 93.481 1.00105.60 N
ANISOU 2918 ND1 HIS B 116 15240 10280 14603 1973 -901 2899 N
ATOM 2919 CD2 HIS B 116 -29.101 2.756 95.138 1.00104.30 C
ANISOU 2919 CD2 HIS B 116 14810 10656 14164 1937 -1247 2970 C
ATOM 2920 CE1 HIS B 116 -29.851 0.866 94.321 1.00107.47 C
ANISOU 2920 CE1 HIS B 116 15608 10617 14609 1924 -785 3204 C
ATOM 2921 NE2 HIS B 116 -29.962 1.704 95.336 1.00106.44 N
ANISOU 2921 NE2 HIS B 116 15352 10712 14379 1707 -1343 3177 N
ATOM 2922 N ALA B 117 -25.718 4.525 90.869 1.00 72.30 N
ANISOU 2922 N ALA B 117 10579 6228 10664 2369 -886 1421 N
ATOM 2923 CA ALA B 117 -24.744 5.536 90.458 1.00 69.10 C
ANISOU 2923 CA ALA B 117 9967 5963 10326 2504 -805 1027 C
ATOM 2924 C ALA B 117 -25.245 6.364 89.271 1.00 74.08 C
ANISOU 2924 C ALA B 117 10646 6605 10897 2323 -654 890 C
ATOM 2925 O ALA B 117 -25.220 7.601 89.314 1.00 75.26 O
ANISOU 2925 O ALA B 117 10635 7024 10936 2351 -569 802 O
ATOM 2926 CB ALA B 117 -23.413 4.863 90.117 1.00 67.34 C
ANISOU 2926 CB ALA B 117 9693 5539 10356 2674 -791 695 C
ATOM 2927 N LEU B 118 -25.673 5.697 88.188 1.00 73.96 N
ANISOU 2927 N LEU B 118 10859 6295 10946 2133 -612 852 N
ATOM 2928 CA LEU B 118 -26.173 6.369 86.988 1.00 66.72 C
ANISOU 2928 CA LEU B 118 9940 5486 9926 1855 -411 715 C
ATOM 2929 C LEU B 118 -27.530 7.038 87.209 1.00 64.24 C
ANISOU 2929 C LEU B 118 9617 5453 9337 1619 -386 1040 C
ATOM 2930 O LEU B 118 -27.946 7.858 86.385 1.00 59.83 O
ANISOU 2930 O LEU B 118 9022 5062 8651 1435 -233 948 O
ATOM 2931 CB LEU B 118 -26.240 5.374 85.815 1.00 61.79 C
ANISOU 2931 CB LEU B 118 9528 4523 9426 1689 -382 559 C
ATOM 2932 CG LEU B 118 -24.890 4.804 85.336 1.00 57.74 C
ANISOU 2932 CG LEU B 118 9013 3744 9183 1912 -353 169 C
ATOM 2933 CD1 LEU B 118 -25.063 3.767 84.230 1.00 55.85 C
ANISOU 2933 CD1 LEU B 118 9015 3165 9040 1757 -343 24 C
ATOM 2934 CD2 LEU B 118 -23.928 5.906 84.888 1.00 55.58 C
ANISOU 2934 CD2 LEU B 118 8507 3669 8944 2025 -138 -181 C
ATOM 2935 N CYS B 119 -28.209 6.714 88.314 1.00 68.37 N
ANISOU 2935 N CYS B 119 10176 6036 9765 1639 -524 1419 N
ATOM 2936 CA CYS B 119 -29.403 7.444 88.720 1.00 68.52 C
ANISOU 2936 CA CYS B 119 10131 6371 9532 1476 -490 1720 C
ATOM 2937 C CYS B 119 -29.058 8.840 89.240 1.00 64.27 C
ANISOU 2937 C CYS B 119 9371 6191 8858 1647 -424 1631 C
ATOM 2938 O CYS B 119 -29.915 9.727 89.216 1.00 57.02 O
ANISOU 2938 O CYS B 119 8375 5551 7740 1510 -346 1757 O
ATOM 2939 CB CYS B 119 -30.172 6.626 89.766 1.00 74.43 C
ANISOU 2939 CB CYS B 119 10971 7079 10230 1444 -624 2144 C
ATOM 2940 SG CYS B 119 -31.631 7.415 90.523 1.00 80.56 S
ANISOU 2940 SG CYS B 119 11633 8315 10662 1224 -604 2418 S
ATOM 2941 N LYS B 120 -27.816 9.052 89.673 1.00 64.96 N
ANISOU 2941 N LYS B 120 9345 6265 9071 1946 -463 1393 N
ATOM 2942 CA LYS B 120 -27.353 10.389 90.030 1.00 60.39 C
ANISOU 2942 CA LYS B 120 8542 5979 8426 2095 -402 1229 C
ATOM 2943 C LYS B 120 -26.699 11.079 88.834 1.00 61.13 C
ANISOU 2943 C LYS B 120 8543 6043 8640 2015 -202 848 C
ATOM 2944 O LYS B 120 -27.056 12.221 88.510 1.00 60.68 O
ANISOU 2944 O LYS B 120 8393 6207 8455 1909 -65 813 O
ATOM 2945 CB LYS B 120 -26.392 10.307 91.225 1.00 58.90 C
ANISOU 2945 CB LYS B 120 8193 5863 8323 2353 -569 1132 C
ATOM 2946 CG LYS B 120 -27.079 9.939 92.540 1.00 62.44 C
ANISOU 2946 CG LYS B 120 8660 6475 8587 2318 -724 1458 C
ATOM 2947 CD LYS B 120 -26.184 10.194 93.740 1.00 63.91 C
ANISOU 2947 CD LYS B 120 8669 6815 8797 2522 -849 1334 C
ATOM 2948 CE LYS B 120 -26.901 9.868 95.041 1.00 68.37 C
ANISOU 2948 CE LYS B 120 9296 7533 9148 2486 -970 1637 C
ATOM 2949 NZ LYS B 120 -27.780 10.978 95.500 1.00 73.54 N
ANISOU 2949 NZ LYS B 120 9888 8514 9538 2374 -905 1702 N
ATOM 2950 N VAL B 121 -25.816 10.360 88.123 1.00 60.74 N
ANISOU 2950 N VAL B 121 8543 5710 8824 2056 -168 583 N
ATOM 2951 CA VAL B 121 -25.012 10.907 87.028 1.00 55.51 C
ANISOU 2951 CA VAL B 121 7793 5000 8298 2018 53 208 C
ATOM 2952 C VAL B 121 -25.903 11.363 85.858 1.00 52.20 C
ANISOU 2952 C VAL B 121 7497 4642 7696 1709 237 246 C
ATOM 2953 O VAL B 121 -25.783 12.500 85.385 1.00 49.40 O
ANISOU 2953 O VAL B 121 7040 4446 7284 1654 425 116 O
ATOM 2954 CB VAL B 121 -23.962 9.887 86.553 1.00 60.04 C
ANISOU 2954 CB VAL B 121 8409 5254 9148 2142 49 -64 C
ATOM 2955 CG1 VAL B 121 -23.121 10.447 85.401 1.00 58.84 C
ANISOU 2955 CG1 VAL B 121 8161 5064 9130 2103 326 -447 C
ATOM 2956 CG2 VAL B 121 -23.052 9.461 87.703 1.00 60.87 C
ANISOU 2956 CG2 VAL B 121 8362 5342 9425 2430 -141 -102 C
ATOM 2957 N ILE B 122 -26.777 10.489 85.355 1.00 54.81 N
ANISOU 2957 N ILE B 122 8050 4832 7942 1512 179 412 N
ATOM 2958 CA ILE B 122 -27.537 10.820 84.158 1.00 53.55 C
ANISOU 2958 CA ILE B 122 8019 4712 7615 1250 318 400 C
ATOM 2959 C ILE B 122 -28.485 11.991 84.407 1.00 47.55 C
ANISOU 2959 C ILE B 122 7178 4277 6612 1147 353 609 C
ATOM 2960 O ILE B 122 -28.385 13.008 83.691 1.00 44.08 O
ANISOU 2960 O ILE B 122 6705 3956 6086 1093 541 471 O
ATOM 2961 CB ILE B 122 -28.295 9.580 83.605 1.00 54.46 C
ANISOU 2961 CB ILE B 122 8375 4596 7720 1060 203 507 C
ATOM 2962 CG1 ILE B 122 -27.281 8.496 83.220 1.00 59.73 C
ANISOU 2962 CG1 ILE B 122 9137 4924 8636 1181 192 246 C
ATOM 2963 CG2 ILE B 122 -29.156 9.936 82.398 1.00 54.02 C
ANISOU 2963 CG2 ILE B 122 8453 4609 7461 806 298 490 C
ATOM 2964 CD1 ILE B 122 -27.874 7.293 82.518 1.00 64.47 C
ANISOU 2964 CD1 ILE B 122 9986 5247 9262 1002 91 267 C
ATOM 2965 N PRO B 123 -29.358 11.962 85.423 1.00 51.42 N
ANISOU 2965 N PRO B 123 7629 4921 6988 1139 198 935 N
ATOM 2966 CA PRO B 123 -30.186 13.154 85.724 1.00 48.39 C
ANISOU 2966 CA PRO B 123 7139 4861 6384 1086 238 1104 C
ATOM 2967 C PRO B 123 -29.381 14.412 85.947 1.00 48.17 C
ANISOU 2967 C PRO B 123 6932 4988 6385 1250 363 909 C
ATOM 2968 O PRO B 123 -29.841 15.511 85.572 1.00 48.22 O
ANISOU 2968 O PRO B 123 6901 5179 6243 1172 477 919 O
ATOM 2969 CB PRO B 123 -30.935 12.726 87.000 1.00 49.43 C
ANISOU 2969 CB PRO B 123 7237 5101 6441 1127 61 1453 C
ATOM 2970 CG PRO B 123 -31.033 11.239 86.867 1.00 55.90 C
ANISOU 2970 CG PRO B 123 8225 5625 7391 1044 -52 1533 C
ATOM 2971 CD PRO B 123 -29.715 10.819 86.277 1.00 60.23 C
ANISOU 2971 CD PRO B 123 8815 5912 8157 1165 0 1184 C
ATOM 2972 N TYR B 124 -28.182 14.297 86.533 1.00 47.18 N
ANISOU 2972 N TYR B 124 6685 4778 6462 1479 337 718 N
ATOM 2973 CA TYR B 124 -27.278 15.430 86.740 1.00 51.07 C
ANISOU 2973 CA TYR B 124 6974 5376 7055 1628 446 481 C
ATOM 2974 C TYR B 124 -26.780 16.001 85.416 1.00 53.38 C
ANISOU 2974 C TYR B 124 7289 5581 7411 1510 713 221 C
ATOM 2975 O TYR B 124 -26.742 17.226 85.237 1.00 57.15 O
ANISOU 2975 O TYR B 124 7674 6194 7846 1488 859 154 O
ATOM 2976 CB TYR B 124 -26.100 14.990 87.626 1.00 52.22 C
ANISOU 2976 CB TYR B 124 6977 5429 7435 1903 318 314 C
ATOM 2977 CG TYR B 124 -24.901 15.934 87.638 1.00 55.95 C
ANISOU 2977 CG TYR B 124 7211 5925 8121 2042 436 -28 C
ATOM 2978 CD1 TYR B 124 -24.878 17.057 88.461 1.00 53.59 C
ANISOU 2978 CD1 TYR B 124 6727 5856 7780 2135 388 -44 C
ATOM 2979 CD2 TYR B 124 -23.789 15.696 86.833 1.00 56.16 C
ANISOU 2979 CD2 TYR B 124 7182 5747 8410 2057 593 -354 C
ATOM 2980 CE1 TYR B 124 -23.788 17.922 88.473 1.00 51.24 C
ANISOU 2980 CE1 TYR B 124 6170 5588 7709 2086 435 -385 C
ATOM 2981 CE2 TYR B 124 -22.695 16.558 86.838 1.00 57.88 C
ANISOU 2981 CE2 TYR B 124 7179 6099 8715 2051 616 -659 C
ATOM 2982 CZ TYR B 124 -22.701 17.668 87.660 1.00 55.95 C
ANISOU 2982 CZ TYR B 124 6790 6094 8374 2099 537 -650 C
ATOM 2983 OH TYR B 124 -21.621 18.526 87.672 1.00 56.22 O
ANISOU 2983 OH TYR B 124 6706 6218 8439 2075 670 -778 O
ATOM 2984 N LEU B 125 -26.381 15.127 84.479 1.00 51.65 N
ANISOU 2984 N LEU B 125 7208 5126 7291 1441 790 73 N
ATOM 2985 CA LEU B 125 -25.873 15.562 83.177 1.00 50.28 C
ANISOU 2985 CA LEU B 125 7089 4864 7150 1343 1073 -169 C
ATOM 2986 C LEU B 125 -26.960 16.197 82.327 1.00 48.81 C
ANISOU 2986 C LEU B 125 7072 4799 6674 1132 1172 -16 C
ATOM 2987 O LEU B 125 -26.671 17.054 81.482 1.00 53.95 O
ANISOU 2987 O LEU B 125 7746 5465 7287 1073 1423 -148 O
ATOM 2988 CB LEU B 125 -25.256 14.376 82.429 1.00 54.91 C
ANISOU 2988 CB LEU B 125 7803 5178 7880 1347 1113 -363 C
ATOM 2989 CG LEU B 125 -23.927 13.825 82.959 1.00 58.72 C
ANISOU 2989 CG LEU B 125 8109 5508 8694 1579 1076 -607 C
ATOM 2990 CD1 LEU B 125 -23.437 12.661 82.110 1.00 59.43 C
ANISOU 2990 CD1 LEU B 125 8353 5325 8903 1581 1128 -800 C
ATOM 2991 CD2 LEU B 125 -22.864 14.919 83.032 1.00 60.48 C
ANISOU 2991 CD2 LEU B 125 8049 5884 9046 1627 1205 -840 C
ATOM 2992 N GLN B 126 -28.223 15.776 82.518 1.00 51.66 N
ANISOU 2992 N GLN B 126 7553 5241 6833 1017 982 268 N
ATOM 2993 CA GLN B 126 -29.336 16.375 81.830 1.00 52.39 C
ANISOU 2993 CA GLN B 126 7775 5475 6655 844 1020 422 C
ATOM 2994 C GLN B 126 -29.521 17.814 82.273 1.00 50.31 C
ANISOU 2994 C GLN B 126 7367 5439 6308 896 1095 491 C
ATOM 2995 O GLN B 126 -29.700 18.728 81.449 1.00 54.79 O
ANISOU 2995 O GLN B 126 8011 6063 6742 824 1269 459 O
ATOM 2996 CB GLN B 126 -30.623 15.584 82.118 1.00 61.79 C
ANISOU 2996 CB GLN B 126 9053 6711 7711 719 780 703 C
ATOM 2997 CG GLN B 126 -31.833 16.081 81.362 1.00 71.39 C
ANISOU 2997 CG GLN B 126 10388 8074 8663 545 775 844 C
ATOM 2998 CD GLN B 126 -31.699 15.871 79.872 1.00 87.52 C
ANISOU 2998 CD GLN B 126 12662 9974 10617 438 897 655 C
ATOM 2999 OE1 GLN B 126 -31.860 14.755 79.375 1.00 92.37 O
ANISOU 2999 OE1 GLN B 126 13426 10413 11259 345 798 604 O
ATOM 3000 NE2 GLN B 126 -31.320 16.922 79.161 1.00 94.77 N
ANISOU 3000 NE2 GLN B 126 13625 10947 11438 463 1124 535 N
ATOM 3001 N ALA B 127 -29.462 18.037 83.593 1.00 48.35 N
ANISOU 3001 N ALA B 127 6925 5316 6131 1041 961 583 N
ATOM 3002 CA ALA B 127 -29.560 19.362 84.165 1.00 44.28 C
ANISOU 3002 CA ALA B 127 6256 5001 5567 1123 1004 615 C
ATOM 3003 C ALA B 127 -28.400 20.243 83.736 1.00 47.89 C
ANISOU 3003 C ALA B 127 6622 5370 6203 1177 1243 331 C
ATOM 3004 O ALA B 127 -28.600 21.388 83.302 1.00 45.74 O
ANISOU 3004 O ALA B 127 6363 5171 5846 1130 1397 330 O
ATOM 3005 CB ALA B 127 -29.621 19.263 85.699 1.00 45.50 C
ANISOU 3005 CB ALA B 127 6240 5294 5755 1298 796 735 C
ATOM 3006 N VAL B 128 -27.169 19.717 83.827 1.00 48.91 N
ANISOU 3006 N VAL B 128 6654 5328 6602 1276 1288 87 N
ATOM 3007 CA VAL B 128 -25.976 20.449 83.380 1.00 46.68 C
ANISOU 3007 CA VAL B 128 6247 4940 6550 1308 1545 -206 C
ATOM 3008 C VAL B 128 -26.135 20.852 81.918 1.00 47.60 C
ANISOU 3008 C VAL B 128 6570 4982 6533 1133 1828 -234 C
ATOM 3009 O VAL B 128 -25.826 21.989 81.536 1.00 52.42 O
ANISOU 3009 O VAL B 128 7121 5638 7157 1045 1969 -288 O
ATOM 3010 CB VAL B 128 -24.706 19.599 83.616 1.00 41.89 C
ANISOU 3010 CB VAL B 128 5492 4194 6229 1402 1480 -456 C
ATOM 3011 CG1 VAL B 128 -23.501 20.130 82.822 1.00 35.26 C
ANISOU 3011 CG1 VAL B 128 4538 3341 5517 1270 1620 -703 C
ATOM 3012 CG2 VAL B 128 -24.351 19.545 85.103 1.00 40.16 C
ANISOU 3012 CG2 VAL B 128 5048 4089 6123 1588 1189 -474 C
ATOM 3013 N SER B 129 -26.667 19.945 81.094 1.00 50.43 N
ANISOU 3013 N SER B 129 7171 5269 6721 1023 1807 -161 N
ATOM 3014 CA SER B 129 -26.890 20.209 79.676 1.00 54.29 C
ANISOU 3014 CA SER B 129 7906 5703 7020 882 2041 -181 C
ATOM 3015 C SER B 129 -27.855 21.386 79.456 1.00 52.44 C
ANISOU 3015 C SER B 129 7760 5636 6530 811 2073 22 C
ATOM 3016 O SER B 129 -27.626 22.219 78.573 1.00 52.93 O
ANISOU 3016 O SER B 129 7930 5659 6523 758 2345 -31 O
ATOM 3017 CB SER B 129 -27.424 18.939 79.010 1.00 58.74 C
ANISOU 3017 CB SER B 129 8707 6176 7435 796 1921 -142 C
ATOM 3018 OG SER B 129 -27.728 19.145 77.645 1.00 64.87 O
ANISOU 3018 OG SER B 129 9752 6922 7973 682 2105 -162 O
ATOM 3019 N VAL B 130 -28.936 21.458 80.248 1.00 50.61 N
ANISOU 3019 N VAL B 130 7486 5586 6157 820 1810 263 N
ATOM 3020 CA VAL B 130 -29.920 22.519 80.118 1.00 53.51 C
ANISOU 3020 CA VAL B 130 7918 6122 6291 782 1804 456 C
ATOM 3021 C VAL B 130 -29.328 23.862 80.545 1.00 54.02 C
ANISOU 3021 C VAL B 130 7817 6208 6500 866 1964 375 C
ATOM 3022 O VAL B 130 -29.503 24.890 79.872 1.00 56.96 O
ANISOU 3022 O VAL B 130 8285 6577 6782 808 2088 407 O
ATOM 3023 CB VAL B 130 -31.189 22.191 80.945 1.00 55.50 C
ANISOU 3023 CB VAL B 130 8121 6574 6392 782 1494 717 C
ATOM 3024 CG1 VAL B 130 -32.184 23.351 80.944 1.00 54.02 C
ANISOU 3024 CG1 VAL B 130 7951 6579 5994 783 1474 899 C
ATOM 3025 CG2 VAL B 130 -31.852 20.917 80.454 1.00 58.97 C
ANISOU 3025 CG2 VAL B 130 8721 6967 6718 662 1337 798 C
ATOM 3026 N SER B 131 -28.610 23.861 81.676 1.00 54.38 N
ANISOU 3026 N SER B 131 7601 6257 6803 993 1885 261 N
ATOM 3027 CA SER B 131 -27.915 25.042 82.199 1.00 51.75 C
ANISOU 3027 CA SER B 131 7059 5931 6673 1034 1928 135 C
ATOM 3028 C SER B 131 -26.927 25.612 81.180 1.00 51.23 C
ANISOU 3028 C SER B 131 7010 5706 6749 873 2114 -27 C
ATOM 3029 O SER B 131 -26.934 26.819 80.905 1.00 47.13 O
ANISOU 3029 O SER B 131 6502 5175 6231 808 2186 0 O
ATOM 3030 CB SER B 131 -27.200 24.659 83.500 1.00 54.71 C
ANISOU 3030 CB SER B 131 7163 6344 7281 1168 1720 -1 C
ATOM 3031 OG SER B 131 -26.546 25.750 84.126 1.00 58.37 O
ANISOU 3031 OG SER B 131 7412 6858 7908 1161 1633 -149 O
ATOM 3032 N VAL B 132 -26.057 24.760 80.621 1.00 52.56 N
ANISOU 3032 N VAL B 132 7181 5746 7042 825 2201 -183 N
ATOM 3033 CA VAL B 132 -25.106 25.220 79.607 1.00 50.97 C
ANISOU 3033 CA VAL B 132 6997 5415 6955 689 2407 -300 C
ATOM 3034 C VAL B 132 -25.854 25.828 78.417 1.00 54.56 C
ANISOU 3034 C VAL B 132 7751 5823 7156 595 2570 -139 C
ATOM 3035 O VAL B 132 -25.520 26.924 77.952 1.00 60.91 O
ANISOU 3035 O VAL B 132 8573 6553 8019 520 2705 -131 O
ATOM 3036 CB VAL B 132 -24.156 24.078 79.177 1.00 48.62 C
ANISOU 3036 CB VAL B 132 6663 5017 6792 679 2463 -478 C
ATOM 3037 CG1 VAL B 132 -23.259 24.508 78.009 1.00 55.82 C
ANISOU 3037 CG1 VAL B 132 7622 5805 7781 546 2723 -562 C
ATOM 3038 CG2 VAL B 132 -23.264 23.630 80.340 1.00 48.37 C
ANISOU 3038 CG2 VAL B 132 6328 5030 7022 795 2256 -650 C
ATOM 3039 N ALA B 133 -26.918 25.155 77.947 1.00 55.34 N
ANISOU 3039 N ALA B 133 8099 5964 6963 610 2529 -5 N
ATOM 3040 CA ALA B 133 -27.689 25.630 76.798 1.00 51.49 C
ANISOU 3040 CA ALA B 133 7892 5468 6203 546 2577 129 C
ATOM 3041 C ALA B 133 -28.302 27.013 77.045 1.00 57.56 C
ANISOU 3041 C ALA B 133 8638 6307 6925 566 2504 262 C
ATOM 3042 O ALA B 133 -28.148 27.924 76.223 1.00 61.92 O
ANISOU 3042 O ALA B 133 9301 6766 7460 519 2628 279 O
ATOM 3043 CB ALA B 133 -28.785 24.622 76.439 1.00 43.47 C
ANISOU 3043 CB ALA B 133 7091 4537 4886 550 2441 231 C
ATOM 3044 N VAL B 134 -29.016 27.184 78.168 1.00 57.62 N
ANISOU 3044 N VAL B 134 8514 6475 6905 652 2312 359 N
ATOM 3045 CA VAL B 134 -29.683 28.461 78.426 1.00 56.10 C
ANISOU 3045 CA VAL B 134 8299 6357 6659 690 2225 472 C
ATOM 3046 C VAL B 134 -28.657 29.568 78.763 1.00 53.71 C
ANISOU 3046 C VAL B 134 7855 5922 6631 677 2388 364 C
ATOM 3047 O VAL B 134 -28.845 30.714 78.351 1.00 57.44 O
ANISOU 3047 O VAL B 134 8415 6327 7084 667 2458 422 O
ATOM 3048 CB VAL B 134 -30.807 28.310 79.492 1.00 51.75 C
ANISOU 3048 CB VAL B 134 7641 6039 5982 784 1961 612 C
ATOM 3049 CG1 VAL B 134 -30.290 28.205 80.928 1.00 51.95 C
ANISOU 3049 CG1 VAL B 134 7424 6125 6190 895 1933 555 C
ATOM 3050 CG2 VAL B 134 -31.855 29.436 79.375 1.00 50.59 C
ANISOU 3050 CG2 VAL B 134 7521 5995 5704 807 1825 730 C
ATOM 3051 N LEU B 135 -27.539 29.235 79.433 1.00 50.38 N
ANISOU 3051 N LEU B 135 7205 5457 6480 667 2428 186 N
ATOM 3052 CA LEU B 135 -26.505 30.254 79.690 1.00 47.71 C
ANISOU 3052 CA LEU B 135 6695 5006 6428 615 2541 50 C
ATOM 3053 C LEU B 135 -25.782 30.676 78.407 1.00 50.30 C
ANISOU 3053 C LEU B 135 7173 5111 6829 483 2826 20 C
ATOM 3054 O LEU B 135 -25.399 31.841 78.261 1.00 51.40 O
ANISOU 3054 O LEU B 135 7305 5115 7111 430 2978 11 O
ATOM 3055 CB LEU B 135 -25.485 29.759 80.727 1.00 47.41 C
ANISOU 3055 CB LEU B 135 6338 5018 6656 650 2416 -168 C
ATOM 3056 CG LEU B 135 -25.835 29.785 82.224 1.00 49.81 C
ANISOU 3056 CG LEU B 135 6437 5514 6974 801 2130 -201 C
ATOM 3057 CD1 LEU B 135 -24.701 29.206 83.061 1.00 54.16 C
ANISOU 3057 CD1 LEU B 135 6724 6097 7756 859 1976 -434 C
ATOM 3058 CD2 LEU B 135 -26.182 31.187 82.714 1.00 47.73 C
ANISOU 3058 CD2 LEU B 135 6129 5277 6728 831 2098 -172 C
ATOM 3059 N THR B 136 -25.572 29.728 77.479 1.00 50.73 N
ANISOU 3059 N THR B 136 7368 5113 6792 435 2918 0 N
ATOM 3060 CA THR B 136 -24.931 30.020 76.192 1.00 48.49 C
ANISOU 3060 CA THR B 136 7254 4637 6534 334 3194 -23 C
ATOM 3061 C THR B 136 -25.777 30.991 75.364 1.00 49.67 C
ANISOU 3061 C THR B 136 7683 4731 6459 356 3251 146 C
ATOM 3062 O THR B 136 -25.264 31.986 74.836 1.00 51.59 O
ANISOU 3062 O THR B 136 7993 4793 6815 303 3477 145 O
ATOM 3063 CB THR B 136 -24.699 28.700 75.432 1.00 51.16 C
ANISOU 3063 CB THR B 136 7697 4975 6767 313 3238 -85 C
ATOM 3064 OG1 THR B 136 -23.819 27.852 76.183 1.00 47.75 O
ANISOU 3064 OG1 THR B 136 6990 4582 6572 319 3178 -263 O
ATOM 3065 CG2 THR B 136 -24.100 28.920 74.037 1.00 49.87 C
ANISOU 3065 CG2 THR B 136 7732 4641 6577 233 3523 -105 C
ATOM 3066 N LEU B 137 -27.085 30.711 75.259 1.00 53.71 N
ANISOU 3066 N LEU B 137 8342 5405 6662 440 3034 281 N
ATOM 3067 CA LEU B 137 -28.018 31.568 74.525 1.00 55.65 C
ANISOU 3067 CA LEU B 137 8804 5668 6673 486 2999 423 C
ATOM 3068 C LEU B 137 -28.090 32.967 75.129 1.00 60.94 C
ANISOU 3068 C LEU B 137 9405 6275 7476 526 3037 472 C
ATOM 3069 O LEU B 137 -28.189 33.964 74.399 1.00 70.42 O
ANISOU 3069 O LEU B 137 10774 7360 8625 537 3172 536 O
ATOM 3070 CB LEU B 137 -29.411 30.923 74.512 1.00 47.27 C
ANISOU 3070 CB LEU B 137 7806 4845 5310 547 2693 528 C
ATOM 3071 CG LEU B 137 -29.605 29.616 73.733 1.00 46.56 C
ANISOU 3071 CG LEU B 137 7849 4807 5032 509 2644 500 C
ATOM 3072 CD1 LEU B 137 -30.933 28.976 74.064 1.00 43.24 C
ANISOU 3072 CD1 LEU B 137 7406 4621 4403 537 2325 592 C
ATOM 3073 CD2 LEU B 137 -29.536 29.863 72.245 1.00 48.54 C
ANISOU 3073 CD2 LEU B 137 8361 4970 5114 484 2790 515 C
ATOM 3074 N SER B 138 -28.059 33.046 76.469 1.00 54.97 N
ANISOU 3074 N SER B 138 8412 5597 6879 561 2924 443 N
ATOM 3075 CA SER B 138 -28.050 34.318 77.198 1.00 53.15 C
ANISOU 3075 CA SER B 138 8090 5302 6802 600 2967 464 C
ATOM 3076 C SER B 138 -26.836 35.166 76.834 1.00 62.32 C
ANISOU 3076 C SER B 138 9237 6177 8263 488 3292 368 C
ATOM 3077 O SER B 138 -26.953 36.385 76.654 1.00 67.75 O
ANISOU 3077 O SER B 138 10027 6714 9000 509 3434 429 O
ATOM 3078 CB SER B 138 -28.046 34.060 78.709 1.00 50.37 C
ANISOU 3078 CB SER B 138 7449 5118 6572 653 2779 401 C
ATOM 3079 OG SER B 138 -29.185 33.344 79.155 1.00 46.22 O
ANISOU 3079 OG SER B 138 6925 4841 5795 759 2507 506 O
ATOM 3080 N PHE B 139 -25.656 34.535 76.766 1.00 63.19 N
ANISOU 3080 N PHE B 139 9204 6209 8598 371 3416 209 N
ATOM 3081 CA PHE B 139 -24.413 35.243 76.464 1.00 64.59 C
ANISOU 3081 CA PHE B 139 9311 6122 9110 239 3725 91 C
ATOM 3082 C PHE B 139 -24.335 35.659 74.995 1.00 68.70 C
ANISOU 3082 C PHE B 139 10150 6442 9511 217 3996 167 C
ATOM 3083 O PHE B 139 -23.625 36.617 74.665 1.00 70.43 O
ANISOU 3083 O PHE B 139 10392 6407 9963 143 4287 125 O
ATOM 3084 CB PHE B 139 -23.196 34.375 76.833 1.00 66.29 C
ANISOU 3084 CB PHE B 139 9237 6357 9592 140 3733 -122 C
ATOM 3085 CG PHE B 139 -22.901 34.286 78.327 1.00 73.50 C
ANISOU 3085 CG PHE B 139 9777 7438 10710 174 3483 -273 C
ATOM 3086 CD1 PHE B 139 -23.906 34.424 79.273 1.00 67.81 C
ANISOU 3086 CD1 PHE B 139 9017 6924 9825 313 3205 -199 C
ATOM 3087 CD2 PHE B 139 -21.603 34.053 78.776 1.00 83.53 C
ANISOU 3087 CD2 PHE B 139 10740 8673 12324 96 3499 -508 C
ATOM 3088 CE1 PHE B 139 -23.625 34.335 80.633 1.00 66.91 C
ANISOU 3088 CE1 PHE B 139 8589 6978 9857 391 2937 -361 C
ATOM 3089 CE2 PHE B 139 -21.318 33.963 80.134 1.00 83.54 C
ANISOU 3089 CE2 PHE B 139 10425 8843 12475 177 3207 -671 C
ATOM 3090 CZ PHE B 139 -22.330 34.105 81.062 1.00 75.60 C
ANISOU 3090 CZ PHE B 139 9412 8040 11271 333 2921 -598 C
ATOM 3091 N ILE B 140 -25.033 34.941 74.098 1.00 64.97 N
ANISOU 3091 N ILE B 140 9912 6092 8681 281 3903 260 N
ATOM 3092 CA ILE B 140 -25.153 35.373 72.701 1.00 61.20 C
ANISOU 3092 CA ILE B 140 9742 5505 8004 295 4095 344 C
ATOM 3093 C ILE B 140 -25.988 36.651 72.626 1.00 63.55 C
ANISOU 3093 C ILE B 140 10192 5773 8182 392 4084 483 C
ATOM 3094 O ILE B 140 -25.602 37.628 71.967 1.00 66.18 O
ANISOU 3094 O ILE B 140 10669 5899 8578 375 4360 512 O
ATOM 3095 CB ILE B 140 -25.751 34.247 71.826 1.00 58.42 C
ANISOU 3095 CB ILE B 140 9569 5328 7300 331 3951 391 C
ATOM 3096 CG1 ILE B 140 -24.802 33.039 71.713 1.00 60.70 C
ANISOU 3096 CG1 ILE B 140 9749 5603 7712 242 4036 245 C
ATOM 3097 CG2 ILE B 140 -26.064 34.754 70.414 1.00 63.23 C
ANISOU 3097 CG2 ILE B 140 10500 5880 7645 365 4092 498 C
ATOM 3098 CD1 ILE B 140 -25.474 31.708 71.285 1.00 60.83 C
ANISOU 3098 CD1 ILE B 140 9873 5810 7428 283 3832 260 C
ATOM 3099 N ALA B 141 -27.128 36.665 73.334 1.00 63.77 N
ANISOU 3099 N ALA B 141 10176 6009 8045 498 3774 571 N
ATOM 3100 CA ALA B 141 -28.011 37.830 73.414 1.00 59.81 C
ANISOU 3100 CA ALA B 141 9781 5516 7430 607 3721 699 C
ATOM 3101 C ALA B 141 -27.288 39.042 73.998 1.00 60.22 C
ANISOU 3101 C ALA B 141 9748 5304 7829 578 3985 649 C
ATOM 3102 O ALA B 141 -27.441 40.166 73.505 1.00 62.33 O
ANISOU 3102 O ALA B 141 10185 5428 8068 622 4156 726 O
ATOM 3103 CB ALA B 141 -29.237 37.488 74.268 1.00 54.82 C
ANISOU 3103 CB ALA B 141 9042 5169 6619 711 3342 771 C
ATOM 3104 N LEU B 142 -26.502 38.811 75.053 1.00 61.27 N
ANISOU 3104 N LEU B 142 9602 5377 8302 492 4011 514 N
ATOM 3105 CA LEU B 142 -25.734 39.855 75.727 1.00 66.00 C
ANISOU 3105 CA LEU B 142 10047 5719 9311 418 4242 425 C
ATOM 3106 C LEU B 142 -24.675 40.462 74.808 1.00 69.61 C
ANISOU 3106 C LEU B 142 10595 5862 9992 312 4647 346 C
ATOM 3107 O LEU B 142 -24.424 41.672 74.840 1.00 65.40 O
ANISOU 3107 O LEU B 142 10086 5090 9673 309 4895 330 O
ATOM 3108 CB LEU B 142 -25.075 39.246 76.964 1.00 64.07 C
ANISOU 3108 CB LEU B 142 9417 5580 9348 306 4100 270 C
ATOM 3109 CG LEU B 142 -24.454 40.183 77.988 1.00 62.14 C
ANISOU 3109 CG LEU B 142 8877 5220 9511 209 4180 143 C
ATOM 3110 CD1 LEU B 142 -25.538 40.952 78.722 1.00 67.58 C
ANISOU 3110 CD1 LEU B 142 9590 6031 10056 359 4020 261 C
ATOM 3111 CD2 LEU B 142 -23.598 39.397 78.958 1.00 53.44 C
ANISOU 3111 CD2 LEU B 142 7354 4315 8636 132 3969 -102 C
ATOM 3112 N ASP B 143 -24.027 39.608 74.008 1.00 73.07 N
ANISOU 3112 N ASP B 143 11070 6302 10391 229 4734 287 N
ATOM 3113 CA ASP B 143 -23.016 40.013 73.036 1.00 71.62 C
ANISOU 3113 CA ASP B 143 10977 5864 10372 133 5122 223 C
ATOM 3114 C ASP B 143 -23.633 40.829 71.901 1.00 76.89 C
ANISOU 3114 C ASP B 143 11999 6489 10725 233 5263 403 C
ATOM 3115 O ASP B 143 -23.077 41.858 71.492 1.00 80.34 O
ANISOU 3115 O ASP B 143 12501 6682 11343 192 5602 396 O
ATOM 3116 CB ASP B 143 -22.327 38.743 72.517 1.00 71.54 C
ANISOU 3116 CB ASP B 143 10920 5925 10337 44 5134 137 C
ATOM 3117 CG ASP B 143 -21.464 38.970 71.292 1.00 84.78 C
ANISOU 3117 CG ASP B 143 12750 7402 12060 -29 5520 115 C
ATOM 3118 OD1 ASP B 143 -20.362 39.536 71.435 1.00 92.15 O
ANISOU 3118 OD1 ASP B 143 13515 8088 13412 -150 5815 -28 O
ATOM 3119 OD2 ASP B 143 -21.859 38.517 70.194 1.00 88.45 O
ANISOU 3119 OD2 ASP B 143 13485 7967 12156 26 5524 230 O
ATOM 3120 N ARG B 144 -24.787 40.374 71.395 1.00 74.63 N
ANISOU 3120 N ARG B 144 11923 6453 9981 352 4992 561 N
ATOM 3121 CA ARG B 144 -25.516 41.074 70.340 1.00 75.65 C
ANISOU 3121 CA ARG B 144 12378 6592 9775 445 5037 747 C
ATOM 3122 C ARG B 144 -26.119 42.376 70.858 1.00 73.24 C
ANISOU 3122 C ARG B 144 12101 6221 9506 534 5037 837 C
ATOM 3123 O ARG B 144 -26.148 43.385 70.142 1.00 71.59 O
ANISOU 3123 O ARG B 144 12105 5865 9232 558 5254 948 O
ATOM 3124 CB ARG B 144 -26.623 40.169 69.776 1.00 71.78 C
ANISOU 3124 CB ARG B 144 12037 6399 8836 533 4694 855 C
ATOM 3125 CG ARG B 144 -26.168 38.876 69.068 1.00 72.44 C
ANISOU 3125 CG ARG B 144 12153 6557 8815 465 4703 788 C
ATOM 3126 CD ARG B 144 -25.306 39.151 67.841 1.00 77.52 C
ANISOU 3126 CD ARG B 144 13001 7000 9452 404 5091 802 C
ATOM 3127 NE ARG B 144 -23.912 39.375 68.213 1.00 78.16 N
ANISOU 3127 NE ARG B 144 12888 6834 9974 272 5425 648 N
ATOM 3128 CZ ARG B 144 -23.104 40.238 67.607 1.00 77.07 C
ANISOU 3128 CZ ARG B 144 12845 6443 9994 211 5828 657 C
ATOM 3129 NH1 ARG B 144 -23.551 40.973 66.598 1.00 72.30 N
ANISOU 3129 NH1 ARG B 144 12556 5799 9115 281 5951 836 N
ATOM 3130 NH2 ARG B 144 -21.851 40.376 68.019 1.00 79.27 N
ANISOU 3130 NH2 ARG B 144 12890 6510 10718 76 6105 488 N
ATOM 3131 N TRP B 145 -26.606 42.359 72.104 1.00 70.92 N
ANISOU 3131 N TRP B 145 11603 6035 9308 588 4803 800 N
ATOM 3132 CA TRP B 145 -27.186 43.547 72.724 1.00 66.96 C
ANISOU 3132 CA TRP B 145 11107 5480 8854 682 4802 874 C
ATOM 3133 C TRP B 145 -26.143 44.658 72.875 1.00 67.20 C
ANISOU 3133 C TRP B 145 11061 5173 9298 587 5221 780 C
ATOM 3134 O TRP B 145 -26.423 45.819 72.561 1.00 71.75 O
ANISOU 3134 O TRP B 145 11796 5631 9833 632 5366 897 O
ATOM 3135 CB TRP B 145 -27.810 43.167 74.074 1.00 58.06 C
ANISOU 3135 CB TRP B 145 9759 4540 7761 757 4493 843 C
ATOM 3136 CG TRP B 145 -28.696 44.223 74.674 1.00 56.59 C
ANISOU 3136 CG TRP B 145 9610 4376 7517 897 4418 950 C
ATOM 3137 CD1 TRP B 145 -29.962 44.558 74.282 1.00 55.51 C
ANISOU 3137 CD1 TRP B 145 9665 4418 7009 1041 4183 1131 C
ATOM 3138 CD2 TRP B 145 -28.377 45.081 75.776 1.00 58.71 C
ANISOU 3138 CD2 TRP B 145 9694 4483 8130 902 4577 872 C
ATOM 3139 NE1 TRP B 145 -30.448 45.575 75.071 1.00 56.37 N
ANISOU 3139 NE1 TRP B 145 9747 4484 7185 1147 4180 1186 N
ATOM 3140 CE2 TRP B 145 -29.494 45.914 75.994 1.00 58.50 C
ANISOU 3140 CE2 TRP B 145 9791 4553 7883 1060 4431 1036 C
ATOM 3141 CE3 TRP B 145 -27.255 45.227 76.596 1.00 60.34 C
ANISOU 3141 CE3 TRP B 145 9589 4519 8817 744 4769 675 C
ATOM 3142 CZ2 TRP B 145 -29.518 46.880 77.002 1.00 60.34 C
ANISOU 3142 CZ2 TRP B 145 9888 4697 8343 1082 4516 1024 C
ATOM 3143 CZ3 TRP B 145 -27.280 46.187 77.594 1.00 62.35 C
ANISOU 3143 CZ3 TRP B 145 9633 4766 9291 705 4812 661 C
ATOM 3144 CH2 TRP B 145 -28.404 47.001 77.788 1.00 62.22 C
ANISOU 3144 CH2 TRP B 145 9800 4796 9044 892 4733 839 C
ATOM 3145 N TYR B 146 -24.927 44.318 73.322 1.00 65.33 N
ANISOU 3145 N TYR B 146 10566 4775 9482 442 5408 564 N
ATOM 3146 CA TYR B 146 -23.871 45.328 73.387 1.00 70.30 C
ANISOU 3146 CA TYR B 146 11067 5092 10553 328 5814 437 C
ATOM 3147 C TYR B 146 -23.246 45.622 72.019 1.00 77.89 C
ANISOU 3147 C TYR B 146 12252 5888 11454 253 6143 505 C
ATOM 3148 O TYR B 146 -22.789 46.744 71.789 1.00 84.17 O
ANISOU 3148 O TYR B 146 13067 6454 12461 196 6463 518 O
ATOM 3149 CB TYR B 146 -22.778 44.917 74.387 1.00 65.89 C
ANISOU 3149 CB TYR B 146 10081 4455 10500 170 5828 166 C
ATOM 3150 CG TYR B 146 -23.119 45.171 75.850 1.00 65.63 C
ANISOU 3150 CG TYR B 146 9720 4594 10622 147 5529 118 C
ATOM 3151 CD1 TYR B 146 -23.096 46.458 76.383 1.00 66.76 C
ANISOU 3151 CD1 TYR B 146 9716 4644 11006 129 5685 89 C
ATOM 3152 CD2 TYR B 146 -23.447 44.121 76.700 1.00 59.63 C
ANISOU 3152 CD2 TYR B 146 8802 4071 9785 125 5135 116 C
ATOM 3153 CE1 TYR B 146 -23.404 46.690 77.718 1.00 58.50 C
ANISOU 3153 CE1 TYR B 146 8348 3776 10101 70 5463 63 C
ATOM 3154 CE2 TYR B 146 -23.755 44.345 78.035 1.00 52.80 C
ANISOU 3154 CE2 TYR B 146 7657 3344 9060 65 4919 111 C
ATOM 3155 CZ TYR B 146 -23.732 45.630 78.538 1.00 54.60 C
ANISOU 3155 CZ TYR B 146 7733 3485 9528 31 5082 81 C
ATOM 3156 OH TYR B 146 -24.036 45.857 79.862 1.00 52.83 O
ANISOU 3156 OH TYR B 146 7243 3382 9448 87 4779 -43 O
ATOM 3157 N ALA B 147 -23.225 44.647 71.098 1.00 75.07 N
ANISOU 3157 N ALA B 147 12062 5645 10814 247 6081 559 N
ATOM 3158 CA ALA B 147 -22.659 44.893 69.769 1.00 74.57 C
ANISOU 3158 CA ALA B 147 12231 5434 10666 187 6411 639 C
ATOM 3159 C ALA B 147 -23.497 45.888 68.969 1.00 80.92 C
ANISOU 3159 C ALA B 147 13387 6221 11138 293 6455 895 C
ATOM 3160 O ALA B 147 -22.940 46.682 68.196 1.00 89.80 O
ANISOU 3160 O ALA B 147 14661 7122 12337 232 6820 969 O
ATOM 3161 CB ALA B 147 -22.530 43.577 68.998 1.00 70.83 C
ANISOU 3161 CB ALA B 147 11854 5115 9945 170 6318 637 C
ATOM 3162 N ILE B 148 -24.818 45.875 69.169 1.00 76.78 N
ANISOU 3162 N ILE B 148 12985 5922 10268 445 6087 1034 N
ATOM 3163 CA ILE B 148 -25.781 46.626 68.367 1.00 78.67 C
ANISOU 3163 CA ILE B 148 13565 6193 10134 568 6030 1281 C
ATOM 3164 C ILE B 148 -26.373 47.812 69.141 1.00 81.88 C
ANISOU 3164 C ILE B 148 13945 6531 10634 640 5978 1354 C
ATOM 3165 O ILE B 148 -26.357 48.944 68.658 1.00 85.76 O
ANISOU 3165 O ILE B 148 14628 6825 11131 644 6200 1493 O
ATOM 3166 CB ILE B 148 -26.890 45.680 67.835 1.00 70.90 C
ANISOU 3166 CB ILE B 148 12740 5526 8671 687 5631 1381 C
ATOM 3167 CG1 ILE B 148 -26.270 44.613 66.921 1.00 71.79 C
ANISOU 3167 CG1 ILE B 148 12921 5675 8679 612 5731 1328 C
ATOM 3168 CG2 ILE B 148 -28.011 46.447 67.118 1.00 75.45 C
ANISOU 3168 CG2 ILE B 148 13632 6157 8877 832 5504 1617 C
ATOM 3169 CD1 ILE B 148 -27.126 43.386 66.702 1.00 68.79 C
ANISOU 3169 CD1 ILE B 148 12565 5611 7959 680 5335 1339 C
ATOM 3170 N CYS B 149 -26.884 47.574 70.364 1.00 73.70 N
ANISOU 3170 N CYS B 149 12676 5647 9678 695 5696 1269 N
ATOM 3171 CA CYS B 149 -27.587 48.635 71.096 1.00 74.07 C
ANISOU 3171 CA CYS B 149 12717 5663 9764 785 5607 1355 C
ATOM 3172 C CYS B 149 -26.660 49.568 71.888 1.00 79.07 C
ANISOU 3172 C CYS B 149 13116 6017 10910 657 5917 1228 C
ATOM 3173 O CYS B 149 -26.963 50.758 72.012 1.00 90.79 O
ANISOU 3173 O CYS B 149 14691 7351 12454 683 5981 1343 O
ATOM 3174 CB CYS B 149 -28.637 48.033 72.035 1.00 73.70 C
ANISOU 3174 CB CYS B 149 12541 5912 9549 916 5173 1346 C
ATOM 3175 SG CYS B 149 -29.991 47.191 71.175 1.00 76.87 S
ANISOU 3175 SG CYS B 149 13167 6655 9384 1063 4748 1502 S
ATOM 3176 N HIS B 150 -25.545 49.064 72.435 1.00 73.94 N
ANISOU 3176 N HIS B 150 12146 5289 10658 512 6086 984 N
ATOM 3177 CA HIS B 150 -24.597 49.881 73.206 1.00 72.08 C
ANISOU 3177 CA HIS B 150 11601 4811 10975 361 6355 814 C
ATOM 3178 C HIS B 150 -23.192 49.562 72.692 1.00 75.92 C
ANISOU 3178 C HIS B 150 11954 5110 11782 192 6704 636 C
ATOM 3179 O HIS B 150 -22.433 48.805 73.312 1.00 75.82 O
ANISOU 3179 O HIS B 150 11613 5119 12075 113 6706 383 O
ATOM 3180 CB HIS B 150 -24.804 49.651 74.708 1.00 67.55 C
ANISOU 3180 CB HIS B 150 10673 4377 10617 373 6123 661 C
ATOM 3181 CG HIS B 150 -26.239 49.812 75.118 1.00 64.81 C
ANISOU 3181 CG HIS B 150 10493 4231 9899 560 5758 855 C
ATOM 3182 ND1 HIS B 150 -26.807 51.040 75.382 1.00 67.78 N
ANISOU 3182 ND1 HIS B 150 10969 4485 10297 608 5698 987 N
ATOM 3183 CD2 HIS B 150 -27.240 48.907 75.216 1.00 63.67 C
ANISOU 3183 CD2 HIS B 150 10455 4384 9353 725 5416 941 C
ATOM 3184 CE1 HIS B 150 -28.086 50.882 75.662 1.00 64.69 C
ANISOU 3184 CE1 HIS B 150 10726 4318 9536 809 5344 1135 C
ATOM 3185 NE2 HIS B 150 -28.379 49.595 75.569 1.00 64.06 N
ANISOU 3185 NE2 HIS B 150 10639 4508 9192 877 5176 1112 N
ATOM 3186 N PRO B 151 -22.804 50.175 71.557 1.00 79.06 N
ANISOU 3186 N PRO B 151 12600 5305 12134 135 7012 768 N
ATOM 3187 CA PRO B 151 -21.668 49.676 70.759 1.00 81.95 C
ANISOU 3187 CA PRO B 151 12949 5542 12646 10 7315 667 C
ATOM 3188 C PRO B 151 -20.252 49.763 71.338 1.00 92.57 C
ANISOU 3188 C PRO B 151 13867 6678 14627 -177 7592 364 C
ATOM 3189 O PRO B 151 -19.431 48.942 70.928 1.00103.38 O
ANISOU 3189 O PRO B 151 15167 8022 16091 -252 7712 236 O
ATOM 3190 CB PRO B 151 -21.758 50.529 69.487 1.00 86.97 C
ANISOU 3190 CB PRO B 151 13975 6008 13062 11 7581 926 C
ATOM 3191 CG PRO B 151 -23.187 50.731 69.313 1.00 84.99 C
ANISOU 3191 CG PRO B 151 14029 5940 12322 199 7258 1168 C
ATOM 3192 CD PRO B 151 -23.689 51.009 70.720 1.00 81.33 C
ANISOU 3192 CD PRO B 151 13303 5558 12042 241 7000 1073 C
ATOM 3193 N LEU B 152 -19.869 50.729 72.172 1.00 92.84 N
ANISOU 3193 N LEU B 152 13608 6549 15118 -269 7702 240 N
ATOM 3194 CA LEU B 152 -18.443 50.752 72.519 1.00 96.78 C
ANISOU 3194 CA LEU B 152 13693 6850 16229 -449 7969 -69 C
ATOM 3195 C LEU B 152 -18.193 50.659 74.028 1.00103.56 C
ANISOU 3195 C LEU B 152 14034 7789 17526 -482 7761 -373 C
ATOM 3196 O LEU B 152 -17.179 51.152 74.530 1.00113.53 O
ANISOU 3196 O LEU B 152 14897 8873 19367 -628 7933 -628 O
ATOM 3197 CB LEU B 152 -17.750 51.968 71.900 1.00 96.76 C
ANISOU 3197 CB LEU B 152 13739 6516 16511 -594 8391 0 C
ATOM 3198 CG LEU B 152 -17.846 52.020 70.363 1.00 98.14 C
ANISOU 3198 CG LEU B 152 14398 6612 16279 -574 8641 289 C
ATOM 3199 CD1 LEU B 152 -17.733 53.453 69.850 1.00103.84 C
ANISOU 3199 CD1 LEU B 152 15292 7038 17127 -660 8958 482 C
ATOM 3200 CD2 LEU B 152 -16.821 51.116 69.667 1.00100.01 C
ANISOU 3200 CD2 LEU B 152 14590 6810 16600 -660 8869 164 C
ATOM 3201 N LEU B 153 -19.084 49.961 74.740 1.00 98.91 N
ANISOU 3201 N LEU B 153 13426 7485 16670 -348 7379 -360 N
ATOM 3202 CA LEU B 153 -18.940 49.718 76.175 1.00 89.17 C
ANISOU 3202 CA LEU B 153 11703 6447 15732 -418 7037 -579 C
ATOM 3203 C LEU B 153 -18.024 48.523 76.464 1.00 82.82 C
ANISOU 3203 C LEU B 153 10618 5771 15079 -523 6808 -802 C
ATOM 3204 O LEU B 153 -17.002 48.668 77.143 1.00 79.33 O
ANISOU 3204 O LEU B 153 9728 5276 15140 -663 6788 -1085 O
ATOM 3205 CB LEU B 153 -20.317 49.488 76.803 1.00 82.00 C
ANISOU 3205 CB LEU B 153 10917 5829 14412 -284 6647 -389 C
ATOM 3206 CG LEU B 153 -21.259 50.672 77.032 1.00 83.09 C
ANISOU 3206 CG LEU B 153 11229 5891 14451 -220 6612 -192 C
ATOM 3207 CD1 LEU B 153 -22.279 50.288 78.089 1.00 75.27 C
ANISOU 3207 CD1 LEU B 153 10180 5175 13246 -137 6126 -129 C
ATOM 3208 CD2 LEU B 153 -20.519 51.957 77.408 1.00 90.37 C
ANISOU 3208 CD2 LEU B 153 11901 6517 15917 -385 6746 -334 C
ATOM 3209 N PHE B 154 -18.381 47.333 75.964 1.00 80.08 N
ANISOU 3209 N PHE B 154 10531 5574 14322 -452 6623 -687 N
ATOM 3210 CA PHE B 154 -17.617 46.109 76.207 1.00 85.35 C
ANISOU 3210 CA PHE B 154 10996 6329 15106 -555 6402 -858 C
ATOM 3211 C PHE B 154 -17.110 45.490 74.905 1.00 95.71 C
ANISOU 3211 C PHE B 154 12579 7491 16297 -573 6705 -811 C
ATOM 3212 O PHE B 154 -17.836 45.438 73.900 1.00 98.63 O
ANISOU 3212 O PHE B 154 13393 7832 16248 -447 6850 -580 O
ATOM 3213 CB PHE B 154 -18.455 45.091 77.023 1.00 78.88 C
ANISOU 3213 CB PHE B 154 10157 5819 13993 -525 5882 -769 C
ATOM 3214 CG PHE B 154 -18.819 45.592 78.400 1.00 76.49 C
ANISOU 3214 CG PHE B 154 9521 5671 13872 -620 5606 -796 C
ATOM 3215 CD1 PHE B 154 -17.906 45.525 79.443 1.00 74.45 C
ANISOU 3215 CD1 PHE B 154 8746 5458 14083 -762 5460 -1105 C
ATOM 3216 CD2 PHE B 154 -20.052 46.180 78.638 1.00 79.39 C
ANISOU 3216 CD2 PHE B 154 10035 6179 13950 -490 5564 -584 C
ATOM 3217 CE1 PHE B 154 -18.224 46.018 80.703 1.00 76.97 C
ANISOU 3217 CE1 PHE B 154 8754 5877 14615 -756 5227 -1238 C
ATOM 3218 CE2 PHE B 154 -20.376 46.675 79.895 1.00 79.74 C
ANISOU 3218 CE2 PHE B 154 9792 6279 14226 -489 5371 -699 C
ATOM 3219 CZ PHE B 154 -19.461 46.593 80.928 1.00 79.17 C
ANISOU 3219 CZ PHE B 154 9227 6206 14649 -629 5193 -1036 C
ATOM 3220 N LYS B 155 -15.851 45.029 74.934 1.00 99.74 N
ANISOU 3220 N LYS B 155 12814 7897 17185 -724 6799 -1047 N
ATOM 3221 CA LYS B 155 -15.163 44.411 73.800 1.00100.96 C
ANISOU 3221 CA LYS B 155 13148 7889 17322 -770 7118 -1057 C
ATOM 3222 C LYS B 155 -15.461 42.913 73.752 1.00 97.84 C
ANISOU 3222 C LYS B 155 12835 7725 16613 -752 6817 -1003 C
ATOM 3223 O LYS B 155 -15.357 42.227 74.776 1.00 97.10 O
ANISOU 3223 O LYS B 155 12431 7841 16620 -807 6438 -1122 O
ATOM 3224 CB LYS B 155 -13.649 44.636 73.908 1.00105.49 C
ANISOU 3224 CB LYS B 155 13350 8236 18494 -942 7377 -1358 C
ATOM 3225 CG LYS B 155 -12.919 44.696 72.566 1.00111.28 C
ANISOU 3225 CG LYS B 155 14315 8656 19311 -987 7936 -1349 C
ATOM 3226 CD LYS B 155 -11.426 44.960 72.722 1.00118.11 C
ANISOU 3226 CD LYS B 155 14779 9282 20815 -1158 8206 -1664 C
ATOM 3227 CE LYS B 155 -10.673 44.663 71.432 1.00123.20 C
ANISOU 3227 CE LYS B 155 15582 9825 21404 -1244 8619 -1594 C
ATOM 3228 NZ LYS B 155 -9.243 45.065 71.527 1.00128.44 N
ANISOU 3228 NZ LYS B 155 15855 10235 22710 -1411 8934 -1888 N
ATOM 3229 N SER B 156 -15.795 42.398 72.562 1.00 99.20 N
ANISOU 3229 N SER B 156 13411 7868 16413 -679 6992 -829 N
ATOM 3230 CA SER B 156 -16.138 40.984 72.386 1.00 96.19 C
ANISOU 3230 CA SER B 156 13102 7775 15672 -651 6705 -751 C
ATOM 3231 C SER B 156 -15.202 40.358 71.354 1.00 97.20 C
ANISOU 3231 C SER B 156 13264 7862 15807 -734 6981 -799 C
ATOM 3232 O SER B 156 -15.265 40.686 70.161 1.00101.77 O
ANISOU 3232 O SER B 156 14153 8370 16144 -700 7274 -643 O
ATOM 3233 CB SER B 156 -17.614 40.813 71.998 1.00 95.60 C
ANISOU 3233 CB SER B 156 13402 7928 14994 -470 6476 -467 C
ATOM 3234 OG SER B 156 -17.869 41.053 70.623 1.00 97.28 O
ANISOU 3234 OG SER B 156 13991 8116 14855 -407 6716 -278 O
ATOM 3235 N THR B 157 -14.376 39.412 71.816 1.00 96.55 N
ANISOU 3235 N THR B 157 12859 7858 15967 -836 6865 -1002 N
ATOM 3236 CA THR B 157 -13.387 38.724 71.000 1.00100.86 C
ANISOU 3236 CA THR B 157 13361 8382 16578 -915 7112 -1090 C
ATOM 3237 C THR B 157 -13.563 37.215 71.175 1.00100.21 C
ANISOU 3237 C THR B 157 13209 8612 16255 -874 6786 -1104 C
ATOM 3238 O THR B 157 -14.063 36.751 72.210 1.00 98.21 O
ANISOU 3238 O THR B 157 12792 8560 15964 -832 6382 -1128 O
ATOM 3239 CB THR B 157 -11.953 39.161 71.415 1.00104.75 C
ANISOU 3239 CB THR B 157 13446 8635 17720 -1080 7348 -1391 C
ATOM 3240 OG1 THR B 157 -11.740 38.867 72.802 1.00108.06 O
ANISOU 3240 OG1 THR B 157 13463 9148 18446 -1127 6979 -1601 O
ATOM 3241 CG2 THR B 157 -11.782 40.691 71.260 1.00101.22 C
ANISOU 3241 CG2 THR B 157 13049 7868 17540 -1111 7694 -1391 C
ATOM 3242 N ALA B 158 -13.093 36.443 70.182 1.00108.32 N
ANISOU 3242 N ALA B 158 14338 9687 17131 -881 6978 -1100 N
ATOM 3243 CA ALA B 158 -13.183 34.979 70.210 1.00104.97 C
ANISOU 3243 CA ALA B 158 13858 9540 16486 -825 6725 -1132 C
ATOM 3244 C ALA B 158 -12.427 34.399 71.398 1.00115.21 C
ANISOU 3244 C ALA B 158 14677 10932 18166 -880 6481 -1387 C
ATOM 3245 O ALA B 158 -12.818 33.358 71.945 1.00113.76 O
ANISOU 3245 O ALA B 158 14405 11013 17806 -794 6125 -1399 O
ATOM 3246 CB ALA B 158 -12.637 34.393 68.902 1.00 99.31 C
ANISOU 3246 CB ALA B 158 13307 8816 15609 -831 7044 -1121 C
ATOM 3247 N ARG B 159 -11.332 35.065 71.783 1.00127.60 N
ANISOU 3247 N ARG B 159 15934 12289 20260 -1011 6669 -1604 N
ATOM 3248 CA ARG B 159 -10.525 34.682 72.939 1.00130.18 C
ANISOU 3248 CA ARG B 159 15779 12691 20991 -1059 6425 -1879 C
ATOM 3249 C ARG B 159 -11.316 34.836 74.236 1.00126.32 C
ANISOU 3249 C ARG B 159 15172 12365 20460 -996 5978 -1857 C
ATOM 3250 O ARG B 159 -11.242 33.976 75.121 1.00126.33 O
ANISOU 3250 O ARG B 159 14924 12615 20460 -922 5607 -1967 O
ATOM 3251 CB ARG B 159 -9.270 35.556 73.006 1.00137.45 C
ANISOU 3251 CB ARG B 159 16416 13310 22499 -1216 6738 -2122 C
ATOM 3252 CG ARG B 159 -8.105 34.902 73.731 1.00144.64 C
ANISOU 3252 CG ARG B 159 16844 14295 23818 -1258 6586 -2447 C
ATOM 3253 CD ARG B 159 -7.193 35.859 74.481 1.00152.76 C
ANISOU 3253 CD ARG B 159 17496 15082 25465 -1390 6643 -2732 C
ATOM 3254 NE ARG B 159 -6.101 35.107 75.100 1.00158.09 N
ANISOU 3254 NE ARG B 159 17727 15861 26478 -1399 6461 -3045 N
ATOM 3255 CZ ARG B 159 -6.152 34.506 76.284 1.00155.88 C
ANISOU 3255 CZ ARG B 159 17187 15830 26211 -1306 5965 -3173 C
ATOM 3256 NH1 ARG B 159 -5.089 33.854 76.738 1.00157.95 N
ANISOU 3256 NH1 ARG B 159 17071 16164 26781 -1290 5829 -3464 N
ATOM 3257 NH2 ARG B 159 -7.274 34.507 76.989 1.00150.55 N
ANISOU 3257 NH2 ARG B 159 16641 15350 25209 -1202 5603 -3003 N
ATOM 3258 N ARG B 160 -12.053 35.951 74.367 1.00124.32 N
ANISOU 3258 N ARG B 160 15094 11975 20166 -1003 6020 -1719 N
ATOM 3259 CA ARG B 160 -12.926 36.180 75.521 1.00118.91 C
ANISOU 3259 CA ARG B 160 14331 11461 19390 -934 5627 -1666 C
ATOM 3260 C ARG B 160 -14.152 35.274 75.489 1.00110.65 C
ANISOU 3260 C ARG B 160 13529 10727 17785 -768 5330 -1438 C
ATOM 3261 O ARG B 160 -14.719 34.968 76.545 1.00107.44 O
ANISOU 3261 O ARG B 160 12985 10568 17269 -672 4936 -1435 O
ATOM 3262 CB ARG B 160 -13.366 37.652 75.579 1.00121.81 C
ANISOU 3262 CB ARG B 160 14829 11571 19881 -976 5797 -1585 C
ATOM 3263 CG ARG B 160 -12.600 38.512 76.588 1.00127.31 C
ANISOU 3263 CG ARG B 160 15127 12101 21146 -1096 5767 -1856 C
ATOM 3264 CD ARG B 160 -13.068 39.963 76.590 1.00131.68 C
ANISOU 3264 CD ARG B 160 15808 12456 21767 -1093 5927 -1766 C
ATOM 3265 NE ARG B 160 -12.474 40.691 75.478 1.00139.82 N
ANISOU 3265 NE ARG B 160 17007 13170 22948 -1132 6429 -1767 N
ATOM 3266 CZ ARG B 160 -11.496 41.575 75.613 1.00146.82 C
ANISOU 3266 CZ ARG B 160 17632 13834 24319 -1224 6652 -1987 C
ATOM 3267 NH1 ARG B 160 -11.019 41.854 76.818 1.00146.57 N
ANISOU 3267 NH1 ARG B 160 17163 13873 24652 -1281 6372 -2232 N
ATOM 3268 NH2 ARG B 160 -10.995 42.182 74.547 1.00152.85 N
ANISOU 3268 NH2 ARG B 160 18569 14293 25214 -1254 7165 -1973 N
ATOM 3269 N ALA B 161 -14.559 34.841 74.290 1.00105.19 N
ANISOU 3269 N ALA B 161 13195 10033 16739 -721 5509 -1263 N
ATOM 3270 CA ALA B 161 -15.673 33.907 74.138 1.00 98.89 C
ANISOU 3270 CA ALA B 161 12628 9500 15445 -575 5249 -1081 C
ATOM 3271 C ALA B 161 -15.329 32.528 74.705 1.00100.03 C
ANISOU 3271 C ALA B 161 12527 9896 15583 -509 4969 -1220 C
ATOM 3272 O ALA B 161 -16.181 31.888 75.334 1.00102.07 O
ANISOU 3272 O ALA B 161 12800 10395 15588 -383 4623 -1147 O
ATOM 3273 CB ALA B 161 -16.064 33.805 72.661 1.00 98.00 C
ANISOU 3273 CB ALA B 161 12937 9313 14987 -544 5509 -907 C
ATOM 3274 N LEU B 162 -14.091 32.061 74.490 1.00 97.38 N
ANISOU 3274 N LEU B 162 11972 9498 15529 -575 5120 -1427 N
ATOM 3275 CA LEU B 162 -13.643 30.787 75.058 1.00 92.62 C
ANISOU 3275 CA LEU B 162 11124 9108 14961 -484 4859 -1584 C
ATOM 3276 C LEU B 162 -13.601 30.838 76.581 1.00 89.09 C
ANISOU 3276 C LEU B 162 10358 8808 14685 -415 4471 -1705 C
ATOM 3277 O LEU B 162 -13.872 29.826 77.245 1.00 89.11 O
ANISOU 3277 O LEU B 162 10286 9038 14533 -261 4135 -1727 O
ATOM 3278 CB LEU B 162 -12.258 30.415 74.504 1.00 97.36 C
ANISOU 3278 CB LEU B 162 11538 9592 15863 -561 5125 -1795 C
ATOM 3279 CG LEU B 162 -11.617 29.102 74.989 1.00100.44 C
ANISOU 3279 CG LEU B 162 11670 10162 16329 -448 4894 -1984 C
ATOM 3280 CD1 LEU B 162 -12.148 27.886 74.227 1.00 98.45 C
ANISOU 3280 CD1 LEU B 162 11673 10042 15690 -332 4875 -1884 C
ATOM 3281 CD2 LEU B 162 -10.089 29.152 74.932 1.00107.90 C
ANISOU 3281 CD2 LEU B 162 12285 10973 17740 -540 5097 -2257 C
ATOM 3282 N GLY B 163 -13.262 31.999 77.148 1.00 84.04 N
ANISOU 3282 N GLY B 163 9543 8030 14360 -514 4512 -1791 N
ATOM 3283 CA GLY B 163 -13.265 32.156 78.593 1.00 79.53 C
ANISOU 3283 CA GLY B 163 8693 7607 13918 -433 4131 -1912 C
ATOM 3284 C GLY B 163 -14.664 32.210 79.167 1.00 80.47 C
ANISOU 3284 C GLY B 163 8996 7923 13655 -292 3844 -1704 C
ATOM 3285 O GLY B 163 -14.896 31.741 80.288 1.00 86.83 O
ANISOU 3285 O GLY B 163 9664 8948 14378 -133 3457 -1755 O
ATOM 3286 N SER B 164 -15.607 32.784 78.412 1.00 75.70 N
ANISOU 3286 N SER B 164 8721 7235 12808 -330 4032 -1469 N
ATOM 3287 CA SER B 164 -17.020 32.755 78.776 1.00 73.07 C
ANISOU 3287 CA SER B 164 8591 7087 12086 -193 3793 -1258 C
ATOM 3288 C SER B 164 -17.547 31.324 78.751 1.00 70.83 C
ANISOU 3288 C SER B 164 8408 7022 11481 -49 3575 -1193 C
ATOM 3289 O SER B 164 -18.182 30.866 79.710 1.00 70.56 O
ANISOU 3289 O SER B 164 8324 7204 11283 107 3231 -1169 O
ATOM 3290 CB SER B 164 -17.823 33.635 77.810 1.00 77.09 C
ANISOU 3290 CB SER B 164 9453 7426 12413 -256 4068 -1029 C
ATOM 3291 OG SER B 164 -17.391 34.986 77.827 1.00 85.54 O
ANISOU 3291 OG SER B 164 10457 8247 13798 -382 4298 -1080 O
ATOM 3292 N ILE B 165 -17.250 30.605 77.661 1.00 68.31 N
ANISOU 3292 N ILE B 165 8235 6633 11087 -94 3786 -1178 N
ATOM 3293 CA ILE B 165 -17.678 29.222 77.454 1.00 67.04 C
ANISOU 3293 CA ILE B 165 8185 6626 10661 20 3639 -1139 C
ATOM 3294 C ILE B 165 -17.205 28.315 78.594 1.00 70.50 C
ANISOU 3294 C ILE B 165 8345 7228 11214 156 3313 -1305 C
ATOM 3295 O ILE B 165 -17.976 27.489 79.101 1.00 68.74 O
ANISOU 3295 O ILE B 165 8187 7166 10766 301 3051 -1237 O
ATOM 3296 CB ILE B 165 -17.189 28.739 76.064 1.00 62.34 C
ANISOU 3296 CB ILE B 165 7759 5902 10026 -59 3958 -1148 C
ATOM 3297 CG1 ILE B 165 -18.125 29.258 74.959 1.00 63.08 C
ANISOU 3297 CG1 ILE B 165 8252 5903 9810 -100 4157 -923 C
ATOM 3298 CG2 ILE B 165 -17.060 27.215 75.990 1.00 55.48 C
ANISOU 3298 CG2 ILE B 165 6873 5155 9053 48 3824 -1229 C
ATOM 3299 CD1 ILE B 165 -17.527 29.282 73.557 1.00 65.79 C
ANISOU 3299 CD1 ILE B 165 8781 6074 10141 -187 4533 -931 C
ATOM 3300 N LEU B 166 -15.943 28.458 79.027 1.00 77.61 N
ANISOU 3300 N LEU B 166 8945 8071 12472 121 3324 -1524 N
ATOM 3301 CA LEU B 166 -15.430 27.658 80.143 1.00 79.42 C
ANISOU 3301 CA LEU B 166 8933 8438 12803 278 2998 -1681 C
ATOM 3302 C LEU B 166 -16.120 28.022 81.452 1.00 78.51 C
ANISOU 3302 C LEU B 166 8769 8476 12584 410 2660 -1632 C
ATOM 3303 O LEU B 166 -16.347 27.156 82.307 1.00 80.58 O
ANISOU 3303 O LEU B 166 9006 8888 12722 596 2359 -1636 O
ATOM 3304 CB LEU B 166 -13.920 27.847 80.290 1.00 82.27 C
ANISOU 3304 CB LEU B 166 8981 8691 13588 203 3091 -1939 C
ATOM 3305 CG LEU B 166 -13.055 27.005 79.358 1.00 82.33 C
ANISOU 3305 CG LEU B 166 8964 8616 13702 167 3312 -2047 C
ATOM 3306 CD1 LEU B 166 -11.674 27.616 79.228 1.00 87.51 C
ANISOU 3306 CD1 LEU B 166 9334 9104 14811 21 3527 -2279 C
ATOM 3307 CD2 LEU B 166 -12.971 25.569 79.860 1.00 78.04 C
ANISOU 3307 CD2 LEU B 166 8385 8216 13053 375 3034 -2103 C
ATOM 3308 N GLY B 167 -16.429 29.309 81.623 1.00 75.08 N
ANISOU 3308 N GLY B 167 8333 7989 12204 325 2721 -1587 N
ATOM 3309 CA GLY B 167 -17.152 29.755 82.799 1.00 69.01 C
ANISOU 3309 CA GLY B 167 7542 7369 11308 459 2425 -1537 C
ATOM 3310 C GLY B 167 -18.584 29.259 82.842 1.00 65.24 C
ANISOU 3310 C GLY B 167 7314 7042 10432 581 2289 -1313 C
ATOM 3311 O GLY B 167 -19.114 28.999 83.925 1.00 69.82 O
ANISOU 3311 O GLY B 167 7874 7792 10863 760 1991 -1284 O
ATOM 3312 N ILE B 168 -19.223 29.128 81.667 1.00 60.17 N
ANISOU 3312 N ILE B 168 6918 6329 9617 488 2517 -1155 N
ATOM 3313 CA ILE B 168 -20.573 28.563 81.563 1.00 59.29 C
ANISOU 3313 CA ILE B 168 7036 6331 9161 573 2418 -959 C
ATOM 3314 C ILE B 168 -20.576 27.121 82.070 1.00 58.83 C
ANISOU 3314 C ILE B 168 6943 6382 9029 723 2198 -1004 C
ATOM 3315 O ILE B 168 -21.470 26.715 82.828 1.00 62.69 O
ANISOU 3315 O ILE B 168 7474 7007 9337 861 1975 -913 O
ATOM 3316 CB ILE B 168 -21.092 28.675 80.106 1.00 60.65 C
ANISOU 3316 CB ILE B 168 7497 6376 9171 440 2719 -803 C
ATOM 3317 CG1 ILE B 168 -21.425 30.138 79.744 1.00 63.66 C
ANISOU 3317 CG1 ILE B 168 7982 6647 9559 343 2900 -697 C
ATOM 3318 CG2 ILE B 168 -22.312 27.757 79.848 1.00 58.43 C
ANISOU 3318 CG2 ILE B 168 7450 6188 8565 513 2632 -638 C
ATOM 3319 CD1 ILE B 168 -21.650 30.428 78.244 1.00 67.61 C
ANISOU 3319 CD1 ILE B 168 8791 6971 9928 225 3224 -560 C
ATOM 3320 N TRP B 169 -19.550 26.343 81.695 1.00 53.88 N
ANISOU 3320 N TRP B 169 6232 5680 8561 706 2269 -1146 N
ATOM 3321 CA TRP B 169 -19.428 24.945 82.111 1.00 51.25 C
ANISOU 3321 CA TRP B 169 5878 5403 8194 856 2082 -1200 C
ATOM 3322 C TRP B 169 -19.130 24.816 83.601 1.00 56.90 C
ANISOU 3322 C TRP B 169 6415 6236 8969 1041 1768 -1271 C
ATOM 3323 O TRP B 169 -19.693 23.948 84.279 1.00 64.85 O
ANISOU 3323 O TRP B 169 7481 7323 9837 1206 1560 -1205 O
ATOM 3324 CB TRP B 169 -18.345 24.246 81.280 1.00 48.64 C
ANISOU 3324 CB TRP B 169 5499 4953 8028 800 2256 -1345 C
ATOM 3325 CG TRP B 169 -18.891 23.810 79.968 1.00 52.24 C
ANISOU 3325 CG TRP B 169 6210 5329 8310 704 2484 -1252 C
ATOM 3326 CD1 TRP B 169 -18.807 24.477 78.782 1.00 55.17 C
ANISOU 3326 CD1 TRP B 169 6709 5591 8660 535 2801 -1207 C
ATOM 3327 CD2 TRP B 169 -19.679 22.639 79.719 1.00 52.94 C
ANISOU 3327 CD2 TRP B 169 6492 5423 8198 778 2414 -1182 C
ATOM 3328 NE1 TRP B 169 -19.475 23.781 77.802 1.00 59.75 N
ANISOU 3328 NE1 TRP B 169 7563 6136 9005 514 2915 -1118 N
ATOM 3329 CE2 TRP B 169 -20.019 22.650 78.352 1.00 58.34 C
ANISOU 3329 CE2 TRP B 169 7420 6019 8727 650 2684 -1112 C
ATOM 3330 CE3 TRP B 169 -20.117 21.576 80.515 1.00 48.61 C
ANISOU 3330 CE3 TRP B 169 5954 4918 7596 942 2159 -1172 C
ATOM 3331 CZ2 TRP B 169 -20.778 21.638 77.764 1.00 57.12 C
ANISOU 3331 CZ2 TRP B 169 7512 5830 8360 674 2692 -1055 C
ATOM 3332 CZ3 TRP B 169 -20.871 20.572 79.929 1.00 47.84 C
ANISOU 3332 CZ3 TRP B 169 6089 4751 7335 950 2189 -1108 C
ATOM 3333 CH2 TRP B 169 -21.194 20.611 78.567 1.00 53.60 C
ANISOU 3333 CH2 TRP B 169 7056 5405 7905 814 2447 -1061 C
ATOM 3334 N ALA B 170 -18.237 25.668 84.119 1.00 58.80 N
ANISOU 3334 N ALA B 170 6450 6464 9425 1014 1749 -1402 N
ATOM 3335 CA ALA B 170 -17.896 25.670 85.541 1.00 62.37 C
ANISOU 3335 CA ALA B 170 6754 7019 9922 1183 1470 -1469 C
ATOM 3336 C ALA B 170 -19.122 25.955 86.408 1.00 66.41 C
ANISOU 3336 C ALA B 170 7382 7684 10168 1315 1285 -1297 C
ATOM 3337 O ALA B 170 -19.361 25.271 87.411 1.00 69.54 O
ANISOU 3337 O ALA B 170 7793 8177 10454 1505 1073 -1238 O
ATOM 3338 CB ALA B 170 -16.799 26.706 85.802 1.00 62.82 C
ANISOU 3338 CB ALA B 170 6571 7007 10291 1080 1515 -1663 C
ATOM 3339 N VAL B 171 -19.903 26.973 86.030 1.00 65.16 N
ANISOU 3339 N VAL B 171 7306 7535 9915 1218 1388 -1204 N
ATOM 3340 CA VAL B 171 -21.114 27.342 86.764 1.00 54.39 C
ANISOU 3340 CA VAL B 171 6036 6327 8304 1341 1236 -1051 C
ATOM 3341 C VAL B 171 -22.150 26.219 86.689 1.00 52.83 C
ANISOU 3341 C VAL B 171 5984 6198 7889 1429 1163 -908 C
ATOM 3342 O VAL B 171 -22.691 25.780 87.713 1.00 52.88 O
ANISOU 3342 O VAL B 171 6002 6340 7749 1620 960 -824 O
ATOM 3343 CB VAL B 171 -21.666 28.682 86.223 1.00 46.63 C
ANISOU 3343 CB VAL B 171 5104 5308 7306 1202 1387 -999 C
ATOM 3344 CG1 VAL B 171 -23.072 28.981 86.738 1.00 44.88 C
ANISOU 3344 CG1 VAL B 171 4983 5249 6819 1310 1257 -842 C
ATOM 3345 CG2 VAL B 171 -20.727 29.838 86.579 1.00 44.06 C
ANISOU 3345 CG2 VAL B 171 4607 4901 7232 1138 1417 -1156 C
ATOM 3346 N SER B 172 -22.408 25.711 85.476 1.00 54.39 N
ANISOU 3346 N SER B 172 6304 6280 8084 1283 1359 -864 N
ATOM 3347 CA SER B 172 -23.400 24.656 85.259 1.00 53.34 C
ANISOU 3347 CA SER B 172 6318 6143 7807 1312 1348 -722 C
ATOM 3348 C SER B 172 -23.071 23.381 86.035 1.00 54.59 C
ANISOU 3348 C SER B 172 6425 6311 8006 1495 1141 -770 C
ATOM 3349 O SER B 172 -23.956 22.763 86.636 1.00 56.48 O
ANISOU 3349 O SER B 172 6709 6594 8159 1593 1008 -630 O
ATOM 3350 CB SER B 172 -23.512 24.356 83.764 1.00 56.32 C
ANISOU 3350 CB SER B 172 6880 6364 8155 1135 1632 -670 C
ATOM 3351 OG SER B 172 -23.982 25.493 83.060 1.00 57.04 O
ANISOU 3351 OG SER B 172 7078 6438 8155 997 1818 -569 O
ATOM 3352 N LEU B 173 -21.797 22.956 86.005 1.00 57.46 N
ANISOU 3352 N LEU B 173 6702 6602 8526 1529 1138 -927 N
ATOM 3353 CA LEU B 173 -21.382 21.751 86.719 1.00 54.15 C
ANISOU 3353 CA LEU B 173 6268 6161 8145 1716 969 -942 C
ATOM 3354 C LEU B 173 -21.578 21.895 88.232 1.00 56.97 C
ANISOU 3354 C LEU B 173 6574 6651 8422 1911 777 -817 C
ATOM 3355 O LEU B 173 -21.935 20.917 88.902 1.00 63.59 O
ANISOU 3355 O LEU B 173 7452 7459 9251 2035 679 -667 O
ATOM 3356 CB LEU B 173 -19.915 21.424 86.377 1.00 52.53 C
ANISOU 3356 CB LEU B 173 5951 5849 8161 1683 1041 -1131 C
ATOM 3357 CG LEU B 173 -19.582 20.873 84.974 1.00 49.97 C
ANISOU 3357 CG LEU B 173 5695 5374 7917 1541 1253 -1221 C
ATOM 3358 CD1 LEU B 173 -18.078 20.816 84.730 1.00 50.07 C
ANISOU 3358 CD1 LEU B 173 5534 5318 8171 1512 1330 -1421 C
ATOM 3359 CD2 LEU B 173 -20.193 19.495 84.728 1.00 48.48 C
ANISOU 3359 CD2 LEU B 173 5678 5084 7659 1616 1203 -1156 C
ATOM 3360 N ALA B 174 -21.394 23.108 88.766 1.00 55.25 N
ANISOU 3360 N ALA B 174 6256 6521 8213 1883 777 -830 N
ATOM 3361 CA ALA B 174 -21.545 23.390 90.193 1.00 50.85 C
ANISOU 3361 CA ALA B 174 5604 6036 7679 1966 645 -720 C
ATOM 3362 C ALA B 174 -23.016 23.486 90.623 1.00 53.23 C
ANISOU 3362 C ALA B 174 5929 6369 7927 1910 609 -500 C
ATOM 3363 O ALA B 174 -23.451 22.762 91.525 1.00 56.63 O
ANISOU 3363 O ALA B 174 6329 6859 8327 1984 358 -444 O
ATOM 3364 CB ALA B 174 -20.802 24.683 90.552 1.00 44.11 C
ANISOU 3364 CB ALA B 174 4613 5224 6921 1910 622 -888 C
ATOM 3365 N ILE B 175 -23.792 24.381 89.994 1.00 50.78 N
ANISOU 3365 N ILE B 175 5660 6059 7575 1742 724 -471 N
ATOM 3366 CA ILE B 175 -25.177 24.641 90.388 1.00 53.59 C
ANISOU 3366 CA ILE B 175 6031 6591 7738 1764 517 -423 C
ATOM 3367 C ILE B 175 -26.106 23.424 90.222 1.00 56.26 C
ANISOU 3367 C ILE B 175 6571 7024 7780 1857 449 -159 C
ATOM 3368 O ILE B 175 -27.203 23.418 90.787 1.00 56.89 O
ANISOU 3368 O ILE B 175 6753 7298 7563 1912 356 98 O
ATOM 3369 CB ILE B 175 -25.771 25.879 89.645 1.00 52.15 C
ANISOU 3369 CB ILE B 175 5902 6467 7446 1656 645 -444 C
ATOM 3370 CG1 ILE B 175 -26.024 25.617 88.149 1.00 52.21 C
ANISOU 3370 CG1 ILE B 175 6091 6419 7329 1573 871 -366 C
ATOM 3371 CG2 ILE B 175 -24.911 27.152 89.852 1.00 48.76 C
ANISOU 3371 CG2 ILE B 175 5322 5925 7281 1519 706 -642 C
ATOM 3372 CD1 ILE B 175 -26.788 26.745 87.430 1.00 47.11 C
ANISOU 3372 CD1 ILE B 175 5567 5800 6534 1467 1046 -233 C
ATOM 3373 N MET B 176 -25.693 22.383 89.492 1.00 57.04 N
ANISOU 3373 N MET B 176 7848 7566 6260 1028 -361 73 N
ATOM 3374 CA MET B 176 -26.546 21.207 89.321 1.00 50.54 C
ANISOU 3374 CA MET B 176 7083 6650 5472 986 -203 187 C
ATOM 3375 C MET B 176 -26.167 20.042 90.248 1.00 54.89 C
ANISOU 3375 C MET B 176 7874 7036 5944 1167 -271 221 C
ATOM 3376 O MET B 176 -26.729 18.950 90.116 1.00 57.24 O
ANISOU 3376 O MET B 176 8227 7239 6284 1139 -148 303 O
ATOM 3377 CB MET B 176 -26.556 20.765 87.848 1.00 45.26 C
ANISOU 3377 CB MET B 176 6155 6056 4984 811 -157 116 C
ATOM 3378 CG MET B 176 -27.213 21.789 86.901 1.00 48.04 C
ANISOU 3378 CG MET B 176 6335 6529 5388 631 -68 116 C
ATOM 3379 SD MET B 176 -28.832 22.370 87.462 1.00 51.32 S
ANISOU 3379 SD MET B 176 6857 6903 5738 602 120 285 S
ATOM 3380 CE MET B 176 -29.199 23.607 86.218 1.00 45.48 C
ANISOU 3380 CE MET B 176 5910 6302 5067 420 121 227 C
ATOM 3381 N VAL B 177 -25.276 20.275 91.219 1.00 57.54 N
ANISOU 3381 N VAL B 177 8379 7321 6163 1358 -470 161 N
ATOM 3382 CA VAL B 177 -24.890 19.267 92.213 1.00 53.99 C
ANISOU 3382 CA VAL B 177 8226 6689 5600 1562 -576 192 C
ATOM 3383 C VAL B 177 -26.051 18.981 93.172 1.00 52.01 C
ANISOU 3383 C VAL B 177 8303 6292 5167 1605 -359 403 C
ATOM 3384 O VAL B 177 -26.280 17.797 93.468 1.00 57.78 O
ANISOU 3384 O VAL B 177 9224 6864 5865 1658 -293 484 O
ATOM 3385 CB VAL B 177 -23.574 19.664 92.932 1.00 48.60 C
ANISOU 3385 CB VAL B 177 7626 5982 4859 1770 -892 36 C
ATOM 3386 CG1 VAL B 177 -23.220 18.697 94.070 1.00 48.09 C
ANISOU 3386 CG1 VAL B 177 7937 5699 4636 2013 -1038 73 C
ATOM 3387 CG2 VAL B 177 -22.384 19.693 91.943 1.00 41.42 C
ANISOU 3387 CG2 VAL B 177 6376 5180 4182 1716 -1071 -202 C
ATOM 3388 N PRO B 178 -26.859 19.949 93.654 1.00 49.34 N
ANISOU 3388 N PRO B 178 8044 5982 4720 1573 -213 497 N
ATOM 3389 CA PRO B 178 -28.009 19.576 94.516 1.00 50.54 C
ANISOU 3389 CA PRO B 178 8498 5975 4730 1590 48 682 C
ATOM 3390 C PRO B 178 -28.992 18.651 93.820 1.00 52.80 C
ANISOU 3390 C PRO B 178 8678 6213 5171 1426 305 764 C
ATOM 3391 O PRO B 178 -29.712 17.877 94.484 1.00 58.11 O
ANISOU 3391 O PRO B 178 9614 6701 5762 1452 513 895 O
ATOM 3392 CB PRO B 178 -28.669 20.919 94.864 1.00 49.08 C
ANISOU 3392 CB PRO B 178 8303 5872 4472 1544 156 722 C
ATOM 3393 CG PRO B 178 -27.630 21.947 94.611 1.00 46.07 C
ANISOU 3393 CG PRO B 178 7745 5647 4114 1584 -112 570 C
ATOM 3394 CD PRO B 178 -26.786 21.418 93.475 1.00 45.57 C
ANISOU 3394 CD PRO B 178 7398 5666 4251 1517 -261 433 C
ATOM 3395 N GLN B 179 -29.055 18.723 92.483 1.00 49.26 N
ANISOU 3395 N GLN B 179 7857 5912 4947 1254 304 684 N
ATOM 3396 CA GLN B 179 -29.856 17.839 91.685 1.00 49.43 C
ANISOU 3396 CA GLN B 179 7737 5897 5147 1107 491 725 C
ATOM 3397 C GLN B 179 -29.395 16.406 91.821 1.00 51.62 C
ANISOU 3397 C GLN B 179 8154 6030 5429 1190 446 736 C
ATOM 3398 O GLN B 179 -30.176 15.500 92.160 1.00 57.21 O
ANISOU 3398 O GLN B 179 9024 6573 6142 1174 658 849 O
ATOM 3399 CB GLN B 179 -29.770 18.259 90.212 1.00 55.85 C
ANISOU 3399 CB GLN B 179 8161 6896 6162 938 430 611 C
ATOM 3400 CG GLN B 179 -30.695 17.502 89.314 1.00 61.24 C
ANISOU 3400 CG GLN B 179 8677 7551 7040 786 604 637 C
ATOM 3401 CD GLN B 179 -32.089 17.558 89.869 1.00 66.28 C
ANISOU 3401 CD GLN B 179 9415 8078 7688 737 879 756 C
ATOM 3402 OE1 GLN B 179 -32.507 18.589 90.391 1.00 66.84 O
ANISOU 3402 OE1 GLN B 179 9538 8180 7677 743 934 786 O
ATOM 3403 NE2 GLN B 179 -32.836 16.475 89.720 1.00 67.70 N
ANISOU 3403 NE2 GLN B 179 9601 8126 7996 678 1063 808 N
ATOM 3404 N ALA B 180 -28.099 16.195 91.589 1.00 51.40 N
ANISOU 3404 N ALA B 180 8068 6049 5412 1283 170 608 N
ATOM 3405 CA ALA B 180 -27.464 14.887 91.741 1.00 53.91 C
ANISOU 3405 CA ALA B 180 8517 6230 5736 1392 60 589 C
ATOM 3406 C ALA B 180 -27.650 14.353 93.157 1.00 62.89 C
ANISOU 3406 C ALA B 180 10120 7135 6642 1568 109 723 C
ATOM 3407 O ALA B 180 -27.877 13.152 93.346 1.00 67.99 O
ANISOU 3407 O ALA B 180 10939 7607 7286 1597 194 797 O
ATOM 3408 CB ALA B 180 -25.981 15.012 91.396 1.00 50.05 C
ANISOU 3408 CB ALA B 180 7881 5832 5304 1481 -266 393 C
ATOM 3409 N ALA B 181 -27.585 15.248 94.149 1.00 59.21 N
ANISOU 3409 N ALA B 181 9878 6651 5969 1683 68 757 N
ATOM 3410 CA ALA B 181 -27.679 14.892 95.562 1.00 53.71 C
ANISOU 3410 CA ALA B 181 9681 5726 5000 1870 96 877 C
ATOM 3411 C ALA B 181 -29.052 14.320 95.954 1.00 58.09 C
ANISOU 3411 C ALA B 181 10447 6113 5512 1773 495 1064 C
ATOM 3412 O ALA B 181 -29.124 13.440 96.818 1.00 63.60 O
ANISOU 3412 O ALA B 181 11556 6571 6039 1892 560 1168 O
ATOM 3413 CB ALA B 181 -27.358 16.123 96.413 1.00 53.55 C
ANISOU 3413 CB ALA B 181 9812 5750 4784 1996 -30 854 C
ATOM 3414 N VAL B 182 -30.148 14.833 95.370 1.00 58.72 N
ANISOU 3414 N VAL B 182 10269 6295 5748 1564 765 1099 N
ATOM 3415 CA VAL B 182 -31.489 14.354 95.741 1.00 56.58 C
ANISOU 3415 CA VAL B 182 10155 5856 5489 1459 1167 1243 C
ATOM 3416 C VAL B 182 -31.903 13.088 94.974 1.00 56.58 C
ANISOU 3416 C VAL B 182 10013 5776 5709 1340 1305 1257 C
ATOM 3417 O VAL B 182 -32.802 12.367 95.423 1.00 57.85 O
ANISOU 3417 O VAL B 182 10378 5732 5871 1289 1618 1371 O
ATOM 3418 CB VAL B 182 -32.583 15.444 95.589 1.00 54.39 C
ANISOU 3418 CB VAL B 182 9683 5683 5301 1304 1404 1257 C
ATOM 3419 CG1 VAL B 182 -32.331 16.628 96.531 1.00 59.74 C
ANISOU 3419 CG1 VAL B 182 10562 6398 5739 1426 1323 1265 C
ATOM 3420 CG2 VAL B 182 -32.745 15.937 94.146 1.00 43.77 C
ANISOU 3420 CG2 VAL B 182 7820 4569 4241 1129 1335 1141 C
ATOM 3421 N MET B 183 -31.238 12.783 93.849 1.00 52.32 N
ANISOU 3421 N MET B 183 9143 5379 5358 1296 1086 1136 N
ATOM 3422 CA MET B 183 -31.554 11.595 93.049 1.00 54.68 C
ANISOU 3422 CA MET B 183 9286 5617 5875 1191 1181 1132 C
ATOM 3423 C MET B 183 -31.288 10.313 93.829 1.00 62.73 C
ANISOU 3423 C MET B 183 10696 6376 6763 1322 1201 1220 C
ATOM 3424 O MET B 183 -30.166 10.084 94.298 1.00 67.58 O
ANISOU 3424 O MET B 183 11518 6946 7214 1513 915 1183 O
ATOM 3425 CB MET B 183 -30.728 11.594 91.758 1.00 48.94 C
ANISOU 3425 CB MET B 183 8169 5094 5333 1141 917 972 C
ATOM 3426 CG MET B 183 -31.051 12.717 90.789 1.00 48.93 C
ANISOU 3426 CG MET B 183 7790 5325 5475 988 911 886 C
ATOM 3427 SD MET B 183 -32.815 13.075 90.667 1.00 56.97 S
ANISOU 3427 SD MET B 183 8703 6306 6639 806 1282 967 S
ATOM 3428 CE MET B 183 -33.415 11.603 89.844 1.00 57.39 C
ANISOU 3428 CE MET B 183 8607 6244 6954 691 1429 964 C
ATOM 3429 N GLU B 184 -32.319 9.468 93.955 1.00 64.38 N
ANISOU 3429 N GLU B 184 11007 6398 7058 1223 1531 1324 N
ATOM 3430 CA GLU B 184 -32.224 8.171 94.620 1.00 66.12 C
ANISOU 3430 CA GLU B 184 11610 6342 7171 1319 1604 1422 C
ATOM 3431 C GLU B 184 -32.975 7.110 93.825 1.00 67.70 C
ANISOU 3431 C GLU B 184 11602 6463 7657 1153 1821 1428 C
ATOM 3432 O GLU B 184 -33.940 7.403 93.113 1.00 67.46 O
ANISOU 3432 O GLU B 184 11238 6520 7874 963 2029 1396 O
ATOM 3433 CB GLU B 184 -32.779 8.196 96.055 1.00 69.90 C
ANISOU 3433 CB GLU B 184 12617 6570 7372 1396 1866 1582 C
ATOM 3434 CG GLU B 184 -32.042 9.092 97.064 1.00 76.85 C
ANISOU 3434 CG GLU B 184 13816 7465 7919 1598 1652 1592 C
ATOM 3435 CD GLU B 184 -30.532 8.862 97.173 1.00 84.01 C
ANISOU 3435 CD GLU B 184 14833 8394 8694 1824 1177 1501 C
ATOM 3436 OE1 GLU B 184 -30.060 7.706 97.088 1.00 87.20 O
ANISOU 3436 OE1 GLU B 184 15360 8657 9116 1898 1062 1500 O
ATOM 3437 OE2 GLU B 184 -29.815 9.867 97.373 1.00 86.38 O
ANISOU 3437 OE2 GLU B 184 15093 8842 8885 1933 913 1416 O
ATOM 3438 N CYS B 185 -32.504 5.865 93.935 1.00 72.20 N
ANISOU 3438 N CYS B 185 12367 6861 8206 1237 1745 1455 N
ATOM 3439 CA CYS B 185 -33.090 4.708 93.263 1.00 73.51 C
ANISOU 3439 CA CYS B 185 12379 6920 8630 1106 1924 1460 C
ATOM 3440 C CYS B 185 -33.688 3.751 94.295 1.00 73.44 C
ANISOU 3440 C CYS B 185 12850 6559 8496 1131 2238 1624 C
ATOM 3441 O CYS B 185 -33.047 3.463 95.312 1.00 71.48 O
ANISOU 3441 O CYS B 185 13085 6135 7941 1323 2126 1706 O
ATOM 3442 CB CYS B 185 -32.038 4.000 92.407 1.00 78.15 C
ANISOU 3442 CB CYS B 185 12764 7599 9331 1165 1582 1340 C
ATOM 3443 SG CYS B 185 -32.739 2.952 91.116 1.00 83.29 S
ANISOU 3443 SG CYS B 185 13022 8247 10378 967 1734 1281 S
ATOM 3444 N SER B 186 -34.963 3.366 94.104 1.00 74.83 N
ANISOU 3444 N SER B 186 12919 6616 8898 940 2645 1667 N
ATOM 3445 CA SER B 186 -35.695 2.505 95.040 1.00 78.50 C
ANISOU 3445 CA SER B 186 13730 6809 9287 910 2979 1754 C
ATOM 3446 C SER B 186 -36.738 1.625 94.344 1.00 79.00 C
ANISOU 3446 C SER B 186 13519 6776 9722 709 3282 1723 C
ATOM 3447 O SER B 186 -37.343 2.031 93.350 1.00 76.16 O
ANISOU 3447 O SER B 186 12731 6523 9682 555 3374 1661 O
ATOM 3448 CB SER B 186 -36.402 3.341 96.107 1.00 84.49 C
ANISOU 3448 CB SER B 186 14654 7577 9873 890 3204 1753 C
ATOM 3449 OG SER B 186 -35.476 4.056 96.901 1.00 88.65 O
ANISOU 3449 OG SER B 186 15468 8168 10049 1082 2931 1767 O
ATOM 3450 N SER B 187 -36.970 0.422 94.885 1.00 86.76 N
ANISOU 3450 N SER B 187 14744 7554 10665 712 3428 1752 N
ATOM 3451 CA SER B 187 -38.015 -0.481 94.404 1.00 87.85 C
ANISOU 3451 CA SER B 187 14658 7580 11141 533 3735 1707 C
ATOM 3452 C SER B 187 -39.323 -0.346 95.207 1.00 88.19 C
ANISOU 3452 C SER B 187 14760 7530 11219 424 4157 1670 C
ATOM 3453 O SER B 187 -39.326 0.125 96.347 1.00 88.07 O
ANISOU 3453 O SER B 187 15084 7472 10905 506 4227 1704 O
ATOM 3454 CB SER B 187 -37.511 -1.930 94.417 1.00 92.61 C
ANISOU 3454 CB SER B 187 15463 8005 11719 595 3650 1749 C
ATOM 3455 OG SER B 187 -36.971 -2.287 95.677 1.00103.22 O
ANISOU 3455 OG SER B 187 17335 9217 12668 755 3586 1824 O
ATOM 3456 N VAL B 188 -40.437 -0.791 94.578 1.00 92.12 N
ANISOU 3456 N VAL B 188 14912 7981 12109 246 4427 1578 N
ATOM 3457 CA VAL B 188 -41.785 -0.705 95.178 1.00 97.99 C
ANISOU 3457 CA VAL B 188 15634 8615 12981 138 4838 1498 C
ATOM 3458 C VAL B 188 -41.779 -1.216 96.618 1.00103.97 C
ANISOU 3458 C VAL B 188 16942 9163 13400 225 5024 1573 C
ATOM 3459 O VAL B 188 -42.228 -0.535 97.541 1.00106.00 O
ANISOU 3459 O VAL B 188 17390 9383 13504 242 5204 1557 O
ATOM 3460 CB VAL B 188 -42.834 -1.447 94.309 1.00 97.76 C
ANISOU 3460 CB VAL B 188 15197 8521 13425 -28 5052 1373 C
ATOM 3461 CG1 VAL B 188 -43.342 -0.576 93.150 1.00 97.23 C
ANISOU 3461 CG1 VAL B 188 14580 8646 13716 -133 4967 1240 C
ATOM 3462 CG2 VAL B 188 -42.329 -2.788 93.765 1.00 96.29 C
ANISOU 3462 CG2 VAL B 188 15022 8244 13320 -23 4944 1414 C
ATOM 3463 N LEU B 189 -41.273 -2.442 96.815 1.00109.50 N
ANISOU 3463 N LEU B 189 17911 9711 13984 282 4978 1647 N
ATOM 3464 CA LEU B 189 -40.983 -3.028 98.123 1.00115.48 C
ANISOU 3464 CA LEU B 189 19248 10267 14363 397 5062 1732 C
ATOM 3465 C LEU B 189 -39.458 -3.077 98.257 1.00123.93 C
ANISOU 3465 C LEU B 189 20598 11394 15096 596 4601 1830 C
ATOM 3466 O LEU B 189 -38.809 -3.790 97.481 1.00121.62 O
ANISOU 3466 O LEU B 189 20189 11113 14906 620 4363 1852 O
ATOM 3467 CB LEU B 189 -41.592 -4.434 98.230 1.00110.33 C
ANISOU 3467 CB LEU B 189 18688 9381 13852 314 5347 1727 C
ATOM 3468 CG LEU B 189 -43.129 -4.542 98.222 1.00107.32 C
ANISOU 3468 CG LEU B 189 18069 8892 13816 136 5824 1602 C
ATOM 3469 CD1 LEU B 189 -43.624 -5.802 97.509 1.00105.07 C
ANISOU 3469 CD1 LEU B 189 17558 8491 13871 22 5968 1556 C
ATOM 3470 CD2 LEU B 189 -43.684 -4.486 99.642 1.00113.34 C
ANISOU 3470 CD2 LEU B 189 19285 9449 14331 161 6168 1607 C
ATOM 3471 N PRO B 190 -38.837 -2.311 99.171 1.00133.83 N
ANISOU 3471 N PRO B 190 22189 12684 15976 749 4439 1867 N
ATOM 3472 CA PRO B 190 -37.365 -2.166 99.156 1.00133.30 C
ANISOU 3472 CA PRO B 190 22291 12707 15651 950 3945 1914 C
ATOM 3473 C PRO B 190 -36.532 -3.454 99.080 1.00134.90 C
ANISOU 3473 C PRO B 190 22708 12775 15774 1053 3713 1962 C
ATOM 3474 O PRO B 190 -35.408 -3.403 98.566 1.00133.24 O
ANISOU 3474 O PRO B 190 22433 12664 15528 1180 3290 1958 O
ATOM 3475 CB PRO B 190 -37.096 -1.407 100.460 1.00134.73 C
ANISOU 3475 CB PRO B 190 22891 12865 15437 1091 3909 1925 C
ATOM 3476 CG PRO B 190 -38.265 -0.484 100.555 1.00134.69 C
ANISOU 3476 CG PRO B 190 22672 12915 15590 945 4261 1870 C
ATOM 3477 CD PRO B 190 -39.454 -1.320 100.081 1.00135.94 C
ANISOU 3477 CD PRO B 190 22596 12951 16104 744 4661 1835 C
ATOM 3478 N GLU B 191 -37.029 -4.590 99.585 1.00127.50 N
ANISOU 3478 N GLU B 191 22025 11606 14814 1010 3969 1994 N
ATOM 3479 CA GLU B 191 -36.268 -5.840 99.572 1.00110.60 C
ANISOU 3479 CA GLU B 191 20111 9321 12593 1110 3748 2039 C
ATOM 3480 C GLU B 191 -36.204 -6.477 98.179 1.00 95.64 C
ANISOU 3480 C GLU B 191 17773 7479 11087 1015 3651 2014 C
ATOM 3481 O GLU B 191 -35.344 -7.330 97.930 1.00 87.69 O
ANISOU 3481 O GLU B 191 16862 6402 10053 1122 3356 2030 O
ATOM 3482 CB GLU B 191 -36.883 -6.800 100.598 1.00113.17 C
ANISOU 3482 CB GLU B 191 20872 9371 12757 1088 4084 2082 C
ATOM 3483 CG GLU B 191 -36.593 -6.441 102.073 1.00120.87 C
ANISOU 3483 CG GLU B 191 22420 10236 13269 1246 4074 2105 C
ATOM 3484 CD GLU B 191 -37.341 -5.214 102.614 1.00129.95 C
ANISOU 3484 CD GLU B 191 23546 11459 14369 1189 4340 2063 C
ATOM 3485 OE1 GLU B 191 -36.936 -4.726 103.692 1.00134.90 O
ANISOU 3485 OE1 GLU B 191 24590 12037 14629 1339 4248 2066 O
ATOM 3486 OE2 GLU B 191 -38.323 -4.748 101.994 1.00132.65 O
ANISOU 3486 OE2 GLU B 191 23465 11895 15040 1005 4626 2014 O
ATOM 3487 N LEU B 192 -37.078 -6.025 97.266 1.00 95.37 N
ANISOU 3487 N LEU B 192 17249 7566 11419 826 3871 1955 N
ATOM 3488 CA LEU B 192 -37.182 -6.533 95.898 1.00 91.47 C
ANISOU 3488 CA LEU B 192 16298 7124 11332 715 3822 1905 C
ATOM 3489 C LEU B 192 -35.951 -6.220 95.039 1.00 89.58 C
ANISOU 3489 C LEU B 192 15883 7034 11119 840 3349 1881 C
ATOM 3490 O LEU B 192 -35.652 -6.972 94.106 1.00 90.46 O
ANISOU 3490 O LEU B 192 15775 7123 11474 821 3213 1846 O
ATOM 3491 CB LEU B 192 -38.445 -5.945 95.252 1.00 87.41 C
ANISOU 3491 CB LEU B 192 15321 6712 11181 501 4153 1818 C
ATOM 3492 CG LEU B 192 -39.120 -6.635 94.061 1.00 83.37 C
ANISOU 3492 CG LEU B 192 14345 6192 11139 332 4280 1732 C
ATOM 3493 CD1 LEU B 192 -39.288 -8.131 94.301 1.00 85.31 C
ANISOU 3493 CD1 LEU B 192 14787 6208 11420 314 4412 1764 C
ATOM 3494 CD2 LEU B 192 -40.472 -5.993 93.763 1.00 79.29 C
ANISOU 3494 CD2 LEU B 192 13451 5748 10928 152 4617 1620 C
ATOM 3495 N ALA B 193 -35.238 -5.116 95.322 1.00 88.00 N
ANISOU 3495 N ALA B 193 15765 6981 10691 971 3101 1882 N
ATOM 3496 CA ALA B 193 -34.072 -4.726 94.525 1.00 85.01 C
ANISOU 3496 CA ALA B 193 15210 6743 10347 1101 2665 1832 C
ATOM 3497 C ALA B 193 -32.931 -5.740 94.602 1.00 85.54 C
ANISOU 3497 C ALA B 193 15504 6693 10305 1286 2304 1823 C
ATOM 3498 O ALA B 193 -32.099 -5.797 93.691 1.00 86.83 O
ANISOU 3498 O ALA B 193 15442 6929 10619 1367 1990 1744 O
ATOM 3499 CB ALA B 193 -33.566 -3.347 94.964 1.00 81.45 C
ANISOU 3499 CB ALA B 193 14832 6461 9653 1214 2485 1823 C
ATOM 3500 N ALA B 194 -32.878 -6.532 95.673 1.00 71.89 N
ANISOU 3500 N ALA B 194 14215 4778 8323 1361 2343 1885 N
ATOM 3501 CA ALA B 194 -31.906 -7.610 95.806 1.00 73.02 C
ANISOU 3501 CA ALA B 194 14582 4785 8377 1526 2019 1871 C
ATOM 3502 C ALA B 194 -32.163 -8.767 94.844 1.00 75.23 C
ANISOU 3502 C ALA B 194 14618 4966 9000 1420 2089 1852 C
ATOM 3503 O ALA B 194 -31.409 -9.746 94.879 1.00 79.82 O
ANISOU 3503 O ALA B 194 15356 5424 9547 1546 1829 1832 O
ATOM 3504 CB ALA B 194 -31.902 -8.126 97.248 1.00 78.38 C
ANISOU 3504 CB ALA B 194 15821 5274 8685 1620 2083 1944 C
ATOM 3505 N ARG B 195 -33.202 -8.683 94.006 1.00 70.56 N
ANISOU 3505 N ARG B 195 13640 4423 8747 1197 2418 1839 N
ATOM 3506 CA ARG B 195 -33.556 -9.712 93.029 1.00 70.21 C
ANISOU 3506 CA ARG B 195 13311 4299 9068 1077 2507 1797 C
ATOM 3507 C ARG B 195 -33.599 -9.190 91.600 1.00 72.91 C
ANISOU 3507 C ARG B 195 13110 4813 9777 987 2453 1688 C
ATOM 3508 O ARG B 195 -33.126 -9.878 90.688 1.00 75.13 O
ANISOU 3508 O ARG B 195 13174 5083 10291 1011 2266 1604 O
ATOM 3509 CB ARG B 195 -34.925 -10.336 93.360 1.00 72.66 C
ANISOU 3509 CB ARG B 195 13641 4472 9495 874 2994 1847 C
ATOM 3510 CG ARG B 195 -35.049 -10.945 94.747 1.00 76.86 C
ANISOU 3510 CG ARG B 195 14716 4801 9687 938 3133 1947 C
ATOM 3511 CD ARG B 195 -36.411 -11.598 94.939 1.00 79.32 C
ANISOU 3511 CD ARG B 195 14997 4970 10170 736 3631 1963 C
ATOM 3512 NE ARG B 195 -36.485 -12.887 94.258 1.00 79.95 N
ANISOU 3512 NE ARG B 195 14936 4923 10520 675 3631 1940 N
ATOM 3513 CZ ARG B 195 -37.560 -13.667 94.240 1.00 82.09 C
ANISOU 3513 CZ ARG B 195 15130 5059 11003 509 4015 1930 C
ATOM 3514 NH1 ARG B 195 -38.668 -13.293 94.863 1.00 83.90 N
ANISOU 3514 NH1 ARG B 195 15405 5256 11218 389 4442 1928 N
ATOM 3515 NH2 ARG B 195 -37.525 -14.825 93.595 1.00 82.55 N
ANISOU 3515 NH2 ARG B 195 15056 5008 11302 469 3970 1904 N
ATOM 3516 N THR B 196 -34.165 -7.997 91.382 1.00 66.40 N
ANISOU 3516 N THR B 196 12055 4156 9016 884 2611 1673 N
ATOM 3517 CA THR B 196 -34.308 -7.422 90.055 1.00 68.20 C
ANISOU 3517 CA THR B 196 11672 4687 9555 762 2516 1511 C
ATOM 3518 C THR B 196 -34.389 -5.895 90.146 1.00 66.74 C
ANISOU 3518 C THR B 196 11356 4752 9252 747 2493 1485 C
ATOM 3519 O THR B 196 -34.610 -5.324 91.220 1.00 69.45 O
ANISOU 3519 O THR B 196 12065 4985 9336 795 2655 1609 O
ATOM 3520 CB THR B 196 -35.530 -8.013 89.321 1.00 71.57 C
ANISOU 3520 CB THR B 196 11769 5037 10388 538 2851 1470 C
ATOM 3521 OG1 THR B 196 -35.573 -7.531 87.973 1.00 77.47 O
ANISOU 3521 OG1 THR B 196 11929 6103 11404 441 2679 1286 O
ATOM 3522 CG2 THR B 196 -36.857 -7.689 90.034 1.00 67.50 C
ANISOU 3522 CG2 THR B 196 11354 4404 9888 391 3317 1547 C
ATOM 3523 N ARG B 197 -34.162 -5.232 89.003 1.00 58.31 N
ANISOU 3523 N ARG B 197 9782 4014 8359 686 2278 1320 N
ATOM 3524 CA ARG B 197 -34.247 -3.796 88.840 1.00 54.11 C
ANISOU 3524 CA ARG B 197 9049 3742 7769 652 2231 1270 C
ATOM 3525 C ARG B 197 -35.480 -3.385 88.081 1.00 53.02 C
ANISOU 3525 C ARG B 197 8513 3692 7939 440 2482 1206 C
ATOM 3526 O ARG B 197 -35.709 -2.193 87.825 1.00 52.35 O
ANISOU 3526 O ARG B 197 8223 3816 7850 390 2460 1154 O
ATOM 3527 CB ARG B 197 -33.006 -3.257 88.107 1.00 51.69 C
ANISOU 3527 CB ARG B 197 8496 3733 7411 745 1790 1120 C
ATOM 3528 CG ARG B 197 -31.730 -3.265 88.916 1.00 57.10 C
ANISOU 3528 CG ARG B 197 9530 4375 7789 973 1491 1141 C
ATOM 3529 CD ARG B 197 -30.541 -2.853 88.066 1.00 61.11 C
ANISOU 3529 CD ARG B 197 9729 5159 8332 1036 1094 954 C
ATOM 3530 NE ARG B 197 -29.333 -2.728 88.871 1.00 65.34 N
ANISOU 3530 NE ARG B 197 10564 5654 8607 1261 790 941 N
ATOM 3531 CZ ARG B 197 -28.121 -2.510 88.372 1.00 64.14 C
ANISOU 3531 CZ ARG B 197 10219 5678 8475 1354 432 766 C
ATOM 3532 NH1 ARG B 197 -27.944 -2.403 87.063 1.00 58.59 N
ANISOU 3532 NH1 ARG B 197 9052 5202 8008 1231 355 604 N
ATOM 3533 NH2 ARG B 197 -27.085 -2.396 89.189 1.00 69.64 N
ANISOU 3533 NH2 ARG B 197 11194 6306 8959 1571 152 739 N
ATOM 3534 N ALA B 198 -36.276 -4.389 87.673 1.00 54.15 N
ANISOU 3534 N ALA B 198 8532 3668 8376 320 2702 1192 N
ATOM 3535 CA ALA B 198 -37.508 -4.223 86.914 1.00 53.63 C
ANISOU 3535 CA ALA B 198 8076 3632 8668 128 2929 1102 C
ATOM 3536 C ALA B 198 -38.549 -3.391 87.658 1.00 61.69 C
ANISOU 3536 C ALA B 198 9186 4573 9679 43 3273 1167 C
ATOM 3537 O ALA B 198 -39.427 -2.799 87.024 1.00 65.63 O
ANISOU 3537 O ALA B 198 9327 5173 10436 -87 3369 1060 O
ATOM 3538 CB ALA B 198 -38.073 -5.606 86.592 1.00 55.36 C
ANISOU 3538 CB ALA B 198 8232 3620 9180 43 3111 1087 C
ATOM 3539 N PHE B 199 -38.487 -3.360 88.991 1.00 67.83 N
ANISOU 3539 N PHE B 199 10448 5154 10170 118 3460 1330 N
ATOM 3540 CA PHE B 199 -39.435 -2.605 89.804 1.00 70.67 C
ANISOU 3540 CA PHE B 199 10923 5444 10485 46 3797 1380 C
ATOM 3541 C PHE B 199 -38.768 -1.427 90.516 1.00 69.66 C
ANISOU 3541 C PHE B 199 11042 5436 9988 172 3652 1458 C
ATOM 3542 O PHE B 199 -39.336 -0.873 91.463 1.00 77.26 O
ANISOU 3542 O PHE B 199 12187 6377 10790 166 3861 1487 O
ATOM 3543 CB PHE B 199 -40.138 -3.545 90.793 1.00 74.73 C
ANISOU 3543 CB PHE B 199 11712 5752 10931 26 4105 1412 C
ATOM 3544 CG PHE B 199 -40.748 -4.761 90.129 1.00 77.70 C
ANISOU 3544 CG PHE B 199 11851 6015 11656 -82 4230 1328 C
ATOM 3545 CD1 PHE B 199 -41.958 -4.671 89.454 1.00 77.86 C
ANISOU 3545 CD1 PHE B 199 11434 6075 12075 -235 4416 1169 C
ATOM 3546 CD2 PHE B 199 -40.090 -5.982 90.146 1.00 81.51 C
ANISOU 3546 CD2 PHE B 199 12537 6354 12080 -14 4124 1390 C
ATOM 3547 CE1 PHE B 199 -42.505 -5.781 88.821 1.00 79.98 C
ANISOU 3547 CE1 PHE B 199 11472 6246 12672 -318 4504 1074 C
ATOM 3548 CE2 PHE B 199 -40.633 -7.095 89.516 1.00 81.57 C
ANISOU 3548 CE2 PHE B 199 12318 6263 12412 -111 4229 1309 C
ATOM 3549 CZ PHE B 199 -41.840 -6.993 88.853 1.00 81.12 C
ANISOU 3549 CZ PHE B 199 11821 6252 12747 -263 4422 1151 C
ATOM 3550 N SER B 200 -37.594 -1.004 90.032 1.00 64.96 N
ANISOU 3550 N SER B 200 10345 5098 9238 297 3207 1397 N
ATOM 3551 CA SER B 200 -36.827 0.085 90.623 1.00 65.62 C
ANISOU 3551 CA SER B 200 10614 5332 8985 433 2998 1432 C
ATOM 3552 C SER B 200 -37.149 1.390 89.912 1.00 67.15 C
ANISOU 3552 C SER B 200 10406 5811 9296 347 2919 1318 C
ATOM 3553 O SER B 200 -37.491 1.416 88.724 1.00 67.46 O
ANISOU 3553 O SER B 200 10008 5996 9627 234 2849 1186 O
ATOM 3554 CB SER B 200 -35.322 -0.194 90.545 1.00 67.57 C
ANISOU 3554 CB SER B 200 10978 5673 9024 620 2564 1406 C
ATOM 3555 OG SER B 200 -34.883 -0.971 91.649 1.00 73.19 O
ANISOU 3555 OG SER B 200 12220 6112 9475 767 2590 1541 O
ATOM 3556 N VAL B 201 -37.044 2.488 90.648 1.00 67.48 N
ANISOU 3556 N VAL B 201 10619 5921 9098 408 2918 1367 N
ATOM 3557 CA VAL B 201 -37.450 3.783 90.134 1.00 66.42 C
ANISOU 3557 CA VAL B 201 10161 6021 9055 328 2879 1277 C
ATOM 3558 C VAL B 201 -36.447 4.835 90.583 1.00 63.93 C
ANISOU 3558 C VAL B 201 9992 5880 8419 473 2603 1289 C
ATOM 3559 O VAL B 201 -36.033 4.859 91.746 1.00 69.87 O
ANISOU 3559 O VAL B 201 11173 6503 8871 607 2624 1402 O
ATOM 3560 CB VAL B 201 -38.897 4.105 90.572 1.00 74.36 C
ANISOU 3560 CB VAL B 201 11147 6883 10224 188 3305 1301 C
ATOM 3561 CG1 VAL B 201 -39.174 5.593 90.580 1.00 76.17 C
ANISOU 3561 CG1 VAL B 201 11227 7302 10412 165 3268 1253 C
ATOM 3562 CG2 VAL B 201 -39.882 3.383 89.647 1.00 78.53 C
ANISOU 3562 CG2 VAL B 201 11316 7336 11183 21 3475 1200 C
ATOM 3563 N CYS B 202 -36.008 5.659 89.634 1.00 61.47 N
ANISOU 3563 N CYS B 202 9339 5847 8168 452 2332 1166 N
ATOM 3564 CA CYS B 202 -35.104 6.770 89.889 1.00 63.98 C
ANISOU 3564 CA CYS B 202 9714 6353 8244 563 2073 1146 C
ATOM 3565 C CYS B 202 -35.938 8.044 90.001 1.00 64.61 C
ANISOU 3565 C CYS B 202 9677 6525 8349 480 2215 1138 C
ATOM 3566 O CYS B 202 -36.641 8.413 89.055 1.00 64.12 O
ANISOU 3566 O CYS B 202 9258 6569 8534 342 2249 1046 O
ATOM 3567 CB CYS B 202 -34.071 6.881 88.764 1.00 63.45 C
ANISOU 3567 CB CYS B 202 9359 6515 8235 579 1717 1007 C
ATOM 3568 SG CYS B 202 -32.789 8.131 89.007 1.00 63.46 S
ANISOU 3568 SG CYS B 202 9402 6729 7980 713 1387 949 S
ATOM 3569 N ASP B 203 -35.867 8.703 91.159 1.00 62.48 N
ANISOU 3569 N ASP B 203 9717 6201 7820 572 2283 1227 N
ATOM 3570 CA ASP B 203 -36.595 9.943 91.398 1.00 60.25 C
ANISOU 3570 CA ASP B 203 9357 5997 7539 511 2411 1220 C
ATOM 3571 C ASP B 203 -35.907 10.718 92.513 1.00 56.21 C
ANISOU 3571 C ASP B 203 9183 5497 6678 670 2309 1288 C
ATOM 3572 O ASP B 203 -35.007 10.210 93.193 1.00 62.49 O
ANISOU 3572 O ASP B 203 10305 6199 7239 830 2173 1346 O
ATOM 3573 CB ASP B 203 -38.082 9.681 91.710 1.00 64.06 C
ANISOU 3573 CB ASP B 203 9833 6285 8221 375 2840 1256 C
ATOM 3574 CG ASP B 203 -38.978 10.901 91.452 1.00 72.90 C
ANISOU 3574 CG ASP B 203 10691 7520 9486 269 2931 1182 C
ATOM 3575 OD1 ASP B 203 -38.563 11.818 90.708 1.00 74.09 O
ANISOU 3575 OD1 ASP B 203 10597 7910 9643 270 2656 1094 O
ATOM 3576 OD2 ASP B 203 -40.143 10.891 91.908 1.00 80.24 O
ANISOU 3576 OD2 ASP B 203 11638 8288 10560 175 3287 1194 O
ATOM 3577 N GLU B 204 -36.317 11.975 92.651 1.00 52.96 N
ANISOU 3577 N GLU B 204 8678 5202 6243 635 2345 1265 N
ATOM 3578 CA GLU B 204 -35.839 12.872 93.695 1.00 49.46 C
ANISOU 3578 CA GLU B 204 8521 4777 5493 772 2271 1316 C
ATOM 3579 C GLU B 204 -36.420 12.440 95.038 1.00 57.08 C
ANISOU 3579 C GLU B 204 9946 5469 6273 825 2591 1455 C
ATOM 3580 O GLU B 204 -37.627 12.214 95.146 1.00 63.47 O
ANISOU 3580 O GLU B 204 10734 6137 7246 693 2963 1484 O
ATOM 3581 CB GLU B 204 -36.309 14.291 93.376 1.00 45.14 C
ANISOU 3581 CB GLU B 204 7717 4416 5019 694 2259 1248 C
ATOM 3582 CG GLU B 204 -35.736 14.882 92.101 1.00 49.11 C
ANISOU 3582 CG GLU B 204 7832 5176 5650 645 1952 1119 C
ATOM 3583 CD GLU B 204 -36.373 16.209 91.728 1.00 57.10 C
ANISOU 3583 CD GLU B 204 8603 6335 6757 554 1964 1056 C
ATOM 3584 OE1 GLU B 204 -37.060 16.805 92.586 1.00 58.65 O
ANISOU 3584 OE1 GLU B 204 8942 6459 6885 558 2165 1105 O
ATOM 3585 OE2 GLU B 204 -36.139 16.681 90.594 1.00 54.66 O
ANISOU 3585 OE2 GLU B 204 7986 6206 6574 485 1766 954 O
ATOM 3586 N ARG B 205 -35.579 12.358 96.072 1.00 62.52 N
ANISOU 3586 N ARG B 205 11061 6069 6623 1020 2453 1527 N
ATOM 3587 CA ARG B 205 -36.031 12.052 97.429 1.00 66.01 C
ANISOU 3587 CA ARG B 205 11919 6295 6869 1082 2667 1583 C
ATOM 3588 C ARG B 205 -35.931 13.324 98.264 1.00 64.86 C
ANISOU 3588 C ARG B 205 11877 6234 6532 1158 2602 1548 C
ATOM 3589 O ARG B 205 -34.856 13.924 98.365 1.00 64.60 O
ANISOU 3589 O ARG B 205 11911 6323 6312 1306 2271 1527 O
ATOM 3590 CB ARG B 205 -35.250 10.882 98.041 1.00 71.89 C
ANISOU 3590 CB ARG B 205 13030 6874 7409 1241 2512 1617 C
ATOM 3591 CG ARG B 205 -35.748 10.433 99.425 1.00 81.04 C
ANISOU 3591 CG ARG B 205 14594 7816 8383 1292 2717 1626 C
ATOM 3592 CD ARG B 205 -35.021 9.201 99.983 1.00 93.00 C
ANISOU 3592 CD ARG B 205 16346 9115 9874 1314 2793 1666 C
ATOM 3593 NE ARG B 205 -35.529 8.844 101.312 1.00108.06 N
ANISOU 3593 NE ARG B 205 18619 10806 11633 1325 3071 1672 N
ATOM 3594 CZ ARG B 205 -36.614 8.120 101.574 1.00113.31 C
ANISOU 3594 CZ ARG B 205 19322 11290 12440 1196 3443 1685 C
ATOM 3595 NH1 ARG B 205 -37.361 7.637 100.592 1.00115.12 N
ANISOU 3595 NH1 ARG B 205 19221 11529 12988 1040 3581 1686 N
ATOM 3596 NH2 ARG B 205 -36.945 7.868 102.837 1.00112.59 N
ANISOU 3596 NH2 ARG B 205 19609 10995 12175 1228 3679 1685 N
ATOM 3597 N TRP B 206 -37.060 13.740 98.844 1.00 63.33 N
ANISOU 3597 N TRP B 206 11681 5969 6414 1058 2911 1523 N
ATOM 3598 CA TRP B 206 -37.145 14.956 99.644 1.00 63.97 C
ANISOU 3598 CA TRP B 206 11845 6106 6352 1111 2895 1488 C
ATOM 3599 C TRP B 206 -37.580 14.606 101.060 1.00 69.09 C
ANISOU 3599 C TRP B 206 12894 6523 6834 1169 3105 1493 C
ATOM 3600 O TRP B 206 -38.576 13.894 101.253 1.00 70.27 O
ANISOU 3600 O TRP B 206 13075 6496 7126 1058 3444 1493 O
ATOM 3601 CB TRP B 206 -38.139 15.936 99.007 1.00 61.38 C
ANISOU 3601 CB TRP B 206 11134 5908 6280 943 3056 1437 C
ATOM 3602 CG TRP B 206 -37.693 16.440 97.665 1.00 59.01 C
ANISOU 3602 CG TRP B 206 10472 5840 6108 893 2848 1424 C
ATOM 3603 CD1 TRP B 206 -38.111 15.999 96.442 1.00 62.44 C
ANISOU 3603 CD1 TRP B 206 10575 6318 6831 747 2928 1411 C
ATOM 3604 CD2 TRP B 206 -36.728 17.468 97.413 1.00 51.81 C
ANISOU 3604 CD2 TRP B 206 9504 5140 5042 993 2526 1411 C
ATOM 3605 NE1 TRP B 206 -37.470 16.696 95.444 1.00 59.93 N
ANISOU 3605 NE1 TRP B 206 9937 6253 6581 742 2603 1328 N
ATOM 3606 CE2 TRP B 206 -36.615 17.602 96.014 1.00 53.26 C
ANISOU 3606 CE2 TRP B 206 9254 5511 5470 887 2370 1332 C
ATOM 3607 CE3 TRP B 206 -35.950 18.290 98.233 1.00 45.81 C
ANISOU 3607 CE3 TRP B 206 8946 4439 4020 1154 2295 1391 C
ATOM 3608 CZ2 TRP B 206 -35.756 18.526 95.419 1.00 49.29 C
ANISOU 3608 CZ2 TRP B 206 8534 5248 4948 926 2019 1241 C
ATOM 3609 CZ3 TRP B 206 -35.097 19.204 97.642 1.00 47.64 C
ANISOU 3609 CZ3 TRP B 206 9014 4892 4196 1210 1995 1353 C
ATOM 3610 CH2 TRP B 206 -35.007 19.316 96.249 1.00 48.71 C
ANISOU 3610 CH2 TRP B 206 8687 5215 4604 1082 1845 1251 C
ATOM 3611 N ALA B 207 -36.838 15.124 102.046 1.00 73.57 N
ANISOU 3611 N ALA B 207 13762 7082 7109 1344 2905 1484 N
ATOM 3612 CA ALA B 207 -37.156 14.905 103.453 1.00 78.50 C
ANISOU 3612 CA ALA B 207 14810 7482 7535 1418 3082 1485 C
ATOM 3613 C ALA B 207 -38.424 15.647 103.887 1.00 82.45 C
ANISOU 3613 C ALA B 207 15238 7931 8157 1296 3418 1454 C
ATOM 3614 O ALA B 207 -39.107 15.189 104.809 1.00 87.44 O
ANISOU 3614 O ALA B 207 16157 8332 8735 1283 3711 1456 O
ATOM 3615 CB ALA B 207 -35.972 15.321 104.331 1.00 79.25 C
ANISOU 3615 CB ALA B 207 15219 7584 7308 1646 2740 1461 C
ATOM 3616 N ASP B 208 -38.758 16.777 103.244 1.00 77.84 N
ANISOU 3616 N ASP B 208 14290 7546 7741 1207 3384 1419 N
ATOM 3617 CA ASP B 208 -39.943 17.554 103.614 1.00 80.47 C
ANISOU 3617 CA ASP B 208 14526 7837 8211 1095 3671 1373 C
ATOM 3618 C ASP B 208 -40.695 18.074 102.378 1.00 77.68 C
ANISOU 3618 C ASP B 208 13660 7647 8208 913 3743 1326 C
ATOM 3619 O ASP B 208 -40.217 17.968 101.241 1.00 75.46 O
ANISOU 3619 O ASP B 208 13109 7531 8031 883 3552 1334 O
ATOM 3620 CB ASP B 208 -39.578 18.711 104.570 1.00 86.93 C
ANISOU 3620 CB ASP B 208 15538 8694 8796 1221 3535 1356 C
ATOM 3621 CG ASP B 208 -38.721 19.782 103.918 1.00 94.03 C
ANISOU 3621 CG ASP B 208 16193 9872 9662 1279 3168 1338 C
ATOM 3622 OD1 ASP B 208 -39.257 20.874 103.635 1.00 97.80 O
ANISOU 3622 OD1 ASP B 208 16414 10479 10267 1197 3206 1299 O
ATOM 3623 OD2 ASP B 208 -37.513 19.541 103.708 1.00 98.47 O
ANISOU 3623 OD2 ASP B 208 16823 10515 10075 1409 2841 1351 O
ATOM 3624 N ASP B 209 -41.902 18.622 102.629 1.00 83.66 N
ANISOU 3624 N ASP B 209 14295 8338 9153 794 4025 1263 N
ATOM 3625 CA ASP B 209 -42.817 19.129 101.596 1.00 83.81 C
ANISOU 3625 CA ASP B 209 13842 8466 9535 620 4121 1183 C
ATOM 3626 C ASP B 209 -42.395 20.494 101.033 1.00 79.02 C
ANISOU 3626 C ASP B 209 12991 8126 8906 640 3853 1162 C
ATOM 3627 O ASP B 209 -42.742 20.817 99.890 1.00 76.69 O
ANISOU 3627 O ASP B 209 12300 7970 8868 529 3811 1108 O
ATOM 3628 CB ASP B 209 -44.256 19.271 102.144 1.00 92.78 C
ANISOU 3628 CB ASP B 209 14942 9416 10893 497 4503 1096 C
ATOM 3629 CG ASP B 209 -44.826 17.982 102.768 1.00108.84 C
ANISOU 3629 CG ASP B 209 17227 11159 12970 463 4826 1097 C
ATOM 3630 OD1 ASP B 209 -44.890 16.934 102.090 1.00112.85 O
ANISOU 3630 OD1 ASP B 209 17621 11619 13637 404 4870 1098 O
ATOM 3631 OD2 ASP B 209 -45.261 18.043 103.942 1.00116.28 O
ANISOU 3631 OD2 ASP B 209 18479 11907 13795 488 5055 1090 O
ATOM 3632 N LEU B 210 -41.677 21.316 101.826 1.00 73.06 N
ANISOU 3632 N LEU B 210 12466 7435 7858 783 3670 1192 N
ATOM 3633 CA LEU B 210 -41.324 22.686 101.441 1.00 67.50 C
ANISOU 3633 CA LEU B 210 11562 6966 7120 807 3439 1163 C
ATOM 3634 C LEU B 210 -40.089 22.752 100.533 1.00 65.69 C
ANISOU 3634 C LEU B 210 11217 6946 6794 879 3079 1194 C
ATOM 3635 O LEU B 210 -40.079 23.512 99.562 1.00 66.62 O
ANISOU 3635 O LEU B 210 11020 7259 7036 818 2958 1156 O
ATOM 3636 CB LEU B 210 -41.118 23.557 102.693 1.00 65.91 C
ANISOU 3636 CB LEU B 210 11641 6731 6671 928 3400 1164 C
ATOM 3637 CG LEU B 210 -40.936 25.078 102.514 1.00 65.49 C
ANISOU 3637 CG LEU B 210 11408 6888 6588 950 3212 1122 C
ATOM 3638 CD1 LEU B 210 -42.060 25.699 101.691 1.00 63.29 C
ANISOU 3638 CD1 LEU B 210 10731 6684 6631 777 3374 1043 C
ATOM 3639 CD2 LEU B 210 -40.825 25.792 103.857 1.00 68.02 C
ANISOU 3639 CD2 LEU B 210 12030 7135 6681 1066 3210 1120 C
ATOM 3640 N ALA B 211 -39.041 21.966 100.829 1.00 65.43 N
ANISOU 3640 N ALA B 211 11444 6867 6549 1012 2903 1250 N
ATOM 3641 CA ALA B 211 -37.818 21.965 100.021 1.00 64.15 C
ANISOU 3641 CA ALA B 211 11189 6881 6305 1088 2560 1263 C
ATOM 3642 C ALA B 211 -38.047 21.754 98.519 1.00 64.21 C
ANISOU 3642 C ALA B 211 10820 7014 6561 947 2570 1255 C
ATOM 3643 O ALA B 211 -37.547 22.561 97.730 1.00 64.94 O
ANISOU 3643 O ALA B 211 10701 7314 6658 948 2359 1228 O
ATOM 3644 CB ALA B 211 -36.832 20.935 100.588 1.00 67.65 C
ANISOU 3644 CB ALA B 211 11964 7203 6536 1241 2411 1305 C
ATOM 3645 N PRO B 212 -38.771 20.713 98.057 1.00 61.36 N
ANISOU 3645 N PRO B 212 10361 6534 6420 826 2801 1265 N
ATOM 3646 CA PRO B 212 -39.012 20.598 96.605 1.00 54.99 C
ANISOU 3646 CA PRO B 212 9174 5846 5874 692 2797 1238 C
ATOM 3647 C PRO B 212 -39.757 21.784 96.005 1.00 54.41 C
ANISOU 3647 C PRO B 212 8743 5914 6018 582 2787 1132 C
ATOM 3648 O PRO B 212 -39.549 22.105 94.829 1.00 57.10 O
ANISOU 3648 O PRO B 212 8747 6425 6525 520 2544 1045 O
ATOM 3649 CB PRO B 212 -39.835 19.305 96.475 1.00 56.75 C
ANISOU 3649 CB PRO B 212 9365 5872 6325 583 3067 1238 C
ATOM 3650 CG PRO B 212 -40.420 19.086 97.814 1.00 57.74 C
ANISOU 3650 CG PRO B 212 9785 5790 6364 616 3290 1242 C
ATOM 3651 CD PRO B 212 -39.387 19.592 98.790 1.00 59.58 C
ANISOU 3651 CD PRO B 212 10356 6055 6227 804 3070 1289 C
ATOM 3652 N LYS B 213 -40.627 22.434 96.789 1.00 51.79 N
ANISOU 3652 N LYS B 213 8472 5504 5701 557 3005 1111 N
ATOM 3653 CA LYS B 213 -41.346 23.615 96.318 1.00 53.02 C
ANISOU 3653 CA LYS B 213 8330 5774 6041 471 3019 1018 C
ATOM 3654 C LYS B 213 -40.399 24.798 96.096 1.00 52.64 C
ANISOU 3654 C LYS B 213 8228 5951 5822 560 2641 992 C
ATOM 3655 O LYS B 213 -40.482 25.480 95.069 1.00 57.59 O
ANISOU 3655 O LYS B 213 8527 6731 6624 490 2437 897 O
ATOM 3656 CB LYS B 213 -42.454 23.986 97.310 1.00 55.21 C
ANISOU 3656 CB LYS B 213 8679 5900 6397 432 3284 967 C
ATOM 3657 CG LYS B 213 -43.599 22.978 97.406 1.00 56.95 C
ANISOU 3657 CG LYS B 213 8840 5898 6901 314 3593 915 C
ATOM 3658 CD LYS B 213 -44.596 23.403 98.472 1.00 63.57 C
ANISOU 3658 CD LYS B 213 9783 6580 7791 286 3847 858 C
ATOM 3659 CE LYS B 213 -45.632 22.326 98.749 1.00 70.71 C
ANISOU 3659 CE LYS B 213 10699 7231 8938 186 4168 805 C
ATOM 3660 NZ LYS B 213 -46.855 22.491 97.918 1.00 72.90 N
ANISOU 3660 NZ LYS B 213 10553 7481 9666 33 4279 644 N
ATOM 3661 N ILE B 214 -39.492 25.056 97.048 1.00 48.06 N
ANISOU 3661 N ILE B 214 7982 5378 4902 718 2538 1066 N
ATOM 3662 CA ILE B 214 -38.546 26.162 96.885 1.00 48.58 C
ANISOU 3662 CA ILE B 214 7993 5642 4825 802 2189 1027 C
ATOM 3663 C ILE B 214 -37.545 25.849 95.771 1.00 42.96 C
ANISOU 3663 C ILE B 214 7089 5070 4164 796 1870 986 C
ATOM 3664 O ILE B 214 -37.310 26.677 94.883 1.00 43.06 O
ANISOU 3664 O ILE B 214 6837 5251 4274 743 1653 905 O
ATOM 3665 CB ILE B 214 -37.851 26.495 98.224 1.00 52.05 C
ANISOU 3665 CB ILE B 214 8829 6032 4916 984 2139 1089 C
ATOM 3666 CG1 ILE B 214 -38.877 27.071 99.212 1.00 52.64 C
ANISOU 3666 CG1 ILE B 214 8988 5995 5018 956 2372 1065 C
ATOM 3667 CG2 ILE B 214 -36.678 27.484 98.025 1.00 50.70 C
ANISOU 3667 CG2 ILE B 214 8602 6054 4607 1085 1757 1039 C
ATOM 3668 CD1 ILE B 214 -38.508 26.940 100.665 1.00 52.62 C
ANISOU 3668 CD1 ILE B 214 9363 5850 4781 1095 2360 1091 C
ATOM 3669 N TYR B 215 -36.997 24.621 95.764 1.00 45.66 N
ANISOU 3669 N TYR B 215 7565 5329 4453 840 1858 1036 N
ATOM 3670 CA TYR B 215 -36.015 24.217 94.755 1.00 43.27 C
ANISOU 3670 CA TYR B 215 7094 5143 4205 836 1581 985 C
ATOM 3671 C TYR B 215 -36.581 24.293 93.335 1.00 42.14 C
ANISOU 3671 C TYR B 215 6562 5095 4356 665 1555 903 C
ATOM 3672 O TYR B 215 -35.929 24.815 92.424 1.00 37.34 O
ANISOU 3672 O TYR B 215 5758 4646 3784 635 1308 829 O
ATOM 3673 CB TYR B 215 -35.495 22.797 95.028 1.00 47.04 C
ANISOU 3673 CB TYR B 215 7784 5487 4604 908 1603 1047 C
ATOM 3674 CG TYR B 215 -34.532 22.349 93.943 1.00 45.65 C
ANISOU 3674 CG TYR B 215 7403 5425 4516 892 1340 975 C
ATOM 3675 CD1 TYR B 215 -33.259 22.897 93.860 1.00 43.39 C
ANISOU 3675 CD1 TYR B 215 7106 5267 4113 988 1032 907 C
ATOM 3676 CD2 TYR B 215 -34.912 21.429 92.970 1.00 47.70 C
ANISOU 3676 CD2 TYR B 215 7463 5663 4997 772 1407 955 C
ATOM 3677 CE1 TYR B 215 -32.380 22.529 92.856 1.00 45.23 C
ANISOU 3677 CE1 TYR B 215 7142 5599 4445 958 824 820 C
ATOM 3678 CE2 TYR B 215 -34.035 21.053 91.958 1.00 45.48 C
ANISOU 3678 CE2 TYR B 215 7000 5488 4791 751 1182 879 C
ATOM 3679 CZ TYR B 215 -32.771 21.608 91.908 1.00 46.82 C
ANISOU 3679 CZ TYR B 215 7168 5780 4841 840 904 811 C
ATOM 3680 OH TYR B 215 -31.890 21.248 90.913 1.00 55.99 O
ANISOU 3680 OH TYR B 215 8147 7036 6092 808 713 717 O
ATOM 3681 N HIS B 216 -37.787 23.749 93.114 1.00 42.99 N
ANISOU 3681 N HIS B 216 6565 5088 4680 553 1810 905 N
ATOM 3682 CA HIS B 216 -38.314 23.719 91.758 1.00 43.14 C
ANISOU 3682 CA HIS B 216 6240 5174 4978 413 1751 815 C
ATOM 3683 C HIS B 216 -38.833 25.068 91.296 1.00 46.35 C
ANISOU 3683 C HIS B 216 6442 5690 5480 353 1662 734 C
ATOM 3684 O HIS B 216 -38.890 25.318 90.084 1.00 44.20 O
ANISOU 3684 O HIS B 216 5929 5510 5355 270 1495 653 O
ATOM 3685 CB HIS B 216 -39.376 22.609 91.643 1.00 45.17 C
ANISOU 3685 CB HIS B 216 6436 5256 5470 323 2027 819 C
ATOM 3686 CG HIS B 216 -38.757 21.267 91.441 1.00 43.52 C
ANISOU 3686 CG HIS B 216 6311 4987 5238 347 2008 863 C
ATOM 3687 ND1 HIS B 216 -38.377 20.807 90.193 1.00 45.93 N
ANISOU 3687 ND1 HIS B 216 6400 5379 5674 290 1822 798 N
ATOM 3688 CD2 HIS B 216 -38.326 20.334 92.327 1.00 48.91 C
ANISOU 3688 CD2 HIS B 216 7295 5534 5753 437 2118 961 C
ATOM 3689 CE1 HIS B 216 -37.799 19.627 90.318 1.00 49.16 C
ANISOU 3689 CE1 HIS B 216 6940 5710 6027 336 1832 848 C
ATOM 3690 NE2 HIS B 216 -37.752 19.316 91.600 1.00 49.42 N
ANISOU 3690 NE2 HIS B 216 7293 5605 5879 429 2000 950 N
ATOM 3691 N SER B 217 -39.140 25.985 92.230 1.00 49.22 N
ANISOU 3691 N SER B 217 6921 6041 5738 402 1745 752 N
ATOM 3692 CA SER B 217 -39.434 27.364 91.865 1.00 41.80 C
ANISOU 3692 CA SER B 217 5818 5214 4848 368 1614 678 C
ATOM 3693 C SER B 217 -38.176 28.065 91.356 1.00 42.06 C
ANISOU 3693 C SER B 217 5836 5423 4722 410 1294 659 C
ATOM 3694 O SER B 217 -38.171 28.624 90.250 1.00 43.55 O
ANISOU 3694 O SER B 217 5823 5710 5013 333 1118 585 O
ATOM 3695 CB SER B 217 -40.043 28.095 93.067 1.00 43.86 C
ANISOU 3695 CB SER B 217 6220 5409 5034 416 1800 699 C
ATOM 3696 OG SER B 217 -41.293 27.517 93.427 1.00 39.70 O
ANISOU 3696 OG SER B 217 5668 4709 4707 348 2129 687 O
ATOM 3697 N CYS B 218 -37.083 27.983 92.126 1.00 47.70 N
ANISOU 3697 N CYS B 218 6773 6159 5190 533 1217 714 N
ATOM 3698 CA CYS B 218 -35.792 28.544 91.718 1.00 45.31 C
ANISOU 3698 CA CYS B 218 6449 6002 4765 575 937 673 C
ATOM 3699 C CYS B 218 -35.317 27.943 90.391 1.00 49.38 C
ANISOU 3699 C CYS B 218 6786 6578 5397 488 808 620 C
ATOM 3700 O CYS B 218 -34.860 28.672 89.503 1.00 52.97 O
ANISOU 3700 O CYS B 218 7104 7151 5873 429 632 551 O
ATOM 3701 CB CYS B 218 -34.750 28.303 92.816 1.00 41.84 C
ANISOU 3701 CB CYS B 218 6278 5535 4085 738 876 718 C
ATOM 3702 SG CYS B 218 -35.103 29.130 94.386 1.00 49.77 S
ANISOU 3702 SG CYS B 218 7541 6475 4892 862 987 772 S
ATOM 3703 N PHE B 219 -35.416 26.614 90.249 1.00 49.35 N
ANISOU 3703 N PHE B 219 6803 6485 5464 476 908 650 N
ATOM 3704 CA PHE B 219 -35.011 25.939 89.023 1.00 41.84 C
ANISOU 3704 CA PHE B 219 5694 5579 4625 397 805 597 C
ATOM 3705 C PHE B 219 -35.733 26.491 87.800 1.00 38.25 C
ANISOU 3705 C PHE B 219 5012 5178 4344 263 755 526 C
ATOM 3706 O PHE B 219 -35.112 26.759 86.761 1.00 42.03 O
ANISOU 3706 O PHE B 219 5388 5753 4827 204 588 461 O
ATOM 3707 CB PHE B 219 -35.237 24.423 89.144 1.00 42.63 C
ANISOU 3707 CB PHE B 219 5850 5550 4796 403 949 644 C
ATOM 3708 CG PHE B 219 -34.616 23.609 88.029 1.00 44.05 C
ANISOU 3708 CG PHE B 219 5902 5773 5062 349 833 588 C
ATOM 3709 CD1 PHE B 219 -33.294 23.196 88.093 1.00 47.51 C
ANISOU 3709 CD1 PHE B 219 6412 6251 5387 425 688 565 C
ATOM 3710 CD2 PHE B 219 -35.363 23.254 86.918 1.00 41.30 C
ANISOU 3710 CD2 PHE B 219 5358 5415 4919 228 861 541 C
ATOM 3711 CE1 PHE B 219 -32.732 22.451 87.067 1.00 41.53 C
ANISOU 3711 CE1 PHE B 219 5530 5530 4720 369 600 500 C
ATOM 3712 CE2 PHE B 219 -34.803 22.511 85.891 1.00 40.68 C
ANISOU 3712 CE2 PHE B 219 5177 5372 4906 179 761 485 C
ATOM 3713 CZ PHE B 219 -33.488 22.110 85.968 1.00 39.79 C
ANISOU 3713 CZ PHE B 219 5134 5305 4678 244 645 467 C
ATOM 3714 N PHE B 220 -37.060 26.650 87.895 1.00 37.95 N
ANISOU 3714 N PHE B 220 4904 5060 4457 215 899 526 N
ATOM 3715 CA PHE B 220 -37.869 27.147 86.771 1.00 36.06 C
ANISOU 3715 CA PHE B 220 4463 4838 4401 110 823 443 C
ATOM 3716 C PHE B 220 -37.489 28.582 86.399 1.00 41.43 C
ANISOU 3716 C PHE B 220 5123 5636 4982 99 632 401 C
ATOM 3717 O PHE B 220 -37.327 28.901 85.213 1.00 42.94 O
ANISOU 3717 O PHE B 220 5224 5884 5207 26 472 338 O
ATOM 3718 CB PHE B 220 -39.360 27.037 87.123 1.00 35.40 C
ANISOU 3718 CB PHE B 220 4297 4621 4530 79 1019 424 C
ATOM 3719 CG PHE B 220 -40.280 27.686 86.112 1.00 36.59 C
ANISOU 3719 CG PHE B 220 4250 4768 4884 1 906 315 C
ATOM 3720 CD1 PHE B 220 -40.339 27.224 84.807 1.00 39.43 C
ANISOU 3720 CD1 PHE B 220 4486 5132 5364 -65 770 247 C
ATOM 3721 CD2 PHE B 220 -41.093 28.751 86.474 1.00 35.39 C
ANISOU 3721 CD2 PHE B 220 4048 4596 4801 4 921 272 C
ATOM 3722 CE1 PHE B 220 -41.178 27.820 83.876 1.00 42.33 C
ANISOU 3722 CE1 PHE B 220 4707 5474 5901 -116 628 139 C
ATOM 3723 CE2 PHE B 220 -41.934 29.350 85.548 1.00 39.94 C
ANISOU 3723 CE2 PHE B 220 4456 5150 5569 -49 778 158 C
ATOM 3724 CZ PHE B 220 -41.975 28.884 84.247 1.00 44.27 C
ANISOU 3724 CZ PHE B 220 4906 5693 6222 -104 622 92 C
ATOM 3725 N ILE B 221 -37.337 29.457 87.403 1.00 41.41 N
ANISOU 3725 N ILE B 221 5227 5661 4847 170 651 435 N
ATOM 3726 CA ILE B 221 -37.013 30.868 87.184 1.00 39.18 C
ANISOU 3726 CA ILE B 221 4934 5476 4475 163 486 399 C
ATOM 3727 C ILE B 221 -35.600 31.021 86.595 1.00 39.67 C
ANISOU 3727 C ILE B 221 5024 5647 4402 153 317 375 C
ATOM 3728 O ILE B 221 -35.389 31.778 85.639 1.00 42.42 O
ANISOU 3728 O ILE B 221 5317 6055 4747 80 177 320 O
ATOM 3729 CB ILE B 221 -37.157 31.648 88.517 1.00 40.68 C
ANISOU 3729 CB ILE B 221 5240 5659 4556 254 562 439 C
ATOM 3730 CG1 ILE B 221 -38.585 31.600 89.117 1.00 43.27 C
ANISOU 3730 CG1 ILE B 221 5534 5870 5038 249 765 440 C
ATOM 3731 CG2 ILE B 221 -36.619 33.074 88.415 1.00 38.23 C
ANISOU 3731 CG2 ILE B 221 4937 5452 4135 261 386 406 C
ATOM 3732 CD1 ILE B 221 -39.720 32.000 88.232 1.00 51.52 C
ANISOU 3732 CD1 ILE B 221 6383 6876 6315 160 725 352 C
ATOM 3733 N VAL B 222 -34.625 30.281 87.150 1.00 40.30 N
ANISOU 3733 N VAL B 222 5199 5735 4380 226 335 404 N
ATOM 3734 CA VAL B 222 -33.201 30.399 86.810 1.00 42.09 C
ANISOU 3734 CA VAL B 222 5438 6047 4506 233 195 355 C
ATOM 3735 C VAL B 222 -32.862 29.718 85.463 1.00 46.13 C
ANISOU 3735 C VAL B 222 5848 6579 5101 128 148 298 C
ATOM 3736 O VAL B 222 -32.080 30.257 84.678 1.00 48.90 O
ANISOU 3736 O VAL B 222 6163 7001 5418 63 44 229 O
ATOM 3737 CB VAL B 222 -32.349 29.838 87.978 1.00 40.14 C
ANISOU 3737 CB VAL B 222 5332 5776 4141 374 205 384 C
ATOM 3738 CG1 VAL B 222 -30.937 29.441 87.542 1.00 39.09 C
ANISOU 3738 CG1 VAL B 222 5171 5696 3986 382 81 304 C
ATOM 3739 CG2 VAL B 222 -32.278 30.839 89.143 1.00 41.62 C
ANISOU 3739 CG2 VAL B 222 5639 5974 4199 480 184 406 C
ATOM 3740 N THR B 223 -33.437 28.538 85.178 1.00 46.37 N
ANISOU 3740 N THR B 223 5839 6537 5243 106 238 321 N
ATOM 3741 CA THR B 223 -33.142 27.847 83.915 1.00 44.92 C
ANISOU 3741 CA THR B 223 5568 6366 5134 14 194 263 C
ATOM 3742 C THR B 223 -34.129 28.157 82.786 1.00 39.29 C
ANISOU 3742 C THR B 223 4769 5631 4529 -91 159 228 C
ATOM 3743 O THR B 223 -33.868 27.762 81.644 1.00 45.73 O
ANISOU 3743 O THR B 223 5541 6459 5377 -169 103 172 O
ATOM 3744 CB THR B 223 -33.077 26.310 84.107 1.00 51.67 C
ANISOU 3744 CB THR B 223 6426 7150 6055 51 281 289 C
ATOM 3745 OG1 THR B 223 -34.357 25.796 84.500 1.00 52.18 O
ANISOU 3745 OG1 THR B 223 6480 7108 6237 59 422 347 O
ATOM 3746 CG2 THR B 223 -32.022 25.909 85.141 1.00 56.29 C
ANISOU 3746 CG2 THR B 223 7123 7735 6528 173 271 308 C
ATOM 3747 N TYR B 224 -35.244 28.859 83.058 1.00 38.04 N
ANISOU 3747 N TYR B 224 4591 5431 4430 -87 177 246 N
ATOM 3748 CA TYR B 224 -36.246 29.120 82.021 1.00 36.23 C
ANISOU 3748 CA TYR B 224 4283 5155 4328 -162 105 192 C
ATOM 3749 C TYR B 224 -36.802 30.557 81.998 1.00 46.80 C
ANISOU 3749 C TYR B 224 5634 6502 5646 -170 11 171 C
ATOM 3750 O TYR B 224 -36.543 31.295 81.042 1.00 52.42 O
ANISOU 3750 O TYR B 224 6384 7244 6289 -232 -132 126 O
ATOM 3751 CB TYR B 224 -37.405 28.115 82.135 1.00 34.28 C
ANISOU 3751 CB TYR B 224 3940 4792 4293 -156 221 191 C
ATOM 3752 CG TYR B 224 -38.346 28.174 80.946 1.00 42.67 C
ANISOU 3752 CG TYR B 224 4908 5791 5516 -219 107 104 C
ATOM 3753 CD1 TYR B 224 -38.109 27.417 79.801 1.00 44.75 C
ANISOU 3753 CD1 TYR B 224 5147 6044 5810 -273 33 55 C
ATOM 3754 CD2 TYR B 224 -39.454 29.013 80.954 1.00 46.87 C
ANISOU 3754 CD2 TYR B 224 5380 6262 6166 -215 53 56 C
ATOM 3755 CE1 TYR B 224 -38.957 27.491 78.700 1.00 50.56 C
ANISOU 3755 CE1 TYR B 224 5826 6708 6676 -312 -105 -35 C
ATOM 3756 CE2 TYR B 224 -40.306 29.093 79.861 1.00 50.45 C
ANISOU 3756 CE2 TYR B 224 5759 6639 6771 -251 -97 -45 C
ATOM 3757 CZ TYR B 224 -40.054 28.332 78.738 1.00 54.08 C
ANISOU 3757 CZ TYR B 224 6219 7085 7243 -295 -183 -88 C
ATOM 3758 OH TYR B 224 -40.902 28.414 77.654 1.00 56.91 O
ANISOU 3758 OH TYR B 224 6531 7353 7740 -312 -361 -197 O
ATOM 3759 N LEU B 225 -37.563 30.971 83.025 1.00 40.80 N
ANISOU 3759 N LEU B 225 4583 5590 5330 157 -878 -37 N
ATOM 3760 CA LEU B 225 -38.314 32.231 82.950 1.00 41.88 C
ANISOU 3760 CA LEU B 225 4771 5642 5499 288 -989 60 C
ATOM 3761 C LEU B 225 -37.397 33.462 82.877 1.00 39.65 C
ANISOU 3761 C LEU B 225 4449 5097 5519 328 -1059 -3 C
ATOM 3762 O LEU B 225 -37.525 34.274 81.952 1.00 37.73 O
ANISOU 3762 O LEU B 225 4620 4614 5101 400 -923 189 O
ATOM 3763 CB LEU B 225 -39.305 32.337 84.121 1.00 44.28 C
ANISOU 3763 CB LEU B 225 5021 5902 5902 278 -938 21 C
ATOM 3764 CG LEU B 225 -40.432 33.378 83.977 1.00 39.57 C
ANISOU 3764 CG LEU B 225 4478 5253 5305 409 -1037 155 C
ATOM 3765 CD1 LEU B 225 -41.361 33.071 82.808 1.00 33.37 C
ANISOU 3765 CD1 LEU B 225 3854 4492 4332 508 -1188 309 C
ATOM 3766 CD2 LEU B 225 -41.240 33.471 85.254 1.00 40.57 C
ANISOU 3766 CD2 LEU B 225 4533 5321 5563 374 -1009 70 C
ATOM 3767 N ALA B 226 -36.466 33.638 83.834 1.00 38.76 N
ANISOU 3767 N ALA B 226 4015 5013 5700 139 -813 -222 N
ATOM 3768 CA ALA B 226 -35.613 34.829 83.815 1.00 40.91 C
ANISOU 3768 CA ALA B 226 4416 5024 6106 4 -375 -250 C
ATOM 3769 C ALA B 226 -34.708 34.926 82.576 1.00 52.42 C
ANISOU 3769 C ALA B 226 6259 6295 7363 -73 -28 -185 C
ATOM 3770 O ALA B 226 -34.715 35.980 81.927 1.00 58.74 O
ANISOU 3770 O ALA B 226 7419 6817 8081 -41 191 -30 O
ATOM 3771 CB ALA B 226 -34.804 34.935 85.115 1.00 35.40 C
ANISOU 3771 CB ALA B 226 3312 4422 5719 -207 -216 -491 C
ATOM 3772 N PRO B 227 -33.932 33.897 82.183 1.00 56.15 N
ANISOU 3772 N PRO B 227 6695 6888 7752 -166 59 -283 N
ATOM 3773 CA PRO B 227 -33.105 34.056 80.965 1.00 55.64 C
ANISOU 3773 CA PRO B 227 7031 6624 7484 -232 433 -214 C
ATOM 3774 C PRO B 227 -33.894 34.376 79.691 1.00 56.05 C
ANISOU 3774 C PRO B 227 7638 6514 7144 -58 340 49 C
ATOM 3775 O PRO B 227 -33.497 35.277 78.944 1.00 60.16 O
ANISOU 3775 O PRO B 227 8524 6771 7564 -91 667 173 O
ATOM 3776 CB PRO B 227 -32.373 32.708 80.845 1.00 54.74 C
ANISOU 3776 CB PRO B 227 6748 6699 7352 -312 470 -366 C
ATOM 3777 CG PRO B 227 -32.399 32.126 82.189 1.00 51.32 C
ANISOU 3777 CG PRO B 227 5758 6522 7218 -364 244 -542 C
ATOM 3778 CD PRO B 227 -33.691 32.589 82.825 1.00 56.34 C
ANISOU 3778 CD PRO B 227 6319 7207 7881 -220 -126 -460 C
ATOM 3779 N LEU B 228 -34.991 33.651 79.418 1.00 50.23 N
ANISOU 3779 N LEU B 228 6972 5932 6179 113 -105 149 N
ATOM 3780 CA LEU B 228 -35.748 33.851 78.177 1.00 48.24 C
ANISOU 3780 CA LEU B 228 7243 5563 5523 260 -247 412 C
ATOM 3781 C LEU B 228 -36.546 35.153 78.181 1.00 46.89 C
ANISOU 3781 C LEU B 228 7231 5198 5387 399 -311 642 C
ATOM 3782 O LEU B 228 -36.755 35.749 77.116 1.00 51.14 O
ANISOU 3782 O LEU B 228 8247 5538 5646 471 -237 878 O
ATOM 3783 CB LEU B 228 -36.696 32.676 77.933 1.00 45.11 C
ANISOU 3783 CB LEU B 228 6846 5402 4892 375 -734 446 C
ATOM 3784 CG LEU B 228 -36.057 31.314 77.662 1.00 49.79 C
ANISOU 3784 CG LEU B 228 7402 6146 5371 272 -691 260 C
ATOM 3785 CD1 LEU B 228 -37.105 30.231 77.797 1.00 48.38 C
ANISOU 3785 CD1 LEU B 228 7099 6211 5073 371 -1215 265 C
ATOM 3786 CD2 LEU B 228 -35.392 31.257 76.286 1.00 56.75 C
ANISOU 3786 CD2 LEU B 228 8818 6854 5889 210 -370 318 C
ATOM 3787 N GLY B 229 -37.033 35.582 79.349 1.00 39.15 N
ANISOU 3787 N GLY B 229 5871 4268 4736 446 -449 587 N
ATOM 3788 CA GLY B 229 -37.705 36.870 79.434 1.00 36.37 C
ANISOU 3788 CA GLY B 229 5647 3695 4476 581 -443 786 C
ATOM 3789 C GLY B 229 -36.758 38.020 79.155 1.00 42.31 C
ANISOU 3789 C GLY B 229 6636 4127 5314 455 72 801 C
ATOM 3790 O GLY B 229 -37.101 38.958 78.427 1.00 49.93 O
ANISOU 3790 O GLY B 229 7986 4836 6148 563 159 1057 O
ATOM 3791 N LEU B 230 -35.545 37.947 79.714 1.00 40.43 N
ANISOU 3791 N LEU B 230 6163 3898 5299 218 413 543 N
ATOM 3792 CA LEU B 230 -34.494 38.919 79.427 1.00 45.68 C
ANISOU 3792 CA LEU B 230 7027 4275 6056 49 929 532 C
ATOM 3793 C LEU B 230 -34.056 38.850 77.966 1.00 44.94 C
ANISOU 3793 C LEU B 230 7440 4040 5597 40 1146 697 C
ATOM 3794 O LEU B 230 -33.863 39.889 77.323 1.00 50.82 O
ANISOU 3794 O LEU B 230 8555 4482 6273 36 1434 873 O
ATOM 3795 CB LEU B 230 -33.304 38.679 80.361 1.00 45.04 C
ANISOU 3795 CB LEU B 230 6525 4293 6295 -218 1187 220 C
ATOM 3796 CG LEU B 230 -33.497 39.114 81.817 1.00 43.23 C
ANISOU 3796 CG LEU B 230 5870 4120 6433 -277 1105 48 C
ATOM 3797 CD1 LEU B 230 -32.439 38.485 82.725 1.00 47.77 C
ANISOU 3797 CD1 LEU B 230 5983 4906 7260 -529 1215 -247 C
ATOM 3798 CD2 LEU B 230 -33.509 40.647 81.938 1.00 42.59 C
ANISOU 3798 CD2 LEU B 230 5984 3688 6511 -302 1383 127 C
ATOM 3799 N MET B 231 -33.906 37.634 77.431 1.00 44.62 N
ANISOU 3799 N MET B 231 7439 4203 5311 33 1024 644 N
ATOM 3800 CA MET B 231 -33.545 37.444 76.028 1.00 54.41 C
ANISOU 3800 CA MET B 231 9188 5331 6154 22 1218 782 C
ATOM 3801 C MET B 231 -34.607 38.018 75.090 1.00 59.47 C
ANISOU 3801 C MET B 231 10314 5830 6454 226 996 1126 C
ATOM 3802 O MET B 231 -34.280 38.693 74.105 1.00 62.39 O
ANISOU 3802 O MET B 231 11153 5952 6600 206 1287 1311 O
ATOM 3803 CB MET B 231 -33.327 35.955 75.747 1.00 60.87 C
ANISOU 3803 CB MET B 231 9937 6402 6788 -9 1085 635 C
ATOM 3804 CG MET B 231 -31.953 35.435 76.140 1.00 61.51 C
ANISOU 3804 CG MET B 231 9718 6542 7112 -223 1465 367 C
ATOM 3805 SD MET B 231 -31.685 33.749 75.561 1.00 54.75 S
ANISOU 3805 SD MET B 231 8901 5902 6001 -231 1385 234 S
ATOM 3806 CE MET B 231 -31.970 32.817 77.063 1.00 47.73 C
ANISOU 3806 CE MET B 231 7315 5343 5479 -225 1002 7 C
ATOM 3807 N ALA B 232 -35.887 37.739 75.371 1.00 55.55 N
ANISOU 3807 N ALA B 232 9703 5493 5912 422 475 1233 N
ATOM 3808 CA ALA B 232 -36.979 38.298 74.575 1.00 50.71 C
ANISOU 3808 CA ALA B 232 9481 4767 5019 630 206 1588 C
ATOM 3809 C ALA B 232 -36.866 39.818 74.499 1.00 61.02 C
ANISOU 3809 C ALA B 232 10992 5722 6471 662 516 1774 C
ATOM 3810 O ALA B 232 -36.908 40.404 73.412 1.00 72.41 O
ANISOU 3810 O ALA B 232 12830 7019 7662 689 620 1982 O
ATOM 3811 CB ALA B 232 -38.331 37.889 75.170 1.00 41.93 C
ANISOU 3811 CB ALA B 232 8076 3877 3977 825 -371 1654 C
ATOM 3812 N MET B 233 -36.676 40.458 75.654 1.00 60.24 N
ANISOU 3812 N MET B 233 10518 5549 6820 618 664 1623 N
ATOM 3813 CA MET B 233 -36.554 41.910 75.719 1.00 63.11 C
ANISOU 3813 CA MET B 233 11046 5557 7377 632 979 1761 C
ATOM 3814 C MET B 233 -35.302 42.430 75.010 1.00 65.06 C
ANISOU 3814 C MET B 233 11624 5552 7545 427 1536 1756 C
ATOM 3815 O MET B 233 -35.327 43.532 74.455 1.00 72.66 O
ANISOU 3815 O MET B 233 12821 6300 8485 461 1705 1918 O
ATOM 3816 CB MET B 233 -36.571 42.354 77.183 1.00 66.31 C
ANISOU 3816 CB MET B 233 10969 5959 8268 591 1019 1541 C
ATOM 3817 CG MET B 233 -37.934 42.210 77.837 1.00 66.11 C
ANISOU 3817 CG MET B 233 10682 6086 8350 832 538 1620 C
ATOM 3818 SD MET B 233 -37.990 42.898 79.501 1.00 65.90 S
ANISOU 3818 SD MET B 233 10181 6001 8855 785 645 1377 S
ATOM 3819 CE MET B 233 -37.186 41.606 80.446 1.00 66.59 C
ANISOU 3819 CE MET B 233 9764 6472 9066 539 596 959 C
ATOM 3820 N ALA B 234 -34.208 41.652 75.027 1.00 61.10 N
ANISOU 3820 N ALA B 234 10986 5185 7042 205 1773 1497 N
ATOM 3821 CA ALA B 234 -32.972 42.039 74.340 1.00 60.99 C
ANISOU 3821 CA ALA B 234 11253 4958 6965 0 2323 1484 C
ATOM 3822 C ALA B 234 -33.156 42.047 72.826 1.00 60.66 C
ANISOU 3822 C ALA B 234 11700 4899 6450 92 2288 1696 C
ATOM 3823 O ALA B 234 -32.770 43.008 72.149 1.00 66.49 O
ANISOU 3823 O ALA B 234 12666 5448 7149 61 2555 1782 O
ATOM 3824 CB ALA B 234 -31.839 41.084 74.725 1.00 59.37 C
ANISOU 3824 CB ALA B 234 10707 4955 6895 -226 2530 1154 C
ATOM 3825 N TYR B 235 -33.736 40.968 72.282 1.00 56.56 N
ANISOU 3825 N TYR B 235 11311 4601 5578 191 1936 1749 N
ATOM 3826 CA TYR B 235 -33.933 40.860 70.839 1.00 59.61 C
ANISOU 3826 CA TYR B 235 12101 5021 5526 245 1855 1890 C
ATOM 3827 C TYR B 235 -35.005 41.818 70.335 1.00 66.50 C
ANISOU 3827 C TYR B 235 13116 5827 6324 430 1572 2172 C
ATOM 3828 O TYR B 235 -34.923 42.277 69.192 1.00 75.83 O
ANISOU 3828 O TYR B 235 14637 6919 7254 430 1670 2314 O
ATOM 3829 CB TYR B 235 -34.257 39.408 70.443 1.00 61.35 C
ANISOU 3829 CB TYR B 235 12363 5518 5428 265 1538 1812 C
ATOM 3830 CG TYR B 235 -33.037 38.506 70.514 1.00 63.28 C
ANISOU 3830 CG TYR B 235 12564 5804 5676 70 1915 1556 C
ATOM 3831 CD1 TYR B 235 -31.980 38.662 69.621 1.00 65.39 C
ANISOU 3831 CD1 TYR B 235 13072 5941 5831 -63 2366 1490 C
ATOM 3832 CD2 TYR B 235 -32.923 37.527 71.494 1.00 58.50 C
ANISOU 3832 CD2 TYR B 235 11599 5386 5243 22 1815 1361 C
ATOM 3833 CE1 TYR B 235 -30.848 37.861 69.698 1.00 67.06 C
ANISOU 3833 CE1 TYR B 235 13157 6200 6123 -227 2720 1243 C
ATOM 3834 CE2 TYR B 235 -31.795 36.721 71.578 1.00 58.48 C
ANISOU 3834 CE2 TYR B 235 11417 5466 5338 -150 2146 1092 C
ATOM 3835 CZ TYR B 235 -30.761 36.893 70.679 1.00 65.54 C
ANISOU 3835 CZ TYR B 235 12600 6198 6105 -276 2637 1068 C
ATOM 3836 OH TYR B 235 -29.642 36.093 70.762 1.00 71.54 O
ANISOU 3836 OH TYR B 235 13154 7027 7001 -425 2974 816 O
ATOM 3837 N PHE B 236 -36.005 42.156 71.165 1.00 63.68 N
ANISOU 3837 N PHE B 236 12484 5508 6204 585 1238 2259 N
ATOM 3838 CA PHE B 236 -36.976 43.171 70.753 1.00 67.90 C
ANISOU 3838 CA PHE B 236 13087 5963 6749 749 1025 2532 C
ATOM 3839 C PHE B 236 -36.287 44.521 70.525 1.00 69.45 C
ANISOU 3839 C PHE B 236 13479 5832 7077 685 1479 2604 C
ATOM 3840 O PHE B 236 -36.611 45.230 69.563 1.00 78.21 O
ANISOU 3840 O PHE B 236 14854 6847 8015 749 1456 2837 O
ATOM 3841 CB PHE B 236 -38.115 43.297 71.779 1.00 67.13 C
ANISOU 3841 CB PHE B 236 12593 5962 6950 918 639 2579 C
ATOM 3842 CG PHE B 236 -39.131 44.365 71.427 1.00 75.01 C
ANISOU 3842 CG PHE B 236 13601 6874 8027 1078 447 2867 C
ATOM 3843 CD1 PHE B 236 -40.156 44.109 70.524 1.00 76.07 C
ANISOU 3843 CD1 PHE B 236 13765 7207 7931 1172 48 3085 C
ATOM 3844 CD2 PHE B 236 -39.037 45.635 71.975 1.00 83.30 C
ANISOU 3844 CD2 PHE B 236 14615 7637 9396 1113 690 2915 C
ATOM 3845 CE1 PHE B 236 -41.071 45.101 70.185 1.00 82.78 C
ANISOU 3845 CE1 PHE B 236 14600 7971 8882 1305 -109 3380 C
ATOM 3846 CE2 PHE B 236 -39.948 46.629 71.640 1.00 87.40 C
ANISOU 3846 CE2 PHE B 236 15153 8053 10001 1261 531 3189 C
ATOM 3847 CZ PHE B 236 -40.964 46.361 70.744 1.00 87.84 C
ANISOU 3847 CZ PHE B 236 15230 8306 9839 1358 126 3438 C
ATOM 3848 N GLN B 237 -35.314 44.865 71.383 1.00 66.35 N
ANISOU 3848 N GLN B 237 12933 5278 6998 536 1890 2395 N
ATOM 3849 CA GLN B 237 -34.524 46.094 71.244 1.00 69.36 C
ANISOU 3849 CA GLN B 237 13442 5371 7541 431 2347 2399 C
ATOM 3850 C GLN B 237 -33.581 46.037 70.038 1.00 76.76 C
ANISOU 3850 C GLN B 237 14734 6251 8181 299 2674 2401 C
ATOM 3851 O GLN B 237 -33.413 47.035 69.328 1.00 83.01 O
ANISOU 3851 O GLN B 237 15783 6843 8914 304 2869 2555 O
ATOM 3852 CB GLN B 237 -33.718 46.346 72.528 1.00 65.30 C
ANISOU 3852 CB GLN B 237 12583 4766 7463 261 2661 2121 C
ATOM 3853 CG GLN B 237 -34.533 46.849 73.720 1.00 63.28 C
ANISOU 3853 CG GLN B 237 12015 4468 7559 375 2458 2110 C
ATOM 3854 CD GLN B 237 -33.713 47.675 74.704 1.00 65.45 C
ANISOU 3854 CD GLN B 237 12052 4572 8244 187 2834 1875 C
ATOM 3855 OE1 GLN B 237 -32.521 47.435 74.905 1.00 68.08 O
ANISOU 3855 OE1 GLN B 237 12267 4928 8673 -55 3160 1639 O
ATOM 3856 NE2 GLN B 237 -34.351 48.671 75.307 1.00 67.37 N
ANISOU 3856 NE2 GLN B 237 12201 4665 8732 292 2779 1929 N
ATOM 3857 N ILE B 238 -32.927 44.880 69.832 1.00 74.23 N
ANISOU 3857 N ILE B 238 14419 6092 7693 179 2757 2220 N
ATOM 3858 CA ILE B 238 -32.084 44.629 68.658 1.00 72.93 C
ANISOU 3858 CA ILE B 238 14582 5900 7229 70 3042 2197 C
ATOM 3859 C ILE B 238 -32.921 44.732 67.380 1.00 76.78 C
ANISOU 3859 C ILE B 238 15456 6419 7300 211 2758 2473 C
ATOM 3860 O ILE B 238 -32.504 45.352 66.392 1.00 81.26 O
ANISOU 3860 O ILE B 238 16350 6832 7692 173 3000 2585 O
ATOM 3861 CB ILE B 238 -31.389 43.249 68.801 1.00 70.54 C
ANISOU 3861 CB ILE B 238 14152 5787 6863 -58 3127 1940 C
ATOM 3862 CG1 ILE B 238 -30.240 43.280 69.834 1.00 67.55 C
ANISOU 3862 CG1 ILE B 238 13386 5364 6915 -256 3513 1661 C
ATOM 3863 CG2 ILE B 238 -30.885 42.685 67.457 1.00 73.87 C
ANISOU 3863 CG2 ILE B 238 14944 6234 6889 -110 3272 1933 C
ATOM 3864 CD1 ILE B 238 -29.953 41.925 70.543 1.00 63.16 C
ANISOU 3864 CD1 ILE B 238 12510 5041 6449 -338 3445 1429 C
ATOM 3865 N PHE B 239 -34.136 44.159 67.408 1.00 75.37 N
ANISOU 3865 N PHE B 239 15207 6449 6981 368 2226 2590 N
ATOM 3866 CA PHE B 239 -35.085 44.252 66.297 1.00 79.94 C
ANISOU 3866 CA PHE B 239 16050 7106 7220 491 1878 2858 C
ATOM 3867 C PHE B 239 -35.404 45.707 65.953 1.00 87.61 C
ANISOU 3867 C PHE B 239 17164 7846 8277 575 1950 3132 C
ATOM 3868 O PHE B 239 -35.369 46.101 64.780 1.00 90.68 O
ANISOU 3868 O PHE B 239 17908 8163 8383 569 2011 3314 O
ATOM 3869 CB PHE B 239 -36.379 43.489 66.637 1.00 76.55 C
ANISOU 3869 CB PHE B 239 15368 6957 6760 632 1282 2913 C
ATOM 3870 CG PHE B 239 -37.528 43.770 65.686 1.00 80.47 C
ANISOU 3870 CG PHE B 239 15996 7549 7030 757 886 3219 C
ATOM 3871 CD1 PHE B 239 -37.594 43.144 64.449 1.00 83.51 C
ANISOU 3871 CD1 PHE B 239 16680 8062 6987 705 778 3264 C
ATOM 3872 CD2 PHE B 239 -38.530 44.671 66.023 1.00 81.47 C
ANISOU 3872 CD2 PHE B 239 15933 7633 7390 916 642 3464 C
ATOM 3873 CE1 PHE B 239 -38.632 43.413 63.566 1.00 87.50 C
ANISOU 3873 CE1 PHE B 239 17282 8669 7294 797 425 3558 C
ATOM 3874 CE2 PHE B 239 -39.572 44.943 65.143 1.00 89.73 C
ANISOU 3874 CE2 PHE B 239 17053 8778 8261 1016 296 3772 C
ATOM 3875 CZ PHE B 239 -39.621 44.312 63.914 1.00 89.42 C
ANISOU 3875 CZ PHE B 239 17302 8886 7787 952 184 3825 C
ATOM 3876 N ARG B 240 -35.725 46.513 66.978 1.00 85.75 N
ANISOU 3876 N ARG B 240 16658 7487 8438 651 1945 3161 N
ATOM 3877 CA ARG B 240 -36.023 47.935 66.799 1.00 85.44 C
ANISOU 3877 CA ARG B 240 16720 7200 8545 734 2032 3402 C
ATOM 3878 C ARG B 240 -34.836 48.711 66.241 1.00 89.04 C
ANISOU 3878 C ARG B 240 17462 7396 8973 586 2575 3372 C
ATOM 3879 O ARG B 240 -35.026 49.685 65.503 1.00 97.48 O
ANISOU 3879 O ARG B 240 18781 8291 9965 640 2633 3624 O
ATOM 3880 CB ARG B 240 -36.442 48.571 68.129 1.00 82.86 C
ANISOU 3880 CB ARG B 240 16032 6770 8681 816 1990 3359 C
ATOM 3881 CG ARG B 240 -37.744 48.087 68.723 1.00 83.24 C
ANISOU 3881 CG ARG B 240 15762 7034 8831 990 1459 3431 C
ATOM 3882 CD ARG B 240 -38.277 49.142 69.675 1.00 90.83 C
ANISOU 3882 CD ARG B 240 16487 7807 10217 1104 1455 3485 C
ATOM 3883 NE ARG B 240 -38.763 50.335 68.984 1.00104.60 N
ANISOU 3883 NE ARG B 240 18434 9346 11964 1210 1451 3798 N
ATOM 3884 CZ ARG B 240 -40.039 50.705 68.954 1.00109.90 C
ANISOU 3884 CZ ARG B 240 18968 10053 12734 1398 1060 4054 C
ATOM 3885 NH1 ARG B 240 -40.952 49.975 69.581 1.00109.22 N
ANISOU 3885 NH1 ARG B 240 18528 10212 12759 1492 653 4019 N
ATOM 3886 NH2 ARG B 240 -40.403 51.806 68.311 1.00112.32 N
ANISOU 3886 NH2 ARG B 240 19470 10152 13054 1484 1082 4349 N
ATOM 3887 N LYS B 241 -33.612 48.306 66.596 1.00 89.71 N
ANISOU 3887 N LYS B 241 17482 7455 9147 396 2971 3074 N
ATOM 3888 CA LYS B 241 -32.409 48.976 66.115 1.00 90.06 C
ANISOU 3888 CA LYS B 241 17732 7277 9209 236 3499 3011 C
ATOM 3889 C LYS B 241 -32.125 48.617 64.651 1.00 96.89 C
ANISOU 3889 C LYS B 241 19020 8175 9617 200 3567 3115 C
ATOM 3890 O LYS B 241 -31.962 49.508 63.813 1.00100.42 O
ANISOU 3890 O LYS B 241 19772 8436 9949 199 3747 3306 O
ATOM 3891 CB LYS B 241 -31.211 48.612 66.999 1.00 86.75 C
ANISOU 3891 CB LYS B 241 17023 6857 9081 35 3870 2652 C
ATOM 3892 CG LYS B 241 -30.034 49.594 66.937 1.00 89.63 C
ANISOU 3892 CG LYS B 241 17433 6972 9652 -131 4399 2561 C
ATOM 3893 CD LYS B 241 -30.112 50.662 68.021 1.00 97.01 C
ANISOU 3893 CD LYS B 241 18105 7736 11018 -140 4484 2518 C
ATOM 3894 CE LYS B 241 -28.863 51.534 68.028 1.00101.82 C
ANISOU 3894 CE LYS B 241 18713 8130 11843 -335 4994 2382 C
ATOM 3895 NZ LYS B 241 -28.892 52.515 69.149 1.00103.43 N
ANISOU 3895 NZ LYS B 241 18649 8185 12464 -372 5074 2292 N
ATOM 3896 N LEU B 242 -32.103 47.310 64.334 1.00 93.86 N
ANISOU 3896 N LEU B 242 18666 8025 8970 169 3413 2990 N
ATOM 3897 CA LEU B 242 -31.764 46.835 62.989 1.00 95.88 C
ANISOU 3897 CA LEU B 242 19319 8320 8792 113 3499 3031 C
ATOM 3898 C LEU B 242 -32.871 47.055 61.952 1.00100.33 C
ANISOU 3898 C LEU B 242 20178 8947 8998 250 3106 3367 C
ATOM 3899 O LEU B 242 -32.565 47.203 60.766 1.00107.99 O
ANISOU 3899 O LEU B 242 21536 9852 9644 201 3255 3477 O
ATOM 3900 CB LEU B 242 -31.397 45.345 63.013 1.00 92.85 C
ANISOU 3900 CB LEU B 242 18863 8153 8264 32 3465 2769 C
ATOM 3901 CG LEU B 242 -30.070 44.934 63.654 1.00 90.29 C
ANISOU 3901 CG LEU B 242 18306 7786 8213 -141 3913 2439 C
ATOM 3902 CD1 LEU B 242 -30.004 43.431 63.884 1.00 86.69 C
ANISOU 3902 CD1 LEU B 242 17705 7566 7668 -176 3767 2217 C
ATOM 3903 CD2 LEU B 242 -28.914 45.390 62.768 1.00 98.15 C
ANISOU 3903 CD2 LEU B 242 19575 8584 9133 -272 4422 2407 C
ATOM 3904 N TRP B 243 -34.147 47.047 62.353 1.00 98.45 N
ANISOU 3904 N TRP B 243 19743 8846 8816 413 2604 3534 N
ATOM 3905 CA TRP B 243 -35.247 47.204 61.403 1.00102.23 C
ANISOU 3905 CA TRP B 243 20420 9427 8996 533 2192 3861 C
ATOM 3906 C TRP B 243 -36.038 48.510 61.591 1.00114.72 C
ANISOU 3906 C TRP B 243 21929 10854 10806 681 2051 4180 C
ATOM 3907 O TRP B 243 -37.027 48.720 60.889 1.00120.97 O
ANISOU 3907 O TRP B 243 22815 11735 11413 789 1687 4488 O
ATOM 3908 CB TRP B 243 -36.196 46.010 61.474 1.00 99.62 C
ANISOU 3908 CB TRP B 243 19907 9429 8513 595 1670 3824 C
ATOM 3909 CG TRP B 243 -35.667 44.753 60.828 1.00100.25 C
ANISOU 3909 CG TRP B 243 20182 9663 8245 466 1725 3602 C
ATOM 3910 CD1 TRP B 243 -35.808 44.376 59.522 1.00105.05 C
ANISOU 3910 CD1 TRP B 243 21155 10355 8406 421 1629 3701 C
ATOM 3911 CD2 TRP B 243 -34.899 43.721 61.461 1.00 95.02 C
ANISOU 3911 CD2 TRP B 243 19362 9071 7669 360 1905 3243 C
ATOM 3912 NE1 TRP B 243 -35.184 43.169 59.307 1.00104.45 N
ANISOU 3912 NE1 TRP B 243 21166 10381 8141 298 1745 3409 N
ATOM 3913 CE2 TRP B 243 -34.617 42.747 60.481 1.00 96.87 C
ANISOU 3913 CE2 TRP B 243 19881 9414 7511 264 1916 3134 C
ATOM 3914 CE3 TRP B 243 -34.425 43.525 62.762 1.00 89.81 C
ANISOU 3914 CE3 TRP B 243 18344 8391 7388 333 2060 3010 C
ATOM 3915 CZ2 TRP B 243 -33.882 41.595 60.763 1.00 93.79 C
ANISOU 3915 CZ2 TRP B 243 19418 9100 7119 154 2083 2807 C
ATOM 3916 CZ3 TRP B 243 -33.695 42.382 63.039 1.00 86.75 C
ANISOU 3916 CZ3 TRP B 243 17874 8101 6986 219 2213 2703 C
ATOM 3917 CH2 TRP B 243 -33.430 41.432 62.044 1.00 88.74 C
ANISOU 3917 CH2 TRP B 243 18405 8448 6865 137 2227 2606 C
ATOM 3918 N GLY B 244 -35.605 49.382 62.503 1.00112.75 N
ANISOU 3918 N GLY B 244 21507 10372 10962 679 2342 4109 N
ATOM 3919 CA GLY B 244 -36.241 50.675 62.697 1.00119.90 C
ANISOU 3919 CA GLY B 244 22364 11078 12113 811 2277 4383 C
ATOM 3920 C GLY B 244 -35.752 51.704 61.682 1.00128.86 C
ANISOU 3920 C GLY B 244 23900 11963 13098 768 2590 4596 C
ATOM 3921 O GLY B 244 -35.025 51.390 60.742 1.00132.49 O
ANISOU 3921 O GLY B 244 24685 12426 13228 645 2818 4556 O
ATOM 3922 N ARG B 245 -36.175 52.954 61.891 1.00134.42 N
ANISOU 3922 N ARG B 245 24579 12436 14060 874 2606 4824 N
ATOM 3923 CA ARG B 245 -35.736 54.066 61.038 1.00141.95 C
ANISOU 3923 CA ARG B 245 25891 13117 14928 841 2914 5044 C
ATOM 3924 C ARG B 245 -34.245 54.326 61.271 1.00140.72 C
ANISOU 3924 C ARG B 245 25810 12761 14896 644 3528 4748 C
ATOM 3925 O ARG B 245 -33.832 54.578 62.405 1.00137.32 O
ANISOU 3925 O ARG B 245 25092 12228 14856 597 3733 4509 O
ATOM 3926 CB ARG B 245 -36.568 55.320 61.343 1.00148.07 C
ANISOU 3926 CB ARG B 245 26578 13677 16006 1008 2782 5336 C
ATOM 3927 CG ARG B 245 -36.223 56.580 60.522 1.00159.28 C
ANISOU 3927 CG ARG B 245 28354 14787 17377 995 3077 5601 C
ATOM 3928 CD ARG B 245 -36.807 57.866 61.135 1.00164.09 C
ANISOU 3928 CD ARG B 245 28829 15118 18400 1139 3065 5783 C
ATOM 3929 NE ARG B 245 -36.565 57.950 62.574 1.00161.93 N
ANISOU 3929 NE ARG B 245 28193 14768 18563 1121 3221 5453 N
ATOM 3930 CZ ARG B 245 -35.505 58.530 63.133 1.00162.17 C
ANISOU 3930 CZ ARG B 245 28210 14568 18837 977 3723 5199 C
ATOM 3931 NH1 ARG B 245 -34.572 59.093 62.378 1.00164.40 N
ANISOU 3931 NH1 ARG B 245 28815 14660 18989 844 4133 5235 N
ATOM 3932 NH2 ARG B 245 -35.380 58.546 64.454 1.00158.93 N
ANISOU 3932 NH2 ARG B 245 27453 14129 18806 954 3812 4906 N
ATOM 3933 N GLN B 246 -33.434 54.255 60.210 1.00139.45 N
ANISOU 3933 N GLN B 246 26013 12555 14416 516 3818 4759 N
ATOM 3934 CA GLN B 246 -31.980 54.378 60.356 1.00136.85 C
ANISOU 3934 CA GLN B 246 25720 12071 14206 313 4394 4470 C
ATOM 3935 C GLN B 246 -31.514 55.839 60.337 1.00135.96 C
ANISOU 3935 C GLN B 246 25722 11607 14329 279 4769 4586 C
ATOM 3936 O GLN B 246 -32.086 56.694 59.654 1.00137.66 O
ANISOU 3936 O GLN B 246 26182 11683 14440 384 4669 4938 O
ATOM 3937 CB GLN B 246 -31.251 53.584 59.261 1.00141.93 C
ANISOU 3937 CB GLN B 246 26682 12817 14429 184 4573 4393 C
ATOM 3938 CG GLN B 246 -31.508 52.062 59.260 1.00141.47 C
ANISOU 3938 CG GLN B 246 26532 13086 14136 181 4279 4216 C
ATOM 3939 CD GLN B 246 -31.249 51.381 60.602 1.00135.02 C
ANISOU 3939 CD GLN B 246 25262 12380 13660 140 4283 3874 C
ATOM 3940 OE1 GLN B 246 -30.109 51.280 61.060 1.00134.37 O
ANISOU 3940 OE1 GLN B 246 25042 12221 13791 -16 4698 3589 O
ATOM 3941 NE2 GLN B 246 -32.314 50.892 61.228 1.00130.59 N
ANISOU 3941 NE2 GLN B 246 24446 12012 13159 276 3806 3910 N
ATOM 3942 N ILE B 247 -30.447 56.105 61.102 1.00131.63 N
ANISOU 3942 N ILE B 247 24978 10924 14111 120 5199 4283 N
ATOM 3943 CA ILE B 247 -29.797 57.407 61.304 1.00133.53 C
ANISOU 3943 CA ILE B 247 25253 10839 14644 38 5613 4289 C
ATOM 3944 C ILE B 247 -29.438 58.022 59.947 1.00138.99 C
ANISOU 3944 C ILE B 247 26411 11361 15038 4 5844 4546 C
ATOM 3945 O ILE B 247 -28.982 57.299 59.052 1.00138.50 O
ANISOU 3945 O ILE B 247 26582 11420 14623 -73 5927 4520 O
ATOM 3946 CB ILE B 247 -28.583 57.237 62.264 1.00131.00 C
ANISOU 3946 CB ILE B 247 24610 10498 14667 -174 6002 3867 C
ATOM 3947 CG1 ILE B 247 -27.994 58.571 62.753 1.00134.62 C
ANISOU 3947 CG1 ILE B 247 25008 10643 15499 -271 6378 3821 C
ATOM 3948 CG2 ILE B 247 -27.484 56.306 61.701 1.00130.94 C
ANISOU 3948 CG2 ILE B 247 24679 10617 14456 -346 6271 3652 C
ATOM 3949 CD1 ILE B 247 -27.509 58.542 64.227 1.00130.36 C
ANISOU 3949 CD1 ILE B 247 23994 10126 15409 -396 6492 3455 C
ATOM 3950 N PRO B 248 -29.673 59.328 59.714 1.00144.42 N
ANISOU 3950 N PRO B 248 27267 11766 15838 63 5943 4808 N
ATOM 3951 CA PRO B 248 -29.443 59.894 58.379 1.00146.14 C
ANISOU 3951 CA PRO B 248 27948 11835 15743 43 6120 5096 C
ATOM 3952 C PRO B 248 -27.964 59.931 58.000 1.00152.67 C
ANISOU 3952 C PRO B 248 28901 12553 16555 -189 6680 4879 C
ATOM 3953 O PRO B 248 -27.098 60.223 58.829 1.00149.64 O
ANISOU 3953 O PRO B 248 28260 12056 16540 -333 7018 4591 O
ATOM 3954 CB PRO B 248 -30.027 61.310 58.473 1.00150.00 C
ANISOU 3954 CB PRO B 248 28509 12028 16456 162 6105 5395 C
ATOM 3955 CG PRO B 248 -30.013 61.634 59.919 1.00145.78 C
ANISOU 3955 CG PRO B 248 27560 11414 16417 156 6156 5139 C
ATOM 3956 CD PRO B 248 -30.268 60.324 60.628 1.00145.36 C
ANISOU 3956 CD PRO B 248 27180 11692 16358 170 5867 4878 C
ATOM 3957 N GLY B 249 -27.683 59.631 56.731 1.00158.10 N
ANISOU 3957 N GLY B 249 29976 13279 16814 -232 6770 5019 N
ATOM 3958 CA GLY B 249 -26.328 59.655 56.217 1.00159.93 C
ANISOU 3958 CA GLY B 249 30362 13403 17002 -438 7298 4851 C
ATOM 3959 C GLY B 249 -25.474 58.489 56.660 1.00153.81 C
ANISOU 3959 C GLY B 249 29327 12824 16290 -577 7450 4437 C
ATOM 3960 O GLY B 249 -24.458 58.683 57.335 1.00151.66 O
ANISOU 3960 O GLY B 249 28794 12457 16375 -735 7815 4157 O
ATOM 3961 N THR B 250 -25.855 57.259 56.287 1.00153.63 N
ANISOU 3961 N THR B 250 29360 13078 15936 -527 7168 4393 N
ATOM 3962 CA THR B 250 -25.120 56.058 56.663 1.00151.76 C
ANISOU 3962 CA THR B 250 28884 13032 15746 -639 7280 4019 C
ATOM 3963 C THR B 250 -24.183 55.618 55.537 1.00157.00 C
ANISOU 3963 C THR B 250 29868 13678 16106 -766 7635 3964 C
ATOM 3964 O THR B 250 -24.597 55.536 54.371 1.00159.28 O
ANISOU 3964 O THR B 250 30590 13990 15940 -714 7528 4207 O
ATOM 3965 CB THR B 250 -26.076 54.919 57.051 1.00149.64 C
ANISOU 3965 CB THR B 250 28447 13068 15342 -515 6770 3966 C
ATOM 3966 OG1 THR B 250 -25.337 53.824 57.614 1.00148.83 O
ANISOU 3966 OG1 THR B 250 28049 13126 15374 -624 6892 3592 O
ATOM 3967 CG2 THR B 250 -26.874 54.421 55.852 1.00153.67 C
ANISOU 3967 CG2 THR B 250 29364 13721 15304 -416 6450 4223 C
ATOM 3968 N THR B 251 -22.920 55.346 55.894 1.00160.58 N
ANISOU 3968 N THR B 251 30097 14093 16824 -937 8052 3648 N
ATOM 3969 CA THR B 251 -21.894 54.858 54.975 1.00149.90 C
ANISOU 3969 CA THR B 251 28970 12715 15272 -1066 8438 3541 C
ATOM 3970 C THR B 251 -22.295 53.506 54.385 1.00148.68 C
ANISOU 3970 C THR B 251 28981 12805 14704 -1010 8185 3491 C
ATOM 3971 O THR B 251 -23.067 52.752 54.987 1.00156.17 O
ANISOU 3971 O THR B 251 29719 13971 15649 -914 7772 3422 O
ATOM 3972 CB THR B 251 -20.535 54.710 55.687 1.00148.10 C
ANISOU 3972 CB THR B 251 28343 12437 15491 -1244 8856 3194 C
ATOM 3973 OG1 THR B 251 -20.606 53.657 56.660 1.00141.73 O
ANISOU 3973 OG1 THR B 251 27108 11862 14880 -1232 8634 2922 O
ATOM 3974 CG2 THR B 251 -20.099 56.002 56.386 1.00149.08 C
ANISOU 3974 CG2 THR B 251 28257 12334 16053 -1326 9091 3197 C
ATOM 3975 N SER B 252 -21.752 53.180 53.206 1.00134.97 N
ANISOU 3975 N SER B 252 24157 13743 13382 -1795 6131 4902 N
ATOM 3976 CA SER B 252 -22.067 51.902 52.566 1.00133.10 C
ANISOU 3976 CA SER B 252 23943 13880 12749 -1635 5949 4813 C
ATOM 3977 C SER B 252 -21.667 50.713 53.441 1.00127.06 C
ANISOU 3977 C SER B 252 22862 13305 12111 -1636 5901 4373 C
ATOM 3978 O SER B 252 -22.348 49.679 53.440 1.00123.52 O
ANISOU 3978 O SER B 252 22393 13056 11483 -1458 5640 4218 O
ATOM 3979 CB SER B 252 -21.392 51.811 51.193 1.00138.79 C
ANISOU 3979 CB SER B 252 24851 14802 13081 -1714 6192 5026 C
ATOM 3980 OG SER B 252 -22.243 52.308 50.173 1.00149.49 O
ANISOU 3980 OG SER B 252 26520 16169 14112 -1612 6040 5438 O
ATOM 3981 N ALA B 285 -20.574 50.863 54.204 1.00126.27 N
ANISOU 3981 N ALA B 285 22499 13149 12329 -1853 6141 4198 N
ATOM 3982 CA ALA B 285 -20.070 49.835 55.115 1.00121.30 C
ANISOU 3982 CA ALA B 285 21516 12703 11870 -1888 6109 3849 C
ATOM 3983 C ALA B 285 -21.041 49.554 56.262 1.00133.21 C
ANISOU 3983 C ALA B 285 22913 14140 13561 -1764 5772 3641 C
ATOM 3984 O ALA B 285 -21.194 48.399 56.684 1.00130.80 O
ANISOU 3984 O ALA B 285 22425 14041 13233 -1660 5609 3405 O
ATOM 3985 CB ALA B 285 -18.716 50.280 55.671 1.00122.97 C
ANISOU 3985 CB ALA B 285 21453 12879 12390 -2192 6414 3800 C
ATOM 3986 N GLU B 286 -21.668 50.610 56.796 1.00127.27 N
ANISOU 3986 N GLU B 286 22267 13079 13012 -1782 5700 3726 N
ATOM 3987 CA GLU B 286 -22.639 50.484 57.883 1.00122.00 C
ANISOU 3987 CA GLU B 286 21525 12305 12526 -1670 5423 3542 C
ATOM 3988 C GLU B 286 -23.877 49.708 57.443 1.00119.56 C
ANISOU 3988 C GLU B 286 21342 12132 11955 -1365 5092 3570 C
ATOM 3989 O GLU B 286 -24.428 48.913 58.217 1.00117.80 O
ANISOU 3989 O GLU B 286 20965 12000 11793 -1258 4861 3336 O
ATOM 3990 CB GLU B 286 -23.045 51.875 58.380 1.00122.70 C
ANISOU 3990 CB GLU B 286 21751 11988 12882 -1746 5491 3653 C
ATOM 3991 CG GLU B 286 -21.931 52.655 59.059 1.00132.13 C
ANISOU 3991 CG GLU B 286 22807 13024 14371 -2097 5783 3560 C
ATOM 3992 CD GLU B 286 -22.348 54.058 59.459 1.00144.90 C
ANISOU 3992 CD GLU B 286 24613 14193 16251 -2176 5900 3652 C
ATOM 3993 OE1 GLU B 286 -23.438 54.502 59.039 1.00150.03 O
ANISOU 3993 OE1 GLU B 286 25498 14647 16857 -1934 5784 3869 O
ATOM 3994 OE2 GLU B 286 -21.583 54.716 60.196 1.00149.95 O
ANISOU 3994 OE2 GLU B 286 25151 14676 17149 -2492 6110 3516 O
ATOM 3995 N VAL B 287 -24.339 49.955 56.209 1.00123.02 N
ANISOU 3995 N VAL B 287 22053 12595 12092 -1246 5055 3876 N
ATOM 3996 CA VAL B 287 -25.493 49.248 55.648 1.00121.02 C
ANISOU 3996 CA VAL B 287 21920 12518 11543 -1003 4724 3947 C
ATOM 3997 C VAL B 287 -25.139 47.785 55.377 1.00117.89 C
ANISOU 3997 C VAL B 287 21418 12462 10911 -972 4688 3695 C
ATOM 3998 O VAL B 287 -25.956 46.885 55.606 1.00115.12 O
ANISOU 3998 O VAL B 287 21019 12247 10475 -816 4404 3544 O
ATOM 3999 CB VAL B 287 -26.002 49.962 54.372 1.00125.50 C
ANISOU 3999 CB VAL B 287 22793 13065 11828 -937 4687 4395 C
ATOM 4000 CG1 VAL B 287 -27.339 49.378 53.899 1.00122.79 C
ANISOU 4000 CG1 VAL B 287 22543 12907 11206 -717 4283 4518 C
ATOM 4001 CG2 VAL B 287 -26.149 51.471 54.587 1.00121.21 C
ANISOU 4001 CG2 VAL B 287 22352 12132 11572 -983 4807 4672 C
ATOM 4002 N LYS B 288 -23.910 47.531 54.892 1.00118.06 N
ANISOU 4002 N LYS B 288 21399 12607 10851 -1122 4999 3651 N
ATOM 4003 CA LYS B 288 -23.410 46.166 54.698 1.00114.31 C
ANISOU 4003 CA LYS B 288 20803 12402 10227 -1100 5053 3401 C
ATOM 4004 C LYS B 288 -23.316 45.418 56.024 1.00110.05 C
ANISOU 4004 C LYS B 288 19925 11887 10002 -1088 4948 3082 C
ATOM 4005 O LYS B 288 -23.589 44.211 56.087 1.00111.12 O
ANISOU 4005 O LYS B 288 19985 12194 10042 -972 4816 2879 O
ATOM 4006 CB LYS B 288 -22.032 46.201 54.023 1.00117.84 C
ANISOU 4006 CB LYS B 288 21236 12930 10609 -1268 5466 3446 C
ATOM 4007 CG LYS B 288 -22.050 46.468 52.523 1.00128.99 C
ANISOU 4007 CG LYS B 288 22994 14429 11588 -1274 5589 3708 C
ATOM 4008 CD LYS B 288 -20.745 47.101 52.058 1.00132.28 C
ANISOU 4008 CD LYS B 288 23402 14806 12053 -1477 6022 3845 C
ATOM 4009 CE LYS B 288 -20.872 47.696 50.667 1.00134.59 C
ANISOU 4009 CE LYS B 288 24064 15139 11936 -1505 6128 4182 C
ATOM 4010 NZ LYS B 288 -19.543 48.131 50.161 1.00140.08 N
ANISOU 4010 NZ LYS B 288 24743 15825 12655 -1703 6586 4285 N
ATOM 4011 N GLN B 289 -22.905 46.126 57.082 1.00105.53 N
ANISOU 4011 N GLN B 289 19154 11149 9794 -1231 5018 3043 N
ATOM 4012 CA GLN B 289 -22.869 45.572 58.435 1.00 97.11 C
ANISOU 4012 CA GLN B 289 17767 10117 9013 -1256 4894 2786 C
ATOM 4013 C GLN B 289 -24.278 45.288 58.956 1.00 93.02 C
ANISOU 4013 C GLN B 289 17309 9546 8490 -1058 4530 2700 C
ATOM 4014 O GLN B 289 -24.512 44.241 59.571 1.00 89.97 O
ANISOU 4014 O GLN B 289 16736 9298 8152 -977 4369 2486 O
ATOM 4015 CB GLN B 289 -22.132 46.541 59.372 1.00 97.61 C
ANISOU 4015 CB GLN B 289 17650 10024 9413 -1513 5054 2784 C
ATOM 4016 CG GLN B 289 -21.908 46.027 60.804 1.00 93.67 C
ANISOU 4016 CG GLN B 289 16791 9614 9184 -1613 4945 2549 C
ATOM 4017 CD GLN B 289 -21.275 47.060 61.741 1.00 98.02 C
ANISOU 4017 CD GLN B 289 17199 10017 10026 -1922 5076 2537 C
ATOM 4018 OE1 GLN B 289 -21.532 48.261 61.638 1.00 99.84 O
ANISOU 4018 OE1 GLN B 289 17658 9963 10315 -1998 5161 2645 O
ATOM 4019 NE2 GLN B 289 -20.450 46.583 62.669 1.00 96.89 N
ANISOU 4019 NE2 GLN B 289 16671 10073 10069 -2115 5091 2416 N
ATOM 4020 N MET B 290 -25.223 46.207 58.709 1.00 94.70 N
ANISOU 4020 N MET B 290 17763 9556 8661 -972 4410 2891 N
ATOM 4021 CA MET B 290 -26.595 46.046 59.196 1.00 91.60 C
ANISOU 4021 CA MET B 290 17408 9102 8295 -781 4081 2852 C
ATOM 4022 C MET B 290 -27.273 44.831 58.565 1.00 90.18 C
ANISOU 4022 C MET B 290 17280 9166 7818 -597 3844 2795 C
ATOM 4023 O MET B 290 -27.864 44.002 59.268 1.00 85.85 O
ANISOU 4023 O MET B 290 16590 8691 7339 -498 3628 2593 O
ATOM 4024 CB MET B 290 -27.425 47.304 58.901 1.00 96.66 C
ANISOU 4024 CB MET B 290 18280 9479 8967 -709 4032 3145 C
ATOM 4025 CG MET B 290 -28.898 47.179 59.338 1.00 99.81 C
ANISOU 4025 CG MET B 290 18692 9817 9416 -490 3699 3157 C
ATOM 4026 SD MET B 290 -29.966 48.592 58.976 1.00107.69 S
ANISOU 4026 SD MET B 290 19904 10503 10512 -357 3628 3571 S
ATOM 4027 CE MET B 290 -30.041 48.480 57.182 1.00114.30 C
ANISOU 4027 CE MET B 290 20973 11578 10878 -305 3547 3945 C
ATOM 4028 N ARG B 291 -27.201 44.718 57.227 1.00 94.24 N
ANISOU 4028 N ARG B 291 18011 9812 7983 -574 3889 2970 N
ATOM 4029 CA ARG B 291 -27.860 43.631 56.497 1.00 94.05 C
ANISOU 4029 CA ARG B 291 18089 10023 7622 -448 3677 2919 C
ATOM 4030 C ARG B 291 -27.332 42.248 56.905 1.00 90.50 C
ANISOU 4030 C ARG B 291 17440 9731 7214 -452 3730 2580 C
ATOM 4031 O ARG B 291 -28.100 41.277 56.923 1.00 88.25 O
ANISOU 4031 O ARG B 291 17151 9565 6813 -339 3493 2440 O
ATOM 4032 CB ARG B 291 -27.732 43.863 54.978 1.00100.05 C
ANISOU 4032 CB ARG B 291 19140 10909 7964 -484 3767 3173 C
ATOM 4033 CG ARG B 291 -28.548 45.089 54.525 1.00103.82 C
ANISOU 4033 CG ARG B 291 19805 11264 8379 -435 3621 3579 C
ATOM 4034 CD ARG B 291 -29.138 44.975 53.120 1.00113.80 C
ANISOU 4034 CD ARG B 291 21334 12763 9143 -407 3463 3855 C
ATOM 4035 NE ARG B 291 -30.144 46.021 52.920 1.00120.01 N
ANISOU 4035 NE ARG B 291 22209 13440 9949 -318 3231 4279 N
ATOM 4036 CZ ARG B 291 -30.790 46.254 51.782 1.00130.63 C
ANISOU 4036 CZ ARG B 291 23751 14977 10906 -300 3039 4660 C
ATOM 4037 NH1 ARG B 291 -30.552 45.507 50.713 1.00136.14 N
ANISOU 4037 NH1 ARG B 291 24618 15997 11110 -383 3064 4627 N
ATOM 4038 NH2 ARG B 291 -31.700 47.219 51.721 1.00134.46 N
ANISOU 4038 NH2 ARG B 291 24254 15335 11498 -203 2820 5089 N
ATOM 4039 N ALA B 292 -26.039 42.159 57.244 1.00 90.37 N
ANISOU 4039 N ALA B 292 17238 9714 7385 -586 4038 2474 N
ATOM 4040 CA ALA B 292 -25.422 40.924 57.740 1.00 87.48 C
ANISOU 4040 CA ALA B 292 16623 9476 7138 -586 4124 2213 C
ATOM 4041 C ALA B 292 -25.870 40.603 59.167 1.00 99.90 C
ANISOU 4041 C ALA B 292 17928 11012 9018 -544 3908 2047 C
ATOM 4042 O ALA B 292 -26.103 39.438 59.508 1.00100.80 O
ANISOU 4042 O ALA B 292 17917 11230 9152 -454 3800 1860 O
ATOM 4043 CB ALA B 292 -23.899 41.064 57.691 1.00 89.78 C
ANISOU 4043 CB ALA B 292 16749 9799 7566 -748 4513 2229 C
ATOM 4044 N ARG B 293 -25.950 41.644 60.006 1.00 92.03 N
ANISOU 4044 N ARG B 293 16855 9855 8258 -627 3877 2113 N
ATOM 4045 CA ARG B 293 -26.420 41.541 61.387 1.00 84.57 C
ANISOU 4045 CA ARG B 293 15696 8860 7576 -621 3691 1970 C
ATOM 4046 C ARG B 293 -27.899 41.178 61.452 1.00 82.66 C
ANISOU 4046 C ARG B 293 15573 8596 7239 -421 3356 1934 C
ATOM 4047 O ARG B 293 -28.341 40.536 62.413 1.00 83.11 O
ANISOU 4047 O ARG B 293 15450 8688 7441 -371 3188 1768 O
ATOM 4048 CB ARG B 293 -26.170 42.873 62.100 1.00 77.51 C
ANISOU 4048 CB ARG B 293 14776 7763 6910 -791 3790 2045 C
ATOM 4049 CG ARG B 293 -24.774 43.043 62.682 1.00 78.23 C
ANISOU 4049 CG ARG B 293 14597 7922 7205 -1045 4035 2009 C
ATOM 4050 CD ARG B 293 -24.554 44.486 63.110 1.00 80.51 C
ANISOU 4050 CD ARG B 293 14953 7976 7663 -1248 4166 2092 C
ATOM 4051 NE ARG B 293 -23.471 44.631 64.077 1.00 81.69 N
ANISOU 4051 NE ARG B 293 14790 8207 8041 -1537 4298 2014 N
ATOM 4052 CZ ARG B 293 -23.072 45.797 64.579 1.00 88.97 C
ANISOU 4052 CZ ARG B 293 15727 8947 9129 -1792 4439 2036 C
ATOM 4053 NH1 ARG B 293 -23.662 46.923 64.199 1.00 89.72 N
ANISOU 4053 NH1 ARG B 293 16143 8731 9217 -1761 4501 2140 N
ATOM 4054 NH2 ARG B 293 -22.083 45.837 65.460 1.00 93.89 N
ANISOU 4054 NH2 ARG B 293 16037 9704 9934 -2091 4520 1971 N
ATOM 4055 N ARG B 294 -28.658 41.583 60.427 1.00 81.37 N
ANISOU 4055 N ARG B 294 15692 8398 6827 -318 3252 2118 N
ATOM 4056 CA ARG B 294 -30.075 41.247 60.308 1.00 79.25 C
ANISOU 4056 CA ARG B 294 15520 8154 6437 -139 2916 2141 C
ATOM 4057 C ARG B 294 -30.290 39.769 59.999 1.00 82.17 C
ANISOU 4057 C ARG B 294 15859 8732 6631 -67 2793 1955 C
ATOM 4058 O ARG B 294 -31.275 39.182 60.467 1.00 83.36 O
ANISOU 4058 O ARG B 294 15948 8913 6812 44 2525 1860 O
ATOM 4059 CB ARG B 294 -30.701 42.083 59.192 1.00 80.69 C
ANISOU 4059 CB ARG B 294 15979 8303 6378 -82 2836 2459 C
ATOM 4060 CG ARG B 294 -31.022 43.513 59.522 1.00 82.41 C
ANISOU 4060 CG ARG B 294 16254 8261 6799 -80 2869 2684 C
ATOM 4061 CD ARG B 294 -31.531 44.192 58.274 1.00 90.34 C
ANISOU 4061 CD ARG B 294 17504 9280 7542 -24 2790 3060 C
ATOM 4062 NE ARG B 294 -32.188 45.453 58.571 1.00 93.52 N
ANISOU 4062 NE ARG B 294 17951 9411 8172 45 2754 3325 N
ATOM 4063 CZ ARG B 294 -32.883 46.146 57.678 1.00 98.74 C
ANISOU 4063 CZ ARG B 294 18771 10052 8694 129 2619 3731 C
ATOM 4064 NH1 ARG B 294 -32.980 45.708 56.430 1.00104.73 N
ANISOU 4064 NH1 ARG B 294 19676 11087 9030 122 2500 3903 N
ATOM 4065 NH2 ARG B 294 -33.486 47.270 58.033 1.00100.01 N
ANISOU 4065 NH2 ARG B 294 18941 9918 9139 213 2608 3977 N
ATOM 4066 N LYS B 295 -29.404 39.156 59.205 1.00 84.24 N
ANISOU 4066 N LYS B 295 16174 9118 6714 -131 3007 1900 N
ATOM 4067 CA LYS B 295 -29.539 37.736 58.906 1.00 84.24 C
ANISOU 4067 CA LYS B 295 16172 9267 6567 -78 2954 1701 C
ATOM 4068 C LYS B 295 -29.108 36.857 60.078 1.00 80.67 C
ANISOU 4068 C LYS B 295 15405 8820 6426 -69 2999 1480 C
ATOM 4069 O LYS B 295 -29.634 35.753 60.230 1.00 85.09 O
ANISOU 4069 O LYS B 295 15929 9443 6959 11 2857 1319 O
ATOM 4070 CB LYS B 295 -28.765 37.345 57.631 1.00 94.66 C
ANISOU 4070 CB LYS B 295 17688 10694 7585 -146 3215 1705 C
ATOM 4071 CG LYS B 295 -29.268 36.005 57.027 1.00102.33 C
ANISOU 4071 CG LYS B 295 18789 11796 8295 -101 3119 1520 C
ATOM 4072 CD LYS B 295 -28.527 35.523 55.769 1.00110.34 C
ANISOU 4072 CD LYS B 295 20034 12903 8987 -182 3420 1475 C
ATOM 4073 CE LYS B 295 -28.705 34.011 55.525 1.00109.23 C
ANISOU 4073 CE LYS B 295 19952 12825 8727 -160 3442 1202 C
ATOM 4074 NZ LYS B 295 -30.115 33.611 55.219 1.00108.61 N
ANISOU 4074 NZ LYS B 295 20031 12855 8381 -137 3043 1166 N
ATOM 4075 N THR B 296 -28.235 37.378 60.951 1.00 75.49 N
ANISOU 4075 N THR B 296 14516 8108 6060 -166 3167 1494 N
ATOM 4076 CA THR B 296 -27.804 36.654 62.149 1.00 72.04 C
ANISOU 4076 CA THR B 296 13740 7722 5910 -183 3186 1348 C
ATOM 4077 C THR B 296 -28.828 36.840 63.261 1.00 74.74 C
ANISOU 4077 C THR B 296 13986 8000 6411 -134 2896 1300 C
ATOM 4078 O THR B 296 -29.134 35.893 63.994 1.00 80.01 O
ANISOU 4078 O THR B 296 14478 8731 7191 -74 2773 1166 O
ATOM 4079 CB THR B 296 -26.432 37.168 62.624 1.00 68.90 C
ANISOU 4079 CB THR B 296 13105 7349 5723 -356 3462 1414 C
ATOM 4080 OG1 THR B 296 -25.494 37.170 61.541 1.00 74.54 O
ANISOU 4080 OG1 THR B 296 13922 8102 6296 -402 3763 1485 O
ATOM 4081 CG2 THR B 296 -25.856 36.345 63.811 1.00 66.02 C
ANISOU 4081 CG2 THR B 296 12344 7113 5629 -395 3483 1322 C
ATOM 4082 N ALA B 297 -29.397 38.049 63.357 1.00 75.46 N
ANISOU 4082 N ALA B 297 14210 7949 6513 -151 2809 1418 N
ATOM 4083 CA ALA B 297 -30.426 38.334 64.356 1.00 73.38 C
ANISOU 4083 CA ALA B 297 13896 7590 6397 -96 2581 1377 C
ATOM 4084 C ALA B 297 -31.685 37.512 64.108 1.00 74.17 C
ANISOU 4084 C ALA B 297 14075 7741 6367 85 2295 1322 C
ATOM 4085 O ALA B 297 -32.263 36.954 65.051 1.00 73.63 O
ANISOU 4085 O ALA B 297 13851 7686 6437 136 2135 1200 O
ATOM 4086 CB ALA B 297 -30.754 39.829 64.356 1.00 76.71 C
ANISOU 4086 CB ALA B 297 14480 7804 6862 -131 2615 1537 C
ATOM 4087 N LYS B 298 -32.122 37.436 62.844 1.00 78.75 N
ANISOU 4087 N LYS B 298 14894 8368 6661 156 2221 1423 N
ATOM 4088 CA LYS B 298 -33.282 36.628 62.469 1.00 79.26 C
ANISOU 4088 CA LYS B 298 15036 8521 6557 280 1935 1383 C
ATOM 4089 C LYS B 298 -33.096 35.178 62.900 1.00 77.74 C
ANISOU 4089 C LYS B 298 14685 8425 6428 293 1930 1149 C
ATOM 4090 O LYS B 298 -33.991 34.584 63.519 1.00 84.09 O
ANISOU 4090 O LYS B 298 15396 9242 7312 373 1705 1056 O
ATOM 4091 CB LYS B 298 -33.498 36.723 60.945 1.00 87.82 C
ANISOU 4091 CB LYS B 298 16400 9704 7264 279 1896 1532 C
ATOM 4092 CG LYS B 298 -34.782 36.079 60.391 1.00 95.89 C
ANISOU 4092 CG LYS B 298 17526 10860 8048 357 1557 1544 C
ATOM 4093 CD LYS B 298 -34.856 36.193 58.860 1.00106.31 C
ANISOU 4093 CD LYS B 298 19123 12333 8936 299 1532 1705 C
ATOM 4094 CE LYS B 298 -36.099 35.519 58.287 1.00108.20 C
ANISOU 4094 CE LYS B 298 19447 12763 8900 324 1172 1718 C
ATOM 4095 NZ LYS B 298 -36.181 35.668 56.804 1.00111.13 N
ANISOU 4095 NZ LYS B 298 20089 13337 8798 232 1129 1893 N
ATOM 4096 N MET B 299 -31.919 34.614 62.616 1.00 72.44 N
ANISOU 4096 N MET B 299 13968 7808 5749 221 2201 1073 N
ATOM 4097 CA MET B 299 -31.632 33.223 62.945 1.00 71.17 C
ANISOU 4097 CA MET B 299 13664 7711 5667 247 2260 890 C
ATOM 4098 C MET B 299 -31.629 32.985 64.461 1.00 74.60 C
ANISOU 4098 C MET B 299 13782 8136 6425 256 2198 825 C
ATOM 4099 O MET B 299 -32.224 32.012 64.940 1.00 85.04 O
ANISOU 4099 O MET B 299 15019 9484 7808 330 2055 711 O
ATOM 4100 CB MET B 299 -30.277 32.830 62.339 1.00 71.80 C
ANISOU 4100 CB MET B 299 13744 7828 5710 183 2626 870 C
ATOM 4101 CG MET B 299 -29.960 31.356 62.479 1.00 73.68 C
ANISOU 4101 CG MET B 299 13881 8095 6019 235 2752 706 C
ATOM 4102 SD MET B 299 -28.287 30.953 61.957 1.00 79.44 S
ANISOU 4102 SD MET B 299 14544 8839 6801 189 3248 710 S
ATOM 4103 CE MET B 299 -27.371 31.709 63.302 1.00 83.02 C
ANISOU 4103 CE MET B 299 14579 9347 7618 108 3318 847 C
ATOM 4104 N LEU B 300 -30.961 33.864 65.225 1.00 67.07 N
ANISOU 4104 N LEU B 300 12662 7160 5662 155 2307 899 N
ATOM 4105 CA LEU B 300 -30.861 33.731 66.684 1.00 54.77 C
ANISOU 4105 CA LEU B 300 10805 5640 4365 105 2256 853 C
ATOM 4106 C LEU B 300 -32.232 33.847 67.349 1.00 56.36 C
ANISOU 4106 C LEU B 300 11034 5772 4607 187 1968 807 C
ATOM 4107 O LEU B 300 -32.501 33.182 68.357 1.00 62.45 O
ANISOU 4107 O LEU B 300 11607 6600 5523 200 1870 727 O
ATOM 4108 CB LEU B 300 -29.915 34.805 67.227 1.00 53.55 C
ANISOU 4108 CB LEU B 300 10522 5483 4342 -80 2422 943 C
ATOM 4109 CG LEU B 300 -28.425 34.644 66.903 1.00 63.42 C
ANISOU 4109 CG LEU B 300 11624 6845 5630 -187 2717 1008 C
ATOM 4110 CD1 LEU B 300 -27.626 35.853 67.373 1.00 64.59 C
ANISOU 4110 CD1 LEU B 300 11672 6984 5885 -410 2845 1107 C
ATOM 4111 CD2 LEU B 300 -27.846 33.368 67.507 1.00 69.38 C
ANISOU 4111 CD2 LEU B 300 12071 7763 6526 -162 2786 971 C
ATOM 4112 N MET B 301 -33.087 34.738 66.832 1.00 59.23 N
ANISOU 4112 N MET B 301 11629 6021 4856 242 1848 887 N
ATOM 4113 CA MET B 301 -34.444 34.887 67.357 1.00 65.81 C
ANISOU 4113 CA MET B 301 12490 6783 5732 347 1598 874 C
ATOM 4114 C MET B 301 -35.267 33.614 67.164 1.00 67.48 C
ANISOU 4114 C MET B 301 12691 7081 5867 465 1389 777 C
ATOM 4115 O MET B 301 -36.090 33.277 68.022 1.00 66.02 O
ANISOU 4115 O MET B 301 12397 6889 5800 524 1221 713 O
ATOM 4116 CB MET B 301 -35.125 36.098 66.708 1.00 71.29 C
ANISOU 4116 CB MET B 301 13413 7348 6325 404 1538 1045 C
ATOM 4117 CG MET B 301 -34.514 37.452 67.087 1.00 77.08 C
ANISOU 4117 CG MET B 301 14178 7928 7180 285 1751 1131 C
ATOM 4118 SD MET B 301 -35.231 38.826 66.159 1.00 84.89 S
ANISOU 4118 SD MET B 301 15432 8747 8074 379 1721 1402 S
ATOM 4119 CE MET B 301 -34.098 40.155 66.572 1.00 88.19 C
ANISOU 4119 CE MET B 301 15882 8979 8647 176 2064 1441 C
ATOM 4120 N VAL B 302 -35.034 32.889 66.063 1.00 70.55 N
ANISOU 4120 N VAL B 302 13209 7545 6054 479 1420 753 N
ATOM 4121 CA VAL B 302 -35.730 31.625 65.809 1.00 69.30 C
ANISOU 4121 CA VAL B 302 13074 7453 5802 547 1257 636 C
ATOM 4122 C VAL B 302 -35.204 30.529 66.747 1.00 68.94 C
ANISOU 4122 C VAL B 302 12792 7441 5962 542 1361 508 C
ATOM 4123 O VAL B 302 -35.978 29.723 67.274 1.00 69.97 O
ANISOU 4123 O VAL B 302 12845 7584 6157 602 1192 422 O
ATOM 4124 CB VAL B 302 -35.627 31.253 64.313 1.00 67.75 C
ANISOU 4124 CB VAL B 302 13136 7321 5286 519 1293 635 C
ATOM 4125 CG1 VAL B 302 -36.111 29.826 64.034 1.00 69.01 C
ANISOU 4125 CG1 VAL B 302 13340 7539 5342 532 1200 467 C
ATOM 4126 CG2 VAL B 302 -36.387 32.255 63.444 1.00 67.90 C
ANISOU 4126 CG2 VAL B 302 13362 7360 5078 531 1112 815 C
ATOM 4127 N VAL B 303 -33.878 30.499 66.986 1.00 65.01 N
ANISOU 4127 N VAL B 303 12157 6971 5574 469 1641 523 N
ATOM 4128 CA VAL B 303 -33.271 29.532 67.913 1.00 56.78 C
ANISOU 4128 CA VAL B 303 10850 5990 4732 470 1759 471 C
ATOM 4129 C VAL B 303 -33.812 29.724 69.337 1.00 59.47 C
ANISOU 4129 C VAL B 303 10974 6359 5264 455 1588 473 C
ATOM 4130 O VAL B 303 -34.155 28.750 70.019 1.00 66.77 O
ANISOU 4130 O VAL B 303 11763 7320 6284 511 1520 415 O
ATOM 4131 CB VAL B 303 -31.726 29.626 67.859 1.00 47.65 C
ANISOU 4131 CB VAL B 303 9554 4894 3655 389 2087 543 C
ATOM 4132 CG1 VAL B 303 -31.057 28.800 68.964 1.00 43.58 C
ANISOU 4132 CG1 VAL B 303 8700 4485 3372 387 2203 567 C
ATOM 4133 CG2 VAL B 303 -31.194 29.169 66.498 1.00 50.95 C
ANISOU 4133 CG2 VAL B 303 10190 5275 3896 417 2310 510 C
ATOM 4134 N VAL B 304 -33.921 30.982 69.793 1.00 57.26 N
ANISOU 4134 N VAL B 304 10685 6043 5029 373 1542 536 N
ATOM 4135 CA VAL B 304 -34.444 31.278 71.131 1.00 53.88 C
ANISOU 4135 CA VAL B 304 10098 5623 4750 325 1419 519 C
ATOM 4136 C VAL B 304 -35.945 30.965 71.220 1.00 59.28 C
ANISOU 4136 C VAL B 304 10877 6236 5410 465 1165 459 C
ATOM 4137 O VAL B 304 -36.417 30.443 72.236 1.00 59.82 O
ANISOU 4137 O VAL B 304 10789 6348 5591 474 1068 410 O
ATOM 4138 CB VAL B 304 -34.124 32.741 71.521 1.00 49.37 C
ANISOU 4138 CB VAL B 304 9560 4981 4217 176 1503 577 C
ATOM 4139 CG1 VAL B 304 -34.830 33.163 72.820 1.00 47.74 C
ANISOU 4139 CG1 VAL B 304 9287 4732 4122 111 1408 529 C
ATOM 4140 CG2 VAL B 304 -32.612 32.938 71.672 1.00 52.10 C
ANISOU 4140 CG2 VAL B 304 9734 5449 4613 -6 1727 641 C
ATOM 4141 N LEU B 305 -36.709 31.249 70.150 1.00 62.48 N
ANISOU 4141 N LEU B 305 11524 6562 5654 566 1046 483 N
ATOM 4142 CA LEU B 305 -38.144 30.942 70.142 1.00 60.42 C
ANISOU 4142 CA LEU B 305 11323 6273 5360 691 778 456 C
ATOM 4143 C LEU B 305 -38.404 29.430 70.195 1.00 59.04 C
ANISOU 4143 C LEU B 305 11074 6173 5185 736 692 345 C
ATOM 4144 O LEU B 305 -39.264 28.975 70.955 1.00 53.79 O
ANISOU 4144 O LEU B 305 10309 5513 4615 790 531 297 O
ATOM 4145 CB LEU B 305 -38.820 31.569 68.912 1.00 61.89 C
ANISOU 4145 CB LEU B 305 11748 6424 5345 759 646 560 C
ATOM 4146 CG LEU B 305 -40.289 31.209 68.611 1.00 64.57 C
ANISOU 4146 CG LEU B 305 12130 6794 5610 869 323 579 C
ATOM 4147 CD1 LEU B 305 -41.252 31.702 69.689 1.00 58.75 C
ANISOU 4147 CD1 LEU B 305 11264 5985 5075 952 204 618 C
ATOM 4148 CD2 LEU B 305 -40.723 31.733 67.248 1.00 72.51 C
ANISOU 4148 CD2 LEU B 305 13339 7840 6372 889 189 733 C
ATOM 4149 N VAL B 306 -37.656 28.645 69.402 1.00 60.40 N
ANISOU 4149 N VAL B 306 11313 6383 5255 713 832 302 N
ATOM 4150 CA VAL B 306 -37.812 27.187 69.390 1.00 54.57 C
ANISOU 4150 CA VAL B 306 10549 5670 4515 748 821 187 C
ATOM 4151 C VAL B 306 -37.360 26.573 70.730 1.00 57.33 C
ANISOU 4151 C VAL B 306 10629 6062 5094 751 924 180 C
ATOM 4152 O VAL B 306 -37.989 25.635 71.230 1.00 59.21 O
ANISOU 4152 O VAL B 306 10803 6302 5392 804 821 109 O
ATOM 4153 CB VAL B 306 -37.079 26.585 68.164 1.00 47.66 C
ANISOU 4153 CB VAL B 306 9855 4790 3462 716 1018 133 C
ATOM 4154 CG1 VAL B 306 -37.010 25.053 68.209 1.00 45.13 C
ANISOU 4154 CG1 VAL B 306 9517 4451 3179 742 1118 -3 C
ATOM 4155 CG2 VAL B 306 -37.770 27.014 66.856 1.00 47.48 C
ANISOU 4155 CG2 VAL B 306 10108 4783 3149 687 850 139 C
ATOM 4156 N PHE B 307 -36.300 27.121 71.348 1.00 57.74 N
ANISOU 4156 N PHE B 307 10508 6169 5260 673 1112 266 N
ATOM 4157 CA PHE B 307 -35.889 26.696 72.694 1.00 56.40 C
ANISOU 4157 CA PHE B 307 10054 6105 5273 636 1175 308 C
ATOM 4158 C PHE B 307 -36.996 26.962 73.723 1.00 58.61 C
ANISOU 4158 C PHE B 307 10255 6390 5624 631 944 285 C
ATOM 4159 O PHE B 307 -37.343 26.080 74.518 1.00 56.17 O
ANISOU 4159 O PHE B 307 9815 6131 5396 669 895 270 O
ATOM 4160 CB PHE B 307 -34.578 27.401 73.092 1.00 52.13 C
ANISOU 4160 CB PHE B 307 9330 5673 4803 492 1370 424 C
ATOM 4161 CG PHE B 307 -33.970 26.937 74.413 1.00 49.28 C
ANISOU 4161 CG PHE B 307 8632 5494 4599 407 1432 531 C
ATOM 4162 CD1 PHE B 307 -34.378 27.504 75.613 1.00 46.23 C
ANISOU 4162 CD1 PHE B 307 8110 5195 4262 269 1283 545 C
ATOM 4163 CD2 PHE B 307 -32.969 25.972 74.449 1.00 49.77 C
ANISOU 4163 CD2 PHE B 307 8505 5641 4764 456 1664 648 C
ATOM 4164 CE1 PHE B 307 -33.823 27.103 76.823 1.00 52.64 C
ANISOU 4164 CE1 PHE B 307 8606 6221 5173 141 1306 677 C
ATOM 4165 CE2 PHE B 307 -32.409 25.568 75.661 1.00 55.36 C
ANISOU 4165 CE2 PHE B 307 8850 6552 5633 370 1694 830 C
ATOM 4166 CZ PHE B 307 -32.840 26.135 76.846 1.00 57.87 C
ANISOU 4166 CZ PHE B 307 9041 7001 5946 191 1486 848 C
ATOM 4167 N ALA B 308 -37.558 28.176 73.714 1.00 55.64 N
ANISOU 4167 N ALA B 308 9977 5942 5222 596 841 292 N
ATOM 4168 CA ALA B 308 -38.670 28.507 74.604 1.00 53.68 C
ANISOU 4168 CA ALA B 308 9701 5657 5039 613 677 267 C
ATOM 4169 C ALA B 308 -39.851 27.543 74.422 1.00 56.65 C
ANISOU 4169 C ALA B 308 10123 6004 5396 760 466 201 C
ATOM 4170 O ALA B 308 -40.435 27.081 75.407 1.00 55.05 O
ANISOU 4170 O ALA B 308 9793 5838 5284 772 382 177 O
ATOM 4171 CB ALA B 308 -39.113 29.954 74.372 1.00 46.95 C
ANISOU 4171 CB ALA B 308 9025 4666 4146 608 666 304 C
ATOM 4172 N LEU B 309 -40.196 27.223 73.165 1.00 58.32 N
ANISOU 4172 N LEU B 309 10520 6168 5469 840 373 169 N
ATOM 4173 CA LEU B 309 -41.320 26.328 72.874 1.00 57.47 C
ANISOU 4173 CA LEU B 309 10470 6052 5315 928 139 90 C
ATOM 4174 C LEU B 309 -41.038 24.887 73.311 1.00 52.88 C
ANISOU 4174 C LEU B 309 9785 5510 4798 932 214 -1 C
ATOM 4175 O LEU B 309 -41.898 24.235 73.913 1.00 49.92 O
ANISOU 4175 O LEU B 309 9315 5137 4515 970 57 -73 O
ATOM 4176 CB LEU B 309 -41.659 26.382 71.377 1.00 64.74 C
ANISOU 4176 CB LEU B 309 11621 6956 6021 939 23 80 C
ATOM 4177 CG LEU B 309 -42.350 27.648 70.853 1.00 68.26 C
ANISOU 4177 CG LEU B 309 12170 7376 6391 980 -132 202 C
ATOM 4178 CD1 LEU B 309 -42.126 27.821 69.360 1.00 70.78 C
ANISOU 4178 CD1 LEU B 309 12709 7727 6455 936 -142 237 C
ATOM 4179 CD2 LEU B 309 -43.844 27.628 71.158 1.00 68.27 C
ANISOU 4179 CD2 LEU B 309 12094 7384 6460 1068 -450 232 C
ATOM 4180 N CYS B 310 -39.832 24.377 73.004 1.00 53.13 N
ANISOU 4180 N CYS B 310 9813 5553 4820 902 478 1 N
ATOM 4181 CA CYS B 310 -39.458 22.989 73.304 1.00 49.56 C
ANISOU 4181 CA CYS B 310 9283 5088 4461 945 634 -78 C
ATOM 4182 C CYS B 310 -39.408 22.697 74.804 1.00 54.78 C
ANISOU 4182 C CYS B 310 9579 5826 5406 930 630 10 C
ATOM 4183 O CYS B 310 -39.720 21.580 75.233 1.00 62.92 O
ANISOU 4183 O CYS B 310 10445 6820 6643 965 612 -34 O
ATOM 4184 CB CYS B 310 -38.096 22.671 72.683 1.00 49.17 C
ANISOU 4184 CB CYS B 310 9268 5019 4393 942 976 -43 C
ATOM 4185 SG CYS B 310 -38.131 22.326 70.918 1.00 57.77 S
ANISOU 4185 SG CYS B 310 10659 6018 5272 901 1011 -175 S
ATOM 4186 N TYR B 311 -38.959 23.666 75.605 1.00 48.13 N
ANISOU 4186 N TYR B 311 8600 5096 4591 842 660 145 N
ATOM 4187 CA TYR B 311 -38.788 23.508 77.047 1.00 44.92 C
ANISOU 4187 CA TYR B 311 7847 4825 4396 758 651 253 C
ATOM 4188 C TYR B 311 -39.981 24.010 77.852 1.00 55.11 C
ANISOU 4188 C TYR B 311 9084 6119 5737 716 437 201 C
ATOM 4189 O TYR B 311 -39.993 23.855 79.080 1.00 58.00 O
ANISOU 4189 O TYR B 311 9198 6606 6231 621 423 266 O
ATOM 4190 CB TYR B 311 -37.498 24.209 77.504 1.00 40.39 C
ANISOU 4190 CB TYR B 311 7146 4405 3794 614 827 414 C
ATOM 4191 CG TYR B 311 -36.234 23.462 77.107 1.00 44.44 C
ANISOU 4191 CG TYR B 311 7538 4956 4390 665 1076 535 C
ATOM 4192 CD1 TYR B 311 -35.745 23.542 75.809 1.00 46.44 C
ANISOU 4192 CD1 TYR B 311 8051 5093 4501 743 1260 480 C
ATOM 4193 CD2 TYR B 311 -35.531 22.683 78.022 1.00 50.90 C
ANISOU 4193 CD2 TYR B 311 7974 5926 5439 641 1146 732 C
ATOM 4194 CE1 TYR B 311 -34.601 22.862 75.426 1.00 50.56 C
ANISOU 4194 CE1 TYR B 311 8455 5617 5138 809 1555 584 C
ATOM 4195 CE2 TYR B 311 -34.378 22.000 77.646 1.00 54.11 C
ANISOU 4195 CE2 TYR B 311 8223 6341 5994 728 1410 885 C
ATOM 4196 CZ TYR B 311 -33.920 22.096 76.347 1.00 56.55 C
ANISOU 4196 CZ TYR B 311 8796 6501 6190 818 1637 793 C
ATOM 4197 OH TYR B 311 -32.780 21.423 75.967 1.00 69.51 O
ANISOU 4197 OH TYR B 311 10272 8121 8017 922 1964 937 O
ATOM 4198 N LEU B 312 -40.995 24.628 77.201 1.00 60.63 N
ANISOU 4198 N LEU B 312 10001 6697 6339 785 281 108 N
ATOM 4199 CA LEU B 312 -42.163 25.088 77.941 1.00 57.08 C
ANISOU 4199 CA LEU B 312 9466 6221 6002 781 128 74 C
ATOM 4200 C LEU B 312 -42.976 23.923 78.519 1.00 55.39 C
ANISOU 4200 C LEU B 312 9036 6020 5988 815 9 24 C
ATOM 4201 O LEU B 312 -43.250 23.936 79.719 1.00 59.86 O
ANISOU 4201 O LEU B 312 9399 6661 6685 736 22 48 O
ATOM 4202 CB LEU B 312 -43.040 26.010 77.085 1.00 53.74 C
ANISOU 4202 CB LEU B 312 9265 5664 5488 880 -10 60 C
ATOM 4203 CG LEU B 312 -44.270 26.621 77.797 1.00 53.26 C
ANISOU 4203 CG LEU B 312 9093 5535 5608 916 -111 51 C
ATOM 4204 CD1 LEU B 312 -43.895 27.689 78.827 1.00 52.87 C
ANISOU 4204 CD1 LEU B 312 9016 5473 5600 785 92 60 C
ATOM 4205 CD2 LEU B 312 -45.281 27.188 76.811 1.00 53.36 C
ANISOU 4205 CD2 LEU B 312 9247 5431 5597 1068 -308 104 C
ATOM 4206 N PRO B 313 -43.365 22.905 77.727 1.00 52.90 N
ANISOU 4206 N PRO B 313 8778 5633 5689 897 -88 -54 N
ATOM 4207 CA PRO B 313 -44.190 21.829 78.326 1.00 52.52 C
ANISOU 4207 CA PRO B 313 8521 5569 5864 901 -186 -100 C
ATOM 4208 C PRO B 313 -43.571 21.177 79.550 1.00 54.96 C
ANISOU 4208 C PRO B 313 8564 5978 6339 834 -41 12 C
ATOM 4209 O PRO B 313 -44.245 21.063 80.585 1.00 55.31 O
ANISOU 4209 O PRO B 313 8413 6075 6529 785 -91 38 O
ATOM 4210 CB PRO B 313 -44.358 20.836 77.161 1.00 51.95 C
ANISOU 4210 CB PRO B 313 8612 5387 5739 943 -243 -228 C
ATOM 4211 CG PRO B 313 -44.238 21.664 75.944 1.00 53.12 C
ANISOU 4211 CG PRO B 313 9066 5518 5601 969 -298 -258 C
ATOM 4212 CD PRO B 313 -43.182 22.697 76.281 1.00 52.65 C
ANISOU 4212 CD PRO B 313 9024 5525 5456 951 -107 -128 C
ATOM 4213 N ILE B 314 -42.287 20.763 79.498 1.00 53.96 N
ANISOU 4213 N ILE B 314 8404 5900 6200 827 149 115 N
ATOM 4214 CA ILE B 314 -41.688 20.067 80.626 1.00 51.22 C
ANISOU 4214 CA ILE B 314 7763 5677 6022 774 251 299 C
ATOM 4215 C ILE B 314 -41.500 21.012 81.823 1.00 50.22 C
ANISOU 4215 C ILE B 314 7502 5766 5811 605 242 403 C
ATOM 4216 O ILE B 314 -41.748 20.619 82.973 1.00 49.81 O
ANISOU 4216 O ILE B 314 7233 5836 5857 519 219 504 O
ATOM 4217 CB ILE B 314 -40.360 19.366 80.227 1.00 51.74 C
ANISOU 4217 CB ILE B 314 7772 5732 6154 838 469 433 C
ATOM 4218 CG1 ILE B 314 -39.885 18.385 81.313 1.00 56.89 C
ANISOU 4218 CG1 ILE B 314 8078 6487 7052 829 546 688 C
ATOM 4219 CG2 ILE B 314 -39.259 20.333 79.822 1.00 43.65 C
ANISOU 4219 CG2 ILE B 314 6834 4809 4943 789 586 496 C
ATOM 4220 CD1 ILE B 314 -40.898 17.326 81.668 1.00 58.17 C
ANISOU 4220 CD1 ILE B 314 8159 6512 7433 875 478 646 C
ATOM 4221 N SER B 315 -41.103 22.275 81.582 1.00 49.81 N
ANISOU 4221 N SER B 315 7607 5756 5564 528 275 366 N
ATOM 4222 CA SER B 315 -40.901 23.223 82.665 1.00 53.13 C
ANISOU 4222 CA SER B 315 7959 6351 5878 314 303 405 C
ATOM 4223 C SER B 315 -42.189 23.482 83.435 1.00 54.78 C
ANISOU 4223 C SER B 315 8148 6523 6142 278 229 293 C
ATOM 4224 O SER B 315 -42.211 23.451 84.677 1.00 56.67 O
ANISOU 4224 O SER B 315 8230 6937 6364 102 255 351 O
ATOM 4225 CB SER B 315 -40.376 24.552 82.093 1.00 56.52 C
ANISOU 4225 CB SER B 315 8613 6741 6122 245 381 347 C
ATOM 4226 OG SER B 315 -39.200 24.324 81.345 1.00 56.73 O
ANISOU 4226 OG SER B 315 8649 6800 6107 279 483 451 O
ATOM 4227 N VAL B 316 -43.288 23.715 82.702 1.00 51.86 N
ANISOU 4227 N VAL B 316 7924 5943 5838 437 139 151 N
ATOM 4228 CA VAL B 316 -44.612 23.912 83.307 1.00 53.08 C
ANISOU 4228 CA VAL B 316 8019 6031 6119 450 92 61 C
ATOM 4229 C VAL B 316 -45.058 22.641 84.028 1.00 52.98 C
ANISOU 4229 C VAL B 316 7769 6089 6273 441 47 120 C
ATOM 4230 O VAL B 316 -45.495 22.695 85.185 1.00 58.71 O
ANISOU 4230 O VAL B 316 8367 6909 7031 319 107 128 O
ATOM 4231 CB VAL B 316 -45.628 24.361 82.231 1.00 52.52 C
ANISOU 4231 CB VAL B 316 8093 5748 6113 639 -34 -31 C
ATOM 4232 CG1 VAL B 316 -47.069 24.367 82.768 1.00 46.25 C
ANISOU 4232 CG1 VAL B 316 7157 4881 5534 693 -87 -86 C
ATOM 4233 CG2 VAL B 316 -45.283 25.755 81.693 1.00 53.14 C
ANISOU 4233 CG2 VAL B 316 8405 5734 6053 645 44 -45 C
ATOM 4234 N LEU B 317 -44.916 21.474 83.380 1.00 51.58 N
ANISOU 4234 N LEU B 317 7549 5852 6198 552 -22 161 N
ATOM 4235 CA LEU B 317 -45.345 20.216 83.997 1.00 56.49 C
ANISOU 4235 CA LEU B 317 7958 6485 7020 549 -40 232 C
ATOM 4236 C LEU B 317 -44.615 19.947 85.314 1.00 58.87 C
ANISOU 4236 C LEU B 317 8063 7020 7285 388 63 436 C
ATOM 4237 O LEU B 317 -45.209 19.416 86.257 1.00 60.49 O
ANISOU 4237 O LEU B 317 8101 7285 7595 321 69 502 O
ATOM 4238 CB LEU B 317 -45.158 19.036 83.030 1.00 55.81 C
ANISOU 4238 CB LEU B 317 7905 6245 7056 673 -67 220 C
ATOM 4239 CG LEU B 317 -46.189 18.802 81.910 1.00 53.22 C
ANISOU 4239 CG LEU B 317 7714 5722 6784 765 -226 24 C
ATOM 4240 CD1 LEU B 317 -45.858 17.552 81.103 1.00 55.21 C
ANISOU 4240 CD1 LEU B 317 8034 5816 7126 817 -182 -24 C
ATOM 4241 CD2 LEU B 317 -47.616 18.716 82.444 1.00 54.40 C
ANISOU 4241 CD2 LEU B 317 7712 5847 7112 741 -344 -31 C
ATOM 4242 N ASN B 318 -43.325 20.317 85.420 1.00 58.07 N
ANISOU 4242 N ASN B 318 7961 7081 7021 300 134 565 N
ATOM 4243 CA ASN B 318 -42.626 20.038 86.664 1.00 57.70 C
ANISOU 4243 CA ASN B 318 7696 7318 6911 115 176 807 C
ATOM 4244 C ASN B 318 -42.944 21.054 87.753 1.00 57.03 C
ANISOU 4244 C ASN B 318 7645 7414 6610 -138 207 731 C
ATOM 4245 O ASN B 318 -42.912 20.714 88.942 1.00 62.68 O
ANISOU 4245 O ASN B 318 8199 8360 7258 -319 216 886 O
ATOM 4246 CB ASN B 318 -41.107 19.935 86.424 1.00 63.85 C
ANISOU 4246 CB ASN B 318 8386 8242 7634 94 224 1022 C
ATOM 4247 CG ASN B 318 -40.684 18.506 86.093 1.00 75.78 C
ANISOU 4247 CG ASN B 318 9721 9653 9419 285 272 1232 C
ATOM 4248 OD1 ASN B 318 -40.177 17.765 86.939 1.00 89.76 O
ANISOU 4248 OD1 ASN B 318 11221 11602 11281 236 282 1547 O
ATOM 4249 ND2 ASN B 318 -40.944 18.104 84.857 1.00 73.25 N
ANISOU 4249 ND2 ASN B 318 9568 9033 9232 495 313 1059 N
ATOM 4250 N VAL B 319 -43.292 22.300 87.388 1.00 51.15 N
ANISOU 4250 N VAL B 319 7127 6555 5753 -163 249 496 N
ATOM 4251 CA VAL B 319 -43.781 23.266 88.369 1.00 49.38 C
ANISOU 4251 CA VAL B 319 6982 6406 5373 -385 354 356 C
ATOM 4252 C VAL B 319 -45.152 22.834 88.895 1.00 53.60 C
ANISOU 4252 C VAL B 319 7438 6846 6081 -320 377 283 C
ATOM 4253 O VAL B 319 -45.384 22.798 90.113 1.00 61.92 O
ANISOU 4253 O VAL B 319 8420 8079 7025 -534 466 308 O
ATOM 4254 CB VAL B 319 -43.803 24.683 87.762 1.00 46.33 C
ANISOU 4254 CB VAL B 319 6860 5843 4901 -387 444 146 C
ATOM 4255 CG1 VAL B 319 -44.718 25.632 88.538 1.00 41.57 C
ANISOU 4255 CG1 VAL B 319 6373 5152 4269 -512 619 -63 C
ATOM 4256 CG2 VAL B 319 -42.387 25.261 87.707 1.00 47.38 C
ANISOU 4256 CG2 VAL B 319 7048 6147 4806 -591 474 218 C
ATOM 4257 N LEU B 320 -46.064 22.454 87.991 1.00 54.25 N
ANISOU 4257 N LEU B 320 7521 6671 6419 -53 294 206 N
ATOM 4258 CA LEU B 320 -47.386 21.983 88.399 1.00 58.46 C
ANISOU 4258 CA LEU B 320 7931 7113 7170 11 305 156 C
ATOM 4259 C LEU B 320 -47.278 20.766 89.321 1.00 59.69 C
ANISOU 4259 C LEU B 320 7872 7445 7361 -92 303 357 C
ATOM 4260 O LEU B 320 -47.991 20.678 90.329 1.00 64.22 O
ANISOU 4260 O LEU B 320 8359 8090 7951 -209 411 352 O
ATOM 4261 CB LEU B 320 -48.230 21.657 87.158 1.00 61.29 C
ANISOU 4261 CB LEU B 320 8293 7217 7776 273 152 77 C
ATOM 4262 CG LEU B 320 -48.579 22.821 86.214 1.00 63.73 C
ANISOU 4262 CG LEU B 320 8782 7346 8085 407 124 -58 C
ATOM 4263 CD1 LEU B 320 -49.423 22.342 85.042 1.00 65.20 C
ANISOU 4263 CD1 LEU B 320 8940 7366 8468 612 -91 -88 C
ATOM 4264 CD2 LEU B 320 -49.287 23.955 86.947 1.00 63.69 C
ANISOU 4264 CD2 LEU B 320 8807 7281 8110 355 320 -169 C
ATOM 4265 N LYS B 321 -46.343 19.858 89.019 1.00 54.60 N
ANISOU 4265 N LYS B 321 7144 6866 6735 -50 219 558 N
ATOM 4266 CA LYS B 321 -46.164 18.642 89.805 1.00 53.05 C
ANISOU 4266 CA LYS B 321 6732 6801 6624 -107 221 819 C
ATOM 4267 C LYS B 321 -45.464 18.928 91.145 1.00 56.40 C
ANISOU 4267 C LYS B 321 7085 7593 6750 -401 280 1007 C
ATOM 4268 O LYS B 321 -45.987 18.575 92.206 1.00 67.35 O
ANISOU 4268 O LYS B 321 8373 9114 8105 -543 342 1099 O
ATOM 4269 CB LYS B 321 -45.350 17.630 88.984 1.00 48.67 C
ANISOU 4269 CB LYS B 321 6110 6145 6236 63 163 986 C
ATOM 4270 CG LYS B 321 -44.847 16.431 89.761 1.00 52.03 C
ANISOU 4270 CG LYS B 321 6297 6698 6775 29 190 1344 C
ATOM 4271 CD LYS B 321 -44.221 15.406 88.836 1.00 56.78 C
ANISOU 4271 CD LYS B 321 6852 7083 7637 246 211 1459 C
ATOM 4272 CE LYS B 321 -43.508 14.328 89.629 1.00 64.57 C
ANISOU 4272 CE LYS B 321 7572 8195 8765 240 265 1898 C
ATOM 4273 NZ LYS B 321 -43.072 13.218 88.742 1.00 69.60 N
ANISOU 4273 NZ LYS B 321 8173 8523 9749 480 369 1982 N
ATOM 4274 N ARG B 322 -44.290 19.589 91.111 1.00 49.09 N
ANISOU 4274 N ARG B 322 6214 6857 5580 -529 259 1065 N
ATOM 4275 CA ARG B 322 -43.447 19.760 92.303 1.00 49.85 C
ANISOU 4275 CA ARG B 322 6215 7367 5359 -856 254 1288 C
ATOM 4276 C ARG B 322 -43.850 20.941 93.193 1.00 54.00 C
ANISOU 4276 C ARG B 322 6926 8034 5557 -1173 378 1047 C
ATOM 4277 O ARG B 322 -43.619 20.887 94.409 1.00 63.03 O
ANISOU 4277 O ARG B 322 7999 9445 6503 -1415 360 1126 O
ATOM 4278 CB ARG B 322 -41.979 19.948 91.905 1.00 50.66 C
ANISOU 4278 CB ARG B 322 6253 7639 5355 -900 173 1470 C
ATOM 4279 CG ARG B 322 -41.371 18.806 91.118 1.00 54.71 C
ANISOU 4279 CG ARG B 322 6578 8026 6186 -610 124 1731 C
ATOM 4280 CD ARG B 322 -41.185 17.563 91.964 1.00 63.75 C
ANISOU 4280 CD ARG B 322 7434 9304 7485 -592 71 2064 C
ATOM 4281 NE ARG B 322 -40.710 16.442 91.160 1.00 69.69 N
ANISOU 4281 NE ARG B 322 8030 9847 8603 -291 106 2285 N
ATOM 4282 CZ ARG B 322 -40.257 15.300 91.665 1.00 72.23 C
ANISOU 4282 CZ ARG B 322 8067 10226 9150 -205 86 2576 C
ATOM 4283 NH1 ARG B 322 -40.208 15.130 92.979 1.00 69.08 N
ANISOU 4283 NH1 ARG B 322 7505 10127 8614 -398 -18 2719 N
ATOM 4284 NH2 ARG B 322 -39.845 14.332 90.858 1.00 77.87 N
ANISOU 4284 NH2 ARG B 322 8672 10686 10228 73 193 2715 N
ATOM 4285 N VAL B 323 -44.393 22.010 92.625 1.00 71.99 N
ANISOU 4285 N VAL B 323 10085 9362 7906 1656 1430 -643 N
ATOM 4286 CA VAL B 323 -44.764 23.200 93.396 1.00 64.44 C
ANISOU 4286 CA VAL B 323 8995 8591 6897 1904 1791 -697 C
ATOM 4287 C VAL B 323 -46.256 23.215 93.728 1.00 65.21 C
ANISOU 4287 C VAL B 323 8503 8933 7339 1724 2213 -741 C
ATOM 4288 O VAL B 323 -46.635 23.592 94.837 1.00 63.07 O
ANISOU 4288 O VAL B 323 8269 8737 6959 1711 2724 -746 O
ATOM 4289 CB VAL B 323 -44.327 24.486 92.653 1.00 58.24 C
ANISOU 4289 CB VAL B 323 8121 7895 6112 2364 1477 -819 C
ATOM 4290 CG1 VAL B 323 -44.656 25.744 93.462 1.00 49.94 C
ANISOU 4290 CG1 VAL B 323 7024 6960 4992 2645 1874 -891 C
ATOM 4291 CG2 VAL B 323 -42.828 24.460 92.347 1.00 52.24 C
ANISOU 4291 CG2 VAL B 323 7912 6952 4986 2503 1082 -775 C
ATOM 4292 N PHE B 324 -47.122 22.764 92.810 1.00 65.21 N
ANISOU 4292 N PHE B 324 7960 9082 7737 1537 2028 -769 N
ATOM 4293 CA PHE B 324 -48.570 22.797 93.009 1.00 68.04 C
ANISOU 4293 CA PHE B 324 7643 9745 8464 1368 2385 -791 C
ATOM 4294 C PHE B 324 -49.176 21.419 93.289 1.00 74.46 C
ANISOU 4294 C PHE B 324 8423 10550 9318 762 2558 -691 C
ATOM 4295 O PHE B 324 -50.405 21.278 93.304 1.00 77.95 O
ANISOU 4295 O PHE B 324 8249 11292 10076 528 2795 -692 O
ATOM 4296 CB PHE B 324 -49.236 23.472 91.805 1.00 66.41 C
ANISOU 4296 CB PHE B 324 6752 9791 8691 1591 2047 -857 C
ATOM 4297 CG PHE B 324 -48.856 24.919 91.680 1.00 66.55 C
ANISOU 4297 CG PHE B 324 6767 9822 8697 2175 1966 -947 C
ATOM 4298 CD1 PHE B 324 -49.522 25.884 92.418 1.00 67.46 C
ANISOU 4298 CD1 PHE B 324 6583 10089 8958 2473 2443 -1013 C
ATOM 4299 CD2 PHE B 324 -47.785 25.307 90.892 1.00 63.75 C
ANISOU 4299 CD2 PHE B 324 6773 9301 8148 2411 1455 -977 C
ATOM 4300 CE1 PHE B 324 -49.152 27.218 92.343 1.00 65.57 C
ANISOU 4300 CE1 PHE B 324 6434 9796 8685 3002 2389 -1101 C
ATOM 4301 CE2 PHE B 324 -47.410 26.641 90.813 1.00 64.65 C
ANISOU 4301 CE2 PHE B 324 6957 9406 8203 2900 1376 -1051 C
ATOM 4302 CZ PHE B 324 -48.096 27.597 91.539 1.00 59.94 C
ANISOU 4302 CZ PHE B 324 6098 8917 7759 3198 1836 -1109 C
ATOM 4303 N GLY B 325 -48.342 20.410 93.553 1.00 75.67 N
ANISOU 4303 N GLY B 325 9227 10368 9158 500 2455 -589 N
ATOM 4304 CA GLY B 325 -48.782 19.098 93.953 1.00 71.61 C
ANISOU 4304 CA GLY B 325 8843 9757 8608 -83 2630 -475 C
ATOM 4305 C GLY B 325 -49.806 18.428 93.057 1.00 75.22 C
ANISOU 4305 C GLY B 325 8769 10398 9413 -486 2473 -486 C
ATOM 4306 O GLY B 325 -50.666 17.688 93.538 1.00 97.16 O
ANISOU 4306 O GLY B 325 11386 13288 12242 -985 2775 -417 O
ATOM 4307 N MET B 326 -49.717 18.663 91.744 1.00 72.91 N
ANISOU 4307 N MET B 326 8223 10154 9326 -335 1986 -564 N
ATOM 4308 CA MET B 326 -50.630 18.081 90.776 1.00 76.31 C
ANISOU 4308 CA MET B 326 8167 10776 10049 -755 1761 -562 C
ATOM 4309 C MET B 326 -50.185 16.692 90.323 1.00 76.15 C
ANISOU 4309 C MET B 326 8686 10375 9873 -1219 1522 -527 C
ATOM 4310 O MET B 326 -49.082 16.227 90.631 1.00 79.41 O
ANISOU 4310 O MET B 326 9816 10358 9999 -1120 1472 -502 O
ATOM 4311 CB MET B 326 -50.762 18.981 89.551 1.00 74.48 C
ANISOU 4311 CB MET B 326 7443 10774 10083 -440 1325 -644 C
ATOM 4312 CG MET B 326 -51.383 20.310 89.831 1.00 77.65 C
ANISOU 4312 CG MET B 326 7235 11537 10732 7 1528 -669 C
ATOM 4313 SD MET B 326 -52.074 20.976 88.318 1.00 86.29 S
ANISOU 4313 SD MET B 326 7555 12983 12250 104 995 -667 S
ATOM 4314 CE MET B 326 -52.475 22.624 88.872 1.00 92.66 C
ANISOU 4314 CE MET B 326 7868 14038 13299 806 1288 -698 C
ATOM 4315 N PHE B 327 -51.077 16.041 89.557 1.00 80.07 N
ANISOU 4315 N PHE B 327 8814 11036 10572 -1734 1368 -517 N
ATOM 4316 CA PHE B 327 -50.900 14.724 88.912 1.00 82.86 C
ANISOU 4316 CA PHE B 327 9602 11054 10828 -2263 1132 -516 C
ATOM 4317 C PHE B 327 -50.628 13.597 89.914 1.00 86.87 C
ANISOU 4317 C PHE B 327 10766 11163 11077 -2605 1439 -406 C
ATOM 4318 O PHE B 327 -49.794 12.719 89.671 1.00 88.34 O
ANISOU 4318 O PHE B 327 11636 10842 11088 -2700 1270 -413 O
ATOM 4319 CB PHE B 327 -49.812 14.744 87.824 1.00 78.81 C
ANISOU 4319 CB PHE B 327 9486 10231 10227 -2006 660 -646 C
ATOM 4320 CG PHE B 327 -49.681 16.059 87.083 1.00 75.47 C
ANISOU 4320 CG PHE B 327 8617 10106 9950 -1511 364 -737 C
ATOM 4321 CD1 PHE B 327 -50.713 16.556 86.297 1.00 77.56 C
ANISOU 4321 CD1 PHE B 327 8128 10828 10512 -1662 163 -729 C
ATOM 4322 CD2 PHE B 327 -48.496 16.777 87.146 1.00 70.24 C
ANISOU 4322 CD2 PHE B 327 8308 9263 9116 -920 251 -805 C
ATOM 4323 CE1 PHE B 327 -50.573 17.764 85.618 1.00 72.75 C
ANISOU 4323 CE1 PHE B 327 7158 10449 10035 -1206 -143 -782 C
ATOM 4324 CE2 PHE B 327 -48.351 17.980 86.470 1.00 64.96 C
ANISOU 4324 CE2 PHE B 327 7298 8836 8546 -502 -34 -880 C
ATOM 4325 CZ PHE B 327 -49.390 18.473 85.705 1.00 66.99 C
ANISOU 4325 CZ PHE B 327 6840 9504 9108 -635 -235 -867 C
ATOM 4326 N ARG B 328 -51.365 13.574 91.024 1.00 92.32 N
ANISOU 4326 N ARG B 328 11254 12072 11751 -2820 1895 -300 N
ATOM 4327 CA ARG B 328 -51.236 12.491 91.995 1.00 99.79 C
ANISOU 4327 CA ARG B 328 12806 12671 12439 -3238 2175 -161 C
ATOM 4328 C ARG B 328 -52.324 11.426 91.870 1.00111.23 C
ANISOU 4328 C ARG B 328 14107 14216 13938 -4060 2268 -95 C
ATOM 4329 O ARG B 328 -52.070 10.260 92.195 1.00116.51 O
ANISOU 4329 O ARG B 328 15433 14438 14396 -4484 2308 3 O
ATOM 4330 CB ARG B 328 -51.210 13.061 93.421 1.00102.70 C
ANISOU 4330 CB ARG B 328 13212 13164 12647 -3032 2644 -81 C
ATOM 4331 CG ARG B 328 -49.845 13.626 93.826 1.00 98.93 C
ANISOU 4331 CG ARG B 328 13268 12380 11942 -2413 2561 -69 C
ATOM 4332 CD ARG B 328 -49.968 14.624 94.964 1.00103.28 C
ANISOU 4332 CD ARG B 328 13655 13203 12382 -2139 2989 -59 C
ATOM 4333 NE ARG B 328 -48.687 15.233 95.307 1.00103.05 N
ANISOU 4333 NE ARG B 328 14112 12937 12107 -1599 2879 -37 N
ATOM 4334 CZ ARG B 328 -48.545 16.229 96.175 1.00106.83 C
ANISOU 4334 CZ ARG B 328 14567 13590 12434 -1292 3183 -53 C
ATOM 4335 NH1 ARG B 328 -47.342 16.724 96.431 1.00104.19 N
ANISOU 4335 NH1 ARG B 328 14701 13048 11838 -872 3032 -11 N
ATOM 4336 NH2 ARG B 328 -49.609 16.735 96.786 1.00111.19 N
ANISOU 4336 NH2 ARG B 328 14625 14535 13087 -1422 3654 -118 N
ATOM 4337 N GLN B 329 -53.496 11.790 91.332 1.00116.40 N
ANISOU 4337 N GLN B 329 13923 15431 14872 -4298 2258 -130 N
ATOM 4338 CA GLN B 329 -54.614 10.868 91.151 1.00124.91 C
ANISOU 4338 CA GLN B 329 14754 16711 15994 -5130 2324 -55 C
ATOM 4339 C GLN B 329 -54.357 9.868 90.025 1.00125.53 C
ANISOU 4339 C GLN B 329 15276 16407 16010 -5554 1900 -99 C
ATOM 4340 O GLN B 329 -53.958 10.251 88.918 1.00121.66 O
ANISOU 4340 O GLN B 329 14703 15890 15633 -5279 1492 -218 O
ATOM 4341 CB GLN B 329 -55.904 11.647 90.859 1.00131.84 C
ANISOU 4341 CB GLN B 329 14515 18356 17221 -5201 2401 -51 C
ATOM 4342 CG GLN B 329 -56.571 12.257 92.088 1.00140.11 C
ANISOU 4342 CG GLN B 329 15085 19822 18328 -5089 2978 -8 C
ATOM 4343 CD GLN B 329 -57.885 12.956 91.775 1.00148.22 C
ANISOU 4343 CD GLN B 329 14949 21607 19760 -5138 3071 11 C
ATOM 4344 OE1 GLN B 329 -57.896 14.090 91.298 1.00148.20 O
ANISOU 4344 OE1 GLN B 329 14407 21855 20046 -4525 2917 -50 O
ATOM 4345 NE2 GLN B 329 -58.999 12.285 92.054 1.00153.62 N
ANISOU 4345 NE2 GLN B 329 15235 22665 20471 -5870 3320 113 N
ATOM 4346 N ALA B 330 -54.619 8.583 90.303 1.00131.20 N
ANISOU 4346 N ALA B 330 16494 16827 16530 -6270 2010 -9 N
ATOM 4347 CA ALA B 330 -54.455 7.523 89.325 1.00132.43 C
ANISOU 4347 CA ALA B 330 17159 16565 16593 -6766 1686 -65 C
ATOM 4348 C ALA B 330 -55.614 7.480 88.340 1.00139.71 C
ANISOU 4348 C ALA B 330 17383 18014 17685 -7361 1476 -78 C
ATOM 4349 O ALA B 330 -55.695 6.599 87.485 1.00136.46 O
ANISOU 4349 O ALA B 330 17329 17345 17174 -7929 1225 -128 O
ATOM 4350 CB ALA B 330 -54.303 6.172 90.051 1.00133.36 C
ANISOU 4350 CB ALA B 330 18135 16113 16422 -7314 1891 54 C
ATOM 4351 N SER B 331 -56.505 8.483 88.485 1.00149.58 N
ANISOU 4351 N SER B 331 17621 20012 19198 -7208 1587 -24 N
ATOM 4352 CA SER B 331 -57.602 8.736 87.553 1.00159.26 C
ANISOU 4352 CA SER B 331 17982 21869 20662 -7617 1340 14 C
ATOM 4353 C SER B 331 -57.068 9.203 86.199 1.00165.97 C
ANISOU 4353 C SER B 331 18809 22642 21610 -7311 806 -116 C
ATOM 4354 O SER B 331 -57.545 8.751 85.147 1.00165.06 O
ANISOU 4354 O SER B 331 18572 22653 21490 -7912 464 -115 O
ATOM 4355 CB SER B 331 -58.545 9.782 88.173 1.00155.00 C
ANISOU 4355 CB SER B 331 16381 22086 20427 -7348 1640 111 C
ATOM 4356 OG SER B 331 -59.617 10.143 87.317 1.00154.44 O
ANISOU 4356 OG SER B 331 15351 22682 20647 -7649 1383 198 O
ATOM 4357 N ASP B 332 -56.042 10.049 86.223 1.00174.09 N
ANISOU 4357 N ASP B 332 20025 23448 22673 -6449 732 -226 N
ATOM 4358 CA ASP B 332 -55.412 10.713 85.093 1.00173.81 C
ANISOU 4358 CA ASP B 332 19960 23365 22715 -6027 273 -357 C
ATOM 4359 C ASP B 332 -54.077 10.054 84.650 1.00169.51 C
ANISOU 4359 C ASP B 332 20446 22060 21899 -5902 99 -536 C
ATOM 4360 O ASP B 332 -53.424 10.581 83.744 1.00165.62 O
ANISOU 4360 O ASP B 332 20009 21495 21423 -5549 -251 -672 O
ATOM 4361 CB ASP B 332 -55.151 12.170 85.504 1.00173.33 C
ANISOU 4361 CB ASP B 332 19414 23584 22861 -5134 348 -360 C
ATOM 4362 CG ASP B 332 -55.222 13.178 84.368 1.00177.36 C
ANISOU 4362 CG ASP B 332 19369 24429 23592 -4829 -117 -393 C
ATOM 4363 OD1 ASP B 332 -55.614 12.825 83.237 1.00182.04 O
ANISOU 4363 OD1 ASP B 332 19816 25151 24201 -5347 -514 -389 O
ATOM 4364 OD2 ASP B 332 -54.787 14.328 84.603 1.00174.48 O
ANISOU 4364 OD2 ASP B 332 18804 24149 23342 -4074 -102 -424 O
ATOM 4365 N ARG B 333 -53.727 8.879 85.199 1.00129.30 N
ANISOU 4365 N ARG B 333 15529 15079 18521 -3157 928 1600 N
ATOM 4366 CA ARG B 333 -52.405 8.255 85.005 1.00119.88 C
ANISOU 4366 CA ARG B 333 14851 13631 17066 -2909 882 1849 C
ATOM 4367 C ARG B 333 -51.972 8.148 83.526 1.00111.64 C
ANISOU 4367 C ARG B 333 14073 12190 16157 -2804 460 1575 C
ATOM 4368 O ARG B 333 -50.793 8.359 83.210 1.00107.30 O
ANISOU 4368 O ARG B 333 13817 11660 15291 -2483 321 1588 O
ATOM 4369 CB ARG B 333 -52.392 6.860 85.659 1.00120.31 C
ANISOU 4369 CB ARG B 333 15144 13375 17192 -3089 1227 2321 C
ATOM 4370 CG ARG B 333 -50.981 6.292 85.823 1.00117.50 C
ANISOU 4370 CG ARG B 333 15290 12891 16464 -2747 1236 2620 C
ATOM 4371 CD ARG B 333 -50.890 4.871 86.373 1.00124.58 C
ANISOU 4371 CD ARG B 333 16523 13391 17421 -2866 1530 3101 C
ATOM 4372 NE ARG B 333 -49.506 4.406 86.252 1.00125.62 N
ANISOU 4372 NE ARG B 333 17129 13377 17223 -2469 1414 3265 N
ATOM 4373 CZ ARG B 333 -48.988 3.372 86.904 1.00131.02 C
ANISOU 4373 CZ ARG B 333 18200 13835 17747 -2359 1632 3712 C
ATOM 4374 NH1 ARG B 333 -49.722 2.703 87.779 1.00134.10 N
ANISOU 4374 NH1 ARG B 333 18589 14111 18252 -2638 2026 4097 N
ATOM 4375 NH2 ARG B 333 -47.719 3.033 86.711 1.00132.45 N
ANISOU 4375 NH2 ARG B 333 18768 13924 17632 -1952 1471 3781 N
ATOM 4376 N GLU B 334 -52.913 7.862 82.608 1.00111.86 N
ANISOU 4376 N GLU B 334 13973 11894 16637 -3056 250 1296 N
ATOM 4377 CA GLU B 334 -52.566 7.651 81.195 1.00110.20 C
ANISOU 4377 CA GLU B 334 14037 11302 16532 -2939 -147 1037 C
ATOM 4378 C GLU B 334 -52.197 8.952 80.486 1.00105.03 C
ANISOU 4378 C GLU B 334 13366 10902 15639 -2649 -455 715 C
ATOM 4379 O GLU B 334 -51.188 9.021 79.773 1.00103.84 O
ANISOU 4379 O GLU B 334 13555 10645 15256 -2383 -633 685 O
ATOM 4380 CB GLU B 334 -53.754 7.021 80.449 1.00116.30 C
ANISOU 4380 CB GLU B 334 14639 11693 17859 -3272 -315 774 C
ATOM 4381 CG GLU B 334 -54.092 5.579 80.778 1.00127.93 C
ANISOU 4381 CG GLU B 334 16210 12720 19678 -3601 -82 1038 C
ATOM 4382 CD GLU B 334 -53.069 4.576 80.255 1.00132.82 C
ANISOU 4382 CD GLU B 334 17370 12879 20217 -3428 -183 1201 C
ATOM 4383 OE1 GLU B 334 -52.344 4.882 79.281 1.00131.06 O
ANISOU 4383 OE1 GLU B 334 17393 12610 19794 -3113 -512 984 O
ATOM 4384 OE2 GLU B 334 -53.007 3.465 80.820 1.00137.50 O
ANISOU 4384 OE2 GLU B 334 18161 13203 20880 -3560 99 1518 O
ATOM 4385 N ALA B 335 -53.016 9.998 80.684 1.00101.57 N
ANISOU 4385 N ALA B 335 12538 10798 15258 -2695 -504 477 N
ATOM 4386 CA ALA B 335 -52.786 11.319 80.101 1.00 91.05 C
ANISOU 4386 CA ALA B 335 11191 9683 13722 -2436 -777 191 C
ATOM 4387 C ALA B 335 -51.549 11.978 80.692 1.00 87.93 C
ANISOU 4387 C ALA B 335 10949 9585 12874 -2168 -641 375 C
ATOM 4388 O ALA B 335 -50.823 12.700 79.997 1.00 84.45 O
ANISOU 4388 O ALA B 335 10706 9156 12224 -1936 -838 244 O
ATOM 4389 CB ALA B 335 -54.017 12.203 80.329 1.00 84.59 C
ANISOU 4389 CB ALA B 335 9906 9141 13093 -2538 -846 -98 C
ATOM 4390 N VAL B 336 -51.327 11.754 81.989 1.00 86.00 N
ANISOU 4390 N VAL B 336 10602 9596 12477 -2200 -296 668 N
ATOM 4391 CA VAL B 336 -50.170 12.302 82.690 1.00 82.58 C
ANISOU 4391 CA VAL B 336 10265 9483 11628 -1940 -167 814 C
ATOM 4392 C VAL B 336 -48.869 11.712 82.140 1.00 83.85 C
ANISOU 4392 C VAL B 336 10849 9414 11597 -1747 -225 950 C
ATOM 4393 O VAL B 336 -47.938 12.455 81.801 1.00 83.90 O
ANISOU 4393 O VAL B 336 10968 9544 11365 -1526 -333 845 O
ATOM 4394 CB VAL B 336 -50.320 12.060 84.208 1.00 78.86 C
ANISOU 4394 CB VAL B 336 9604 9343 11018 -1989 203 1094 C
ATOM 4395 CG1 VAL B 336 -49.034 12.376 84.966 1.00 73.79 C
ANISOU 4395 CG1 VAL B 336 9090 9008 9937 -1689 319 1249 C
ATOM 4396 CG2 VAL B 336 -51.476 12.896 84.773 1.00 79.92 C
ANISOU 4396 CG2 VAL B 336 9278 9818 11271 -2112 259 899 C
ATOM 4397 N TYR B 337 -48.780 10.383 82.005 1.00 85.98 N
ANISOU 4397 N TYR B 337 11353 9332 11985 -1830 -154 1163 N
ATOM 4398 CA TYR B 337 -47.539 9.810 81.482 1.00 85.59 C
ANISOU 4398 CA TYR B 337 11690 9085 11744 -1604 -223 1257 C
ATOM 4399 C TYR B 337 -47.338 10.150 79.998 1.00 81.86 C
ANISOU 4399 C TYR B 337 11385 8395 11321 -1518 -545 960 C
ATOM 4400 O TYR B 337 -46.209 10.406 79.569 1.00 80.20 O
ANISOU 4400 O TYR B 337 11376 8244 10853 -1278 -603 931 O
ATOM 4401 CB TYR B 337 -47.461 8.302 81.764 1.00 94.46 C
ANISOU 4401 CB TYR B 337 13059 9862 12971 -1672 -77 1562 C
ATOM 4402 CG TYR B 337 -47.167 7.996 83.237 1.00104.90 C
ANISOU 4402 CG TYR B 337 14355 11444 14059 -1610 258 1925 C
ATOM 4403 CD1 TYR B 337 -46.468 8.902 84.036 1.00103.37 C
ANISOU 4403 CD1 TYR B 337 14029 11756 13492 -1374 347 1933 C
ATOM 4404 CD2 TYR B 337 -47.618 6.823 83.833 1.00113.85 C
ANISOU 4404 CD2 TYR B 337 15602 12310 15344 -1785 484 2253 C
ATOM 4405 CE1 TYR B 337 -46.219 8.638 85.382 1.00106.74 C
ANISOU 4405 CE1 TYR B 337 14442 12458 13656 -1265 627 2242 C
ATOM 4406 CE2 TYR B 337 -47.374 6.553 85.176 1.00116.76 C
ANISOU 4406 CE2 TYR B 337 15993 12925 15446 -1693 801 2616 C
ATOM 4407 CZ TYR B 337 -46.675 7.463 85.945 1.00114.09 C
ANISOU 4407 CZ TYR B 337 15525 13133 14692 -1410 858 2601 C
ATOM 4408 OH TYR B 337 -46.433 7.196 87.276 1.00119.67 O
ANISOU 4408 OH TYR B 337 16268 14117 15084 -1265 1146 2941 O
ATOM 4409 N ALA B 338 -48.421 10.174 79.206 1.00 76.68 N
ANISOU 4409 N ALA B 338 10639 7516 10980 -1696 -751 727 N
ATOM 4410 CA ALA B 338 -48.317 10.603 77.809 1.00 69.82 C
ANISOU 4410 CA ALA B 338 9940 6483 10103 -1572 -1068 440 C
ATOM 4411 C ALA B 338 -47.781 12.033 77.704 1.00 73.25 C
ANISOU 4411 C ALA B 338 10330 7238 10265 -1395 -1111 321 C
ATOM 4412 O ALA B 338 -46.915 12.320 76.868 1.00 78.24 O
ANISOU 4412 O ALA B 338 11215 7823 10690 -1202 -1212 256 O
ATOM 4413 CB ALA B 338 -49.682 10.494 77.123 1.00 65.73 C
ANISOU 4413 CB ALA B 338 9273 5742 9960 -1765 -1305 172 C
ATOM 4414 N ALA B 339 -48.288 12.934 78.558 1.00 69.52 N
ANISOU 4414 N ALA B 339 9535 7083 9797 -1463 -1018 289 N
ATOM 4415 CA ALA B 339 -47.848 14.328 78.582 1.00 60.07 C
ANISOU 4415 CA ALA B 339 8277 6153 8393 -1322 -1054 167 C
ATOM 4416 C ALA B 339 -46.373 14.452 78.970 1.00 61.47 C
ANISOU 4416 C ALA B 339 8588 6512 8255 -1149 -882 321 C
ATOM 4417 O ALA B 339 -45.611 15.176 78.319 1.00 62.27 O
ANISOU 4417 O ALA B 339 8838 6628 8195 -1020 -952 226 O
ATOM 4418 CB ALA B 339 -48.725 15.133 79.546 1.00 56.50 C
ANISOU 4418 CB ALA B 339 7433 6005 8028 -1415 -988 84 C
ATOM 4419 N PHE B 340 -45.955 13.756 80.034 1.00 58.31 N
ANISOU 4419 N PHE B 340 8132 6260 7764 -1138 -651 554 N
ATOM 4420 CA PHE B 340 -44.564 13.834 80.478 1.00 54.77 C
ANISOU 4420 CA PHE B 340 7762 6028 7020 -940 -515 657 C
ATOM 4421 C PHE B 340 -43.616 13.196 79.457 1.00 60.52 C
ANISOU 4421 C PHE B 340 8825 6517 7653 -803 -586 672 C
ATOM 4422 O PHE B 340 -42.506 13.693 79.237 1.00 59.74 O
ANISOU 4422 O PHE B 340 8783 6566 7350 -653 -557 614 O
ATOM 4423 CB PHE B 340 -44.420 13.187 81.863 1.00 56.30 C
ANISOU 4423 CB PHE B 340 7847 6441 7104 -905 -280 905 C
ATOM 4424 CG PHE B 340 -44.648 14.149 83.012 1.00 60.44 C
ANISOU 4424 CG PHE B 340 8043 7394 7528 -894 -171 852 C
ATOM 4425 CD1 PHE B 340 -45.910 14.313 83.567 1.00 65.04 C
ANISOU 4425 CD1 PHE B 340 8375 8062 8276 -1068 -118 842 C
ATOM 4426 CD2 PHE B 340 -43.604 14.916 83.510 1.00 60.81 C
ANISOU 4426 CD2 PHE B 340 8003 7774 7329 -706 -131 769 C
ATOM 4427 CE1 PHE B 340 -46.122 15.212 84.609 1.00 64.93 C
ANISOU 4427 CE1 PHE B 340 8057 8467 8147 -1021 -28 759 C
ATOM 4428 CE2 PHE B 340 -43.810 15.815 84.553 1.00 61.39 C
ANISOU 4428 CE2 PHE B 340 7775 8240 7313 -671 -64 670 C
ATOM 4429 CZ PHE B 340 -45.071 15.961 85.102 1.00 62.36 C
ANISOU 4429 CZ PHE B 340 7676 8451 7565 -812 -14 669 C
ATOM 4430 N THR B 341 -44.068 12.118 78.804 1.00 67.68 N
ANISOU 4430 N THR B 341 9932 7056 8726 -862 -680 717 N
ATOM 4431 CA THR B 341 -43.292 11.424 77.773 1.00 67.82 C
ANISOU 4431 CA THR B 341 10276 6831 8663 -710 -773 695 C
ATOM 4432 C THR B 341 -43.011 12.330 76.574 1.00 66.75 C
ANISOU 4432 C THR B 341 10253 6675 8434 -641 -920 479 C
ATOM 4433 O THR B 341 -41.858 12.485 76.149 1.00 69.81 O
ANISOU 4433 O THR B 341 10775 7155 8596 -471 -867 460 O
ATOM 4434 CB THR B 341 -44.066 10.167 77.354 1.00 70.21 C
ANISOU 4434 CB THR B 341 10736 6715 9226 -817 -881 733 C
ATOM 4435 OG1 THR B 341 -44.065 9.230 78.436 1.00 72.25 O
ANISOU 4435 OG1 THR B 341 10979 6951 9521 -852 -693 1001 O
ATOM 4436 CG2 THR B 341 -43.486 9.497 76.113 1.00 72.97 C
ANISOU 4436 CG2 THR B 341 11424 6781 9520 -649 -1042 633 C
ATOM 4437 N PHE B 342 -44.070 12.935 76.016 1.00 59.89 N
ANISOU 4437 N PHE B 342 9333 5693 7729 -760 -1099 315 N
ATOM 4438 CA PHE B 342 -43.926 13.856 74.890 1.00 58.46 C
ANISOU 4438 CA PHE B 342 9307 5469 7436 -679 -1240 143 C
ATOM 4439 C PHE B 342 -43.069 15.059 75.273 1.00 61.84 C
ANISOU 4439 C PHE B 342 9633 6194 7671 -637 -1084 147 C
ATOM 4440 O PHE B 342 -42.302 15.573 74.450 1.00 66.58 O
ANISOU 4440 O PHE B 342 10420 6787 8089 -539 -1068 101 O
ATOM 4441 CB PHE B 342 -45.307 14.314 74.396 1.00 58.07 C
ANISOU 4441 CB PHE B 342 9196 5271 7596 -775 -1485 -41 C
ATOM 4442 CG PHE B 342 -45.243 15.373 73.324 1.00 55.83 C
ANISOU 4442 CG PHE B 342 9107 4942 7166 -660 -1636 -186 C
ATOM 4443 CD1 PHE B 342 -44.936 15.034 72.015 1.00 56.91 C
ANISOU 4443 CD1 PHE B 342 9593 4872 7158 -502 -1773 -254 C
ATOM 4444 CD2 PHE B 342 -45.450 16.710 73.631 1.00 53.19 C
ANISOU 4444 CD2 PHE B 342 8637 4761 6812 -685 -1630 -244 C
ATOM 4445 CE1 PHE B 342 -44.848 16.006 71.030 1.00 58.09 C
ANISOU 4445 CE1 PHE B 342 9974 4977 7121 -376 -1878 -338 C
ATOM 4446 CE2 PHE B 342 -45.363 17.687 72.649 1.00 54.42 C
ANISOU 4446 CE2 PHE B 342 9031 4824 6821 -572 -1749 -332 C
ATOM 4447 CZ PHE B 342 -45.062 17.334 71.348 1.00 56.40 C
ANISOU 4447 CZ PHE B 342 9652 4877 6902 -419 -1860 -358 C
ATOM 4448 N SER B 343 -43.183 15.504 76.529 1.00 61.48 N
ANISOU 4448 N SER B 343 9284 6411 7664 -714 -954 195 N
ATOM 4449 CA SER B 343 -42.406 16.639 77.019 1.00 56.73 C
ANISOU 4449 CA SER B 343 8539 6086 6929 -690 -824 153 C
ATOM 4450 C SER B 343 -40.915 16.315 77.102 1.00 56.85 C
ANISOU 4450 C SER B 343 8611 6256 6734 -561 -649 221 C
ATOM 4451 O SER B 343 -40.078 17.160 76.769 1.00 58.07 O
ANISOU 4451 O SER B 343 8777 6508 6779 -541 -572 143 O
ATOM 4452 CB SER B 343 -42.950 17.077 78.380 1.00 57.33 C
ANISOU 4452 CB SER B 343 8270 6427 7086 -766 -756 150 C
ATOM 4453 OG SER B 343 -44.238 17.647 78.228 1.00 59.14 O
ANISOU 4453 OG SER B 343 8406 6564 7502 -865 -920 25 O
ATOM 4454 N HIS B 344 -40.569 15.095 77.545 1.00 54.50 N
ANISOU 4454 N HIS B 344 8345 5973 6390 -469 -581 358 N
ATOM 4455 CA HIS B 344 -39.166 14.678 77.596 1.00 55.83 C
ANISOU 4455 CA HIS B 344 8558 6299 6355 -292 -450 389 C
ATOM 4456 C HIS B 344 -38.580 14.568 76.195 1.00 65.84 C
ANISOU 4456 C HIS B 344 10099 7391 7525 -214 -483 319 C
ATOM 4457 O HIS B 344 -37.413 14.916 75.974 1.00 75.26 O
ANISOU 4457 O HIS B 344 11266 8768 8560 -130 -352 256 O
ATOM 4458 CB HIS B 344 -39.029 13.330 78.313 1.00 57.50 C
ANISOU 4458 CB HIS B 344 8811 6503 6535 -167 -407 564 C
ATOM 4459 CG HIS B 344 -39.454 13.359 79.750 1.00 60.19 C
ANISOU 4459 CG HIS B 344 8911 7067 6890 -198 -322 673 C
ATOM 4460 ND1 HIS B 344 -40.220 12.366 80.313 1.00 64.81 N
ANISOU 4460 ND1 HIS B 344 9550 7503 7572 -239 -307 871 N
ATOM 4461 CD2 HIS B 344 -39.235 14.270 80.725 1.00 60.33 C
ANISOU 4461 CD2 HIS B 344 8642 7448 6831 -194 -238 607 C
ATOM 4462 CE1 HIS B 344 -40.458 12.657 81.578 1.00 65.18 C
ANISOU 4462 CE1 HIS B 344 9364 7839 7563 -245 -194 948 C
ATOM 4463 NE2 HIS B 344 -39.870 13.812 81.856 1.00 63.00 N
ANISOU 4463 NE2 HIS B 344 8874 7889 7175 -199 -171 770 N
ATOM 4464 N TRP B 345 -39.377 14.080 75.235 1.00 65.61 N
ANISOU 4464 N TRP B 345 10316 7028 7584 -235 -654 307 N
ATOM 4465 CA TRP B 345 -38.909 13.954 73.860 1.00 64.46 C
ANISOU 4465 CA TRP B 345 10460 6730 7301 -124 -699 232 C
ATOM 4466 C TRP B 345 -38.635 15.329 73.241 1.00 70.59 C
ANISOU 4466 C TRP B 345 11260 7580 7982 -191 -635 152 C
ATOM 4467 O TRP B 345 -37.632 15.504 72.538 1.00 76.37 O
ANISOU 4467 O TRP B 345 12108 8387 8520 -104 -502 125 O
ATOM 4468 CB TRP B 345 -39.924 13.157 73.023 1.00 63.01 C
ANISOU 4468 CB TRP B 345 10518 6182 7241 -114 -941 192 C
ATOM 4469 CG TRP B 345 -39.574 13.124 71.557 1.00 63.11 C
ANISOU 4469 CG TRP B 345 10849 6059 7071 35 -1017 89 C
ATOM 4470 CD1 TRP B 345 -38.671 12.301 70.940 1.00 59.06 C
ANISOU 4470 CD1 TRP B 345 10529 5531 6379 244 -976 65 C
ATOM 4471 CD2 TRP B 345 -40.093 13.984 70.536 1.00 61.92 C
ANISOU 4471 CD2 TRP B 345 10875 5795 6857 24 -1140 -4 C
ATOM 4472 NE1 TRP B 345 -38.606 12.593 69.596 1.00 57.74 N
ANISOU 4472 NE1 TRP B 345 10639 5272 6027 354 -1045 -36 N
ATOM 4473 CE2 TRP B 345 -39.469 13.623 69.324 1.00 60.92 C
ANISOU 4473 CE2 TRP B 345 11057 5604 6486 227 -1148 -64 C
ATOM 4474 CE3 TRP B 345 -41.028 15.024 70.529 1.00 64.04 C
ANISOU 4474 CE3 TRP B 345 11086 6015 7229 -101 -1254 -48 C
ATOM 4475 CZ2 TRP B 345 -39.753 14.266 68.117 1.00 65.48 C
ANISOU 4475 CZ2 TRP B 345 11912 6074 6892 308 -1252 -135 C
ATOM 4476 CZ3 TRP B 345 -41.308 15.661 69.332 1.00 64.16 C
ANISOU 4476 CZ3 TRP B 345 11385 5897 7097 -10 -1382 -125 C
ATOM 4477 CH2 TRP B 345 -40.673 15.280 68.143 1.00 65.05 C
ANISOU 4477 CH2 TRP B 345 11828 5950 6938 192 -1373 -153 C
ATOM 4478 N LEU B 346 -39.491 16.320 73.539 1.00 66.80 N
ANISOU 4478 N LEU B 346 10663 7080 7637 -343 -709 118 N
ATOM 4479 CA LEU B 346 -39.366 17.674 72.987 1.00 60.77 C
ANISOU 4479 CA LEU B 346 9969 6307 6816 -411 -668 63 C
ATOM 4480 C LEU B 346 -38.044 18.343 73.353 1.00 57.46 C
ANISOU 4480 C LEU B 346 9387 6148 6297 -451 -398 55 C
ATOM 4481 O LEU B 346 -37.509 19.148 72.580 1.00 60.69 O
ANISOU 4481 O LEU B 346 9941 6516 6601 -490 -281 46 O
ATOM 4482 CB LEU B 346 -40.527 18.541 73.482 1.00 58.51 C
ANISOU 4482 CB LEU B 346 9541 5971 6721 -533 -815 5 C
ATOM 4483 CG LEU B 346 -41.655 18.818 72.492 1.00 59.16 C
ANISOU 4483 CG LEU B 346 9867 5767 6843 -499 -1077 -63 C
ATOM 4484 CD1 LEU B 346 -42.616 19.827 73.075 1.00 63.67 C
ANISOU 4484 CD1 LEU B 346 10253 6347 7591 -588 -1199 -152 C
ATOM 4485 CD2 LEU B 346 -41.102 19.323 71.171 1.00 60.19 C
ANISOU 4485 CD2 LEU B 346 10367 5758 6746 -408 -1041 -44 C
ATOM 4486 N VAL B 347 -37.554 18.077 74.568 1.00 52.71 N
ANISOU 4486 N VAL B 347 8474 5819 5736 -448 -297 51 N
ATOM 4487 CA VAL B 347 -36.263 18.586 75.039 1.00 53.17 C
ANISOU 4487 CA VAL B 347 8303 6172 5729 -467 -71 -17 C
ATOM 4488 C VAL B 347 -35.152 18.116 74.096 1.00 56.77 C
ANISOU 4488 C VAL B 347 8916 6660 5995 -359 82 -17 C
ATOM 4489 O VAL B 347 -34.271 18.887 73.699 1.00 61.85 O
ANISOU 4489 O VAL B 347 9515 7399 6584 -445 284 -76 O
ATOM 4490 CB VAL B 347 -36.025 18.115 76.485 1.00 52.01 C
ANISOU 4490 CB VAL B 347 7833 6320 5607 -393 -51 -30 C
ATOM 4491 CG1 VAL B 347 -34.563 18.236 76.927 1.00 47.12 C
ANISOU 4491 CG1 VAL B 347 6966 6043 4892 -324 139 -142 C
ATOM 4492 CG2 VAL B 347 -36.973 18.837 77.451 1.00 55.08 C
ANISOU 4492 CG2 VAL B 347 8017 6759 6153 -505 -144 -66 C
ATOM 4493 N TYR B 348 -35.192 16.824 73.743 1.00 55.58 N
ANISOU 4493 N TYR B 348 8940 6424 5753 -173 -3 40 N
ATOM 4494 CA TYR B 348 -34.227 16.238 72.846 1.00 51.96 C
ANISOU 4494 CA TYR B 348 8636 6007 5097 -16 113 14 C
ATOM 4495 C TYR B 348 -34.446 16.683 71.408 1.00 52.83 C
ANISOU 4495 C TYR B 348 9090 5895 5090 -43 121 32 C
ATOM 4496 O TYR B 348 -33.482 16.968 70.677 1.00 54.52 O
ANISOU 4496 O TYR B 348 9360 6223 5133 -24 343 2 O
ATOM 4497 CB TYR B 348 -34.291 14.702 72.980 1.00 48.29 C
ANISOU 4497 CB TYR B 348 8277 5475 4595 216 -21 53 C
ATOM 4498 CG TYR B 348 -33.997 14.234 74.400 1.00 47.05 C
ANISOU 4498 CG TYR B 348 7839 5544 4493 293 -10 76 C
ATOM 4499 CD1 TYR B 348 -32.770 14.493 74.992 1.00 47.57 C
ANISOU 4499 CD1 TYR B 348 7616 5985 4473 368 164 -26 C
ATOM 4500 CD2 TYR B 348 -34.949 13.544 75.145 1.00 41.67 C
ANISOU 4500 CD2 TYR B 348 7179 4713 3939 297 -166 195 C
ATOM 4501 CE1 TYR B 348 -32.493 14.081 76.280 1.00 46.04 C
ANISOU 4501 CE1 TYR B 348 7193 6023 4278 498 146 -16 C
ATOM 4502 CE2 TYR B 348 -34.678 13.126 76.438 1.00 42.95 C
ANISOU 4502 CE2 TYR B 348 7137 5089 4094 398 -136 253 C
ATOM 4503 CZ TYR B 348 -33.448 13.398 76.998 1.00 48.00 C
ANISOU 4503 CZ TYR B 348 7522 6111 4605 525 2 146 C
ATOM 4504 OH TYR B 348 -33.170 12.987 78.281 1.00 50.95 O
ANISOU 4504 OH TYR B 348 7717 6720 4921 685 3 193 O
ATOM 4505 N ALA B 349 -35.713 16.832 70.996 1.00 51.11 N
ANISOU 4505 N ALA B 349 9091 5381 4949 -86 -107 72 N
ATOM 4506 CA ALA B 349 -36.043 17.324 69.663 1.00 50.60 C
ANISOU 4506 CA ALA B 349 9388 5101 4738 -65 -145 90 C
ATOM 4507 C ALA B 349 -35.385 18.677 69.370 1.00 60.81 C
ANISOU 4507 C ALA B 349 10677 6466 5961 -228 117 124 C
ATOM 4508 O ALA B 349 -35.050 18.962 68.215 1.00 72.92 O
ANISOU 4508 O ALA B 349 12509 7926 7270 -176 236 173 O
ATOM 4509 CB ALA B 349 -37.566 17.411 69.510 1.00 47.34 C
ANISOU 4509 CB ALA B 349 9120 4404 4464 -82 -468 82 C
ATOM 4510 N ASN B 350 -35.164 19.498 70.406 1.00 58.86 N
ANISOU 4510 N ASN B 350 10102 6360 5901 -422 222 97 N
ATOM 4511 CA ASN B 350 -34.525 20.805 70.242 1.00 61.22 C
ANISOU 4511 CA ASN B 350 10365 6684 6210 -624 477 110 C
ATOM 4512 C ASN B 350 -33.084 20.682 69.725 1.00 61.43 C
ANISOU 4512 C ASN B 350 10343 6932 6064 -625 825 97 C
ATOM 4513 O ASN B 350 -32.638 21.509 68.920 1.00 66.00 O
ANISOU 4513 O ASN B 350 11101 7433 6544 -749 1064 171 O
ATOM 4514 CB ASN B 350 -34.566 21.567 71.576 1.00 63.52 C
ANISOU 4514 CB ASN B 350 10266 7103 6767 -804 477 17 C
ATOM 4515 CG ASN B 350 -33.888 22.933 71.513 1.00 74.27 C
ANISOU 4515 CG ASN B 350 11555 8451 8215 -1050 730 -6 C
ATOM 4516 OD1 ASN B 350 -32.754 23.099 71.967 1.00 79.12 O
ANISOU 4516 OD1 ASN B 350 11851 9328 8883 -1155 970 -112 O
ATOM 4517 ND2 ASN B 350 -34.587 23.920 70.960 1.00 78.78 N
ANISOU 4517 ND2 ASN B 350 12417 8699 8818 -1139 665 78 N
ATOM 4518 N SER B 351 -32.345 19.662 70.194 1.00 59.68 N
ANISOU 4518 N SER B 351 9882 6991 5804 -481 869 4 N
ATOM 4519 CA SER B 351 -30.977 19.396 69.732 1.00 63.56 C
ANISOU 4519 CA SER B 351 10272 7749 6130 -431 1177 -59 C
ATOM 4520 C SER B 351 -30.934 19.052 68.246 1.00 67.89 C
ANISOU 4520 C SER B 351 11249 8170 6377 -282 1250 30 C
ATOM 4521 O SER B 351 -29.942 19.351 67.564 1.00 71.62 O
ANISOU 4521 O SER B 351 11724 8799 6691 -332 1589 29 O
ATOM 4522 CB SER B 351 -30.361 18.241 70.535 1.00 61.37 C
ANISOU 4522 CB SER B 351 9700 7767 5851 -215 1121 -189 C
ATOM 4523 OG SER B 351 -30.276 18.527 71.922 1.00 59.65 O
ANISOU 4523 OG SER B 351 9085 7732 5848 -300 1070 -283 O
ATOM 4524 N ALA B 352 -31.978 18.393 67.742 1.00 65.21 N
ANISOU 4524 N ALA B 352 11251 7573 5951 -92 942 85 N
ATOM 4525 CA ALA B 352 -32.120 18.086 66.329 1.00 69.27 C
ANISOU 4525 CA ALA B 352 12211 7951 6160 95 935 141 C
ATOM 4526 C ALA B 352 -32.511 19.328 65.513 1.00 67.25 C
ANISOU 4526 C ALA B 352 12280 7471 5799 -49 1035 296 C
ATOM 4527 O ALA B 352 -32.080 19.468 64.366 1.00 69.08 O
ANISOU 4527 O ALA B 352 12815 7712 5720 36 1240 373 O
ATOM 4528 CB ALA B 352 -33.151 16.964 66.153 1.00 71.26 C
ANISOU 4528 CB ALA B 352 12677 7990 6410 340 525 93 C
ATOM 4529 N ALA B 353 -33.264 20.240 66.144 1.00 62.89 N
ANISOU 4529 N ALA B 353 11664 6736 5493 -250 909 342 N
ATOM 4530 CA ALA B 353 -33.795 21.445 65.497 1.00 60.54 C
ANISOU 4530 CA ALA B 353 11707 6161 5135 -355 932 491 C
ATOM 4531 C ALA B 353 -32.710 22.486 65.195 1.00 72.23 C
ANISOU 4531 C ALA B 353 13172 7711 6562 -603 1405 601 C
ATOM 4532 O ALA B 353 -32.669 23.043 64.094 1.00 79.81 O
ANISOU 4532 O ALA B 353 14556 8510 7260 -583 1569 775 O
ATOM 4533 CB ALA B 353 -34.883 22.059 66.383 1.00 53.13 C
ANISOU 4533 CB ALA B 353 10649 5032 4507 -472 642 461 C
ATOM 4534 N ASN B 354 -31.840 22.786 66.172 1.00 68.91 N
ANISOU 4534 N ASN B 354 12268 7520 6392 -844 1631 499 N
ATOM 4535 CA ASN B 354 -30.843 23.848 66.016 1.00 72.25 C
ANISOU 4535 CA ASN B 354 12600 7984 6868 -1154 2082 564 C
ATOM 4536 C ASN B 354 -30.021 23.752 64.724 1.00 77.08 C
ANISOU 4536 C ASN B 354 13488 8681 7116 -1107 2468 699 C
ATOM 4537 O ASN B 354 -29.936 24.758 64.007 1.00 84.38 O
ANISOU 4537 O ASN B 354 14732 9382 7947 -1279 2727 907 O
ATOM 4538 CB ASN B 354 -29.923 23.888 67.243 1.00 74.46 C
ANISOU 4538 CB ASN B 354 12247 8591 7454 -1352 2228 344 C
ATOM 4539 CG ASN B 354 -30.655 24.239 68.544 1.00 78.50 C
ANISOU 4539 CG ASN B 354 12489 9034 8303 -1429 1916 222 C
ATOM 4540 OD1 ASN B 354 -31.510 25.130 68.589 1.00 78.12 O
ANISOU 4540 OD1 ASN B 354 12642 8663 8376 -1529 1769 304 O
ATOM 4541 ND2 ASN B 354 -30.350 23.493 69.597 1.00 83.45 N
ANISOU 4541 ND2 ASN B 354 12682 9977 9049 -1337 1801 26 N
ATOM 4542 N PRO B 355 -29.403 22.614 64.358 1.00 73.91 N
ANISOU 4542 N PRO B 355 13010 8587 6485 -871 2538 600 N
ATOM 4543 CA PRO B 355 -28.647 22.599 63.091 1.00 73.27 C
ANISOU 4543 CA PRO B 355 13201 8616 6023 -813 2933 724 C
ATOM 4544 C PRO B 355 -29.529 22.764 61.858 1.00 72.68 C
ANISOU 4544 C PRO B 355 13809 8226 5579 -597 2803 950 C
ATOM 4545 O PRO B 355 -29.076 23.338 60.861 1.00 78.15 O
ANISOU 4545 O PRO B 355 14793 8890 6011 -653 3164 1147 O
ATOM 4546 CB PRO B 355 -27.937 21.234 63.103 1.00 73.37 C
ANISOU 4546 CB PRO B 355 12958 9025 5892 -532 2930 507 C
ATOM 4547 CG PRO B 355 -27.978 20.785 64.532 1.00 73.47 C
ANISOU 4547 CG PRO B 355 12476 9167 6271 -553 2666 291 C
ATOM 4548 CD PRO B 355 -29.295 21.314 65.047 1.00 73.30 C
ANISOU 4548 CD PRO B 355 12616 8770 6464 -632 2295 379 C
ATOM 4549 N ILE B 356 -30.779 22.278 61.911 1.00 70.74 N
ANISOU 4549 N ILE B 356 13787 7759 5332 -342 2277 909 N
ATOM 4550 CA ILE B 356 -31.734 22.471 60.819 1.00 73.92 C
ANISOU 4550 CA ILE B 356 14814 7863 5409 -99 2064 1069 C
ATOM 4551 C ILE B 356 -32.046 23.965 60.648 1.00 77.71 C
ANISOU 4551 C ILE B 356 15507 8021 5999 -332 2173 1290 C
ATOM 4552 O ILE B 356 -32.142 24.464 59.518 1.00 81.42 O
ANISOU 4552 O ILE B 356 16310 8365 6260 -207 2237 1438 O
ATOM 4553 CB ILE B 356 -32.994 21.601 61.064 1.00 70.32 C
ANISOU 4553 CB ILE B 356 14414 7266 5037 184 1454 900 C
ATOM 4554 CG1 ILE B 356 -32.634 20.095 61.023 1.00 70.91 C
ANISOU 4554 CG1 ILE B 356 14324 7601 5016 448 1344 685 C
ATOM 4555 CG2 ILE B 356 -34.115 21.894 60.054 1.00 63.83 C
ANISOU 4555 CG2 ILE B 356 14092 6144 4017 444 1129 971 C
ATOM 4556 CD1 ILE B 356 -33.715 19.104 61.530 1.00 66.00 C
ANISOU 4556 CD1 ILE B 356 13625 6850 4603 632 800 494 C
ATOM 4557 N ILE B 357 -32.131 24.713 61.766 1.00 74.73 N
ANISOU 4557 N ILE B 357 14853 7529 6011 -659 2184 1275 N
ATOM 4558 CA ILE B 357 -32.320 26.168 61.725 1.00 72.14 C
ANISOU 4558 CA ILE B 357 14712 6867 5830 -907 2310 1463 C
ATOM 4559 C ILE B 357 -31.126 26.855 61.051 1.00 73.46 C
ANISOU 4559 C ILE B 357 14853 7120 5940 -1130 2863 1614 C
ATOM 4560 O ILE B 357 -31.301 27.677 60.141 1.00 80.38 O
ANISOU 4560 O ILE B 357 16076 7768 6696 -1087 2928 1808 O
ATOM 4561 CB ILE B 357 -32.576 26.733 63.146 1.00 69.60 C
ANISOU 4561 CB ILE B 357 13970 6463 6012 -1186 2167 1321 C
ATOM 4562 CG1 ILE B 357 -33.830 26.108 63.790 1.00 60.21 C
ANISOU 4562 CG1 ILE B 357 12678 5232 4966 -948 1582 1135 C
ATOM 4563 CG2 ILE B 357 -32.703 28.277 63.127 1.00 74.47 C
ANISOU 4563 CG2 ILE B 357 14806 6687 6800 -1455 2312 1499 C
ATOM 4564 CD1 ILE B 357 -33.941 26.282 65.312 1.00 56.81 C
ANISOU 4564 CD1 ILE B 357 11688 4898 5000 -1150 1441 923 C
ATOM 4565 N TYR B 358 -29.890 26.527 61.479 1.00 73.48 N
ANISOU 4565 N TYR B 358 14419 7472 6027 -1361 3268 1513 N
ATOM 4566 CA TYR B 358 -28.690 27.110 60.867 1.00 81.35 C
ANISOU 4566 CA TYR B 358 15300 8600 7009 -1595 3801 1624 C
ATOM 4567 C TYR B 358 -28.581 26.772 59.378 1.00 88.21 C
ANISOU 4567 C TYR B 358 16542 9547 7426 -1280 3880 1779 C
ATOM 4568 O TYR B 358 -27.928 27.507 58.630 1.00 90.39 O
ANISOU 4568 O TYR B 358 16906 9802 7637 -1435 4258 1970 O
ATOM 4569 CB TYR B 358 -27.390 26.647 61.567 1.00 84.06 C
ANISOU 4569 CB TYR B 358 15024 9393 7522 -1832 4169 1403 C
ATOM 4570 CG TYR B 358 -27.368 26.629 63.094 1.00 83.70 C
ANISOU 4570 CG TYR B 358 14485 9429 7887 -2059 4058 1150 C
ATOM 4571 CD1 TYR B 358 -28.119 27.525 63.846 1.00 84.44 C
ANISOU 4571 CD1 TYR B 358 14582 9171 8330 -2238 3805 1153 C
ATOM 4572 CD2 TYR B 358 -26.577 25.708 63.780 1.00 83.39 C
ANISOU 4572 CD2 TYR B 358 13859 9867 7956 -1994 4068 841 C
ATOM 4573 CE1 TYR B 358 -28.092 27.493 65.242 1.00 80.45 C
ANISOU 4573 CE1 TYR B 358 13508 8813 8245 -2348 3580 857 C
ATOM 4574 CE2 TYR B 358 -26.546 25.669 65.166 1.00 83.77 C
ANISOU 4574 CE2 TYR B 358 13367 10048 8414 -2091 3835 566 C
ATOM 4575 CZ TYR B 358 -27.303 26.561 65.892 1.00 80.02 C
ANISOU 4575 CZ TYR B 358 12901 9244 8257 -2271 3600 576 C
ATOM 4576 OH TYR B 358 -27.262 26.510 67.270 1.00 75.91 O
ANISOU 4576 OH TYR B 358 11852 8897 8094 -2331 3374 292 O
ATOM 4577 N ASN B 359 -29.216 25.677 58.943 1.00 86.62 N
ANISOU 4577 N ASN B 359 16552 9434 6927 -843 3522 1690 N
ATOM 4578 CA ASN B 359 -29.197 25.307 57.529 1.00 91.36 C
ANISOU 4578 CA ASN B 359 17500 10115 7096 -505 3540 1790 C
ATOM 4579 C ASN B 359 -30.076 26.245 56.691 1.00 88.92 C
ANISOU 4579 C ASN B 359 17717 9411 6658 -385 3381 2016 C
ATOM 4580 O ASN B 359 -29.631 26.754 55.660 1.00 93.17 O
ANISOU 4580 O ASN B 359 18486 9953 6960 -376 3680 2225 O
ATOM 4581 CB ASN B 359 -29.638 23.848 57.359 1.00 87.93 C
ANISOU 4581 CB ASN B 359 17099 9864 6446 -75 3159 1566 C
ATOM 4582 CG ASN B 359 -29.527 23.368 55.922 1.00 87.28 C
ANISOU 4582 CG ASN B 359 17318 9916 5928 286 3178 1611 C
ATOM 4583 OD1 ASN B 359 -28.430 23.170 55.395 1.00 90.55 O
ANISOU 4583 OD1 ASN B 359 17581 10660 6162 254 3579 1633 O
ATOM 4584 ND2 ASN B 359 -30.671 23.222 55.265 1.00 85.90 N
ANISOU 4584 ND2 ASN B 359 17553 9499 5586 631 2744 1605 N
ATOM 4585 N PHE B 360 -31.323 26.491 57.135 1.00 86.63 N
ANISOU 4585 N PHE B 360 17604 8798 6514 -282 2913 1967 N
ATOM 4586 CA PHE B 360 -32.261 27.345 56.386 1.00 90.82 C
ANISOU 4586 CA PHE B 360 18615 8973 6921 -104 2695 2122 C
ATOM 4587 C PHE B 360 -32.111 28.853 56.686 1.00 95.59 C
ANISOU 4587 C PHE B 360 19264 9274 7782 -463 2929 2325 C
ATOM 4588 O PHE B 360 -32.603 29.661 55.894 1.00102.53 O
ANISOU 4588 O PHE B 360 20563 9892 8504 -328 2875 2504 O
ATOM 4589 CB PHE B 360 -33.720 26.921 56.647 1.00 85.20 C
ANISOU 4589 CB PHE B 360 18041 8082 6249 207 2057 1928 C
ATOM 4590 CG PHE B 360 -34.043 25.487 56.243 1.00 85.71 C
ANISOU 4590 CG PHE B 360 18113 8358 6093 588 1755 1711 C
ATOM 4591 CD1 PHE B 360 -34.019 25.087 54.912 1.00 87.86 C
ANISOU 4591 CD1 PHE B 360 18695 8721 5969 937 1753 1736 C
ATOM 4592 CD2 PHE B 360 -34.393 24.548 57.204 1.00 84.56 C
ANISOU 4592 CD2 PHE B 360 17672 8305 6153 600 1462 1475 C
ATOM 4593 CE1 PHE B 360 -34.317 23.772 54.554 1.00 86.89 C
ANISOU 4593 CE1 PHE B 360 18559 8763 5691 1284 1453 1500 C
ATOM 4594 CE2 PHE B 360 -34.692 23.237 56.851 1.00 82.18 C
ANISOU 4594 CE2 PHE B 360 17373 8152 5700 933 1172 1263 C
ATOM 4595 CZ PHE B 360 -34.654 22.850 55.527 1.00 82.99 C
ANISOU 4595 CZ PHE B 360 17762 8327 5442 1273 1160 1261 C
ATOM 4596 N LEU B 361 -31.461 29.253 57.784 1.00 92.39 N
ANISOU 4596 N LEU B 361 18444 8891 7769 -894 3168 2283 N
ATOM 4597 CA LEU B 361 -31.331 30.677 58.101 1.00 94.34 C
ANISOU 4597 CA LEU B 361 18708 8822 8315 -1236 3353 2434 C
ATOM 4598 C LEU B 361 -29.887 31.199 58.070 1.00 95.09 C
ANISOU 4598 C LEU B 361 18528 9047 8555 -1666 3971 2549 C
ATOM 4599 O LEU B 361 -29.669 32.381 58.357 1.00 97.95 O
ANISOU 4599 O LEU B 361 18862 9138 9216 -1989 4147 2656 O
ATOM 4600 CB LEU B 361 -31.978 30.980 59.465 1.00 88.45 C
ANISOU 4600 CB LEU B 361 17709 7903 7994 -1391 3036 2250 C
ATOM 4601 CG LEU B 361 -33.512 30.875 59.534 1.00 82.55 C
ANISOU 4601 CG LEU B 361 17223 6950 7193 -1029 2424 2153 C
ATOM 4602 CD1 LEU B 361 -33.987 31.066 60.951 1.00 77.89 C
ANISOU 4602 CD1 LEU B 361 16294 6275 7026 -1206 2167 1958 C
ATOM 4603 CD2 LEU B 361 -34.191 31.898 58.642 1.00 87.10 C
ANISOU 4603 CD2 LEU B 361 18292 7189 7612 -844 2306 2340 C
ATOM 4604 N SER B 362 -28.913 30.365 57.684 1.00106.26 N
ANISOU 4604 N SER B 362 22992 8649 8733 -751 5457 1095 N
ATOM 4605 CA SER B 362 -27.514 30.780 57.549 1.00106.55 C
ANISOU 4605 CA SER B 362 22885 8629 8969 -513 5751 1151 C
ATOM 4606 C SER B 362 -26.932 30.175 56.275 1.00115.15 C
ANISOU 4606 C SER B 362 24354 9545 9851 -351 5934 1111 C
ATOM 4607 O SER B 362 -26.787 28.947 56.169 1.00114.89 O
ANISOU 4607 O SER B 362 24641 9345 9667 -311 5962 1035 O
ATOM 4608 CB SER B 362 -26.691 30.378 58.777 1.00105.22 C
ANISOU 4608 CB SER B 362 22480 8450 9049 -452 5861 1162 C
ATOM 4609 OG SER B 362 -25.302 30.604 58.588 1.00106.04 O
ANISOU 4609 OG SER B 362 22477 8517 9297 -226 6162 1208 O
ATOM 4610 N GLY B 363 -26.606 31.042 55.313 1.00110.53 N
ANISOU 4610 N GLY B 363 23763 8993 9239 -255 6049 1169 N
ATOM 4611 CA GLY B 363 -26.015 30.600 54.062 1.00113.42 C
ANISOU 4611 CA GLY B 363 24451 9237 9407 -87 6237 1147 C
ATOM 4612 C GLY B 363 -24.617 30.038 54.225 1.00114.58 C
ANISOU 4612 C GLY B 363 24568 9330 9635 135 6535 1157 C
ATOM 4613 O GLY B 363 -24.219 29.143 53.472 1.00117.07 O
ANISOU 4613 O GLY B 363 25233 9513 9735 297 6657 1101 O
ATOM 4614 N LYS B 364 -23.862 30.543 55.212 1.00112.98 N
ANISOU 4614 N LYS B 364 23962 9240 9726 163 6648 1225 N
ATOM 4615 CA LYS B 364 -22.514 30.039 55.466 1.00114.14 C
ANISOU 4615 CA LYS B 364 24040 9380 9950 385 6935 1235 C
ATOM 4616 C LYS B 364 -22.544 28.613 56.025 1.00128.59 C
ANISOU 4616 C LYS B 364 26155 11031 11672 462 6903 1129 C
ATOM 4617 O LYS B 364 -21.744 27.770 55.605 1.00131.08 O
ANISOU 4617 O LYS B 364 26721 11255 11829 705 7096 1085 O
ATOM 4618 CB LYS B 364 -21.751 30.982 56.406 1.00112.44 C
ANISOU 4618 CB LYS B 364 23314 9335 10075 372 7040 1334 C
ATOM 4619 CG LYS B 364 -21.391 32.345 55.788 1.00113.11 C
ANISOU 4619 CG LYS B 364 23170 9570 10235 318 7120 1455 C
ATOM 4620 CD LYS B 364 -20.278 33.044 56.566 1.00112.55 C
ANISOU 4620 CD LYS B 364 22654 9656 10455 341 7293 1552 C
ATOM 4621 CE LYS B 364 -20.281 34.559 56.364 1.00113.20 C
ANISOU 4621 CE LYS B 364 22506 9853 10654 179 7241 1681 C
ATOM 4622 NZ LYS B 364 -20.314 35.023 54.960 1.00116.33 N
ANISOU 4622 NZ LYS B 364 23112 10261 10825 158 7294 1734 N
ATOM 4623 N PHE B 365 -23.460 28.333 56.971 1.00112.18 N
ANISOU 4623 N PHE B 365 24056 8915 9652 259 6650 1091 N
ATOM 4624 CA PHE B 365 -23.646 26.977 57.505 1.00112.61 C
ANISOU 4624 CA PHE B 365 24444 8775 9569 263 6563 999 C
ATOM 4625 C PHE B 365 -24.171 26.029 56.424 1.00120.18 C
ANISOU 4625 C PHE B 365 25984 9527 10151 274 6472 909 C
ATOM 4626 O PHE B 365 -23.691 24.896 56.287 1.00121.93 O
ANISOU 4626 O PHE B 365 26612 9541 10174 457 6547 839 O
ATOM 4627 CB PHE B 365 -24.619 26.995 58.702 1.00112.16 C
ANISOU 4627 CB PHE B 365 24195 8776 9644 -21 6280 996 C
ATOM 4628 CG PHE B 365 -23.960 27.165 60.069 1.00110.12 C
ANISOU 4628 CG PHE B 365 23557 8594 9689 27 6359 1040 C
ATOM 4629 CD1 PHE B 365 -23.227 26.136 60.648 1.00108.74 C
ANISOU 4629 CD1 PHE B 365 23576 8256 9485 191 6474 999 C
ATOM 4630 CD2 PHE B 365 -24.130 28.338 60.796 1.00105.45 C
ANISOU 4630 CD2 PHE B 365 22456 8223 9389 -82 6294 1118 C
ATOM 4631 CE1 PHE B 365 -22.642 26.293 61.903 1.00106.95 C
ANISOU 4631 CE1 PHE B 365 23007 8098 9532 242 6542 1038 C
ATOM 4632 CE2 PHE B 365 -23.549 28.498 62.050 1.00103.50 C
ANISOU 4632 CE2 PHE B 365 21864 8040 9419 -36 6352 1154 C
ATOM 4633 CZ PHE B 365 -22.806 27.474 62.602 1.00104.27 C
ANISOU 4633 CZ PHE B 365 22128 7988 9504 120 6481 1115 C
ATOM 4634 N ARG B 366 -25.176 26.487 55.655 1.00115.31 N
ANISOU 4634 N ARG B 366 25438 8959 9416 94 6294 906 N
ATOM 4635 CA ARG B 366 -25.783 25.715 54.566 1.00119.42 C
ANISOU 4635 CA ARG B 366 26489 9301 9586 75 6179 823 C
ATOM 4636 C ARG B 366 -24.718 25.190 53.599 1.00120.94 C
ANISOU 4636 C ARG B 366 26990 9363 9600 423 6441 798 C
ATOM 4637 O ARG B 366 -24.765 24.027 53.175 1.00123.33 O
ANISOU 4637 O ARG B 366 27814 9425 9620 517 6386 706 O
ATOM 4638 CB ARG B 366 -26.788 26.608 53.810 1.00117.41 C
ANISOU 4638 CB ARG B 366 26159 9179 9272 -104 6018 847 C
ATOM 4639 CG ARG B 366 -27.809 25.874 52.926 1.00119.38 C
ANISOU 4639 CG ARG B 366 26896 9282 9180 -236 5796 758 C
ATOM 4640 CD ARG B 366 -28.777 26.810 52.171 1.00119.12 C
ANISOU 4640 CD ARG B 366 26786 9400 9075 -376 5647 781 C
ATOM 4641 NE ARG B 366 -29.737 27.541 52.992 1.00116.56 N
ANISOU 4641 NE ARG B 366 26111 9299 8878 -633 5428 817 N
ATOM 4642 CZ ARG B 366 -29.759 28.866 53.121 1.00119.46 C
ANISOU 4642 CZ ARG B 366 26102 9865 9423 -618 5454 902 C
ATOM 4643 NH1 ARG B 366 -28.871 29.617 52.484 1.00118.27 N
ANISOU 4643 NH1 ARG B 366 25862 9717 9357 -406 5685 967 N
ATOM 4644 NH2 ARG B 366 -30.679 29.441 53.884 1.00116.79 N
ANISOU 4644 NH2 ARG B 366 25497 9727 9149 -820 5239 926 N
ATOM 4645 N GLU B 367 -23.751 26.055 53.252 1.00121.23 N
ANISOU 4645 N GLU B 367 26705 9574 9784 612 6710 882 N
ATOM 4646 CA GLU B 367 -22.652 25.736 52.337 1.00124.39 C
ANISOU 4646 CA GLU B 367 27268 9964 10032 950 6980 878 C
ATOM 4647 C GLU B 367 -21.785 24.587 52.853 1.00125.85 C
ANISOU 4647 C GLU B 367 27663 10018 10136 1222 7098 807 C
ATOM 4648 O GLU B 367 -21.423 23.678 52.096 1.00132.80 O
ANISOU 4648 O GLU B 367 28965 10760 10733 1480 7145 728 O
ATOM 4649 CB GLU B 367 -21.788 26.990 52.116 1.00124.25 C
ANISOU 4649 CB GLU B 367 26761 10223 10224 1013 7223 1003 C
ATOM 4650 CG GLU B 367 -22.331 27.950 51.053 1.00124.71 C
ANISOU 4650 CG GLU B 367 26797 10368 10218 886 7169 1063 C
ATOM 4651 CD GLU B 367 -21.476 29.195 50.836 1.00129.46 C
ANISOU 4651 CD GLU B 367 26970 11223 10997 900 7384 1200 C
ATOM 4652 OE1 GLU B 367 -21.431 30.064 51.734 1.00128.11 O
ANISOU 4652 OE1 GLU B 367 26396 11170 11111 748 7355 1276 O
ATOM 4653 OE2 GLU B 367 -20.868 29.313 49.749 1.00134.43 O
ANISOU 4653 OE2 GLU B 367 27677 11938 11463 1047 7567 1235 O
ATOM 4654 N GLN B 368 -21.412 24.641 54.137 1.00123.75 N
ANISOU 4654 N GLN B 368 27105 9803 10111 1199 7136 830 N
ATOM 4655 CA GLN B 368 -20.565 23.638 54.769 1.00125.69 C
ANISOU 4655 CA GLN B 368 27515 9942 10299 1474 7238 760 C
ATOM 4656 C GLN B 368 -21.316 22.342 55.056 1.00126.79 C
ANISOU 4656 C GLN B 368 28248 9740 10186 1398 6975 648 C
ATOM 4657 O GLN B 368 -20.697 21.273 55.114 1.00128.06 O
ANISOU 4657 O GLN B 368 28771 9730 10155 1695 7003 553 O
ATOM 4658 CB GLN B 368 -20.038 24.199 56.094 1.00122.93 C
ANISOU 4658 CB GLN B 368 26650 9757 10302 1435 7339 826 C
ATOM 4659 CG GLN B 368 -19.181 25.460 55.973 1.00121.84 C
ANISOU 4659 CG GLN B 368 25922 9948 10425 1481 7582 941 C
ATOM 4660 CD GLN B 368 -17.765 25.232 55.486 1.00124.99 C
ANISOU 4660 CD GLN B 368 26225 10518 10746 1867 7875 921 C
ATOM 4661 OE1 GLN B 368 -17.237 24.122 55.532 1.00127.20 O
ANISOU 4661 OE1 GLN B 368 26797 10694 10838 2175 7907 806 O
ATOM 4662 NE2 GLN B 368 -17.133 26.305 55.025 1.00125.49 N
ANISOU 4662 NE2 GLN B 368 25863 10874 10944 1848 8064 1028 N
ATOM 4663 N PHE B 369 -22.650 22.427 55.156 1.00125.41 N
ANISOU 4663 N PHE B 369 28178 9485 9988 1006 6686 651 N
ATOM 4664 CA PHE B 369 -23.492 21.249 55.334 1.00125.05 C
ANISOU 4664 CA PHE B 369 28699 9133 9680 834 6390 559 C
ATOM 4665 C PHE B 369 -23.675 20.520 54.004 1.00133.37 C
ANISOU 4665 C PHE B 369 30333 9978 10365 971 6319 474 C
ATOM 4666 O PHE B 369 -23.650 19.284 53.968 1.00131.05 O
ANISOU 4666 O PHE B 369 30624 9375 9795 1076 6181 377 O
ATOM 4667 CB PHE B 369 -24.867 21.634 55.925 1.00122.36 C
ANISOU 4667 CB PHE B 369 28156 8878 9457 338 6080 591 C
ATOM 4668 CG PHE B 369 -24.845 22.139 57.375 1.00119.08 C
ANISOU 4668 CG PHE B 369 27223 8638 9384 181 6060 661 C
ATOM 4669 CD1 PHE B 369 -23.749 21.938 58.200 1.00118.78 C
ANISOU 4669 CD1 PHE B 369 27070 8577 9484 434 6267 679 C
ATOM 4670 CD2 PHE B 369 -25.978 22.740 57.926 1.00116.56 C
ANISOU 4670 CD2 PHE B 369 26555 8516 9217 -209 5808 700 C
ATOM 4671 CE1 PHE B 369 -23.757 22.388 59.522 1.00115.85 C
ANISOU 4671 CE1 PHE B 369 26231 8357 9431 291 6230 742 C
ATOM 4672 CE2 PHE B 369 -25.993 23.180 59.248 1.00113.75 C
ANISOU 4672 CE2 PHE B 369 25727 8331 9162 -335 5764 759 C
ATOM 4673 CZ PHE B 369 -24.881 23.003 60.044 1.00113.45 C
ANISOU 4673 CZ PHE B 369 25574 8244 9289 -93 5971 781 C
ATOM 4674 N LYS B 370 -23.843 21.269 52.897 1.00130.65 N
ANISOU 4674 N LYS B 370 29854 9781 10004 983 6391 510 N
ATOM 4675 CA LYS B 370 -23.900 20.663 51.561 1.00132.56 C
ANISOU 4675 CA LYS B 370 30593 9857 9916 1160 6352 440 C
ATOM 4676 C LYS B 370 -22.554 20.046 51.179 1.00135.69 C
ANISOU 4676 C LYS B 370 31145 10223 10187 1671 6575 396 C
ATOM 4677 O LYS B 370 -22.509 18.965 50.580 1.00138.98 O
ANISOU 4677 O LYS B 370 32121 10389 10296 1870 6449 300 O
ATOM 4678 CB LYS B 370 -24.345 21.708 50.520 1.00132.27 C
ANISOU 4678 CB LYS B 370 30331 10017 9909 1061 6389 500 C
ATOM 4679 CG LYS B 370 -24.660 21.176 49.092 1.00136.68 C
ANISOU 4679 CG LYS B 370 31390 10413 10128 1177 6302 434 C
ATOM 4680 CD LYS B 370 -25.638 19.985 49.066 1.00144.24 C
ANISOU 4680 CD LYS B 370 32968 11030 10806 978 5949 326 C
ATOM 4681 CE LYS B 370 -27.108 20.392 49.152 1.00146.26 C
ANISOU 4681 CE LYS B 370 33154 11340 11080 496 5663 328 C
ATOM 4682 NZ LYS B 370 -27.994 19.191 49.251 1.00149.67 N
ANISOU 4682 NZ LYS B 370 34160 11467 11243 245 5311 231 N
ATOM 4683 N ALA B 371 -21.458 20.706 51.581 1.00134.87 N
ANISOU 4683 N ALA B 371 30524 10397 10324 1883 6872 461 N
ATOM 4684 CA ALA B 371 -20.094 20.222 51.372 1.00137.80 C
ANISOU 4684 CA ALA B 371 30881 10861 10618 2373 7085 412 C
ATOM 4685 C ALA B 371 -19.847 18.900 52.092 1.00139.25 C
ANISOU 4685 C ALA B 371 31484 10768 10657 2565 6922 295 C
ATOM 4686 O ALA B 371 -18.975 18.122 51.689 1.00142.78 O
ANISOU 4686 O ALA B 371 32126 11204 10919 3004 6956 206 O
ATOM 4687 CB ALA B 371 -19.098 21.278 51.859 1.00136.27 C
ANISOU 4687 CB ALA B 371 29978 11052 10746 2453 7396 510 C
ATOM 4688 N ALA B 372 -20.551 18.694 53.212 1.00136.67 N
ANISOU 4688 N ALA B 372 31246 10258 10425 2248 6736 296 N
ATOM 4689 CA ALA B 372 -20.472 17.481 54.024 1.00137.80 C
ANISOU 4689 CA ALA B 372 31818 10100 10440 2339 6526 201 C
ATOM 4690 C ALA B 372 -21.247 16.318 53.403 1.00140.70 C
ANISOU 4690 C ALA B 372 32954 10073 10434 2264 6179 120 C
ATOM 4691 O ALA B 372 -20.807 15.166 53.491 1.00143.74 O
ANISOU 4691 O ALA B 372 33762 10234 10621 2543 6008 35 O
ATOM 4692 CB ALA B 372 -20.998 17.776 55.429 1.00134.04 C
ANISOU 4692 CB ALA B 372 31136 9605 10190 1971 6457 248 C
ATOM 4693 N PHE B 373 -22.409 16.593 52.797 1.00140.01 N
ANISOU 4693 N PHE B 373 33035 9911 10253 1884 6031 149 N
ATOM 4694 CA PHE B 373 -23.173 15.555 52.107 1.00150.90 C
ANISOU 4694 CA PHE B 373 35122 10934 11279 1778 5695 83 C
ATOM 4695 C PHE B 373 -22.531 15.199 50.765 1.00155.11 C
ANISOU 4695 C PHE B 373 35869 11475 11590 2233 5764 36 C
ATOM 4696 O PHE B 373 -22.683 14.067 50.294 1.00158.35 O
ANISOU 4696 O PHE B 373 36891 11583 11694 2349 5494 -31 O
ATOM 4697 CB PHE B 373 -24.636 16.005 51.915 1.00141.08 C
ANISOU 4697 CB PHE B 373 33909 9672 10025 1214 5499 112 C
ATOM 4698 CG PHE B 373 -25.454 16.074 53.202 1.00140.24 C
ANISOU 4698 CG PHE B 373 33679 9552 10053 721 5317 135 C
ATOM 4699 CD1 PHE B 373 -25.750 17.300 53.779 1.00135.65 C
ANISOU 4699 CD1 PHE B 373 32387 9341 9812 477 5440 226 C
ATOM 4700 CD2 PHE B 373 -25.861 14.921 53.867 1.00141.69 C
ANISOU 4700 CD2 PHE B 373 34410 9385 10040 513 5002 83 C
ATOM 4701 CE1 PHE B 373 -26.473 17.381 54.962 1.00132.00 C
ANISOU 4701 CE1 PHE B 373 31680 8961 9512 51 5244 263 C
ATOM 4702 CE2 PHE B 373 -26.604 14.999 55.046 1.00137.11 C
ANISOU 4702 CE2 PHE B 373 33612 8884 9598 39 4818 98 C
ATOM 4703 CZ PHE B 373 -26.900 16.231 55.595 1.00133.10 C
ANISOU 4703 CZ PHE B 373 32295 8811 9464 -177 4936 202 C
ATOM 4704 N SER B 374 -21.805 16.151 50.157 1.00155.51 N
ANISOU 4704 N SER B 374 35415 11886 11784 2479 6106 78 N
ATOM 4705 CA SER B 374 -21.045 15.886 48.933 1.00159.01 C
ANISOU 4705 CA SER B 374 35972 12422 12023 2942 6217 30 C
ATOM 4706 C SER B 374 -19.859 14.959 49.208 1.00165.43 C
ANISOU 4706 C SER B 374 36900 13225 12731 3462 6225 -64 C
ATOM 4707 O SER B 374 -19.554 14.078 48.395 1.00173.10 O
ANISOU 4707 O SER B 374 38290 14074 13405 3811 6095 -152 O
ATOM 4708 CB SER B 374 -20.557 17.204 48.322 1.00153.36 C
ANISOU 4708 CB SER B 374 34644 12134 11491 3005 6579 118 C
ATOM 4709 OG SER B 374 -21.624 17.961 47.777 1.00149.35 O
ANISOU 4709 OG SER B 374 34098 11634 11015 2615 6520 184 O
ATOM 4710 N TRP B 375 -19.194 15.156 50.350 1.00164.08 N
ANISOU 4710 N TRP B 375 36344 13197 12801 3531 6355 -53 N
ATOM 4711 CA TRP B 375 -18.084 14.307 50.779 1.00168.45 C
ANISOU 4711 CA TRP B 375 36947 13771 13287 4015 6331 -154 C
ATOM 4712 C TRP B 375 -18.573 12.940 51.259 1.00173.61 C
ANISOU 4712 C TRP B 375 38289 13960 13714 3971 5899 -222 C
ATOM 4713 O TRP B 375 -17.845 11.950 51.145 1.00180.08 O
ANISOU 4713 O TRP B 375 39387 14704 14330 4422 5757 -327 O
ATOM 4714 CB TRP B 375 -17.301 15.021 51.889 1.00166.05 C
ANISOU 4714 CB TRP B 375 35985 13772 13334 4054 6590 -114 C
ATOM 4715 CG TRP B 375 -16.152 14.244 52.478 1.00169.66 C
ANISOU 4715 CG TRP B 375 36401 14296 13764 4535 6560 -225 C
ATOM 4716 CD1 TRP B 375 -14.889 14.122 51.974 1.00174.81 C
ANISOU 4716 CD1 TRP B 375 36798 15286 14335 5076 6735 -314 C
ATOM 4717 CD2 TRP B 375 -16.171 13.490 53.699 1.00169.67 C
ANISOU 4717 CD2 TRP B 375 36604 14053 13811 4513 6322 -266 C
ATOM 4718 NE1 TRP B 375 -14.124 13.331 52.803 1.00177.41 N
ANISOU 4718 NE1 TRP B 375 37156 15593 14658 5414 6609 -419 N
ATOM 4719 CE2 TRP B 375 -14.888 12.931 53.867 1.00174.56 C
ANISOU 4719 CE2 TRP B 375 37084 14861 14378 5077 6351 -384 C
ATOM 4720 CE3 TRP B 375 -17.152 13.229 54.662 1.00167.66 C
ANISOU 4720 CE3 TRP B 375 36622 13464 13617 4059 6076 -216 C
ATOM 4721 CZ2 TRP B 375 -14.562 12.127 54.961 1.00176.03 C
ANISOU 4721 CZ2 TRP B 375 37414 14884 14584 5214 6130 -449 C
ATOM 4722 CZ3 TRP B 375 -16.826 12.431 55.747 1.00169.14 C
ANISOU 4722 CZ3 TRP B 375 36950 13495 13820 4170 5868 -268 C
ATOM 4723 CH2 TRP B 375 -15.542 11.890 55.888 1.00173.03 C
ANISOU 4723 CH2 TRP B 375 37319 14154 14272 4750 5891 -381 C
ATOM 4724 N TRP B 376 -19.801 12.881 51.782 1.00174.38 N
ANISOU 4724 N TRP B 376 38657 13774 13827 3421 5670 -161 N
ATOM 4725 CA TRP B 376 -20.403 11.624 52.220 1.00178.17 C
ANISOU 4725 CA TRP B 376 39801 13826 14068 3256 5229 -192 C
ATOM 4726 C TRP B 376 -20.956 10.829 51.037 1.00183.19 C
ANISOU 4726 C TRP B 376 41078 14195 14333 3279 4955 -228 C
ATOM 4727 O TRP B 376 -20.861 9.598 51.015 1.00187.11 O
ANISOU 4727 O TRP B 376 42133 14408 14552 3453 4623 -286 O
ATOM 4728 CB TRP B 376 -21.508 11.918 53.239 1.00177.71 C
ANISOU 4728 CB TRP B 376 39726 13644 14152 2609 5098 -109 C
ATOM 4729 CG TRP B 376 -22.010 10.728 54.005 1.00183.81 C
ANISOU 4729 CG TRP B 376 41041 14075 14724 2372 4669 -116 C
ATOM 4730 CD1 TRP B 376 -21.497 10.222 55.164 1.00186.16 C
ANISOU 4730 CD1 TRP B 376 41299 14334 15097 2469 4573 -134 C
ATOM 4731 CD2 TRP B 376 -23.144 9.914 53.679 1.00187.07 C
ANISOU 4731 CD2 TRP B 376 42087 14175 14817 1961 4262 -97 C
ATOM 4732 NE1 TRP B 376 -22.233 9.136 55.574 1.00188.65 N
ANISOU 4732 NE1 TRP B 376 42186 14343 15149 2138 4128 -127 N
ATOM 4733 CE2 TRP B 376 -23.250 8.926 54.680 1.00189.45 C
ANISOU 4733 CE2 TRP B 376 42702 14285 14997 1808 3930 -103 C
ATOM 4734 CE3 TRP B 376 -24.075 9.920 52.636 1.00187.94 C
ANISOU 4734 CE3 TRP B 376 42512 14170 14727 1697 4132 -78 C
ATOM 4735 CZ2 TRP B 376 -24.250 7.954 54.667 1.00191.86 C
ANISOU 4735 CZ2 TRP B 376 43609 14321 14970 1373 3477 -88 C
ATOM 4736 CZ3 TRP B 376 -25.067 8.954 52.625 1.00191.07 C
ANISOU 4736 CZ3 TRP B 376 43510 14282 14805 1277 3686 -60 C
ATOM 4737 CH2 TRP B 376 -25.147 7.985 53.633 1.00193.11 C
ANISOU 4737 CH2 TRP B 376 44056 14387 14929 1106 3364 -65 C
ATOM 4738 N LEU B 377 -21.528 11.529 50.057 1.00182.29 N
ANISOU 4738 N LEU B 377 40884 14169 14207 3109 5073 -194 N
ATOM 4739 CA LEU B 377 -22.070 10.938 48.831 1.00184.32 C
ANISOU 4739 CA LEU B 377 41682 14210 14140 3131 4849 -226 C
ATOM 4740 C LEU B 377 -21.368 11.532 47.611 1.00182.69 C
ANISOU 4740 C LEU B 377 41191 14307 13916 3553 5158 -258 C
ATOM 4741 O LEU B 377 -20.933 10.810 46.714 1.00183.92 O
ANISOU 4741 O LEU B 377 41691 14391 13799 3966 5062 -338 O
ATOM 4742 CB LEU B 377 -23.584 11.177 48.733 1.00181.70 C
ANISOU 4742 CB LEU B 377 41556 13703 13778 2471 4644 -161 C
ATOM 4743 CG LEU B 377 -24.314 10.770 47.444 1.00182.26 C
ANISOU 4743 CG LEU B 377 42112 13580 13559 2402 4426 -184 C
ATOM 4744 CD1 LEU B 377 -24.454 9.262 47.332 1.00185.01 C
ANISOU 4744 CD1 LEU B 377 43216 13532 13548 2478 3990 -223 C
ATOM 4745 CD2 LEU B 377 -25.681 11.430 47.359 1.00178.21 C
ANISOU 4745 CD2 LEU B 377 41529 13062 13119 1775 4339 -131 C
TER 4746 LEU B 377
HETATM 4747 C1 NVH A 401 -35.717 47.186 92.153 1.00117.36 C
HETATM 4748 C10 NVH A 401 -35.454 51.591 94.693 1.00111.93 C
HETATM 4749 C11 NVH A 401 -36.746 52.112 94.466 1.00110.76 C
HETATM 4750 C12 NVH A 401 -36.009 47.565 96.989 1.00108.32 C
HETATM 4751 C13 NVH A 401 -33.246 44.194 97.150 0.00 98.34 C
HETATM 4752 C14 NVH A 401 -32.753 45.508 97.163 1.00 99.12 C
HETATM 4753 C15 NVH A 401 -33.643 46.590 97.112 0.43101.93 C
HETATM 4754 C16 NVH A 401 -35.043 46.369 97.062 0.00102.74 C
HETATM 4755 C17 NVH A 401 -35.521 45.042 97.031 1.00 98.03 C
HETATM 4756 C18 NVH A 401 -34.629 43.961 97.083 0.59 98.01 C
HETATM 4757 C19 NVH A 401 -31.873 54.252 95.084 1.00106.10 C
HETATM 4758 C2 NVH A 401 -36.270 45.915 92.293 1.00116.84 C
HETATM 4759 C3 NVH A 401 -36.581 45.465 93.572 1.00117.88 C
HETATM 4760 C4 NVH A 401 -35.842 47.454 94.562 1.00117.87 C
HETATM 4761 C5 NVH A 401 -35.112 49.510 95.818 1.00115.48 C
HETATM 4762 C6 NVH A 401 -35.509 47.954 93.294 1.00118.84 C
HETATM 4763 C7 NVH A 401 -36.038 54.270 94.836 1.00110.48 C
HETATM 4764 C8 NVH A 401 -34.728 53.829 95.060 1.00109.91 C
HETATM 4765 C9 NVH A 401 -34.415 52.475 94.990 1.00110.28 C
HETATM 4766 F1 NVH A 401 -32.385 43.155 97.201 1.00 97.80 F
HETATM 4767 F2 NVH A 401 -33.140 47.842 97.127 0.93104.25 F
HETATM 4768 F3 NVH A 401 -36.837 44.799 96.971 0.99 96.01 F
HETATM 4769 N1 NVH A 401 -36.371 46.210 94.673 1.00119.42 N
HETATM 4770 N2 NVH A 401 -37.049 53.429 94.538 1.00110.77 N
HETATM 4771 N3 NVH A 401 -35.641 48.249 95.759 1.00114.23 N
HETATM 4772 N4 NVH A 401 -35.243 50.217 94.587 1.00116.49 N
HETATM 4773 O1 NVH A 401 -34.943 50.147 96.856 1.00112.93 O
HETATM 4774 O2 NVH A 401 -35.562 50.282 92.115 1.00124.12 O
HETATM 4775 O3 NVH A 401 -33.382 49.361 93.121 1.00121.33 O
HETATM 4776 O4 NVH A 401 -33.668 56.155 94.547 1.00104.22 O
HETATM 4777 O5 NVH A 401 -33.650 55.211 96.862 1.00105.30 O
HETATM 4778 S1 NVH A 401 -34.826 49.526 93.127 1.00120.92 S
HETATM 4779 S2 NVH A 401 -33.492 55.021 95.436 1.00105.10 S
HETATM 4780 S SO4 A 402 -5.822 28.605 97.073 1.00115.57 S
HETATM 4781 O1 SO4 A 402 -5.956 27.482 96.148 1.00115.82 O
HETATM 4782 O2 SO4 A 402 -6.022 29.857 96.345 1.00112.67 O
HETATM 4783 O3 SO4 A 402 -4.491 28.592 97.670 1.00121.59 O
HETATM 4784 O4 SO4 A 402 -6.799 28.474 98.149 1.00113.21 O
HETATM 4785 S SO4 A 403 -5.220 36.727 106.004 1.00152.02 S
HETATM 4786 O1 SO4 A 403 -4.937 36.974 104.592 1.00152.19 O
HETATM 4787 O2 SO4 A 403 -6.592 36.249 106.158 1.00152.28 O
HETATM 4788 O3 SO4 A 403 -5.060 37.967 106.755 1.00152.24 O
HETATM 4789 O4 SO4 A 403 -4.289 35.734 106.530 1.00153.84 O
HETATM 4790 CAD PGW A 404 -41.593 52.372 78.463 1.00119.58 C
HETATM 4791 OAE PGW A 404 -43.006 52.413 78.239 1.00121.26 O
HETATM 4792 OAF PGW A 404 -41.183 50.022 78.882 1.00118.75 O
HETATM 4793 P PGW A 404 -37.807 50.199 75.790 1.00120.20 P
HETATM 4794 C01 PGW A 404 -38.347 46.749 78.198 1.00 94.25 C
HETATM 4795 C1 PGW A 404 -35.010 45.783 78.209 1.00 91.84 C
HETATM 4796 O01 PGW A 404 -36.055 46.487 77.477 1.00 93.23 O
HETATM 4797 C02 PGW A 404 -36.918 47.285 78.286 1.00 95.33 C
HETATM 4798 C2 PGW A 404 -33.638 45.649 77.599 1.00 85.28 C
HETATM 4799 O02 PGW A 404 -35.250 45.281 79.295 1.00 96.31 O
HETATM 4800 C03 PGW A 404 -36.853 48.741 77.817 1.00105.98 C
HETATM 4801 C3 PGW A 404 -33.207 44.190 77.650 1.00 79.79 C
HETATM 4802 O03 PGW A 404 -39.103 47.349 79.249 1.00 96.23 O
HETATM 4803 C04 PGW A 404 -39.580 51.244 77.518 1.00120.30 C
HETATM 4804 C4 PGW A 404 -32.196 44.013 78.772 1.00 77.38 C
HETATM 4805 O04 PGW A 404 -41.343 46.941 79.588 1.00 96.95 O
HETATM 4806 C05 PGW A 404 -41.047 51.063 77.903 1.00119.31 C
HETATM 4807 C5 PGW A 404 -30.909 43.392 78.250 1.00 76.48 C
HETATM 4808 C06 PGW A 404 -29.017 37.692 80.263 1.00 70.95 C
HETATM 4809 C6 PGW A 404 -30.982 41.877 78.358 1.00 76.15 C
HETATM 4810 C07 PGW A 404 -29.645 36.519 81.008 1.00 77.80 C
HETATM 4811 C7 PGW A 404 -29.841 41.225 77.590 1.00 75.13 C
HETATM 4812 C08 PGW A 404 -28.945 36.175 82.315 1.00 82.75 C
HETATM 4813 C8 PGW A 404 -29.215 40.137 78.456 1.00 73.45 C
HETATM 4814 C09 PGW A 404 -29.992 35.650 83.294 1.00 87.87 C
HETATM 4815 C9 PGW A 404 -29.850 38.803 78.148 1.00 71.93 C
HETATM 4816 C10 PGW A 404 -29.739 37.734 78.937 1.00 70.68 C
HETATM 4817 C11 PGW A 404 -29.518 35.698 84.743 1.00 88.46 C
HETATM 4818 O11 PGW A 404 -37.237 48.835 76.442 1.00116.44 O
HETATM 4819 C12 PGW A 404 -30.494 35.010 85.699 1.00 88.37 C
HETATM 4820 O12 PGW A 404 -39.256 50.296 76.499 1.00121.03 O
HETATM 4821 C13 PGW A 404 -30.785 33.546 85.363 1.00 89.19 C
HETATM 4822 O13 PGW A 404 -38.025 49.954 74.315 1.00120.02 O
HETATM 4823 C14 PGW A 404 -29.584 32.644 85.557 1.00 90.89 C
HETATM 4824 O14 PGW A 404 -36.939 51.350 76.241 1.00120.84 O
HETATM 4825 C15 PGW A 404 -39.082 37.914 83.669 1.00 54.15 C
HETATM 4826 C16 PGW A 404 -37.825 38.786 83.643 1.00 48.27 C
HETATM 4827 C17 PGW A 404 -36.752 38.361 84.649 1.00 48.25 C
HETATM 4828 C18 PGW A 404 -36.499 39.466 85.675 1.00 49.32 C
HETATM 4829 C19 PGW A 404 -40.201 46.666 79.920 1.00 92.68 C
HETATM 4830 C20 PGW A 404 -39.892 45.630 80.989 1.00 83.39 C
HETATM 4831 C21 PGW A 404 -41.042 45.360 81.960 1.00 75.24 C
HETATM 4832 C22 PGW A 404 -40.764 44.117 82.812 1.00 69.35 C
HETATM 4833 C23 PGW A 404 -41.565 42.903 82.339 1.00 65.07 C
HETATM 4834 C24 PGW A 404 -41.516 41.737 83.329 1.00 64.48 C
HETATM 4835 C25 PGW A 404 -41.784 40.404 82.626 1.00 65.47 C
HETATM 4836 C26 PGW A 404 -41.246 39.205 83.412 1.00 67.87 C
HETATM 4837 C27 PGW A 404 -40.142 38.427 82.690 1.00 60.94 C
HETATM 4838 C28 PGW A 404 -35.337 39.173 86.626 1.00 50.24 C
HETATM 4839 C29 PGW A 404 -33.318 40.219 87.756 1.00 41.39 C
HETATM 4840 C30 PGW A 404 -34.350 40.340 86.652 1.00 44.41 C
HETATM 4841 C1 SOG A 405 -33.857 68.556 90.572 1.00126.22 C
HETATM 4842 C2 SOG A 405 -33.553 68.796 89.090 1.00124.57 C
HETATM 4843 C3 SOG A 405 -32.315 68.024 88.626 1.00126.13 C
HETATM 4844 C4 SOG A 405 -31.136 68.186 89.586 1.00127.99 C
HETATM 4845 C5 SOG A 405 -31.588 67.855 91.008 1.00125.66 C
HETATM 4846 C6 SOG A 405 -30.449 67.966 92.024 1.00123.79 C
HETATM 4847 C1' SOG A 405 -36.617 68.864 90.808 1.00128.59 C
HETATM 4848 C2' SOG A 405 -37.765 69.871 90.862 1.00127.29 C
HETATM 4849 C3' SOG A 405 -38.558 69.881 89.559 1.00126.87 C
HETATM 4850 C4' SOG A 405 -38.698 71.289 88.988 1.00126.98 C
HETATM 4851 C5' SOG A 405 -40.020 71.435 88.241 1.00126.92 C
HETATM 4852 C6' SOG A 405 -39.870 72.274 86.977 1.00127.15 C
HETATM 4853 C7' SOG A 405 -41.193 72.360 86.223 1.00126.39 C
HETATM 4854 C8' SOG A 405 -41.190 73.520 85.251 1.00125.63 C
HETATM 4855 S1 SOG A 405 -35.094 69.693 91.141 1.00129.12 S
HETATM 4856 O2 SOG A 405 -34.677 68.401 88.288 1.00122.71 O
HETATM 4857 O3 SOG A 405 -31.941 68.436 87.302 1.00125.20 O
HETATM 4858 O4 SOG A 405 -30.064 67.319 89.184 1.00131.08 O
HETATM 4859 O5 SOG A 405 -32.674 68.717 91.372 1.00125.52 O
HETATM 4860 O6 SOG A 405 -29.736 66.723 92.075 1.00123.00 O
HETATM 4861 C1 SOG A 406 -15.864 34.762 82.862 1.00124.81 C
HETATM 4862 C2 SOG A 406 -14.467 34.251 82.477 1.00123.09 C
HETATM 4863 C3 SOG A 406 -13.628 35.298 81.742 1.00121.44 C
HETATM 4864 C4 SOG A 406 -14.423 35.955 80.617 1.00119.99 C
HETATM 4865 C5 SOG A 406 -15.746 36.486 81.171 1.00119.80 C
HETATM 4866 C6 SOG A 406 -16.578 37.211 80.108 1.00118.39 C
HETATM 4867 C1' SOG A 406 -18.498 33.880 83.490 1.00121.26 C
HETATM 4868 C2' SOG A 406 -19.290 32.814 84.251 1.00117.21 C
HETATM 4869 C3' SOG A 406 -20.734 32.701 83.766 1.00115.87 C
HETATM 4870 C4' SOG A 406 -21.709 32.815 84.936 1.00116.87 C
HETATM 4871 C5' SOG A 406 -22.988 33.577 84.585 1.00114.71 C
HETATM 4872 C6' SOG A 406 -23.597 34.240 85.819 1.00112.16 C
HETATM 4873 C7' SOG A 406 -25.038 33.798 86.055 1.00111.99 C
HETATM 4874 C8' SOG A 406 -26.019 34.725 85.370 1.00113.23 C
HETATM 4875 S1 SOG A 406 -16.808 33.367 83.426 1.00125.54 S
HETATM 4876 O2 SOG A 406 -13.747 33.789 83.635 1.00123.30 O
HETATM 4877 O3 SOG A 406 -12.443 34.686 81.210 1.00121.89 O
HETATM 4878 O4 SOG A 406 -13.646 37.018 80.045 1.00121.45 O
HETATM 4879 O5 SOG A 406 -16.496 35.402 81.742 1.00123.41 O
HETATM 4880 O6 SOG A 406 -16.020 38.504 79.838 1.00117.46 O
HETATM 4881 C1 SOG A 407 -44.499 47.781 80.790 1.00150.35 C
HETATM 4882 C2 SOG A 407 -45.626 47.246 81.666 1.00149.90 C
HETATM 4883 C3 SOG A 407 -45.669 45.718 81.716 1.00149.23 C
HETATM 4884 C4 SOG A 407 -45.470 45.048 80.355 1.00148.87 C
HETATM 4885 C5 SOG A 407 -44.390 45.733 79.513 1.00150.16 C
HETATM 4886 C6 SOG A 407 -44.394 45.215 78.073 1.00149.27 C
HETATM 4887 C1' SOG A 407 -43.428 50.194 81.626 1.00148.94 C
HETATM 4888 C2' SOG A 407 -43.933 51.481 82.275 1.00148.87 C
HETATM 4889 C3' SOG A 407 -43.253 52.724 81.712 1.00149.61 C
HETATM 4890 C4' SOG A 407 -44.267 53.849 81.526 1.00151.23 C
HETATM 4891 C5' SOG A 407 -43.846 54.801 80.409 1.00152.26 C
HETATM 4892 C6' SOG A 407 -44.430 56.197 80.605 1.00151.89 C
HETATM 4893 C7' SOG A 407 -43.483 57.263 80.059 1.00150.59 C
HETATM 4894 C8' SOG A 407 -43.909 58.655 80.475 1.00149.30 C
HETATM 4895 S1 SOG A 407 -44.711 49.530 80.611 1.00149.28 S
HETATM 4896 O2 SOG A 407 -45.474 47.760 82.997 1.00150.29 O
HETATM 4897 O3 SOG A 407 -46.941 45.324 82.252 1.00148.64 O
HETATM 4898 O4 SOG A 407 -45.106 43.673 80.566 1.00147.46 O
HETATM 4899 O5 SOG A 407 -44.548 47.158 79.503 1.00151.80 O
HETATM 4900 O6 SOG A 407 -43.257 44.369 77.860 1.00149.40 O
HETATM 4901 C1 SOG A 408 -49.758 34.780 95.653 1.00105.77 C
HETATM 4902 C2 SOG A 408 -50.207 35.240 94.260 1.00101.64 C
HETATM 4903 C3 SOG A 408 -50.959 36.572 94.329 1.00 97.93 C
HETATM 4904 C4 SOG A 408 -52.054 36.553 95.393 1.00 95.68 C
HETATM 4905 C5 SOG A 408 -51.483 36.053 96.720 1.00 98.69 C
HETATM 4906 C6 SOG A 408 -52.542 36.076 97.826 1.00 94.01 C
HETATM 4907 C1' SOG A 408 -49.927 32.004 96.180 1.00110.84 C
HETATM 4908 C2' SOG A 408 -49.168 31.003 97.054 1.00106.35 C
HETATM 4909 C3' SOG A 408 -49.715 30.989 98.481 1.00101.91 C
HETATM 4910 C4' SOG A 408 -48.950 30.026 99.389 1.00 97.68 C
HETATM 4911 C5' SOG A 408 -47.877 30.733 100.214 1.00 92.01 C
HETATM 4912 C6' SOG A 408 -46.458 30.320 99.822 1.00 86.81 C
HETATM 4913 C7' SOG A 408 -45.828 31.321 98.857 1.00 86.24 C
HETATM 4914 C8' SOG A 408 -44.416 31.701 99.258 1.00 86.86 C
HETATM 4915 S1 SOG A 408 -48.850 33.247 95.535 1.00111.94 S
HETATM 4916 O2 SOG A 408 -49.063 35.385 93.406 1.00103.12 O
HETATM 4917 O3 SOG A 408 -51.535 36.878 93.053 1.00100.36 O
HETATM 4918 O4 SOG A 408 -52.605 37.870 95.552 1.00 93.28 O
HETATM 4919 O5 SOG A 408 -50.894 34.748 96.543 1.00103.33 O
HETATM 4920 O6 SOG A 408 -52.678 37.419 98.313 1.00 91.40 O
HETATM 4921 O1 PG4 A 409 -48.595 51.784 96.566 1.00107.61 O
HETATM 4922 C1 PG4 A 409 -47.558 50.822 96.344 1.00105.49 C
HETATM 4923 C2 PG4 A 409 -46.339 51.516 95.749 1.00102.38 C
HETATM 4924 O2 PG4 A 409 -46.152 52.768 96.402 1.00102.28 O
HETATM 4925 C3 PG4 A 409 -44.779 53.152 96.400 1.00101.95 C
HETATM 4926 C4 PG4 A 409 -44.568 54.211 97.472 1.00102.09 C
HETATM 4927 O3 PG4 A 409 -45.203 53.736 98.653 1.00103.25 O
HETATM 4928 C5 PG4 A 409 -44.817 54.465 99.811 1.00104.19 C
HETATM 4929 C6 PG4 A 409 -45.002 53.560 101.021 1.00104.94 C
HETATM 4930 O4 PG4 A 409 -44.505 52.257 100.719 1.00104.21 O
HETATM 4931 C7 PG4 A 409 -43.187 52.359 100.191 1.00102.11 C
HETATM 4932 C8 PG4 A 409 -42.196 52.329 101.345 1.00 99.57 C
HETATM 4933 O5 PG4 A 409 -42.673 53.190 102.385 1.00 98.42 O
HETATM 4934 C1 NVH B 401 -34.302 18.640 87.220 0.81135.03 C
HETATM 4935 C10 NVH B 401 -34.564 14.295 84.815 0.81137.46 C
HETATM 4936 C11 NVH B 401 -35.186 13.582 85.877 0.81136.51 C
HETATM 4937 C12 NVH B 401 -37.598 17.619 83.827 0.81135.83 C
HETATM 4938 C13 NVH B 401 -36.144 21.401 82.133 0.81134.25 C
HETATM 4939 C14 NVH B 401 -35.660 20.178 81.653 0.81135.66 C
HETATM 4940 C15 NVH B 401 -36.121 18.973 82.201 0.81137.28 C
HETATM 4941 C16 NVH B 401 -37.125 18.962 83.209 0.81137.00 C
HETATM 4942 C17 NVH B 401 -37.575 20.214 83.696 0.81136.30 C
HETATM 4943 C18 NVH B 401 -37.097 21.417 83.156 0.81135.13 C
HETATM 4944 C19 NVH B 401 -31.800 12.382 81.994 0.81129.09 C
HETATM 4945 C2 NVH B 401 -35.190 19.612 87.687 0.81134.19 C
HETATM 4946 C3 NVH B 401 -36.402 19.756 87.030 0.81134.89 C
HETATM 4947 C4 NVH B 401 -35.886 18.041 85.501 0.81135.65 C
HETATM 4948 C5 NVH B 401 -35.552 16.240 83.812 0.81137.59 C
HETATM 4949 C6 NVH B 401 -34.647 17.837 86.132 0.81135.84 C
HETATM 4950 C7 NVH B 401 -34.489 11.538 85.051 0.81133.52 C
HETATM 4951 C8 NVH B 401 -33.840 12.170 83.979 0.81134.02 C
HETATM 4952 C9 NVH B 401 -33.865 13.561 83.855 0.81136.32 C
HETATM 4953 F1 NVH B 401 -35.696 22.565 81.612 0.81132.49 F
HETATM 4954 F2 NVH B 401 -35.621 17.832 81.681 0.81138.15 F
HETATM 4955 F3 NVH B 401 -38.489 20.279 84.682 0.81136.25 F
HETATM 4956 N1 NVH B 401 -36.731 18.978 85.991 0.81135.68 N
HETATM 4957 N2 NVH B 401 -35.160 12.227 86.005 0.81134.61 N
HETATM 4958 N3 NVH B 401 -36.310 17.219 84.392 0.81135.97 N
HETATM 4959 N4 NVH B 401 -34.657 15.695 84.789 0.81138.38 N
HETATM 4960 O1 NVH B 401 -35.903 15.582 82.831 0.81136.51 O
HETATM 4961 O2 NVH B 401 -33.024 15.862 86.704 0.81137.72 O
HETATM 4962 O3 NVH B 401 -32.663 17.270 84.552 0.81134.12 O
HETATM 4963 O4 NVH B 401 -32.205 10.147 83.404 0.81131.36 O
HETATM 4964 O5 NVH B 401 -34.007 10.849 81.787 0.81129.09 O
HETATM 4965 S1 NVH B 401 -33.517 16.644 85.566 0.81136.36 S
HETATM 4966 S2 NVH B 401 -32.982 11.214 82.765 0.81130.03 S
HETATM 4967 S SO4 B 402 -20.527 42.600 64.908 1.00101.97 S
HETATM 4968 O1 SO4 B 402 -21.672 42.443 64.010 1.00100.87 O
HETATM 4969 O2 SO4 B 402 -19.460 41.685 64.513 1.00104.21 O
HETATM 4970 O3 SO4 B 402 -20.916 42.293 66.278 1.00100.14 O
HETATM 4971 O4 SO4 B 402 -20.045 43.978 64.872 1.00104.18 O
HETATM 4972 S SO4 B 403 -24.726 34.302 56.947 1.00134.34 S
HETATM 4973 O1 SO4 B 403 -25.796 33.432 56.471 1.00131.69 O
HETATM 4974 O2 SO4 B 403 -23.879 34.664 55.814 1.00134.65 O
HETATM 4975 O3 SO4 B 403 -25.311 35.506 57.530 1.00134.69 O
HETATM 4976 O4 SO4 B 403 -23.933 33.600 57.955 1.00135.27 O
HETATM 4977 CAD PGW B 404 -27.317 15.242 102.681 1.00114.28 C
HETATM 4978 OAE PGW B 404 -27.663 14.255 103.662 1.00112.22 O
HETATM 4979 OAF PGW B 404 -27.221 17.223 104.064 1.00116.64 O
HETATM 4980 P PGW B 404 -23.327 16.904 100.888 1.00115.85 P
HETATM 4981 C01 PGW B 404 -26.705 19.163 99.376 1.00 87.79 C
HETATM 4982 C1 PGW B 404 -24.311 20.687 97.212 1.00 80.16 C
HETATM 4983 O01 PGW B 404 -24.663 20.100 98.497 1.00 84.96 O
HETATM 4984 C02 PGW B 404 -25.539 18.976 98.411 1.00 90.61 C
HETATM 4985 C2 PGW B 404 -23.093 21.569 97.092 1.00 74.59 C
HETATM 4986 O02 PGW B 404 -25.010 20.478 96.234 1.00 87.72 O
HETATM 4987 C03 PGW B 404 -24.775 17.713 98.793 1.00102.83 C
HETATM 4988 C3 PGW B 404 -23.469 22.772 96.238 1.00 72.72 C
HETATM 4989 O03 PGW B 404 -27.925 18.796 98.733 1.00 90.54 O
HETATM 4990 C04 PGW B 404 -25.647 17.087 102.233 1.00118.34 C
HETATM 4991 C4 PGW B 404 -22.547 22.915 95.036 1.00 71.10 C
HETATM 4992 O04 PGW B 404 -29.274 17.576 100.167 1.00 93.52 O
HETATM 4993 C05 PGW B 404 -26.418 16.308 103.305 1.00117.20 C
HETATM 4994 C5 PGW B 404 -21.824 24.252 95.110 1.00 70.11 C
HETATM 4995 C06 PGW B 404 -23.520 29.528 92.373 1.00 73.78 C
HETATM 4996 C6 PGW B 404 -22.226 25.171 93.966 1.00 68.82 C
HETATM 4997 C07 PGW B 404 -24.173 30.874 92.060 1.00 77.71 C
HETATM 4998 C7 PGW B 404 -21.391 26.446 93.996 1.00 67.32 C
HETATM 4999 C08 PGW B 404 -24.443 31.040 90.565 1.00 78.37 C
HETATM 5000 C8 PGW B 404 -22.251 27.647 94.374 1.00 68.69 C
HETATM 5001 C09 PGW B 404 -25.514 32.097 90.302 1.00 79.71 C
HETATM 5002 C9 PGW B 404 -21.596 28.918 93.882 1.00 69.72 C
HETATM 5003 C10 PGW B 404 -22.158 29.747 92.995 1.00 70.54 C
HETATM 5004 C11 PGW B 404 -26.893 31.488 90.053 1.00 82.88 C
HETATM 5005 O11 PGW B 404 -23.916 18.025 99.890 1.00112.96 O
HETATM 5006 C12 PGW B 404 -28.001 32.504 90.325 1.00 88.24 C
HETATM 5007 O12 PGW B 404 -24.634 16.282 101.618 1.00117.92 O
HETATM 5008 C13 PGW B 404 -28.629 33.055 89.046 1.00 91.60 C
HETATM 5009 O13 PGW B 404 -22.693 15.818 100.050 1.00117.10 O
HETATM 5010 C14 PGW B 404 -28.050 34.394 88.637 1.00 91.91 C
HETATM 5011 O14 PGW B 404 -22.493 17.626 101.920 1.00113.10 O
HETATM 5012 C15 PGW B 404 -31.565 26.889 96.812 1.00 60.77 C
HETATM 5013 C16 PGW B 404 -31.801 27.317 95.369 1.00 55.07 C
HETATM 5014 C17 PGW B 404 -31.266 26.291 94.378 1.00 51.99 C
HETATM 5015 C18 PGW B 404 -31.202 26.900 92.982 1.00 53.37 C
HETATM 5016 C19 PGW B 404 -29.141 18.597 99.508 1.00 90.63 C
HETATM 5017 C20 PGW B 404 -30.210 19.667 99.528 1.00 83.45 C
HETATM 5018 C21 PGW B 404 -30.480 20.232 98.136 1.00 74.56 C
HETATM 5019 C22 PGW B 404 -31.888 20.819 98.073 1.00 70.08 C
HETATM 5020 C23 PGW B 404 -31.865 22.329 97.860 1.00 66.90 C
HETATM 5021 C24 PGW B 404 -32.865 23.030 98.776 1.00 66.79 C
HETATM 5022 C25 PGW B 404 -33.476 24.262 98.112 1.00 68.51 C
HETATM 5023 C26 PGW B 404 -32.779 25.548 98.553 1.00 71.60 C
HETATM 5024 C27 PGW B 404 -32.895 26.670 97.524 1.00 67.47 C
HETATM 5025 C28 PGW B 404 -31.356 25.836 91.901 1.00 54.31 C
HETATM 5026 C29 PGW B 404 -30.520 25.389 89.575 1.00 52.67 C
HETATM 5027 C30 PGW B 404 -31.092 26.425 90.519 1.00 53.75 C
HETATM 5028 C1 SOG B 405 -24.291 -0.120 84.367 1.00 97.09 C
HETATM 5029 C2 SOG B 405 -24.463 -1.165 85.465 1.00 90.79 C
HETATM 5030 C3 SOG B 405 -24.017 -0.591 86.807 1.00 91.07 C
HETATM 5031 C4 SOG B 405 -22.631 0.055 86.736 1.00 97.49 C
HETATM 5032 C5 SOG B 405 -22.441 0.914 85.478 1.00100.15 C
HETATM 5033 C6 SOG B 405 -20.978 1.316 85.282 1.00100.45 C
HETATM 5034 C1' SOG B 405 -24.422 0.536 81.711 1.00100.13 C
HETATM 5035 C2' SOG B 405 -25.620 0.930 80.852 1.00 98.44 C
HETATM 5036 C3' SOG B 405 -25.270 2.059 79.888 1.00 95.68 C
HETATM 5037 C4' SOG B 405 -25.708 3.416 80.429 1.00 96.99 C
HETATM 5038 C5' SOG B 405 -25.160 4.538 79.552 1.00 98.72 C
HETATM 5039 C6' SOG B 405 -26.101 5.736 79.464 1.00 97.90 C
HETATM 5040 C7' SOG B 405 -26.956 5.689 78.202 1.00 97.20 C
HETATM 5041 C8' SOG B 405 -28.336 5.157 78.517 1.00 97.70 C
HETATM 5042 S1 SOG B 405 -24.876 -0.759 82.821 1.00 99.43 S
HETATM 5043 O2 SOG B 405 -25.841 -1.545 85.557 1.00 88.42 O
HETATM 5044 O3 SOG B 405 -24.050 -1.617 87.812 1.00 88.22 O
HETATM 5045 O4 SOG B 405 -22.458 0.883 87.896 1.00 99.34 O
HETATM 5046 O5 SOG B 405 -22.911 0.246 84.298 1.00100.71 O
HETATM 5047 O6 SOG B 405 -20.688 2.469 86.082 1.00102.21 O
HETATM 5048 C1 SOG B 406 -33.007 -11.671 86.639 1.00 71.53 C
HETATM 5049 C2 SOG B 406 -33.079 -10.256 87.210 1.00 70.64 C
HETATM 5050 C3 SOG B 406 -31.725 -9.557 87.136 1.00 75.13 C
HETATM 5051 C4 SOG B 406 -30.578 -10.427 87.654 1.00 79.32 C
HETATM 5052 C5 SOG B 406 -30.656 -11.864 87.132 1.00 75.12 C
HETATM 5053 C6 SOG B 406 -29.640 -12.766 87.836 1.00 77.10 C
HETATM 5054 C1' SOG B 406 -34.835 -12.658 88.523 1.00 64.38 C
HETATM 5055 C2' SOG B 406 -36.257 -13.152 88.773 1.00 59.17 C
HETATM 5056 C3' SOG B 406 -36.799 -12.525 90.050 1.00 56.37 C
HETATM 5057 C4' SOG B 406 -38.308 -12.699 90.141 1.00 55.97 C
HETATM 5058 C5' SOG B 406 -39.012 -11.348 90.150 1.00 59.88 C
HETATM 5059 C6' SOG B 406 -39.309 -10.889 91.572 1.00 57.10 C
HETATM 5060 C7' SOG B 406 -40.806 -10.682 91.773 1.00 57.98 C
HETATM 5061 C8' SOG B 406 -41.388 -11.794 92.617 1.00 60.59 C
HETATM 5062 S1 SOG B 406 -34.585 -12.476 86.786 1.00 69.86 S
HETATM 5063 O2 SOG B 406 -34.014 -9.494 86.439 1.00 62.53 O
HETATM 5064 O3 SOG B 406 -31.800 -8.323 87.868 1.00 77.02 O
HETATM 5065 O4 SOG B 406 -29.336 -9.852 87.224 1.00 88.09 O
HETATM 5066 O5 SOG B 406 -31.971 -12.414 87.292 1.00 73.76 O
HETATM 5067 O6 SOG B 406 -30.303 -13.616 88.782 1.00 83.51 O
HETATM 5068 C1 SOG B 407 -40.300 22.576 107.446 1.00123.21 C
HETATM 5069 C2 SOG B 407 -40.959 23.937 107.658 1.00123.56 C
HETATM 5070 C3 SOG B 407 -42.484 23.832 107.689 1.00124.68 C
HETATM 5071 C4 SOG B 407 -43.017 23.026 106.509 1.00122.39 C
HETATM 5072 C5 SOG B 407 -42.304 21.677 106.405 1.00121.35 C
HETATM 5073 C6 SOG B 407 -42.749 20.894 105.169 1.00121.00 C
HETATM 5074 C1' SOG B 407 -37.883 22.305 108.678 1.00124.41 C
HETATM 5075 C2' SOG B 407 -36.662 21.417 108.455 1.00122.22 C
HETATM 5076 C3' SOG B 407 -35.354 22.201 108.498 1.00119.64 C
HETATM 5077 C4' SOG B 407 -34.685 22.261 107.127 1.00118.43 C
HETATM 5078 C5' SOG B 407 -33.215 21.854 107.215 1.00117.64 C
HETATM 5079 C6' SOG B 407 -32.281 22.942 106.691 1.00114.64 C
HETATM 5080 C7' SOG B 407 -31.218 23.315 107.721 1.00110.91 C
HETATM 5081 C8' SOG B 407 -29.869 22.710 107.393 1.00109.36 C
HETATM 5082 S1 SOG B 407 -38.571 22.808 107.134 1.00124.20 S
HETATM 5083 O2 SOG B 407 -40.489 24.507 108.889 1.00122.30 O
HETATM 5084 O3 SOG B 407 -43.069 25.142 107.667 1.00127.41 O
HETATM 5085 O4 SOG B 407 -44.435 22.856 106.668 1.00122.47 O
HETATM 5086 O5 SOG B 407 -40.885 21.867 106.344 1.00121.44 O
HETATM 5087 O6 SOG B 407 -42.889 19.505 105.494 1.00121.34 O
HETATM 5088 C1 SOG B 408 -22.688 12.102 93.608 1.00113.59 C
HETATM 5089 C2 SOG B 408 -22.254 11.150 94.721 1.00114.75 C
HETATM 5090 C3 SOG B 408 -23.340 11.119 95.800 1.00112.94 C
HETATM 5091 C4 SOG B 408 -23.861 12.508 96.211 1.00112.50 C
HETATM 5092 C5 SOG B 408 -23.842 13.570 95.101 1.00110.69 C
HETATM 5093 C6 SOG B 408 -23.869 14.998 95.667 1.00106.42 C
HETATM 5094 C1' SOG B 408 -22.577 12.761 90.919 1.00101.10 C
HETATM 5095 C2' SOG B 408 -22.411 14.280 90.895 1.00 95.22 C
HETATM 5096 C3' SOG B 408 -21.219 14.756 90.068 1.00 90.54 C
HETATM 5097 C4' SOG B 408 -20.556 15.971 90.715 1.00 88.13 C
HETATM 5098 C5' SOG B 408 -19.543 16.629 89.782 1.00 85.98 C
HETATM 5099 C6' SOG B 408 -18.834 17.793 90.469 1.00 84.16 C
HETATM 5100 C7' SOG B 408 -17.780 18.420 89.562 1.00 82.45 C
HETATM 5101 C8' SOG B 408 -18.053 19.894 89.351 1.00 81.81 C
HETATM 5102 S1 SOG B 408 -21.596 12.047 92.207 1.00109.11 S
HETATM 5103 O2 SOG B 408 -22.017 9.824 94.221 1.00117.13 O
HETATM 5104 O3 SOG B 408 -22.846 10.416 96.952 1.00111.31 O
HETATM 5105 O4 SOG B 408 -25.220 12.363 96.662 1.00112.99 O
HETATM 5106 O5 SOG B 408 -22.744 13.411 94.189 1.00113.64 O
HETATM 5107 O6 SOG B 408 -22.605 15.375 96.232 1.00102.85 O
HETATM 5108 C1 SOG B 409 -48.961 26.424 98.130 1.00101.33 C
HETATM 5109 C2 SOG B 409 -50.223 25.678 98.516 1.00104.61 C
HETATM 5110 C3 SOG B 409 -50.460 25.796 100.015 1.00102.61 C
HETATM 5111 C4 SOG B 409 -49.180 25.446 100.777 1.00 99.54 C
HETATM 5112 C5 SOG B 409 -47.961 26.132 100.177 1.00 95.65 C
HETATM 5113 C6 SOG B 409 -46.702 25.673 100.885 1.00 88.74 C
HETATM 5114 C1' SOG B 409 -47.005 26.098 96.355 1.00 88.99 C
HETATM 5115 C2' SOG B 409 -46.370 27.453 96.118 1.00 80.78 C
HETATM 5116 C3' SOG B 409 -45.048 27.445 96.858 1.00 76.26 C
HETATM 5117 C4' SOG B 409 -44.094 28.405 96.187 1.00 70.58 C
HETATM 5118 C5' SOG B 409 -42.839 28.548 97.021 1.00 68.65 C
HETATM 5119 C6' SOG B 409 -42.048 29.662 96.371 1.00 67.45 C
HETATM 5120 C7' SOG B 409 -40.664 29.784 96.972 1.00 66.65 C
HETATM 5121 C8' SOG B 409 -39.981 30.959 96.315 1.00 66.25 C
HETATM 5122 S1 SOG B 409 -48.748 26.291 96.390 1.00 96.47 S
HETATM 5123 O2 SOG B 409 -51.339 26.169 97.760 1.00104.33 O
HETATM 5124 O3 SOG B 409 -51.496 24.874 100.361 1.00101.27 O
HETATM 5125 O4 SOG B 409 -49.262 25.838 102.152 1.00 98.19 O
HETATM 5126 O5 SOG B 409 -47.878 25.802 98.803 1.00 99.08 O
HETATM 5127 O6 SOG B 409 -47.007 25.692 102.280 1.00 88.00 O
HETATM 5128 C1 SOG B 410 -32.256 16.145 101.477 1.00122.03 C
HETATM 5129 C2 SOG B 410 -33.681 16.658 101.672 1.00117.26 C
HETATM 5130 C3 SOG B 410 -33.666 18.105 102.140 1.00118.22 C
HETATM 5131 C4 SOG B 410 -32.793 18.279 103.386 1.00124.69 C
HETATM 5132 C5 SOG B 410 -31.468 17.498 103.329 1.00124.90 C
HETATM 5133 C6 SOG B 410 -30.894 17.365 104.742 1.00121.37 C
HETATM 5134 C1' SOG B 410 -31.267 13.499 101.717 1.00122.18 C
HETATM 5135 C2' SOG B 410 -31.707 12.041 101.560 1.00121.47 C
HETATM 5136 C3' SOG B 410 -31.098 11.367 100.332 1.00121.90 C
HETATM 5137 C4' SOG B 410 -30.049 10.332 100.734 1.00121.78 C
HETATM 5138 C5' SOG B 410 -30.614 8.915 100.797 1.00119.23 C
HETATM 5139 C6' SOG B 410 -29.768 8.023 101.702 1.00116.39 C
HETATM 5140 C7' SOG B 410 -29.795 6.571 101.238 1.00114.80 C
HETATM 5141 C8' SOG B 410 -29.682 5.620 102.409 1.00115.21 C
HETATM 5142 S1 SOG B 410 -32.343 14.520 100.761 1.00123.32 S
HETATM 5143 O2 SOG B 410 -34.439 16.570 100.459 1.00114.79 O
HETATM 5144 O3 SOG B 410 -35.021 18.494 102.412 1.00113.18 O
HETATM 5145 O4 SOG B 410 -32.538 19.680 103.605 1.00125.63 O
HETATM 5146 O5 SOG B 410 -31.604 16.184 102.753 1.00125.46 O
HETATM 5147 O6 SOG B 410 -29.749 16.502 104.751 1.00119.75 O
HETATM 5148 O1 PG4 B 411 -46.747 12.432 89.430 1.00 91.73 O
HETATM 5149 C1 PG4 B 411 -46.051 11.480 88.616 1.00 91.52 C
HETATM 5150 C2 PG4 B 411 -46.111 11.874 87.141 1.00 91.45 C
HETATM 5151 O2 PG4 B 411 -44.825 12.335 86.724 1.00 92.39 O
HETATM 5152 C3 PG4 B 411 -44.304 11.605 85.613 1.00 96.77 C
HETATM 5153 C4 PG4 B 411 -42.794 11.434 85.786 1.00104.63 C
HETATM 5154 O3 PG4 B 411 -42.508 10.916 87.091 1.00111.45 O
HETATM 5155 C5 PG4 B 411 -41.133 10.564 87.277 1.00110.52 C
HETATM 5156 C6 PG4 B 411 -41.031 9.187 87.935 1.00107.13 C
HETATM 5157 O4 PG4 B 411 -39.725 8.635 87.734 1.00106.52 O
HETATM 5158 C7 PG4 B 411 -39.760 7.287 87.251 1.00110.62 C
HETATM 5159 C8 PG4 B 411 -38.346 6.810 86.916 1.00113.28 C
HETATM 5160 O5 PG4 B 411 -38.249 5.380 86.984 1.00114.08 O
HETATM 5161 O HOH A 501 -46.144 51.039 91.866 1.00 60.67 O
HETATM 5162 O HOH A 502 -9.604 40.819 116.530 1.00 83.73 O
HETATM 5163 O HOH A 503 -18.909 18.514 95.874 1.00 54.06 O
HETATM 5164 O HOH A 504 -42.574 56.330 110.471 1.00 55.68 O
HETATM 5165 O HOH A 505 -39.112 48.586 93.850 1.00 72.99 O
HETATM 5166 O HOH A 506 -48.487 44.122 92.253 1.00 61.80 O
HETATM 5167 O HOH A 507 -51.983 45.309 103.597 1.00 76.12 O
HETATM 5168 O HOH A 508 -38.715 49.767 98.213 1.00 87.41 O
HETATM 5169 O HOH A 509 -48.138 51.067 88.914 1.00 66.75 O
HETATM 5170 O HOH A 510 -32.482 50.329 98.869 1.00 93.70 O
HETATM 5171 O HOH A 511 -41.707 55.229 96.640 1.00 30.00 O
HETATM 5172 O HOH A 512 -40.887 49.821 96.770 1.00 82.85 O
HETATM 5173 O HOH A 513 -41.255 58.548 96.374 1.00 93.18 O
HETATM 5174 O HOH A 514 -37.945 41.558 95.774 1.00 55.62 O
HETATM 5175 O HOH B 501 -48.619 20.951 97.500 1.00 85.36 O
HETATM 5176 O HOH B 502 -41.642 16.089 94.828 1.00 66.88 O
HETATM 5177 O HOH B 503 -29.373 58.990 54.907 1.00102.37 O
HETATM 5178 O HOH B 504 -41.026 20.089 77.002 1.00 46.22 O
HETATM 5179 O HOH B 505 -21.742 34.676 63.014 1.00 72.28 O
HETATM 5180 O HOH B 506 -18.322 20.744 56.901 1.00 85.03 O
HETATM 5181 O HOH B 507 -28.016 -1.299 92.235 1.00 68.40 O
HETATM 5182 O HOH B 508 -43.847 18.257 96.138 1.00 99.78 O
HETATM 5183 O HOH B 509 -39.196 23.416 86.154 1.00 55.01 O
HETATM 5184 O HOH B 510 -39.837 14.308 87.218 1.00 87.60 O
HETATM 5185 O HOH B 511 -43.560 15.665 99.037 1.00 75.62 O
HETATM 5186 O HOH B 512 -20.383 41.012 75.989 1.00 71.58 O
CONECT 747 1292
CONECT 1292 747
CONECT 2940 3568
CONECT 3568 2940
CONECT 4747 4758 4762
CONECT 4748 4749 4765 4772
CONECT 4749 4748 4770
CONECT 4750 4754 4771
CONECT 4751 4752 4756 4766
CONECT 4752 4751 4753
CONECT 4753 4752 4754 4767
CONECT 4754 4750 4753 4755
CONECT 4755 4754 4756 4768
CONECT 4756 4751 4755
CONECT 4757 4779
CONECT 4758 4747 4759
CONECT 4759 4758 4769
CONECT 4760 4762 4769 4771
CONECT 4761 4771 4772 4773
CONECT 4762 4747 4760 4778
CONECT 4763 4764 4770
CONECT 4764 4763 4765 4779
CONECT 4765 4748 4764
CONECT 4766 4751
CONECT 4767 4753
CONECT 4768 4755
CONECT 4769 4759 4760
CONECT 4770 4749 4763
CONECT 4771 4750 4760 4761
CONECT 4772 4748 4761 4778
CONECT 4773 4761
CONECT 4774 4778
CONECT 4775 4778
CONECT 4776 4779
CONECT 4777 4779
CONECT 4778 4762 4772 4774 4775
CONECT 4779 4757 4764 4776 4777
CONECT 4780 4781 4782 4783 4784
CONECT 4781 4780
CONECT 4782 4780
CONECT 4783 4780
CONECT 4784 4780
CONECT 4785 4786 4787 4788 4789
CONECT 4786 4785
CONECT 4787 4785
CONECT 4788 4785
CONECT 4789 4785
CONECT 4790 4791 4806
CONECT 4791 4790
CONECT 4792 4806
CONECT 4793 4818 4820 4822 4824
CONECT 4794 4797 4802
CONECT 4795 4796 4798 4799
CONECT 4796 4795 4797
CONECT 4797 4794 4796 4800
CONECT 4798 4795 4801
CONECT 4799 4795
CONECT 4800 4797 4818
CONECT 4801 4798 4804
CONECT 4802 4794 4829
CONECT 4803 4806 4820
CONECT 4804 4801 4807
CONECT 4805 4829
CONECT 4806 4790 4792 4803
CONECT 4807 4804 4809
CONECT 4808 4810 4816
CONECT 4809 4807 4811
CONECT 4810 4808 4812
CONECT 4811 4809 4813
CONECT 4812 4810 4814
CONECT 4813 4811 4815
CONECT 4814 4812 4817
CONECT 4815 4813 4816
CONECT 4816 4808 4815
CONECT 4817 4814 4819
CONECT 4818 4793 4800
CONECT 4819 4817 4821
CONECT 4820 4793 4803
CONECT 4821 4819 4823
CONECT 4822 4793
CONECT 4823 4821
CONECT 4824 4793
CONECT 4825 4826 4837
CONECT 4826 4825 4827
CONECT 4827 4826 4828
CONECT 4828 4827 4838
CONECT 4829 4802 4805 4830
CONECT 4830 4829 4831
CONECT 4831 4830 4832
CONECT 4832 4831 4833
CONECT 4833 4832 4834
CONECT 4834 4833 4835
CONECT 4835 4834 4836
CONECT 4836 4835 4837
CONECT 4837 4825 4836
CONECT 4838 4828 4840
CONECT 4839 4840
CONECT 4840 4838 4839
CONECT 4841 4842 4855 4859
CONECT 4842 4841 4843 4856
CONECT 4843 4842 4844 4857
CONECT 4844 4843 4845 4858
CONECT 4845 4844 4846 4859
CONECT 4846 4845 4860
CONECT 4847 4848 4855
CONECT 4848 4847 4849
CONECT 4849 4848 4850
CONECT 4850 4849 4851
CONECT 4851 4850 4852
CONECT 4852 4851 4853
CONECT 4853 4852 4854
CONECT 4854 4853
CONECT 4855 4841 4847
CONECT 4856 4842
CONECT 4857 4843
CONECT 4858 4844
CONECT 4859 4841 4845
CONECT 4860 4846
CONECT 4861 4862 4875 4879
CONECT 4862 4861 4863 4876
CONECT 4863 4862 4864 4877
CONECT 4864 4863 4865 4878
CONECT 4865 4864 4866 4879
CONECT 4866 4865 4880
CONECT 4867 4868 4875
CONECT 4868 4867 4869
CONECT 4869 4868 4870
CONECT 4870 4869 4871
CONECT 4871 4870 4872
CONECT 4872 4871 4873
CONECT 4873 4872 4874
CONECT 4874 4873
CONECT 4875 4861 4867
CONECT 4876 4862
CONECT 4877 4863
CONECT 4878 4864
CONECT 4879 4861 4865
CONECT 4880 4866
CONECT 4881 4882 4895 4899
CONECT 4882 4881 4883 4896
CONECT 4883 4882 4884 4897
CONECT 4884 4883 4885 4898
CONECT 4885 4884 4886 4899
CONECT 4886 4885 4900
CONECT 4887 4888 4895
CONECT 4888 4887 4889
CONECT 4889 4888 4890
CONECT 4890 4889 4891
CONECT 4891 4890 4892
CONECT 4892 4891 4893
CONECT 4893 4892 4894
CONECT 4894 4893
CONECT 4895 4881 4887
CONECT 4896 4882
CONECT 4897 4883
CONECT 4898 4884
CONECT 4899 4881 4885
CONECT 4900 4886
CONECT 4901 4902 4915 4919
CONECT 4902 4901 4903 4916
CONECT 4903 4902 4904 4917
CONECT 4904 4903 4905 4918
CONECT 4905 4904 4906 4919
CONECT 4906 4905 4920
CONECT 4907 4908 4915
CONECT 4908 4907 4909
CONECT 4909 4908 4910
CONECT 4910 4909 4911
CONECT 4911 4910 4912
CONECT 4912 4911 4913
CONECT 4913 4912 4914
CONECT 4914 4913
CONECT 4915 4901 4907
CONECT 4916 4902
CONECT 4917 4903
CONECT 4918 4904
CONECT 4919 4901 4905
CONECT 4920 4906
CONECT 4921 4922
CONECT 4922 4921 4923
CONECT 4923 4922 4924
CONECT 4924 4923 4925
CONECT 4925 4924 4926
CONECT 4926 4925 4927
CONECT 4927 4926 4928
CONECT 4928 4927 4929
CONECT 4929 4928 4930
CONECT 4930 4929 4931
CONECT 4931 4930 4932
CONECT 4932 4931 4933
CONECT 4933 4932
CONECT 4934 4945 4949
CONECT 4935 4936 4952 4959
CONECT 4936 4935 4957
CONECT 4937 4941 4958
CONECT 4938 4939 4943 4953
CONECT 4939 4938 4940
CONECT 4940 4939 4941 4954
CONECT 4941 4937 4940 4942
CONECT 4942 4941 4943 4955
CONECT 4943 4938 4942
CONECT 4944 4966
CONECT 4945 4934 4946
CONECT 4946 4945 4956
CONECT 4947 4949 4956 4958
CONECT 4948 4958 4959 4960
CONECT 4949 4934 4947 4965
CONECT 4950 4951 4957
CONECT 4951 4950 4952 4966
CONECT 4952 4935 4951
CONECT 4953 4938
CONECT 4954 4940
CONECT 4955 4942
CONECT 4956 4946 4947
CONECT 4957 4936 4950
CONECT 4958 4937 4947 4948
CONECT 4959 4935 4948 4965
CONECT 4960 4948
CONECT 4961 4965
CONECT 4962 4965
CONECT 4963 4966
CONECT 4964 4966
CONECT 4965 4949 4959 4961 4962
CONECT 4966 4944 4951 4963 4964
CONECT 4967 4968 4969 4970 4971
CONECT 4968 4967
CONECT 4969 4967
CONECT 4970 4967
CONECT 4971 4967
CONECT 4972 4973 4974 4975 4976
CONECT 4973 4972
CONECT 4974 4972
CONECT 4975 4972
CONECT 4976 4972
CONECT 4977 4978 4993
CONECT 4978 4977
CONECT 4979 4993
CONECT 4980 5005 5007 5009 5011
CONECT 4981 4984 4989
CONECT 4982 4983 4985 4986
CONECT 4983 4982 4984
CONECT 4984 4981 4983 4987
CONECT 4985 4982 4988
CONECT 4986 4982
CONECT 4987 4984 5005
CONECT 4988 4985 4991
CONECT 4989 4981 5016
CONECT 4990 4993 5007
CONECT 4991 4988 4994
CONECT 4992 5016
CONECT 4993 4977 4979 4990
CONECT 4994 4991 4996
CONECT 4995 4997 5003
CONECT 4996 4994 4998
CONECT 4997 4995 4999
CONECT 4998 4996 5000
CONECT 4999 4997 5001
CONECT 5000 4998 5002
CONECT 5001 4999 5004
CONECT 5002 5000 5003
CONECT 5003 4995 5002
CONECT 5004 5001 5006
CONECT 5005 4980 4987
CONECT 5006 5004 5008
CONECT 5007 4980 4990
CONECT 5008 5006 5010
CONECT 5009 4980
CONECT 5010 5008
CONECT 5011 4980
CONECT 5012 5013 5024
CONECT 5013 5012 5014
CONECT 5014 5013 5015
CONECT 5015 5014 5025
CONECT 5016 4989 4992 5017
CONECT 5017 5016 5018
CONECT 5018 5017 5019
CONECT 5019 5018 5020
CONECT 5020 5019 5021
CONECT 5021 5020 5022
CONECT 5022 5021 5023
CONECT 5023 5022 5024
CONECT 5024 5012 5023
CONECT 5025 5015 5027
CONECT 5026 5027
CONECT 5027 5025 5026
CONECT 5028 5029 5042 5046
CONECT 5029 5028 5030 5043
CONECT 5030 5029 5031 5044
CONECT 5031 5030 5032 5045
CONECT 5032 5031 5033 5046
CONECT 5033 5032 5047
CONECT 5034 5035 5042
CONECT 5035 5034 5036
CONECT 5036 5035 5037
CONECT 5037 5036 5038
CONECT 5038 5037 5039
CONECT 5039 5038 5040
CONECT 5040 5039 5041
CONECT 5041 5040
CONECT 5042 5028 5034
CONECT 5043 5029
CONECT 5044 5030
CONECT 5045 5031
CONECT 5046 5028 5032
CONECT 5047 5033
CONECT 5048 5049 5062 5066
CONECT 5049 5048 5050 5063
CONECT 5050 5049 5051 5064
CONECT 5051 5050 5052 5065
CONECT 5052 5051 5053 5066
CONECT 5053 5052 5067
CONECT 5054 5055 5062
CONECT 5055 5054 5056
CONECT 5056 5055 5057
CONECT 5057 5056 5058
CONECT 5058 5057 5059
CONECT 5059 5058 5060
CONECT 5060 5059 5061
CONECT 5061 5060
CONECT 5062 5048 5054
CONECT 5063 5049
CONECT 5064 5050
CONECT 5065 5051
CONECT 5066 5048 5052
CONECT 5067 5053
CONECT 5068 5069 5082 5086
CONECT 5069 5068 5070 5083
CONECT 5070 5069 5071 5084
CONECT 5071 5070 5072 5085
CONECT 5072 5071 5073 5086
CONECT 5073 5072 5087
CONECT 5074 5075 5082
CONECT 5075 5074 5076
CONECT 5076 5075 5077
CONECT 5077 5076 5078
CONECT 5078 5077 5079
CONECT 5079 5078 5080
CONECT 5080 5079 5081
CONECT 5081 5080
CONECT 5082 5068 5074
CONECT 5083 5069
CONECT 5084 5070
CONECT 5085 5071
CONECT 5086 5068 5072
CONECT 5087 5073
CONECT 5088 5089 5102 5106
CONECT 5089 5088 5090 5103
CONECT 5090 5089 5091 5104
CONECT 5091 5090 5092 5105
CONECT 5092 5091 5093 5106
CONECT 5093 5092 5107
CONECT 5094 5095 5102
CONECT 5095 5094 5096
CONECT 5096 5095 5097
CONECT 5097 5096 5098
CONECT 5098 5097 5099
CONECT 5099 5098 5100
CONECT 5100 5099 5101
CONECT 5101 5100
CONECT 5102 5088 5094
CONECT 5103 5089
CONECT 5104 5090
CONECT 5105 5091
CONECT 5106 5088 5092
CONECT 5107 5093
CONECT 5108 5109 5122 5126
CONECT 5109 5108 5110 5123
CONECT 5110 5109 5111 5124
CONECT 5111 5110 5112 5125
CONECT 5112 5111 5113 5126
CONECT 5113 5112 5127
CONECT 5114 5115 5122
CONECT 5115 5114 5116
CONECT 5116 5115 5117
CONECT 5117 5116 5118
CONECT 5118 5117 5119
CONECT 5119 5118 5120
CONECT 5120 5119 5121
CONECT 5121 5120
CONECT 5122 5108 5114
CONECT 5123 5109
CONECT 5124 5110
CONECT 5125 5111
CONECT 5126 5108 5112
CONECT 5127 5113
CONECT 5128 5129 5142 5146
CONECT 5129 5128 5130 5143
CONECT 5130 5129 5131 5144
CONECT 5131 5130 5132 5145
CONECT 5132 5131 5133 5146
CONECT 5133 5132 5147
CONECT 5134 5135 5142
CONECT 5135 5134 5136
CONECT 5136 5135 5137
CONECT 5137 5136 5138
CONECT 5138 5137 5139
CONECT 5139 5138 5140
CONECT 5140 5139 5141
CONECT 5141 5140
CONECT 5142 5128 5134
CONECT 5143 5129
CONECT 5144 5130
CONECT 5145 5131
CONECT 5146 5128 5132
CONECT 5147 5133
CONECT 5148 5149
CONECT 5149 5148 5150
CONECT 5150 5149 5151
CONECT 5151 5150 5152
CONECT 5152 5151 5153
CONECT 5153 5152 5154
CONECT 5154 5153 5155
CONECT 5155 5154 5156
CONECT 5156 5155 5157
CONECT 5157 5156 5158
CONECT 5158 5157 5159
CONECT 5159 5158 5160
CONECT 5160 5159
MASTER 634 0 20 25 4 0 0 6 5184 2 418 58
END