HEADER UNKNOWN FUNCTION 26-APR-23 8SMQ TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE CRYPTIC SURFACE TITLE 2 PROTEIN (CD630_25440) FROM CLOSTRIDIUM DIFFICILE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN CD630_25440; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIOIDES DIFFICILE 630; SOURCE 3 ORGANISM_TAXID: 272563; SOURCE 4 GENE: CD630_25440; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21 MAGIC; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG53 KEYWDS CENTER FOR STRUCTURAL BIOLOGY OF INFECTIOUS DISEASES (CSBID), KEYWDS 2 STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS KEYWDS 3 DISEASES, CSGID, CD630_25440, UNKNOWN FUNCTION EXPDTA X-RAY DIFFRACTION AUTHOR G.MINASOV,L.SHUVALOVA,J.S.BRUNZELLE,O.KIRYUKHINA,Z.WAWRZAK, AUTHOR 2 K.J.F.SATCHELL,CENTER FOR STRUCTURAL BIOLOGY OF INFECTIOUS DISEASES AUTHOR 3 (CSBID),CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES AUTHOR 4 (CSGID) REVDAT 4 06-DEC-23 8SMQ 1 JRNL REVDAT 3 15-NOV-23 8SMQ 1 REMARK REVDAT 2 11-OCT-23 8SMQ 1 JRNL REVDAT 1 10-MAY-23 8SMQ 0 JRNL AUTH L.T.ALEXANDER,J.DURAIRAJ,A.KRYSHTAFOVYCH,L.A.ABRIATA,Y.BAYO, JRNL AUTH 2 G.BHABHA,C.BREYTON,S.G.CAULTON,J.CHEN,S.DEGROUX,D.C.EKIERT, JRNL AUTH 3 B.S.ERLANDSEN,P.L.FREDDOLINO,D.GILZER,C.GREENING,J.M.GRIMES, JRNL AUTH 4 R.GRINTER,M.GURUSARAN,M.D.HARTMANN,C.J.HITCHMAN,J.R.KEOWN, JRNL AUTH 5 A.KROPP,P.KURSULA,A.L.LOVERING,B.LEMAITRE,A.LIA,S.LIU, JRNL AUTH 6 M.LOGOTHETI,S.LU,S.MARKUSSON,M.D.MILLER,G.MINASOV, JRNL AUTH 7 H.H.NIEMANN,F.OPAZO,G.N.PHILLIPS JR.,O.R.DAVIES, JRNL AUTH 8 S.ROMMELAERE,M.ROSAS-LEMUS,P.ROVERSI,K.SATCHELL,N.SMITH, JRNL AUTH 9 M.A.WILSON,K.L.WU,X.XIA,H.XIAO,W.ZHANG,Z.H.ZHOU,K.FIDELIS, JRNL AUTH10 M.TOPF,J.MOULT,T.SCHWEDE JRNL TITL PROTEIN TARGET HIGHLIGHTS IN CASP15: ANALYSIS OF MODELS BY JRNL TITL 2 STRUCTURE PROVIDERS. JRNL REF PROTEINS V. 91 1571 2023 JRNL REFN ESSN 1097-0134 JRNL PMID 37493353 JRNL DOI 10.1002/PROT.26545 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0405 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.18 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 3 NUMBER OF REFLECTIONS : 55804 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2964 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3939 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.43 REMARK 3 BIN R VALUE (WORKING SET) : 0.3220 REMARK 3 BIN FREE R VALUE SET COUNT : 215 REMARK 3 BIN FREE R VALUE : 0.3530 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5572 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 285 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -28.93000 REMARK 3 B22 (A**2) : 47.19000 REMARK 3 B33 (A**2) : -18.26000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 7.64000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.040 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.342 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5708 ; 0.003 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 5456 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7677 ; 1.190 ; 1.634 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12666 ; 0.361 ; 1.571 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 684 ; 2.167 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 9 ; 0.778 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1108 ; 3.933 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 853 ; 0.054 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6639 ; 0.016 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1257 ; 0.014 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2736 ; 1.848 ; 1.827 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2736 ; 1.848 ; 1.827 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3420 ; 3.032 ; 3.265 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3421 ; 3.032 ; 3.266 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2972 ; 1.767 ; 2.005 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2973 ; 1.767 ; 2.006 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4258 ; 2.913 ; 3.617 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6664 ; 8.263 ;20.410 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6634 ; 8.262 ;20.060 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 32 A 109 REMARK 3 ORIGIN FOR THE GROUP (A): -51.2258 -19.8310 29.1153 REMARK 3 T TENSOR REMARK 3 T11: 0.5082 T22: 0.0956 REMARK 3 T33: 0.3666 T12: -0.0042 REMARK 3 T13: -0.0347 T23: 0.0322 REMARK 3 L TENSOR REMARK 3 L11: 2.3133 L22: 0.5063 REMARK 3 L33: 1.0973 L12: -0.7577 REMARK 3 L13: -0.8334 L23: 0.2865 REMARK 3 S TENSOR REMARK 3 S11: 0.0635 S12: 0.1134 S13: -0.0601 REMARK 3 S21: 0.0752 S22: 0.0016 S23: 0.0489 REMARK 3 S31: 0.0002 S32: 0.0018 S33: -0.0651 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 110 A 169 REMARK 3 ORIGIN FOR THE GROUP (A): -42.1045 -14.1370 21.0740 REMARK 3 T TENSOR REMARK 3 T11: 0.4682 T22: 0.1431 REMARK 3 T33: 0.3497 T12: -0.0038 REMARK 3 T13: -0.0242 T23: 0.0192 REMARK 3 L TENSOR REMARK 3 L11: 1.7597 L22: 0.2513 REMARK 3 L33: 1.4524 L12: -0.1774 REMARK 3 L13: -0.4098 L23: -0.1605 REMARK 3 S TENSOR REMARK 3 S11: 0.0686 S12: 0.0238 S13: -0.0739 REMARK 3 S21: 0.0522 S22: 0.0160 S23: 0.0275 REMARK 3 S31: -0.0839 S32: 0.1165 S33: -0.0846 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 170 A 202 REMARK 3 ORIGIN FOR THE GROUP (A): -4.8998 -27.6951 20.4533 REMARK 3 T TENSOR REMARK 3 T11: 0.2279 T22: 0.1602 REMARK 3 T33: 0.0823 T12: -0.0870 REMARK 3 T13: -0.0780 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 0.4917 L22: 0.2698 REMARK 3 L33: 0.8401 L12: 0.1535 REMARK 3 L13: -0.6190 L23: -0.1944 REMARK 3 S TENSOR REMARK 3 S11: -0.0634 S12: 0.1756 S13: -0.0149 REMARK 3 S21: 0.0429 S22: 0.0314 S23: 0.0070 REMARK 3 S31: -0.0235 S32: -0.1591 S33: 0.0320 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 33 B 90 REMARK 3 ORIGIN FOR THE GROUP (A): -1.9655 -23.8254 22.8946 REMARK 3 T TENSOR REMARK 3 T11: 0.5008 T22: 0.1404 REMARK 3 T33: 0.3497 T12: -0.0293 REMARK 3 T13: -0.0208 T23: -0.0260 REMARK 3 L TENSOR REMARK 3 L11: 1.4379 L22: 0.8432 REMARK 3 L33: 0.5619 L12: -0.4378 REMARK 3 L13: -0.1235 L23: -0.4561 REMARK 3 S TENSOR REMARK 3 S11: 0.0228 S12: 0.1096 S13: 0.1583 REMARK 3 S21: -0.0811 S22: 0.0813 S23: -0.0798 REMARK 3 S31: -0.1358 S32: 0.0090 S33: -0.1042 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 91 B 172 REMARK 3 ORIGIN FOR THE GROUP (A): -9.2149 -34.5891 21.9211 REMARK 3 T TENSOR REMARK 3 T11: 0.4281 T22: 0.1601 REMARK 3 T33: 0.3069 T12: -0.0328 REMARK 3 T13: -0.0478 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 3.3580 L22: 0.8450 REMARK 3 L33: 0.5041 L12: -1.0246 REMARK 3 L13: 0.0903 L23: -0.1313 REMARK 3 S TENSOR REMARK 3 S11: 0.0167 S12: 0.1426 S13: -0.0932 REMARK 3 S21: 0.0094 S22: 0.0632 S23: -0.0509 REMARK 3 S31: 0.0140 S32: -0.0872 S33: -0.0799 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 173 B 202 REMARK 3 ORIGIN FOR THE GROUP (A): -50.8415 -19.0695 26.3310 REMARK 3 T TENSOR REMARK 3 T11: 0.1996 T22: 0.0423 REMARK 3 T33: 0.0495 T12: 0.0838 REMARK 3 T13: -0.0766 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 1.9565 L22: 1.1925 REMARK 3 L33: 2.2247 L12: -0.0515 REMARK 3 L13: -2.0836 L23: -0.0055 REMARK 3 S TENSOR REMARK 3 S11: 0.1188 S12: 0.1268 S13: 0.0653 REMARK 3 S21: 0.0761 S22: -0.0406 S23: -0.0528 REMARK 3 S31: -0.1099 S32: -0.1240 S33: -0.0782 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 33 C 86 REMARK 3 ORIGIN FOR THE GROUP (A): -19.7257 -62.3848 57.1483 REMARK 3 T TENSOR REMARK 3 T11: 0.4791 T22: 0.1090 REMARK 3 T33: 0.3872 T12: 0.0447 REMARK 3 T13: -0.0320 T23: 0.0119 REMARK 3 L TENSOR REMARK 3 L11: 2.5924 L22: 0.0708 REMARK 3 L33: 2.5905 L12: -0.2952 REMARK 3 L13: -0.9700 L23: -0.0133 REMARK 3 S TENSOR REMARK 3 S11: -0.1049 S12: -0.0812 S13: 0.1028 REMARK 3 S21: 0.0273 S22: 0.0558 S23: 0.0504 REMARK 3 S31: -0.1614 S32: 0.0510 S33: 0.0491 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 87 C 151 REMARK 3 ORIGIN FOR THE GROUP (A): -11.2805 -70.5951 50.5924 REMARK 3 T TENSOR REMARK 3 T11: 0.4577 T22: 0.1367 REMARK 3 T33: 0.3433 T12: 0.0419 REMARK 3 T13: -0.0257 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 1.6620 L22: 0.5012 REMARK 3 L33: 1.9406 L12: -0.3597 REMARK 3 L13: 0.2240 L23: -0.3653 REMARK 3 S TENSOR REMARK 3 S11: -0.0768 S12: 0.1223 S13: -0.1116 REMARK 3 S21: 0.0350 S22: 0.0191 S23: 0.0724 REMARK 3 S31: -0.0861 S32: 0.1751 S33: 0.0577 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 152 C 201 REMARK 3 ORIGIN FOR THE GROUP (A): -17.5294 -59.6805 18.9729 REMARK 3 T TENSOR REMARK 3 T11: 0.2460 T22: 0.1369 REMARK 3 T33: 0.1423 T12: 0.0235 REMARK 3 T13: -0.0283 T23: 0.0267 REMARK 3 L TENSOR REMARK 3 L11: 0.6349 L22: 0.3866 REMARK 3 L33: 2.4076 L12: 0.1546 REMARK 3 L13: 0.4499 L23: 0.0790 REMARK 3 S TENSOR REMARK 3 S11: 0.0173 S12: -0.2104 S13: -0.1394 REMARK 3 S21: 0.1523 S22: 0.0560 S23: -0.0134 REMARK 3 S31: 0.1917 S32: 0.0219 S33: -0.0733 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 33 D 74 REMARK 3 ORIGIN FOR THE GROUP (A): -24.9084 -59.5465 2.8813 REMARK 3 T TENSOR REMARK 3 T11: 0.4133 T22: 0.1191 REMARK 3 T33: 0.2463 T12: -0.0249 REMARK 3 T13: -0.0229 T23: -0.0188 REMARK 3 L TENSOR REMARK 3 L11: 4.4104 L22: 1.4226 REMARK 3 L33: 2.0258 L12: -1.2504 REMARK 3 L13: -0.3437 L23: -0.7359 REMARK 3 S TENSOR REMARK 3 S11: 0.0220 S12: -0.0968 S13: -0.1659 REMARK 3 S21: -0.0566 S22: 0.0859 S23: 0.0892 REMARK 3 S31: 0.0851 S32: 0.0383 S33: -0.1079 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 75 D 106 REMARK 3 ORIGIN FOR THE GROUP (A): -17.6199 -55.9646 9.8857 REMARK 3 T TENSOR REMARK 3 T11: 0.5129 T22: 0.1520 REMARK 3 T33: 0.3487 T12: -0.0383 REMARK 3 T13: -0.0445 T23: -0.0710 REMARK 3 L TENSOR REMARK 3 L11: 2.2006 L22: 0.6073 REMARK 3 L33: 0.8814 L12: -1.0058 REMARK 3 L13: 0.2693 L23: -0.4542 REMARK 3 S TENSOR REMARK 3 S11: -0.1145 S12: -0.0669 S13: 0.0146 REMARK 3 S21: -0.0149 S22: 0.0935 S23: -0.0814 REMARK 3 S31: 0.0577 S32: -0.1021 S33: 0.0211 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 107 D 202 REMARK 3 ORIGIN FOR THE GROUP (A): -17.8345 -54.1124 28.4833 REMARK 3 T TENSOR REMARK 3 T11: 0.4667 T22: 0.1880 REMARK 3 T33: 0.3347 T12: 0.0126 REMARK 3 T13: -0.0195 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 0.0575 L22: 0.1623 REMARK 3 L33: 1.7783 L12: -0.0595 REMARK 3 L13: 0.2913 L23: -0.4745 REMARK 3 S TENSOR REMARK 3 S11: -0.0375 S12: 0.0332 S13: -0.0081 REMARK 3 S21: -0.0713 S22: 0.0680 S23: 0.0263 REMARK 3 S31: -0.0220 S32: -0.0118 S33: -0.0306 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 8SMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-23. REMARK 100 THE DEPOSITION ID IS D_1000274101. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97864 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59250 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.12300 REMARK 200 R SYM (I) : 0.12300 REMARK 200 FOR THE DATA SET : 14.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 0.91700 REMARK 200 R SYM FOR SHELL (I) : 0.91700 REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 13.0 MG/ML, 0.5M SODIUM REMARK 280 CHLORIDE, 0.01M TRIS HCL (PH 8.3);SCREEN: COMPAS (A1), 0.1M REMARK 280 POTASSIUM CHLORIDE, 12% (W/V) PEG800, 5% (W/V) GLYCEROL CRYO: REMARK 280 COMPAS (A2), 0.5M POTASSIUM CHLORIDE, 12% (W/V) PEG800, 10% (W/V) REMARK 280 GLYCEROL., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 74.89850 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.65100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 74.89850 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.65100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13010 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 12440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 SER A 30 REMARK 465 ASN A 31 REMARK 465 SER B 30 REMARK 465 ASN B 31 REMARK 465 ALA B 32 REMARK 465 SER C 30 REMARK 465 ASN C 31 REMARK 465 ALA C 32 REMARK 465 GLU C 202 REMARK 465 SER D 30 REMARK 465 ASN D 31 REMARK 465 ALA D 32 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 46 25.19 -143.20 REMARK 500 SER A 64 -150.65 -146.32 REMARK 500 LYS A 80 73.39 -159.17 REMARK 500 MSE A 112 -68.49 -144.86 REMARK 500 SER A 169 -162.81 -119.19 REMARK 500 THR B 56 40.66 -103.90 REMARK 500 TYR B 72 131.99 -171.86 REMARK 500 ASN B 111 7.92 -67.22 REMARK 500 GLU B 146 12.86 57.19 REMARK 500 GLU B 148 85.39 -154.60 REMARK 500 LEU C 38 78.99 -104.17 REMARK 500 MSE C 112 -41.43 -153.30 REMARK 500 ASP C 168 46.02 -91.29 REMARK 500 SER C 169 -159.52 -151.48 REMARK 500 TYR D 72 143.60 -174.37 REMARK 500 LYS D 80 80.49 -154.21 REMARK 500 SER D 177 146.47 -178.66 REMARK 500 LYS D 196 140.79 -170.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: CSGID-IDP97509.103 RELATED DB: TARGETTRACK DBREF 8SMQ A 33 202 UNP Q182N1 Q182N1_CLOD6 33 202 DBREF 8SMQ B 33 202 UNP Q182N1 Q182N1_CLOD6 33 202 DBREF 8SMQ C 33 202 UNP Q182N1 Q182N1_CLOD6 33 202 DBREF 8SMQ D 33 202 UNP Q182N1 Q182N1_CLOD6 33 202 SEQADV 8SMQ SER A 30 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ASN A 31 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ALA A 32 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ SER B 30 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ASN B 31 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ALA B 32 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ SER C 30 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ASN C 31 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ALA C 32 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ SER D 30 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ASN D 31 UNP Q182N1 EXPRESSION TAG SEQADV 8SMQ ALA D 32 UNP Q182N1 EXPRESSION TAG SEQRES 1 A 173 SER ASN ALA ASP LYS ILE LEU ASP LEU SER PHE LYS LYS SEQRES 2 A 173 ILE GLU THR ASP LEU SER SER LYS ILE THR TYR GLU ASP SEQRES 3 A 173 THR GLY VAL LYS ILE GLU THR ASP SER SER LYS SER ASP SEQRES 4 A 173 LYS GLU ARG TYR LEU TYR ILE TYR GLN ASN ILE LYS GLU SEQRES 5 A 173 ASN TRP SER MSE TYR ASN ASN PHE TYR ILE GLU ILE GLN SEQRES 6 A 173 ASN LYS ASN LYS SER SER GLN LYS ILE ASN LEU SER ILE SEQRES 7 A 173 GLN SER LYS ASN MSE PHE GLU PHE ARG LEU LYS GLU GLY SEQRES 8 A 173 SER GLU VAL PHE LEU GLU GLY LYS ASN ILE ILE TYR SER SEQRES 9 A 173 ASP LYS ILE LYS GLU GLY OCS ILE GLU VAL PRO GLY GLU SEQRES 10 A 173 PHE GLU GLY LYS ILE TYR VAL ASN PHE ASN SER LEU ILE SEQRES 11 A 173 ASN GLU GLU SER ASN VAL VAL LEU ASP SER ASN MSE LEU SEQRES 12 A 173 SER ASN ILE VAL SER TRP GLY ILE THR PHE ILE PRO SER SEQRES 13 A 173 ASP GLU GLU HIS ASN ILE VAL ILE ILE LYS LYS ILE SER SEQRES 14 A 173 LEU LEU SER GLU SEQRES 1 B 173 SER ASN ALA ASP LYS ILE LEU ASP LEU SER PHE LYS LYS SEQRES 2 B 173 ILE GLU THR ASP LEU SER SER LYS ILE THR TYR GLU ASP SEQRES 3 B 173 THR GLY VAL LYS ILE GLU THR ASP SER SER LYS SER ASP SEQRES 4 B 173 LYS GLU ARG TYR LEU TYR ILE TYR GLN ASN ILE LYS GLU SEQRES 5 B 173 ASN TRP SER MSE TYR ASN ASN PHE TYR ILE GLU ILE GLN SEQRES 6 B 173 ASN LYS ASN LYS SER SER GLN LYS ILE ASN LEU SER ILE SEQRES 7 B 173 GLN SER LYS ASN MSE PHE GLU PHE ARG LEU LYS GLU GLY SEQRES 8 B 173 SER GLU VAL PHE LEU GLU GLY LYS ASN ILE ILE TYR SER SEQRES 9 B 173 ASP LYS ILE LYS GLU GLY OCS ILE GLU VAL PRO GLY GLU SEQRES 10 B 173 PHE GLU GLY LYS ILE TYR VAL ASN PHE ASN SER LEU ILE SEQRES 11 B 173 ASN GLU GLU SER ASN VAL VAL LEU ASP SER ASN MSE LEU SEQRES 12 B 173 SER ASN ILE VAL SER TRP GLY ILE THR PHE ILE PRO SER SEQRES 13 B 173 ASP GLU GLU HIS ASN ILE VAL ILE ILE LYS LYS ILE SER SEQRES 14 B 173 LEU LEU SER GLU SEQRES 1 C 173 SER ASN ALA ASP LYS ILE LEU ASP LEU SER PHE LYS LYS SEQRES 2 C 173 ILE GLU THR ASP LEU SER SER LYS ILE THR TYR GLU ASP SEQRES 3 C 173 THR GLY VAL LYS ILE GLU THR ASP SER SER LYS SER ASP SEQRES 4 C 173 LYS GLU ARG TYR LEU TYR ILE TYR GLN ASN ILE LYS GLU SEQRES 5 C 173 ASN TRP SER MSE TYR ASN ASN PHE TYR ILE GLU ILE GLN SEQRES 6 C 173 ASN LYS ASN LYS SER SER GLN LYS ILE ASN LEU SER ILE SEQRES 7 C 173 GLN SER LYS ASN MSE PHE GLU PHE ARG LEU LYS GLU GLY SEQRES 8 C 173 SER GLU VAL PHE LEU GLU GLY LYS ASN ILE ILE TYR SER SEQRES 9 C 173 ASP LYS ILE LYS GLU GLY OCS ILE GLU VAL PRO GLY GLU SEQRES 10 C 173 PHE GLU GLY LYS ILE TYR VAL ASN PHE ASN SER LEU ILE SEQRES 11 C 173 ASN GLU GLU SER ASN VAL VAL LEU ASP SER ASN MSE LEU SEQRES 12 C 173 SER ASN ILE VAL SER TRP GLY ILE THR PHE ILE PRO SER SEQRES 13 C 173 ASP GLU GLU HIS ASN ILE VAL ILE ILE LYS LYS ILE SER SEQRES 14 C 173 LEU LEU SER GLU SEQRES 1 D 173 SER ASN ALA ASP LYS ILE LEU ASP LEU SER PHE LYS LYS SEQRES 2 D 173 ILE GLU THR ASP LEU SER SER LYS ILE THR TYR GLU ASP SEQRES 3 D 173 THR GLY VAL LYS ILE GLU THR ASP SER SER LYS SER ASP SEQRES 4 D 173 LYS GLU ARG TYR LEU TYR ILE TYR GLN ASN ILE LYS GLU SEQRES 5 D 173 ASN TRP SER MSE TYR ASN ASN PHE TYR ILE GLU ILE GLN SEQRES 6 D 173 ASN LYS ASN LYS SER SER GLN LYS ILE ASN LEU SER ILE SEQRES 7 D 173 GLN SER LYS ASN MSE PHE GLU PHE ARG LEU LYS GLU GLY SEQRES 8 D 173 SER GLU VAL PHE LEU GLU GLY LYS ASN ILE ILE TYR SER SEQRES 9 D 173 ASP LYS ILE LYS GLU GLY OCS ILE GLU VAL PRO GLY GLU SEQRES 10 D 173 PHE GLU GLY LYS ILE TYR VAL ASN PHE ASN SER LEU ILE SEQRES 11 D 173 ASN GLU GLU SER ASN VAL VAL LEU ASP SER ASN MSE LEU SEQRES 12 D 173 SER ASN ILE VAL SER TRP GLY ILE THR PHE ILE PRO SER SEQRES 13 D 173 ASP GLU GLU HIS ASN ILE VAL ILE ILE LYS LYS ILE SER SEQRES 14 D 173 LEU LEU SER GLU MODRES 8SMQ MSE A 85 MET MODIFIED RESIDUE MODRES 8SMQ MSE A 112 MET MODIFIED RESIDUE MODRES 8SMQ OCS A 140 CYS MODIFIED RESIDUE MODRES 8SMQ MSE A 171 MET MODIFIED RESIDUE MODRES 8SMQ MSE B 85 MET MODIFIED RESIDUE MODRES 8SMQ MSE B 112 MET MODIFIED RESIDUE MODRES 8SMQ OCS B 140 CYS MODIFIED RESIDUE MODRES 8SMQ MSE B 171 MET MODIFIED RESIDUE MODRES 8SMQ MSE C 85 MET MODIFIED RESIDUE MODRES 8SMQ MSE C 112 MET MODIFIED RESIDUE MODRES 8SMQ OCS C 140 CYS MODIFIED RESIDUE MODRES 8SMQ MSE C 171 MET MODIFIED RESIDUE MODRES 8SMQ MSE D 85 MET MODIFIED RESIDUE MODRES 8SMQ MSE D 112 MET MODIFIED RESIDUE MODRES 8SMQ OCS D 140 CYS MODIFIED RESIDUE MODRES 8SMQ MSE D 171 MET MODIFIED RESIDUE HET MSE A 85 8 HET MSE A 112 8 HET OCS A 140 9 HET MSE A 171 8 HET MSE B 85 8 HET MSE B 112 8 HET OCS B 140 9 HET MSE B 171 8 HET MSE C 85 8 HET MSE C 112 8 HET OCS C 140 9 HET MSE C 171 8 HET MSE D 85 8 HET MSE D 112 16 HET OCS D 140 9 HET MSE D 171 8 HET CL A 401 1 HET CL A 402 1 HET CL A 403 1 HET CL A 404 1 HET EDO A 405 4 HET CL B 401 1 HET CL B 402 1 HET CL B 403 1 HET CL B 404 1 HET CL B 405 1 HET GOL B 406 6 HET CL C 401 1 HET CL C 402 1 HET CL C 403 1 HET CL C 404 1 HET CL C 405 1 HET CL D 401 1 HET CL D 402 1 HET CL D 403 1 HET CL D 404 1 HETNAM MSE SELENOMETHIONINE HETNAM OCS CYSTEINESULFONIC ACID HETNAM CL CHLORIDE ION HETNAM EDO 1,2-ETHANEDIOL HETNAM GOL GLYCEROL HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 1 MSE 12(C5 H11 N O2 SE) FORMUL 1 OCS 4(C3 H7 N O5 S) FORMUL 5 CL 18(CL 1-) FORMUL 9 EDO C2 H6 O2 FORMUL 15 GOL C3 H8 O3 FORMUL 25 HOH *285(H2 O) HELIX 1 AA1 ASN A 170 SER A 173 5 4 HELIX 2 AA2 ASN B 170 SER B 173 5 4 HELIX 3 AA3 ASN C 170 SER C 173 5 4 HELIX 4 AA4 ASN D 170 SER D 173 5 4 SHEET 1 AA1 4 LYS A 34 ILE A 35 0 SHEET 2 AA1 4 HIS B 189 LEU B 200 -1 O LEU B 199 N LYS A 34 SHEET 3 AA1 4 VAL A 58 ASP A 63 -1 N ILE A 60 O VAL B 192 SHEET 4 AA1 4 SER A 48 TYR A 53 -1 N THR A 52 O LYS A 59 SHEET 1 AA2 6 LYS A 34 ILE A 35 0 SHEET 2 AA2 6 HIS B 189 LEU B 200 -1 O LEU B 199 N LYS A 34 SHEET 3 AA2 6 ASN A 88 ASN A 95 -1 N GLN A 94 O ILE B 193 SHEET 4 AA2 6 GLU A 148 ASN A 154 -1 O ILE A 151 N ILE A 91 SHEET 5 AA2 6 GLU A 122 GLU A 126 -1 N PHE A 124 O TYR A 152 SHEET 6 AA2 6 ILE A 131 LYS A 135 -1 O ASP A 134 N VAL A 123 SHEET 1 AA3 5 ILE A 43 THR A 45 0 SHEET 2 AA3 5 LEU A 73 GLU A 81 -1 O TYR A 74 N GLU A 44 SHEET 3 AA3 5 ILE B 175 ILE B 183 -1 O VAL B 176 N ILE A 79 SHEET 4 AA3 5 GLN A 101 SER A 109 -1 N GLN A 108 O SER B 177 SHEET 5 AA3 5 ILE A 141 VAL A 143 -1 O VAL A 143 N GLN A 101 SHEET 1 AA4 7 ILE A 43 THR A 45 0 SHEET 2 AA4 7 LEU A 73 GLU A 81 -1 O TYR A 74 N GLU A 44 SHEET 3 AA4 7 ILE B 175 ILE B 183 -1 O VAL B 176 N ILE A 79 SHEET 4 AA4 7 GLN A 101 SER A 109 -1 N GLN A 108 O SER B 177 SHEET 5 AA4 7 PHE A 113 LEU A 117 -1 O PHE A 115 N ILE A 107 SHEET 6 AA4 7 LEU A 158 ASN A 160 -1 O ILE A 159 N ARG A 116 SHEET 7 AA4 7 VAL A 165 VAL A 166 -1 O VAL A 165 N ASN A 160 SHEET 1 AA5 5 LYS B 41 THR B 45 0 SHEET 2 AA5 5 TYR B 72 GLU B 81 -1 O TYR B 72 N THR B 45 SHEET 3 AA5 5 ILE A 175 ILE A 183 -1 N PHE A 182 O LEU B 73 SHEET 4 AA5 5 GLN B 101 SER B 109 -1 O GLN B 108 N VAL A 176 SHEET 5 AA5 5 ILE B 141 VAL B 143 -1 O VAL B 143 N GLN B 101 SHEET 1 AA6 7 LYS B 41 THR B 45 0 SHEET 2 AA6 7 TYR B 72 GLU B 81 -1 O TYR B 72 N THR B 45 SHEET 3 AA6 7 ILE A 175 ILE A 183 -1 N PHE A 182 O LEU B 73 SHEET 4 AA6 7 GLN B 101 SER B 109 -1 O GLN B 108 N VAL A 176 SHEET 5 AA6 7 PHE B 113 LEU B 117 -1 O PHE B 115 N ILE B 107 SHEET 6 AA6 7 LEU B 158 ASN B 160 -1 O ILE B 159 N ARG B 116 SHEET 7 AA6 7 VAL B 165 VAL B 166 -1 O VAL B 165 N ASN B 160 SHEET 1 AA7 4 LYS B 34 ILE B 35 0 SHEET 2 AA7 4 HIS A 189 LEU A 200 -1 N LEU A 199 O LYS B 34 SHEET 3 AA7 4 GLY B 57 ASP B 63 -1 O ILE B 60 N VAL A 192 SHEET 4 AA7 4 SER B 48 GLU B 54 -1 N SER B 48 O ASP B 63 SHEET 1 AA8 6 LYS B 34 ILE B 35 0 SHEET 2 AA8 6 HIS A 189 LEU A 200 -1 N LEU A 199 O LYS B 34 SHEET 3 AA8 6 ASN B 88 ASN B 95 -1 O TYR B 90 N SER A 198 SHEET 4 AA8 6 GLU B 148 ASN B 154 -1 O VAL B 153 N PHE B 89 SHEET 5 AA8 6 GLU B 122 GLU B 126 -1 N PHE B 124 O TYR B 152 SHEET 6 AA8 6 ILE B 131 LYS B 135 -1 O ASP B 134 N VAL B 123 SHEET 1 AA9 4 LYS C 34 ILE C 35 0 SHEET 2 AA9 4 HIS D 189 LEU D 200 -1 O LEU D 199 N LYS C 34 SHEET 3 AA9 4 VAL C 58 ASP C 63 -1 N ILE C 60 O VAL D 192 SHEET 4 AA9 4 SER C 48 TYR C 53 -1 N THR C 52 O LYS C 59 SHEET 1 AB1 6 LYS C 34 ILE C 35 0 SHEET 2 AB1 6 HIS D 189 LEU D 200 -1 O LEU D 199 N LYS C 34 SHEET 3 AB1 6 ASN C 88 ASN C 95 -1 N GLU C 92 O LYS D 196 SHEET 4 AB1 6 GLU C 148 ASN C 154 -1 O ILE C 151 N ILE C 91 SHEET 5 AB1 6 GLU C 122 GLU C 126 -1 N GLU C 126 O LYS C 150 SHEET 6 AB1 6 ILE C 131 LYS C 135 -1 O ASP C 134 N VAL C 123 SHEET 1 AB2 5 ILE C 43 THR C 45 0 SHEET 2 AB2 5 LEU C 73 GLU C 81 -1 O TYR C 74 N GLU C 44 SHEET 3 AB2 5 ILE D 175 ILE D 183 -1 O PHE D 182 N LEU C 73 SHEET 4 AB2 5 GLN C 101 SER C 109 -1 N GLN C 108 O SER D 177 SHEET 5 AB2 5 ILE C 141 VAL C 143 -1 O ILE C 141 N ILE C 103 SHEET 1 AB3 7 ILE C 43 THR C 45 0 SHEET 2 AB3 7 LEU C 73 GLU C 81 -1 O TYR C 74 N GLU C 44 SHEET 3 AB3 7 ILE D 175 ILE D 183 -1 O PHE D 182 N LEU C 73 SHEET 4 AB3 7 GLN C 101 SER C 109 -1 N GLN C 108 O SER D 177 SHEET 5 AB3 7 PHE C 113 LEU C 117 -1 O PHE C 113 N SER C 109 SHEET 6 AB3 7 LEU C 158 ASN C 160 -1 O ILE C 159 N ARG C 116 SHEET 7 AB3 7 VAL C 165 VAL C 166 -1 O VAL C 165 N ASN C 160 SHEET 1 AB4 5 LYS D 41 THR D 45 0 SHEET 2 AB4 5 TYR D 72 GLU D 81 -1 O TYR D 72 N THR D 45 SHEET 3 AB4 5 ILE C 175 ILE C 183 -1 N ILE C 180 O ILE D 75 SHEET 4 AB4 5 GLN D 101 SER D 109 -1 O LYS D 102 N ILE C 183 SHEET 5 AB4 5 ILE D 141 VAL D 143 -1 O ILE D 141 N ILE D 103 SHEET 1 AB5 7 LYS D 41 THR D 45 0 SHEET 2 AB5 7 TYR D 72 GLU D 81 -1 O TYR D 72 N THR D 45 SHEET 3 AB5 7 ILE C 175 ILE C 183 -1 N ILE C 180 O ILE D 75 SHEET 4 AB5 7 GLN D 101 SER D 109 -1 O LYS D 102 N ILE C 183 SHEET 5 AB5 7 GLU D 114 LEU D 117 -1 O PHE D 115 N ILE D 107 SHEET 6 AB5 7 LEU D 158 ASN D 160 -1 O ILE D 159 N ARG D 116 SHEET 7 AB5 7 VAL D 165 VAL D 166 -1 O VAL D 165 N ASN D 160 SHEET 1 AB6 4 LYS D 34 ILE D 35 0 SHEET 2 AB6 4 HIS C 189 LEU C 199 -1 N LEU C 199 O LYS D 34 SHEET 3 AB6 4 GLY D 57 ASP D 63 -1 O ILE D 60 N VAL C 192 SHEET 4 AB6 4 SER D 48 GLU D 54 -1 N THR D 52 O LYS D 59 SHEET 1 AB7 6 LYS D 34 ILE D 35 0 SHEET 2 AB7 6 HIS C 189 LEU C 199 -1 N LEU C 199 O LYS D 34 SHEET 3 AB7 6 ASN D 88 ASN D 95 -1 O GLU D 92 N LYS C 196 SHEET 4 AB7 6 GLU D 148 ASN D 154 -1 O VAL D 153 N PHE D 89 SHEET 5 AB7 6 GLU D 122 GLU D 126 -1 N GLU D 126 O LYS D 150 SHEET 6 AB7 6 ILE D 131 LYS D 135 -1 O ASP D 134 N VAL D 123 LINK C SER A 84 N MSE A 85 1555 1555 1.34 LINK C MSE A 85 N TYR A 86 1555 1555 1.34 LINK C ASN A 111 N MSE A 112 1555 1555 1.34 LINK C MSE A 112 N PHE A 113 1555 1555 1.34 LINK C GLY A 139 N OCS A 140 1555 1555 1.35 LINK C OCS A 140 N ILE A 141 1555 1555 1.34 LINK C ASN A 170 N MSE A 171 1555 1555 1.34 LINK C MSE A 171 N LEU A 172 1555 1555 1.34 LINK C SER B 84 N MSE B 85 1555 1555 1.34 LINK C MSE B 85 N TYR B 86 1555 1555 1.34 LINK C ASN B 111 N MSE B 112 1555 1555 1.34 LINK C MSE B 112 N PHE B 113 1555 1555 1.34 LINK C GLY B 139 N OCS B 140 1555 1555 1.34 LINK C OCS B 140 N ILE B 141 1555 1555 1.34 LINK C ASN B 170 N MSE B 171 1555 1555 1.34 LINK C MSE B 171 N LEU B 172 1555 1555 1.34 LINK C SER C 84 N MSE C 85 1555 1555 1.34 LINK C MSE C 85 N TYR C 86 1555 1555 1.34 LINK C ASN C 111 N MSE C 112 1555 1555 1.34 LINK C MSE C 112 N PHE C 113 1555 1555 1.34 LINK C GLY C 139 N OCS C 140 1555 1555 1.34 LINK C OCS C 140 N ILE C 141 1555 1555 1.34 LINK C ASN C 170 N MSE C 171 1555 1555 1.34 LINK C MSE C 171 N LEU C 172 1555 1555 1.34 LINK C SER D 84 N MSE D 85 1555 1555 1.34 LINK C MSE D 85 N TYR D 86 1555 1555 1.34 LINK C ASN D 111 N AMSE D 112 1555 1555 1.35 LINK C ASN D 111 N BMSE D 112 1555 1555 1.34 LINK C AMSE D 112 N PHE D 113 1555 1555 1.34 LINK C BMSE D 112 N PHE D 113 1555 1555 1.34 LINK C GLY D 139 N OCS D 140 1555 1555 1.34 LINK C OCS D 140 N ILE D 141 1555 1555 1.34 LINK C ASN D 170 N MSE D 171 1555 1555 1.34 LINK C MSE D 171 N LEU D 172 1555 1555 1.34 CRYST1 149.797 81.302 93.751 90.00 128.81 90.00 C 1 2 1 16 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 0.006676 0.000000 0.005370 0.00000 SCALE2 0.000000 0.012300 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013689 0.00000 ATOM 1 N ALA A 32 -46.948 -31.188 9.722 1.00 55.10 N ANISOU 1 N ALA A 32 7591 6407 6935 569 -919 -1408 N ATOM 2 CA ALA A 32 -46.988 -32.038 10.938 1.00 55.14 C ANISOU 2 CA ALA A 32 7678 6128 7141 462 -892 -1429 C ATOM 3 C ALA A 32 -46.982 -31.163 12.192 1.00 54.17 C ANISOU 3 C ALA A 32 7681 5849 7049 416 -849 -1208 C ATOM 4 O ALA A 32 -46.047 -31.220 12.988 1.00 52.64 O ANISOU 4 O ALA A 32 7584 5506 6910 393 -825 -1107 O ATOM 5 CB ALA A 32 -45.824 -33.002 10.929 1.00 55.01 C ANISOU 5 CB ALA A 32 7686 6017 7197 465 -892 -1497 C ATOM 6 N ASP A 33 -48.047 -30.368 12.362 1.00 55.66 N ANISOU 6 N ASP A 33 7862 6086 7200 407 -841 -1143 N ATOM 7 CA ASP A 33 -48.182 -29.480 13.508 1.00 54.26 C ANISOU 7 CA ASP A 33 7792 5776 7046 366 -800 -952 C ATOM 8 C ASP A 33 -48.410 -30.305 14.773 1.00 52.85 C ANISOU 8 C ASP A 33 7684 5352 7042 272 -773 -965 C ATOM 9 O ASP A 33 -49.292 -31.161 14.802 1.00 51.73 O ANISOU 9 O ASP A 33 7491 5162 7002 226 -774 -1100 O ATOM 10 CB ASP A 33 -49.362 -28.518 13.340 1.00 56.59 C ANISOU 10 CB ASP A 33 8052 6184 7265 385 -795 -896 C ATOM 11 CG ASP A 33 -49.283 -27.632 12.110 1.00 60.22 C ANISOU 11 CG ASP A 33 8438 6897 7545 496 -807 -856 C ATOM 12 OD1 ASP A 33 -48.286 -27.743 11.368 1.00 63.44 O ANISOU 12 OD1 ASP A 33 8821 7398 7883 554 -820 -872 O ATOM 13 OD2 ASP A 33 -50.234 -26.850 11.892 1.00 61.89 O ANISOU 13 OD2 ASP A 33 8613 7216 7684 532 -798 -804 O ATOM 14 N LYS A 34 -47.628 -30.015 15.822 1.00 51.27 N ANISOU 14 N LYS A 34 7594 5008 6878 249 -744 -822 N ATOM 15 CA LYS A 34 -47.744 -30.709 17.093 1.00 50.18 C ANISOU 15 CA LYS A 34 7528 4651 6884 182 -709 -798 C ATOM 16 C LYS A 34 -48.575 -29.862 18.051 1.00 49.53 C ANISOU 16 C LYS A 34 7502 4511 6807 144 -680 -676 C ATOM 17 O LYS A 34 -48.168 -28.760 18.410 1.00 48.49 O ANISOU 17 O LYS A 34 7425 4401 6598 160 -670 -539 O ATOM 18 CB LYS A 34 -46.360 -30.962 17.695 1.00 49.75 C ANISOU 18 CB LYS A 34 7550 4501 6850 195 -698 -724 C ATOM 19 CG LYS A 34 -46.347 -31.718 19.019 1.00 50.11 C ANISOU 19 CG LYS A 34 7670 4339 7029 152 -657 -681 C ATOM 20 CD LYS A 34 -44.953 -31.898 19.579 1.00 50.31 C ANISOU 20 CD LYS A 34 7759 4306 7050 183 -651 -604 C ATOM 21 CE LYS A 34 -44.911 -32.655 20.889 1.00 51.27 C ANISOU 21 CE LYS A 34 7949 4244 7286 164 -604 -543 C ATOM 22 NZ LYS A 34 -45.415 -34.041 20.748 1.00 52.48 N ANISOU 22 NZ LYS A 34 8069 4280 7589 146 -572 -659 N ATOM 23 N ILE A 35 -49.730 -30.398 18.465 1.00 50.43 N ANISOU 23 N ILE A 35 7595 4545 7020 91 -660 -733 N ATOM 24 CA ILE A 35 -50.618 -29.711 19.388 1.00 50.81 C ANISOU 24 CA ILE A 35 7689 4536 7081 55 -630 -630 C ATOM 25 C ILE A 35 -50.140 -30.000 20.811 1.00 49.28 C ANISOU 25 C ILE A 35 7597 4157 6968 24 -588 -525 C ATOM 26 O ILE A 35 -49.949 -31.156 21.181 1.00 49.15 O ANISOU 26 O ILE A 35 7590 4015 7068 3 -564 -574 O ATOM 27 CB ILE A 35 -52.082 -30.141 19.157 1.00 52.72 C ANISOU 27 CB ILE A 35 7849 4793 7387 14 -625 -742 C ATOM 28 CG1 ILE A 35 -52.490 -29.975 17.690 1.00 54.34 C ANISOU 28 CG1 ILE A 35 7935 5215 7496 61 -673 -867 C ATOM 29 CG2 ILE A 35 -53.022 -29.399 20.098 1.00 52.37 C ANISOU 29 CG2 ILE A 35 7848 4699 7349 -16 -592 -632 C ATOM 30 CD1 ILE A 35 -53.917 -30.382 17.387 1.00 56.02 C ANISOU 30 CD1 ILE A 35 8046 5475 7763 23 -675 -1001 C ATOM 31 N LEU A 36 -49.945 -28.938 21.600 1.00 47.94 N ANISOU 31 N LEU A 36 7499 3977 6737 29 -575 -383 N ATOM 32 CA LEU A 36 -49.469 -29.072 22.969 1.00 46.34 C ANISOU 32 CA LEU A 36 7384 3640 6580 14 -542 -282 C ATOM 33 C LEU A 36 -50.654 -29.247 23.916 1.00 47.99 C ANISOU 33 C LEU A 36 7613 3752 6868 -29 -498 -249 C ATOM 34 O LEU A 36 -51.630 -28.507 23.821 1.00 46.99 O ANISOU 34 O LEU A 36 7464 3680 6708 -44 -497 -237 O ATOM 35 CB LEU A 36 -48.659 -27.821 23.323 1.00 43.42 C ANISOU 35 CB LEU A 36 7066 3321 6107 38 -549 -171 C ATOM 36 CG LEU A 36 -47.430 -27.558 22.452 1.00 43.12 C ANISOU 36 CG LEU A 36 7010 3378 5995 80 -581 -187 C ATOM 37 CD1 LEU A 36 -46.570 -26.450 23.041 1.00 42.22 C ANISOU 37 CD1 LEU A 36 6946 3278 5815 87 -573 -85 C ATOM 38 CD2 LEU A 36 -46.599 -28.822 22.276 1.00 42.85 C ANISOU 38 CD2 LEU A 36 6967 3298 6015 97 -592 -254 C ATOM 39 N ASP A 37 -50.553 -30.235 24.820 1.00 48.25 N ANISOU 39 N ASP A 37 7683 3644 7005 -42 -456 -227 N ATOM 40 CA ASP A 37 -51.598 -30.504 25.797 1.00 51.14 C ANISOU 40 CA ASP A 37 8068 3908 7454 -79 -401 -182 C ATOM 41 C ASP A 37 -51.700 -29.325 26.761 1.00 48.97 C ANISOU 41 C ASP A 37 7855 3658 7093 -71 -394 -56 C ATOM 42 O ASP A 37 -50.698 -28.908 27.337 1.00 48.11 O ANISOU 42 O ASP A 37 7801 3558 6919 -38 -404 18 O ATOM 43 CB ASP A 37 -51.344 -31.800 26.573 1.00 54.48 C ANISOU 43 CB ASP A 37 8521 4173 8004 -77 -341 -158 C ATOM 44 CG ASP A 37 -51.358 -33.065 25.729 1.00 57.58 C ANISOU 44 CG ASP A 37 8851 4505 8520 -94 -329 -294 C ATOM 45 OD1 ASP A 37 -51.585 -32.959 24.508 1.00 59.80 O ANISOU 45 OD1 ASP A 37 9057 4888 8776 -107 -377 -423 O ATOM 46 OD2 ASP A 37 -51.148 -34.150 26.306 1.00 61.19 O ANISOU 46 OD2 ASP A 37 9332 4817 9100 -87 -266 -271 O ATOM 47 N LEU A 38 -52.928 -28.822 26.939 1.00 48.83 N ANISOU 47 N LEU A 38 7819 3653 7079 -102 -377 -46 N ATOM 48 CA LEU A 38 -53.205 -27.688 27.804 1.00 49.34 C ANISOU 48 CA LEU A 38 7934 3740 7072 -97 -366 54 C ATOM 49 C LEU A 38 -53.732 -28.160 29.160 1.00 47.23 C ANISOU 49 C LEU A 38 7708 3365 6870 -109 -305 131 C ATOM 50 O LEU A 38 -54.934 -28.348 29.327 1.00 47.16 O ANISOU 50 O LEU A 38 7671 3324 6923 -143 -270 121 O ATOM 51 CB LEU A 38 -54.238 -26.796 27.102 1.00 52.59 C ANISOU 51 CB LEU A 38 8296 4246 7439 -109 -381 24 C ATOM 52 CG LEU A 38 -53.834 -26.243 25.734 1.00 54.13 C ANISOU 52 CG LEU A 38 8443 4568 7555 -80 -430 -31 C ATOM 53 CD1 LEU A 38 -54.805 -25.164 25.275 1.00 54.08 C ANISOU 53 CD1 LEU A 38 8401 4660 7485 -68 -432 -17 C ATOM 54 CD2 LEU A 38 -52.415 -25.694 25.758 1.00 56.18 C ANISOU 54 CD2 LEU A 38 8749 4850 7743 -47 -450 18 C ATOM 55 N SER A 39 -52.819 -28.363 30.118 1.00 46.04 N ANISOU 55 N SER A 39 7618 3172 6702 -73 -290 209 N ATOM 56 CA SER A 39 -53.198 -28.771 31.464 1.00 45.84 C ANISOU 56 CA SER A 39 7634 3067 6715 -61 -228 303 C ATOM 57 C SER A 39 -53.021 -27.581 32.408 1.00 42.54 C ANISOU 57 C SER A 39 7264 2715 6185 -37 -236 379 C ATOM 58 O SER A 39 -52.003 -26.896 32.351 1.00 40.96 O ANISOU 58 O SER A 39 7082 2582 5898 -13 -279 377 O ATOM 59 CB SER A 39 -52.399 -29.966 31.911 1.00 47.92 C ANISOU 59 CB SER A 39 7920 3246 7038 -21 -193 340 C ATOM 60 OG SER A 39 -52.784 -30.375 33.215 1.00 51.04 O ANISOU 60 OG SER A 39 8352 3575 7466 4 -122 450 O ATOM 61 N PHE A 40 -54.008 -27.343 33.283 1.00 42.37 N ANISOU 61 N PHE A 40 7255 2672 6171 -45 -192 437 N ATOM 62 CA PHE A 40 -53.956 -26.212 34.203 1.00 41.51 C ANISOU 62 CA PHE A 40 7185 2625 5961 -23 -196 491 C ATOM 63 C PHE A 40 -53.882 -26.665 35.657 1.00 40.19 C ANISOU 63 C PHE A 40 7055 2433 5780 25 -145 589 C ATOM 64 O PHE A 40 -54.501 -26.066 36.531 1.00 40.06 O ANISOU 64 O PHE A 40 7055 2443 5720 34 -120 635 O ATOM 65 CB PHE A 40 -55.149 -25.282 33.972 1.00 42.97 C ANISOU 65 CB PHE A 40 7349 2840 6137 -59 -192 473 C ATOM 66 CG PHE A 40 -55.155 -24.687 32.592 1.00 45.22 C ANISOU 66 CG PHE A 40 7595 3178 6408 -83 -238 396 C ATOM 67 CD1 PHE A 40 -55.311 -25.493 31.476 1.00 47.67 C ANISOU 67 CD1 PHE A 40 7853 3476 6783 -104 -253 325 C ATOM 68 CD2 PHE A 40 -54.851 -23.351 32.404 1.00 45.17 C ANISOU 68 CD2 PHE A 40 7601 3237 6322 -75 -263 394 C ATOM 69 CE1 PHE A 40 -55.256 -24.954 30.203 1.00 48.03 C ANISOU 69 CE1 PHE A 40 7856 3596 6794 -108 -295 261 C ATOM 70 CE2 PHE A 40 -54.791 -22.814 31.130 1.00 46.16 C ANISOU 70 CE2 PHE A 40 7690 3417 6429 -80 -293 346 C ATOM 71 CZ PHE A 40 -54.992 -23.617 30.032 1.00 46.32 C ANISOU 71 CZ PHE A 40 7657 3448 6494 -90 -312 284 C ATOM 72 N LYS A 41 -53.063 -27.684 35.915 1.00 39.30 N ANISOU 72 N LYS A 41 6955 2283 5692 69 -129 625 N ATOM 73 CA LYS A 41 -52.888 -28.211 37.257 1.00 39.49 C ANISOU 73 CA LYS A 41 7012 2299 5693 140 -75 735 C ATOM 74 C LYS A 41 -51.749 -27.497 37.980 1.00 36.89 C ANISOU 74 C LYS A 41 6705 2089 5222 200 -120 748 C ATOM 75 O LYS A 41 -51.736 -27.450 39.208 1.00 36.46 O ANISOU 75 O LYS A 41 6669 2085 5099 264 -89 826 O ATOM 76 CB LYS A 41 -52.494 -29.690 37.202 1.00 40.81 C ANISOU 76 CB LYS A 41 7178 2368 5958 176 -25 778 C ATOM 77 CG LYS A 41 -53.493 -30.667 36.596 1.00 42.84 C ANISOU 77 CG LYS A 41 7403 2487 6384 118 35 756 C ATOM 78 CD LYS A 41 -54.752 -30.868 37.402 1.00 44.29 C ANISOU 78 CD LYS A 41 7585 2615 6627 106 121 834 C ATOM 79 CE LYS A 41 -55.633 -31.962 36.829 1.00 45.43 C ANISOU 79 CE LYS A 41 7686 2613 6963 44 192 799 C ATOM 80 NZ LYS A 41 -56.829 -32.205 37.668 1.00 46.43 N ANISOU 80 NZ LYS A 41 7804 2678 7156 33 288 885 N ATOM 81 N LYS A 42 -50.788 -26.974 37.204 1.00 35.05 N ANISOU 81 N LYS A 42 6460 1908 4947 183 -189 667 N ATOM 82 CA LYS A 42 -49.594 -26.342 37.746 1.00 34.36 C ANISOU 82 CA LYS A 42 6378 1934 4743 229 -234 653 C ATOM 83 C LYS A 42 -49.627 -24.839 37.480 1.00 33.27 C ANISOU 83 C LYS A 42 6230 1858 4551 175 -276 574 C ATOM 84 O LYS A 42 -49.334 -24.392 36.373 1.00 32.50 O ANISOU 84 O LYS A 42 6115 1756 4476 127 -312 506 O ATOM 85 CB LYS A 42 -48.396 -27.061 37.123 1.00 34.47 C ANISOU 85 CB LYS A 42 6380 1947 4769 256 -264 630 C ATOM 86 CG LYS A 42 -48.393 -28.564 37.394 1.00 35.52 C ANISOU 86 CG LYS A 42 6525 1997 4975 316 -207 714 C ATOM 87 CD LYS A 42 -47.287 -29.341 36.732 1.00 35.66 C ANISOU 87 CD LYS A 42 6531 2000 5017 347 -229 690 C ATOM 88 CE LYS A 42 -47.407 -30.823 37.028 1.00 36.80 C ANISOU 88 CE LYS A 42 6688 2034 5257 407 -152 780 C ATOM 89 NZ LYS A 42 -46.373 -31.612 36.324 1.00 36.89 N ANISOU 89 NZ LYS A 42 6689 2021 5306 440 -169 750 N ATOM 90 N ILE A 43 -49.915 -24.067 38.534 1.00 33.24 N ANISOU 90 N ILE A 43 6236 1917 4476 192 -265 587 N ATOM 91 CA ILE A 43 -50.049 -22.626 38.403 1.00 32.71 C ANISOU 91 CA ILE A 43 6162 1888 4378 143 -286 515 C ATOM 92 C ILE A 43 -49.415 -21.860 39.559 1.00 33.14 C ANISOU 92 C ILE A 43 6210 2053 4329 180 -300 482 C ATOM 93 O ILE A 43 -49.769 -22.064 40.718 1.00 33.43 O ANISOU 93 O ILE A 43 6254 2137 4310 235 -274 532 O ATOM 94 CB ILE A 43 -51.541 -22.250 38.292 1.00 32.48 C ANISOU 94 CB ILE A 43 6142 1802 4398 105 -248 535 C ATOM 95 CG1 ILE A 43 -52.191 -22.862 37.048 1.00 32.09 C ANISOU 95 CG1 ILE A 43 6078 1667 4444 62 -241 535 C ATOM 96 CG2 ILE A 43 -51.723 -20.734 38.311 1.00 32.21 C ANISOU 96 CG2 ILE A 43 6104 1797 4334 69 -254 474 C ATOM 97 CD1 ILE A 43 -53.652 -22.500 36.876 1.00 32.01 C ANISOU 97 CD1 ILE A 43 6064 1620 4478 28 -208 546 C ATOM 98 N GLU A 44 -48.495 -20.950 39.204 1.00 33.20 N ANISOU 98 N GLU A 44 6194 2106 4315 147 -338 391 N ATOM 99 CA GLU A 44 -47.888 -20.031 40.154 1.00 34.00 C ANISOU 99 CA GLU A 44 6271 2311 4335 160 -353 317 C ATOM 100 C GLU A 44 -48.564 -18.695 39.866 1.00 33.56 C ANISOU 100 C GLU A 44 6219 2208 4324 92 -331 260 C ATOM 101 O GLU A 44 -48.480 -18.200 38.743 1.00 33.30 O ANISOU 101 O GLU A 44 6181 2111 4358 35 -331 233 O ATOM 102 CB GLU A 44 -46.366 -19.937 40.022 1.00 34.51 C ANISOU 102 CB GLU A 44 6295 2454 4360 165 -400 244 C ATOM 103 CG GLU A 44 -45.658 -21.259 40.233 1.00 35.34 C ANISOU 103 CG GLU A 44 6397 2606 4424 244 -418 307 C ATOM 104 CD GLU A 44 -44.143 -21.173 40.273 1.00 35.71 C ANISOU 104 CD GLU A 44 6394 2759 4414 264 -466 233 C ATOM 105 OE1 GLU A 44 -43.540 -20.725 39.278 1.00 35.95 O ANISOU 105 OE1 GLU A 44 6404 2758 4496 201 -485 171 O ATOM 106 OE2 GLU A 44 -43.573 -21.544 41.313 1.00 36.40 O ANISOU 106 OE2 GLU A 44 6456 2974 4400 348 -482 241 O ATOM 107 N THR A 45 -49.229 -18.113 40.872 1.00 33.82 N ANISOU 107 N THR A 45 6256 2276 4316 107 -307 247 N ATOM 108 CA THR A 45 -49.976 -16.887 40.650 1.00 33.40 C ANISOU 108 CA THR A 45 6210 2166 4314 53 -274 203 C ATOM 109 C THR A 45 -50.088 -16.063 41.932 1.00 34.48 C ANISOU 109 C THR A 45 6331 2381 4386 73 -262 132 C ATOM 110 O THR A 45 -49.610 -16.467 42.993 1.00 34.75 O ANISOU 110 O THR A 45 6346 2534 4324 134 -283 118 O ATOM 111 CB THR A 45 -51.354 -17.266 40.083 1.00 32.34 C ANISOU 111 CB THR A 45 6107 1941 4238 44 -240 295 C ATOM 112 OG1 THR A 45 -52.150 -16.112 39.806 1.00 31.65 O ANISOU 112 OG1 THR A 45 6026 1801 4198 6 -205 269 O ATOM 113 CG2 THR A 45 -52.137 -18.172 41.009 1.00 32.45 C ANISOU 113 CG2 THR A 45 6138 1980 4211 100 -219 379 C ATOM 114 N ASP A 46 -50.705 -14.884 41.790 1.00 35.06 N ANISOU 114 N ASP A 46 6409 2396 4513 28 -225 83 N ATOM 115 CA ASP A 46 -50.952 -13.974 42.901 1.00 36.77 C ANISOU 115 CA ASP A 46 6612 2670 4689 38 -205 -2 C ATOM 116 C ASP A 46 -52.312 -13.313 42.678 1.00 35.73 C ANISOU 116 C ASP A 46 6511 2445 4618 20 -150 34 C ATOM 117 O ASP A 46 -52.557 -12.207 43.155 1.00 36.45 O ANISOU 117 O ASP A 46 6593 2530 4726 4 -118 -51 O ATOM 118 CB ASP A 46 -49.849 -12.924 43.047 1.00 39.00 C ANISOU 118 CB ASP A 46 6845 2984 4988 -5 -213 -159 C ATOM 119 CG ASP A 46 -49.681 -12.006 41.850 1.00 40.19 C ANISOU 119 CG ASP A 46 6998 3004 5268 -83 -177 -187 C ATOM 120 OD1 ASP A 46 -50.393 -12.203 40.846 1.00 41.27 O ANISOU 120 OD1 ASP A 46 7171 3044 5463 -93 -155 -83 O ATOM 121 OD2 ASP A 46 -48.871 -11.071 41.953 1.00 43.80 O ANISOU 121 OD2 ASP A 46 7413 3462 5767 -131 -165 -316 O ATOM 122 N LEU A 47 -53.167 -14.018 41.924 1.00 34.12 N ANISOU 122 N LEU A 47 6337 2173 4452 23 -139 152 N ATOM 123 CA LEU A 47 -54.510 -13.595 41.566 1.00 33.43 C ANISOU 123 CA LEU A 47 6271 2011 4417 14 -93 204 C ATOM 124 C LEU A 47 -55.483 -14.728 41.868 1.00 32.78 C ANISOU 124 C LEU A 47 6204 1942 4306 53 -87 312 C ATOM 125 O LEU A 47 -55.057 -15.800 42.288 1.00 32.65 O ANISOU 125 O LEU A 47 6186 1977 4242 87 -111 353 O ATOM 126 CB LEU A 47 -54.530 -13.366 40.052 1.00 33.03 C ANISOU 126 CB LEU A 47 6224 1871 4454 -25 -85 233 C ATOM 127 CG LEU A 47 -53.502 -12.389 39.495 1.00 33.22 C ANISOU 127 CG LEU A 47 6231 1860 4529 -68 -78 153 C ATOM 128 CD1 LEU A 47 -53.794 -12.095 38.032 1.00 32.79 C ANISOU 128 CD1 LEU A 47 6179 1728 4549 -86 -53 210 C ATOM 129 CD2 LEU A 47 -53.483 -11.112 40.317 1.00 34.16 C ANISOU 129 CD2 LEU A 47 6341 1973 4663 -80 -37 54 C ATOM 130 N SER A 48 -56.780 -14.463 41.668 1.00 32.15 N ANISOU 130 N SER A 48 6135 1817 4263 51 -47 359 N ATOM 131 CA SER A 48 -57.816 -15.481 41.777 1.00 31.94 C ANISOU 131 CA SER A 48 6111 1785 4238 72 -30 457 C ATOM 132 C SER A 48 -58.384 -15.620 40.370 1.00 31.46 C ANISOU 132 C SER A 48 6041 1653 4257 37 -29 490 C ATOM 133 O SER A 48 -58.414 -14.638 39.640 1.00 30.85 O ANISOU 133 O SER A 48 5962 1542 4216 18 -20 458 O ATOM 134 CB SER A 48 -58.886 -15.171 42.798 1.00 32.11 C ANISOU 134 CB SER A 48 6137 1838 4224 106 12 479 C ATOM 135 OG SER A 48 -58.341 -15.083 44.099 1.00 32.48 O ANISOU 135 OG SER A 48 6183 1978 4179 151 8 442 O ATOM 136 N SER A 49 -58.824 -16.823 39.981 1.00 31.51 N ANISOU 136 N SER A 49 6036 1640 4294 33 -32 552 N ATOM 137 CA SER A 49 -59.304 -17.016 38.622 1.00 31.51 C ANISOU 137 CA SER A 49 6012 1600 4358 3 -40 561 C ATOM 138 C SER A 49 -60.300 -18.167 38.501 1.00 32.56 C ANISOU 138 C SER A 49 6119 1716 4536 -4 -21 612 C ATOM 139 O SER A 49 -60.426 -18.990 39.404 1.00 33.11 O ANISOU 139 O SER A 49 6196 1785 4599 11 1 657 O ATOM 140 CB SER A 49 -58.116 -17.257 37.720 1.00 31.07 C ANISOU 140 CB SER A 49 5952 1537 4315 -13 -84 527 C ATOM 141 OG SER A 49 -58.513 -17.623 36.405 1.00 30.50 O ANISOU 141 OG SER A 49 5848 1449 4291 -32 -96 530 O ATOM 142 N LYS A 50 -60.979 -18.200 37.349 1.00 33.27 N ANISOU 142 N LYS A 50 6171 1795 4674 -26 -26 602 N ATOM 143 CA LYS A 50 -61.938 -19.235 37.005 1.00 35.08 C ANISOU 143 CA LYS A 50 6355 2007 4964 -48 -11 619 C ATOM 144 C LYS A 50 -61.614 -19.718 35.591 1.00 34.90 C ANISOU 144 C LYS A 50 6293 1986 4980 -72 -52 572 C ATOM 145 O LYS A 50 -61.801 -18.984 34.626 1.00 34.34 O ANISOU 145 O LYS A 50 6198 1953 4895 -64 -69 546 O ATOM 146 CB LYS A 50 -63.381 -18.737 37.120 1.00 36.34 C ANISOU 146 CB LYS A 50 6486 2189 5132 -44 26 636 C ATOM 147 CG LYS A 50 -64.444 -19.781 36.791 1.00 37.71 C ANISOU 147 CG LYS A 50 6597 2351 5380 -76 47 638 C ATOM 148 CD LYS A 50 -65.869 -19.287 36.954 1.00 39.05 C ANISOU 148 CD LYS A 50 6727 2555 5552 -70 84 653 C ATOM 149 CE LYS A 50 -66.904 -20.336 36.599 1.00 40.81 C ANISOU 149 CE LYS A 50 6872 2771 5862 -113 108 636 C ATOM 150 NZ LYS A 50 -66.769 -21.548 37.443 1.00 41.99 N ANISOU 150 NZ LYS A 50 7033 2846 6074 -137 152 677 N ATOM 151 N ILE A 51 -61.137 -20.968 35.496 1.00 34.75 N ANISOU 151 N ILE A 51 6265 1927 5008 -91 -60 564 N ATOM 152 CA ILE A 51 -60.747 -21.593 34.240 1.00 35.05 C ANISOU 152 CA ILE A 51 6264 1968 5085 -112 -99 506 C ATOM 153 C ILE A 51 -61.832 -22.584 33.818 1.00 36.91 C ANISOU 153 C ILE A 51 6430 2184 5409 -149 -78 474 C ATOM 154 O ILE A 51 -62.198 -23.470 34.590 1.00 36.35 O ANISOU 154 O ILE A 51 6360 2049 5402 -166 -31 507 O ATOM 155 CB ILE A 51 -59.356 -22.241 34.401 1.00 34.88 C ANISOU 155 CB ILE A 51 6277 1913 5060 -104 -122 506 C ATOM 156 CG1 ILE A 51 -58.305 -21.189 34.775 1.00 34.06 C ANISOU 156 CG1 ILE A 51 6224 1842 4875 -76 -144 515 C ATOM 157 CG2 ILE A 51 -58.941 -23.017 33.158 1.00 35.08 C ANISOU 157 CG2 ILE A 51 6259 1936 5131 -124 -158 439 C ATOM 158 CD1 ILE A 51 -56.920 -21.747 34.995 1.00 33.80 C ANISOU 158 CD1 ILE A 51 6218 1798 4826 -62 -169 512 C ATOM 159 N THR A 52 -62.319 -22.441 32.574 1.00 38.20 N ANISOU 159 N THR A 52 6526 2409 5578 -158 -108 407 N ATOM 160 CA THR A 52 -63.387 -23.289 32.067 1.00 39.77 C ANISOU 160 CA THR A 52 6637 2611 5859 -199 -94 345 C ATOM 161 C THR A 52 -63.061 -23.870 30.692 1.00 40.20 C ANISOU 161 C THR A 52 6626 2710 5938 -212 -142 240 C ATOM 162 O THR A 52 -62.762 -23.129 29.757 1.00 41.27 O ANISOU 162 O THR A 52 6745 2938 5995 -175 -187 217 O ATOM 163 CB THR A 52 -64.687 -22.482 31.951 1.00 40.46 C ANISOU 163 CB THR A 52 6677 2776 5917 -187 -80 348 C ATOM 164 OG1 THR A 52 -64.954 -21.890 33.222 1.00 40.43 O ANISOU 164 OG1 THR A 52 6736 2738 5886 -169 -36 437 O ATOM 165 CG2 THR A 52 -65.865 -23.323 31.505 1.00 42.44 C ANISOU 165 CG2 THR A 52 6823 3045 6256 -234 -64 271 C ATOM 166 N TYR A 53 -63.115 -25.205 30.577 1.00 41.24 N ANISOU 166 N TYR A 53 6716 2772 6180 -260 -125 179 N ATOM 167 CA TYR A 53 -62.899 -25.860 29.296 1.00 41.55 C ANISOU 167 CA TYR A 53 6679 2854 6251 -276 -168 55 C ATOM 168 C TYR A 53 -64.175 -25.772 28.464 1.00 45.53 C ANISOU 168 C TYR A 53 7065 3468 6763 -292 -181 -39 C ATOM 169 O TYR A 53 -65.274 -25.941 28.985 1.00 46.86 O ANISOU 169 O TYR A 53 7196 3615 6992 -326 -136 -36 O ATOM 170 CB TYR A 53 -62.447 -27.319 29.426 1.00 39.74 C ANISOU 170 CB TYR A 53 6444 2502 6153 -321 -139 9 C ATOM 171 CG TYR A 53 -61.023 -27.520 29.879 1.00 37.26 C ANISOU 171 CG TYR A 53 6222 2117 5818 -290 -143 75 C ATOM 172 CD1 TYR A 53 -60.587 -27.169 31.148 1.00 35.88 C ANISOU 172 CD1 TYR A 53 6140 1887 5603 -261 -111 205 C ATOM 173 CD2 TYR A 53 -60.075 -27.962 28.968 1.00 36.39 C ANISOU 173 CD2 TYR A 53 6096 2024 5705 -280 -189 0 C ATOM 174 CE1 TYR A 53 -59.260 -27.329 31.519 1.00 35.04 C ANISOU 174 CE1 TYR A 53 6104 1745 5465 -225 -122 254 C ATOM 175 CE2 TYR A 53 -58.746 -28.111 29.315 1.00 35.35 C ANISOU 175 CE2 TYR A 53 6039 1844 5545 -247 -198 55 C ATOM 176 CZ TYR A 53 -58.337 -27.797 30.597 1.00 34.78 C ANISOU 176 CZ TYR A 53 6054 1720 5438 -219 -166 182 C ATOM 177 OH TYR A 53 -57.019 -27.979 30.914 1.00 34.08 O ANISOU 177 OH TYR A 53 6025 1606 5317 -181 -179 225 O ATOM 178 N GLU A 54 -64.003 -25.478 27.169 1.00 50.48 N ANISOU 178 N GLU A 54 7631 4230 7319 -258 -242 -121 N ATOM 179 CA GLU A 54 -65.108 -25.374 26.227 1.00 55.55 C ANISOU 179 CA GLU A 54 8146 5020 7940 -253 -267 -225 C ATOM 180 C GLU A 54 -64.884 -26.392 25.112 1.00 56.84 C ANISOU 180 C GLU A 54 8211 5231 8153 -278 -306 -392 C ATOM 181 O GLU A 54 -63.985 -27.227 25.215 1.00 55.43 O ANISOU 181 O GLU A 54 8071 4942 8047 -308 -301 -416 O ATOM 182 CB GLU A 54 -65.207 -23.938 25.709 1.00 58.42 C ANISOU 182 CB GLU A 54 8515 5532 8149 -163 -297 -156 C ATOM 183 CG GLU A 54 -65.475 -22.931 26.810 1.00 62.25 C ANISOU 183 CG GLU A 54 9089 5961 8599 -141 -253 -12 C ATOM 184 CD GLU A 54 -65.550 -21.484 26.360 1.00 67.77 C ANISOU 184 CD GLU A 54 9802 6775 9170 -51 -263 65 C ATOM 185 OE1 GLU A 54 -65.367 -21.224 25.154 1.00 73.17 O ANISOU 185 OE1 GLU A 54 10426 7595 9777 5 -303 25 O ATOM 186 OE2 GLU A 54 -65.799 -20.621 27.221 1.00 76.17 O ANISOU 186 OE2 GLU A 54 10933 7793 10213 -31 -224 167 O ATOM 187 N ASP A 55 -65.715 -26.338 24.061 1.00 59.21 N ANISOU 187 N ASP A 55 8379 5706 8413 -261 -345 -514 N ATOM 188 CA ASP A 55 -65.572 -27.263 22.946 1.00 60.22 C ANISOU 188 CA ASP A 55 8394 5907 8576 -281 -387 -700 C ATOM 189 C ASP A 55 -64.096 -27.346 22.571 1.00 57.15 C ANISOU 189 C ASP A 55 8080 5490 8144 -245 -418 -676 C ATOM 190 O ASP A 55 -63.543 -28.438 22.448 1.00 55.19 O ANISOU 190 O ASP A 55 7821 5147 8000 -293 -414 -770 O ATOM 191 CB ASP A 55 -66.427 -26.857 21.743 1.00 64.07 C ANISOU 191 CB ASP A 55 8735 6651 8958 -226 -442 -813 C ATOM 192 CG ASP A 55 -67.922 -26.851 22.014 1.00 68.74 C ANISOU 192 CG ASP A 55 9229 7293 9594 -262 -416 -862 C ATOM 193 OD1 ASP A 55 -68.314 -27.152 23.160 1.00 73.03 O ANISOU 193 OD1 ASP A 55 9824 7664 10257 -334 -350 -800 O ATOM 194 OD2 ASP A 55 -68.685 -26.571 21.067 1.00 73.78 O ANISOU 194 OD2 ASP A 55 9733 8157 10144 -212 -462 -963 O ATOM 195 N THR A 56 -63.475 -26.171 22.418 1.00 54.29 N ANISOU 195 N THR A 56 7789 5201 7635 -160 -440 -547 N ATOM 196 CA THR A 56 -62.065 -26.070 22.086 1.00 52.28 C ANISOU 196 CA THR A 56 7604 4932 7327 -121 -466 -507 C ATOM 197 C THR A 56 -61.411 -25.060 23.025 1.00 48.09 C ANISOU 197 C THR A 56 7214 4312 6746 -94 -436 -319 C ATOM 198 O THR A 56 -62.064 -24.130 23.494 1.00 47.10 O ANISOU 198 O THR A 56 7112 4205 6577 -71 -411 -227 O ATOM 199 CB THR A 56 -61.867 -25.676 20.617 1.00 54.64 C ANISOU 199 CB THR A 56 7816 5450 7491 -37 -524 -574 C ATOM 200 OG1 THR A 56 -62.442 -24.383 20.418 1.00 57.58 O ANISOU 200 OG1 THR A 56 8182 5954 7741 41 -521 -471 O ATOM 201 CG2 THR A 56 -62.486 -26.666 19.654 1.00 56.47 C ANISOU 201 CG2 THR A 56 7895 5799 7762 -60 -561 -788 C ATOM 202 N GLY A 57 -60.128 -25.286 23.325 1.00 44.61 N ANISOU 202 N GLY A 57 6857 3773 6319 -98 -436 -276 N ATOM 203 CA GLY A 57 -59.365 -24.400 24.188 1.00 42.29 C ANISOU 203 CA GLY A 57 6681 3402 5982 -78 -413 -128 C ATOM 204 C GLY A 57 -59.936 -24.282 25.599 1.00 39.60 C ANISOU 204 C GLY A 57 6404 2942 5700 -117 -362 -46 C ATOM 205 O GLY A 57 -60.610 -25.183 26.087 1.00 39.35 O ANISOU 205 O GLY A 57 6345 2834 5769 -171 -334 -90 O ATOM 206 N VAL A 58 -59.705 -23.121 26.224 1.00 37.24 N ANISOU 206 N VAL A 58 6180 2630 5338 -86 -342 68 N ATOM 207 CA VAL A 58 -60.154 -22.895 27.584 1.00 35.82 C ANISOU 207 CA VAL A 58 6061 2356 5191 -111 -296 145 C ATOM 208 C VAL A 58 -60.248 -21.397 27.866 1.00 34.51 C ANISOU 208 C VAL A 58 5941 2225 4946 -67 -278 236 C ATOM 209 O VAL A 58 -59.426 -20.618 27.386 1.00 35.27 O ANISOU 209 O VAL A 58 6061 2357 4981 -29 -290 266 O ATOM 210 CB VAL A 58 -59.201 -23.603 28.566 1.00 35.27 C ANISOU 210 CB VAL A 58 6066 2163 5172 -136 -281 178 C ATOM 211 CG1 VAL A 58 -57.747 -23.249 28.318 1.00 35.20 C ANISOU 211 CG1 VAL A 58 6103 2163 5106 -108 -310 197 C ATOM 212 CG2 VAL A 58 -59.568 -23.351 30.016 1.00 35.20 C ANISOU 212 CG2 VAL A 58 6118 2079 5176 -145 -233 263 C ATOM 213 N LYS A 59 -61.280 -21.014 28.629 1.00 33.66 N ANISOU 213 N LYS A 59 5840 2100 4850 -73 -241 277 N ATOM 214 CA LYS A 59 -61.506 -19.629 29.025 1.00 32.78 C ANISOU 214 CA LYS A 59 5770 2001 4681 -33 -211 356 C ATOM 215 C LYS A 59 -60.756 -19.380 30.332 1.00 31.81 C ANISOU 215 C LYS A 59 5740 1781 4565 -49 -188 409 C ATOM 216 O LYS A 59 -60.816 -20.194 31.254 1.00 31.76 O ANISOU 216 O LYS A 59 5754 1708 4603 -82 -174 412 O ATOM 217 CB LYS A 59 -63.000 -19.345 29.220 1.00 33.21 C ANISOU 217 CB LYS A 59 5780 2096 4740 -25 -183 366 C ATOM 218 CG LYS A 59 -63.336 -17.936 29.697 1.00 32.98 C ANISOU 218 CG LYS A 59 5795 2070 4666 19 -143 445 C ATOM 219 CD LYS A 59 -64.794 -17.731 30.058 1.00 33.79 C ANISOU 219 CD LYS A 59 5858 2205 4776 27 -112 458 C ATOM 220 CE LYS A 59 -65.771 -17.938 28.922 1.00 34.72 C ANISOU 220 CE LYS A 59 5865 2452 4875 54 -134 408 C ATOM 221 NZ LYS A 59 -67.168 -17.773 29.389 1.00 35.33 N ANISOU 221 NZ LYS A 59 5900 2561 4963 58 -102 419 N ATOM 222 N ILE A 60 -60.046 -18.249 30.400 1.00 31.23 N ANISOU 222 N ILE A 60 5713 1704 4447 -21 -178 449 N ATOM 223 CA ILE A 60 -59.278 -17.878 31.574 1.00 30.71 C ANISOU 223 CA ILE A 60 5719 1571 4376 -32 -161 475 C ATOM 224 C ILE A 60 -59.764 -16.514 32.054 1.00 31.36 C ANISOU 224 C ILE A 60 5828 1648 4438 -7 -116 515 C ATOM 225 O ILE A 60 -59.598 -15.516 31.355 1.00 30.92 O ANISOU 225 O ILE A 60 5768 1611 4366 23 -99 534 O ATOM 226 CB ILE A 60 -57.768 -17.898 31.260 1.00 30.09 C ANISOU 226 CB ILE A 60 5664 1484 4284 -36 -189 457 C ATOM 227 CG1 ILE A 60 -57.334 -19.267 30.720 1.00 30.02 C ANISOU 227 CG1 ILE A 60 5625 1479 4300 -53 -230 413 C ATOM 228 CG2 ILE A 60 -56.953 -17.484 32.478 1.00 29.87 C ANISOU 228 CG2 ILE A 60 5694 1412 4244 -45 -177 464 C ATOM 229 CD1 ILE A 60 -55.878 -19.352 30.326 1.00 29.69 C ANISOU 229 CD1 ILE A 60 5597 1441 4242 -51 -259 394 C ATOM 230 N GLU A 61 -60.388 -16.504 33.240 1.00 32.14 N ANISOU 230 N GLU A 61 5951 1718 4542 -14 -89 532 N ATOM 231 CA GLU A 61 -60.917 -15.289 33.834 1.00 32.91 C ANISOU 231 CA GLU A 61 6073 1804 4625 9 -43 558 C ATOM 232 C GLU A 61 -60.094 -14.953 35.074 1.00 33.41 C ANISOU 232 C GLU A 61 6190 1828 4673 -1 -33 542 C ATOM 233 O GLU A 61 -59.901 -15.811 35.937 1.00 34.02 O ANISOU 233 O GLU A 61 6281 1901 4741 -14 -46 540 O ATOM 234 CB GLU A 61 -62.370 -15.482 34.260 1.00 33.36 C ANISOU 234 CB GLU A 61 6105 1879 4689 16 -17 581 C ATOM 235 CG GLU A 61 -63.282 -15.999 33.169 1.00 33.72 C ANISOU 235 CG GLU A 61 6078 1984 4748 22 -32 574 C ATOM 236 CD GLU A 61 -64.729 -16.144 33.609 1.00 34.10 C ANISOU 236 CD GLU A 61 6090 2056 4809 25 -2 590 C ATOM 237 OE1 GLU A 61 -65.349 -15.097 33.906 1.00 33.92 O ANISOU 237 OE1 GLU A 61 6078 2042 4765 64 35 622 O ATOM 238 OE2 GLU A 61 -65.217 -17.307 33.723 1.00 32.90 O ANISOU 238 OE2 GLU A 61 5898 1903 4698 -11 -9 569 O ATOM 239 N THR A 62 -59.596 -13.716 35.152 1.00 33.55 N ANISOU 239 N THR A 62 6233 1822 4692 7 -5 529 N ATOM 240 CA THR A 62 -58.805 -13.296 36.297 1.00 34.11 C ANISOU 240 CA THR A 62 6338 1873 4747 -4 0 485 C ATOM 241 C THR A 62 -59.440 -12.066 36.938 1.00 35.43 C ANISOU 241 C THR A 62 6521 2016 4923 14 57 476 C ATOM 242 O THR A 62 -60.066 -11.266 36.250 1.00 36.25 O ANISOU 242 O THR A 62 6616 2098 5056 38 98 508 O ATOM 243 CB THR A 62 -57.344 -13.023 35.909 1.00 33.68 C ANISOU 243 CB THR A 62 6288 1805 4702 -25 -17 442 C ATOM 244 OG1 THR A 62 -57.314 -12.018 34.891 1.00 34.08 O ANISOU 244 OG1 THR A 62 6329 1823 4793 -16 20 459 O ATOM 245 CG2 THR A 62 -56.617 -14.248 35.397 1.00 33.58 C ANISOU 245 CG2 THR A 62 6261 1818 4677 -38 -73 443 C ATOM 246 N ASP A 63 -59.313 -11.979 38.269 1.00 37.03 N ANISOU 246 N ASP A 63 6743 2233 5093 14 62 436 N ATOM 247 CA ASP A 63 -59.786 -10.851 39.058 1.00 38.93 C ANISOU 247 CA ASP A 63 6997 2455 5339 31 114 402 C ATOM 248 C ASP A 63 -58.590 -10.347 39.858 1.00 40.93 C ANISOU 248 C ASP A 63 7257 2711 5581 10 107 302 C ATOM 249 O ASP A 63 -58.032 -11.075 40.684 1.00 43.34 O ANISOU 249 O ASP A 63 7560 3080 5824 12 67 274 O ATOM 250 CB ASP A 63 -60.990 -11.206 39.932 1.00 38.70 C ANISOU 250 CB ASP A 63 6968 2465 5271 60 129 436 C ATOM 251 CG ASP A 63 -62.224 -11.595 39.136 1.00 38.57 C ANISOU 251 CG ASP A 63 6928 2451 5274 75 139 515 C ATOM 252 OD1 ASP A 63 -62.729 -10.736 38.372 1.00 37.04 O ANISOU 252 OD1 ASP A 63 6727 2229 5117 95 175 535 O ATOM 253 OD2 ASP A 63 -62.660 -12.764 39.264 1.00 37.36 O ANISOU 253 OD2 ASP A 63 6759 2331 5104 70 117 555 O ATOM 254 N SER A 64 -58.211 -9.096 39.588 1.00 41.78 N ANISOU 254 N SER A 64 7366 2753 5753 -4 154 250 N ATOM 255 CA SER A 64 -57.064 -8.459 40.208 1.00 42.78 C ANISOU 255 CA SER A 64 7484 2875 5894 -36 158 130 C ATOM 256 C SER A 64 -57.330 -6.963 40.395 1.00 43.79 C ANISOU 256 C SER A 64 7615 2918 6103 -40 240 69 C ATOM 257 O SER A 64 -58.479 -6.560 40.581 1.00 42.47 O ANISOU 257 O SER A 64 7461 2730 5943 -3 283 107 O ATOM 258 CB SER A 64 -55.839 -8.744 39.374 1.00 42.53 C ANISOU 258 CB SER A 64 7438 2832 5888 -72 127 121 C ATOM 259 OG SER A 64 -56.036 -8.336 38.025 1.00 41.89 O ANISOU 259 OG SER A 64 7359 2677 5877 -71 166 196 O ATOM 260 N SER A 65 -56.268 -6.144 40.368 1.00 46.28 N ANISOU 260 N SER A 65 7913 3181 6490 -85 269 -31 N ATOM 261 CA SER A 65 -56.445 -4.710 40.559 1.00 47.93 C ANISOU 261 CA SER A 65 8122 3286 6803 -95 362 -102 C ATOM 262 C SER A 65 -55.422 -3.913 39.749 1.00 49.71 C ANISOU 262 C SER A 65 8329 3405 7152 -146 418 -137 C ATOM 263 O SER A 65 -54.378 -4.432 39.353 1.00 49.14 O ANISOU 263 O SER A 65 8238 3365 7068 -181 372 -150 O ATOM 264 CB SER A 65 -56.379 -4.363 42.024 1.00 49.37 C ANISOU 264 CB SER A 65 8286 3524 6946 -100 356 -250 C ATOM 265 OG SER A 65 -55.128 -4.748 42.578 1.00 50.80 O ANISOU 265 OG SER A 65 8430 3791 7081 -138 295 -366 O ATOM 266 N LYS A 66 -55.753 -2.637 39.518 1.00 50.73 N ANISOU 266 N LYS A 66 8466 3402 7407 -145 528 -147 N ATOM 267 CA LYS A 66 -54.919 -1.719 38.761 1.00 53.04 C ANISOU 267 CA LYS A 66 8742 3564 7846 -188 615 -166 C ATOM 268 C LYS A 66 -53.608 -1.451 39.497 1.00 55.16 C ANISOU 268 C LYS A 66 8961 3841 8154 -270 601 -358 C ATOM 269 O LYS A 66 -52.563 -1.320 38.863 1.00 51.70 O ANISOU 269 O LYS A 66 8496 3361 7786 -320 620 -373 O ATOM 270 CB LYS A 66 -55.674 -0.400 38.546 1.00 54.33 C ANISOU 270 CB LYS A 66 8923 3575 8142 -157 752 -134 C ATOM 271 CG LYS A 66 -54.925 0.669 37.760 1.00 55.61 C ANISOU 271 CG LYS A 66 9071 3574 8484 -193 875 -132 C ATOM 272 CD LYS A 66 -55.718 1.941 37.566 1.00 56.49 C ANISOU 272 CD LYS A 66 9203 3524 8734 -148 1023 -84 C ATOM 273 CE LYS A 66 -54.968 2.989 36.771 1.00 58.26 C ANISOU 273 CE LYS A 66 9412 3570 9153 -179 1167 -62 C ATOM 274 NZ LYS A 66 -55.770 4.223 36.600 1.00 59.91 N ANISOU 274 NZ LYS A 66 9645 3610 9506 -122 1326 0 N ATOM 275 N SER A 67 -53.686 -1.388 40.834 1.00 59.89 N ANISOU 275 N SER A 67 9541 4513 8699 -279 568 -507 N ATOM 276 CA SER A 67 -52.546 -1.095 41.692 1.00 65.18 C ANISOU 276 CA SER A 67 10150 5226 9390 -348 548 -720 C ATOM 277 C SER A 67 -51.458 -2.167 41.620 1.00 68.26 C ANISOU 277 C SER A 67 10507 5747 9679 -371 441 -733 C ATOM 278 O SER A 67 -50.281 -1.837 41.502 1.00 73.03 O ANISOU 278 O SER A 67 11058 6332 10356 -439 453 -844 O ATOM 279 CB SER A 67 -53.003 -0.897 43.116 1.00 65.68 C ANISOU 279 CB SER A 67 10195 5374 9384 -328 527 -863 C ATOM 280 OG SER A 67 -53.928 0.177 43.203 1.00 68.37 O ANISOU 280 OG SER A 67 10561 5584 9833 -310 634 -869 O ATOM 281 N ASP A 68 -51.851 -3.443 41.711 1.00 71.21 N ANISOU 281 N ASP A 68 10909 6251 9894 -313 344 -624 N ATOM 282 CA ASP A 68 -50.895 -4.542 41.692 1.00 71.30 C ANISOU 282 CA ASP A 68 10895 6388 9805 -318 246 -624 C ATOM 283 C ASP A 68 -50.173 -4.588 40.344 1.00 71.95 C ANISOU 283 C ASP A 68 10976 6392 9970 -354 267 -545 C ATOM 284 O ASP A 68 -50.723 -5.076 39.358 1.00 70.44 O ANISOU 284 O ASP A 68 10826 6167 9767 -319 266 -380 O ATOM 285 CB ASP A 68 -51.588 -5.873 41.999 1.00 71.08 C ANISOU 285 CB ASP A 68 10903 6482 9619 -246 162 -505 C ATOM 286 CG ASP A 68 -50.649 -7.069 42.056 1.00 72.17 C ANISOU 286 CG ASP A 68 11019 6747 9654 -236 68 -496 C ATOM 287 OD1 ASP A 68 -49.428 -6.872 41.882 1.00 72.88 O ANISOU 287 OD1 ASP A 68 11061 6848 9780 -285 57 -589 O ATOM 288 OD2 ASP A 68 -51.148 -8.192 42.269 1.00 71.33 O ANISOU 288 OD2 ASP A 68 10939 6720 9440 -179 14 -393 O ATOM 289 N LYS A 69 -48.919 -4.110 40.325 1.00 71.43 N ANISOU 289 N LYS A 69 10850 6311 9977 -423 283 -674 N ATOM 290 CA LYS A 69 -48.114 -4.098 39.111 1.00 69.59 C ANISOU 290 CA LYS A 69 10605 6011 9823 -459 310 -610 C ATOM 291 C LYS A 69 -47.211 -5.331 39.047 1.00 66.73 C ANISOU 291 C LYS A 69 10219 5790 9343 -451 200 -602 C ATOM 292 O LYS A 69 -46.275 -5.368 38.252 1.00 61.83 O ANISOU 292 O LYS A 69 9570 5148 8772 -487 208 -592 O ATOM 293 CB LYS A 69 -47.276 -2.818 39.024 1.00 71.47 C ANISOU 293 CB LYS A 69 10786 6129 10237 -546 410 -745 C ATOM 294 CG LYS A 69 -48.070 -1.520 38.950 1.00 72.62 C ANISOU 294 CG LYS A 69 10955 6101 10534 -553 543 -744 C ATOM 295 CD LYS A 69 -47.197 -0.288 38.840 1.00 75.27 C ANISOU 295 CD LYS A 69 11230 6296 11071 -646 660 -879 C ATOM 296 CE LYS A 69 -47.991 0.999 38.767 1.00 76.71 C ANISOU 296 CE LYS A 69 11438 6286 11419 -646 807 -870 C ATOM 297 NZ LYS A 69 -47.105 2.184 38.661 1.00 78.34 N ANISOU 297 NZ LYS A 69 11580 6334 11850 -743 937 -1006 N ATOM 298 N GLU A 70 -47.487 -6.331 39.896 1.00 66.44 N ANISOU 298 N GLU A 70 10194 5897 9153 -397 106 -599 N ATOM 299 CA GLU A 70 -46.707 -7.561 39.905 1.00 62.63 C ANISOU 299 CA GLU A 70 9693 5544 8557 -372 10 -578 C ATOM 300 C GLU A 70 -47.610 -8.726 39.496 1.00 55.64 C ANISOU 300 C GLU A 70 8871 4681 7586 -302 -33 -403 C ATOM 301 O GLU A 70 -47.152 -9.860 39.392 1.00 54.28 O ANISOU 301 O GLU A 70 8697 4594 7331 -271 -102 -356 O ATOM 302 CB GLU A 70 -46.108 -7.797 41.294 1.00 67.97 C ANISOU 302 CB GLU A 70 10314 6382 9127 -358 -53 -727 C ATOM 303 CG GLU A 70 -45.224 -6.659 41.783 1.00 72.55 C ANISOU 303 CG GLU A 70 10813 6958 9793 -433 -15 -937 C ATOM 304 CD GLU A 70 -44.016 -6.353 40.914 1.00 75.98 C ANISOU 304 CD GLU A 70 11196 7340 10330 -506 8 -980 C ATOM 305 OE1 GLU A 70 -43.928 -5.216 40.405 1.00 81.15 O ANISOU 305 OE1 GLU A 70 11836 7844 11151 -577 108 -1025 O ATOM 306 OE2 GLU A 70 -43.157 -7.244 40.764 1.00 79.48 O ANISOU 306 OE2 GLU A 70 11613 7893 10693 -488 -64 -965 O ATOM 307 N ARG A 71 -48.888 -8.405 39.254 1.00 50.35 N ANISOU 307 N ARG A 71 8251 3929 6949 -280 15 -316 N ATOM 308 CA ARG A 71 -49.932 -9.344 38.865 1.00 45.96 C ANISOU 308 CA ARG A 71 7744 3381 6335 -225 -10 -168 C ATOM 309 C ARG A 71 -49.476 -10.276 37.742 1.00 41.52 C ANISOU 309 C ARG A 71 7185 2827 5762 -218 -49 -79 C ATOM 310 O ARG A 71 -48.844 -9.837 36.785 1.00 40.27 O ANISOU 310 O ARG A 71 7009 2616 5674 -250 -19 -74 O ATOM 311 CB ARG A 71 -51.164 -8.533 38.445 1.00 48.45 C ANISOU 311 CB ARG A 71 8094 3594 6722 -214 65 -102 C ATOM 312 CG ARG A 71 -50.907 -7.579 37.285 1.00 50.13 C ANISOU 312 CG ARG A 71 8301 3692 7055 -244 142 -74 C ATOM 313 CD ARG A 71 -52.084 -6.680 36.957 1.00 52.61 C ANISOU 313 CD ARG A 71 8643 3909 7436 -218 227 -8 C ATOM 314 NE ARG A 71 -51.784 -5.801 35.834 1.00 54.62 N ANISOU 314 NE ARG A 71 8891 4060 7803 -231 313 40 N ATOM 315 CZ ARG A 71 -52.599 -4.855 35.379 1.00 54.67 C ANISOU 315 CZ ARG A 71 8914 3968 7886 -200 408 109 C ATOM 316 NH1 ARG A 71 -53.734 -4.607 36.005 1.00 56.78 N ANISOU 316 NH1 ARG A 71 9207 4230 8137 -165 425 117 N ATOM 317 NH2 ARG A 71 -52.253 -4.121 34.336 1.00 53.97 N ANISOU 317 NH2 ARG A 71 8817 3792 7896 -199 494 174 N ATOM 318 N TYR A 72 -49.808 -11.574 37.873 1.00 37.14 N ANISOU 318 N TYR A 72 6649 2338 5124 -174 -108 -8 N ATOM 319 CA TYR A 72 -49.458 -12.566 36.867 1.00 35.58 C ANISOU 319 CA TYR A 72 6451 2149 4915 -163 -147 62 C ATOM 320 C TYR A 72 -50.171 -13.889 37.152 1.00 34.77 C ANISOU 320 C TYR A 72 6373 2086 4749 -116 -187 138 C ATOM 321 O TYR A 72 -50.597 -14.131 38.276 1.00 33.89 O ANISOU 321 O TYR A 72 6272 2019 4585 -88 -193 133 O ATOM 322 CB TYR A 72 -47.956 -12.873 36.856 1.00 34.84 C ANISOU 322 CB TYR A 72 6320 2113 4802 -180 -188 -1 C ATOM 323 CG TYR A 72 -47.444 -13.565 38.096 1.00 34.63 C ANISOU 323 CG TYR A 72 6279 2195 4683 -147 -241 -51 C ATOM 324 CD1 TYR A 72 -47.467 -12.950 39.337 1.00 35.12 C ANISOU 324 CD1 TYR A 72 6323 2309 4709 -144 -234 -140 C ATOM 325 CD2 TYR A 72 -47.025 -14.885 38.045 1.00 34.10 C ANISOU 325 CD2 TYR A 72 6213 2186 4556 -104 -295 -1 C ATOM 326 CE1 TYR A 72 -47.021 -13.596 40.478 1.00 35.22 C ANISOU 326 CE1 TYR A 72 6316 2450 4616 -94 -281 -175 C ATOM 327 CE2 TYR A 72 -46.579 -15.551 39.176 1.00 34.29 C ANISOU 327 CE2 TYR A 72 6223 2318 4486 -53 -334 -22 C ATOM 328 CZ TYR A 72 -46.573 -14.905 40.397 1.00 35.17 C ANISOU 328 CZ TYR A 72 6312 2501 4547 -43 -329 -105 C ATOM 329 OH TYR A 72 -46.142 -15.559 41.525 1.00 35.58 O ANISOU 329 OH TYR A 72 6343 2689 4487 26 -366 -119 O ATOM 330 N LEU A 73 -50.294 -14.727 36.112 1.00 35.57 N ANISOU 330 N LEU A 73 6478 2173 4863 -107 -207 206 N ATOM 331 CA LEU A 73 -50.880 -16.059 36.211 1.00 36.69 C ANISOU 331 CA LEU A 73 6634 2330 4975 -73 -235 269 C ATOM 332 C LEU A 73 -50.067 -16.991 35.316 1.00 37.12 C ANISOU 332 C LEU A 73 6673 2396 5034 -70 -274 279 C ATOM 333 O LEU A 73 -50.397 -17.185 34.150 1.00 39.38 O ANISOU 333 O LEU A 73 6950 2656 5354 -76 -273 308 O ATOM 334 CB LEU A 73 -52.360 -16.048 35.808 1.00 37.12 C ANISOU 334 CB LEU A 73 6701 2342 5060 -68 -204 329 C ATOM 335 CG LEU A 73 -53.061 -17.411 35.848 1.00 37.72 C ANISOU 335 CG LEU A 73 6780 2416 5133 -48 -219 384 C ATOM 336 CD1 LEU A 73 -53.336 -17.846 37.274 1.00 37.81 C ANISOU 336 CD1 LEU A 73 6809 2453 5101 -19 -210 403 C ATOM 337 CD2 LEU A 73 -54.361 -17.387 35.055 1.00 38.34 C ANISOU 337 CD2 LEU A 73 6847 2466 5251 -53 -197 420 C ATOM 338 N TYR A 74 -48.964 -17.506 35.868 1.00 38.14 N ANISOU 338 N TYR A 74 6792 2578 5121 -54 -308 249 N ATOM 339 CA TYR A 74 -48.070 -18.411 35.167 1.00 38.76 C ANISOU 339 CA TYR A 74 6855 2673 5199 -43 -345 252 C ATOM 340 C TYR A 74 -48.685 -19.802 35.145 1.00 38.39 C ANISOU 340 C TYR A 74 6824 2602 5160 -10 -352 314 C ATOM 341 O TYR A 74 -49.103 -20.295 36.184 1.00 39.49 O ANISOU 341 O TYR A 74 6981 2750 5273 21 -341 349 O ATOM 342 CB TYR A 74 -46.705 -18.448 35.855 1.00 39.90 C ANISOU 342 CB TYR A 74 6976 2892 5291 -28 -376 198 C ATOM 343 CG TYR A 74 -45.684 -19.371 35.236 1.00 40.71 C ANISOU 343 CG TYR A 74 7060 3019 5386 -7 -413 199 C ATOM 344 CD1 TYR A 74 -45.322 -19.249 33.906 1.00 41.17 C ANISOU 344 CD1 TYR A 74 7101 3053 5486 -34 -417 191 C ATOM 345 CD2 TYR A 74 -45.002 -20.299 36.007 1.00 42.24 C ANISOU 345 CD2 TYR A 74 7248 3275 5523 48 -441 210 C ATOM 346 CE1 TYR A 74 -44.351 -20.057 33.341 1.00 42.56 C ANISOU 346 CE1 TYR A 74 7257 3258 5654 -13 -450 184 C ATOM 347 CE2 TYR A 74 -44.022 -21.111 35.462 1.00 43.96 C ANISOU 347 CE2 TYR A 74 7449 3517 5737 74 -472 209 C ATOM 348 CZ TYR A 74 -43.693 -20.988 34.124 1.00 43.92 C ANISOU 348 CZ TYR A 74 7427 3481 5779 39 -478 190 C ATOM 349 OH TYR A 74 -42.733 -21.797 33.575 1.00 47.78 O ANISOU 349 OH TYR A 74 7896 3996 6262 67 -507 185 O ATOM 350 N ILE A 75 -48.732 -20.405 33.952 1.00 38.99 N ANISOU 350 N ILE A 75 6887 2649 5277 -17 -364 322 N ATOM 351 CA ILE A 75 -49.297 -21.730 33.742 1.00 38.92 C ANISOU 351 CA ILE A 75 6882 2600 5305 0 -363 358 C ATOM 352 C ILE A 75 -48.258 -22.534 32.968 1.00 37.80 C ANISOU 352 C ILE A 75 6721 2469 5172 14 -396 334 C ATOM 353 O ILE A 75 -47.891 -22.139 31.860 1.00 37.03 O ANISOU 353 O ILE A 75 6598 2389 5080 -3 -412 299 O ATOM 354 CB ILE A 75 -50.627 -21.622 32.967 1.00 40.55 C ANISOU 354 CB ILE A 75 7077 2769 5560 -25 -343 365 C ATOM 355 CG1 ILE A 75 -51.577 -20.603 33.604 1.00 43.04 C ANISOU 355 CG1 ILE A 75 7408 3081 5863 -37 -309 385 C ATOM 356 CG2 ILE A 75 -51.271 -22.991 32.805 1.00 39.76 C ANISOU 356 CG2 ILE A 75 6968 2619 5519 -20 -333 381 C ATOM 357 CD1 ILE A 75 -52.866 -20.388 32.838 1.00 43.73 C ANISOU 357 CD1 ILE A 75 7476 3153 5986 -53 -290 393 C ATOM 358 N TYR A 76 -47.794 -23.656 33.542 1.00 36.42 N ANISOU 358 N TYR A 76 6555 2285 4996 56 -399 360 N ATOM 359 CA TYR A 76 -46.765 -24.439 32.878 1.00 35.93 C ANISOU 359 CA TYR A 76 6475 2231 4942 78 -427 336 C ATOM 360 C TYR A 76 -47.069 -25.933 32.937 1.00 36.28 C ANISOU 360 C TYR A 76 6527 2205 5052 110 -404 370 C ATOM 361 O TYR A 76 -47.997 -26.368 33.620 1.00 35.47 O ANISOU 361 O TYR A 76 6442 2047 4984 116 -362 420 O ATOM 362 CB TYR A 76 -45.386 -24.175 33.494 1.00 36.40 C ANISOU 362 CB TYR A 76 6528 2370 4931 111 -453 323 C ATOM 363 CG TYR A 76 -45.227 -24.588 34.936 1.00 37.79 C ANISOU 363 CG TYR A 76 6722 2576 5057 170 -440 374 C ATOM 364 CD1 TYR A 76 -45.965 -23.997 35.950 1.00 38.17 C ANISOU 364 CD1 TYR A 76 6789 2640 5075 170 -416 399 C ATOM 365 CD2 TYR A 76 -44.356 -25.611 35.278 1.00 38.69 C ANISOU 365 CD2 TYR A 76 6834 2714 5152 241 -447 405 C ATOM 366 CE1 TYR A 76 -45.823 -24.395 37.269 1.00 39.93 C ANISOU 366 CE1 TYR A 76 7021 2914 5235 240 -401 452 C ATOM 367 CE2 TYR A 76 -44.203 -26.023 36.591 1.00 40.49 C ANISOU 367 CE2 TYR A 76 7073 2989 5321 316 -429 468 C ATOM 368 CZ TYR A 76 -44.941 -25.414 37.589 1.00 40.23 C ANISOU 368 CZ TYR A 76 7054 2985 5246 317 -407 492 C ATOM 369 OH TYR A 76 -44.783 -25.834 38.881 1.00 41.43 O ANISOU 369 OH TYR A 76 7211 3205 5323 407 -387 560 O ATOM 370 N GLN A 77 -46.247 -26.701 32.209 1.00 36.93 N ANISOU 370 N GLN A 77 6591 2283 5156 130 -425 340 N ATOM 371 CA GLN A 77 -46.383 -28.146 32.128 1.00 38.53 C ANISOU 371 CA GLN A 77 6796 2402 5441 159 -396 357 C ATOM 372 C GLN A 77 -45.001 -28.771 32.258 1.00 38.52 C ANISOU 372 C GLN A 77 6793 2430 5410 224 -413 366 C ATOM 373 O GLN A 77 -44.011 -28.134 31.899 1.00 38.22 O ANISOU 373 O GLN A 77 6737 2479 5305 224 -459 326 O ATOM 374 CB GLN A 77 -46.887 -28.569 30.747 1.00 39.56 C ANISOU 374 CB GLN A 77 6890 2492 5647 118 -403 279 C ATOM 375 CG GLN A 77 -48.070 -27.762 30.241 1.00 41.09 C ANISOU 375 CG GLN A 77 7066 2699 5847 60 -404 249 C ATOM 376 CD GLN A 77 -49.303 -27.829 31.104 1.00 41.83 C ANISOU 376 CD GLN A 77 7177 2733 5981 43 -355 301 C ATOM 377 OE1 GLN A 77 -49.379 -28.580 32.073 1.00 42.18 O ANISOU 377 OE1 GLN A 77 7248 2714 6062 73 -311 366 O ATOM 378 NE2 GLN A 77 -50.302 -27.051 30.719 1.00 41.66 N ANISOU 378 NE2 GLN A 77 7137 2735 5954 1 -356 279 N ATOM 379 N ASN A 78 -44.957 -30.013 32.764 1.00 38.42 N ANISOU 379 N ASN A 78 6797 2343 5455 280 -369 422 N ATOM 380 CA ASN A 78 -43.731 -30.782 32.884 1.00 38.73 C ANISOU 380 CA ASN A 78 6834 2400 5478 357 -374 442 C ATOM 381 C ASN A 78 -43.776 -31.841 31.788 1.00 38.74 C ANISOU 381 C ASN A 78 6817 2306 5594 347 -360 384 C ATOM 382 O ASN A 78 -44.744 -32.591 31.700 1.00 38.81 O ANISOU 382 O ASN A 78 6828 2196 5719 324 -305 388 O ATOM 383 CB ASN A 78 -43.552 -31.428 34.264 1.00 39.36 C ANISOU 383 CB ASN A 78 6944 2472 5537 450 -323 561 C ATOM 384 CG ASN A 78 -43.442 -30.432 35.399 1.00 39.02 C ANISOU 384 CG ASN A 78 6909 2549 5368 472 -342 600 C ATOM 385 OD1 ASN A 78 -44.237 -30.457 36.335 1.00 38.16 O ANISOU 385 OD1 ASN A 78 6822 2419 5255 490 -294 676 O ATOM 386 ND2 ASN A 78 -42.450 -29.555 35.338 1.00 39.71 N ANISOU 386 ND2 ASN A 78 6970 2765 5354 469 -406 542 N ATOM 387 N ILE A 79 -42.746 -31.876 30.937 1.00 38.53 N ANISOU 387 N ILE A 79 6763 2335 5539 360 -407 319 N ATOM 388 CA ILE A 79 -42.715 -32.817 29.829 1.00 39.47 C ANISOU 388 CA ILE A 79 6856 2383 5757 353 -400 242 C ATOM 389 C ILE A 79 -41.320 -33.418 29.684 1.00 40.05 C ANISOU 389 C ILE A 79 6921 2490 5805 431 -417 241 C ATOM 390 O ILE A 79 -40.450 -33.213 30.525 1.00 40.05 O ANISOU 390 O ILE A 79 6934 2565 5717 494 -428 309 O ATOM 391 CB ILE A 79 -43.135 -32.104 28.523 1.00 38.14 C ANISOU 391 CB ILE A 79 6645 2268 5576 278 -447 133 C ATOM 392 CG1 ILE A 79 -42.115 -31.039 28.109 1.00 37.13 C ANISOU 392 CG1 ILE A 79 6498 2279 5327 279 -509 112 C ATOM 393 CG2 ILE A 79 -44.536 -31.529 28.648 1.00 37.68 C ANISOU 393 CG2 ILE A 79 6590 2185 5541 212 -430 136 C ATOM 394 CD1 ILE A 79 -42.419 -30.372 26.798 1.00 36.52 C ANISOU 394 CD1 ILE A 79 6379 2266 5231 229 -543 29 C ATOM 395 N LYS A 80 -41.155 -34.195 28.607 1.00 41.19 N ANISOU 395 N LYS A 80 7036 2586 6027 429 -417 154 N ATOM 396 CA LYS A 80 -39.886 -34.802 28.254 1.00 41.64 C ANISOU 396 CA LYS A 80 7078 2672 6070 500 -433 135 C ATOM 397 C LYS A 80 -39.978 -35.134 26.767 1.00 41.89 C ANISOU 397 C LYS A 80 7062 2696 6158 462 -456 -1 C ATOM 398 O LYS A 80 -40.106 -36.293 26.383 1.00 44.01 O ANISOU 398 O LYS A 80 7321 2853 6547 481 -414 -51 O ATOM 399 CB LYS A 80 -39.583 -36.022 29.131 1.00 43.14 C ANISOU 399 CB LYS A 80 7300 2756 6333 593 -362 228 C ATOM 400 CG LYS A 80 -38.201 -36.615 28.904 1.00 44.27 C ANISOU 400 CG LYS A 80 7429 2941 6449 685 -376 224 C ATOM 401 CD LYS A 80 -37.106 -35.583 29.135 1.00 44.33 C ANISOU 401 CD LYS A 80 7417 3135 6288 707 -449 238 C ATOM 402 CE LYS A 80 -35.702 -36.102 28.918 1.00 45.28 C ANISOU 402 CE LYS A 80 7514 3320 6370 799 -468 233 C ATOM 403 NZ LYS A 80 -34.704 -35.020 29.109 1.00 43.88 N ANISOU 403 NZ LYS A 80 7304 3328 6041 801 -538 227 N ATOM 404 N GLU A 81 -39.906 -34.089 25.939 1.00 40.86 N ANISOU 404 N GLU A 81 6898 2687 5939 413 -516 -63 N ATOM 405 CA GLU A 81 -40.059 -34.225 24.503 1.00 40.60 C ANISOU 405 CA GLU A 81 6810 2689 5926 385 -544 -190 C ATOM 406 C GLU A 81 -38.891 -33.598 23.754 1.00 41.78 C ANISOU 406 C GLU A 81 6924 2984 5964 409 -599 -218 C ATOM 407 O GLU A 81 -38.183 -32.739 24.279 1.00 41.58 O ANISOU 407 O GLU A 81 6912 3041 5846 417 -620 -150 O ATOM 408 CB GLU A 81 -41.348 -33.511 24.086 1.00 38.93 C ANISOU 408 CB GLU A 81 6580 2497 5714 308 -551 -228 C ATOM 409 CG GLU A 81 -42.606 -34.067 24.734 1.00 38.23 C ANISOU 409 CG GLU A 81 6512 2272 5739 273 -495 -211 C ATOM 410 CD GLU A 81 -43.882 -33.288 24.447 1.00 37.70 C ANISOU 410 CD GLU A 81 6424 2239 5660 203 -504 -238 C ATOM 411 OE1 GLU A 81 -43.794 -32.223 23.779 1.00 36.52 O ANISOU 411 OE1 GLU A 81 6249 2220 5406 190 -550 -254 O ATOM 412 OE2 GLU A 81 -44.970 -33.748 24.879 1.00 37.09 O ANISOU 412 OE2 GLU A 81 6352 2058 5682 167 -457 -237 O ATOM 413 N ASN A 82 -38.723 -34.049 22.506 1.00 43.33 N ANISOU 413 N ASN A 82 7069 3217 6176 418 -618 -330 N ATOM 414 CA ASN A 82 -37.707 -33.536 21.602 1.00 44.35 C ANISOU 414 CA ASN A 82 7155 3488 6207 443 -662 -365 C ATOM 415 C ASN A 82 -38.428 -32.580 20.651 1.00 42.44 C ANISOU 415 C ASN A 82 6872 3347 5905 395 -685 -406 C ATOM 416 O ASN A 82 -39.389 -32.974 20.000 1.00 41.52 O ANISOU 416 O ASN A 82 6723 3213 5838 374 -682 -493 O ATOM 417 CB ASN A 82 -36.975 -34.682 20.891 1.00 47.19 C ANISOU 417 CB ASN A 82 7482 3837 6611 502 -663 -453 C ATOM 418 CG ASN A 82 -35.891 -34.211 19.944 1.00 49.69 C ANISOU 418 CG ASN A 82 7748 4308 6823 535 -704 -486 C ATOM 419 OD1 ASN A 82 -35.662 -33.012 19.791 1.00 51.59 O ANISOU 419 OD1 ASN A 82 7976 4657 6965 510 -724 -439 O ATOM 420 ND2 ASN A 82 -35.214 -35.148 19.300 1.00 52.24 N ANISOU 420 ND2 ASN A 82 8039 4635 7174 592 -708 -567 N ATOM 421 N TRP A 83 -37.996 -31.312 20.611 1.00 41.41 N ANISOU 421 N TRP A 83 6737 3320 5675 382 -701 -343 N ATOM 422 CA TRP A 83 -38.636 -30.310 19.768 1.00 41.23 C ANISOU 422 CA TRP A 83 6679 3393 5591 353 -708 -351 C ATOM 423 C TRP A 83 -37.703 -29.786 18.676 1.00 42.54 C ANISOU 423 C TRP A 83 6791 3704 5667 388 -725 -365 C ATOM 424 O TRP A 83 -37.932 -28.698 18.145 1.00 43.60 O ANISOU 424 O TRP A 83 6902 3926 5737 377 -717 -326 O ATOM 425 CB TRP A 83 -39.155 -29.150 20.628 1.00 39.07 C ANISOU 425 CB TRP A 83 6448 3099 5298 304 -689 -253 C ATOM 426 CG TRP A 83 -40.302 -29.465 21.540 1.00 37.58 C ANISOU 426 CG TRP A 83 6303 2793 5181 269 -668 -235 C ATOM 427 CD1 TRP A 83 -40.966 -30.649 21.690 1.00 37.65 C ANISOU 427 CD1 TRP A 83 6316 2702 5285 269 -655 -289 C ATOM 428 CD2 TRP A 83 -40.966 -28.525 22.401 1.00 36.25 C ANISOU 428 CD2 TRP A 83 6173 2594 5003 227 -648 -157 C ATOM 429 NE1 TRP A 83 -41.974 -30.517 22.609 1.00 37.32 N ANISOU 429 NE1 TRP A 83 6314 2575 5289 230 -628 -239 N ATOM 430 CE2 TRP A 83 -42.004 -29.220 23.055 1.00 36.29 C ANISOU 430 CE2 TRP A 83 6207 2492 5090 207 -627 -160 C ATOM 431 CE3 TRP A 83 -40.781 -27.165 22.683 1.00 35.60 C ANISOU 431 CE3 TRP A 83 6102 2559 4863 203 -639 -89 C ATOM 432 CZ2 TRP A 83 -42.848 -28.597 23.974 1.00 36.02 C ANISOU 432 CZ2 TRP A 83 6211 2411 5062 170 -604 -95 C ATOM 433 CZ3 TRP A 83 -41.615 -26.551 23.593 1.00 34.90 C ANISOU 433 CZ3 TRP A 83 6054 2418 4789 165 -617 -36 C ATOM 434 CH2 TRP A 83 -42.639 -27.258 24.223 1.00 34.78 C ANISOU 434 CH2 TRP A 83 6066 2310 4837 152 -603 -37 C ATOM 435 N SER A 84 -36.689 -30.577 18.307 1.00 43.87 N ANISOU 435 N SER A 84 6935 3897 5835 438 -740 -416 N ATOM 436 CA SER A 84 -35.727 -30.160 17.295 1.00 44.35 C ANISOU 436 CA SER A 84 6940 4099 5810 476 -751 -426 C ATOM 437 C SER A 84 -36.332 -30.118 15.891 1.00 43.81 C ANISOU 437 C SER A 84 6805 4146 5692 502 -761 -501 C ATOM 438 O SER A 84 -35.744 -29.512 15.001 1.00 42.91 O ANISOU 438 O SER A 84 6643 4169 5492 536 -759 -484 O ATOM 439 CB SER A 84 -34.509 -31.052 17.317 1.00 45.83 C ANISOU 439 CB SER A 84 7118 4287 6009 529 -764 -463 C ATOM 440 OG SER A 84 -33.844 -30.973 18.570 1.00 47.58 O ANISOU 440 OG SER A 84 7386 4445 6248 521 -758 -387 O HETATM 441 N MSE A 85 -37.500 -30.751 15.697 1.00 43.48 N ANISOU 441 N MSE A 85 6754 4062 5703 490 -769 -585 N HETATM 442 CA MSE A 85 -38.132 -30.800 14.386 1.00 44.31 C ANISOU 442 CA MSE A 85 6782 4301 5753 523 -786 -679 C HETATM 443 C MSE A 85 -39.169 -29.689 14.203 1.00 42.63 C ANISOU 443 C MSE A 85 6560 4151 5485 502 -773 -615 C HETATM 444 O MSE A 85 -39.904 -29.700 13.218 1.00 42.77 O ANISOU 444 O MSE A 85 6509 4290 5451 534 -788 -689 O HETATM 445 CB MSE A 85 -38.778 -32.176 14.166 1.00 46.43 C ANISOU 445 CB MSE A 85 7022 4503 6115 522 -801 -839 C HETATM 446 CG MSE A 85 -39.981 -32.477 15.050 1.00 48.07 C ANISOU 446 CG MSE A 85 7271 4561 6433 456 -783 -843 C HETATM 447 SE MSE A 85 -39.520 -33.213 16.824 0.66 53.57 SE ANISOU 447 SE MSE A 85 8074 5011 7266 424 -746 -756 SE HETATM 448 CE MSE A 85 -38.096 -34.460 16.292 1.00 53.08 C ANISOU 448 CE MSE A 85 7985 4948 7233 499 -755 -850 C ATOM 449 N TYR A 86 -39.222 -28.728 15.135 1.00 40.87 N ANISOU 449 N TYR A 86 6399 3858 5269 457 -744 -483 N ATOM 450 CA TYR A 86 -40.176 -27.632 15.051 1.00 39.87 C ANISOU 450 CA TYR A 86 6272 3774 5102 443 -721 -410 C ATOM 451 C TYR A 86 -39.401 -26.318 15.045 1.00 38.60 C ANISOU 451 C TYR A 86 6123 3661 4882 448 -682 -277 C ATOM 452 O TYR A 86 -38.276 -26.268 15.542 1.00 37.67 O ANISOU 452 O TYR A 86 6031 3502 4780 435 -675 -242 O ATOM 453 CB TYR A 86 -41.168 -27.717 16.213 1.00 39.51 C ANISOU 453 CB TYR A 86 6287 3581 5144 377 -712 -390 C ATOM 454 CG TYR A 86 -41.929 -29.015 16.276 1.00 40.63 C ANISOU 454 CG TYR A 86 6414 3652 5372 361 -733 -516 C ATOM 455 CD1 TYR A 86 -42.800 -29.391 15.266 1.00 41.68 C ANISOU 455 CD1 TYR A 86 6468 3885 5484 384 -754 -631 C ATOM 456 CD2 TYR A 86 -41.707 -29.913 17.306 1.00 41.23 C ANISOU 456 CD2 TYR A 86 6544 3568 5552 331 -726 -526 C ATOM 457 CE1 TYR A 86 -43.477 -30.601 15.311 1.00 42.31 C ANISOU 457 CE1 TYR A 86 6522 3887 5664 358 -765 -766 C ATOM 458 CE2 TYR A 86 -42.367 -31.131 17.362 1.00 42.04 C ANISOU 458 CE2 TYR A 86 6631 3583 5760 313 -726 -637 C ATOM 459 CZ TYR A 86 -43.256 -31.474 16.361 1.00 42.47 C ANISOU 459 CZ TYR A 86 6604 3719 5811 319 -744 -766 C ATOM 460 OH TYR A 86 -43.911 -32.675 16.423 1.00 43.85 O ANISOU 460 OH TYR A 86 6754 3794 6111 290 -736 -892 O ATOM 461 N ASN A 87 -40.008 -25.258 14.496 1.00 38.59 N ANISOU 461 N ASN A 87 6097 3744 4818 470 -649 -204 N ATOM 462 CA ASN A 87 -39.325 -23.972 14.438 1.00 38.48 C ANISOU 462 CA ASN A 87 6090 3758 4771 473 -592 -75 C ATOM 463 C ASN A 87 -40.129 -22.849 15.102 1.00 37.15 C ANISOU 463 C ASN A 87 5966 3516 4632 432 -544 25 C ATOM 464 O ASN A 87 -39.623 -21.730 15.201 1.00 35.92 O ANISOU 464 O ASN A 87 5820 3347 4478 421 -483 128 O ATOM 465 CB ASN A 87 -38.968 -23.569 13.004 1.00 40.61 C ANISOU 465 CB ASN A 87 6283 4211 4935 560 -568 -46 C ATOM 466 CG ASN A 87 -38.026 -24.531 12.310 1.00 42.20 C ANISOU 466 CG ASN A 87 6436 4498 5100 606 -607 -139 C ATOM 467 OD1 ASN A 87 -37.676 -25.576 12.853 1.00 44.13 O ANISOU 467 OD1 ASN A 87 6703 4658 5404 576 -653 -231 O ATOM 468 ND2 ASN A 87 -37.624 -24.200 11.096 1.00 43.36 N ANISOU 468 ND2 ASN A 87 6512 4815 5146 688 -585 -110 N ATOM 469 N ASN A 88 -41.356 -23.108 15.574 1.00 36.43 N ANISOU 469 N ASN A 88 5899 3368 4574 407 -563 -6 N ATOM 470 CA ASN A 88 -42.050 -21.992 16.202 1.00 36.12 C ANISOU 470 CA ASN A 88 5901 3262 4560 375 -513 91 C ATOM 471 C ASN A 88 -43.325 -22.382 16.941 1.00 35.28 C ANISOU 471 C ASN A 88 5827 3075 4502 337 -536 52 C ATOM 472 O ASN A 88 -43.862 -23.485 16.787 1.00 35.49 O ANISOU 472 O ASN A 88 5831 3112 4542 339 -584 -51 O ATOM 473 CB ASN A 88 -42.466 -20.920 15.185 1.00 37.45 C ANISOU 473 CB ASN A 88 6025 3549 4654 443 -458 184 C ATOM 474 CG ASN A 88 -43.450 -21.409 14.141 1.00 38.84 C ANISOU 474 CG ASN A 88 6131 3873 4750 517 -492 124 C ATOM 475 OD1 ASN A 88 -43.137 -22.286 13.339 1.00 39.85 O ANISOU 475 OD1 ASN A 88 6202 4107 4829 560 -538 29 O ATOM 476 ND2 ASN A 88 -44.634 -20.818 14.113 1.00 39.69 N ANISOU 476 ND2 ASN A 88 6234 4004 4840 537 -469 171 N ATOM 477 N PHE A 89 -43.730 -21.437 17.800 1.00 34.16 N ANISOU 477 N PHE A 89 5736 2844 4398 296 -493 133 N ATOM 478 CA PHE A 89 -44.969 -21.453 18.556 1.00 34.19 C ANISOU 478 CA PHE A 89 5772 2775 4442 262 -495 130 C ATOM 479 C PHE A 89 -46.043 -20.715 17.771 1.00 35.17 C ANISOU 479 C PHE A 89 5856 2995 4511 316 -466 178 C ATOM 480 O PHE A 89 -45.769 -19.684 17.154 1.00 34.82 O ANISOU 480 O PHE A 89 5794 3011 4422 362 -412 271 O ATOM 481 CB PHE A 89 -44.861 -20.736 19.906 1.00 33.57 C ANISOU 481 CB PHE A 89 5765 2565 4424 200 -461 189 C ATOM 482 CG PHE A 89 -44.281 -21.516 21.056 1.00 32.92 C ANISOU 482 CG PHE A 89 5727 2385 4394 151 -493 144 C ATOM 483 CD1 PHE A 89 -44.993 -22.579 21.592 1.00 32.82 C ANISOU 483 CD1 PHE A 89 5730 2317 4421 134 -526 88 C ATOM 484 CD2 PHE A 89 -43.049 -21.202 21.605 1.00 32.78 C ANISOU 484 CD2 PHE A 89 5729 2336 4389 127 -483 160 C ATOM 485 CE1 PHE A 89 -44.506 -23.279 22.681 1.00 32.44 C ANISOU 485 CE1 PHE A 89 5724 2184 4416 107 -542 71 C ATOM 486 CE2 PHE A 89 -42.551 -21.925 22.679 1.00 32.40 C ANISOU 486 CE2 PHE A 89 5715 2223 4372 101 -513 126 C ATOM 487 CZ PHE A 89 -43.285 -22.957 23.215 1.00 32.37 C ANISOU 487 CZ PHE A 89 5734 2165 4400 98 -539 92 C ATOM 488 N TYR A 90 -47.250 -21.279 17.807 1.00 36.66 N ANISOU 488 N TYR A 90 6025 3196 4705 314 -496 118 N ATOM 489 CA TYR A 90 -48.411 -20.717 17.150 1.00 38.12 C ANISOU 489 CA TYR A 90 6163 3485 4833 369 -479 149 C ATOM 490 C TYR A 90 -49.475 -20.743 18.246 1.00 39.03 C ANISOU 490 C TYR A 90 6321 3490 5016 311 -476 145 C ATOM 491 O TYR A 90 -49.923 -21.820 18.652 1.00 38.81 O ANISOU 491 O TYR A 90 6289 3414 5040 268 -517 47 O ATOM 492 CB TYR A 90 -48.707 -21.533 15.888 1.00 39.91 C ANISOU 492 CB TYR A 90 6292 3883 4987 433 -528 44 C ATOM 493 CG TYR A 90 -49.600 -20.876 14.866 1.00 41.69 C ANISOU 493 CG TYR A 90 6443 4287 5108 528 -511 83 C ATOM 494 CD1 TYR A 90 -49.230 -19.665 14.301 1.00 42.57 C ANISOU 494 CD1 TYR A 90 6552 4469 5152 603 -444 228 C ATOM 495 CD2 TYR A 90 -50.728 -21.504 14.364 1.00 42.87 C ANISOU 495 CD2 TYR A 90 6511 4552 5224 553 -556 -26 C ATOM 496 CE1 TYR A 90 -49.994 -19.058 13.318 1.00 44.30 C ANISOU 496 CE1 TYR A 90 6698 4869 5262 715 -420 284 C ATOM 497 CE2 TYR A 90 -51.502 -20.914 13.376 1.00 44.81 C ANISOU 497 CE2 TYR A 90 6675 4997 5354 659 -545 8 C ATOM 498 CZ TYR A 90 -51.136 -19.682 12.856 1.00 45.86 C ANISOU 498 CZ TYR A 90 6814 5202 5408 748 -476 174 C ATOM 499 OH TYR A 90 -51.876 -19.065 11.877 1.00 49.15 O ANISOU 499 OH TYR A 90 7148 5825 5699 874 -454 232 O ATOM 500 N ILE A 91 -49.777 -19.559 18.795 1.00 38.62 N ANISOU 500 N ILE A 91 6315 3381 4976 307 -418 254 N ATOM 501 CA ILE A 91 -50.702 -19.419 19.909 1.00 38.67 C ANISOU 501 CA ILE A 91 6367 3283 5040 257 -406 264 C ATOM 502 C ILE A 91 -52.009 -18.774 19.467 1.00 38.34 C ANISOU 502 C ILE A 91 6285 3325 4954 311 -381 307 C ATOM 503 O ILE A 91 -52.057 -17.572 19.197 1.00 37.77 O ANISOU 503 O ILE A 91 6220 3276 4852 361 -320 415 O ATOM 504 CB ILE A 91 -50.028 -18.615 21.042 1.00 40.04 C ANISOU 504 CB ILE A 91 6622 3320 5269 206 -362 334 C ATOM 505 CG1 ILE A 91 -48.749 -19.313 21.516 1.00 40.59 C ANISOU 505 CG1 ILE A 91 6720 3331 5371 162 -393 286 C ATOM 506 CG2 ILE A 91 -50.993 -18.368 22.193 1.00 40.09 C ANISOU 506 CG2 ILE A 91 6673 3234 5323 165 -345 350 C ATOM 507 CD1 ILE A 91 -48.022 -18.591 22.624 1.00 41.39 C ANISOU 507 CD1 ILE A 91 6882 3327 5517 113 -359 327 C ATOM 508 N AGLU A 92 -53.067 -19.592 19.412 0.50 38.30 N ANISOU 508 N AGLU A 92 6235 3363 4955 302 -423 220 N ATOM 509 N BGLU A 92 -53.067 -19.592 19.430 0.50 38.37 N ANISOU 509 N BGLU A 92 6244 3368 4964 301 -423 220 N ATOM 510 CA AGLU A 92 -54.388 -19.128 19.031 0.50 38.93 C ANISOU 510 CA AGLU A 92 6262 3539 4988 354 -409 240 C ATOM 511 CA BGLU A 92 -54.390 -19.138 19.044 0.50 38.97 C ANISOU 511 CA BGLU A 92 6268 3543 4995 353 -410 239 C ATOM 512 C AGLU A 92 -55.081 -18.624 20.295 0.50 38.54 C ANISOU 512 C AGLU A 92 6279 3358 5004 304 -373 293 C ATOM 513 C BGLU A 92 -55.083 -18.625 20.303 0.50 38.56 C ANISOU 513 C BGLU A 92 6283 3361 5007 303 -373 293 C ATOM 514 O AGLU A 92 -55.666 -19.405 21.045 0.50 37.79 O ANISOU 514 O AGLU A 92 6192 3195 4971 241 -397 226 O ATOM 515 O BGLU A 92 -55.668 -19.400 21.057 0.50 37.80 O ANISOU 515 O BGLU A 92 6194 3194 4973 240 -396 227 O ATOM 516 CB AGLU A 92 -55.150 -20.245 18.315 0.50 39.48 C ANISOU 516 CB AGLU A 92 6233 3731 5036 363 -471 99 C ATOM 517 CB BGLU A 92 -55.143 -20.273 18.349 0.50 39.56 C ANISOU 517 CB BGLU A 92 6244 3735 5049 360 -471 97 C ATOM 518 CG AGLU A 92 -56.542 -19.844 17.867 0.50 40.25 C ANISOU 518 CG AGLU A 92 6256 3962 5075 422 -466 102 C ATOM 519 CG BGLU A 92 -54.382 -20.823 17.157 0.50 40.15 C ANISOU 519 CG BGLU A 92 6253 3942 5060 409 -510 26 C ATOM 520 CD AGLU A 92 -57.278 -20.924 17.094 0.50 41.05 C ANISOU 520 CD AGLU A 92 6237 4205 5155 429 -528 -64 C ATOM 521 CD BGLU A 92 -55.090 -21.896 16.352 0.50 41.15 C ANISOU 521 CD BGLU A 92 6264 4205 5163 421 -571 -140 C ATOM 522 OE1AGLU A 92 -56.685 -21.998 16.876 0.50 41.28 O ANISOU 522 OE1AGLU A 92 6245 4216 5223 387 -570 -182 O ATOM 523 OE1BGLU A 92 -56.238 -22.235 16.697 0.50 41.48 O ANISOU 523 OE1BGLU A 92 6271 4241 5247 386 -581 -203 O ATOM 524 OE2AGLU A 92 -58.441 -20.692 16.721 0.50 41.79 O ANISOU 524 OE2AGLU A 92 6252 4427 5196 476 -533 -83 O ATOM 525 OE2BGLU A 92 -54.481 -22.395 15.384 0.50 41.62 O ANISOU 525 OE2BGLU A 92 6265 4380 5168 463 -605 -216 O ATOM 526 N ILE A 93 -54.983 -17.308 20.523 1.00 38.77 N ANISOU 526 N ILE A 93 6354 3350 5026 335 -306 415 N ATOM 527 CA ILE A 93 -55.554 -16.672 21.700 1.00 38.94 C ANISOU 527 CA ILE A 93 6439 3253 5103 296 -265 466 C ATOM 528 C ILE A 93 -56.588 -15.625 21.299 1.00 39.98 C ANISOU 528 C ILE A 93 6543 3457 5190 377 -213 553 C ATOM 529 O ILE A 93 -56.552 -15.085 20.193 1.00 42.03 O ANISOU 529 O ILE A 93 6753 3837 5377 469 -187 612 O ATOM 530 CB ILE A 93 -54.424 -16.063 22.562 1.00 39.10 C ANISOU 530 CB ILE A 93 6543 3134 5179 247 -226 512 C ATOM 531 CG1 ILE A 93 -54.944 -15.489 23.884 1.00 39.28 C ANISOU 531 CG1 ILE A 93 6628 3037 5257 204 -189 540 C ATOM 532 CG2 ILE A 93 -53.632 -15.026 21.776 1.00 39.80 C ANISOU 532 CG2 ILE A 93 6628 3250 5242 303 -168 600 C ATOM 533 CD1 ILE A 93 -53.870 -14.893 24.767 1.00 39.22 C ANISOU 533 CD1 ILE A 93 6686 2912 5301 155 -156 557 C ATOM 534 N GLN A 94 -57.512 -15.362 22.232 1.00 39.46 N ANISOU 534 N GLN A 94 6506 3321 5163 349 -193 565 N ATOM 535 CA GLN A 94 -58.559 -14.374 22.051 1.00 39.23 C ANISOU 535 CA GLN A 94 6458 3344 5104 424 -139 648 C ATOM 536 C GLN A 94 -58.710 -13.555 23.328 1.00 38.01 C ANISOU 536 C GLN A 94 6386 3033 5019 382 -81 699 C ATOM 537 O GLN A 94 -58.842 -14.110 24.417 1.00 36.49 O ANISOU 537 O GLN A 94 6232 2752 4879 302 -107 641 O ATOM 538 CB GLN A 94 -59.904 -15.024 21.728 1.00 40.30 C ANISOU 538 CB GLN A 94 6509 3603 5198 447 -183 583 C ATOM 539 CG GLN A 94 -61.025 -14.003 21.581 1.00 41.19 C ANISOU 539 CG GLN A 94 6597 3779 5271 534 -128 672 C ATOM 540 CD GLN A 94 -62.353 -14.638 21.258 1.00 41.52 C ANISOU 540 CD GLN A 94 6541 3962 5271 556 -174 596 C ATOM 541 OE1 GLN A 94 -62.472 -15.856 21.149 1.00 40.80 O ANISOU 541 OE1 GLN A 94 6397 3908 5194 496 -242 467 O ATOM 542 NE2 GLN A 94 -63.367 -13.804 21.097 1.00 42.13 N ANISOU 542 NE2 GLN A 94 6586 4116 5303 642 -131 671 N ATOM 543 N ASN A 95 -58.699 -12.228 23.159 1.00 36.69 N ANISOU 543 N ASN A 95 6243 2840 4856 445 3 809 N ATOM 544 CA ASN A 95 -58.862 -11.289 24.252 1.00 36.11 C ANISOU 544 CA ASN A 95 6239 2627 4853 418 69 850 C ATOM 545 C ASN A 95 -60.292 -10.752 24.217 1.00 36.33 C ANISOU 545 C ASN A 95 6239 2710 4855 489 105 904 C ATOM 546 O ASN A 95 -60.702 -10.159 23.220 1.00 37.19 O ANISOU 546 O ASN A 95 6301 2921 4909 598 146 989 O ATOM 547 CB ASN A 95 -57.871 -10.126 24.142 1.00 36.08 C ANISOU 547 CB ASN A 95 6278 2529 4901 432 158 928 C ATOM 548 CG ASN A 95 -58.032 -9.107 25.248 1.00 35.88 C ANISOU 548 CG ASN A 95 6316 2355 4959 402 232 949 C ATOM 549 OD1 ASN A 95 -58.847 -9.287 26.149 1.00 35.05 O ANISOU 549 OD1 ASN A 95 6229 2225 4863 374 213 910 O ATOM 550 ND2 ASN A 95 -57.250 -8.040 25.196 1.00 36.25 N ANISOU 550 ND2 ASN A 95 6393 2303 5076 407 323 1004 N ATOM 551 N LYS A 96 -61.025 -10.941 25.321 1.00 35.98 N ANISOU 551 N LYS A 96 6220 2605 4844 438 93 861 N ATOM 552 CA LYS A 96 -62.401 -10.482 25.453 1.00 36.94 C ANISOU 552 CA LYS A 96 6316 2772 4946 496 124 902 C ATOM 553 C LYS A 96 -62.494 -9.068 26.031 1.00 36.40 C ANISOU 553 C LYS A 96 6308 2587 4934 529 226 984 C ATOM 554 O LYS A 96 -63.602 -8.566 26.201 1.00 36.21 O ANISOU 554 O LYS A 96 6269 2588 4898 585 263 1027 O ATOM 555 CB LYS A 96 -63.204 -11.422 26.357 1.00 37.29 C ANISOU 555 CB LYS A 96 6352 2813 5003 426 69 816 C ATOM 556 CG LYS A 96 -63.568 -12.785 25.784 1.00 38.54 C ANISOU 556 CG LYS A 96 6430 3088 5125 402 -14 728 C ATOM 557 CD LYS A 96 -64.564 -12.694 24.642 1.00 40.74 C ANISOU 557 CD LYS A 96 6606 3549 5324 501 -22 745 C ATOM 558 CE LYS A 96 -65.012 -14.046 24.129 1.00 42.01 C ANISOU 558 CE LYS A 96 6672 3825 5462 466 -103 626 C ATOM 559 NZ LYS A 96 -66.025 -13.915 23.054 1.00 43.09 N ANISOU 559 NZ LYS A 96 6693 4168 5510 567 -115 624 N ATOM 560 N ASN A 97 -61.364 -8.437 26.373 1.00 36.28 N ANISOU 560 N ASN A 97 6355 2441 4986 490 275 996 N ATOM 561 CA ASN A 97 -61.440 -7.086 26.918 1.00 36.85 C ANISOU 561 CA ASN A 97 6478 2389 5134 514 382 1055 C ATOM 562 C ASN A 97 -60.998 -6.075 25.865 1.00 38.25 C ANISOU 562 C ASN A 97 6647 2558 5329 603 478 1173 C ATOM 563 O ASN A 97 -60.211 -6.392 24.977 1.00 37.79 O ANISOU 563 O ASN A 97 6562 2556 5240 614 460 1191 O ATOM 564 CB ASN A 97 -60.606 -6.886 28.186 1.00 36.40 C ANISOU 564 CB ASN A 97 6488 2180 5160 409 391 974 C ATOM 565 CG ASN A 97 -61.043 -7.755 29.348 1.00 35.91 C ANISOU 565 CG ASN A 97 6441 2122 5080 338 318 880 C ATOM 566 OD1 ASN A 97 -60.948 -8.978 29.291 1.00 34.32 O ANISOU 566 OD1 ASN A 97 6216 1990 4833 298 230 827 O ATOM 567 ND2 ASN A 97 -61.475 -7.127 30.431 1.00 36.25 N ANISOU 567 ND2 ASN A 97 6521 2085 5166 324 361 859 N ATOM 568 N LYS A 98 -61.490 -4.841 26.016 1.00 40.16 N ANISOU 568 N LYS A 98 6911 2718 5627 668 591 1258 N ATOM 569 CA LYS A 98 -61.167 -3.759 25.101 1.00 42.04 C ANISOU 569 CA LYS A 98 7145 2924 5903 765 713 1395 C ATOM 570 C LYS A 98 -59.730 -3.294 25.328 1.00 41.72 C ANISOU 570 C LYS A 98 7148 2728 5975 683 769 1369 C ATOM 571 O LYS A 98 -59.116 -2.724 24.426 1.00 43.25 O ANISOU 571 O LYS A 98 7329 2907 6197 740 853 1471 O ATOM 572 CB LYS A 98 -62.155 -2.602 25.277 1.00 44.21 C ANISOU 572 CB LYS A 98 7434 3141 6222 861 826 1493 C ATOM 573 CG LYS A 98 -63.597 -2.883 24.869 1.00 45.75 C ANISOU 573 CG LYS A 98 7570 3509 6302 969 790 1541 C ATOM 574 CD LYS A 98 -64.267 -4.043 25.571 1.00 46.24 C ANISOU 574 CD LYS A 98 7613 3655 6301 890 658 1411 C ATOM 575 CE LYS A 98 -65.718 -4.202 25.164 1.00 48.09 C ANISOU 575 CE LYS A 98 7776 4057 6437 995 636 1453 C ATOM 576 NZ LYS A 98 -65.862 -4.386 23.699 1.00 49.66 N ANISOU 576 NZ LYS A 98 7891 4451 6524 1115 624 1534 N ATOM 577 N SER A 99 -59.227 -3.494 26.550 1.00 40.85 N ANISOU 577 N SER A 99 7081 2509 5929 556 730 1235 N ATOM 578 CA SER A 99 -57.868 -3.118 26.895 1.00 41.16 C ANISOU 578 CA SER A 99 7149 2417 6073 465 770 1177 C ATOM 579 C SER A 99 -56.931 -4.237 26.453 1.00 41.15 C ANISOU 579 C SER A 99 7121 2507 6004 414 666 1124 C ATOM 580 O SER A 99 -57.317 -5.407 26.465 1.00 40.10 O ANISOU 580 O SER A 99 6968 2496 5769 402 548 1073 O ATOM 581 CB SER A 99 -57.734 -2.852 28.369 1.00 41.20 C ANISOU 581 CB SER A 99 7196 2299 6156 367 769 1047 C ATOM 582 OG SER A 99 -58.630 -1.836 28.785 1.00 42.97 O ANISOU 582 OG SER A 99 7443 2439 6445 418 866 1087 O ATOM 583 N SER A 100 -55.697 -3.873 26.092 1.00 41.81 N ANISOU 583 N SER A 100 7203 2525 6156 379 718 1130 N ATOM 584 CA SER A 100 -54.734 -4.862 25.635 1.00 42.30 C ANISOU 584 CA SER A 100 7240 2672 6160 337 629 1084 C ATOM 585 C SER A 100 -54.216 -5.698 26.804 1.00 40.92 C ANISOU 585 C SER A 100 7085 2480 5979 220 523 926 C ATOM 586 O SER A 100 -54.036 -5.189 27.911 1.00 40.63 O ANISOU 586 O SER A 100 7079 2336 6021 154 551 846 O ATOM 587 CB SER A 100 -53.600 -4.214 24.872 1.00 44.68 C ANISOU 587 CB SER A 100 7525 2916 6532 341 722 1147 C ATOM 588 OG SER A 100 -52.895 -3.278 25.672 1.00 46.96 O ANISOU 588 OG SER A 100 7840 3029 6971 259 810 1089 O ATOM 589 N GLN A 101 -54.045 -7.005 26.542 1.00 39.36 N ANISOU 589 N GLN A 101 6866 2401 5685 207 406 882 N ATOM 590 CA GLN A 101 -53.509 -7.957 27.499 1.00 37.97 C ANISOU 590 CA GLN A 101 6705 2231 5490 120 307 757 C ATOM 591 C GLN A 101 -52.005 -8.070 27.264 1.00 38.71 C ANISOU 591 C GLN A 101 6784 2308 5612 69 301 717 C ATOM 592 O GLN A 101 -51.442 -7.329 26.461 1.00 39.94 O ANISOU 592 O GLN A 101 6923 2433 5817 92 383 783 O ATOM 593 CB GLN A 101 -54.105 -9.359 27.294 1.00 36.65 C ANISOU 593 CB GLN A 101 6518 2184 5222 135 197 735 C ATOM 594 CG GLN A 101 -55.609 -9.468 27.489 1.00 35.80 C ANISOU 594 CG GLN A 101 6408 2114 5078 179 189 762 C ATOM 595 CD GLN A 101 -56.065 -9.251 28.910 1.00 34.92 C ANISOU 595 CD GLN A 101 6339 1929 5000 134 194 708 C ATOM 596 OE1 GLN A 101 -55.265 -9.072 29.822 1.00 34.34 O ANISOU 596 OE1 GLN A 101 6292 1787 4968 71 195 638 O ATOM 597 NE2 GLN A 101 -57.368 -9.335 29.116 1.00 34.60 N ANISOU 597 NE2 GLN A 101 6292 1921 4931 169 192 732 N ATOM 598 N LYS A 102 -51.371 -9.004 27.981 1.00 38.52 N ANISOU 598 N LYS A 102 6766 2310 5560 6 211 616 N ATOM 599 CA LYS A 102 -49.950 -9.274 27.837 1.00 39.08 C ANISOU 599 CA LYS A 102 6818 2387 5644 -39 190 566 C ATOM 600 C LYS A 102 -49.709 -10.753 28.133 1.00 36.97 C ANISOU 600 C LYS A 102 6547 2202 5297 -56 71 503 C ATOM 601 O LYS A 102 -50.344 -11.322 29.014 1.00 35.50 O ANISOU 601 O LYS A 102 6384 2024 5080 -66 23 465 O ATOM 602 CB LYS A 102 -49.110 -8.374 28.750 1.00 41.32 C ANISOU 602 CB LYS A 102 7105 2571 6021 -112 243 486 C ATOM 603 CG LYS A 102 -49.222 -6.880 28.463 1.00 44.47 C ANISOU 603 CG LYS A 102 7504 2857 6533 -104 381 541 C ATOM 604 CD LYS A 102 -48.361 -5.992 29.342 1.00 47.26 C ANISOU 604 CD LYS A 102 7849 3107 6999 -188 439 433 C ATOM 605 CE LYS A 102 -48.699 -6.075 30.815 1.00 48.11 C ANISOU 605 CE LYS A 102 7977 3208 7093 -229 392 314 C ATOM 606 NZ LYS A 102 -47.844 -5.180 31.631 1.00 50.56 N ANISOU 606 NZ LYS A 102 8262 3436 7512 -310 448 184 N ATOM 607 N ILE A 103 -48.839 -11.387 27.340 1.00 36.77 N ANISOU 607 N ILE A 103 6492 2235 5241 -51 35 502 N ATOM 608 CA ILE A 103 -48.495 -12.782 27.556 1.00 35.16 C ANISOU 608 CA ILE A 103 6285 2095 4978 -61 -63 445 C ATOM 609 C ILE A 103 -47.023 -12.976 27.224 1.00 35.06 C ANISOU 609 C ILE A 103 6245 2105 4970 -85 -78 410 C ATOM 610 O ILE A 103 -46.461 -12.253 26.401 1.00 34.92 O ANISOU 610 O ILE A 103 6202 2081 4985 -77 -18 451 O ATOM 611 CB ILE A 103 -49.371 -13.756 26.736 1.00 35.09 C ANISOU 611 CB ILE A 103 6260 2164 4908 -10 -112 476 C ATOM 612 CG1 ILE A 103 -49.112 -13.649 25.230 1.00 35.76 C ANISOU 612 CG1 ILE A 103 6301 2319 4966 42 -93 530 C ATOM 613 CG2 ILE A 103 -50.843 -13.593 27.074 1.00 35.24 C ANISOU 613 CG2 ILE A 103 6295 2171 4922 11 -98 505 C ATOM 614 CD1 ILE A 103 -49.954 -14.584 24.399 1.00 35.65 C ANISOU 614 CD1 ILE A 103 6254 2401 4888 93 -144 531 C ATOM 615 N ASN A 104 -46.402 -13.959 27.883 1.00 34.99 N ANISOU 615 N ASN A 104 6239 2125 4929 -108 -151 341 N ATOM 616 CA ASN A 104 -45.014 -14.274 27.602 1.00 36.03 C ANISOU 616 CA ASN A 104 6339 2293 5056 -124 -174 303 C ATOM 617 C ASN A 104 -44.820 -15.780 27.752 1.00 35.45 C ANISOU 617 C ASN A 104 6268 2274 4925 -104 -261 271 C ATOM 618 O ASN A 104 -45.671 -16.484 28.301 1.00 33.88 O ANISOU 618 O ASN A 104 6097 2069 4706 -91 -294 270 O ATOM 619 CB ASN A 104 -44.024 -13.432 28.413 1.00 37.53 C ANISOU 619 CB ASN A 104 6515 2446 5297 -182 -142 238 C ATOM 620 CG ASN A 104 -44.088 -13.641 29.910 1.00 38.56 C ANISOU 620 CG ASN A 104 6666 2575 5410 -206 -179 165 C ATOM 621 OD1 ASN A 104 -43.766 -14.719 30.405 1.00 38.10 O ANISOU 621 OD1 ASN A 104 6609 2571 5293 -189 -250 136 O ATOM 622 ND2 ASN A 104 -44.400 -12.586 30.644 1.00 39.63 N ANISOU 622 ND2 ASN A 104 6809 2653 5596 -239 -126 134 N ATOM 623 N LEU A 105 -43.709 -16.254 27.188 1.00 36.16 N ANISOU 623 N LEU A 105 6326 2413 4999 -98 -288 249 N ATOM 624 CA LEU A 105 -43.353 -17.662 27.189 1.00 36.22 C ANISOU 624 CA LEU A 105 6331 2464 4965 -72 -358 220 C ATOM 625 C LEU A 105 -42.054 -17.886 27.951 1.00 37.28 C ANISOU 625 C LEU A 105 6451 2625 5089 -89 -387 163 C ATOM 626 O LEU A 105 -41.230 -16.982 28.081 1.00 37.84 O ANISOU 626 O LEU A 105 6494 2697 5184 -125 -355 136 O ATOM 627 CB LEU A 105 -43.198 -18.122 25.735 1.00 36.55 C ANISOU 627 CB LEU A 105 6339 2562 4985 -34 -368 239 C ATOM 628 CG LEU A 105 -44.466 -18.130 24.885 1.00 36.55 C ANISOU 628 CG LEU A 105 6336 2577 4975 0 -356 280 C ATOM 629 CD1 LEU A 105 -44.208 -18.772 23.531 1.00 36.55 C ANISOU 629 CD1 LEU A 105 6291 2660 4936 46 -380 273 C ATOM 630 CD2 LEU A 105 -45.581 -18.881 25.596 1.00 36.43 C ANISOU 630 CD2 LEU A 105 6351 2525 4964 -2 -385 266 C ATOM 631 N SER A 106 -41.897 -19.134 28.408 1.00 38.31 N ANISOU 631 N SER A 106 6592 2776 5186 -59 -442 146 N ATOM 632 CA SER A 106 -40.733 -19.600 29.137 1.00 40.12 C ANISOU 632 CA SER A 106 6804 3052 5385 -50 -478 102 C ATOM 633 C SER A 106 -40.610 -21.107 28.921 1.00 40.94 C ANISOU 633 C SER A 106 6916 3170 5468 3 -522 110 C ATOM 634 O SER A 106 -41.570 -21.832 29.166 1.00 41.94 O ANISOU 634 O SER A 106 7076 3252 5605 23 -525 138 O ATOM 635 CB SER A 106 -40.829 -19.229 30.587 1.00 41.31 C ANISOU 635 CB SER A 106 6970 3205 5521 -62 -477 76 C ATOM 636 OG SER A 106 -42.033 -19.718 31.158 1.00 42.40 O ANISOU 636 OG SER A 106 7154 3300 5654 -41 -476 117 O ATOM 637 N ILE A 107 -39.448 -21.551 28.413 1.00 42.59 N ANISOU 637 N ILE A 107 7089 3433 5659 24 -546 84 N ATOM 638 CA ILE A 107 -39.188 -22.960 28.127 1.00 43.44 C ANISOU 638 CA ILE A 107 7199 3547 5759 79 -580 84 C ATOM 639 C ILE A 107 -37.947 -23.395 28.902 1.00 43.71 C ANISOU 639 C ILE A 107 7212 3642 5751 115 -610 62 C ATOM 640 O ILE A 107 -37.031 -22.594 29.083 1.00 42.01 O ANISOU 640 O ILE A 107 6957 3487 5515 89 -610 26 O ATOM 641 CB ILE A 107 -38.969 -23.166 26.612 1.00 44.77 C ANISOU 641 CB ILE A 107 7335 3739 5935 89 -583 72 C ATOM 642 CG1 ILE A 107 -40.030 -22.464 25.757 1.00 46.07 C ANISOU 642 CG1 ILE A 107 7500 3884 6117 64 -552 94 C ATOM 643 CG2 ILE A 107 -38.837 -24.642 26.270 1.00 46.50 C ANISOU 643 CG2 ILE A 107 7555 3949 6162 142 -612 55 C ATOM 644 CD1 ILE A 107 -41.437 -22.922 26.012 1.00 46.18 C ANISOU 644 CD1 ILE A 107 7549 3837 6158 65 -549 110 C ATOM 645 N GLN A 108 -37.903 -24.665 29.333 1.00 44.27 N ANISOU 645 N GLN A 108 7303 3699 5817 178 -627 83 N ATOM 646 CA GLN A 108 -36.744 -25.155 30.065 1.00 47.09 C ANISOU 646 CA GLN A 108 7638 4130 6123 234 -653 75 C ATOM 647 C GLN A 108 -36.228 -26.438 29.414 1.00 47.62 C ANISOU 647 C GLN A 108 7700 4188 6205 297 -668 79 C ATOM 648 O GLN A 108 -37.009 -27.304 29.028 1.00 47.01 O ANISOU 648 O GLN A 108 7653 4025 6183 313 -653 99 O ATOM 649 CB GLN A 108 -37.064 -25.360 31.549 1.00 49.30 C ANISOU 649 CB GLN A 108 7945 4419 6367 273 -649 112 C ATOM 650 CG GLN A 108 -35.850 -25.768 32.377 1.00 52.37 C ANISOU 650 CG GLN A 108 8297 4917 6681 347 -677 106 C ATOM 651 CD GLN A 108 -36.125 -25.872 33.859 1.00 55.33 C ANISOU 651 CD GLN A 108 8688 5336 6997 401 -672 146 C ATOM 652 OE1 GLN A 108 -35.503 -25.189 34.670 1.00 58.55 O ANISOU 652 OE1 GLN A 108 9052 5861 7333 404 -693 97 O ATOM 653 NE2 GLN A 108 -37.050 -26.743 34.232 1.00 56.04 N ANISOU 653 NE2 GLN A 108 8833 5341 7118 446 -639 229 N ATOM 654 N SER A 109 -34.896 -26.521 29.297 1.00 50.85 N ANISOU 654 N SER A 109 8061 4687 6572 329 -693 48 N ATOM 655 CA SER A 109 -34.201 -27.661 28.719 1.00 55.39 C ANISOU 655 CA SER A 109 8622 5268 7154 397 -707 44 C ATOM 656 C SER A 109 -33.152 -28.173 29.705 1.00 57.77 C ANISOU 656 C SER A 109 8902 5654 7393 481 -726 60 C ATOM 657 O SER A 109 -32.577 -27.385 30.451 1.00 58.22 O ANISOU 657 O SER A 109 8922 5809 7388 468 -743 37 O ATOM 658 CB SER A 109 -33.571 -27.283 27.403 1.00 55.01 C ANISOU 658 CB SER A 109 8528 5266 7108 366 -717 -6 C ATOM 659 OG SER A 109 -32.872 -28.384 26.840 1.00 55.34 O ANISOU 659 OG SER A 109 8553 5319 7154 436 -731 -20 O ATOM 660 N LYS A 110 -32.923 -29.496 29.704 1.00 68.94 N ANISOU 660 N LYS A 110 9744 7086 9364 851 -320 962 N ATOM 661 CA LYS A 110 -31.948 -30.138 30.579 1.00 74.97 C ANISOU 661 CA LYS A 110 10443 7950 10091 962 -309 1085 C ATOM 662 C LYS A 110 -32.133 -29.743 32.044 1.00 77.73 C ANISOU 662 C LYS A 110 10756 8432 10346 946 -308 1194 C ATOM 663 O LYS A 110 -31.156 -29.659 32.785 1.00 77.11 O ANISOU 663 O LYS A 110 10603 8533 10160 1000 -316 1261 O ATOM 664 CB LYS A 110 -30.517 -29.836 30.118 1.00 79.02 C ANISOU 664 CB LYS A 110 10896 8616 10512 1003 -330 1036 C ATOM 665 CG LYS A 110 -30.082 -30.529 28.835 1.00 82.96 C ANISOU 665 CG LYS A 110 11411 9008 11100 1066 -323 960 C ATOM 666 CD LYS A 110 -30.044 -32.046 28.968 1.00 85.63 C ANISOU 666 CD LYS A 110 11761 9202 11571 1196 -283 1054 C ATOM 667 CE LYS A 110 -29.096 -32.524 30.050 1.00 88.74 C ANISOU 667 CE LYS A 110 12079 9733 11905 1314 -270 1205 C ATOM 668 NZ LYS A 110 -29.079 -34.002 30.156 1.00 92.16 N ANISOU 668 NZ LYS A 110 12530 10005 12481 1448 -222 1306 N ATOM 669 N ASN A 111 -33.387 -29.533 32.459 1.00 79.66 N ANISOU 669 N ASN A 111 11044 8599 10623 877 -298 1211 N ATOM 670 CA ASN A 111 -33.694 -29.179 33.837 1.00 79.75 C ANISOU 670 CA ASN A 111 11023 8732 10545 862 -293 1309 C ATOM 671 C ASN A 111 -32.754 -28.077 34.330 1.00 79.80 C ANISOU 671 C ASN A 111 10968 8978 10374 829 -324 1269 C ATOM 672 O ASN A 111 -32.444 -28.021 35.520 1.00 79.89 O ANISOU 672 O ASN A 111 10919 9148 10286 859 -324 1363 O ATOM 673 CB ASN A 111 -33.559 -30.395 34.760 1.00 79.83 C ANISOU 673 CB ASN A 111 10997 8730 10603 978 -260 1488 C ATOM 674 CG ASN A 111 -34.428 -31.563 34.345 1.00 79.73 C ANISOU 674 CG ASN A 111 11044 8470 10779 1008 -222 1535 C ATOM 675 OD1 ASN A 111 -35.650 -31.452 34.309 1.00 80.12 O ANISOU 675 OD1 ASN A 111 11142 8409 10889 931 -212 1518 O ATOM 676 ND2 ASN A 111 -33.808 -32.693 34.043 1.00 81.56 N ANISOU 676 ND2 ASN A 111 11269 8613 11105 1118 -198 1593 N HETATM 677 N MSE A 112 -32.311 -27.204 33.414 1.00 77.63 N ANISOU 677 N MSE A 112 10704 8735 10056 762 -350 1129 N HETATM 678 CA MSE A 112 -31.389 -26.139 33.778 1.00 76.04 C ANISOU 678 CA MSE A 112 10446 8746 9697 712 -378 1077 C HETATM 679 C MSE A 112 -31.668 -24.870 32.976 1.00 70.72 C ANISOU 679 C MSE A 112 9821 8051 8996 589 -394 927 C HETATM 680 O MSE A 112 -32.110 -23.864 33.527 1.00 76.47 O ANISOU 680 O MSE A 112 10563 8838 9651 503 -397 888 O HETATM 681 CB MSE A 112 -29.943 -26.553 33.482 1.00 77.97 C ANISOU 681 CB MSE A 112 10619 9104 9902 792 -391 1091 C HETATM 682 CG MSE A 112 -29.378 -27.636 34.363 1.00 81.43 C ANISOU 682 CG MSE A 112 10989 9617 10332 925 -376 1246 C HETATM 683 SE MSE A 112 -27.803 -28.406 33.478 1.00 83.45 SE ANISOU 683 SE MSE A 112 11180 9926 10599 1049 -380 1248 SE HETATM 684 CE MSE A 112 -26.831 -26.740 33.108 1.00 81.18 C ANISOU 684 CE MSE A 112 10840 9862 10140 913 -426 1093 C ATOM 685 N PHE A 113 -31.390 -24.947 31.668 1.00 64.60 N ANISOU 685 N PHE A 113 9070 7192 8282 588 -400 848 N ATOM 686 CA PHE A 113 -31.531 -23.821 30.758 1.00 58.08 C ANISOU 686 CA PHE A 113 8283 6346 7435 486 -411 720 C ATOM 687 C PHE A 113 -32.986 -23.379 30.630 1.00 54.60 C ANISOU 687 C PHE A 113 7921 5771 7052 418 -397 688 C ATOM 688 O PHE A 113 -33.836 -24.153 30.199 1.00 53.71 O ANISOU 688 O PHE A 113 7850 5505 7053 449 -383 708 O ATOM 689 CB PHE A 113 -30.998 -24.202 29.376 1.00 58.32 C ANISOU 689 CB PHE A 113 8316 6318 7525 519 -416 659 C ATOM 690 CG PHE A 113 -29.557 -24.642 29.347 1.00 59.75 C ANISOU 690 CG PHE A 113 8417 6631 7653 594 -427 685 C ATOM 691 CD1 PHE A 113 -28.543 -23.789 29.754 1.00 61.21 C ANISOU 691 CD1 PHE A 113 8537 7014 7706 547 -446 663 C ATOM 692 CD2 PHE A 113 -29.215 -25.914 28.913 1.00 62.21 C ANISOU 692 CD2 PHE A 113 8715 6871 8048 711 -416 728 C ATOM 693 CE1 PHE A 113 -27.218 -24.197 29.721 1.00 61.80 C ANISOU 693 CE1 PHE A 113 8526 7228 7725 618 -457 691 C ATOM 694 CE2 PHE A 113 -27.891 -26.319 28.879 1.00 63.73 C ANISOU 694 CE2 PHE A 113 8830 7194 8190 793 -423 756 C ATOM 695 CZ PHE A 113 -26.895 -25.460 29.285 1.00 64.01 C ANISOU 695 CZ PHE A 113 8792 7442 8085 747 -444 742 C ATOM 696 N GLU A 114 -33.240 -22.109 30.967 1.00 50.80 N ANISOU 696 N GLU A 114 7458 5351 6492 325 -399 632 N ATOM 697 CA GLU A 114 -34.570 -21.532 30.883 1.00 48.99 C ANISOU 697 CA GLU A 114 7297 5015 6299 265 -383 601 C ATOM 698 C GLU A 114 -34.536 -20.510 29.746 1.00 44.25 C ANISOU 698 C GLU A 114 6733 4383 5694 192 -385 492 C ATOM 699 O GLU A 114 -33.629 -19.680 29.695 1.00 42.33 O ANISOU 699 O GLU A 114 6466 4246 5371 143 -394 441 O ATOM 700 CB GLU A 114 -34.941 -20.879 32.217 1.00 51.78 C ANISOU 700 CB GLU A 114 7647 5458 6569 227 -374 626 C ATOM 701 CG GLU A 114 -36.396 -20.452 32.327 1.00 54.87 C ANISOU 701 CG GLU A 114 8101 5748 6999 189 -352 617 C ATOM 702 CD GLU A 114 -37.386 -21.606 32.312 1.00 57.94 C ANISOU 702 CD GLU A 114 8504 6012 7497 245 -339 698 C ATOM 703 OE1 GLU A 114 -37.269 -22.490 33.191 1.00 60.63 O ANISOU 703 OE1 GLU A 114 8806 6389 7839 306 -334 800 O ATOM 704 OE2 GLU A 114 -38.292 -21.601 31.455 1.00 58.29 O ANISOU 704 OE2 GLU A 114 8595 5929 7620 224 -331 663 O ATOM 705 N PHE A 115 -35.495 -20.598 28.818 1.00 41.48 N ANISOU 705 N PHE A 115 6434 3897 5430 184 -376 463 N ATOM 706 CA PHE A 115 -35.537 -19.679 27.689 1.00 40.85 C ANISOU 706 CA PHE A 115 6385 3788 5346 127 -375 377 C ATOM 707 C PHE A 115 -36.751 -18.761 27.813 1.00 39.86 C ANISOU 707 C PHE A 115 6317 3602 5223 71 -354 357 C ATOM 708 O PHE A 115 -37.857 -19.226 28.062 1.00 38.52 O ANISOU 708 O PHE A 115 6170 3354 5109 91 -343 396 O ATOM 709 CB PHE A 115 -35.535 -20.445 26.362 1.00 40.44 C ANISOU 709 CB PHE A 115 6333 3657 5373 169 -383 350 C ATOM 710 CG PHE A 115 -34.329 -21.326 26.153 1.00 40.34 C ANISOU 710 CG PHE A 115 6266 3699 5360 235 -399 364 C ATOM 711 CD1 PHE A 115 -34.101 -22.427 26.968 1.00 41.51 C ANISOU 711 CD1 PHE A 115 6385 3851 5535 309 -399 443 C ATOM 712 CD2 PHE A 115 -33.376 -21.006 25.200 1.00 40.01 C ANISOU 712 CD2 PHE A 115 6199 3718 5285 228 -409 307 C ATOM 713 CE1 PHE A 115 -32.983 -23.225 26.788 1.00 41.44 C ANISOU 713 CE1 PHE A 115 6325 3893 5526 384 -408 461 C ATOM 714 CE2 PHE A 115 -32.255 -21.802 25.025 1.00 40.85 C ANISOU 714 CE2 PHE A 115 6250 3886 5385 298 -420 320 C ATOM 715 CZ PHE A 115 -32.061 -22.908 25.821 1.00 41.46 C ANISOU 715 CZ PHE A 115 6300 3958 5493 380 -420 396 C ATOM 716 N ARG A 116 -36.514 -17.454 27.631 1.00 40.00 N ANISOU 716 N ARG A 116 6357 3657 5184 2 -343 299 N ATOM 717 CA ARG A 116 -37.544 -16.429 27.724 1.00 41.08 C ANISOU 717 CA ARG A 116 6551 3739 5317 -44 -316 276 C ATOM 718 C ARG A 116 -37.580 -15.643 26.415 1.00 38.74 C ANISOU 718 C ARG A 116 6283 3398 5036 -78 -305 223 C ATOM 719 O ARG A 116 -36.653 -15.737 25.615 1.00 37.16 O ANISOU 719 O ARG A 116 6054 3235 4829 -79 -320 198 O ATOM 720 CB ARG A 116 -37.202 -15.466 28.868 1.00 44.05 C ANISOU 720 CB ARG A 116 6932 4195 5607 -97 -303 255 C ATOM 721 CG ARG A 116 -37.092 -16.096 30.251 1.00 48.41 C ANISOU 721 CG ARG A 116 7446 4827 6119 -66 -311 309 C ATOM 722 CD ARG A 116 -38.384 -16.588 30.880 1.00 51.79 C ANISOU 722 CD ARG A 116 7894 5197 6585 -27 -297 369 C ATOM 723 NE ARG A 116 -39.303 -15.477 31.112 1.00 57.04 N ANISOU 723 NE ARG A 116 8614 5823 7233 -69 -265 331 N ATOM 724 CZ ARG A 116 -40.477 -15.566 31.734 1.00 58.87 C ANISOU 724 CZ ARG A 116 8865 6022 7478 -47 -245 370 C ATOM 725 NH1 ARG A 116 -40.865 -16.709 32.271 1.00 60.47 N ANISOU 725 NH1 ARG A 116 9035 6229 7712 4 -253 454 N ATOM 726 NH2 ARG A 116 -41.233 -14.490 31.874 1.00 57.63 N ANISOU 726 NH2 ARG A 116 8759 5834 7303 -77 -212 330 N ATOM 727 N LEU A 117 -38.647 -14.858 26.213 1.00 39.03 N ANISOU 727 N LEU A 117 6372 3366 5090 -99 -277 213 N ATOM 728 CA LEU A 117 -38.784 -14.024 25.026 1.00 38.10 C ANISOU 728 CA LEU A 117 6282 3211 4983 -124 -260 180 C ATOM 729 C LEU A 117 -37.609 -13.054 24.934 1.00 38.54 C ANISOU 729 C LEU A 117 6335 3324 4983 -188 -252 138 C ATOM 730 O LEU A 117 -37.339 -12.309 25.875 1.00 41.23 O ANISOU 730 O LEU A 117 6693 3695 5278 -236 -235 118 O ATOM 731 CB LEU A 117 -40.108 -13.253 25.098 1.00 37.67 C ANISOU 731 CB LEU A 117 6282 3085 4945 -129 -225 188 C ATOM 732 CG LEU A 117 -41.381 -14.082 24.946 1.00 37.10 C ANISOU 732 CG LEU A 117 6207 2959 4930 -78 -230 226 C ATOM 733 CD1 LEU A 117 -42.605 -13.187 24.847 1.00 36.63 C ANISOU 733 CD1 LEU A 117 6192 2847 4876 -77 -193 235 C ATOM 734 CD2 LEU A 117 -41.296 -14.968 23.716 1.00 36.61 C ANISOU 734 CD2 LEU A 117 6110 2886 4912 -48 -258 219 C ATOM 735 N LYS A 118 -36.930 -13.063 23.782 1.00 37.86 N ANISOU 735 N LYS A 118 6225 3260 4900 -191 -261 122 N ATOM 736 CA LYS A 118 -35.796 -12.185 23.543 1.00 38.45 C ANISOU 736 CA LYS A 118 6288 3392 4928 -257 -251 90 C ATOM 737 C LYS A 118 -36.322 -10.780 23.261 1.00 39.38 C ANISOU 737 C LYS A 118 6469 3441 5049 -309 -203 78 C ATOM 738 O LYS A 118 -37.117 -10.577 22.348 1.00 38.12 O ANISOU 738 O LYS A 118 6335 3222 4927 -281 -186 97 O ATOM 739 CB LYS A 118 -34.941 -12.727 22.396 1.00 38.19 C ANISOU 739 CB LYS A 118 6202 3414 4895 -233 -274 85 C ATOM 740 CG LYS A 118 -33.733 -11.878 22.025 1.00 38.47 C ANISOU 740 CG LYS A 118 6213 3521 4882 -304 -263 60 C ATOM 741 CD LYS A 118 -32.925 -12.475 20.903 1.00 38.19 C ANISOU 741 CD LYS A 118 6117 3553 4839 -270 -284 59 C ATOM 742 CE LYS A 118 -31.737 -11.633 20.500 1.00 38.41 C ANISOU 742 CE LYS A 118 6113 3661 4818 -345 -271 43 C ATOM 743 NZ LYS A 118 -30.969 -12.277 19.410 1.00 38.63 N ANISOU 743 NZ LYS A 118 6075 3769 4832 -300 -291 43 N ATOM 744 N GLU A 119 -35.851 -9.816 24.059 1.00 42.10 N ANISOU 744 N GLU A 119 6838 3801 5357 -384 -180 44 N ATOM 745 CA GLU A 119 -36.269 -8.430 23.956 1.00 44.04 C ANISOU 745 CA GLU A 119 7152 3966 5614 -437 -126 27 C ATOM 746 C GLU A 119 -35.901 -7.875 22.581 1.00 46.02 C ANISOU 746 C GLU A 119 7402 4201 5882 -456 -106 42 C ATOM 747 O GLU A 119 -34.747 -7.966 22.163 1.00 47.78 O ANISOU 747 O GLU A 119 7573 4502 6077 -493 -123 31 O ATOM 748 CB GLU A 119 -35.565 -7.615 25.045 1.00 45.44 C ANISOU 748 CB GLU A 119 7344 4175 5745 -527 -109 -30 C ATOM 749 CG GLU A 119 -36.064 -6.186 25.195 1.00 46.72 C ANISOU 749 CG GLU A 119 7589 4232 5927 -581 -46 -59 C ATOM 750 CD GLU A 119 -37.478 -6.055 25.740 1.00 45.67 C ANISOU 750 CD GLU A 119 7516 4015 5820 -523 -19 -45 C ATOM 751 OE1 GLU A 119 -38.108 -7.089 26.016 1.00 44.18 O ANISOU 751 OE1 GLU A 119 7300 3852 5634 -449 -52 -10 O ATOM 752 OE2 GLU A 119 -37.925 -4.915 25.942 1.00 47.47 O ANISOU 752 OE2 GLU A 119 7816 4153 6067 -554 37 -71 O ATOM 753 N GLY A 120 -36.897 -7.315 21.880 1.00 47.00 N ANISOU 753 N GLY A 120 7575 4237 6046 -425 -68 75 N ATOM 754 CA GLY A 120 -36.684 -6.706 20.574 1.00 46.22 C ANISOU 754 CA GLY A 120 7476 4125 5960 -435 -41 106 C ATOM 755 C GLY A 120 -37.030 -7.619 19.399 1.00 45.16 C ANISOU 755 C GLY A 120 7293 4030 5834 -356 -72 142 C ATOM 756 O GLY A 120 -37.236 -7.129 18.290 1.00 47.11 O ANISOU 756 O GLY A 120 7542 4266 6089 -341 -46 180 O ATOM 757 N SER A 121 -37.063 -8.938 19.637 1.00 43.48 N ANISOU 757 N SER A 121 7034 3866 5619 -305 -125 129 N ATOM 758 CA SER A 121 -37.378 -9.895 18.587 1.00 41.46 C ANISOU 758 CA SER A 121 6733 3645 5375 -236 -156 142 C ATOM 759 C SER A 121 -38.793 -9.666 18.060 1.00 39.48 C ANISOU 759 C SER A 121 6512 3335 5153 -188 -134 177 C ATOM 760 O SER A 121 -39.699 -9.321 18.815 1.00 37.76 O ANISOU 760 O SER A 121 6341 3050 4954 -182 -112 189 O ATOM 761 CB SER A 121 -37.190 -11.316 19.052 1.00 42.07 C ANISOU 761 CB SER A 121 6766 3757 5458 -195 -207 121 C ATOM 762 OG SER A 121 -35.832 -11.561 19.389 1.00 44.47 O ANISOU 762 OG SER A 121 7029 4138 5728 -225 -227 98 O ATOM 763 N GLU A 122 -38.967 -9.939 16.760 1.00 38.30 N ANISOU 763 N GLU A 122 6325 3228 4999 -148 -143 190 N ATOM 764 CA GLU A 122 -40.231 -9.744 16.073 1.00 37.83 C ANISOU 764 CA GLU A 122 6274 3146 4952 -99 -126 226 C ATOM 765 C GLU A 122 -41.161 -10.942 16.242 1.00 36.40 C ANISOU 765 C GLU A 122 6069 2961 4798 -51 -165 207 C ATOM 766 O GLU A 122 -40.736 -12.084 16.082 1.00 37.48 O ANISOU 766 O GLU A 122 6162 3136 4941 -36 -209 167 O ATOM 767 CB GLU A 122 -39.974 -9.584 14.574 1.00 39.19 C ANISOU 767 CB GLU A 122 6402 3394 5094 -78 -123 245 C ATOM 768 CG GLU A 122 -39.040 -8.439 14.225 1.00 40.52 C ANISOU 768 CG GLU A 122 6584 3572 5239 -128 -81 276 C ATOM 769 CD GLU A 122 -38.727 -8.319 12.743 1.00 41.91 C ANISOU 769 CD GLU A 122 6706 3840 5376 -104 -76 305 C ATOM 770 OE1 GLU A 122 -39.244 -9.147 11.960 1.00 42.46 O ANISOU 770 OE1 GLU A 122 6727 3975 5431 -46 -109 288 O ATOM 771 OE2 GLU A 122 -37.940 -7.415 12.376 1.00 42.16 O ANISOU 771 OE2 GLU A 122 6742 3886 5390 -147 -40 340 O ATOM 772 N VAL A 123 -42.436 -10.653 16.538 1.00 35.33 N ANISOU 772 N VAL A 123 5963 2778 4682 -26 -144 238 N ATOM 773 CA VAL A 123 -43.484 -11.661 16.645 1.00 34.95 C ANISOU 773 CA VAL A 123 5891 2726 4662 9 -174 229 C ATOM 774 C VAL A 123 -44.593 -11.222 15.686 1.00 34.08 C ANISOU 774 C VAL A 123 5765 2643 4539 49 -154 266 C ATOM 775 O VAL A 123 -44.675 -10.045 15.340 1.00 34.88 O ANISOU 775 O VAL A 123 5894 2737 4620 55 -109 313 O ATOM 776 CB VAL A 123 -43.970 -11.859 18.094 1.00 34.93 C ANISOU 776 CB VAL A 123 5922 2661 4686 0 -170 235 C ATOM 777 CG1 VAL A 123 -42.872 -12.442 18.969 1.00 34.88 C ANISOU 777 CG1 VAL A 123 5913 2655 4682 -29 -194 205 C ATOM 778 CG2 VAL A 123 -44.515 -10.577 18.707 1.00 34.92 C ANISOU 778 CG2 VAL A 123 5981 2609 4677 -4 -116 273 C ATOM 779 N PHE A 124 -45.436 -12.161 15.248 1.00 32.73 N ANISOU 779 N PHE A 124 5547 2505 4381 76 -187 248 N ATOM 780 CA PHE A 124 -46.485 -11.854 14.282 1.00 32.08 C ANISOU 780 CA PHE A 124 5433 2480 4276 116 -176 279 C ATOM 781 C PHE A 124 -47.855 -12.211 14.849 1.00 31.82 C ANISOU 781 C PHE A 124 5393 2427 4270 131 -178 295 C ATOM 782 O PHE A 124 -48.086 -13.343 15.282 1.00 31.37 O ANISOU 782 O PHE A 124 5315 2352 4250 114 -215 254 O ATOM 783 CB PHE A 124 -46.165 -12.572 12.970 1.00 31.87 C ANISOU 783 CB PHE A 124 5337 2549 4222 127 -214 231 C ATOM 784 CG PHE A 124 -44.856 -12.141 12.360 1.00 31.60 C ANISOU 784 CG PHE A 124 5300 2551 4152 117 -206 226 C ATOM 785 CD1 PHE A 124 -44.710 -10.883 11.792 1.00 31.75 C ANISOU 785 CD1 PHE A 124 5333 2596 4132 129 -160 293 C ATOM 786 CD2 PHE A 124 -43.718 -12.907 12.540 1.00 31.38 C ANISOU 786 CD2 PHE A 124 5263 2521 4137 93 -237 167 C ATOM 787 CE1 PHE A 124 -43.492 -10.484 11.266 1.00 31.78 C ANISOU 787 CE1 PHE A 124 5330 2637 4106 110 -150 296 C ATOM 788 CE2 PHE A 124 -42.496 -12.496 12.034 1.00 31.56 C ANISOU 788 CE2 PHE A 124 5277 2589 4123 81 -229 167 C ATOM 789 CZ PHE A 124 -42.383 -11.280 11.406 1.00 31.80 C ANISOU 789 CZ PHE A 124 5315 2653 4113 84 -186 231 C ATOM 790 N LEU A 125 -48.746 -11.212 14.843 1.00 31.68 N ANISOU 790 N LEU A 125 5393 2409 4233 166 -135 361 N ATOM 791 CA LEU A 125 -50.092 -11.362 15.363 1.00 31.91 C ANISOU 791 CA LEU A 125 5412 2434 4278 188 -128 388 C ATOM 792 C LEU A 125 -51.080 -11.222 14.207 1.00 32.89 C ANISOU 792 C LEU A 125 5471 2662 4362 233 -128 418 C ATOM 793 O LEU A 125 -51.087 -10.211 13.506 1.00 32.63 O ANISOU 793 O LEU A 125 5443 2664 4289 274 -91 474 O ATOM 794 CB LEU A 125 -50.361 -10.292 16.432 1.00 31.90 C ANISOU 794 CB LEU A 125 5482 2354 4282 203 -72 440 C ATOM 795 CG LEU A 125 -49.359 -10.219 17.588 1.00 31.41 C ANISOU 795 CG LEU A 125 5481 2210 4241 157 -66 411 C ATOM 796 CD1 LEU A 125 -48.144 -9.382 17.205 1.00 31.36 C ANISOU 796 CD1 LEU A 125 5511 2185 4217 136 -44 407 C ATOM 797 CD2 LEU A 125 -50.003 -9.685 18.858 1.00 31.46 C ANISOU 797 CD2 LEU A 125 5537 2157 4257 169 -27 438 C ATOM 798 N GLU A 126 -51.902 -12.258 14.019 1.00 33.66 N ANISOU 798 N GLU A 126 5505 2811 4470 223 -168 384 N ATOM 799 CA GLU A 126 -52.912 -12.275 12.979 1.00 34.85 C ANISOU 799 CA GLU A 126 5578 3084 4577 257 -177 400 C ATOM 800 C GLU A 126 -54.299 -12.175 13.604 1.00 35.78 C ANISOU 800 C GLU A 126 5679 3212 4702 279 -159 449 C ATOM 801 O GLU A 126 -54.774 -13.126 14.224 1.00 36.06 O ANISOU 801 O GLU A 126 5694 3225 4781 238 -187 414 O ATOM 802 CB GLU A 126 -52.811 -13.558 12.155 1.00 34.96 C ANISOU 802 CB GLU A 126 5520 3168 4594 219 -238 306 C ATOM 803 CG GLU A 126 -53.895 -13.662 11.099 1.00 35.63 C ANISOU 803 CG GLU A 126 5511 3401 4623 243 -254 308 C ATOM 804 CD GLU A 126 -53.843 -14.933 10.275 1.00 35.89 C ANISOU 804 CD GLU A 126 5471 3504 4658 198 -313 196 C ATOM 805 OE1 GLU A 126 -52.925 -15.735 10.509 1.00 36.33 O ANISOU 805 OE1 GLU A 126 5557 3482 4765 156 -338 122 O ATOM 806 OE2 GLU A 126 -54.723 -15.117 9.412 1.00 35.89 O ANISOU 806 OE2 GLU A 126 5386 3641 4609 206 -333 180 O ATOM 807 N GLY A 127 -54.930 -11.008 13.428 1.00 37.20 N ANISOU 807 N GLY A 127 5866 3427 4842 347 -108 537 N ATOM 808 CA GLY A 127 -56.268 -10.753 13.928 1.00 38.38 C ANISOU 808 CA GLY A 127 5993 3605 4984 386 -83 595 C ATOM 809 C GLY A 127 -57.324 -11.133 12.892 1.00 40.41 C ANISOU 809 C GLY A 127 6137 4024 5191 407 -110 600 C ATOM 810 O GLY A 127 -57.016 -11.764 11.882 1.00 40.20 O ANISOU 810 O GLY A 127 6053 4081 5141 379 -155 540 O ATOM 811 N LYS A 128 -58.563 -10.690 13.126 1.00 43.10 N ANISOU 811 N LYS A 128 6444 4423 5507 461 -80 671 N ATOM 812 CA LYS A 128 -59.670 -11.008 12.239 1.00 44.65 C ANISOU 812 CA LYS A 128 6522 4795 5648 480 -105 682 C ATOM 813 C LYS A 128 -59.444 -10.453 10.834 1.00 44.54 C ANISOU 813 C LYS A 128 6462 4903 5558 534 -102 712 C ATOM 814 O LYS A 128 -59.792 -11.110 9.858 1.00 43.70 O ANISOU 814 O LYS A 128 6255 4944 5404 512 -149 664 O ATOM 815 CB LYS A 128 -60.994 -10.484 12.805 1.00 46.89 C ANISOU 815 CB LYS A 128 6778 5125 5912 544 -64 770 C ATOM 816 CG LYS A 128 -61.417 -11.085 14.138 1.00 48.75 C ANISOU 816 CG LYS A 128 7034 5278 6207 494 -68 751 C ATOM 817 CD LYS A 128 -62.742 -10.561 14.655 1.00 51.20 C ANISOU 817 CD LYS A 128 7308 5654 6490 563 -26 837 C ATOM 818 CE LYS A 128 -63.908 -10.848 13.732 1.00 53.99 C ANISOU 818 CE LYS A 128 7523 6211 6779 580 -51 858 C ATOM 819 NZ LYS A 128 -65.183 -10.323 14.274 1.00 56.26 N ANISOU 819 NZ LYS A 128 7769 6571 7036 655 -7 949 N ATOM 820 N ASN A 129 -58.859 -9.255 10.729 1.00 45.11 N ANISOU 820 N ASN A 129 6606 4916 5617 601 -44 789 N ATOM 821 CA ASN A 129 -58.660 -8.662 9.415 1.00 46.41 C ANISOU 821 CA ASN A 129 6726 5200 5709 660 -32 839 C ATOM 822 C ASN A 129 -57.212 -8.246 9.169 1.00 45.70 C ANISOU 822 C ASN A 129 6711 5015 5635 642 -17 829 C ATOM 823 O ASN A 129 -56.816 -8.100 8.017 1.00 49.71 O ANISOU 823 O ASN A 129 7172 5629 6084 664 -24 842 O ATOM 824 CB ASN A 129 -59.535 -7.416 9.224 1.00 47.95 C ANISOU 824 CB ASN A 129 6910 5451 5856 782 37 982 C ATOM 825 CG ASN A 129 -61.023 -7.683 9.326 1.00 49.62 C ANISOU 825 CG ASN A 129 7027 5793 6032 816 28 1012 C ATOM 826 OD1 ASN A 129 -61.456 -8.813 9.545 1.00 49.71 O ANISOU 826 OD1 ASN A 129 6979 5851 6057 738 -30 925 O ATOM 827 ND2 ASN A 129 -61.821 -6.640 9.166 1.00 51.53 N ANISOU 827 ND2 ASN A 129 7253 6094 6231 935 91 1141 N ATOM 828 N ILE A 130 -56.418 -8.073 10.230 1.00 44.29 N ANISOU 828 N ILE A 130 6642 4655 5530 601 3 805 N ATOM 829 CA ILE A 130 -55.059 -7.596 10.033 1.00 43.09 C ANISOU 829 CA ILE A 130 6557 4422 5392 581 22 801 C ATOM 830 C ILE A 130 -54.021 -8.506 10.686 1.00 40.01 C ANISOU 830 C ILE A 130 6208 3934 5057 485 -23 690 C ATOM 831 O ILE A 130 -54.242 -9.048 11.767 1.00 38.62 O ANISOU 831 O ILE A 130 6061 3678 4932 445 -38 647 O ATOM 832 CB ILE A 130 -54.923 -6.165 10.601 1.00 43.95 C ANISOU 832 CB ILE A 130 6765 4404 5527 634 109 897 C ATOM 833 CG1 ILE A 130 -55.958 -5.193 10.025 1.00 46.43 C ANISOU 833 CG1 ILE A 130 7047 4799 5795 747 166 1025 C ATOM 834 CG2 ILE A 130 -53.509 -5.642 10.407 1.00 44.24 C ANISOU 834 CG2 ILE A 130 6867 4358 5582 598 130 894 C ATOM 835 CD1 ILE A 130 -55.852 -4.980 8.537 1.00 47.39 C ANISOU 835 CD1 ILE A 130 7089 5074 5839 793 163 1081 C ATOM 836 N ILE A 131 -52.881 -8.634 9.996 1.00 38.29 N ANISOU 836 N ILE A 131 5988 3734 4824 456 -41 653 N ATOM 837 CA ILE A 131 -51.716 -9.347 10.495 1.00 36.95 C ANISOU 837 CA ILE A 131 5857 3481 4700 380 -76 563 C ATOM 838 C ILE A 131 -50.593 -8.321 10.489 1.00 37.14 C ANISOU 838 C ILE A 131 5950 3434 4727 377 -29 606 C ATOM 839 O ILE A 131 -50.384 -7.650 9.482 1.00 36.72 O ANISOU 839 O ILE A 131 5873 3451 4626 415 -3 666 O ATOM 840 CB ILE A 131 -51.334 -10.613 9.697 1.00 36.13 C ANISOU 840 CB ILE A 131 5679 3470 4577 342 -145 462 C ATOM 841 CG1 ILE A 131 -50.121 -11.287 10.347 1.00 35.23 C ANISOU 841 CG1 ILE A 131 5612 3258 4516 279 -172 383 C ATOM 842 CG2 ILE A 131 -51.079 -10.298 8.231 1.00 37.02 C ANISOU 842 CG2 ILE A 131 5728 3726 4611 380 -145 483 C ATOM 843 CD1 ILE A 131 -49.657 -12.564 9.685 1.00 35.08 C ANISOU 843 CD1 ILE A 131 5533 3302 4493 248 -233 276 C ATOM 844 N TYR A 132 -49.880 -8.206 11.613 1.00 37.68 N ANISOU 844 N TYR A 132 6097 3369 4848 328 -17 578 N ATOM 845 CA TYR A 132 -48.812 -7.227 11.722 1.00 39.18 C ANISOU 845 CA TYR A 132 6353 3485 5048 308 27 609 C ATOM 846 C TYR A 132 -47.674 -7.749 12.589 1.00 39.67 C ANISOU 846 C TYR A 132 6453 3472 5145 232 0 531 C ATOM 847 O TYR A 132 -47.844 -8.686 13.361 1.00 38.05 O ANISOU 847 O TYR A 132 6244 3244 4969 207 -39 472 O ATOM 848 CB TYR A 132 -49.325 -5.929 12.354 1.00 39.61 C ANISOU 848 CB TYR A 132 6483 3439 5125 343 104 689 C ATOM 849 CG TYR A 132 -49.947 -6.118 13.714 1.00 38.92 C ANISOU 849 CG TYR A 132 6440 3269 5078 334 107 661 C ATOM 850 CD1 TYR A 132 -51.135 -6.816 13.861 1.00 39.19 C ANISOU 850 CD1 TYR A 132 6423 3360 5106 366 79 657 C ATOM 851 CD2 TYR A 132 -49.294 -5.709 14.865 1.00 38.42 C ANISOU 851 CD2 TYR A 132 6458 3087 5053 285 131 630 C ATOM 852 CE1 TYR A 132 -51.705 -7.025 15.106 1.00 38.93 C ANISOU 852 CE1 TYR A 132 6423 3264 5105 359 82 639 C ATOM 853 CE2 TYR A 132 -49.844 -5.916 16.120 1.00 38.00 C ANISOU 853 CE2 TYR A 132 6437 2976 5025 280 132 604 C ATOM 854 CZ TYR A 132 -51.051 -6.584 16.242 1.00 38.12 C ANISOU 854 CZ TYR A 132 6402 3047 5034 320 108 613 C ATOM 855 OH TYR A 132 -51.616 -6.810 17.472 1.00 36.58 O ANISOU 855 OH TYR A 132 6230 2807 4858 317 112 596 O ATOM 856 N SER A 133 -46.529 -7.075 12.466 1.00 43.51 N ANISOU 856 N SER A 133 6974 3926 5630 198 26 541 N ATOM 857 CA SER A 133 -45.332 -7.393 13.218 1.00 45.78 C ANISOU 857 CA SER A 133 7290 4163 5939 127 6 477 C ATOM 858 C SER A 133 -45.226 -6.453 14.416 1.00 48.18 C ANISOU 858 C SER A 133 7683 4344 6279 96 56 490 C ATOM 859 O SER A 133 -45.456 -5.250 14.293 1.00 50.69 O ANISOU 859 O SER A 133 8047 4607 6602 113 121 553 O ATOM 860 CB SER A 133 -44.112 -7.285 12.337 1.00 46.80 C ANISOU 860 CB SER A 133 7391 4353 6039 100 1 473 C ATOM 861 OG SER A 133 -42.927 -7.593 13.059 1.00 47.52 O ANISOU 861 OG SER A 133 7498 4411 6143 35 -18 414 O ATOM 862 N ASP A 134 -44.890 -7.025 15.574 1.00 49.33 N ANISOU 862 N ASP A 134 7848 4448 6445 54 29 429 N ATOM 863 CA ASP A 134 -44.716 -6.265 16.798 1.00 49.09 C ANISOU 863 CA ASP A 134 7893 4320 6437 17 68 418 C ATOM 864 C ASP A 134 -43.515 -6.867 17.516 1.00 47.42 C ANISOU 864 C ASP A 134 7675 4119 6223 -50 29 350 C ATOM 865 O ASP A 134 -43.348 -8.083 17.540 1.00 47.27 O ANISOU 865 O ASP A 134 7604 4153 6201 -45 -28 315 O ATOM 866 CB ASP A 134 -45.977 -6.289 17.667 1.00 51.64 C ANISOU 866 CB ASP A 134 8241 4600 6777 58 82 429 C ATOM 867 CG ASP A 134 -45.890 -5.426 18.916 1.00 54.21 C ANISOU 867 CG ASP A 134 8646 4832 7118 28 129 410 C ATOM 868 OD1 ASP A 134 -44.853 -4.755 19.101 1.00 58.32 O ANISOU 868 OD1 ASP A 134 9205 5313 7641 -33 152 385 O ATOM 869 OD2 ASP A 134 -46.856 -5.442 19.706 1.00 55.50 O ANISOU 869 OD2 ASP A 134 8829 4969 7289 63 143 416 O ATOM 870 N LYS A 135 -42.676 -6.005 18.084 1.00 46.61 N ANISOU 870 N LYS A 135 7621 3966 6122 -112 62 332 N ATOM 871 CA LYS A 135 -41.485 -6.456 18.777 1.00 43.88 C ANISOU 871 CA LYS A 135 7260 3649 5761 -177 28 272 C ATOM 872 C LYS A 135 -41.792 -6.752 20.240 1.00 40.03 C ANISOU 872 C LYS A 135 6798 3133 5277 -186 18 236 C ATOM 873 O LYS A 135 -42.663 -6.132 20.842 1.00 38.42 O ANISOU 873 O LYS A 135 6645 2864 5086 -167 58 247 O ATOM 874 CB LYS A 135 -40.400 -5.377 18.707 1.00 47.49 C ANISOU 874 CB LYS A 135 7747 4081 6213 -254 68 263 C ATOM 875 CG LYS A 135 -39.942 -5.005 17.305 1.00 49.84 C ANISOU 875 CG LYS A 135 8017 4416 6502 -253 83 309 C ATOM 876 CD LYS A 135 -38.876 -3.935 17.298 1.00 51.62 C ANISOU 876 CD LYS A 135 8271 4612 6730 -341 127 305 C ATOM 877 CE LYS A 135 -38.392 -3.588 15.908 1.00 53.36 C ANISOU 877 CE LYS A 135 8456 4881 6938 -340 145 363 C ATOM 878 NZ LYS A 135 -39.490 -3.088 15.047 1.00 55.33 N ANISOU 878 NZ LYS A 135 8722 5097 7201 -262 186 446 N ATOM 879 N ILE A 136 -41.068 -7.729 20.789 1.00 36.81 N ANISOU 879 N ILE A 136 6347 2783 4853 -207 -32 198 N ATOM 880 CA ILE A 136 -41.182 -8.080 22.193 1.00 35.33 C ANISOU 880 CA ILE A 136 6171 2594 4657 -217 -44 171 C ATOM 881 C ILE A 136 -40.701 -6.896 23.023 1.00 35.75 C ANISOU 881 C ILE A 136 6280 2609 4692 -285 -1 133 C ATOM 882 O ILE A 136 -39.575 -6.433 22.850 1.00 35.64 O ANISOU 882 O ILE A 136 6261 2618 4660 -351 3 105 O ATOM 883 CB ILE A 136 -40.393 -9.368 22.481 1.00 34.02 C ANISOU 883 CB ILE A 136 5943 2505 4477 -217 -104 153 C ATOM 884 CG1 ILE A 136 -41.071 -10.543 21.770 1.00 32.94 C ANISOU 884 CG1 ILE A 136 5763 2379 4371 -151 -139 179 C ATOM 885 CG2 ILE A 136 -40.272 -9.594 23.985 1.00 33.99 C ANISOU 885 CG2 ILE A 136 5944 2520 4449 -234 -112 133 C ATOM 886 CD1 ILE A 136 -40.341 -11.852 21.859 1.00 32.89 C ANISOU 886 CD1 ILE A 136 5700 2429 4367 -137 -190 166 C ATOM 887 N LYS A 137 -41.583 -6.428 23.915 1.00 36.33 N ANISOU 887 N LYS A 137 6403 2630 4769 -269 32 127 N ATOM 888 CA LYS A 137 -41.323 -5.285 24.773 1.00 37.49 C ANISOU 888 CA LYS A 137 6611 2729 4902 -328 79 76 C ATOM 889 C LYS A 137 -41.405 -5.705 26.235 1.00 37.41 C ANISOU 889 C LYS A 137 6594 2764 4854 -334 61 38 C ATOM 890 O LYS A 137 -42.358 -6.375 26.630 1.00 37.09 O ANISOU 890 O LYS A 137 6541 2735 4818 -270 48 72 O ATOM 891 CB LYS A 137 -42.369 -4.199 24.508 1.00 38.58 C ANISOU 891 CB LYS A 137 6821 2759 5076 -291 149 102 C ATOM 892 CG LYS A 137 -42.434 -3.704 23.069 1.00 39.63 C ANISOU 892 CG LYS A 137 6961 2854 5243 -271 176 159 C ATOM 893 CD LYS A 137 -43.465 -2.614 22.850 1.00 40.38 C ANISOU 893 CD LYS A 137 7125 2844 5372 -221 251 198 C ATOM 894 CE LYS A 137 -43.534 -2.160 21.410 1.00 40.81 C ANISOU 894 CE LYS A 137 7175 2876 5451 -192 278 271 C ATOM 895 NZ LYS A 137 -44.559 -1.110 21.219 1.00 41.14 N ANISOU 895 NZ LYS A 137 7283 2820 5528 -128 355 323 N ATOM 896 N GLU A 138 -40.389 -5.316 27.016 1.00 38.23 N ANISOU 896 N GLU A 138 6699 2908 4917 -414 60 -29 N ATOM 897 CA GLU A 138 -40.320 -5.619 28.439 1.00 39.12 C ANISOU 897 CA GLU A 138 6798 3089 4977 -427 43 -70 C ATOM 898 C GLU A 138 -40.611 -7.099 28.678 1.00 36.92 C ANISOU 898 C GLU A 138 6451 2886 4689 -359 -11 -12 C ATOM 899 O GLU A 138 -41.299 -7.448 29.638 1.00 36.42 O ANISOU 899 O GLU A 138 6386 2848 4605 -322 -12 -1 O ATOM 900 CB GLU A 138 -41.283 -4.713 29.210 1.00 41.74 C ANISOU 900 CB GLU A 138 7201 3348 5308 -413 102 -102 C ATOM 901 CG GLU A 138 -40.949 -3.237 29.070 1.00 45.31 C ANISOU 901 CG GLU A 138 7729 3706 5779 -483 165 -167 C ATOM 902 CD GLU A 138 -41.902 -2.290 29.780 1.00 48.58 C ANISOU 902 CD GLU A 138 8222 4033 6199 -460 231 -207 C ATOM 903 OE1 GLU A 138 -42.883 -2.776 30.385 1.00 51.76 O ANISOU 903 OE1 GLU A 138 8617 4463 6586 -385 227 -179 O ATOM 904 OE2 GLU A 138 -41.656 -1.068 29.735 1.00 51.00 O ANISOU 904 OE2 GLU A 138 8600 4244 6532 -517 291 -266 O ATOM 905 N GLY A 139 -40.092 -7.940 27.769 1.00 35.13 N ANISOU 905 N GLY A 139 6173 2692 4483 -343 -53 25 N ATOM 906 CA GLY A 139 -40.242 -9.387 27.823 1.00 33.82 C ANISOU 906 CA GLY A 139 5946 2578 4326 -283 -102 77 C ATOM 907 C GLY A 139 -41.661 -9.884 27.531 1.00 32.73 C ANISOU 907 C GLY A 139 5817 2381 4236 -211 -96 133 C ATOM 908 O GLY A 139 -41.933 -11.076 27.721 1.00 31.99 O ANISOU 908 O GLY A 139 5680 2315 4159 -167 -130 176 O HETATM 909 N OCS A 140 -42.549 -9.007 27.030 1.00 32.11 N ANISOU 909 N OCS A 140 5790 2224 4184 -197 -52 138 N HETATM 910 CA OCS A 140 -43.932 -9.418 26.805 1.00 31.87 C ANISOU 910 CA OCS A 140 5759 2158 4190 -132 -46 190 C HETATM 911 CB OCS A 140 -44.865 -8.754 27.818 1.00 32.41 C ANISOU 911 CB OCS A 140 5870 2203 4239 -114 -2 187 C HETATM 912 SG OCS A 140 -44.749 -9.359 29.474 1.00 33.38 S ANISOU 912 SG OCS A 140 5967 2405 4310 -118 -19 182 S HETATM 913 C OCS A 140 -44.447 -9.127 25.391 1.00 31.24 C ANISOU 913 C OCS A 140 5687 2032 4149 -104 -32 216 C HETATM 914 O OCS A 140 -43.849 -8.373 24.634 1.00 31.38 O ANISOU 914 O OCS A 140 5725 2029 4167 -133 -14 199 O HETATM 915 OD1 OCS A 140 -43.279 -9.316 29.933 1.00 33.06 O ANISOU 915 OD1 OCS A 140 5908 2429 4222 -180 -43 130 O HETATM 916 OD2 OCS A 140 -45.546 -8.455 30.261 1.00 33.50 O ANISOU 916 OD2 OCS A 140 6030 2397 4300 -104 31 161 O HETATM 917 OD3 OCS A 140 -45.133 -10.748 29.411 1.00 32.90 O ANISOU 917 OD3 OCS A 140 5848 2372 4279 -78 -60 245 O ATOM 918 N ILE A 141 -45.592 -9.754 25.073 1.00 30.68 N ANISOU 918 N ILE A 141 5592 1955 4107 -51 -41 261 N ATOM 919 CA ILE A 141 -46.313 -9.621 23.814 1.00 30.40 C ANISOU 919 CA ILE A 141 5547 1902 4098 -14 -32 291 C ATOM 920 C ILE A 141 -47.633 -8.902 24.095 1.00 30.59 C ANISOU 920 C ILE A 141 5604 1894 4124 30 15 324 C ATOM 921 O ILE A 141 -48.451 -9.407 24.856 1.00 30.05 O ANISOU 921 O ILE A 141 5520 1839 4057 54 11 345 O ATOM 922 CB ILE A 141 -46.564 -11.016 23.191 1.00 30.18 C ANISOU 922 CB ILE A 141 5454 1910 4100 5 -85 306 C ATOM 923 CG1 ILE A 141 -45.259 -11.702 22.782 1.00 29.95 C ANISOU 923 CG1 ILE A 141 5394 1912 4073 -23 -127 274 C ATOM 924 CG2 ILE A 141 -47.512 -10.939 22.005 1.00 30.35 C ANISOU 924 CG2 ILE A 141 5454 1938 4137 43 -79 334 C ATOM 925 CD1 ILE A 141 -45.450 -13.133 22.274 1.00 29.83 C ANISOU 925 CD1 ILE A 141 5322 1914 4095 -3 -173 275 C ATOM 926 N GLU A 142 -47.854 -7.731 23.477 1.00 30.95 N ANISOU 926 N GLU A 142 5692 1898 4170 47 64 337 N ATOM 927 CA GLU A 142 -49.106 -7.015 23.681 1.00 31.46 C ANISOU 927 CA GLU A 142 5785 1932 4236 106 116 374 C ATOM 928 C GLU A 142 -50.227 -7.682 22.883 1.00 32.00 C ANISOU 928 C GLU A 142 5793 2049 4316 159 95 427 C ATOM 929 O GLU A 142 -50.078 -7.932 21.689 1.00 32.78 O ANISOU 929 O GLU A 142 5855 2179 4421 164 73 440 O ATOM 930 CB GLU A 142 -48.984 -5.537 23.288 1.00 32.02 C ANISOU 930 CB GLU A 142 5924 1931 4310 116 183 379 C ATOM 931 CG GLU A 142 -50.299 -4.788 23.424 1.00 32.18 C ANISOU 931 CG GLU A 142 5973 1919 4334 194 243 425 C ATOM 932 CD GLU A 142 -50.262 -3.310 23.072 1.00 33.11 C ANISOU 932 CD GLU A 142 6166 1946 4468 217 321 441 C ATOM 933 OE1 GLU A 142 -49.176 -2.805 22.747 1.00 32.78 O ANISOU 933 OE1 GLU A 142 6157 1860 4436 158 331 413 O ATOM 934 OE2 GLU A 142 -51.337 -2.687 23.082 1.00 33.69 O ANISOU 934 OE2 GLU A 142 6261 1993 4545 296 374 487 O ATOM 935 N VAL A 143 -51.346 -7.979 23.558 1.00 32.90 N ANISOU 935 N VAL A 143 5889 2182 4428 197 103 454 N ATOM 936 CA VAL A 143 -52.503 -8.603 22.926 1.00 33.93 C ANISOU 936 CA VAL A 143 5954 2370 4567 238 85 501 C ATOM 937 C VAL A 143 -53.621 -7.562 22.931 1.00 35.61 C ANISOU 937 C VAL A 143 6189 2574 4764 312 148 550 C ATOM 938 O VAL A 143 -54.368 -7.466 23.901 1.00 37.65 O ANISOU 938 O VAL A 143 6455 2836 5013 340 173 564 O ATOM 939 CB VAL A 143 -52.917 -9.902 23.646 1.00 33.73 C ANISOU 939 CB VAL A 143 5877 2383 4557 217 42 503 C ATOM 940 CG1 VAL A 143 -54.123 -10.561 22.992 1.00 33.85 C ANISOU 940 CG1 VAL A 143 5818 2459 4583 242 23 542 C ATOM 941 CG2 VAL A 143 -51.764 -10.885 23.723 1.00 33.27 C ANISOU 941 CG2 VAL A 143 5802 2319 4516 157 -10 461 C ATOM 942 N PRO A 144 -53.831 -6.821 21.818 1.00 36.75 N ANISOU 942 N PRO A 144 6336 2721 4903 355 176 587 N ATOM 943 CA PRO A 144 -54.819 -5.739 21.782 1.00 37.34 C ANISOU 943 CA PRO A 144 6437 2781 4966 441 245 644 C ATOM 944 C PRO A 144 -56.263 -6.116 22.106 1.00 37.48 C ANISOU 944 C PRO A 144 6398 2872 4971 496 248 690 C ATOM 945 O PRO A 144 -56.639 -7.286 22.093 1.00 37.51 O ANISOU 945 O PRO A 144 6328 2946 4977 466 193 686 O ATOM 946 CB PRO A 144 -54.723 -5.200 20.344 1.00 37.80 C ANISOU 946 CB PRO A 144 6481 2858 5019 475 259 689 C ATOM 947 CG PRO A 144 -54.119 -6.324 19.541 1.00 37.45 C ANISOU 947 CG PRO A 144 6372 2882 4976 416 183 657 C ATOM 948 CD PRO A 144 -53.218 -7.070 20.505 1.00 36.51 C ANISOU 948 CD PRO A 144 6272 2724 4875 336 143 585 C ATOM 949 N GLY A 145 -57.066 -5.091 22.407 1.00 37.82 N ANISOU 949 N GLY A 145 6476 2892 5001 579 319 733 N ATOM 950 CA GLY A 145 -58.468 -5.288 22.728 1.00 37.71 C ANISOU 950 CA GLY A 145 6405 2955 4965 644 332 784 C ATOM 951 C GLY A 145 -59.215 -6.009 21.607 1.00 37.63 C ANISOU 951 C GLY A 145 6288 3066 4941 657 288 831 C ATOM 952 O GLY A 145 -59.010 -5.720 20.434 1.00 37.58 O ANISOU 952 O GLY A 145 6265 3083 4927 675 286 855 O ATOM 953 N GLU A 146 -60.053 -6.972 22.000 1.00 38.21 N ANISOU 953 N GLU A 146 6285 3224 5009 640 253 840 N ATOM 954 CA GLU A 146 -60.865 -7.776 21.097 1.00 38.77 C ANISOU 954 CA GLU A 146 6244 3420 5066 635 208 868 C ATOM 955 C GLU A 146 -60.018 -8.599 20.128 1.00 37.83 C ANISOU 955 C GLU A 146 6094 3313 4964 558 141 816 C ATOM 956 O GLU A 146 -60.562 -9.215 19.216 1.00 39.72 O ANISOU 956 O GLU A 146 6243 3658 5190 548 102 822 O ATOM 957 CB GLU A 146 -61.908 -6.919 20.385 1.00 40.37 C ANISOU 957 CB GLU A 146 6407 3704 5227 744 255 949 C ATOM 958 CG GLU A 146 -62.922 -6.333 21.347 1.00 42.08 C ANISOU 958 CG GLU A 146 6632 3931 5423 825 316 999 C ATOM 959 CD GLU A 146 -64.009 -5.496 20.703 1.00 43.55 C ANISOU 959 CD GLU A 146 6774 4207 5566 948 367 1091 C ATOM 960 OE1 GLU A 146 -64.894 -5.044 21.438 1.00 44.81 O ANISOU 960 OE1 GLU A 146 6932 4387 5706 1024 419 1133 O ATOM 961 OE2 GLU A 146 -63.954 -5.282 19.476 1.00 47.14 O ANISOU 961 OE2 GLU A 146 7193 4715 6001 974 359 1123 O ATOM 962 N PHE A 147 -58.697 -8.634 20.317 1.00 36.55 N ANISOU 962 N PHE A 147 6001 3057 4830 503 127 760 N ATOM 963 CA PHE A 147 -57.901 -9.468 19.434 1.00 35.42 C ANISOU 963 CA PHE A 147 5825 2931 4702 438 66 708 C ATOM 964 C PHE A 147 -58.484 -10.877 19.474 1.00 35.21 C ANISOU 964 C PHE A 147 5713 2966 4696 381 8 683 C ATOM 965 O PHE A 147 -58.803 -11.376 20.548 1.00 34.33 O ANISOU 965 O PHE A 147 5604 2832 4609 357 7 686 O ATOM 966 CB PHE A 147 -56.448 -9.579 19.897 1.00 34.58 C ANISOU 966 CB PHE A 147 5790 2726 4623 378 52 649 C ATOM 967 CG PHE A 147 -55.563 -10.421 19.006 1.00 33.99 C ANISOU 967 CG PHE A 147 5683 2669 4562 322 -5 593 C ATOM 968 CD1 PHE A 147 -55.231 -10.002 17.726 1.00 34.12 C ANISOU 968 CD1 PHE A 147 5683 2728 4552 343 -6 598 C ATOM 969 CD2 PHE A 147 -55.129 -11.672 19.417 1.00 33.56 C ANISOU 969 CD2 PHE A 147 5610 2595 4547 256 -56 542 C ATOM 970 CE1 PHE A 147 -54.415 -10.776 16.914 1.00 33.72 C ANISOU 970 CE1 PHE A 147 5601 2704 4507 297 -57 541 C ATOM 971 CE2 PHE A 147 -54.330 -12.454 18.596 1.00 33.27 C ANISOU 971 CE2 PHE A 147 5545 2570 4524 214 -104 486 C ATOM 972 CZ PHE A 147 -53.972 -12.004 17.345 1.00 33.38 C ANISOU 972 CZ PHE A 147 5544 2632 4505 234 -106 479 C ATOM 973 N GLU A 148 -58.624 -11.495 18.302 1.00 35.13 N ANISOU 973 N GLU A 148 5631 3038 4679 359 -35 659 N ATOM 974 CA GLU A 148 -59.149 -12.844 18.177 1.00 35.43 C ANISOU 974 CA GLU A 148 5588 3127 4745 294 -89 621 C ATOM 975 C GLU A 148 -58.402 -13.485 17.017 1.00 34.92 C ANISOU 975 C GLU A 148 5494 3086 4686 251 -139 549 C ATOM 976 O GLU A 148 -58.832 -13.407 15.870 1.00 35.10 O ANISOU 976 O GLU A 148 5451 3218 4666 271 -153 546 O ATOM 977 CB GLU A 148 -60.667 -12.825 17.975 1.00 36.56 C ANISOU 977 CB GLU A 148 5643 3390 4856 325 -80 672 C ATOM 978 CG GLU A 148 -61.286 -14.204 17.833 1.00 37.76 C ANISOU 978 CG GLU A 148 5707 3596 5044 243 -133 629 C ATOM 979 CD GLU A 148 -62.796 -14.207 17.669 1.00 39.09 C ANISOU 979 CD GLU A 148 5776 3900 5176 263 -126 678 C ATOM 980 OE1 GLU A 148 -63.372 -15.298 17.539 1.00 39.53 O ANISOU 980 OE1 GLU A 148 5753 4002 5262 185 -166 642 O ATOM 981 OE2 GLU A 148 -63.398 -13.114 17.688 1.00 41.48 O ANISOU 981 OE2 GLU A 148 6078 4259 5422 356 -78 754 O ATOM 982 N GLY A 149 -57.246 -14.069 17.325 1.00 34.17 N ANISOU 982 N GLY A 149 5447 2899 4636 201 -163 493 N ATOM 983 CA GLY A 149 -56.460 -14.670 16.268 1.00 34.70 C ANISOU 983 CA GLY A 149 5490 2985 4706 169 -206 419 C ATOM 984 C GLY A 149 -55.325 -15.540 16.785 1.00 34.23 C ANISOU 984 C GLY A 149 5473 2825 4706 116 -233 362 C ATOM 985 O GLY A 149 -55.402 -16.087 17.882 1.00 35.76 O ANISOU 985 O GLY A 149 5687 2950 4948 88 -232 373 O ATOM 986 N LYS A 150 -54.255 -15.610 15.992 1.00 34.45 N ANISOU 986 N LYS A 150 5511 2854 4724 112 -252 309 N ATOM 987 CA LYS A 150 -53.128 -16.466 16.297 1.00 34.69 C ANISOU 987 CA LYS A 150 5570 2805 4804 74 -278 253 C ATOM 988 C LYS A 150 -51.861 -15.629 16.426 1.00 33.38 C ANISOU 988 C LYS A 150 5467 2604 4610 94 -258 263 C ATOM 989 O LYS A 150 -51.755 -14.555 15.839 1.00 33.63 O ANISOU 989 O LYS A 150 5510 2679 4588 129 -232 293 O ATOM 990 CB LYS A 150 -53.035 -17.491 15.165 1.00 36.24 C ANISOU 990 CB LYS A 150 5707 3048 5015 45 -324 164 C ATOM 991 CG LYS A 150 -54.367 -18.159 14.842 1.00 38.69 C ANISOU 991 CG LYS A 150 5943 3415 5340 14 -343 146 C ATOM 992 CD LYS A 150 -54.307 -19.181 13.732 1.00 41.30 C ANISOU 992 CD LYS A 150 6214 3791 5685 -22 -387 39 C ATOM 993 CE LYS A 150 -55.659 -19.749 13.361 1.00 43.44 C ANISOU 993 CE LYS A 150 6404 4137 5963 -63 -406 13 C ATOM 994 NZ LYS A 150 -56.570 -18.691 12.858 1.00 45.65 N ANISOU 994 NZ LYS A 150 6637 4554 6154 -17 -389 75 N ATOM 995 N ILE A 151 -50.903 -16.145 17.203 1.00 32.05 N ANISOU 995 N ILE A 151 5336 2360 4479 71 -268 243 N ATOM 996 CA ILE A 151 -49.638 -15.464 17.413 1.00 30.70 C ANISOU 996 CA ILE A 151 5215 2163 4283 76 -252 245 C ATOM 997 C ILE A 151 -48.501 -16.409 17.034 1.00 30.22 C ANISOU 997 C ILE A 151 5141 2092 4246 59 -289 181 C ATOM 998 O ILE A 151 -48.482 -17.576 17.444 1.00 30.25 O ANISOU 998 O ILE A 151 5132 2053 4307 42 -313 155 O ATOM 999 CB ILE A 151 -49.511 -14.945 18.857 1.00 30.19 C ANISOU 999 CB ILE A 151 5207 2040 4222 73 -222 290 C ATOM 1000 CG1 ILE A 151 -50.671 -14.001 19.205 1.00 30.20 C ANISOU 1000 CG1 ILE A 151 5223 2051 4199 101 -180 348 C ATOM 1001 CG2 ILE A 151 -48.155 -14.272 19.062 1.00 29.87 C ANISOU 1001 CG2 ILE A 151 5212 1983 4154 64 -210 280 C ATOM 1002 CD1 ILE A 151 -50.610 -13.422 20.602 1.00 29.86 C ANISOU 1002 CD1 ILE A 151 5235 1959 4150 102 -147 380 C ATOM 1003 N TYR A 152 -47.576 -15.868 16.234 1.00 29.43 N ANISOU 1003 N TYR A 152 5043 2034 4104 69 -287 161 N ATOM 1004 CA TYR A 152 -46.400 -16.564 15.737 1.00 29.20 C ANISOU 1004 CA TYR A 152 4997 2015 4080 65 -315 102 C ATOM 1005 C TYR A 152 -45.156 -16.074 16.472 1.00 28.97 C ANISOU 1005 C TYR A 152 5009 1961 4036 55 -301 119 C ATOM 1006 O TYR A 152 -44.832 -14.887 16.415 1.00 27.24 O ANISOU 1006 O TYR A 152 4817 1759 3773 52 -271 151 O ATOM 1007 CB TYR A 152 -46.280 -16.358 14.222 1.00 29.17 C ANISOU 1007 CB TYR A 152 4950 2104 4029 82 -324 67 C ATOM 1008 CG TYR A 152 -44.982 -16.808 13.601 1.00 29.22 C ANISOU 1008 CG TYR A 152 4937 2142 4022 88 -345 10 C ATOM 1009 CD1 TYR A 152 -43.783 -16.192 13.929 1.00 28.28 C ANISOU 1009 CD1 TYR A 152 4846 2021 3877 82 -329 32 C ATOM 1010 CD2 TYR A 152 -44.932 -17.881 12.726 1.00 29.58 C ANISOU 1010 CD2 TYR A 152 4934 2222 4081 96 -379 -71 C ATOM 1011 CE1 TYR A 152 -42.581 -16.606 13.384 1.00 29.02 C ANISOU 1011 CE1 TYR A 152 4915 2157 3953 91 -346 -14 C ATOM 1012 CE2 TYR A 152 -43.741 -18.298 12.159 1.00 29.65 C ANISOU 1012 CE2 TYR A 152 4924 2266 4075 111 -394 -125 C ATOM 1013 CZ TYR A 152 -42.560 -17.671 12.501 1.00 29.26 C ANISOU 1013 CZ TYR A 152 4897 2222 3995 112 -378 -92 C ATOM 1014 OH TYR A 152 -41.374 -18.074 11.954 1.00 29.72 O ANISOU 1014 OH TYR A 152 4928 2329 4032 131 -391 -140 O ATOM 1015 N VAL A 153 -44.482 -17.004 17.159 1.00 27.41 N ANISOU 1015 N VAL A 153 4812 1724 3876 50 -322 99 N ATOM 1016 CA VAL A 153 -43.255 -16.733 17.892 1.00 29.00 C ANISOU 1016 CA VAL A 153 5037 1923 4058 41 -316 110 C ATOM 1017 C VAL A 153 -42.233 -17.794 17.486 1.00 29.54 C ANISOU 1017 C VAL A 153 5071 2006 4144 59 -346 61 C ATOM 1018 O VAL A 153 -42.355 -18.947 17.893 1.00 29.53 O ANISOU 1018 O VAL A 153 5061 1957 4202 73 -364 50 O ATOM 1019 CB VAL A 153 -43.461 -16.758 19.421 1.00 28.89 C ANISOU 1019 CB VAL A 153 5053 1860 4061 29 -304 155 C ATOM 1020 CG1 VAL A 153 -42.151 -16.532 20.157 1.00 28.92 C ANISOU 1020 CG1 VAL A 153 5067 1885 4033 17 -304 158 C ATOM 1021 CG2 VAL A 153 -44.510 -15.760 19.890 1.00 28.80 C ANISOU 1021 CG2 VAL A 153 5076 1832 4033 21 -271 197 C ATOM 1022 N ASN A 154 -41.205 -17.393 16.730 1.00 29.97 N ANISOU 1022 N ASN A 154 5108 2124 4152 62 -348 36 N ATOM 1023 CA ASN A 154 -40.189 -18.326 16.271 1.00 30.69 C ANISOU 1023 CA ASN A 154 5164 2244 4252 90 -372 -12 C ATOM 1024 C ASN A 154 -39.276 -18.688 17.443 1.00 31.22 C ANISOU 1024 C ASN A 154 5238 2294 4328 95 -375 13 C ATOM 1025 O ASN A 154 -39.076 -17.885 18.348 1.00 30.84 O ANISOU 1025 O ASN A 154 5216 2252 4250 64 -359 55 O ATOM 1026 CB ASN A 154 -39.434 -17.767 15.065 1.00 31.09 C ANISOU 1026 CB ASN A 154 5184 2385 4241 95 -370 -40 C ATOM 1027 CG ASN A 154 -38.459 -18.758 14.461 1.00 31.41 C ANISOU 1027 CG ASN A 154 5182 2466 4286 135 -393 -100 C ATOM 1028 OD1 ASN A 154 -37.506 -19.177 15.108 1.00 31.54 O ANISOU 1028 OD1 ASN A 154 5193 2482 4308 149 -399 -94 O ATOM 1029 ND2 ASN A 154 -38.668 -19.104 13.201 1.00 31.96 N ANISOU 1029 ND2 ASN A 154 5217 2583 4344 158 -405 -158 N ATOM 1030 N PHE A 155 -38.722 -19.907 17.426 1.00 31.58 N ANISOU 1030 N PHE A 155 5259 2325 4414 136 -395 -15 N ATOM 1031 CA PHE A 155 -37.854 -20.348 18.508 1.00 32.20 C ANISOU 1031 CA PHE A 155 5334 2403 4497 155 -398 20 C ATOM 1032 C PHE A 155 -36.568 -19.523 18.585 1.00 33.17 C ANISOU 1032 C PHE A 155 5437 2623 4541 138 -394 27 C ATOM 1033 O PHE A 155 -35.885 -19.555 19.608 1.00 33.34 O ANISOU 1033 O PHE A 155 5452 2672 4543 139 -394 64 O ATOM 1034 CB PHE A 155 -37.526 -21.840 18.430 1.00 32.31 C ANISOU 1034 CB PHE A 155 5327 2370 4578 216 -412 -3 C ATOM 1035 CG PHE A 155 -38.710 -22.763 18.556 1.00 32.19 C ANISOU 1035 CG PHE A 155 5330 2245 4653 221 -413 -6 C ATOM 1036 CD1 PHE A 155 -39.661 -22.559 19.544 1.00 31.95 C ANISOU 1036 CD1 PHE A 155 5328 2165 4646 189 -402 55 C ATOM 1037 CD2 PHE A 155 -38.737 -23.970 17.871 1.00 32.90 C ANISOU 1037 CD2 PHE A 155 5407 2278 4814 260 -422 -65 C ATOM 1038 CE1 PHE A 155 -40.722 -23.440 19.705 1.00 32.20 C ANISOU 1038 CE1 PHE A 155 5369 2101 4763 186 -401 60 C ATOM 1039 CE2 PHE A 155 -39.785 -24.859 18.048 1.00 33.00 C ANISOU 1039 CE2 PHE A 155 5435 2181 4920 251 -420 -69 C ATOM 1040 CZ PHE A 155 -40.768 -24.599 18.969 1.00 32.64 C ANISOU 1040 CZ PHE A 155 5413 2094 4893 212 -410 0 C ATOM 1041 N ASN A 156 -36.213 -18.809 17.513 1.00 34.31 N ANISOU 1041 N ASN A 156 5566 2833 4638 121 -389 -3 N ATOM 1042 CA ASN A 156 -35.021 -17.978 17.597 1.00 35.69 C ANISOU 1042 CA ASN A 156 5719 3099 4742 90 -382 6 C ATOM 1043 C ASN A 156 -35.378 -16.703 18.363 1.00 36.06 C ANISOU 1043 C ASN A 156 5809 3131 4759 21 -358 43 C ATOM 1044 O ASN A 156 -34.550 -15.806 18.494 1.00 36.18 O ANISOU 1044 O ASN A 156 5817 3209 4721 -27 -345 49 O ATOM 1045 CB ASN A 156 -34.407 -17.683 16.226 1.00 36.92 C ANISOU 1045 CB ASN A 156 5837 3336 4854 96 -381 -29 C ATOM 1046 CG ASN A 156 -35.333 -16.931 15.298 1.00 37.42 C ANISOU 1046 CG ASN A 156 5919 3387 4909 73 -365 -32 C ATOM 1047 OD1 ASN A 156 -36.453 -16.589 15.666 1.00 38.63 O ANISOU 1047 OD1 ASN A 156 6116 3470 5090 54 -354 -9 O ATOM 1048 ND2 ASN A 156 -34.869 -16.655 14.092 1.00 39.52 N ANISOU 1048 ND2 ASN A 156 6148 3735 5131 81 -362 -54 N ATOM 1049 N SER A 157 -36.622 -16.636 18.860 1.00 37.86 N ANISOU 1049 N SER A 157 6081 3277 5026 15 -348 64 N ATOM 1050 CA SER A 157 -37.090 -15.493 19.631 1.00 39.94 C ANISOU 1050 CA SER A 157 6391 3514 5268 -37 -320 93 C ATOM 1051 C SER A 157 -37.029 -15.797 21.130 1.00 39.83 C ANISOU 1051 C SER A 157 6386 3491 5256 -41 -325 119 C ATOM 1052 O SER A 157 -37.357 -14.941 21.941 1.00 42.06 O ANISOU 1052 O SER A 157 6705 3759 5516 -82 -302 133 O ATOM 1053 CB SER A 157 -38.477 -15.080 19.217 1.00 41.08 C ANISOU 1053 CB SER A 157 6572 3597 5440 -36 -302 104 C ATOM 1054 OG SER A 157 -38.515 -14.714 17.846 1.00 43.33 O ANISOU 1054 OG SER A 157 6841 3912 5710 -30 -296 89 O ATOM 1055 N LEU A 158 -36.678 -17.035 21.501 1.00 40.13 N ANISOU 1055 N LEU A 158 6391 3535 5320 7 -349 129 N ATOM 1056 CA LEU A 158 -36.542 -17.384 22.909 1.00 39.31 C ANISOU 1056 CA LEU A 158 6284 3443 5208 14 -353 168 C ATOM 1057 C LEU A 158 -35.062 -17.612 23.179 1.00 38.56 C ANISOU 1057 C LEU A 158 6137 3449 5064 23 -369 166 C ATOM 1058 O LEU A 158 -34.411 -18.379 22.471 1.00 37.81 O ANISOU 1058 O LEU A 158 6004 3377 4985 70 -385 152 O ATOM 1059 CB LEU A 158 -37.394 -18.598 23.291 1.00 40.56 C ANISOU 1059 CB LEU A 158 6445 3526 5438 66 -361 203 C ATOM 1060 CG LEU A 158 -38.905 -18.407 23.166 1.00 41.28 C ANISOU 1060 CG LEU A 158 6576 3535 5572 53 -346 210 C ATOM 1061 CD1 LEU A 158 -39.369 -18.604 21.733 1.00 40.01 C ANISOU 1061 CD1 LEU A 158 6412 3340 5448 64 -352 167 C ATOM 1062 CD2 LEU A 158 -39.653 -19.329 24.120 1.00 43.32 C ANISOU 1062 CD2 LEU A 158 6836 3740 5882 81 -345 265 C ATOM 1063 N ILE A 159 -34.550 -16.956 24.227 1.00 37.68 N ANISOU 1063 N ILE A 159 6020 3406 4889 -20 -364 176 N ATOM 1064 CA ILE A 159 -33.132 -17.042 24.513 1.00 37.51 C ANISOU 1064 CA ILE A 159 5938 3506 4806 -22 -379 174 C ATOM 1065 C ILE A 159 -32.858 -17.294 25.994 1.00 37.18 C ANISOU 1065 C ILE A 159 5871 3532 4721 -14 -386 216 C ATOM 1066 O ILE A 159 -33.641 -16.921 26.863 1.00 36.47 O ANISOU 1066 O ILE A 159 5818 3414 4626 -39 -373 230 O ATOM 1067 CB ILE A 159 -32.460 -15.737 24.038 1.00 37.52 C ANISOU 1067 CB ILE A 159 5939 3566 4751 -108 -367 128 C ATOM 1068 CG1 ILE A 159 -30.933 -15.808 24.106 1.00 37.97 C ANISOU 1068 CG1 ILE A 159 5921 3764 4741 -117 -384 120 C ATOM 1069 CG2 ILE A 159 -33.014 -14.540 24.807 1.00 37.61 C ANISOU 1069 CG2 ILE A 159 6004 3550 4735 -187 -340 112 C ATOM 1070 CD1 ILE A 159 -30.242 -14.581 23.556 1.00 38.57 C ANISOU 1070 CD1 ILE A 159 5991 3894 4770 -211 -369 78 C ATOM 1071 N ASN A 160 -31.733 -17.977 26.231 1.00 37.92 N ANISOU 1071 N ASN A 160 5896 3728 4781 30 -406 239 N ATOM 1072 CA ASN A 160 -31.205 -18.254 27.555 1.00 39.30 C ANISOU 1072 CA ASN A 160 6024 4011 4895 47 -416 285 C ATOM 1073 C ASN A 160 -30.244 -17.107 27.852 1.00 40.68 C ANISOU 1073 C ASN A 160 6166 4319 4969 -46 -419 235 C ATOM 1074 O ASN A 160 -29.168 -17.045 27.267 1.00 40.13 O ANISOU 1074 O ASN A 160 6044 4337 4866 -54 -430 214 O ATOM 1075 CB ASN A 160 -30.470 -19.594 27.622 1.00 39.28 C ANISOU 1075 CB ASN A 160 5959 4057 4909 154 -433 344 C ATOM 1076 CG ASN A 160 -29.846 -19.865 28.976 1.00 39.49 C ANISOU 1076 CG ASN A 160 5924 4222 4858 180 -443 405 C ATOM 1077 OD1 ASN A 160 -28.626 -19.846 29.110 1.00 39.79 O ANISOU 1077 OD1 ASN A 160 5887 4409 4822 187 -458 406 O ATOM 1078 ND2 ASN A 160 -30.664 -20.036 30.001 1.00 39.86 N ANISOU 1078 ND2 ASN A 160 5993 4241 4910 190 -434 456 N ATOM 1079 N GLU A 161 -30.659 -16.205 28.744 1.00 43.56 N ANISOU 1079 N GLU A 161 6561 4698 5289 -120 -406 211 N ATOM 1080 CA GLU A 161 -29.907 -15.008 29.095 1.00 46.72 C ANISOU 1080 CA GLU A 161 6943 5203 5604 -229 -402 147 C ATOM 1081 C GLU A 161 -28.424 -15.290 29.358 1.00 48.57 C ANISOU 1081 C GLU A 161 7075 5624 5755 -227 -429 154 C ATOM 1082 O GLU A 161 -27.566 -14.794 28.631 1.00 50.17 O ANISOU 1082 O GLU A 161 7247 5881 5934 -280 -431 113 O ATOM 1083 CB GLU A 161 -30.586 -14.352 30.300 1.00 49.17 C ANISOU 1083 CB GLU A 161 7291 5515 5874 -279 -387 128 C ATOM 1084 CG GLU A 161 -29.941 -13.056 30.759 1.00 51.27 C ANISOU 1084 CG GLU A 161 7550 5869 6059 -404 -378 43 C ATOM 1085 CD GLU A 161 -30.649 -12.406 31.936 1.00 52.88 C ANISOU 1085 CD GLU A 161 7796 6073 6223 -448 -359 8 C ATOM 1086 OE1 GLU A 161 -31.670 -12.965 32.394 1.00 53.69 O ANISOU 1086 OE1 GLU A 161 7928 6113 6358 -377 -353 62 O ATOM 1087 OE2 GLU A 161 -30.175 -11.354 32.401 1.00 54.73 O ANISOU 1087 OE2 GLU A 161 8028 6372 6392 -555 -348 -74 O ATOM 1088 N GLU A 162 -28.136 -16.089 30.391 1.00 51.04 N ANISOU 1088 N GLU A 162 7327 6042 6020 -161 -448 214 N ATOM 1089 CA GLU A 162 -26.774 -16.407 30.809 1.00 53.94 C ANISOU 1089 CA GLU A 162 7585 6613 6297 -145 -474 234 C ATOM 1090 C GLU A 162 -25.857 -16.810 29.651 1.00 52.72 C ANISOU 1090 C GLU A 162 7382 6487 6160 -107 -484 236 C ATOM 1091 O GLU A 162 -24.754 -16.277 29.527 1.00 52.04 O ANISOU 1091 O GLU A 162 7228 6545 5997 -171 -495 198 O ATOM 1092 CB GLU A 162 -26.777 -17.549 31.831 1.00 57.29 C ANISOU 1092 CB GLU A 162 7957 7111 6698 -32 -487 334 C ATOM 1093 CG GLU A 162 -27.521 -17.246 33.124 1.00 60.64 C ANISOU 1093 CG GLU A 162 8403 7557 7078 -58 -480 344 C ATOM 1094 CD GLU A 162 -26.967 -16.108 33.967 1.00 64.18 C ANISOU 1094 CD GLU A 162 8814 8167 7402 -179 -486 263 C ATOM 1095 OE1 GLU A 162 -27.551 -15.831 35.034 1.00 63.78 O ANISOU 1095 OE1 GLU A 162 8778 8148 7304 -199 -479 260 O ATOM 1096 OE2 GLU A 162 -25.948 -15.509 33.569 1.00 70.83 O ANISOU 1096 OE2 GLU A 162 9609 9108 8192 -255 -497 201 O ATOM 1097 N SER A 163 -26.301 -17.765 28.825 1.00 50.59 N ANISOU 1097 N SER A 163 7142 6090 5987 -5 -479 276 N ATOM 1098 CA SER A 163 -25.487 -18.273 27.729 1.00 49.45 C ANISOU 1098 CA SER A 163 6953 5975 5861 50 -486 276 C ATOM 1099 C SER A 163 -25.669 -17.482 26.434 1.00 47.07 C ANISOU 1099 C SER A 163 6699 5587 5596 -21 -472 207 C ATOM 1100 O SER A 163 -24.789 -17.512 25.576 1.00 46.86 O ANISOU 1100 O SER A 163 6621 5632 5549 -13 -477 190 O ATOM 1101 CB SER A 163 -25.785 -19.731 27.502 1.00 50.22 C ANISOU 1101 CB SER A 163 7054 5987 6041 198 -486 344 C ATOM 1102 OG SER A 163 -27.155 -19.913 27.186 1.00 50.23 O ANISOU 1102 OG SER A 163 7150 5790 6143 206 -470 340 O ATOM 1103 N ASN A 164 -26.815 -16.806 26.290 1.00 45.78 N ANISOU 1103 N ASN A 164 6630 5281 5484 -81 -452 175 N ATOM 1104 CA ASN A 164 -27.131 -16.038 25.094 1.00 44.14 C ANISOU 1104 CA ASN A 164 6471 4986 5312 -140 -433 125 C ATOM 1105 C ASN A 164 -27.450 -17.011 23.957 1.00 42.32 C ANISOU 1105 C ASN A 164 6251 4668 5159 -39 -435 138 C ATOM 1106 O ASN A 164 -27.500 -16.613 22.797 1.00 41.69 O ANISOU 1106 O ASN A 164 6187 4553 5098 -62 -424 105 O ATOM 1107 CB ASN A 164 -26.003 -15.072 24.716 1.00 45.26 C ANISOU 1107 CB ASN A 164 6562 5250 5383 -238 -430 83 C ATOM 1108 CG ASN A 164 -26.327 -14.208 23.515 1.00 45.97 C ANISOU 1108 CG ASN A 164 6702 5255 5510 -300 -404 48 C ATOM 1109 OD1 ASN A 164 -27.248 -13.394 23.558 1.00 45.90 O ANISOU 1109 OD1 ASN A 164 6773 5131 5534 -358 -379 29 O ATOM 1110 ND2 ASN A 164 -25.560 -14.354 22.446 1.00 46.61 N ANISOU 1110 ND2 ASN A 164 6731 5399 5578 -281 -407 45 N ATOM 1111 N VAL A 165 -27.700 -18.282 24.308 1.00 41.06 N ANISOU 1111 N VAL A 165 6083 4473 5045 69 -446 185 N ATOM 1112 CA VAL A 165 -28.003 -19.317 23.327 1.00 40.60 C ANISOU 1112 CA VAL A 165 6035 4325 5065 165 -446 185 C ATOM 1113 C VAL A 165 -29.502 -19.321 23.038 1.00 39.16 C ANISOU 1113 C VAL A 165 5939 3973 4965 156 -433 174 C ATOM 1114 O VAL A 165 -30.302 -19.483 23.954 1.00 38.75 O ANISOU 1114 O VAL A 165 5923 3860 4940 158 -429 210 O ATOM 1115 CB VAL A 165 -27.538 -20.701 23.826 1.00 41.69 C ANISOU 1115 CB VAL A 165 6126 4487 5224 287 -457 242 C ATOM 1116 CG1 VAL A 165 -27.991 -21.826 22.906 1.00 41.94 C ANISOU 1116 CG1 VAL A 165 6184 4397 5355 382 -452 229 C ATOM 1117 CG2 VAL A 165 -26.033 -20.747 24.030 1.00 43.09 C ANISOU 1117 CG2 VAL A 165 6207 4852 5313 310 -470 257 C ATOM 1118 N VAL A 166 -29.872 -19.152 21.760 1.00 38.88 N ANISOU 1118 N VAL A 166 5927 3880 4963 150 -427 128 N ATOM 1119 CA VAL A 166 -31.275 -19.157 21.373 1.00 38.77 C ANISOU 1119 CA VAL A 166 5982 3728 5019 143 -417 115 C ATOM 1120 C VAL A 166 -31.732 -20.614 21.319 1.00 39.01 C ANISOU 1120 C VAL A 166 6017 3670 5135 237 -424 129 C ATOM 1121 O VAL A 166 -30.948 -21.502 21.000 1.00 39.92 O ANISOU 1121 O VAL A 166 6088 3817 5260 312 -432 124 O ATOM 1122 CB VAL A 166 -31.536 -18.381 20.064 1.00 38.27 C ANISOU 1122 CB VAL A 166 5936 3654 4950 101 -406 68 C ATOM 1123 CG1 VAL A 166 -31.171 -16.911 20.225 1.00 37.99 C ANISOU 1123 CG1 VAL A 166 5907 3677 4848 2 -389 65 C ATOM 1124 CG2 VAL A 166 -30.815 -18.975 18.863 1.00 38.52 C ANISOU 1124 CG2 VAL A 166 5919 3737 4978 158 -415 31 C ATOM 1125 N LEU A 167 -33.020 -20.827 21.604 1.00 39.03 N ANISOU 1125 N LEU A 167 6072 3556 5201 231 -417 143 N ATOM 1126 CA LEU A 167 -33.630 -22.148 21.713 1.00 40.77 C ANISOU 1126 CA LEU A 167 6305 3671 5514 299 -418 161 C ATOM 1127 C LEU A 167 -33.384 -23.070 20.510 1.00 42.35 C ANISOU 1127 C LEU A 167 6489 3836 5765 362 -424 103 C ATOM 1128 O LEU A 167 -33.383 -24.284 20.690 1.00 42.37 O ANISOU 1128 O LEU A 167 6488 3769 5840 432 -422 119 O ATOM 1129 CB LEU A 167 -35.127 -21.946 21.983 1.00 39.83 C ANISOU 1129 CB LEU A 167 6240 3450 5443 257 -408 174 C ATOM 1130 CG LEU A 167 -35.957 -23.216 22.162 1.00 40.56 C ANISOU 1130 CG LEU A 167 6350 3421 5641 303 -405 197 C ATOM 1131 CD1 LEU A 167 -35.657 -23.892 23.494 1.00 41.10 C ANISOU 1131 CD1 LEU A 167 6404 3489 5722 347 -399 285 C ATOM 1132 CD2 LEU A 167 -37.441 -22.909 22.056 1.00 39.71 C ANISOU 1132 CD2 LEU A 167 6283 3232 5570 253 -397 191 C ATOM 1133 N ASP A 168 -33.142 -22.542 19.302 1.00 44.23 N ANISOU 1133 N ASP A 168 6714 4124 5967 342 -427 38 N ATOM 1134 CA ASP A 168 -32.952 -23.454 18.179 1.00 46.13 C ANISOU 1134 CA ASP A 168 6936 4340 6249 405 -432 -28 C ATOM 1135 C ASP A 168 -31.470 -23.658 17.869 1.00 47.44 C ANISOU 1135 C ASP A 168 7042 4619 6362 461 -436 -39 C ATOM 1136 O ASP A 168 -31.137 -24.192 16.813 1.00 47.62 O ANISOU 1136 O ASP A 168 7042 4655 6395 512 -438 -105 O ATOM 1137 CB ASP A 168 -33.654 -22.966 16.905 1.00 46.44 C ANISOU 1137 CB ASP A 168 6987 4376 6281 367 -434 -97 C ATOM 1138 CG ASP A 168 -33.087 -21.681 16.322 1.00 47.13 C ANISOU 1138 CG ASP A 168 7051 4583 6271 316 -430 -103 C ATOM 1139 OD1 ASP A 168 -32.136 -21.132 16.915 1.00 47.34 O ANISOU 1139 OD1 ASP A 168 7053 4694 6238 298 -428 -64 O ATOM 1140 OD2 ASP A 168 -33.572 -21.265 15.252 1.00 48.44 O ANISOU 1140 OD2 ASP A 168 7218 4766 6420 295 -429 -147 O ATOM 1141 N SER A 169 -30.582 -23.257 18.787 1.00 50.39 N ANISOU 1141 N SER A 169 7384 5086 6673 454 -437 20 N ATOM 1142 CA SER A 169 -29.156 -23.393 18.536 1.00 52.27 C ANISOU 1142 CA SER A 169 7554 5455 6851 504 -441 16 C ATOM 1143 C SER A 169 -28.505 -24.301 19.580 1.00 55.40 C ANISOU 1143 C SER A 169 7919 5865 7263 587 -440 83 C ATOM 1144 O SER A 169 -29.188 -25.074 20.247 1.00 54.72 O ANISOU 1144 O SER A 169 7870 5663 7256 622 -434 123 O ATOM 1145 CB SER A 169 -28.506 -22.035 18.489 1.00 52.46 C ANISOU 1145 CB SER A 169 7546 5613 6771 417 -443 20 C ATOM 1146 OG SER A 169 -27.124 -22.151 18.197 1.00 53.89 O ANISOU 1146 OG SER A 169 7650 5936 6888 460 -447 17 O ATOM 1147 N ASN A 170 -27.170 -24.217 19.671 1.00 51.08 N ANISOU 1147 N ASN A 170 6159 8057 5192 -502 -618 205 N ATOM 1148 CA ASN A 170 -26.384 -24.998 20.612 1.00 52.25 C ANISOU 1148 CA ASN A 170 6413 8043 5396 -555 -612 112 C ATOM 1149 C ASN A 170 -25.306 -24.097 21.215 1.00 54.18 C ANISOU 1149 C ASN A 170 6772 8112 5700 -482 -603 135 C ATOM 1150 O ASN A 170 -25.157 -22.948 20.803 1.00 49.02 O ANISOU 1150 O ASN A 170 6118 7464 5043 -402 -600 214 O ATOM 1151 CB ASN A 170 -25.792 -26.249 19.955 1.00 54.50 C ANISOU 1151 CB ASN A 170 6692 8353 5660 -680 -634 13 C ATOM 1152 CG ASN A 170 -24.904 -25.940 18.769 1.00 56.42 C ANISOU 1152 CG ASN A 170 6929 8625 5883 -693 -663 21 C ATOM 1153 OD1 ASN A 170 -24.758 -24.784 18.378 1.00 60.97 O ANISOU 1153 OD1 ASN A 170 7498 9211 6455 -609 -668 103 O ATOM 1154 ND2 ASN A 170 -24.331 -26.971 18.170 1.00 57.58 N ANISOU 1154 ND2 ASN A 170 7078 8785 6014 -797 -676 -61 N HETATM 1155 N MSE A 171 -24.548 -24.649 22.173 1.00 53.37 N ANISOU 1155 N MSE A 171 6769 7860 5649 -514 -597 64 N HETATM 1156 CA MSE A 171 -23.503 -23.924 22.883 1.00 52.10 C ANISOU 1156 CA MSE A 171 6720 7531 5541 -462 -590 73 C HETATM 1157 C MSE A 171 -22.416 -23.422 21.930 1.00 50.94 C ANISOU 1157 C MSE A 171 6590 7372 5390 -461 -614 85 C HETATM 1158 O MSE A 171 -21.735 -22.448 22.250 1.00 50.93 O ANISOU 1158 O MSE A 171 6660 7270 5421 -401 -605 121 O HETATM 1159 CB MSE A 171 -22.919 -24.808 23.990 1.00 52.75 C ANISOU 1159 CB MSE A 171 6889 7484 5669 -511 -584 -7 C HETATM 1160 CG MSE A 171 -23.910 -25.159 25.087 1.00 56.56 C ANISOU 1160 CG MSE A 171 7373 7954 6164 -501 -555 -14 C HETATM 1161 SE MSE A 171 -24.340 -23.618 26.230 1.00 55.60 SE ANISOU 1161 SE MSE A 171 7313 7737 6075 -372 -513 74 SE HETATM 1162 CE MSE A 171 -26.297 -23.755 26.203 1.00 60.27 C ANISOU 1162 CE MSE A 171 7784 8488 6626 -347 -487 123 C ATOM 1163 N LEU A 172 -22.244 -24.088 20.778 1.00 49.10 N ANISOU 1163 N LEU A 172 6295 7241 5119 -532 -642 52 N ATOM 1164 CA LEU A 172 -21.267 -23.659 19.786 1.00 53.12 C ANISOU 1164 CA LEU A 172 6812 7750 5619 -534 -665 63 C ATOM 1165 C LEU A 172 -21.628 -22.278 19.240 1.00 57.95 C ANISOU 1165 C LEU A 172 7389 8416 6210 -439 -656 168 C ATOM 1166 O LEU A 172 -20.792 -21.627 18.618 1.00 58.08 O ANISOU 1166 O LEU A 172 7431 8405 6229 -417 -666 192 O ATOM 1167 CB LEU A 172 -21.215 -24.671 18.633 1.00 52.58 C ANISOU 1167 CB LEU A 172 6676 7797 5505 -631 -690 10 C ATOM 1168 CG LEU A 172 -20.602 -26.038 18.932 1.00 52.04 C ANISOU 1168 CG LEU A 172 6649 7665 5457 -728 -691 -93 C ATOM 1169 CD1 LEU A 172 -20.474 -26.863 17.660 1.00 54.59 C ANISOU 1169 CD1 LEU A 172 6912 8097 5732 -821 -708 -140 C ATOM 1170 CD2 LEU A 172 -19.229 -25.879 19.561 1.00 52.01 C ANISOU 1170 CD2 LEU A 172 6754 7493 5513 -714 -693 -117 C ATOM 1171 N SER A 173 -22.872 -21.841 19.475 1.00 55.13 N ANISOU 1171 N SER A 173 6976 8136 5833 -380 -633 232 N ATOM 1172 CA SER A 173 -23.324 -20.557 18.966 1.00 54.79 C ANISOU 1172 CA SER A 173 6895 8151 5769 -281 -615 342 C ATOM 1173 C SER A 173 -22.583 -19.396 19.622 1.00 50.80 C ANISOU 1173 C SER A 173 6499 7487 5316 -201 -584 380 C ATOM 1174 O SER A 173 -22.510 -18.325 19.030 1.00 47.57 O ANISOU 1174 O SER A 173 6082 7095 4895 -129 -569 459 O ATOM 1175 CB SER A 173 -24.818 -20.395 19.118 1.00 56.28 C ANISOU 1175 CB SER A 173 6996 8459 5926 -234 -593 405 C ATOM 1176 OG SER A 173 -25.210 -20.438 20.482 1.00 54.97 O ANISOU 1176 OG SER A 173 6887 8194 5803 -207 -561 393 O ATOM 1177 N ASN A 174 -22.048 -19.605 20.834 1.00 47.23 N ANISOU 1177 N ASN A 174 6146 6882 4915 -215 -573 326 N ATOM 1178 CA ASN A 174 -21.344 -18.534 21.525 1.00 48.66 C ANISOU 1178 CA ASN A 174 6434 6913 5141 -153 -541 354 C ATOM 1179 C ASN A 174 -20.075 -19.049 22.203 1.00 44.37 C ANISOU 1179 C ASN A 174 5988 6231 4639 -217 -560 268 C ATOM 1180 O ASN A 174 -20.033 -19.192 23.424 1.00 44.87 O ANISOU 1180 O ASN A 174 6118 6193 4735 -218 -542 237 O ATOM 1181 CB ASN A 174 -22.221 -17.832 22.570 1.00 49.58 C ANISOU 1181 CB ASN A 174 6580 6981 5277 -72 -487 408 C ATOM 1182 CG ASN A 174 -23.458 -17.184 21.989 1.00 51.60 C ANISOU 1182 CG ASN A 174 6743 7367 5496 7 -458 509 C ATOM 1183 OD1 ASN A 174 -23.564 -15.960 21.974 1.00 47.63 O ANISOU 1183 OD1 ASN A 174 6268 6828 5000 99 -412 592 O ATOM 1184 ND2 ASN A 174 -24.369 -17.984 21.458 1.00 53.61 N ANISOU 1184 ND2 ASN A 174 6885 7777 5707 -27 -483 506 N ATOM 1185 N ILE A 175 -19.034 -19.282 21.399 1.00 44.98 N ANISOU 1185 N ILE A 175 6069 6307 4711 -266 -594 234 N ATOM 1186 CA ILE A 175 -17.748 -19.734 21.899 1.00 45.94 C ANISOU 1186 CA ILE A 175 6273 6312 4869 -322 -613 162 C ATOM 1187 C ILE A 175 -16.933 -18.495 22.259 1.00 45.47 C ANISOU 1187 C ILE A 175 6303 6135 4836 -272 -589 196 C ATOM 1188 O ILE A 175 -16.804 -17.580 21.449 1.00 47.28 O ANISOU 1188 O ILE A 175 6521 6391 5051 -228 -579 253 O ATOM 1189 CB ILE A 175 -17.028 -20.624 20.866 1.00 47.06 C ANISOU 1189 CB ILE A 175 6377 6510 4993 -400 -655 109 C ATOM 1190 CG1 ILE A 175 -17.882 -21.833 20.474 1.00 47.62 C ANISOU 1190 CG1 ILE A 175 6362 6698 5032 -459 -669 72 C ATOM 1191 CG2 ILE A 175 -15.660 -21.054 21.377 1.00 47.77 C ANISOU 1191 CG2 ILE A 175 6546 6481 5121 -449 -672 45 C ATOM 1192 CD1 ILE A 175 -18.254 -22.726 21.638 1.00 46.05 C ANISOU 1192 CD1 ILE A 175 6189 6450 4855 -490 -659 19 C ATOM 1193 N VAL A 176 -16.380 -18.482 23.475 1.00 47.55 N ANISOU 1193 N VAL A 176 6656 6273 5136 -282 -579 160 N ATOM 1194 CA VAL A 176 -15.604 -17.344 23.942 1.00 45.27 C ANISOU 1194 CA VAL A 176 6460 5869 4870 -249 -552 181 C ATOM 1195 C VAL A 176 -14.149 -17.741 24.184 1.00 46.61 C ANISOU 1195 C VAL A 176 6688 5959 5061 -314 -584 117 C ATOM 1196 O VAL A 176 -13.302 -16.862 24.335 1.00 48.95 O ANISOU 1196 O VAL A 176 7052 6174 5370 -304 -570 127 O ATOM 1197 CB VAL A 176 -16.216 -16.714 25.211 1.00 45.36 C ANISOU 1197 CB VAL A 176 6533 5801 4899 -199 -502 205 C ATOM 1198 CG1 VAL A 176 -17.574 -16.090 24.939 1.00 43.50 C ANISOU 1198 CG1 VAL A 176 6244 5637 4645 -119 -460 285 C ATOM 1199 CG2 VAL A 176 -16.300 -17.702 26.368 1.00 46.28 C ANISOU 1199 CG2 VAL A 176 6675 5874 5033 -244 -514 143 C ATOM 1200 N SER A 177 -13.851 -19.048 24.214 1.00 43.73 N ANISOU 1200 N SER A 177 6297 5617 4700 -381 -622 54 N ATOM 1201 CA SER A 177 -12.477 -19.454 24.463 1.00 40.40 C ANISOU 1201 CA SER A 177 5925 5125 4298 -436 -649 1 C ATOM 1202 C SER A 177 -12.217 -20.886 23.997 1.00 40.13 C ANISOU 1202 C SER A 177 5840 5144 4260 -501 -684 -54 C ATOM 1203 O SER A 177 -13.083 -21.751 24.111 1.00 37.90 O ANISOU 1203 O SER A 177 5514 4915 3970 -516 -682 -72 O ATOM 1204 CB SER A 177 -12.152 -19.294 25.933 1.00 40.51 C ANISOU 1204 CB SER A 177 6024 5032 4337 -438 -635 -19 C ATOM 1205 OG SER A 177 -10.813 -19.665 26.214 1.00 38.64 O ANISOU 1205 OG SER A 177 5828 4737 4115 -488 -662 -63 O ATOM 1206 N TRP A 178 -11.024 -21.094 23.422 1.00 41.31 N ANISOU 1206 N TRP A 178 5998 5279 4416 -539 -709 -78 N ATOM 1207 CA TRP A 178 -10.561 -22.403 22.985 1.00 37.75 C ANISOU 1207 CA TRP A 178 5514 4859 3966 -601 -733 -131 C ATOM 1208 C TRP A 178 -9.095 -22.518 23.394 1.00 35.07 C ANISOU 1208 C TRP A 178 5231 4438 3653 -630 -750 -159 C ATOM 1209 O TRP A 178 -8.363 -21.534 23.345 1.00 31.75 O ANISOU 1209 O TRP A 178 4850 3974 3237 -614 -752 -136 O ATOM 1210 CB TRP A 178 -10.727 -22.659 21.478 1.00 40.11 C ANISOU 1210 CB TRP A 178 5741 5262 4237 -621 -746 -127 C ATOM 1211 CG TRP A 178 -9.942 -21.738 20.596 1.00 42.73 C ANISOU 1211 CG TRP A 178 6078 5592 4563 -606 -755 -96 C ATOM 1212 CD1 TRP A 178 -10.171 -20.412 20.367 1.00 47.26 C ANISOU 1212 CD1 TRP A 178 6664 6164 5127 -548 -739 -36 C ATOM 1213 CD2 TRP A 178 -8.671 -22.030 19.988 1.00 46.06 C ANISOU 1213 CD2 TRP A 178 6510 5995 4994 -646 -775 -123 C ATOM 1214 NE1 TRP A 178 -9.192 -19.890 19.565 1.00 48.70 N ANISOU 1214 NE1 TRP A 178 6856 6336 5309 -554 -750 -25 N ATOM 1215 CE2 TRP A 178 -8.251 -20.857 19.325 1.00 48.21 C ANISOU 1215 CE2 TRP A 178 6792 6264 5258 -614 -774 -79 C ATOM 1216 CE3 TRP A 178 -7.873 -23.178 19.898 1.00 46.96 C ANISOU 1216 CE3 TRP A 178 6623 6096 5123 -703 -789 -176 C ATOM 1217 CZ2 TRP A 178 -7.066 -20.801 18.592 1.00 45.68 C ANISOU 1217 CZ2 TRP A 178 6480 5932 4945 -642 -791 -90 C ATOM 1218 CZ3 TRP A 178 -6.704 -23.122 19.170 1.00 46.16 C ANISOU 1218 CZ3 TRP A 178 6527 5982 5027 -727 -804 -184 C ATOM 1219 CH2 TRP A 178 -6.308 -21.949 18.527 1.00 46.11 C ANISOU 1219 CH2 TRP A 178 6529 5976 5012 -698 -807 -143 C ATOM 1220 N GLY A 179 -8.675 -23.716 23.813 1.00 33.83 N ANISOU 1220 N GLY A 179 5078 4262 3512 -673 -758 -207 N ATOM 1221 CA GLY A 179 -7.295 -23.906 24.218 1.00 34.23 C ANISOU 1221 CA GLY A 179 5173 4248 3585 -697 -773 -227 C ATOM 1222 C GLY A 179 -6.858 -25.369 24.191 1.00 33.79 C ANISOU 1222 C GLY A 179 5101 4196 3542 -742 -776 -273 C ATOM 1223 O GLY A 179 -7.669 -26.277 24.002 1.00 33.66 O ANISOU 1223 O GLY A 179 5048 4222 3517 -760 -761 -296 O ATOM 1224 N ILE A 180 -5.551 -25.564 24.390 1.00 34.42 N ANISOU 1224 N ILE A 180 5207 4229 3639 -761 -790 -283 N ATOM 1225 CA ILE A 180 -4.943 -26.884 24.413 1.00 39.34 C ANISOU 1225 CA ILE A 180 5823 4844 4280 -795 -785 -318 C ATOM 1226 C ILE A 180 -4.095 -27.001 25.676 1.00 38.74 C ANISOU 1226 C ILE A 180 5796 4701 4223 -791 -792 -317 C ATOM 1227 O ILE A 180 -3.330 -26.092 26.006 1.00 38.86 O ANISOU 1227 O ILE A 180 5842 4684 4239 -783 -811 -297 O ATOM 1228 CB ILE A 180 -4.102 -27.128 23.141 1.00 40.25 C ANISOU 1228 CB ILE A 180 5909 4990 4395 -822 -792 -325 C ATOM 1229 CG1 ILE A 180 -4.920 -26.917 21.865 1.00 44.45 C ANISOU 1229 CG1 ILE A 180 6390 5598 4899 -828 -789 -322 C ATOM 1230 CG2 ILE A 180 -3.442 -28.503 23.170 1.00 41.17 C ANISOU 1230 CG2 ILE A 180 6022 5089 4531 -852 -776 -357 C ATOM 1231 CD1 ILE A 180 -4.140 -27.124 20.583 1.00 46.42 C ANISOU 1231 CD1 ILE A 180 6613 5880 5145 -856 -794 -331 C ATOM 1232 N THR A 181 -4.284 -28.104 26.410 1.00 35.72 N ANISOU 1232 N THR A 181 5420 4298 3852 -799 -773 -339 N ATOM 1233 CA THR A 181 -3.491 -28.372 27.593 1.00 34.02 C ANISOU 1233 CA THR A 181 5243 4031 3652 -795 -779 -335 C ATOM 1234 C THR A 181 -2.459 -29.423 27.195 1.00 36.11 C ANISOU 1234 C THR A 181 5492 4293 3934 -815 -771 -347 C ATOM 1235 O THR A 181 -2.795 -30.421 26.566 1.00 31.13 O ANISOU 1235 O THR A 181 4835 3683 3308 -832 -743 -371 O ATOM 1236 CB THR A 181 -4.347 -28.774 28.798 1.00 34.32 C ANISOU 1236 CB THR A 181 5306 4043 3691 -781 -761 -342 C ATOM 1237 OG1 THR A 181 -5.035 -29.980 28.475 1.00 38.36 O ANISOU 1237 OG1 THR A 181 5791 4576 4208 -796 -728 -371 O ATOM 1238 CG2 THR A 181 -5.336 -27.702 29.201 1.00 34.96 C ANISOU 1238 CG2 THR A 181 5404 4121 3755 -757 -762 -327 C ATOM 1239 N PHE A 182 -1.199 -29.167 27.548 1.00 37.20 N ANISOU 1239 N PHE A 182 5645 4408 4078 -814 -793 -328 N ATOM 1240 CA PHE A 182 -0.098 -30.049 27.204 1.00 39.17 C ANISOU 1240 CA PHE A 182 5879 4656 4346 -825 -785 -328 C ATOM 1241 C PHE A 182 0.557 -30.571 28.478 1.00 40.97 C ANISOU 1241 C PHE A 182 6130 4852 4583 -812 -784 -312 C ATOM 1242 O PHE A 182 0.874 -29.795 29.380 1.00 40.35 O ANISOU 1242 O PHE A 182 6078 4761 4493 -806 -812 -294 O ATOM 1243 CB PHE A 182 0.887 -29.285 26.313 1.00 37.93 C ANISOU 1243 CB PHE A 182 5708 4517 4187 -836 -811 -314 C ATOM 1244 CG PHE A 182 2.167 -30.003 25.967 1.00 37.55 C ANISOU 1244 CG PHE A 182 5642 4467 4157 -843 -805 -306 C ATOM 1245 CD1 PHE A 182 2.153 -31.197 25.266 1.00 39.90 C ANISOU 1245 CD1 PHE A 182 5918 4770 4471 -852 -766 -325 C ATOM 1246 CD2 PHE A 182 3.396 -29.477 26.341 1.00 34.75 C ANISOU 1246 CD2 PHE A 182 5292 4108 3802 -844 -835 -279 C ATOM 1247 CE1 PHE A 182 3.337 -31.847 24.954 1.00 37.79 C ANISOU 1247 CE1 PHE A 182 5636 4498 4223 -853 -753 -313 C ATOM 1248 CE2 PHE A 182 4.579 -30.126 26.018 1.00 35.66 C ANISOU 1248 CE2 PHE A 182 5385 4227 3934 -845 -828 -265 C ATOM 1249 CZ PHE A 182 4.545 -31.317 25.333 1.00 34.07 C ANISOU 1249 CZ PHE A 182 5165 4026 3754 -846 -785 -280 C ATOM 1250 N ILE A 183 0.681 -31.901 28.560 1.00 38.27 N ANISOU 1250 N ILE A 183 5780 4499 4261 -809 -747 -320 N ATOM 1251 CA ILE A 183 1.344 -32.557 29.673 1.00 37.81 C ANISOU 1251 CA ILE A 183 5737 4417 4212 -790 -740 -298 C ATOM 1252 C ILE A 183 2.579 -33.231 29.082 1.00 35.28 C ANISOU 1252 C ILE A 183 5392 4101 3910 -789 -726 -282 C ATOM 1253 O ILE A 183 2.462 -34.279 28.449 1.00 33.31 O ANISOU 1253 O ILE A 183 5132 3845 3680 -792 -678 -298 O ATOM 1254 CB ILE A 183 0.420 -33.553 30.400 1.00 39.66 C ANISOU 1254 CB ILE A 183 5989 4626 4453 -778 -697 -314 C ATOM 1255 CG1 ILE A 183 -0.899 -32.893 30.807 1.00 43.15 C ANISOU 1255 CG1 ILE A 183 6449 5067 4877 -779 -706 -331 C ATOM 1256 CG2 ILE A 183 1.134 -34.182 31.588 1.00 37.41 C ANISOU 1256 CG2 ILE A 183 5719 4319 4174 -752 -689 -282 C ATOM 1257 CD1 ILE A 183 -1.842 -33.799 31.565 1.00 45.58 C ANISOU 1257 CD1 ILE A 183 6774 5350 5190 -770 -665 -348 C ATOM 1258 N PRO A 184 3.771 -32.602 29.197 1.00 34.18 N ANISOU 1258 N PRO A 184 5244 3978 3765 -788 -764 -250 N ATOM 1259 CA PRO A 184 5.007 -33.157 28.648 1.00 34.72 C ANISOU 1259 CA PRO A 184 5283 4055 3851 -783 -752 -228 C ATOM 1260 C PRO A 184 5.417 -34.491 29.262 1.00 32.28 C ANISOU 1260 C PRO A 184 4973 3727 3562 -753 -707 -205 C ATOM 1261 O PRO A 184 5.079 -34.789 30.405 1.00 32.42 O ANISOU 1261 O PRO A 184 5011 3730 3573 -734 -702 -194 O ATOM 1262 CB PRO A 184 6.082 -32.108 28.978 1.00 36.73 C ANISOU 1262 CB PRO A 184 5531 4336 4088 -791 -807 -197 C ATOM 1263 CG PRO A 184 5.308 -30.839 29.260 1.00 37.54 C ANISOU 1263 CG PRO A 184 5661 4436 4164 -809 -842 -215 C ATOM 1264 CD PRO A 184 3.990 -31.297 29.841 1.00 37.92 C ANISOU 1264 CD PRO A 184 5734 4460 4212 -796 -815 -236 C ATOM 1265 N SER A 185 6.148 -35.281 28.467 1.00 35.02 N ANISOU 1265 N SER A 185 5298 4073 3934 -747 -669 -196 N ATOM 1266 CA SER A 185 6.645 -36.580 28.883 1.00 34.74 C ANISOU 1266 CA SER A 185 5261 4016 3921 -712 -613 -167 C ATOM 1267 C SER A 185 7.651 -36.409 30.019 1.00 35.96 C ANISOU 1267 C SER A 185 5403 4193 4064 -682 -646 -108 C ATOM 1268 O SER A 185 7.964 -35.291 30.415 1.00 30.02 O ANISOU 1268 O SER A 185 4647 3473 3286 -698 -711 -98 O ATOM 1269 CB SER A 185 7.281 -37.292 27.718 1.00 35.73 C ANISOU 1269 CB SER A 185 5367 4134 4074 -713 -564 -168 C ATOM 1270 OG SER A 185 8.404 -36.564 27.231 1.00 34.02 O ANISOU 1270 OG SER A 185 5119 3953 3853 -718 -607 -141 O ATOM 1271 N ASP A 186 8.179 -37.537 30.511 1.00 37.56 N ANISOU 1271 N ASP A 186 5601 4383 4286 -640 -597 -68 N ATOM 1272 CA ASP A 186 9.172 -37.527 31.571 1.00 41.12 C ANISOU 1272 CA ASP A 186 6032 4868 4724 -607 -623 -4 C ATOM 1273 C ASP A 186 10.493 -36.938 31.072 1.00 39.00 C ANISOU 1273 C ASP A 186 5718 4649 4450 -614 -663 29 C ATOM 1274 O ASP A 186 11.381 -36.680 31.880 1.00 42.97 O ANISOU 1274 O ASP A 186 6195 5199 4932 -600 -700 81 O ATOM 1275 CB ASP A 186 9.338 -38.921 32.181 1.00 47.32 C ANISOU 1275 CB ASP A 186 6822 5626 5530 -552 -551 36 C ATOM 1276 CG ASP A 186 8.100 -39.410 32.919 1.00 54.17 C ANISOU 1276 CG ASP A 186 7734 6450 6397 -546 -519 7 C ATOM 1277 OD1 ASP A 186 7.114 -38.647 32.984 1.00 59.92 O ANISOU 1277 OD1 ASP A 186 8485 7173 7106 -583 -556 -40 O ATOM 1278 OD2 ASP A 186 8.130 -40.549 33.425 1.00 56.71 O ANISOU 1278 OD2 ASP A 186 8067 6742 6737 -501 -453 37 O ATOM 1279 N GLU A 187 10.635 -36.736 29.753 1.00 36.89 N ANISOU 1279 N GLU A 187 5440 4377 4199 -639 -655 1 N ATOM 1280 CA GLU A 187 11.855 -36.131 29.237 1.00 38.26 C ANISOU 1280 CA GLU A 187 5572 4595 4368 -649 -691 30 C ATOM 1281 C GLU A 187 11.922 -34.696 29.763 1.00 38.34 C ANISOU 1281 C GLU A 187 5584 4645 4337 -688 -774 23 C ATOM 1282 O GLU A 187 10.897 -34.041 29.940 1.00 34.55 O ANISOU 1282 O GLU A 187 5139 4146 3841 -715 -796 -19 O ATOM 1283 CB GLU A 187 11.941 -36.248 27.712 1.00 37.83 C ANISOU 1283 CB GLU A 187 5510 4523 4339 -668 -661 0 C ATOM 1284 CG GLU A 187 12.100 -37.686 27.238 1.00 38.34 C ANISOU 1284 CG GLU A 187 5575 4549 4442 -632 -570 11 C ATOM 1285 CD GLU A 187 12.168 -37.894 25.736 1.00 37.32 C ANISOU 1285 CD GLU A 187 5443 4401 4335 -655 -531 -21 C ATOM 1286 OE1 GLU A 187 13.053 -37.286 25.083 1.00 41.33 O ANISOU 1286 OE1 GLU A 187 5919 4941 4842 -668 -562 -7 O ATOM 1287 OE2 GLU A 187 11.356 -38.686 25.221 1.00 36.16 O ANISOU 1287 OE2 GLU A 187 5324 4208 4204 -663 -467 -63 O ATOM 1288 N GLU A 188 13.142 -34.238 30.041 1.00 40.19 N ANISOU 1288 N GLU A 188 5779 4935 4554 -692 -815 67 N ATOM 1289 CA GLU A 188 13.350 -32.913 30.600 1.00 43.84 C ANISOU 1289 CA GLU A 188 6245 5436 4974 -736 -886 62 C ATOM 1290 C GLU A 188 12.879 -31.839 29.622 1.00 40.55 C ANISOU 1290 C GLU A 188 5850 5002 4555 -782 -908 9 C ATOM 1291 O GLU A 188 12.160 -30.925 30.017 1.00 36.92 O ANISOU 1291 O GLU A 188 5427 4531 4070 -811 -938 -21 O ATOM 1292 CB GLU A 188 14.814 -32.762 31.016 1.00 48.00 C ANISOU 1292 CB GLU A 188 6719 6036 5481 -736 -918 121 C ATOM 1293 CG GLU A 188 15.236 -33.813 32.033 1.00 51.66 C ANISOU 1293 CG GLU A 188 7158 6525 5944 -683 -895 183 C ATOM 1294 CD GLU A 188 16.662 -33.726 32.546 1.00 52.48 C ANISOU 1294 CD GLU A 188 7200 6718 6022 -678 -929 252 C ATOM 1295 OE1 GLU A 188 17.373 -32.783 32.162 1.00 56.41 O ANISOU 1295 OE1 GLU A 188 7674 7258 6500 -725 -973 247 O ATOM 1296 OE2 GLU A 188 17.068 -34.631 33.304 1.00 55.87 O ANISOU 1296 OE2 GLU A 188 7602 7175 6450 -627 -906 313 O ATOM 1297 N HIS A 189 13.261 -31.960 28.346 1.00 41.54 N ANISOU 1297 N HIS A 189 5955 5122 4706 -785 -888 2 N ATOM 1298 CA HIS A 189 12.857 -30.981 27.350 1.00 40.75 C ANISOU 1298 CA HIS A 189 5871 5009 4602 -823 -906 -41 C ATOM 1299 C HIS A 189 11.982 -31.628 26.283 1.00 39.75 C ANISOU 1299 C HIS A 189 5757 4841 4504 -813 -856 -77 C ATOM 1300 O HIS A 189 12.409 -32.564 25.609 1.00 37.54 O ANISOU 1300 O HIS A 189 5456 4554 4253 -793 -812 -66 O ATOM 1301 CB HIS A 189 14.066 -30.312 26.687 1.00 40.25 C ANISOU 1301 CB HIS A 189 5773 4983 4535 -848 -933 -24 C ATOM 1302 CG HIS A 189 14.921 -29.517 27.612 1.00 45.18 C ANISOU 1302 CG HIS A 189 6384 5657 5123 -874 -984 3 C ATOM 1303 ND1 HIS A 189 15.096 -28.161 27.451 1.00 43.91 N ANISOU 1303 ND1 HIS A 189 6239 5509 4936 -925 -1023 -17 N ATOM 1304 CD2 HIS A 189 15.626 -29.854 28.697 1.00 46.26 C ANISOU 1304 CD2 HIS A 189 6495 5838 5242 -863 -999 47 C ATOM 1305 CE1 HIS A 189 15.890 -27.707 28.407 1.00 43.39 C ANISOU 1305 CE1 HIS A 189 6158 5492 4836 -951 -1061 8 C ATOM 1306 NE2 HIS A 189 16.228 -28.719 29.171 1.00 45.93 N ANISOU 1306 NE2 HIS A 189 6451 5840 5160 -913 -1051 49 N ATOM 1307 N ASN A 190 10.766 -31.094 26.117 1.00 37.35 N ANISOU 1307 N ASN A 190 5487 4513 4189 -830 -862 -120 N ATOM 1308 CA ASN A 190 9.851 -31.604 25.114 1.00 39.14 C ANISOU 1308 CA ASN A 190 5721 4715 4432 -831 -821 -157 C ATOM 1309 C ASN A 190 9.566 -30.523 24.082 1.00 40.41 C ANISOU 1309 C ASN A 190 5886 4886 4581 -861 -845 -183 C ATOM 1310 O ASN A 190 9.666 -29.333 24.376 1.00 44.78 O ANISOU 1310 O ASN A 190 6451 5449 5112 -878 -887 -179 O ATOM 1311 CB ASN A 190 8.539 -32.126 25.698 1.00 37.00 C ANISOU 1311 CB ASN A 190 5480 4416 4160 -820 -796 -182 C ATOM 1312 CG ASN A 190 8.734 -33.304 26.621 1.00 34.92 C ANISOU 1312 CG ASN A 190 5217 4137 3911 -786 -761 -157 C ATOM 1313 OD1 ASN A 190 8.470 -34.434 26.223 1.00 30.96 O ANISOU 1313 OD1 ASN A 190 4716 3612 3432 -774 -703 -168 O ATOM 1314 ND2 ASN A 190 9.312 -33.074 27.790 1.00 37.47 N ANISOU 1314 ND2 ASN A 190 5539 4476 4219 -773 -792 -121 N ATOM 1315 N ILE A 191 9.249 -30.965 22.860 1.00 41.32 N ANISOU 1315 N ILE A 191 5991 4998 4709 -869 -812 -207 N ATOM 1316 CA ILE A 191 8.920 -30.056 21.778 1.00 39.74 C ANISOU 1316 CA ILE A 191 5790 4812 4496 -892 -829 -227 C ATOM 1317 C ILE A 191 7.825 -30.661 20.908 1.00 39.86 C ANISOU 1317 C ILE A 191 5805 4827 4511 -901 -791 -265 C ATOM 1318 O ILE A 191 7.936 -31.790 20.437 1.00 36.78 O ANISOU 1318 O ILE A 191 5405 4428 4139 -902 -744 -276 O ATOM 1319 CB ILE A 191 10.149 -29.686 20.918 1.00 40.81 C ANISOU 1319 CB ILE A 191 5901 4966 4639 -905 -839 -211 C ATOM 1320 CG1 ILE A 191 11.281 -29.067 21.744 1.00 41.72 C ANISOU 1320 CG1 ILE A 191 6010 5094 4748 -906 -877 -176 C ATOM 1321 CG2 ILE A 191 9.725 -28.771 19.776 1.00 41.14 C ANISOU 1321 CG2 ILE A 191 5944 5022 4665 -926 -852 -230 C ATOM 1322 CD1 ILE A 191 12.501 -28.680 20.932 1.00 42.37 C ANISOU 1322 CD1 ILE A 191 6064 5197 4836 -921 -888 -159 C ATOM 1323 N VAL A 192 6.755 -29.889 20.721 1.00 39.61 N ANISOU 1323 N VAL A 192 5786 4807 4458 -909 -808 -282 N ATOM 1324 CA VAL A 192 5.673 -30.273 19.842 1.00 42.03 C ANISOU 1324 CA VAL A 192 6084 5130 4753 -924 -782 -315 C ATOM 1325 C VAL A 192 5.555 -29.144 18.821 1.00 41.10 C ANISOU 1325 C VAL A 192 5957 5044 4615 -937 -807 -314 C ATOM 1326 O VAL A 192 5.826 -27.982 19.142 1.00 33.96 O ANISOU 1326 O VAL A 192 5064 4136 3701 -929 -843 -292 O ATOM 1327 CB VAL A 192 4.348 -30.554 20.579 1.00 44.07 C ANISOU 1327 CB VAL A 192 6358 5384 5002 -917 -771 -333 C ATOM 1328 CG1 VAL A 192 4.448 -31.781 21.471 1.00 45.06 C ANISOU 1328 CG1 VAL A 192 6494 5476 5149 -905 -736 -335 C ATOM 1329 CG2 VAL A 192 3.861 -29.354 21.372 1.00 47.28 C ANISOU 1329 CG2 VAL A 192 6785 5787 5390 -902 -810 -317 C ATOM 1330 N ILE A 193 5.247 -29.523 17.578 1.00 38.23 N ANISOU 1330 N ILE A 193 5571 4709 4243 -959 -785 -336 N ATOM 1331 CA ILE A 193 5.090 -28.581 16.483 1.00 39.01 C ANISOU 1331 CA ILE A 193 5656 4845 4319 -969 -803 -332 C ATOM 1332 C ILE A 193 3.638 -28.627 16.023 1.00 39.17 C ANISOU 1332 C ILE A 193 5663 4908 4310 -978 -794 -353 C ATOM 1333 O ILE A 193 3.164 -29.675 15.585 1.00 37.58 O ANISOU 1333 O ILE A 193 5448 4724 4105 -1004 -759 -385 O ATOM 1334 CB ILE A 193 6.044 -28.917 15.315 1.00 37.82 C ANISOU 1334 CB ILE A 193 5487 4705 4178 -990 -787 -337 C ATOM 1335 CG1 ILE A 193 7.513 -29.005 15.743 1.00 36.33 C ANISOU 1335 CG1 ILE A 193 5301 4482 4017 -981 -792 -314 C ATOM 1336 CG2 ILE A 193 5.862 -27.930 14.171 1.00 41.72 C ANISOU 1336 CG2 ILE A 193 5966 5239 4644 -999 -806 -331 C ATOM 1337 CD1 ILE A 193 8.078 -27.723 16.318 1.00 33.99 C ANISOU 1337 CD1 ILE A 193 5018 4176 3717 -968 -837 -283 C ATOM 1338 N ILE A 194 2.932 -27.496 16.135 1.00 38.83 N ANISOU 1338 N ILE A 194 5624 4883 4245 -959 -820 -333 N ATOM 1339 CA ILE A 194 1.552 -27.432 15.680 1.00 42.66 C ANISOU 1339 CA ILE A 194 6088 5421 4699 -962 -814 -343 C ATOM 1340 C ILE A 194 1.509 -26.654 14.367 1.00 45.65 C ANISOU 1340 C ILE A 194 6441 5852 5050 -967 -825 -328 C ATOM 1341 O ILE A 194 1.591 -25.429 14.364 1.00 48.30 O ANISOU 1341 O ILE A 194 6789 6184 5379 -940 -846 -294 O ATOM 1342 CB ILE A 194 0.619 -26.860 16.764 1.00 42.82 C ANISOU 1342 CB ILE A 194 6126 5430 4713 -931 -825 -327 C ATOM 1343 CG1 ILE A 194 0.638 -27.756 18.007 1.00 45.52 C ANISOU 1343 CG1 ILE A 194 6491 5725 5079 -929 -811 -343 C ATOM 1344 CG2 ILE A 194 -0.793 -26.690 16.217 1.00 45.99 C ANISOU 1344 CG2 ILE A 194 6496 5898 5079 -929 -820 -327 C ATOM 1345 CD1 ILE A 194 -0.266 -27.303 19.130 1.00 45.96 C ANISOU 1345 CD1 ILE A 194 6568 5764 5130 -901 -818 -332 C ATOM 1346 N LYS A 195 1.366 -27.392 13.256 1.00 48.27 N ANISOU 1346 N LYS A 195 6742 6232 5365 -1004 -805 -355 N ATOM 1347 CA LYS A 195 1.335 -26.805 11.926 1.00 50.60 C ANISOU 1347 CA LYS A 195 7010 6585 5629 -1014 -813 -343 C ATOM 1348 C LYS A 195 -0.020 -26.175 11.622 1.00 49.14 C ANISOU 1348 C LYS A 195 6796 6471 5402 -998 -823 -324 C ATOM 1349 O LYS A 195 -0.074 -25.100 11.028 1.00 49.76 O ANISOU 1349 O LYS A 195 6866 6578 5461 -974 -839 -287 O ATOM 1350 CB LYS A 195 1.628 -27.852 10.846 1.00 54.78 C ANISOU 1350 CB LYS A 195 7518 7146 6150 -1066 -784 -381 C ATOM 1351 CG LYS A 195 2.998 -28.514 10.924 1.00 61.59 C ANISOU 1351 CG LYS A 195 8401 7945 7052 -1079 -766 -395 C ATOM 1352 CD LYS A 195 3.245 -29.541 9.832 1.00 69.55 C ANISOU 1352 CD LYS A 195 9395 8979 8052 -1130 -727 -433 C ATOM 1353 CE LYS A 195 3.176 -28.965 8.432 1.00 74.76 C ANISOU 1353 CE LYS A 195 10027 9705 8673 -1150 -737 -427 C ATOM 1354 NZ LYS A 195 3.430 -29.999 7.401 1.00 80.75 N ANISOU 1354 NZ LYS A 195 10776 10484 9419 -1207 -694 -470 N ATOM 1355 N LYS A 196 -1.112 -26.833 12.025 1.00 46.44 N ANISOU 1355 N LYS A 196 6439 6158 5046 -1010 -810 -345 N ATOM 1356 CA LYS A 196 -2.409 -26.274 11.689 1.00 46.85 C ANISOU 1356 CA LYS A 196 6454 6291 5055 -994 -818 -321 C ATOM 1357 C LYS A 196 -3.527 -26.843 12.558 1.00 44.80 C ANISOU 1357 C LYS A 196 6187 6041 4791 -995 -807 -338 C ATOM 1358 O LYS A 196 -3.510 -28.012 12.948 1.00 39.17 O ANISOU 1358 O LYS A 196 5483 5305 4093 -1032 -783 -383 O ATOM 1359 CB LYS A 196 -2.693 -26.554 10.208 1.00 49.96 C ANISOU 1359 CB LYS A 196 6798 6779 5402 -1037 -813 -334 C ATOM 1360 CG LYS A 196 -4.022 -26.035 9.672 1.00 55.86 C ANISOU 1360 CG LYS A 196 7493 7635 6096 -1024 -823 -305 C ATOM 1361 CD LYS A 196 -4.227 -26.287 8.186 1.00 59.91 C ANISOU 1361 CD LYS A 196 7955 8252 6556 -1072 -821 -316 C ATOM 1362 CE LYS A 196 -4.208 -27.754 7.808 1.00 65.35 C ANISOU 1362 CE LYS A 196 8635 8960 7235 -1154 -791 -387 C ATOM 1363 NZ LYS A 196 -4.430 -27.949 6.355 1.00 68.82 N ANISOU 1363 NZ LYS A 196 9025 9506 7615 -1207 -788 -400 N ATOM 1364 N ILE A 197 -4.497 -25.961 12.826 1.00 41.96 N ANISOU 1364 N ILE A 197 5813 5717 4411 -952 -819 -297 N ATOM 1365 CA ILE A 197 -5.703 -26.255 13.578 1.00 44.30 C ANISOU 1365 CA ILE A 197 6096 6037 4697 -944 -810 -302 C ATOM 1366 C ILE A 197 -6.859 -25.641 12.796 1.00 45.56 C ANISOU 1366 C ILE A 197 6196 6309 4805 -928 -817 -265 C ATOM 1367 O ILE A 197 -6.798 -24.471 12.432 1.00 46.03 O ANISOU 1367 O ILE A 197 6253 6381 4853 -880 -830 -211 O ATOM 1368 CB ILE A 197 -5.654 -25.699 15.015 1.00 46.93 C ANISOU 1368 CB ILE A 197 6480 6283 5066 -893 -814 -280 C ATOM 1369 CG1 ILE A 197 -4.465 -26.259 15.799 1.00 47.54 C ANISOU 1369 CG1 ILE A 197 6609 6262 5190 -907 -810 -308 C ATOM 1370 CG2 ILE A 197 -6.970 -25.969 15.732 1.00 49.90 C ANISOU 1370 CG2 ILE A 197 6839 6688 5431 -883 -802 -282 C ATOM 1371 CD1 ILE A 197 -4.358 -25.745 17.214 1.00 49.03 C ANISOU 1371 CD1 ILE A 197 6849 6372 5408 -866 -815 -290 C ATOM 1372 N SER A 198 -7.893 -26.440 12.518 1.00 48.81 N ANISOU 1372 N SER A 198 6559 6806 5181 -969 -806 -292 N ATOM 1373 CA SER A 198 -9.044 -25.938 11.788 1.00 50.00 C ANISOU 1373 CA SER A 198 6641 7081 5275 -956 -815 -254 C ATOM 1374 C SER A 198 -10.311 -26.641 12.262 1.00 50.11 C ANISOU 1374 C SER A 198 6618 7152 5267 -981 -801 -276 C ATOM 1375 O SER A 198 -10.246 -27.607 13.021 1.00 46.14 O ANISOU 1375 O SER A 198 6146 6593 4792 -1015 -782 -328 O ATOM 1376 CB SER A 198 -8.854 -26.066 10.294 1.00 51.70 C ANISOU 1376 CB SER A 198 6810 7388 5445 -1001 -821 -260 C ATOM 1377 OG SER A 198 -8.676 -27.418 9.906 1.00 54.94 O ANISOU 1377 OG SER A 198 7213 7813 5845 -1088 -802 -334 O ATOM 1378 N LEU A 199 -11.457 -26.093 11.835 1.00 48.89 N ANISOU 1378 N LEU A 199 6398 7113 5064 -956 -809 -230 N ATOM 1379 CA LEU A 199 -12.766 -26.621 12.172 1.00 49.24 C ANISOU 1379 CA LEU A 199 6394 7235 5079 -977 -799 -241 C ATOM 1380 C LEU A 199 -13.387 -27.174 10.892 1.00 52.81 C ANISOU 1380 C LEU A 199 6764 7841 5459 -1049 -802 -261 C ATOM 1381 O LEU A 199 -13.576 -26.432 9.931 1.00 54.30 O ANISOU 1381 O LEU A 199 6902 8123 5603 -1026 -820 -210 O ATOM 1382 CB LEU A 199 -13.621 -25.493 12.765 1.00 48.03 C ANISOU 1382 CB LEU A 199 6227 7098 4925 -886 -802 -163 C ATOM 1383 CG LEU A 199 -13.045 -24.787 13.995 1.00 44.89 C ANISOU 1383 CG LEU A 199 5913 6554 4590 -817 -797 -140 C ATOM 1384 CD1 LEU A 199 -14.108 -23.957 14.692 1.00 45.54 C ANISOU 1384 CD1 LEU A 199 5980 6653 4668 -742 -786 -77 C ATOM 1385 CD2 LEU A 199 -12.433 -25.774 14.975 1.00 43.83 C ANISOU 1385 CD2 LEU A 199 5841 6308 4503 -858 -785 -208 C ATOM 1386 N LEU A 200 -13.690 -28.476 10.887 1.00 55.69 N ANISOU 1386 N LEU A 200 7118 8232 5809 -1138 -781 -337 N ATOM 1387 CA LEU A 200 -14.259 -29.129 9.719 1.00 61.25 C ANISOU 1387 CA LEU A 200 7749 9080 6441 -1225 -778 -370 C ATOM 1388 C LEU A 200 -15.778 -29.215 9.845 1.00 64.19 C ANISOU 1388 C LEU A 200 8044 9581 6761 -1236 -778 -355 C ATOM 1389 O LEU A 200 -16.324 -29.198 10.946 1.00 65.60 O ANISOU 1389 O LEU A 200 8238 9715 6970 -1199 -769 -346 O ATOM 1390 CB LEU A 200 -13.650 -30.529 9.584 1.00 57.30 C ANISOU 1390 CB LEU A 200 7289 8528 5953 -1325 -743 -467 C ATOM 1391 CG LEU A 200 -12.127 -30.590 9.463 1.00 55.54 C ANISOU 1391 CG LEU A 200 7139 8181 5781 -1319 -737 -485 C ATOM 1392 CD1 LEU A 200 -11.689 -31.954 8.950 1.00 54.59 C ANISOU 1392 CD1 LEU A 200 7039 8049 5654 -1425 -696 -573 C ATOM 1393 CD2 LEU A 200 -11.589 -29.484 8.566 1.00 55.26 C ANISOU 1393 CD2 LEU A 200 7086 8179 5729 -1272 -770 -425 C ATOM 1394 N SER A 201 -16.444 -29.313 8.689 1.00 75.44 N ANISOU 1394 N SER A 201 9383 11175 8106 -1291 -789 -351 N ATOM 1395 CA SER A 201 -17.892 -29.418 8.624 1.00 81.20 C ANISOU 1395 CA SER A 201 10021 12057 8773 -1312 -792 -334 C ATOM 1396 C SER A 201 -18.272 -30.325 7.455 1.00 82.61 C ANISOU 1396 C SER A 201 10135 12383 8869 -1439 -786 -394 C ATOM 1397 O SER A 201 -17.742 -30.171 6.357 1.00 83.10 O ANISOU 1397 O SER A 201 10182 12496 8896 -1466 -799 -392 O ATOM 1398 CB SER A 201 -18.529 -28.056 8.499 1.00 82.43 C ANISOU 1398 CB SER A 201 10119 12295 8905 -1206 -820 -221 C ATOM 1399 OG SER A 201 -19.946 -28.160 8.480 1.00 85.92 O ANISOU 1399 OG SER A 201 10466 12890 9287 -1221 -823 -198 O ATOM 1400 N GLU A 202 -19.182 -31.274 7.710 1.00 82.45 N ANISOU 1400 N GLU A 202 10080 12429 8816 -1522 -763 -451 N ATOM 1401 CA GLU A 202 -19.623 -32.207 6.684 1.00 87.87 C ANISOU 1401 CA GLU A 202 10708 13258 9420 -1658 -749 -519 C ATOM 1402 C GLU A 202 -20.357 -31.440 5.577 1.00 87.81 C ANISOU 1402 C GLU A 202 10584 13458 9319 -1649 -790 -447 C ATOM 1403 O GLU A 202 -19.927 -31.566 4.414 1.00 86.72 O ANISOU 1403 O GLU A 202 10427 13389 9131 -1710 -797 -466 O ATOM 1404 CB GLU A 202 -20.535 -33.284 7.276 1.00 87.17 C ANISOU 1404 CB GLU A 202 10604 13200 9315 -1744 -713 -589 C ATOM 1405 CG GLU A 202 -19.879 -34.120 8.361 1.00 88.50 C ANISOU 1405 CG GLU A 202 10884 13172 9570 -1755 -666 -658 C ATOM 1406 CD GLU A 202 -20.769 -35.215 8.927 1.00 89.49 C ANISOU 1406 CD GLU A 202 10999 13321 9679 -1843 -623 -730 C ATOM 1407 OE1 GLU A 202 -21.181 -36.098 8.148 1.00 93.06 O ANISOU 1407 OE1 GLU A 202 11413 13881 10062 -1974 -597 -802 O ATOM 1408 OE2 GLU A 202 -21.062 -35.174 10.137 1.00 86.11 O ANISOU 1408 OE2 GLU A 202 10604 12807 9305 -1785 -613 -717 O TER 1409 GLU A 202 ANISOU 1410 N ASP B 33 8782 6250 6043 -98 -723 444 N ANISOU 1411 CA ASP B 33 8783 6117 6145 -123 -665 375 C ANISOU 1412 C ASP B 33 8818 6087 6251 -102 -551 472 C ANISOU 1413 O ASP B 33 8979 6292 6348 -68 -494 561 O ANISOU 1414 CB ASP B 33 8759 6064 6028 -135 -653 247 C ANISOU 1415 CG ASP B 33 8806 6150 6013 -159 -762 129 C ANISOU 1416 OD1 ASP B 33 8675 6076 5921 -172 -856 148 O ANISOU 1417 OD2 ASP B 33 8719 6034 5848 -164 -753 19 O ANISOU 1418 N LYS B 34 8796 5961 6364 -120 -520 452 N ANISOU 1419 CA LYS B 34 9045 6131 6693 -106 -422 522 C ANISOU 1420 C LYS B 34 8976 5969 6652 -129 -368 432 C ANISOU 1421 O LYS B 34 9167 6114 6899 -155 -400 343 O ANISOU 1422 CB LYS B 34 9046 6092 6821 -98 -430 584 C ANISOU 1423 CG LYS B 34 9107 6058 6970 -80 -336 646 C ANISOU 1424 CD LYS B 34 9213 6127 7185 -61 -340 704 C ANISOU 1425 CE LYS B 34 9165 5970 7219 -42 -249 748 C ANISOU 1426 NZ LYS B 34 9433 6253 7463 -18 -185 849 N ANISOU 1427 N ILE B 35 8980 5957 6629 -118 -285 465 N ANISOU 1428 CA ILE B 35 9058 5962 6745 -140 -229 394 C ANISOU 1429 C ILE B 35 9221 6021 7047 -148 -184 419 C ANISOU 1430 O ILE B 35 9694 6468 7564 -130 -123 510 O ANISOU 1431 CB ILE B 35 9220 6161 6832 -124 -159 425 C ANISOU 1432 CG1 ILE B 35 9470 6520 6918 -104 -203 402 C ANISOU 1433 CG2 ILE B 35 9021 5894 6694 -149 -104 358 C ANISOU 1434 CD1 ILE B 35 9576 6624 6980 -128 -271 263 C ANISOU 1435 N LEU B 36 9035 5779 6929 -170 -214 336 N ANISOU 1436 CA LEU B 36 8982 5631 6991 -174 -180 340 C ANISOU 1437 C LEU B 36 8805 5398 6854 -188 -103 335 C ANISOU 1438 O LEU B 36 8762 5380 6775 -204 -88 287 O ANISOU 1439 CB LEU B 36 8950 5572 7006 -190 -229 251 C ANISOU 1440 CG LEU B 36 9034 5712 7082 -181 -306 257 C ANISOU 1441 CD1 LEU B 36 8985 5628 7111 -187 -335 198 C ANISOU 1442 CD2 LEU B 36 9155 5854 7213 -149 -306 368 C ANISOU 1443 N ASP B 37 8678 5197 6811 -180 -54 390 N ANISOU 1444 CA ASP B 37 8527 4985 6731 -199 14 390 C ANISOU 1445 C ASP B 37 8159 4565 6422 -230 -1 279 C ANISOU 1446 O ASP B 37 8394 4751 6696 -226 -31 242 O ANISOU 1447 CB ASP B 37 8906 5291 7194 -181 66 478 C ANISOU 1448 CG ASP B 37 9138 5448 7530 -207 132 478 C ANISOU 1449 OD1 ASP B 37 9296 5620 7697 -239 137 414 O ANISOU 1450 OD2 ASP B 37 9494 5732 7969 -195 178 546 O ANISOU 1451 N LEU B 38 7752 4178 6017 -257 19 233 N ANISOU 1452 CA LEU B 38 7576 3968 5899 -286 4 135 C ANISOU 1453 C LEU B 38 7588 3893 6031 -307 45 135 C ANISOU 1454 O LEU B 38 7865 4169 6366 -333 88 135 O ANISOU 1455 CB LEU B 38 7458 3916 5740 -302 8 88 C ANISOU 1456 CG LEU B 38 7359 3891 5527 -285 -39 63 C ANISOU 1457 CD1 LEU B 38 7419 3992 5566 -299 -37 -8 C ANISOU 1458 CD2 LEU B 38 7109 3631 5276 -275 -105 36 C ANISOU 1459 N SER B 39 7370 3602 5852 -292 33 136 N ANISOU 1460 CA SER B 39 7353 3485 5942 -308 60 118 C ANISOU 1461 C SER B 39 6933 3026 5523 -295 12 42 C ANISOU 1462 O SER B 39 7000 3090 5546 -257 -7 69 O ANISOU 1463 CB SER B 39 7520 3595 6152 -290 110 215 C ANISOU 1464 OG SER B 39 7817 3781 6563 -309 133 186 O ANISOU 1465 N PHE B 40 6657 2726 5301 -323 -3 -44 N ANISOU 1466 CA PHE B 40 6425 2481 5051 -302 -49 -115 C ANISOU 1467 C PHE B 40 6369 2339 5066 -313 -52 -185 C ANISOU 1468 O PHE B 40 6421 2340 5202 -351 -27 -196 O ANISOU 1469 CB PHE B 40 6251 2395 4852 -317 -86 -173 C ANISOU 1470 CG PHE B 40 6189 2418 4715 -307 -100 -138 C ANISOU 1471 CD1 PHE B 40 6148 2401 4620 -270 -130 -109 C ANISOU 1472 CD2 PHE B 40 6132 2416 4647 -332 -82 -133 C ANISOU 1473 CE1 PHE B 40 6092 2420 4505 -266 -154 -88 C ANISOU 1474 CE2 PHE B 40 6119 2473 4556 -320 -100 -115 C ANISOU 1475 CZ PHE B 40 6084 2457 4473 -291 -140 -97 C ANISOU 1476 N LYS B 41 6270 2228 4928 -275 -85 -228 N ANISOU 1477 CA LYS B 41 6204 2102 4889 -270 -106 -314 C ANISOU 1478 C LYS B 41 6094 2088 4745 -267 -152 -371 C ANISOU 1479 O LYS B 41 5970 2045 4575 -252 -163 -332 O ANISOU 1480 CB LYS B 41 6260 2075 4917 -214 -97 -308 C ANISOU 1481 CG LYS B 41 6350 2056 5057 -212 -47 -254 C ANISOU 1482 CD LYS B 41 6394 2018 5070 -148 -35 -252 C ANISOU 1483 CE LYS B 41 6500 2009 5240 -142 18 -196 C ANISOU 1484 NZ LYS B 41 6573 2003 5279 -70 35 -192 N ANISOU 1485 N LYS B 42 6119 2109 4797 -279 -181 -459 N ANISOU 1486 CA LYS B 42 6042 2137 4700 -274 -220 -497 C ANISOU 1487 C LYS B 42 6021 2118 4654 -240 -257 -574 C ANISOU 1488 O LYS B 42 6000 2018 4651 -242 -262 -632 O ANISOU 1489 CB LYS B 42 6070 2214 4797 -335 -220 -519 C ANISOU 1490 CG LYS B 42 6243 2327 5056 -380 -222 -576 C ANISOU 1491 CD LYS B 42 6342 2480 5244 -440 -216 -583 C ANISOU 1492 CE LYS B 42 6422 2675 5321 -439 -250 -619 C ANISOU 1493 NZ LYS B 42 6506 2810 5504 -495 -239 -623 N ANISOU 1494 N ILE B 43 5854 2048 4450 -207 -282 -573 N ANISOU 1495 CA ILE B 43 5869 2105 4434 -167 -317 -632 C ANISOU 1496 C ILE B 43 5837 2184 4442 -195 -343 -652 C ANISOU 1497 O ILE B 43 5681 2086 4301 -205 -333 -601 O ANISOU 1498 CB ILE B 43 5832 2093 4327 -87 -315 -590 C ANISOU 1499 CG1 ILE B 43 5894 2057 4357 -55 -281 -545 C ANISOU 1500 CG2 ILE B 43 5844 2156 4298 -38 -346 -650 C ANISOU 1501 CD1 ILE B 43 6054 2102 4509 -50 -275 -612 C ANISOU 1502 N GLU B 44 5967 2343 4595 -207 -377 -729 N ANISOU 1503 CA GLU B 44 5974 2459 4653 -231 -401 -747 C ANISOU 1504 C GLU B 44 5958 2532 4594 -173 -437 -777 C ANISOU 1505 O GLU B 44 6000 2545 4590 -145 -461 -837 O ANISOU 1506 CB GLU B 44 6135 2602 4896 -298 -415 -807 C ANISOU 1507 CG GLU B 44 6272 2665 5093 -356 -375 -772 C ANISOU 1508 CD GLU B 44 6454 2826 5378 -422 -389 -824 C ANISOU 1509 OE1 GLU B 44 6536 2943 5478 -424 -438 -898 O ANISOU 1510 OE2 GLU B 44 6597 2928 5590 -469 -352 -787 O ANISOU 1511 N THR B 45 5836 2520 4488 -152 -440 -735 N ANISOU 1512 CA THR B 45 5793 2575 4412 -91 -469 -748 C ANISOU 1513 C THR B 45 5760 2662 4454 -113 -489 -754 C ANISOU 1514 O THR B 45 5545 2496 4288 -119 -470 -698 O ANISOU 1515 CB THR B 45 5791 2601 4363 -19 -450 -676 C ANISOU 1516 OG1 THR B 45 5845 2546 4354 2 -431 -674 O ANISOU 1517 CG2 THR B 45 5799 2724 4340 52 -472 -673 C ANISOU 1518 N ASP B 46 5834 2782 4536 -122 -531 -824 N ANISOU 1519 CA ASP B 46 5805 2877 4584 -140 -555 -830 C ANISOU 1520 C ASP B 46 5674 2730 4551 -213 -528 -809 C ANISOU 1521 O ASP B 46 5500 2641 4439 -212 -516 -769 O ANISOU 1522 CB ASP B 46 5790 2989 4558 -69 -556 -774 C ANISOU 1523 CG ASP B 46 5937 3188 4610 7 -586 -799 C ANISOU 1524 OD1 ASP B 46 5987 3169 4595 3 -612 -876 O ANISOU 1525 OD2 ASP B 46 6021 3382 4688 74 -581 -740 O ANISOU 1526 N LEU B 47 5645 2591 4539 -269 -514 -835 N ANISOU 1527 CA LEU B 47 5589 2521 4570 -333 -483 -813 C ANISOU 1528 C LEU B 47 5708 2521 4707 -385 -470 -839 C ANISOU 1529 O LEU B 47 5785 2504 4719 -367 -473 -858 O ANISOU 1530 CB LEU B 47 5453 2379 4421 -318 -436 -742 C ANISOU 1531 CG LEU B 47 5461 2290 4346 -294 -412 -708 C ANISOU 1532 CD1 LEU B 47 5525 2246 4414 -340 -386 -710 C ANISOU 1533 CD2 LEU B 47 5379 2235 4257 -271 -388 -649 C ANISOU 1534 N SER B 48 5754 2575 4854 -446 -451 -832 N ANISOU 1535 CA SER B 48 5863 2582 5010 -498 -429 -836 C ANISOU 1536 C SER B 48 5800 2498 4952 -511 -365 -762 C ANISOU 1537 O SER B 48 5729 2503 4885 -497 -347 -730 O ANISOU 1538 CB SER B 48 5957 2704 5227 -558 -461 -883 C ANISOU 1539 OG SER B 48 6015 2870 5376 -582 -447 -853 O ANISOU 1540 N SER B 49 5841 2438 4994 -534 -330 -737 N ANISOU 1541 CA SER B 49 5806 2388 4944 -538 -271 -667 C ANISOU 1542 C SER B 49 5930 2433 5129 -579 -231 -635 C ANISOU 1543 O SER B 49 5962 2392 5205 -601 -249 -668 O ANISOU 1544 CB SER B 49 5735 2291 4752 -486 -263 -635 C ANISOU 1545 OG SER B 49 5717 2185 4684 -465 -277 -647 O ANISOU 1546 N LYS B 50 5995 2516 5194 -585 -175 -571 N ANISOU 1547 CA LYS B 50 6182 2649 5432 -613 -122 -514 C ANISOU 1548 C LYS B 50 6304 2759 5440 -577 -81 -449 C ANISOU 1549 O LYS B 50 6187 2705 5255 -551 -76 -444 O ANISOU 1550 CB LYS B 50 6225 2757 5603 -656 -88 -488 C ANISOU 1551 CG LYS B 50 6258 2826 5775 -702 -132 -545 C ANISOU 1552 CD LYS B 50 6248 2886 5910 -743 -90 -501 C ANISOU 1553 CE LYS B 50 6145 2880 5761 -713 -49 -466 C ANISOU 1554 NZ LYS B 50 6124 2932 5881 -744 1 -414 N ANISOU 1555 N ILE B 51 6452 2826 5571 -574 -53 -403 N ANISOU 1556 CA ILE B 51 6519 2889 5533 -540 -19 -337 C ANISOU 1557 C ILE B 51 6782 3143 5855 -560 47 -257 C ANISOU 1558 O ILE B 51 6727 3011 5862 -574 65 -226 O ANISOU 1559 CB ILE B 51 6515 2815 5446 -505 -44 -334 C ANISOU 1560 CG1 ILE B 51 6466 2783 5352 -480 -104 -402 C ANISOU 1561 CG2 ILE B 51 6529 2838 5356 -472 -17 -263 C ANISOU 1562 CD1 ILE B 51 6479 2741 5287 -438 -123 -391 C ANISOU 1563 N THR B 52 6955 3394 6014 -556 87 -223 N ANISOU 1564 CA THR B 52 7159 3612 6266 -564 159 -136 C ANISOU 1565 C THR B 52 7493 3960 6452 -517 185 -76 C ANISOU 1566 O THR B 52 7526 4033 6364 -487 158 -108 O ANISOU 1567 CB THR B 52 7131 3671 6317 -582 196 -129 C ANISOU 1568 OG1 THR B 52 7019 3561 6336 -625 156 -192 O ANISOU 1569 CG2 THR B 52 7272 3835 6527 -588 278 -27 C ANISOU 1570 N TYR B 53 7897 4331 6873 -512 233 12 N ANISOU 1571 CA TYR B 53 8456 4916 7296 -467 256 79 C ANISOU 1572 C TYR B 53 8948 5488 7784 -453 331 156 C ANISOU 1573 O TYR B 53 8890 5422 7824 -463 391 243 O ANISOU 1574 CB TYR B 53 8660 5042 7508 -456 258 135 C ANISOU 1575 CG TYR B 53 8663 4971 7496 -456 192 66 C ANISOU 1576 CD1 TYR B 53 8631 4886 7566 -490 158 -11 C ANISOU 1577 CD2 TYR B 53 8759 5066 7472 -417 159 77 C ANISOU 1578 CE1 TYR B 53 8500 4696 7408 -479 103 -72 C ANISOU 1579 CE2 TYR B 53 8540 4791 7242 -408 106 23 C ANISOU 1580 CZ TYR B 53 8425 4619 7217 -435 81 -50 C ANISOU 1581 OH TYR B 53 8342 4489 7107 -416 35 -99 O ANISOU 1582 N GLU B 54 9806 6424 8531 -427 330 124 N ANISOU 1583 CA GLU B 54 10661 7364 9353 -401 403 186 C ANISOU 1584 C GLU B 54 11199 7940 9722 -348 417 245 C ANISOU 1585 O GLU B 54 11558 8262 10005 -336 366 236 O ANISOU 1586 CB GLU B 54 11160 7921 9828 -396 397 110 C ANISOU 1587 CG GLU B 54 11268 8014 10105 -446 380 59 C ANISOU 1588 CD GLU B 54 11595 8400 10424 -439 377 -7 C ANISOU 1589 OE1 GLU B 54 11840 8688 10526 -394 388 -24 O ANISOU 1590 OE2 GLU B 54 11510 8321 10479 -477 362 -43 O ANISOU 1591 N ASP B 55 11746 8571 10214 -312 488 310 N ANISOU 1592 CA ASP B 55 12132 9015 10427 -255 503 368 C ANISOU 1593 C ASP B 55 12490 9397 10608 -229 438 265 C ANISOU 1594 O ASP B 55 12715 9651 10682 -193 410 279 O ANISOU 1595 CB ASP B 55 12133 9106 10422 -217 605 475 C ANISOU 1596 CG ASP B 55 12123 9158 10415 -207 646 433 C ANISOU 1597 OD1 ASP B 55 11580 8584 9886 -232 594 319 O ANISOU 1598 OD2 ASP B 55 12297 9416 10581 -168 735 521 O ANISOU 1599 N THR B 56 12718 9612 10868 -249 411 164 N ANISOU 1600 CA THR B 56 12631 9536 10648 -230 351 60 C ANISOU 1601 C THR B 56 12000 8831 10068 -266 263 -14 C ANISOU 1602 O THR B 56 11610 8432 9676 -272 224 -106 O ANISOU 1603 CB THR B 56 13435 10387 11445 -213 393 10 C ANISOU 1604 OG1 THR B 56 14160 11108 12048 -194 333 -93 O ANISOU 1605 CG2 THR B 56 13432 10364 11630 -257 410 -8 C ANISOU 1606 N GLY B 57 11232 8013 9347 -283 238 30 N ANISOU 1607 CA GLY B 57 10490 7208 8646 -307 163 -26 C ANISOU 1608 C GLY B 57 9697 6358 8019 -349 167 -37 C ANISOU 1609 O GLY B 57 9503 6166 7924 -366 225 6 O ANISOU 1610 N VAL B 58 8776 5392 7127 -362 104 -98 N ANISOU 1611 CA VAL B 58 8157 4723 6641 -396 92 -125 C ANISOU 1612 C VAL B 58 7503 4097 6028 -408 68 -207 C ANISOU 1613 O VAL B 58 7257 3867 5721 -391 24 -256 O ANISOU 1614 CB VAL B 58 8177 4679 6661 -392 45 -126 C ANISOU 1615 CG1 VAL B 58 8187 4639 6785 -419 25 -170 C ANISOU 1616 CG2 VAL B 58 8405 4880 6860 -376 72 -37 C ANISOU 1617 N LYS B 59 7133 3737 5778 -437 96 -215 N ANISOU 1618 CA LYS B 59 7092 3733 5796 -449 77 -280 C ANISOU 1619 C LYS B 59 6938 3542 5714 -467 23 -325 C ANISOU 1620 O LYS B 59 6894 3449 5741 -491 24 -311 O ANISOU 1621 CB LYS B 59 7179 3870 5980 -468 135 -258 C ANISOU 1622 CG LYS B 59 7195 3934 6078 -480 120 -315 C ANISOU 1623 CD LYS B 59 7320 4119 6320 -500 177 -284 C ANISOU 1624 CE LYS B 59 7649 4494 6579 -467 249 -238 C ANISOU 1625 NZ LYS B 59 7793 4703 6855 -483 310 -197 N ANISOU 1626 N ILE B 60 6790 3416 5547 -453 -22 -380 N ANISOU 1627 CA ILE B 60 6639 3247 5443 -458 -73 -422 C ANISOU 1628 C ILE B 60 6418 3093 5306 -468 -82 -465 C ANISOU 1629 O ILE B 60 6131 2851 4996 -449 -85 -483 O ANISOU 1630 CB ILE B 60 6784 3375 5507 -424 -117 -430 C ANISOU 1631 CG1 ILE B 60 6994 3533 5641 -411 -108 -379 C ANISOU 1632 CG2 ILE B 60 6729 3314 5491 -417 -163 -468 C ANISOU 1633 CD1 ILE B 60 6935 3466 5516 -380 -150 -375 C ANISOU 1634 N GLU B 61 6289 2966 5279 -500 -89 -481 N ANISOU 1635 CA GLU B 61 6218 2969 5304 -515 -103 -515 C ANISOU 1636 C GLU B 61 6142 2895 5248 -510 -165 -563 C ANISOU 1637 O GLU B 61 6321 3018 5444 -527 -185 -577 O ANISOU 1638 CB GLU B 61 6385 3153 5588 -559 -68 -494 C ANISOU 1639 CG GLU B 61 6551 3327 5736 -557 2 -436 C ANISOU 1640 CD GLU B 61 6643 3434 5962 -600 42 -397 C ANISOU 1641 OE1 GLU B 61 6694 3552 6135 -625 35 -413 O ANISOU 1642 OE2 GLU B 61 6656 3399 5971 -608 81 -344 O ANISOU 1643 N THR B 62 6008 2827 5115 -484 -192 -586 N ANISOU 1644 CA THR B 62 5955 2798 5071 -469 -248 -625 C ANISOU 1645 C THR B 62 6038 2984 5255 -480 -264 -647 C ANISOU 1646 O THR B 62 5946 2951 5204 -477 -234 -628 O ANISOU 1647 CB THR B 62 5858 2700 4892 -418 -269 -618 C ANISOU 1648 OG1 THR B 62 5827 2724 4874 -401 -251 -604 O ANISOU 1649 CG2 THR B 62 5915 2669 4857 -404 -260 -592 C ANISOU 1650 N ASP B 63 6179 3146 5433 -490 -313 -687 N ANISOU 1651 CA ASP B 63 6330 3408 5678 -498 -344 -710 C ANISOU 1652 C ASP B 63 6251 3366 5542 -452 -398 -738 C ANISOU 1653 O ASP B 63 6122 3184 5363 -449 -432 -776 O ANISOU 1654 CB ASP B 63 6626 3709 6083 -559 -357 -733 C ANISOU 1655 CG ASP B 63 6989 4201 6557 -574 -396 -755 C ANISOU 1656 OD1 ASP B 63 7253 4554 6808 -531 -410 -747 O ANISOU 1657 OD2 ASP B 63 7388 4616 7065 -628 -414 -773 O ANISOU 1658 N SER B 64 6139 3342 5437 -410 -399 -715 N ANISOU 1659 CA SER B 64 6323 3579 5572 -356 -440 -723 C ANISOU 1660 C SER B 64 6405 3801 5732 -331 -450 -703 C ANISOU 1661 O SER B 64 6561 4002 5977 -354 -421 -683 O ANISOU 1662 CB SER B 64 6303 3492 5459 -313 -423 -692 C ANISOU 1663 OG SER B 64 6204 3389 5378 -308 -380 -650 O ANISOU 1664 N SER B 65 6583 4053 5878 -277 -486 -700 N ANISOU 1665 CA SER B 65 6543 4158 5912 -243 -497 -670 C ANISOU 1666 C SER B 65 6596 4227 5956 -184 -468 -608 C ANISOU 1667 O SER B 65 6380 3961 5658 -147 -470 -596 O ANISOU 1668 CB SER B 65 6724 4436 6077 -222 -561 -706 C ANISOU 1669 OG SER B 65 6682 4381 6068 -284 -596 -769 O ANISOU 1670 N LYS B 66 6506 4211 5965 -173 -440 -566 N ANISOU 1671 CA LYS B 66 6849 4573 6340 -123 -411 -506 C ANISOU 1672 C LYS B 66 6895 4697 6351 -56 -440 -472 C ANISOU 1673 O LYS B 66 6710 4492 6166 -16 -421 -423 O ANISOU 1674 CB LYS B 66 7001 4809 6621 -121 -381 -475 C ANISOU 1675 CG LYS B 66 7087 4923 6776 -69 -350 -412 C ANISOU 1676 CD LYS B 66 7308 5210 7128 -66 -313 -385 C ANISOU 1677 CE LYS B 66 7542 5599 7434 -59 -340 -372 C ANISOU 1678 NZ LYS B 66 7768 5890 7798 -50 -296 -337 N ANISOU 1679 N SER B 67 7295 5189 6725 -42 -488 -498 N ANISOU 1680 CA SER B 67 7438 5424 6821 30 -514 -466 C ANISOU 1681 C SER B 67 7608 5501 6859 50 -525 -489 C ANISOU 1682 O SER B 67 7817 5754 7037 119 -520 -436 O ANISOU 1683 CB SER B 67 7547 5680 6944 43 -565 -490 C ANISOU 1684 OG SER B 67 7882 5962 7231 -16 -605 -580 O ANISOU 1685 N ASP B 68 7437 5209 6621 -3 -535 -559 N ANISOU 1686 CA ASP B 68 7342 5018 6408 15 -540 -579 C ANISOU 1687 C ASP B 68 7068 4665 6139 27 -496 -519 C ANISOU 1688 O ASP B 68 6924 4408 5995 -24 -474 -533 O ANISOU 1689 CB ASP B 68 7652 5218 6668 -46 -559 -663 C ANISOU 1690 CG ASP B 68 8025 5659 7039 -63 -614 -735 C ANISOU 1691 OD1 ASP B 68 8545 6325 7580 -21 -642 -719 O ANISOU 1692 OD2 ASP B 68 8035 5580 7035 -119 -632 -803 O ANISOU 1693 N LYS B 69 6906 4566 5980 98 -486 -449 N ANISOU 1694 CA LYS B 69 7070 4674 6173 111 -452 -385 C ANISOU 1695 C LYS B 69 6934 4425 5939 113 -449 -396 C ANISOU 1696 O LYS B 69 6585 4023 5614 115 -428 -348 O ANISOU 1697 CB LYS B 69 7302 5024 6472 186 -441 -295 C ANISOU 1698 CG LYS B 69 7492 5323 6781 191 -435 -265 C ANISOU 1699 CD LYS B 69 7716 5665 7088 269 -417 -161 C ANISOU 1700 CE LYS B 69 8084 6137 7369 349 -434 -136 C ANISOU 1701 NZ LYS B 69 8224 6402 7602 429 -409 -18 N ANISOU 1702 N GLU B 70 7029 4484 5934 112 -471 -459 N ANISOU 1703 CA GLU B 70 7011 4356 5829 118 -463 -468 C ANISOU 1704 C GLU B 70 6654 3874 5460 38 -458 -522 C ANISOU 1705 O GLU B 70 6676 3799 5411 35 -453 -541 O ANISOU 1706 CB GLU B 70 7522 4890 6235 178 -482 -501 C ANISOU 1707 CG GLU B 70 7949 5444 6656 272 -477 -431 C ANISOU 1708 CD GLU B 70 8651 6135 7388 314 -442 -333 C ANISOU 1709 OE1 GLU B 70 9059 6435 7810 269 -427 -325 O ANISOU 1710 OE2 GLU B 70 9268 6862 8023 393 -430 -258 O ANISOU 1711 N ARG B 71 6355 3579 5233 -20 -453 -539 N ANISOU 1712 CA ARG B 71 6126 3249 5002 -90 -441 -576 C ANISOU 1713 C ARG B 71 6058 3085 4892 -91 -419 -540 C ANISOU 1714 O ARG B 71 5925 2972 4783 -64 -409 -483 O ANISOU 1715 CB ARG B 71 6136 3285 5098 -136 -424 -573 C ANISOU 1716 CG ARG B 71 6177 3434 5207 -140 -442 -595 C ANISOU 1717 CD ARG B 71 6123 3397 5238 -177 -414 -585 C ANISOU 1718 NE ARG B 71 6032 3300 5174 -154 -390 -535 N ANISOU 1719 CZ ARG B 71 6045 3391 5274 -132 -379 -503 C ANISOU 1720 NH1 ARG B 71 6156 3607 5450 -123 -389 -505 N ANISOU 1721 NH2 ARG B 71 6111 3429 5368 -117 -361 -467 N ANISOU 1722 N TYR B 72 5933 2859 4720 -125 -411 -568 N ANISOU 1723 CA TYR B 72 5883 2732 4631 -121 -392 -527 C ANISOU 1724 C TYR B 72 5744 2490 4460 -165 -378 -555 C ANISOU 1725 O TYR B 72 5743 2459 4442 -171 -389 -604 O ANISOU 1726 CB TYR B 72 6015 2879 4717 -52 -398 -493 C ANISOU 1727 CG TYR B 72 6114 2951 4809 -31 -386 -424 C ANISOU 1728 CD1 TYR B 72 6076 2961 4834 -32 -387 -378 C ANISOU 1729 CD2 TYR B 72 6119 2888 4755 -6 -375 -404 C ANISOU 1730 CE1 TYR B 72 6018 2888 4786 -17 -386 -316 C ANISOU 1731 CE2 TYR B 72 6067 2829 4711 13 -368 -333 C ANISOU 1732 CZ TYR B 72 5993 2808 4704 5 -377 -290 C ANISOU 1733 OH TYR B 72 6039 2852 4772 18 -380 -223 O ANISOU 1734 N LEU B 73 5569 2266 4282 -197 -355 -525 N ANISOU 1735 CA LEU B 73 5563 2169 4253 -232 -335 -531 C ANISOU 1736 C LEU B 73 5485 2040 4126 -214 -321 -474 C ANISOU 1737 O LEU B 73 5446 2021 4085 -221 -317 -439 O ANISOU 1738 CB LEU B 73 5553 2160 4287 -288 -314 -545 C ANISOU 1739 CG LEU B 73 5617 2138 4341 -321 -284 -532 C ANISOU 1740 CD1 LEU B 73 5692 2159 4440 -333 -292 -575 C ANISOU 1741 CD2 LEU B 73 5612 2151 4370 -363 -254 -521 C ANISOU 1742 N TYR B 74 5426 1914 4031 -192 -315 -469 N ANISOU 1743 CA TYR B 74 5375 1818 3941 -170 -301 -408 C ANISOU 1744 C TYR B 74 5422 1780 3983 -202 -271 -399 C ANISOU 1745 O TYR B 74 5460 1755 4030 -207 -262 -435 O ANISOU 1746 CB TYR B 74 5352 1792 3888 -106 -308 -394 C ANISOU 1747 CG TYR B 74 5360 1753 3865 -76 -291 -329 C ANISOU 1748 CD1 TYR B 74 5308 1728 3818 -81 -293 -263 C ANISOU 1749 CD2 TYR B 74 5415 1738 3888 -37 -274 -335 C ANISOU 1750 CE1 TYR B 74 5345 1735 3835 -51 -281 -195 C ANISOU 1751 CE2 TYR B 74 5453 1736 3907 -2 -253 -268 C ANISOU 1752 CZ TYR B 74 5402 1724 3868 -11 -257 -193 C ANISOU 1753 OH TYR B 74 5297 1591 3752 25 -238 -121 O ANISOU 1754 N ILE B 75 5404 1765 3953 -223 -256 -351 N ANISOU 1755 CA ILE B 75 5489 1786 4034 -247 -221 -318 C ANISOU 1756 C ILE B 75 5535 1821 4038 -214 -218 -243 C ANISOU 1757 O ILE B 75 5314 1660 3797 -201 -242 -216 O ANISOU 1758 CB ILE B 75 5348 1676 3909 -293 -203 -319 C ANISOU 1759 CG1 ILE B 75 5420 1815 3941 -288 -220 -297 C ANISOU 1760 CG2 ILE B 75 5326 1671 3946 -324 -206 -384 C ANISOU 1761 CD1 ILE B 75 5449 1878 3969 -321 -199 -306 C ANISOU 1762 N TYR B 76 5620 1828 4122 -199 -190 -211 N ANISOU 1763 CA TYR B 76 5749 1952 4221 -163 -184 -132 C ANISOU 1764 C TYR B 76 6026 2149 4511 -164 -140 -83 C ANISOU 1765 O TYR B 76 5975 2032 4502 -189 -114 -117 O ANISOU 1766 CB TYR B 76 5715 1912 4180 -106 -197 -127 C ANISOU 1767 CG TYR B 76 5741 1845 4216 -85 -174 -168 C ANISOU 1768 CD1 TYR B 76 5722 1806 4215 -105 -184 -259 C ANISOU 1769 CD2 TYR B 76 5727 1756 4200 -51 -140 -118 C ANISOU 1770 CE1 TYR B 76 5794 1785 4294 -89 -170 -310 C ANISOU 1771 CE2 TYR B 76 5891 1818 4375 -31 -118 -165 C ANISOU 1772 CZ TYR B 76 5861 1765 4356 -52 -136 -267 C ANISOU 1773 OH TYR B 76 5874 1670 4377 -34 -121 -325 O ANISOU 1774 N GLN B 77 6313 2447 4775 -135 -132 1 N ANISOU 1775 CA GLN B 77 6727 2795 5206 -124 -87 68 C ANISOU 1776 C GLN B 77 6824 2890 5291 -66 -87 137 C ANISOU 1777 O GLN B 77 6707 2857 5149 -50 -124 169 O ANISOU 1778 CB GLN B 77 6958 3069 5421 -154 -70 126 C ANISOU 1779 CG GLN B 77 7339 3393 5832 -139 -17 213 C ANISOU 1780 CD GLN B 77 7560 3670 6030 -160 4 279 C ANISOU 1781 OE1 GLN B 77 7541 3729 5964 -185 -19 253 O ANISOU 1782 NE2 GLN B 77 7996 4068 6501 -144 54 369 N ANISOU 1783 N ASN B 78 6979 2947 5476 -34 -47 154 N ANISOU 1784 CA ASN B 78 7129 3083 5625 28 -33 225 C ANISOU 1785 C ASN B 78 7409 3367 5920 33 -1 337 C ANISOU 1786 O ASN B 78 7000 2903 5542 6 36 349 O ANISOU 1787 CB ASN B 78 7196 3039 5709 70 -5 174 C ANISOU 1788 CG ASN B 78 7157 3021 5641 80 -40 77 C ANISOU 1789 OD1 ASN B 78 6983 2947 5448 61 -82 64 O ANISOU 1790 ND2 ASN B 78 7108 2882 5588 117 -22 14 N ANISOU 1791 N ILE B 79 7703 3736 6200 70 -17 425 N ANISOU 1792 CA ILE B 79 8012 4079 6516 82 2 542 C ANISOU 1793 C ILE B 79 8146 4244 6668 145 3 632 C ANISOU 1794 O ILE B 79 8380 4450 6913 186 3 604 O ANISOU 1795 CB ILE B 79 7981 4164 6435 37 -40 555 C ANISOU 1796 CG1 ILE B 79 7905 4190 6333 35 -110 535 C ANISOU 1797 CG2 ILE B 79 8033 4189 6477 -17 -29 479 C ANISOU 1798 CD1 ILE B 79 7951 4338 6325 -6 -158 529 C ANISOU 1799 N LYS B 80 8206 4368 6733 158 7 748 N ANISOU 1800 CA LYS B 80 8212 4430 6767 214 4 854 C ANISOU 1801 C LYS B 80 8189 4538 6719 195 -35 943 C ANISOU 1802 O LYS B 80 8087 4436 6626 206 2 1029 O ANISOU 1803 CB LYS B 80 8440 4553 7052 275 79 918 C ANISOU 1804 CG LYS B 80 8612 4588 7238 304 118 825 C ANISOU 1805 CD LYS B 80 8844 4714 7524 374 191 888 C ANISOU 1806 CE LYS B 80 9129 4938 7857 366 246 959 C ANISOU 1807 NZ LYS B 80 9383 5081 8175 439 320 1020 N ANISOU 1808 N GLU B 81 7991 4452 6491 168 -112 919 N ANISOU 1809 CA GLU B 81 8038 4628 6499 146 -165 978 C ANISOU 1810 C GLU B 81 7759 4464 6247 149 -243 1004 C ANISOU 1811 O GLU B 81 7831 4520 6370 168 -250 979 O ANISOU 1812 CB GLU B 81 8230 4833 6615 86 -186 891 C ANISOU 1813 CG GLU B 81 8537 5048 6913 77 -112 882 C ANISOU 1814 CD GLU B 81 8638 5168 6948 25 -124 802 C ANISOU 1815 OE1 GLU B 81 8569 5169 6832 -2 -190 739 O ANISOU 1816 OE2 GLU B 81 9064 5539 7377 15 -65 809 O ANISOU 1817 N ASN B 82 7510 4337 5965 131 -301 1057 N ANISOU 1818 CA ASN B 82 7225 4174 5716 123 -388 1084 C ANISOU 1819 C ASN B 82 7194 4204 5608 61 -463 993 C ANISOU 1820 O ASN B 82 7414 4461 5742 46 -467 999 O ANISOU 1821 CB ASN B 82 7180 4223 5714 163 -398 1232 C ANISOU 1822 CG ASN B 82 7080 4260 5672 150 -496 1270 C ANISOU 1823 OD1 ASN B 82 6965 4171 5559 105 -562 1182 O ANISOU 1824 ND2 ASN B 82 7102 4374 5750 186 -508 1404 N ANISOU 1825 N TRP B 83 7014 4030 5461 32 -514 910 N ANISOU 1826 CA TRP B 83 6910 3968 5299 -22 -583 812 C ANISOU 1827 C TRP B 83 6985 4154 5440 -41 -684 831 C ANISOU 1828 O TRP B 83 6788 3975 5241 -85 -746 740 O ANISOU 1829 CB TRP B 83 6687 3654 5073 -45 -557 691 C ANISOU 1830 CG TRP B 83 6632 3497 4963 -41 -473 655 C ANISOU 1831 CD1 TRP B 83 6739 3575 5030 -19 -413 717 C ANISOU 1832 CD2 TRP B 83 6547 3329 4874 -60 -441 552 C ANISOU 1833 NE1 TRP B 83 6737 3475 5009 -29 -348 656 N ANISOU 1834 CE2 TRP B 83 6632 3339 4921 -54 -367 553 C ANISOU 1835 CE3 TRP B 83 6402 3172 4764 -80 -468 465 C ANISOU 1836 CZ2 TRP B 83 6536 3161 4822 -72 -327 466 C ANISOU 1837 CZ3 TRP B 83 6380 3074 4729 -93 -425 383 C ANISOU 1838 CH2 TRP B 83 6391 3016 4703 -91 -358 381 C ANISOU 1839 N SER B 84 7076 4320 5602 -9 -701 953 N ANISOU 1840 CA SER B 84 7152 4511 5766 -29 -800 987 C ANISOU 1841 C SER B 84 7146 4587 5672 -78 -893 930 C ANISOU 1842 O SER B 84 7100 4593 5679 -120 -983 877 O ANISOU 1843 CB SER B 84 7189 4621 5894 18 -793 1139 C ANISOU 1844 OG SER B 84 7183 4537 5963 71 -708 1184 O ANISOU 1845 N MSE B 85 7160 4612 5552 -69 -868 941 N ANISOU 1846 CA MSE B 85 7166 4702 5444 -102 -947 891 C ANISOU 1847 C MSE B 85 7255 4731 5460 -147 -967 732 C ANISOU 1848 O MSE B 85 7393 4928 5496 -173 -1036 667 O ANISOU 1849 CB MSE B 85 7213 4783 5369 -68 -898 964 C ANISOU 1850 CG MSE B 85 7125 4578 5205 -53 -786 928 C ANISOU 1851 SE MSE B 85 6814 4128 5018 -6 -657 1002 SE ANISOU 1852 CE MSE B 85 6947 4372 5222 49 -661 1202 C ANISOU 1853 N TYR B 86 7152 4514 5403 -151 -907 669 N ANISOU 1854 CA TYR B 86 7111 4414 5305 -187 -915 528 C ANISOU 1855 C TYR B 86 7078 4374 5403 -219 -977 472 C ANISOU 1856 O TYR B 86 6841 4167 5303 -207 -993 549 O ANISOU 1857 CB TYR B 86 7036 4229 5182 -170 -805 498 C ANISOU 1858 CG TYR B 86 7034 4234 5079 -140 -741 565 C ANISOU 1859 CD1 TYR B 86 7140 4408 5049 -144 -767 552 C ANISOU 1860 CD2 TYR B 86 7022 4161 5111 -104 -652 646 C ANISOU 1861 CE1 TYR B 86 7247 4533 5076 -111 -703 631 C ANISOU 1862 CE2 TYR B 86 7131 4272 5152 -77 -589 717 C ANISOU 1863 CZ TYR B 86 7262 4482 5157 -80 -612 718 C ANISOU 1864 OH TYR B 86 7487 4718 5327 -48 -543 805 O ANISOU 1865 N ASN B 87 7282 4543 5573 -255 -1006 346 N ANISOU 1866 CA ASN B 87 7365 4616 5791 -286 -1062 293 C ANISOU 1867 C ASN B 87 7214 4372 5633 -301 -1021 182 C ANISOU 1868 O ASN B 87 7277 4417 5830 -315 -1041 160 O ANISOU 1869 CB ASN B 87 7673 5003 6113 -328 -1187 250 C ANISOU 1870 CG ASN B 87 7929 5372 6405 -319 -1246 361 C ANISOU 1871 OD1 ASN B 87 8175 5659 6535 -292 -1222 420 O ANISOU 1872 ND2 ASN B 87 8063 5563 6707 -343 -1326 396 N ANISOU 1873 N ASN B 88 7287 4398 5566 -296 -965 120 N ANISOU 1874 CA ASN B 88 7627 4659 5908 -308 -926 21 C ANISOU 1875 C ASN B 88 7828 4801 6028 -284 -823 23 C ANISOU 1876 O ASN B 88 7630 4618 5743 -264 -785 80 O ANISOU 1877 CB ASN B 88 7879 4910 6095 -340 -983 -98 C ANISOU 1878 CG ASN B 88 7944 5014 6271 -373 -1089 -123 C ANISOU 1879 OD1 ASN B 88 8078 5107 6501 -395 -1108 -191 O ANISOU 1880 ND2 ASN B 88 8192 5345 6528 -378 -1159 -60 N ANISOU 1881 N PHE B 89 8162 5071 6403 -289 -780 -39 N ANISOU 1882 CA PHE B 89 8290 5142 6485 -275 -691 -49 C ANISOU 1883 C PHE B 89 8690 5521 6808 -292 -679 -151 C ANISOU 1884 O PHE B 89 9030 5841 7207 -308 -700 -222 O ANISOU 1885 CB PHE B 89 8195 5005 6503 -262 -654 -35 C ANISOU 1886 CG PHE B 89 8179 4934 6462 -248 -570 -31 C ANISOU 1887 CD1 PHE B 89 8123 4864 6369 -226 -528 41 C ANISOU 1888 CD2 PHE B 89 8155 4871 6460 -256 -536 -98 C ANISOU 1889 CE1 PHE B 89 8240 4922 6482 -218 -458 40 C ANISOU 1890 CE2 PHE B 89 8164 4834 6459 -248 -470 -97 C ANISOU 1891 CZ PHE B 89 8150 4798 6416 -231 -433 -32 C ANISOU 1892 N TYR B 90 9142 5982 7135 -284 -640 -150 N ANISOU 1893 CA TYR B 90 9192 6021 7098 -289 -617 -235 C ANISOU 1894 C TYR B 90 8634 5413 6560 -284 -528 -239 C ANISOU 1895 O TYR B 90 8746 5515 6662 -272 -475 -170 O ANISOU 1896 CB TYR B 90 9846 6732 7600 -276 -630 -223 C ANISOU 1897 CG TYR B 90 10189 7076 7824 -268 -596 -296 C ANISOU 1898 CD1 TYR B 90 10293 7151 7918 -258 -503 -287 C ANISOU 1899 CD2 TYR B 90 10429 7350 7963 -269 -655 -374 C ANISOU 1900 CE1 TYR B 90 10631 7500 8152 -243 -463 -342 C ANISOU 1901 CE2 TYR B 90 10816 7741 8229 -250 -617 -441 C ANISOU 1902 CZ TYR B 90 10802 7704 8210 -235 -516 -419 C ANISOU 1903 OH TYR B 90 10886 7799 8181 -211 -469 -474 O ANISOU 1904 N ILE B 91 7336 5489 6163 -155 -215 -62 N ANISOU 1905 CA ILE B 91 7176 5206 6122 -176 -199 -42 C ANISOU 1906 C ILE B 91 6844 4959 5783 -159 -194 -107 C ANISOU 1907 O ILE B 91 7004 5067 5892 -176 -246 -238 O ANISOU 1908 CB ILE B 91 7080 4869 6057 -226 -251 -105 C ANISOU 1909 CG1 ILE B 91 7173 4849 6268 -244 -255 -122 C ANISOU 1910 CG2 ILE B 91 7357 5093 6234 -248 -311 -222 C ANISOU 1911 CD1 ILE B 91 7139 4835 6407 -233 -202 -8 C ANISOU 1912 N GLU B 92 6562 4821 5576 -119 -127 -3 N ANISOU 1913 CA GLU B 92 6532 4898 5556 -92 -108 -45 C ANISOU 1914 C GLU B 92 6217 4404 5397 -135 -108 -33 C ANISOU 1915 O GLU B 92 5848 4004 5184 -142 -66 90 O ANISOU 1916 CB GLU B 92 6853 5524 5865 -11 -29 75 C ANISOU 1917 CG GLU B 92 7120 5952 6129 36 -2 32 C ANISOU 1918 CD GLU B 92 7346 6536 6328 136 82 161 C ANISOU 1919 OE1 GLU B 92 7169 6487 6137 171 122 299 O ANISOU 1920 OE2 GLU B 92 7677 7036 6652 189 112 130 O ANISOU 1921 N ILE B 93 5907 3980 5070 -161 -160 -165 N ANISOU 1922 CA ILE B 93 5759 3676 5061 -197 -174 -172 C ANISOU 1923 C ILE B 93 5617 3566 4925 -185 -183 -259 C ANISOU 1924 O ILE B 93 5813 3835 5015 -162 -204 -357 O ANISOU 1925 CB ILE B 93 5769 3467 5056 -243 -243 -235 C ANISOU 1926 CG1 ILE B 93 5761 3321 5195 -270 -268 -251 C ANISOU 1927 CG2 ILE B 93 5747 3398 4902 -252 -299 -352 C ANISOU 1928 CD1 ILE B 93 5798 3195 5202 -293 -334 -312 C ANISOU 1929 N GLN B 94 5360 3255 4823 -200 -171 -230 N ANISOU 1930 CA GLN B 94 5278 3190 4776 -190 -179 -301 C ANISOU 1931 C GLN B 94 5160 2874 4754 -234 -238 -355 C ANISOU 1932 O GLN B 94 5053 2692 4782 -258 -240 -301 O ANISOU 1933 CB GLN B 94 5263 3367 4876 -149 -97 -201 C ANISOU 1934 CG GLN B 94 5251 3380 4907 -134 -103 -280 C ANISOU 1935 CD GLN B 94 5276 3615 5054 -89 -15 -172 C ANISOU 1936 OE1 GLN B 94 5344 3822 5195 -66 58 -16 O ANISOU 1937 NE2 GLN B 94 5261 3634 5080 -70 -17 -241 N ANISOU 1938 N ASN B 95 5071 2718 4613 -236 -288 -465 N ANISOU 1939 CA ASN B 95 5030 2531 4643 -260 -347 -516 C ANISOU 1940 C ASN B 95 5053 2613 4792 -246 -327 -524 C ANISOU 1941 O ASN B 95 5024 2667 4727 -217 -311 -571 O ANISOU 1942 CB ASN B 95 5015 2416 4521 -265 -408 -601 C ANISOU 1943 CG ASN B 95 4982 2269 4541 -274 -467 -638 C ANISOU 1944 OD1 ASN B 95 4901 2173 4572 -279 -477 -624 O ANISOU 1945 ND2 ASN B 95 5007 2227 4506 -270 -510 -680 N ANISOU 1946 N LYS B 96 5059 2587 4969 -264 -330 -486 N ANISOU 1947 CA LYS B 96 5130 2717 5194 -255 -312 -483 C ANISOU 1948 C LYS B 96 5037 2540 5093 -253 -379 -583 C ANISOU 1949 O LYS B 96 5040 2599 5210 -240 -367 -593 O ANISOU 1950 CB LYS B 96 5268 2842 5571 -280 -305 -420 C ANISOU 1951 CG LYS B 96 5396 3077 5822 -279 -222 -280 C ANISOU 1952 CD LYS B 96 5487 3369 5961 -241 -130 -194 C ANISOU 1953 CE LYS B 96 5596 3611 6232 -231 -38 -16 C ANISOU 1954 NZ LYS B 96 5731 3982 6424 -179 57 81 N ANISOU 1955 N ASN B 97 4623 2010 4562 -259 -444 -642 N ANISOU 1956 CA ASN B 97 4615 1942 4568 -247 -503 -708 C ANISOU 1957 C ASN B 97 4644 1958 4489 -228 -508 -752 C ANISOU 1958 O ASN B 97 4627 1962 4373 -229 -483 -750 O ANISOU 1959 CB ASN B 97 4595 1833 4537 -251 -577 -731 C ANISOU 1960 CG ASN B 97 4577 1821 4664 -268 -588 -720 C ANISOU 1961 OD1 ASN B 97 4546 1801 4652 -286 -549 -670 O ANISOU 1962 ND2 ASN B 97 4585 1827 4796 -260 -645 -769 N ANISOU 1963 N LYS B 98 4957 2242 4854 -209 -543 -795 N ANISOU 1964 CA LYS B 98 5085 2339 4948 -191 -556 -841 C ANISOU 1965 C LYS B 98 5163 2320 4950 -199 -600 -819 C ANISOU 1966 O LYS B 98 5168 2294 4934 -197 -604 -838 O ANISOU 1967 CB LYS B 98 5077 2339 5054 -162 -572 -879 C ANISOU 1968 CG LYS B 98 5100 2481 5156 -142 -519 -903 C ANISOU 1969 CD LYS B 98 5122 2510 5294 -109 -536 -949 C ANISOU 1970 CE LYS B 98 5153 2685 5400 -78 -477 -974 C ANISOU 1971 NZ LYS B 98 5186 2721 5550 -41 -495 -1025 N ANISOU 1972 N SER B 99 5315 2442 5079 -202 -635 -782 N ANISOU 1973 CA SER B 99 5426 2501 5110 -196 -670 -746 C ANISOU 1974 C SER B 99 5579 2649 5162 -221 -645 -724 C ANISOU 1975 O SER B 99 5616 2719 5198 -238 -619 -722 O ANISOU 1976 CB SER B 99 5501 2588 5191 -169 -723 -736 C ANISOU 1977 OG SER B 99 5488 2595 5273 -140 -749 -752 O ANISOU 1978 N SER B 100 5549 2583 5073 -222 -653 -693 N ANISOU 1979 CA SER B 100 5528 2562 4962 -243 -633 -670 C ANISOU 1980 C SER B 100 5356 2396 4728 -237 -647 -646 C ANISOU 1981 O SER B 100 5336 2384 4717 -208 -686 -649 O ANISOU 1982 CB SER B 100 5716 2715 5143 -245 -640 -639 C ANISOU 1983 OG SER B 100 5999 2984 5429 -214 -671 -578 O ANISOU 1984 N GLN B 101 5208 2262 4528 -258 -617 -633 N ANISOU 1985 CA GLN B 101 5103 2158 4388 -252 -627 -621 C ANISOU 1986 C GLN B 101 5129 2176 4313 -251 -623 -580 C ANISOU 1987 O GLN B 101 5050 2092 4219 -266 -608 -564 O ANISOU 1988 CB GLN B 101 5028 2110 4364 -275 -586 -614 C ANISOU 1989 CG GLN B 101 4983 2094 4446 -280 -571 -631 C ANISOU 1990 CD GLN B 101 4974 2070 4535 -264 -622 -674 C ANISOU 1991 OE1 GLN B 101 4949 2027 4473 -241 -671 -701 O ANISOU 1992 NE2 GLN B 101 4979 2103 4673 -270 -612 -686 N ANISOU 1993 N LYS B 102 5158 2214 4294 -231 -639 -573 N ANISOU 1994 CA LYS B 102 5248 2312 4295 -227 -629 -527 C ANISOU 1995 C LYS B 102 5285 2355 4320 -230 -614 -531 C ANISOU 1996 O LYS B 102 5322 2391 4411 -211 -637 -575 O ANISOU 1997 CB LYS B 102 5352 2448 4343 -178 -659 -495 C ANISOU 1998 CG LYS B 102 5352 2445 4384 -169 -668 -457 C ANISOU 1999 CD LYS B 102 5442 2604 4425 -109 -685 -387 C ANISOU 2000 CE LYS B 102 5550 2791 4475 -42 -728 -434 C ANISOU 2001 NZ LYS B 102 5660 3020 4515 37 -739 -354 N ANISOU 2002 N ILE B 103 5312 2391 4303 -253 -579 -491 N ANISOU 2003 CA ILE B 103 5344 2434 4336 -254 -559 -476 C ANISOU 2004 C ILE B 103 5350 2461 4250 -244 -553 -434 C ANISOU 2005 O ILE B 103 5109 2231 3971 -257 -549 -405 O ANISOU 2006 CB ILE B 103 5398 2515 4445 -282 -514 -450 C ANISOU 2007 CG1 ILE B 103 5431 2595 4416 -301 -490 -430 C ANISOU 2008 CG2 ILE B 103 5489 2602 4648 -288 -511 -474 C ANISOU 2009 CD1 ILE B 103 5411 2658 4421 -307 -445 -400 C ANISOU 2010 N ASN B 104 5275 2393 4168 -221 -553 -434 N ANISOU 2011 CA ASN B 104 5359 2508 4174 -206 -542 -393 C ANISOU 2012 C ASN B 104 5399 2549 4259 -206 -518 -381 C ANISOU 2013 O ASN B 104 5135 2257 4103 -211 -516 -403 O ANISOU 2014 CB ASN B 104 5530 2716 4282 -149 -572 -404 C ANISOU 2015 CG ASN B 104 5656 2897 4336 -125 -555 -352 C ANISOU 2016 OD1 ASN B 104 5819 3060 4498 -154 -525 -314 O ANISOU 2017 ND2 ASN B 104 5807 3118 4423 -63 -572 -344 N ANISOU 2018 N LEU B 105 5559 2745 4362 -205 -496 -332 N ANISOU 2019 CA LEU B 105 5863 3060 4710 -199 -470 -300 C ANISOU 2020 C LEU B 105 5965 3176 4783 -150 -484 -318 C ANISOU 2021 O LEU B 105 6221 3467 4948 -125 -498 -319 O ANISOU 2022 CB LEU B 105 6067 3325 4872 -228 -437 -234 C ANISOU 2023 CG LEU B 105 6290 3581 5110 -261 -422 -229 C ANISOU 2024 CD1 LEU B 105 6333 3724 5116 -269 -397 -181 C ANISOU 2025 CD2 LEU B 105 6386 3655 5313 -259 -406 -227 C ANISOU 2026 N SER B 106 6024 3217 4936 -130 -475 -323 N ANISOU 2027 CA SER B 106 6162 3376 5064 -74 -488 -356 C ANISOU 2028 C SER B 106 6167 3375 5169 -73 -454 -303 C ANISOU 2029 O SER B 106 6088 3245 5263 -76 -451 -312 O ANISOU 2030 CB SER B 106 6298 3496 5255 -22 -540 -475 C ANISOU 2031 OG SER B 106 6546 3674 5697 -39 -550 -516 O ANISOU 2032 N ILE B 107 6076 3342 4992 -70 -427 -235 N ANISOU 2033 CA ILE B 107 5982 3266 4978 -61 -393 -167 C ANISOU 2034 C ILE B 107 5967 3275 4945 0 -404 -206 C ANISOU 2035 O ILE B 107 5821 3192 4662 16 -409 -206 O ANISOU 2036 CB ILE B 107 5958 3318 4878 -100 -358 -65 C ANISOU 2037 CG1 ILE B 107 5955 3319 4884 -145 -350 -47 C ANISOU 2038 CG2 ILE B 107 6068 3474 5060 -80 -323 19 C ANISOU 2039 CD1 ILE B 107 5913 3386 4773 -168 -326 20 C ANISOU 2040 N GLN B 108 6018 3285 5160 36 -405 -233 N ANISOU 2041 CA GLN B 108 6238 3533 5391 108 -419 -295 C ANISOU 2042 C GLN B 108 6413 3728 5647 120 -378 -204 C ANISOU 2043 O GLN B 108 6340 3618 5730 95 -350 -124 O ANISOU 2044 CB GLN B 108 6277 3509 5597 156 -469 -444 C ANISOU 2045 CG GLN B 108 6441 3712 5801 248 -494 -547 C ANISOU 2046 CD GLN B 108 6550 3768 6113 298 -558 -726 C ANISOU 2047 OE1 GLN B 108 6575 3724 6254 260 -584 -765 O ANISOU 2048 NE2 GLN B 108 6529 3792 6150 389 -589 -849 N ANISOU 2049 N SER B 109 6594 3985 5729 167 -373 -205 N ANISOU 2050 CA SER B 109 6738 4165 5940 192 -339 -128 C ANISOU 2051 C SER B 109 6798 4199 6137 277 -364 -246 C ANISOU 2052 O SER B 109 6914 4324 6215 325 -409 -387 O ANISOU 2053 CB SER B 109 6730 4270 5759 182 -314 -45 C ANISOU 2054 OG SER B 109 7131 4737 6026 224 -331 -110 O ANISOU 2055 N LYS B 110 6926 4313 6428 305 -339 -195 N ANISOU 2056 CA LYS B 110 7131 4481 6823 388 -367 -321 C ANISOU 2057 C LYS B 110 7079 4528 6611 472 -400 -460 C ANISOU 2058 O LYS B 110 7298 4731 6940 543 -452 -638 O ANISOU 2059 CB LYS B 110 7457 4795 7340 411 -327 -219 C ANISOU 2060 CG LYS B 110 7686 4964 7833 496 -360 -361 C ANISOU 2061 CD LYS B 110 8015 5264 8411 521 -320 -251 C ANISOU 2062 CE LYS B 110 8064 5435 8289 544 -276 -137 C ANISOU 2063 NZ LYS B 110 8162 5508 8653 577 -239 -27 N ANISOU 2064 N ASN B 111 6939 4509 6229 470 -372 -384 N ANISOU 2065 CA ASN B 111 7117 4821 6256 560 -388 -479 C ANISOU 2066 C ASN B 111 7463 5191 6511 584 -438 -604 C ANISOU 2067 O ASN B 111 7788 5665 6680 663 -446 -658 O ANISOU 2068 CB ASN B 111 6821 4658 5769 547 -340 -341 C ANISOU 2069 CG ASN B 111 6622 4453 5446 447 -325 -228 C ANISOU 2070 OD1 ASN B 111 6340 4073 5196 389 -347 -247 O ANISOU 2071 ND2 ASN B 111 6438 4378 5146 428 -291 -117 N ANISOU 2072 N MSE B 112 7758 5363 6907 522 -466 -635 N ANISOU 2073 CA MSE B 112 8020 5641 7111 541 -519 -754 C ANISOU 2074 C MSE B 112 7645 5336 6505 494 -496 -645 C ANISOU 2075 O MSE B 112 7484 5244 6247 531 -531 -717 O ANISOU 2076 CB MSE B 112 8635 6368 7730 676 -575 -957 C ANISOU 2077 CG MSE B 112 9446 7086 8837 721 -619 -1111 C ANISOU 2078 SE MSE B 112 10850 8421 10443 738 -725 -1352 SE ANISOU 2079 CE MSE B 112 10892 8753 10218 914 -786 -1553 C ANISOU 2080 N PHE B 113 7481 5167 6276 418 -442 -475 N ANISOU 2081 CA PHE B 113 7416 5148 6059 364 -424 -377 C ANISOU 2082 C PHE B 113 7009 4617 5708 276 -438 -368 C ANISOU 2083 O PHE B 113 6857 4372 5674 221 -425 -330 O ANISOU 2084 CB PHE B 113 7652 5448 6230 324 -372 -227 C ANISOU 2085 CG PHE B 113 8107 6060 6605 406 -348 -202 C ANISOU 2086 CD1 PHE B 113 8308 6310 6849 503 -355 -293 C ANISOU 2087 CD2 PHE B 113 8245 6305 6655 386 -313 -80 C ANISOU 2088 CE1 PHE B 113 8390 6561 6852 587 -326 -265 C ANISOU 2089 CE2 PHE B 113 8572 6797 6927 463 -281 -33 C ANISOU 2090 CZ PHE B 113 8409 6698 6774 567 -285 -125 C ANISOU 2091 N GLU B 114 6750 4377 5371 274 -463 -399 N ANISOU 2092 CA GLU B 114 6544 4071 5207 199 -477 -395 C ANISOU 2093 C GLU B 114 6222 3777 4787 136 -448 -278 C ANISOU 2094 O GLU B 114 6196 3850 4663 169 -441 -239 O ANISOU 2095 CB GLU B 114 6768 4294 5446 244 -532 -525 C ANISOU 2096 CG GLU B 114 6948 4380 5677 172 -546 -522 C ANISOU 2097 CD GLU B 114 7252 4697 6004 217 -607 -651 C ANISOU 2098 OE1 GLU B 114 7573 5113 6296 313 -645 -758 O ANISOU 2099 OE2 GLU B 114 7166 4547 5959 163 -618 -649 O ANISOU 2100 N PHE B 115 6015 3502 4627 54 -431 -219 N ANISOU 2101 CA PHE B 115 5974 3483 4536 -5 -415 -140 C ANISOU 2102 C PHE B 115 5932 3376 4510 -45 -437 -173 C ANISOU 2103 O PHE B 115 5774 3148 4423 -59 -447 -219 O ANISOU 2104 CB PHE B 115 5885 3411 4474 -52 -387 -68 C ANISOU 2105 CG PHE B 115 5821 3420 4402 -14 -366 -27 C ANISOU 2106 CD1 PHE B 115 5851 3436 4477 43 -364 -66 C ANISOU 2107 CD2 PHE B 115 5762 3445 4314 -31 -349 45 C ANISOU 2108 CE1 PHE B 115 5800 3456 4423 85 -343 -31 C ANISOU 2109 CE2 PHE B 115 5778 3539 4328 6 -327 86 C ANISOU 2110 CZ PHE B 115 5783 3533 4357 67 -323 48 C ANISOU 2111 N AARG B 116 6054 3526 4591 -59 -441 -141 N ANISOU 2112 N BARG B 116 5966 3438 4503 -59 -441 -140 N ANISOU 2113 CA AARG B 116 6121 3537 4678 -91 -461 -168 C ANISOU 2114 CA BARG B 116 5967 3385 4523 -90 -461 -168 C ANISOU 2115 C AARG B 116 6027 3452 4609 -149 -451 -110 C ANISOU 2116 C BARG B 116 5940 3367 4520 -146 -451 -109 C ANISOU 2117 O AARG B 116 6066 3547 4656 -161 -433 -49 O ANISOU 2118 O BARG B 116 5962 3448 4547 -153 -434 -44 O ANISOU 2119 CB AARG B 116 6229 3679 4746 -32 -487 -201 C ANISOU 2120 CB BARG B 116 5963 3415 4478 -24 -488 -210 C ANISOU 2121 CG AARG B 116 6362 3827 4872 38 -514 -296 C ANISOU 2122 CG BARG B 116 5979 3432 4504 37 -513 -307 C ANISOU 2123 CD AARG B 116 6454 3986 4914 105 -549 -340 C ANISOU 2124 CD BARG B 116 6002 3529 4478 119 -552 -375 C ANISOU 2125 NE AARG B 116 6622 4196 5089 184 -589 -464 N ANISOU 2126 NE BARG B 116 5961 3450 4460 98 -580 -401 N ANISOU 2127 CZ AARG B 116 6700 4357 5131 253 -585 -490 C ANISOU 2128 CZ BARG B 116 6032 3496 4587 122 -627 -515 C ANISOU 2129 NH1AARG B 116 6739 4453 5114 251 -538 -382 N ANISOU 2130 NH1BARG B 116 6050 3509 4672 162 -654 -620 N ANISOU 2131 NH2AARG B 116 6822 4517 5289 330 -633 -634 N ANISOU 2132 NH2BARG B 116 6073 3513 4649 104 -649 -528 N ANISOU 2133 N LEU B 117 6010 3382 4629 -183 -467 -138 N ANISOU 2134 CA LEU B 117 6059 3428 4742 -234 -468 -115 C ANISOU 2135 C LEU B 117 6080 3502 4798 -222 -460 -31 C ANISOU 2136 O LEU B 117 6134 3586 4822 -172 -459 4 O ANISOU 2137 CB LEU B 117 6133 3441 4852 -252 -488 -168 C ANISOU 2138 CG LEU B 117 6284 3559 5003 -268 -487 -229 C ANISOU 2139 CD1 LEU B 117 6428 3659 5194 -285 -503 -274 C ANISOU 2140 CD2 LEU B 117 6298 3623 5024 -297 -472 -225 C ANISOU 2141 N LYS B 118 6010 3461 4814 -266 -454 3 N ANISOU 2142 CA LYS B 118 6171 3679 5067 -263 -439 104 C ANISOU 2143 C LYS B 118 6304 3768 5335 -287 -452 124 C ANISOU 2144 O LYS B 118 6055 3459 5165 -335 -478 45 O ANISOU 2145 CB LYS B 118 6177 3737 5148 -302 -434 123 C ANISOU 2146 CG LYS B 118 6272 3903 5382 -304 -412 243 C ANISOU 2147 CD LYS B 118 6287 3979 5488 -342 -414 250 C ANISOU 2148 CE LYS B 118 6324 4094 5702 -347 -387 386 C ANISOU 2149 NZ LYS B 118 6379 4218 5861 -384 -394 384 N ANISOU 2150 N GLU B 119 6591 4107 5659 -244 -430 237 N ANISOU 2151 CA GLU B 119 6808 4291 6025 -254 -436 287 C ANISOU 2152 C GLU B 119 6950 4401 6414 -328 -447 292 C ANISOU 2153 O GLU B 119 6757 4266 6308 -347 -432 348 O ANISOU 2154 CB GLU B 119 7161 4755 6368 -176 -401 441 C ANISOU 2155 CG GLU B 119 7401 4977 6738 -164 -403 512 C ANISOU 2156 CD GLU B 119 7711 5218 6939 -148 -439 401 C ANISOU 2157 OE1 GLU B 119 7737 5212 6799 -146 -460 274 O ANISOU 2158 OE2 GLU B 119 7813 5302 7149 -137 -444 451 O ANISOU 2159 N GLY B 120 7290 4654 6881 -367 -479 215 N ANISOU 2160 CA GLY B 120 7274 4605 7136 -432 -505 179 C ANISOU 2161 C GLY B 120 7330 4663 7160 -475 -542 17 C ANISOU 2162 O GLY B 120 7423 4747 7471 -522 -579 -60 O ANISOU 2163 N SER B 121 7143 4503 6720 -451 -535 -34 N ANISOU 2164 CA SER B 121 6886 4286 6413 -474 -562 -160 C ANISOU 2165 C SER B 121 6711 4075 6269 -486 -597 -298 C ANISOU 2166 O SER B 121 6588 3880 6168 -475 -595 -294 O ANISOU 2167 CB SER B 121 6808 4250 6101 -441 -537 -148 C ANISOU 2168 OG SER B 121 7110 4499 6260 -407 -523 -154 O ANISOU 2169 N GLU B 122 6630 4069 6176 -497 -626 -420 N ANISOU 2170 CA GLU B 122 6635 4084 6207 -494 -658 -562 C ANISOU 2171 C GLU B 122 6669 4183 6012 -458 -636 -593 C ANISOU 2172 O GLU B 122 6378 3973 5603 -444 -619 -558 O ANISOU 2173 CB GLU B 122 6839 4367 6606 -518 -717 -696 C ANISOU 2174 CG GLU B 122 6807 4283 6859 -561 -736 -645 C ANISOU 2175 CD GLU B 122 6825 4173 7054 -572 -725 -574 C ANISOU 2176 OE1 GLU B 122 6851 4140 6980 -547 -713 -588 O ANISOU 2177 OE2 GLU B 122 7018 4333 7487 -600 -724 -482 O ANISOU 2178 N VAL B 123 6509 3993 5815 -440 -633 -644 N ANISOU 2179 CA VAL B 123 6593 4145 5733 -405 -605 -658 C ANISOU 2180 C VAL B 123 6593 4213 5785 -388 -630 -795 C ANISOU 2181 O VAL B 123 6750 4293 6082 -402 -657 -853 O ANISOU 2182 CB VAL B 123 6479 3936 5522 -393 -565 -562 C ANISOU 2183 CG1 VAL B 123 6360 3783 5344 -393 -545 -454 C ANISOU 2184 CG2 VAL B 123 6626 3972 5751 -399 -576 -571 C ANISOU 2185 N PHE B 124 6547 4327 5631 -348 -617 -838 N ANISOU 2186 CA PHE B 124 6651 4549 5761 -312 -638 -977 C ANISOU 2187 C PHE B 124 6854 4761 5871 -280 -587 -930 C ANISOU 2188 O PHE B 124 6850 4820 5751 -258 -537 -826 O ANISOU 2189 CB PHE B 124 6543 4670 5607 -272 -662 -1061 C ANISOU 2190 CG PHE B 124 6470 4785 5554 -215 -695 -1236 C ANISOU 2191 CD1 PHE B 124 6533 4798 5806 -227 -758 -1400 C ANISOU 2192 CD2 PHE B 124 6414 4980 5346 -138 -665 -1237 C ANISOU 2193 CE1 PHE B 124 6605 5061 5904 -163 -796 -1590 C ANISOU 2194 CE2 PHE B 124 6533 5314 5467 -67 -695 -1408 C ANISOU 2195 CZ PHE B 124 6640 5366 5753 -78 -765 -1599 C ANISOU 2196 N LEU B 125 6883 4723 5984 -279 -600 -999 N ANISOU 2197 CA LEU B 125 7129 4987 6178 -250 -556 -967 C ANISOU 2198 C LEU B 125 7513 5546 6579 -194 -569 -1112 C ANISOU 2199 O LEU B 125 8001 5987 7196 -196 -613 -1237 O ANISOU 2200 CB LEU B 125 7009 4665 6129 -283 -556 -919 C ANISOU 2201 CG LEU B 125 6970 4489 6053 -317 -542 -787 C ANISOU 2202 CD1 LEU B 125 6911 4354 6062 -350 -577 -778 C ANISOU 2203 CD2 LEU B 125 6922 4324 6030 -321 -532 -741 C ANISOU 2204 N GLU B 126 7762 6014 6710 -135 -526 -1086 N ANISOU 2205 CA GLU B 126 7924 6410 6854 -57 -530 -1215 C ANISOU 2206 C GLU B 126 7714 6231 6629 -26 -469 -1154 C ANISOU 2207 O GLU B 126 7181 5806 6016 1 -399 -1010 O ANISOU 2208 CB GLU B 126 8249 7015 7057 6 -518 -1213 C ANISOU 2209 CG GLU B 126 8571 7647 7332 110 -523 -1353 C ANISOU 2210 CD GLU B 126 8807 8208 7435 192 -514 -1347 C ANISOU 2211 OE1 GLU B 126 9267 8633 7850 160 -506 -1229 O ANISOU 2212 OE2 GLU B 126 9159 8867 7725 297 -516 -1459 O ANISOU 2213 N GLY B 127 7531 5954 6553 -31 -495 -1256 N ANISOU 2214 CA GLY B 127 7684 6139 6718 -1 -445 -1219 C ANISOU 2215 C GLY B 127 7829 6564 6837 97 -440 -1358 C ANISOU 2216 O GLY B 127 7429 6316 6420 139 -489 -1506 O ANISOU 2217 N LYS B 128 8283 7102 7299 139 -385 -1322 N ANISOU 2218 CA LYS B 128 9007 8126 7990 249 -371 -1449 C ANISOU 2219 C LYS B 128 9349 8425 8450 264 -459 -1703 C ANISOU 2220 O LYS B 128 9903 9210 8975 343 -499 -1881 O ANISOU 2221 CB LYS B 128 9108 8331 8098 291 -286 -1337 C ANISOU 2222 CG LYS B 128 9411 8763 8333 303 -190 -1094 C ANISOU 2223 CD LYS B 128 9446 8919 8425 346 -103 -982 C ANISOU 2224 CE LYS B 128 9545 9176 8511 367 -2 -729 C ANISOU 2225 NZ LYS B 128 9419 8778 8440 262 -10 -591 N ANISOU 2226 N ASN B 129 9587 8381 8838 197 -491 -1722 N ANISOU 2227 CA ASN B 129 9933 8661 9353 209 -569 -1943 C ANISOU 2228 C ASN B 129 9840 8378 9380 138 -650 -2009 C ANISOU 2229 O ASN B 129 9489 8070 9169 165 -723 -2223 O ANISOU 2230 CB ASN B 129 10341 8896 9891 189 -559 -1926 C ANISOU 2231 CG ASN B 129 10729 9480 10206 261 -481 -1876 C ANISOU 2232 OD1 ASN B 129 11124 10152 10454 331 -427 -1835 O ANISOU 2233 ND2 ASN B 129 11061 9687 10651 250 -473 -1864 N ANISOU 2234 N ILE B 130 9597 7937 9106 51 -637 -1831 N ANISOU 2235 CA ILE B 130 9103 7273 8739 -15 -701 -1859 C ANISOU 2236 C ILE B 130 9003 7214 8494 -44 -685 -1743 C ANISOU 2237 O ILE B 130 8687 6894 8030 -57 -621 -1565 O ANISOU 2238 CB ILE B 130 9086 6963 8873 -86 -710 -1765 C ANISOU 2239 CG1 ILE B 130 8824 6664 8767 -53 -724 -1870 C ANISOU 2240 CG2 ILE B 130 9118 6841 9060 -150 -764 -1761 C ANISOU 2241 CD1 ILE B 130 8756 6343 8850 -107 -732 -1765 C ANISOU 2242 N ILE B 131 8772 7018 8344 -54 -748 -1854 N ANISOU 2243 CA ILE B 131 8523 6816 7993 -79 -747 -1774 C ANISOU 2244 C ILE B 131 8234 6339 7909 -153 -808 -1797 C ANISOU 2245 O ILE B 131 8294 6379 8195 -150 -876 -1971 O ANISOU 2246 CB ILE B 131 8751 7372 8107 6 -763 -1900 C ANISOU 2247 CG1 ILE B 131 9004 7852 8191 95 -694 -1870 C ANISOU 2248 CG2 ILE B 131 8638 7315 7895 -15 -762 -1808 C ANISOU 2249 CD1 ILE B 131 9143 8369 8204 204 -704 -1983 C ANISOU 2250 N TYR B 132 8067 6046 7691 -213 -784 -1624 N ANISOU 2251 CA TYR B 132 7811 5636 7643 -277 -830 -1616 C ANISOU 2252 C TYR B 132 7395 5151 7121 -322 -796 -1428 C ANISOU 2253 O TYR B 132 6820 4593 6335 -312 -736 -1296 O ANISOU 2254 CB TYR B 132 8096 5707 8124 -311 -835 -1580 C ANISOU 2255 CG TYR B 132 8325 5809 8220 -326 -772 -1387 C ANISOU 2256 CD1 TYR B 132 8433 5986 8140 -287 -724 -1357 C ANISOU 2257 CD2 TYR B 132 8351 5669 8320 -372 -761 -1235 C ANISOU 2258 CE1 TYR B 132 8457 5901 8075 -301 -679 -1205 C ANISOU 2259 CE2 TYR B 132 8503 5735 8350 -373 -716 -1085 C ANISOU 2260 CZ TYR B 132 8469 5756 8148 -341 -681 -1082 C ANISOU 2261 OH TYR B 132 8792 6001 8383 -342 -649 -959 O ANISOU 2262 N SER B 133 6923 4604 6832 -371 -834 -1423 N ANISOU 2263 CA SER B 133 6948 4565 6798 -411 -805 -1254 C ANISOU 2264 C SER B 133 7253 4677 7153 -440 -771 -1098 C ANISOU 2265 O SER B 133 7483 4805 7612 -457 -796 -1122 O ANISOU 2266 CB SER B 133 6724 4382 6759 -442 -858 -1313 C ANISOU 2267 OG SER B 133 6480 4098 6451 -473 -825 -1146 O ANISOU 2268 N ASP B 134 7493 4880 7193 -436 -717 -946 N ANISOU 2269 CA ASP B 134 7695 4943 7413 -445 -690 -813 C ANISOU 2270 C ASP B 134 7926 5146 7623 -463 -669 -666 C ANISOU 2271 O ASP B 134 8339 5634 7950 -467 -663 -654 O ANISOU 2272 CB ASP B 134 7834 5072 7373 -414 -656 -785 C ANISOU 2273 CG ASP B 134 7738 4866 7290 -409 -640 -677 C ANISOU 2274 OD1 ASP B 134 7546 4615 7233 -423 -647 -600 O ANISOU 2275 OD2 ASP B 134 7672 4791 7117 -387 -622 -668 O ANISOU 2276 N LYS B 135 7936 5068 7712 -463 -654 -549 N ANISOU 2277 CA LYS B 135 8326 5456 8089 -463 -627 -396 C ANISOU 2278 C LYS B 135 7971 5095 7512 -422 -594 -313 C ANISOU 2279 O LYS B 135 7715 4808 7190 -402 -595 -348 O ANISOU 2280 CB LYS B 135 8727 5803 8746 -473 -629 -301 C ANISOU 2281 CG LYS B 135 9027 6136 9057 -460 -592 -118 C ANISOU 2282 CD LYS B 135 9088 6167 9389 -458 -581 16 C ANISOU 2283 CE LYS B 135 9106 6141 9761 -512 -618 -51 C ANISOU 2284 NZ LYS B 135 9243 6247 10208 -508 -598 113 N ANISOU 2285 N ILE B 136 7988 5154 7434 -407 -569 -216 N ANISOU 2286 CA ILE B 136 7770 4948 7037 -360 -548 -159 C ANISOU 2287 C ILE B 136 7745 4921 7079 -324 -540 -48 C ANISOU 2288 O ILE B 136 7570 4786 7010 -320 -523 64 O ANISOU 2289 CB ILE B 136 7577 4815 6719 -346 -527 -119 C ANISOU 2290 CG1 ILE B 136 7458 4718 6542 -372 -531 -206 C ANISOU 2291 CG2 ILE B 136 7548 4807 6541 -287 -516 -84 C ANISOU 2292 CD1 ILE B 136 7521 4758 6524 -364 -534 -285 C ANISOU 2293 N LYS B 137 7665 4814 6950 -294 -551 -71 N ANISOU 2294 CA LYS B 137 7785 4959 7123 -246 -547 33 C ANISOU 2295 C LYS B 137 7798 5053 6947 -173 -545 60 C ANISOU 2296 O LYS B 137 7482 4717 6526 -161 -566 -34 O ANISOU 2297 CB LYS B 137 7744 4848 7190 -256 -569 -19 C ANISOU 2298 CG LYS B 137 7785 4821 7441 -316 -582 -81 C ANISOU 2299 CD LYS B 137 7963 4937 7731 -317 -604 -147 C ANISOU 2300 CE LYS B 137 8205 5127 8193 -365 -626 -244 C ANISOU 2301 NZ LYS B 137 8276 5189 8512 -386 -621 -145 N ANISOU 2302 N GLU B 138 8147 5507 7275 -121 -520 189 N ANISOU 2303 CA GLU B 138 8478 5957 7432 -32 -522 207 C ANISOU 2304 C GLU B 138 8023 5485 6837 -39 -533 87 C ANISOU 2305 O GLU B 138 8426 5939 7124 18 -558 18 O ANISOU 2306 CB GLU B 138 8901 6410 7828 22 -552 188 C ANISOU 2307 CG GLU B 138 9536 7072 8622 40 -537 330 C ANISOU 2308 CD GLU B 138 10070 7656 9132 102 -568 325 C ANISOU 2309 OE1 GLU B 138 10536 8135 9464 129 -608 194 O ANISOU 2310 OE2 GLU B 138 10813 8430 10017 126 -552 456 O ANISOU 2311 N GLY B 139 7681 5082 6532 -106 -519 61 N ANISOU 2312 CA GLY B 139 7525 4911 6277 -115 -521 -22 C ANISOU 2313 C GLY B 139 7182 4478 5929 -151 -543 -142 C ANISOU 2314 O GLY B 139 7334 4618 6031 -152 -543 -199 O ANISOU 2315 N OCS B 140 6895 4136 5716 -176 -558 -169 N ANISOU 2316 CA OCS B 140 6675 3854 5507 -204 -571 -264 C ANISOU 2317 CB OCS B 140 7102 4280 5937 -166 -601 -302 C ANISOU 2318 SG OCS B 140 7631 4889 6373 -84 -629 -331 S ANISOU 2319 C OCS B 140 6257 3391 5178 -262 -564 -292 C ANISOU 2320 O OCS B 140 5850 2982 4856 -282 -562 -253 O ANISOU 2321 OD1 OCS B 140 7943 5225 6705 -47 -666 -363 O ANISOU 2322 OD2 OCS B 140 7649 5002 6331 -37 -612 -233 O ANISOU 2323 OD3 OCS B 140 7419 4649 6155 -99 -626 -394 O ANISOU 2324 N ILE B 141 5949 3063 4870 -282 -561 -361 N ANISOU 2325 CA ILE B 141 5789 2900 4773 -318 -557 -411 C ANISOU 2326 C ILE B 141 5529 2610 4563 -310 -569 -455 C ANISOU 2327 O ILE B 141 5251 2329 4264 -295 -569 -471 O ANISOU 2328 CB ILE B 141 5997 3159 4938 -331 -533 -433 C ANISOU 2329 CG1 ILE B 141 6009 3207 4903 -334 -522 -387 C ANISOU 2330 CG2 ILE B 141 6006 3213 4993 -346 -530 -498 C ANISOU 2331 CD1 ILE B 141 6136 3404 4989 -337 -497 -388 C ANISOU 2332 N GLU B 142 5382 2441 4511 -320 -582 -478 N ANISOU 2333 CA GLU B 142 5239 2276 4425 -310 -592 -520 C ANISOU 2334 C GLU B 142 5093 2176 4278 -320 -573 -591 C ANISOU 2335 O GLU B 142 5048 2177 4247 -333 -567 -634 O ANISOU 2336 CB GLU B 142 5303 2301 4619 -308 -612 -515 C ANISOU 2337 CG GLU B 142 5330 2309 4711 -294 -622 -563 C ANISOU 2338 CD GLU B 142 5459 2394 5002 -288 -640 -559 C ANISOU 2339 OE1 GLU B 142 5462 2375 5097 -297 -644 -504 O ANISOU 2340 OE2 GLU B 142 5550 2475 5156 -274 -648 -608 O ANISOU 2341 N VAL B 143 4967 2060 4145 -309 -563 -600 N ANISOU 2342 CA VAL B 143 4922 2088 4112 -308 -532 -638 C ANISOU 2343 C VAL B 143 4929 2084 4206 -295 -543 -688 C ANISOU 2344 O VAL B 143 4867 1990 4180 -287 -554 -675 O ANISOU 2345 CB VAL B 143 4869 2065 4044 -305 -504 -592 C ANISOU 2346 CG1 VAL B 143 4869 2178 4068 -295 -457 -593 C ANISOU 2347 CG2 VAL B 143 4854 2044 3961 -311 -498 -543 C ANISOU 2348 N PRO B 144 5017 2205 4344 -290 -547 -758 N ANISOU 2349 CA PRO B 144 5081 2259 4506 -272 -558 -813 C ANISOU 2350 C PRO B 144 5147 2381 4588 -256 -530 -808 C ANISOU 2351 O PRO B 144 5147 2452 4544 -257 -492 -768 O ANISOU 2352 CB PRO B 144 5116 2359 4589 -261 -563 -916 C ANISOU 2353 CG PRO B 144 5083 2325 4516 -282 -575 -906 C ANISOU 2354 CD PRO B 144 5039 2291 4349 -294 -547 -807 C ANISOU 2355 N GLY B 145 5231 2435 4762 -241 -546 -838 N ANISOU 2356 CA GLY B 145 5309 2571 4891 -227 -521 -835 C ANISOU 2357 C GLY B 145 5418 2832 4988 -202 -468 -866 C ANISOU 2358 O GLY B 145 5440 2915 4990 -183 -469 -942 O ANISOU 2359 N GLU B 146 5465 2959 5061 -198 -424 -805 N ANISOU 2360 CA GLU B 146 5577 3258 5169 -161 -359 -796 C ANISOU 2361 C GLU B 146 5605 3384 5079 -146 -342 -804 C ANISOU 2362 O GLU B 146 5813 3787 5256 -96 -296 -818 O ANISOU 2363 CB GLU B 146 5682 3440 5332 -117 -356 -888 C ANISOU 2364 CG GLU B 146 5713 3393 5487 -125 -374 -883 C ANISOU 2365 CD GLU B 146 5797 3558 5642 -77 -366 -970 C ANISOU 2366 OE1 GLU B 146 5950 3840 5748 -30 -347 -1049 O ANISOU 2367 OE2 GLU B 146 5760 3466 5712 -78 -384 -969 O ANISOU 2368 N PHE B 147 5589 3260 4998 -181 -378 -795 N ANISOU 2369 CA PHE B 147 5537 3300 4845 -170 -369 -802 C ANISOU 2370 C PHE B 147 5744 3680 5027 -141 -297 -697 C ANISOU 2371 O PHE B 147 5624 3527 4982 -159 -266 -593 O ANISOU 2372 CB PHE B 147 5392 3018 4652 -214 -404 -765 C ANISOU 2373 CG PHE B 147 5302 3018 4470 -206 -402 -773 C ANISOU 2374 CD1 PHE B 147 5311 3080 4473 -190 -437 -891 C ANISOU 2375 CD2 PHE B 147 5215 2986 4329 -207 -364 -668 C ANISOU 2376 CE1 PHE B 147 5308 3178 4398 -181 -444 -909 C ANISOU 2377 CE2 PHE B 147 5245 3119 4275 -193 -363 -671 C ANISOU 2378 CZ PHE B 147 5292 3222 4303 -180 -405 -795 C ANISOU 2379 N GLU B 148 5999 4135 5200 -90 -271 -725 N ANISOU 2380 CA GLU B 148 6097 4436 5273 -49 -195 -599 C ANISOU 2381 C GLU B 148 6188 4701 5235 -4 -203 -650 C ANISOU 2382 O GLU B 148 6602 5331 5598 66 -196 -740 O ANISOU 2383 CB GLU B 148 6240 4749 5489 2 -130 -554 C ANISOU 2384 CG GLU B 148 6440 5167 5707 46 -37 -375 C ANISOU 2385 CD GLU B 148 6685 5609 6049 102 40 -297 C ANISOU 2386 OE1 GLU B 148 6677 5568 6082 108 19 -400 O ANISOU 2387 OE2 GLU B 148 6817 5935 6232 143 127 -119 O ANISOU 2388 N GLY B 149 6100 4521 5100 -42 -226 -609 N ANISOU 2389 CA GLY B 149 6110 4683 5001 -7 -243 -655 C ANISOU 2390 C GLY B 149 6091 4589 4953 -43 -237 -540 C ANISOU 2391 O GLY B 149 5951 4380 4877 -65 -192 -396 O ANISOU 2392 N LYS B 150 6070 4577 4866 -50 -288 -619 N ANISOU 2393 CA LYS B 150 6222 4682 4981 -75 -288 -529 C ANISOU 2394 C LYS B 150 6068 4313 4848 -141 -358 -608 C ANISOU 2395 O LYS B 150 6075 4279 4891 -152 -412 -746 O ANISOU 2396 CB LYS B 150 6482 5226 5142 -6 -276 -530 C ANISOU 2397 CG LYS B 150 6771 5793 5402 79 -197 -427 C ANISOU 2398 CD LYS B 150 6930 6288 5444 171 -194 -450 C ANISOU 2399 CE LYS B 150 7176 6636 5647 201 -276 -696 C ANISOU 2400 NZ LYS B 150 7210 6697 5722 228 -273 -797 N ANISOU 2401 N ILE B 151 6051 4170 4831 -178 -353 -512 N ANISOU 2402 CA ILE B 151 5984 3934 4780 -229 -405 -550 C ANISOU 2403 C ILE B 151 6135 4157 4873 -223 -401 -493 C ANISOU 2404 O ILE B 151 6260 4326 4980 -205 -354 -375 O ANISOU 2405 CB ILE B 151 5804 3542 4654 -268 -407 -504 C ANISOU 2406 CG1 ILE B 151 5770 3466 4680 -265 -408 -551 C ANISOU 2407 CG2 ILE B 151 5807 3412 4667 -304 -451 -521 C ANISOU 2408 CD1 ILE B 151 5751 3276 4714 -291 -419 -521 C ANISOU 2409 N TYR B 152 6137 4183 4878 -237 -451 -577 N ANISOU 2410 CA TYR B 152 6323 4451 5020 -231 -456 -537 C ANISOU 2411 C TYR B 152 6249 4206 4989 -283 -482 -515 C ANISOU 2412 O TYR B 152 6201 4068 5024 -316 -524 -587 O ANISOU 2413 CB TYR B 152 6421 4757 5108 -198 -498 -658 C ANISOU 2414 CG TYR B 152 6612 5187 5235 -124 -473 -687 C ANISOU 2415 CD1 TYR B 152 6667 5235 5313 -108 -460 -737 C ANISOU 2416 CD2 TYR B 152 6873 5707 5409 -60 -458 -656 C ANISOU 2417 CE1 TYR B 152 6944 5764 5529 -28 -429 -755 C ANISOU 2418 CE2 TYR B 152 6972 6072 5438 25 -428 -666 C ANISOU 2419 CZ TYR B 152 6971 6067 5461 42 -411 -716 C ANISOU 2420 OH TYR B 152 7258 6647 5677 138 -373 -716 O ANISOU 2421 N VAL B 153 6383 4314 5084 -282 -454 -406 N ANISOU 2422 CA VAL B 153 6488 4294 5214 -313 -468 -371 C ANISOU 2423 C VAL B 153 6627 4532 5316 -299 -459 -313 C ANISOU 2424 O VAL B 153 6622 4573 5269 -269 -419 -228 O ANISOU 2425 CB VAL B 153 6537 4189 5263 -317 -446 -310 C ANISOU 2426 CG1 VAL B 153 6565 4136 5297 -330 -456 -271 C ANISOU 2427 CG2 VAL B 153 6578 4148 5343 -327 -456 -361 C ANISOU 2428 N ASN B 154 6477 4409 5211 -322 -497 -353 N ANISOU 2429 CA ASN B 154 6432 4465 5147 -311 -497 -308 C ANISOU 2430 C ASN B 154 6188 4106 4887 -312 -466 -206 C ANISOU 2431 O ASN B 154 6247 4030 4969 -329 -466 -199 O ANISOU 2432 CB ASN B 154 6690 4793 5503 -338 -554 -398 C ANISOU 2433 CG ASN B 154 6869 5113 5677 -325 -565 -372 C ANISOU 2434 OD1 ASN B 154 7109 5308 5901 -326 -538 -274 O ANISOU 2435 ND2 ASN B 154 6947 5379 5772 -305 -609 -469 N ANISOU 2436 N PHE B 155 6063 4053 4722 -284 -442 -131 N ANISOU 2437 CA PHE B 155 6037 3935 4688 -273 -415 -55 C ANISOU 2438 C PHE B 155 6193 4061 4887 -297 -434 -54 C ANISOU 2439 O PHE B 155 5975 3778 4657 -280 -415 -6 O ANISOU 2440 CB PHE B 155 6024 4003 4653 -233 -383 27 C ANISOU 2441 CG PHE B 155 5919 3912 4549 -202 -346 76 C ANISOU 2442 CD1 PHE B 155 5875 3733 4539 -204 -332 70 C ANISOU 2443 CD2 PHE B 155 5917 4070 4540 -164 -322 147 C ANISOU 2444 CE1 PHE B 155 5896 3767 4614 -180 -294 130 C ANISOU 2445 CE2 PHE B 155 5966 4142 4629 -131 -276 228 C ANISOU 2446 CZ PHE B 155 5968 3996 4694 -143 -261 221 C ANISOU 2447 N ASN B 156 6258 4190 5025 -330 -472 -106 N ANISOU 2448 CA ASN B 156 6467 4380 5323 -355 -481 -78 C ANISOU 2449 C ASN B 156 6453 4243 5353 -370 -481 -78 C ANISOU 2450 O ASN B 156 6290 4068 5281 -384 -479 -28 O ANISOU 2451 CB ASN B 156 6493 4514 5475 -389 -526 -132 C ANISOU 2452 CG ASN B 156 6470 4490 5535 -416 -571 -250 C ANISOU 2453 OD1 ASN B 156 6500 4447 5510 -408 -562 -278 O ANISOU 2454 ND2 ASN B 156 6454 4565 5672 -445 -623 -330 N ANISOU 2455 N SER B 157 6593 4314 5444 -365 -481 -122 N ANISOU 2456 CA SER B 157 6707 4326 5591 -371 -482 -121 C ANISOU 2457 C SER B 157 6576 4136 5359 -326 -454 -75 C ANISOU 2458 O SER B 157 6548 4041 5327 -316 -457 -81 O ANISOU 2459 CB SER B 157 6856 4446 5774 -389 -506 -209 C ANISOU 2460 OG SER B 157 7137 4792 6172 -421 -544 -281 O ANISOU 2461 N LEU B 158 6491 4087 5208 -295 -433 -42 N ANISOU 2462 CA LEU B 158 6536 4092 5188 -245 -415 -25 C ANISOU 2463 C LEU B 158 6239 3855 4880 -213 -398 37 C ANISOU 2464 O LEU B 158 6323 4009 4991 -225 -391 73 O ANISOU 2465 CB LEU B 158 6858 4406 5489 -228 -402 -39 C ANISOU 2466 CG LEU B 158 7286 4803 5936 -249 -407 -80 C ANISOU 2467 CD1 LEU B 158 7524 5031 6197 -223 -384 -60 C ANISOU 2468 CD2 LEU B 158 7692 5131 6350 -255 -426 -125 C ANISOU 2469 N ILE B 159 6019 3630 4621 -164 -394 49 N ANISOU 2470 CA ILE B 159 5874 3576 4460 -119 -370 117 C ANISOU 2471 C ILE B 159 5685 3409 4189 -34 -369 88 C ANISOU 2472 O ILE B 159 5777 3449 4257 -17 -392 26 O ANISOU 2473 CB ILE B 159 5872 3621 4543 -146 -363 198 C ANISOU 2474 CG1 ILE B 159 5905 3777 4589 -104 -328 299 C ANISOU 2475 CG2 ILE B 159 5912 3625 4584 -133 -374 197 C ANISOU 2476 CD1 ILE B 159 5907 3835 4732 -131 -312 408 C ANISOU 2477 N ASN B 160 5670 3486 4140 24 -347 119 N ANISOU 2478 CA ASN B 160 5812 3696 4206 126 -349 76 C ANISOU 2479 C ASN B 160 6016 4029 4384 168 -327 173 C ANISOU 2480 O ASN B 160 5927 4028 4335 161 -290 282 O ANISOU 2481 CB ASN B 160 5672 3607 4054 180 -334 54 C ANISOU 2482 CG ASN B 160 5651 3679 3964 299 -346 -24 C ANISOU 2483 OD1 ASN B 160 5633 3811 3896 373 -317 24 O ANISOU 2484 ND2 ASN B 160 5586 3546 3904 325 -390 -149 N ANISOU 2485 N GLU B 161 6582 4622 4899 217 -347 142 N ANISOU 2486 CA GLU B 161 7115 5293 5419 266 -322 258 C ANISOU 2487 C GLU B 161 7629 6012 5882 362 -276 348 C ANISOU 2488 O GLU B 161 7757 6231 6088 348 -230 509 O ANISOU 2489 CB GLU B 161 7450 5643 5690 321 -359 192 C ANISOU 2490 CG GLU B 161 7782 6143 6009 387 -330 332 C ANISOU 2491 CD GLU B 161 8106 6500 6273 444 -371 274 C ANISOU 2492 OE1 GLU B 161 7973 6243 6125 422 -425 114 O ANISOU 2493 OE2 GLU B 161 8351 6911 6501 516 -346 400 O ANISOU 2494 N GLU B 162 8317 6787 6467 463 -288 246 N ANISOU 2495 CA GLU B 162 8851 7550 6939 574 -243 321 C ANISOU 2496 C GLU B 162 8702 7404 6876 518 -195 426 C ANISOU 2497 O GLU B 162 9051 7905 7269 539 -139 593 O ANISOU 2498 CB GLU B 162 9311 8106 7285 703 -277 151 C ANISOU 2499 CG GLU B 162 9883 8722 7780 773 -332 39 C ANISOU 2500 CD GLU B 162 10217 9259 8052 845 -303 182 C ANISOU 2501 OE1 GLU B 162 10888 10039 8763 838 -233 388 O ANISOU 2502 OE2 GLU B 162 10284 9380 8055 906 -350 98 O ANISOU 2503 N SER B 163 8423 6975 6638 453 -216 339 N ANISOU 2504 CA SER B 163 8286 6853 6583 405 -181 422 C ANISOU 2505 C SER B 163 8146 6651 6582 285 -170 539 C ANISOU 2506 O SER B 163 8318 6896 6850 257 -135 648 O ANISOU 2507 CB SER B 163 8123 6568 6432 379 -206 310 C ANISOU 2508 OG SER B 163 7823 6080 6174 286 -246 244 O ANISOU 2509 N ASN B 164 8106 6478 6571 218 -204 501 N ANISOU 2510 CA ASN B 164 7862 6163 6480 110 -207 572 C ANISOU 2511 C ASN B 164 7522 5746 6205 30 -225 526 C ANISOU 2512 O ASN B 164 7516 5742 6348 -44 -226 581 O ANISOU 2513 CB ASN B 164 7951 6396 6691 124 -158 752 C ANISOU 2514 CG ASN B 164 7992 6357 6946 15 -170 808 C ANISOU 2515 OD1 ASN B 164 8047 6307 7027 -20 -201 765 O ANISOU 2516 ND2 ASN B 164 8016 6438 7149 -34 -151 895 N ANISOU 2517 N VAL B 165 7270 5437 5860 51 -243 422 N ANISOU 2518 CA VAL B 165 6936 5060 5567 -2 -256 391 C ANISOU 2519 C VAL B 165 6648 4643 5288 -67 -295 308 C ANISOU 2520 O VAL B 165 6550 4463 5126 -46 -310 236 O ANISOU 2521 CB VAL B 165 7153 5308 5717 66 -243 355 C ANISOU 2522 CG1 VAL B 165 6983 5104 5588 21 -255 338 C ANISOU 2523 CG2 VAL B 165 7268 5578 5821 140 -201 433 C ANISOU 2524 N VAL B 166 6460 4457 5189 -141 -313 312 N ANISOU 2525 CA VAL B 166 6452 4372 5188 -192 -346 236 C ANISOU 2526 C VAL B 166 6300 4213 4973 -166 -341 207 C ANISOU 2527 O VAL B 166 6409 4392 5084 -138 -324 248 O ANISOU 2528 CB VAL B 166 6531 4492 5394 -262 -374 229 C ANISOU 2529 CG1 VAL B 166 6601 4524 5455 -297 -408 138 C ANISOU 2530 CG2 VAL B 166 6548 4506 5533 -287 -373 278 C ANISOU 2531 N LEU B 167 6355 4191 4999 -173 -352 152 N ANISOU 2532 CA LEU B 167 6456 4279 5084 -145 -340 149 C ANISOU 2533 C LEU B 167 6636 4564 5286 -158 -339 184 C ANISOU 2534 O LEU B 167 6923 4875 5581 -120 -317 224 O ANISOU 2535 CB LEU B 167 6371 4102 4997 -156 -349 98 C ANISOU 2536 CG LEU B 167 6334 4044 4995 -131 -330 113 C ANISOU 2537 CD1 LEU B 167 6314 3973 5009 -74 -319 104 C ANISOU 2538 CD2 LEU B 167 6327 3980 5010 -153 -335 80 C ANISOU 2539 N ASP B 168 6851 4853 5527 -202 -365 166 N ANISOU 2540 CA ASP B 168 6977 5117 5664 -201 -374 184 C ANISOU 2541 C ASP B 168 6983 5223 5725 -209 -384 213 C ANISOU 2542 O ASP B 168 7070 5448 5832 -208 -403 216 O ANISOU 2543 CB ASP B 168 6997 5200 5686 -228 -406 117 C ANISOU 2544 CG ASP B 168 6815 5000 5575 -281 -448 41 C ANISOU 2545 OD1 ASP B 168 6737 4858 5550 -298 -443 66 O ANISOU 2546 OD2 ASP B 168 6841 5096 5622 -298 -484 -38 O ANISOU 2547 N SER B 169 7242 5436 6013 -210 -370 241 N ANISOU 2548 CA SER B 169 7466 5761 6317 -218 -372 286 C ANISOU 2549 C SER B 169 7384 5749 6204 -164 -343 348 C ANISOU 2550 O SER B 169 7253 5555 6017 -112 -309 372 O ANISOU 2551 CB SER B 169 7668 5924 6570 -225 -355 325 C ANISOU 2552 OG SER B 169 8006 6374 7020 -235 -349 386 O ANISOU 2553 N ASN B 170 7396 5902 6270 -173 -364 362 N ANISOU 2554 CA ASN B 170 7426 6020 6290 -122 -340 428 C ANISOU 2555 C ASN B 170 7060 5668 5965 -99 -308 486 C ANISOU 2556 O ASN B 170 7110 5734 6094 -136 -313 494 O ANISOU 2557 CB ASN B 170 7720 6489 6627 -131 -379 421 C ANISOU 2558 CG ASN B 170 8043 6850 6891 -129 -403 375 C ANISOU 2559 OD1 ASN B 170 8400 7087 7189 -127 -387 356 O ANISOU 2560 ND2 ASN B 170 8267 7264 7132 -120 -441 357 N ANISOU 2561 N MSE B 171 6840 5457 5711 -32 -271 533 N ANISOU 2562 CA MSE B 171 7023 5681 5915 12 -233 584 C ANISOU 2563 C MSE B 171 7369 6183 6373 -15 -242 637 C ANISOU 2564 O MSE B 171 7853 6713 6914 -13 -217 685 O ANISOU 2565 CB MSE B 171 7094 5733 5952 95 -201 600 C ANISOU 2566 CG MSE B 171 7210 5697 6012 125 -196 540 C ANISOU 2567 SE MSE B 171 7600 6020 6336 154 -184 485 SE ANISOU 2568 CE MSE B 171 7667 5962 6375 66 -224 427 C ANISOU 2569 N LEU B 172 7686 6601 6732 -34 -276 635 N ANISOU 2570 CA LEU B 172 7986 7063 7165 -63 -297 667 C ANISOU 2571 C LEU B 172 8162 7247 7476 -143 -331 637 C ANISOU 2572 O LEU B 172 8018 7219 7495 -171 -341 673 O ANISOU 2573 CB LEU B 172 7904 7107 7085 -57 -340 650 C ANISOU 2574 CG LEU B 172 7972 7211 7091 23 -305 715 C ANISOU 2575 CD1 LEU B 172 7947 7365 7083 35 -347 722 C ANISOU 2576 CD2 LEU B 172 8047 7327 7217 67 -258 786 C ANISOU 2577 N SER B 173 7065 5696 7048 1401 -223 370 N ANISOU 2578 CA SER B 173 7385 5863 7373 1511 -57 473 C ANISOU 2579 C SER B 173 7310 5786 7204 1572 -75 539 C ANISOU 2580 O SER B 173 7261 5490 7065 1604 82 558 O ANISOU 2581 CB SER B 173 7770 6390 7966 1637 9 608 C ANISOU 2582 OG SER B 173 8278 6857 8552 1580 53 545 O ANISOU 2583 N ASN B 174 7214 5952 7121 1581 -249 563 N ANISOU 2584 CA ASN B 174 7051 5800 6859 1650 -267 637 C ANISOU 2585 C ASN B 174 6463 5328 6166 1547 -445 543 C ANISOU 2586 O ASN B 174 5885 5046 5646 1560 -587 574 O ANISOU 2587 CB ASN B 174 7204 6203 7136 1830 -267 830 C ANISOU 2588 CG ASN B 174 7594 6479 7641 1965 -66 956 C ANISOU 2589 OD1 ASN B 174 7572 6481 7751 1943 -32 933 O ANISOU 2590 ND2 ASN B 174 8151 6913 8153 2117 81 1102 N ANISOU 2591 N ILE B 175 6686 5329 6233 1444 -427 427 N ANISOU 2592 CA ILE B 175 6379 5087 5819 1354 -565 343 C ANISOU 2593 C ILE B 175 6359 5000 5679 1414 -542 405 C ANISOU 2594 O ILE B 175 6527 4926 5775 1432 -398 410 O ANISOU 2595 CB ILE B 175 6567 5124 5925 1220 -566 195 C ANISOU 2596 CG1 ILE B 175 6638 5240 6096 1176 -569 147 C ANISOU 2597 CG2 ILE B 175 6427 5031 5678 1145 -681 126 C ANISOU 2598 CD1 ILE B 175 6427 5278 5996 1163 -688 155 C ANISOU 2599 N VAL B 176 6375 5225 5664 1430 -673 437 N ANISOU 2600 CA VAL B 176 6377 5189 5541 1499 -659 509 C ANISOU 2601 C VAL B 176 6457 5214 5479 1385 -742 397 C ANISOU 2602 O VAL B 176 6319 4955 5217 1415 -699 424 O ANISOU 2603 CB VAL B 176 6620 5736 5836 1630 -732 657 C ANISOU 2604 CG1 VAL B 176 6810 5976 6170 1779 -623 802 C ANISOU 2605 CG2 VAL B 176 6309 5751 5574 1544 -919 589 C ANISOU 2606 N SER B 177 6035 4869 5076 1264 -843 280 N ANISOU 2607 CA SER B 177 5750 4523 4662 1171 -901 187 C ANISOU 2608 C SER B 177 5408 4165 4349 1055 -937 67 C ANISOU 2609 O SER B 177 4950 3811 4005 1038 -959 54 O ANISOU 2610 CB SER B 177 5827 4793 4675 1184 -1007 220 C ANISOU 2611 OG SER B 177 5753 4636 4473 1096 -1043 133 O ANISOU 2612 N TRP B 178 5469 4097 4307 989 -930 -8 N ANISOU 2613 CA TRP B 178 5417 4025 4261 906 -949 -98 C ANISOU 2614 C TRP B 178 5654 4203 4377 859 -971 -144 C ANISOU 2615 O TRP B 178 5022 3487 3663 881 -943 -127 O ANISOU 2616 CB TRP B 178 5141 3644 4016 897 -871 -130 C ANISOU 2617 CG TRP B 178 5486 3863 4277 882 -810 -163 C ANISOU 2618 CD1 TRP B 178 5312 3588 4098 903 -716 -152 C ANISOU 2619 CD2 TRP B 178 5179 3532 3900 831 -819 -225 C ANISOU 2620 NE1 TRP B 178 5537 3745 4254 852 -676 -217 N ANISOU 2621 CE2 TRP B 178 5705 3979 4387 816 -747 -256 C ANISOU 2622 CE3 TRP B 178 5364 3754 4054 802 -864 -254 C ANISOU 2623 CZ2 TRP B 178 6117 4398 4746 772 -740 -314 C ANISOU 2624 CZ3 TRP B 178 5658 4028 4289 780 -848 -291 C ANISOU 2625 CH2 TRP B 178 5865 4207 4473 766 -797 -320 C ANISOU 2626 N GLY B 179 5440 4013 4152 797 -1001 -202 N ANISOU 2627 CA GLY B 179 5530 4033 4133 758 -1003 -240 C ANISOU 2628 C GLY B 179 5635 4093 4240 715 -972 -291 C ANISOU 2629 O GLY B 179 5332 3822 4013 703 -959 -304 O ANISOU 2630 N ILE B 180 5621 3995 4139 704 -944 -310 N ANISOU 2631 CA ILE B 180 5595 3912 4100 689 -890 -334 C ANISOU 2632 C ILE B 180 5846 4092 4254 647 -873 -362 C ANISOU 2633 O ILE B 180 5492 3712 3828 650 -891 -356 O ANISOU 2634 CB ILE B 180 5859 4171 4371 738 -851 -315 C ANISOU 2635 CG1 ILE B 180 6561 4836 5062 758 -783 -307 C ANISOU 2636 CG2 ILE B 180 6154 4454 4616 747 -852 -314 C ANISOU 2637 CD1 ILE B 180 6480 4826 4990 819 -756 -278 C ANISOU 2638 N THR B 181 5471 3668 3873 600 -822 -399 N ANISOU 2639 CA THR B 181 5819 3919 4122 544 -774 -442 C ANISOU 2640 C THR B 181 5348 3320 3632 584 -657 -420 C ANISOU 2641 O THR B 181 5351 3310 3694 620 -601 -398 O ANISOU 2642 CB THR B 181 5630 3764 3929 438 -775 -519 C ANISOU 2643 OG1 THR B 181 6107 4415 4429 425 -891 -516 O ANISOU 2644 CG2 THR B 181 6181 4196 4359 356 -704 -585 C ANISOU 2645 N PHE B 182 5271 3156 3469 593 -615 -414 N ANISOU 2646 CA PHE B 182 5566 3340 3741 649 -492 -375 C ANISOU 2647 C PHE B 182 5584 3184 3666 569 -383 -434 C ANISOU 2648 O PHE B 182 5590 3166 3586 494 -417 -489 O ANISOU 2649 CB PHE B 182 5908 3734 4078 723 -509 -322 C ANISOU 2650 CG PHE B 182 6083 3831 4234 795 -383 -267 C ANISOU 2651 CD1 PHE B 182 6706 4446 4898 876 -289 -206 C ANISOU 2652 CD2 PHE B 182 6643 4326 4735 797 -345 -264 C ANISOU 2653 CE1 PHE B 182 6737 4416 4914 969 -157 -130 C ANISOU 2654 CE2 PHE B 182 6366 3986 4454 878 -215 -199 C ANISOU 2655 CZ PHE B 182 6753 4379 4886 971 -120 -126 C ANISOU 2656 N ILE B 183 5691 3161 3781 580 -238 -428 N ANISOU 2657 CA ILE B 183 5663 2926 3664 495 -86 -495 C ANISOU 2658 C ILE B 183 5626 2742 3605 612 78 -401 C ANISOU 2659 O ILE B 183 5330 2422 3363 714 170 -320 O ANISOU 2660 CB ILE B 183 6044 3255 4076 391 -19 -580 C ANISOU 2661 CG1 ILE B 183 5923 3353 4006 303 -200 -648 C ANISOU 2662 CG2 ILE B 183 6496 3473 4429 275 168 -675 C ANISOU 2663 CD1 ILE B 183 6102 3540 4241 186 -151 -744 C ANISOU 2664 N PRO B 184 5949 2977 3847 615 123 -397 N ANISOU 2665 CA PRO B 184 6211 3135 4105 745 279 -291 C ANISOU 2666 C PRO B 184 6558 3211 4409 752 535 -283 C ANISOU 2667 O PRO B 184 6563 3059 4355 605 612 -403 O ANISOU 2668 CB PRO B 184 6303 3175 4113 710 269 -317 C ANISOU 2669 CG PRO B 184 6433 3430 4209 593 75 -412 C ANISOU 2670 CD PRO B 184 6089 3124 3893 504 34 -484 C ANISOU 2671 N SER B 185 6932 3544 4815 925 676 -139 N ANISOU 2672 CA SER B 185 6887 3209 4727 971 963 -96 C ANISOU 2673 C SER B 185 7087 3147 4808 865 1110 -180 C ANISOU 2674 O SER B 185 6701 2828 4370 755 969 -272 O ANISOU 2675 CB SER B 185 6732 3122 4634 1213 1072 105 C ANISOU 2676 OG SER B 185 6387 2881 4302 1298 1044 177 O ANISOU 2677 N ASP B 186 7223 2975 4893 912 1412 -137 N ANISOU 2678 CA ASP B 186 7544 3001 5091 818 1604 -212 C ANISOU 2679 C ASP B 186 7080 2616 4643 962 1592 -89 C ANISOU 2680 O ASP B 186 7309 2666 4771 880 1681 -155 O ANISOU 2681 CB ASP B 186 8259 3322 5747 818 1970 -210 C ANISOU 2682 CG ASP B 186 8895 3851 6362 626 2013 -375 C ANISOU 2683 OD1 ASP B 186 9612 4819 7110 493 1747 -490 O ANISOU 2684 OD2 ASP B 186 10141 4771 7573 621 2326 -378 O ANISOU 2685 N GLU B 187 6617 2430 4307 1170 1495 84 N ANISOU 2686 CA GLU B 187 6795 2739 4530 1299 1476 194 C ANISOU 2687 C GLU B 187 6698 2722 4379 1137 1275 55 C ANISOU 2688 O GLU B 187 6130 2277 3799 1004 1070 -60 O ANISOU 2689 CB GLU B 187 6674 2986 4560 1517 1370 373 C ANISOU 2690 CG GLU B 187 7098 3333 5016 1715 1594 544 C ANISOU 2691 CD GLU B 187 6979 3632 5029 1929 1478 718 C ANISOU 2692 OE1 GLU B 187 7022 3947 5155 2028 1400 798 O ANISOU 2693 OE2 GLU B 187 7220 3937 5287 1991 1473 768 O ANISOU 2694 N GLU B 188 7412 3339 5050 1152 1360 71 N ANISOU 2695 CA GLU B 188 8295 4257 5859 1015 1208 -44 C ANISOU 2696 C GLU B 188 7839 4180 5520 1053 931 -19 C ANISOU 2697 O GLU B 188 8820 5242 6455 924 745 -129 O ANISOU 2698 CB GLU B 188 8844 4618 6351 1050 1384 -10 C ANISOU 2699 CG GLU B 188 9570 5346 6977 916 1255 -122 C ANISOU 2700 CD GLU B 188 10468 6040 7810 944 1437 -95 C ANISOU 2701 OE1 GLU B 188 11114 6544 8502 1076 1676 20 O ANISOU 2702 OE2 GLU B 188 10814 6364 8057 843 1354 -179 O ANISOU 2703 N HIS B 189 7887 4470 5718 1232 919 126 N ANISOU 2704 CA HIS B 189 7574 4518 5522 1259 691 139 C ANISOU 2705 C HIS B 189 7009 4175 5053 1332 604 194 C ANISOU 2706 O HIS B 189 6880 4121 4993 1491 715 327 O ANISOU 2707 CB HIS B 189 7858 4982 5914 1379 724 237 C ANISOU 2708 CG HIS B 189 8266 5740 6435 1368 516 215 C ANISOU 2709 ND1 HIS B 189 8324 5766 6430 1224 382 92 N ANISOU 2710 CD2 HIS B 189 8368 6219 6697 1471 439 290 C ANISOU 2711 CE1 HIS B 189 8002 5751 6230 1234 249 88 C ANISOU 2712 NE2 HIS B 189 7713 5729 6079 1370 273 194 N ANISOU 2713 N ASN B 190 6396 3661 4434 1225 418 99 N ANISOU 2714 CA ASN B 190 6262 3727 4378 1275 326 133 C ANISOU 2715 C ASN B 190 6576 4360 4784 1265 129 111 C ANISOU 2716 O ASN B 190 6395 4170 4575 1162 36 25 O ANISOU 2717 CB ASN B 190 6166 3482 4217 1163 298 43 C ANISOU 2718 CG ASN B 190 6325 3331 4295 1151 513 43 C ANISOU 2719 OD1 ASN B 190 6139 3114 4133 1212 592 93 O ANISOU 2720 ND2 ASN B 190 6926 3688 4793 1076 631 -12 N ANISOU 2721 N ILE B 191 6374 4434 4682 1370 84 188 N ANISOU 2722 CA ILE B 191 6151 4526 4547 1348 -76 153 C ANISOU 2723 C ILE B 191 6260 4775 4682 1368 -150 161 C ANISOU 2724 O ILE B 191 6441 5018 4877 1492 -73 265 O ANISOU 2725 CB ILE B 191 6269 4941 4775 1452 -58 229 C ANISOU 2726 CG1 ILE B 191 6605 5126 5094 1454 45 241 C ANISOU 2727 CG2 ILE B 191 6302 5299 4897 1391 -209 158 C ANISOU 2728 CD1 ILE B 191 6704 5548 5327 1556 67 317 C ANISOU 2729 N VAL B 192 5745 4287 4163 1254 -281 60 N ANISOU 2730 CA VAL B 192 5994 4666 4437 1257 -353 53 C ANISOU 2731 C VAL B 192 5858 4762 4361 1189 -473 -22 C ANISOU 2732 O VAL B 192 5764 4591 4258 1096 -508 -98 O ANISOU 2733 CB VAL B 192 5975 4414 4359 1182 -361 2 C ANISOU 2734 CG1 VAL B 192 6512 4728 4843 1232 -215 58 C ANISOU 2735 CG2 VAL B 192 6191 4492 4534 1051 -431 -98 C ANISOU 2736 N ILE B 193 5859 5042 4414 1235 -516 -2 N ANISOU 2737 CA ILE B 193 5902 5312 4511 1152 -604 -93 C ANISOU 2738 C ILE B 193 5646 5046 4234 1106 -658 -138 C ANISOU 2739 O ILE B 193 6210 5680 4782 1184 -646 -74 O ANISOU 2740 CB ILE B 193 5775 5584 4465 1217 -611 -59 C ANISOU 2741 CG1 ILE B 193 5966 5787 4692 1286 -540 6 C ANISOU 2742 CG2 ILE B 193 5945 5986 4689 1095 -683 -188 C ANISOU 2743 CD1 ILE B 193 5678 5949 4507 1363 -549 52 C ANISOU 2744 N ILE B 194 5852 5141 4435 989 -700 -236 N ANISOU 2745 CA ILE B 194 6180 5444 4754 941 -736 -282 C ANISOU 2746 C ILE B 194 6356 5842 4971 860 -762 -378 C ANISOU 2747 O ILE B 194 5580 4992 4209 772 -751 -454 O ANISOU 2748 CB ILE B 194 6347 5322 4886 883 -743 -309 C ANISOU 2749 CG1 ILE B 194 6471 5252 4967 928 -710 -247 C ANISOU 2750 CG2 ILE B 194 6782 5742 5329 846 -767 -344 C ANISOU 2751 CD1 ILE B 194 6387 4962 4851 869 -731 -276 C ANISOU 2752 N LYS B 195 6678 6436 5304 888 -781 -377 N ANISOU 2753 CA LYS B 195 6836 6835 5494 786 -797 -493 C ANISOU 2754 C LYS B 195 6719 6544 5351 689 -784 -577 C ANISOU 2755 O LYS B 195 7022 6864 5675 570 -753 -694 O ANISOU 2756 CB LYS B 195 7109 7508 5770 837 -828 -476 C ANISOU 2757 CG LYS B 195 7895 8593 6606 933 -835 -399 C ANISOU 2758 CD LYS B 195 8328 9481 7034 991 -875 -376 C ANISOU 2759 CE LYS B 195 8925 10450 7698 1102 -882 -287 C ANISOU 2760 NZ LYS B 195 9547 11209 8421 985 -883 -398 N ANISOU 2761 N LYS B 196 6407 6052 5001 741 -788 -518 N ANISOU 2762 CA LYS B 196 6533 6037 5115 667 -765 -583 C ANISOU 2763 C LYS B 196 6414 5701 4980 731 -769 -504 C ANISOU 2764 O LYS B 196 6552 5862 5101 822 -780 -419 O ANISOU 2765 CB LYS B 196 6728 6494 5292 615 -765 -661 C ANISOU 2766 CG LYS B 196 7460 7102 6003 531 -716 -741 C ANISOU 2767 CD LYS B 196 7712 7641 6215 468 -714 -831 C ANISOU 2768 CE LYS B 196 8428 8215 6901 376 -641 -920 C ANISOU 2769 NZ LYS B 196 8962 9050 7372 299 -638 -1023 N ANISOU 2770 N ILE B 197 6109 5191 4688 683 -743 -533 N ANISOU 2771 CA ILE B 197 6137 5047 4727 722 -745 -477 C ANISOU 2772 C ILE B 197 5977 4823 4580 667 -697 -532 C ANISOU 2773 O ILE B 197 6640 5384 5254 615 -650 -575 O ANISOU 2774 CB ILE B 197 5896 4633 4498 742 -761 -430 C ANISOU 2775 CG1 ILE B 197 6046 4811 4624 783 -782 -387 C ANISOU 2776 CG2 ILE B 197 5788 4412 4423 767 -768 -387 C ANISOU 2777 CD1 ILE B 197 6360 4970 4925 785 -796 -359 C ANISOU 2778 N SER B 198 5784 4665 4379 687 -687 -523 N ANISOU 2779 CA SER B 198 6144 4954 4747 636 -623 -575 C ANISOU 2780 C SER B 198 5755 4473 4390 690 -616 -514 C ANISOU 2781 O SER B 198 5823 4541 4472 755 -657 -444 O ANISOU 2782 CB SER B 198 6478 5468 5024 564 -594 -674 C ANISOU 2783 OG SER B 198 6264 5448 4762 621 -642 -638 O ANISOU 2784 N LEU B 199 5927 4548 4580 655 -544 -547 N ANISOU 2785 CA LEU B 199 5636 4174 4336 695 -516 -501 C ANISOU 2786 C LEU B 199 6415 5016 5046 657 -461 -563 C ANISOU 2787 O LEU B 199 6945 5551 5530 574 -395 -657 O ANISOU 2788 CB LEU B 199 5727 4104 4508 702 -460 -472 C ANISOU 2789 CG LEU B 199 5702 4046 4531 741 -517 -410 C ANISOU 2790 CD1 LEU B 199 5568 3807 4484 784 -466 -348 C ANISOU 2791 CD2 LEU B 199 5726 4142 4573 781 -608 -361 C ANISOU 2792 N LEU B 200 6503 5152 5115 711 -476 -519 N ANISOU 2793 CA LEU B 200 6598 5321 5120 688 -428 -567 C ANISOU 2794 C LEU B 200 6914 5474 5490 699 -349 -547 C ANISOU 2795 O LEU B 200 6493 4966 5167 761 -360 -467 O ANISOU 2796 CB LEU B 200 6745 5630 5191 762 -477 -513 C ANISOU 2797 CG LEU B 200 6837 5913 5240 779 -549 -507 C ANISOU 2798 CD1 LEU B 200 6993 6258 5299 867 -564 -447 C ANISOU 2799 CD2 LEU B 200 7291 6484 5667 669 -549 -624 C ANISOU 2800 N SER B 201 7242 5776 5755 629 -260 -630 N ANISOU 2801 CA SER B 201 7714 6089 6269 636 -161 -618 C ANISOU 2802 C SER B 201 7754 6197 6226 678 -156 -596 C ANISOU 2803 O SER B 201 7421 6044 5754 662 -188 -636 O ANISOU 2804 CB SER B 201 8168 6439 6686 537 -36 -721 C ANISOU 2805 OG SER B 201 8617 7047 6979 441 -26 -843 O ANISOU 2806 N GLU B 202 8219 6536 6781 737 -113 -525 N ANISOU 2807 CA GLU B 202 8710 7043 7202 786 -81 -492 C ANISOU 2808 C GLU B 202 8427 6579 7018 796 27 -471 C ANISOU 2809 O GLU B 202 9368 7496 7884 820 88 -461 O ANISOU 2810 CB GLU B 202 8744 7135 7255 876 -148 -400 C ANISOU 2811 CG GLU B 202 9132 7702 7552 889 -239 -400 C ANISOU 2812 CD GLU B 202 9779 8367 8207 986 -267 -303 C ANISOU 2813 OE1 GLU B 202 10240 8696 8745 1027 -211 -249 O ANISOU 2814 OE2 GLU B 202 9961 8689 8326 1016 -326 -284 O TER 2815 GLU B 202 ANISOU 2816 N ASP C 33 7857 5288 6867 -1318 -386 408 N ANISOU 2817 CA ASP C 33 7544 4917 6535 -1132 -412 349 C ANISOU 2818 C ASP C 33 7601 4552 6591 -1123 -385 314 C ANISOU 2819 O ASP C 33 7715 4463 6713 -1276 -345 272 O ANISOU 2820 CB ASP C 33 7489 5177 6466 -1117 -435 236 C ANISOU 2821 CG ASP C 33 7326 5449 6299 -1094 -455 274 C ANISOU 2822 OD1 ASP C 33 7355 5531 6336 -1091 -456 378 O ANISOU 2823 OD2 ASP C 33 7181 5610 6141 -1078 -467 202 O ANISOU 2824 N LYS C 34 7322 4145 6301 -945 -400 325 N ANISOU 2825 CA LYS C 34 7439 3900 6413 -901 -376 299 C ANISOU 2826 C LYS C 34 7256 3758 6218 -762 -401 217 C ANISOU 2827 O LYS C 34 6992 3673 5951 -640 -426 247 O ANISOU 2828 CB LYS C 34 7504 3756 6483 -817 -360 437 C ANISOU 2829 CG LYS C 34 7668 3563 6639 -743 -332 431 C ANISOU 2830 CD LYS C 34 7764 3518 6738 -649 -313 583 C ANISOU 2831 CE LYS C 34 7959 3389 6922 -552 -280 586 C ANISOU 2832 NZ LYS C 34 8273 3388 7227 -667 -221 525 N ANISOU 2833 N ILE C 35 7424 3748 6377 -783 -384 114 N ANISOU 2834 CA ILE C 35 7423 3782 6364 -658 -401 42 C ANISOU 2835 C ILE C 35 7531 3592 6471 -542 -388 84 C ANISOU 2836 O ILE C 35 7539 3313 6474 -585 -354 72 O ANISOU 2837 CB ILE C 35 7516 3951 6445 -744 -394 -109 C ANISOU 2838 CG1 ILE C 35 7528 4309 6460 -871 -405 -152 C ANISOU 2839 CG2 ILE C 35 7392 3896 6310 -600 -408 -162 C ANISOU 2840 CD1 ILE C 35 7682 4615 6605 -968 -400 -315 C ANISOU 2841 N LEU C 36 7484 3618 6429 -396 -407 133 N ANISOU 2842 CA LEU C 36 7730 3659 6677 -282 -399 171 C ANISOU 2843 C LEU C 36 8206 4032 7140 -245 -390 66 C ANISOU 2844 O LEU C 36 8324 4303 7249 -281 -397 -26 O ANISOU 2845 CB LEU C 36 7431 3509 6393 -168 -418 231 C ANISOU 2846 CG LEU C 36 7312 3519 6285 -191 -427 322 C ANISOU 2847 CD1 LEU C 36 7084 3394 6074 -84 -435 354 C ANISOU 2848 CD2 LEU C 36 7413 3456 6385 -245 -408 408 C ANISOU 2849 N ASP C 37 8881 4479 7811 -165 -372 84 N ANISOU 2850 CA ASP C 37 9595 5095 8510 -114 -361 -12 C ANISOU 2851 C ASP C 37 9375 5046 8301 8 -382 -10 C ANISOU 2852 O ASP C 37 9188 4901 8132 82 -390 74 O ANISOU 2853 CB ASP C 37 10189 5369 9091 -69 -323 8 C ANISOU 2854 CG ASP C 37 11279 6225 10171 -193 -280 12 C ANISOU 2855 OD1 ASP C 37 12381 7445 11280 -331 -287 -6 O ANISOU 2856 OD2 ASP C 37 11666 6313 10543 -149 -233 38 O ANISOU 2857 N LEU C 38 9707 5486 8623 22 -385 -106 N ANISOU 2858 CA LEU C 38 9468 5404 8396 129 -392 -98 C ANISOU 2859 C LEU C 38 9148 4970 8069 217 -380 -140 C ANISOU 2860 O LEU C 38 9573 5467 8479 228 -376 -230 O ANISOU 2861 CB LEU C 38 9763 5954 8685 105 -397 -149 C ANISOU 2862 CG LEU C 38 9858 6213 8783 38 -406 -109 C ANISOU 2863 CD1 LEU C 38 9863 6505 8781 72 -402 -128 C ANISOU 2864 CD2 LEU C 38 9891 6217 8839 75 -407 -4 C ANISOU 2865 N SER C 39 8597 4279 7527 287 -374 -74 N ANISOU 2866 CA SER C 39 8025 3624 6948 389 -361 -100 C ANISOU 2867 C SER C 39 7437 3209 6391 473 -367 -53 C ANISOU 2868 O SER C 39 7149 3006 6130 464 -373 17 O ANISOU 2869 CB SER C 39 8309 3673 7219 428 -342 -55 C ANISOU 2870 OG SER C 39 8342 3655 7242 545 -327 -79 O ANISOU 2871 N PHE C 40 7172 2994 6123 550 -358 -99 N ANISOU 2872 CA PHE C 40 7081 3065 6066 614 -352 -58 C ANISOU 2873 C PHE C 40 6899 2850 5887 713 -345 -49 C ANISOU 2874 O PHE C 40 6606 2701 5621 764 -335 -34 O ANISOU 2875 CB PHE C 40 7126 3281 6111 616 -343 -94 C ANISOU 2876 CG PHE C 40 7275 3507 6256 541 -346 -89 C ANISOU 2877 CD1 PHE C 40 7653 3831 6603 463 -361 -147 C ANISOU 2878 CD2 PHE C 40 7298 3644 6307 543 -328 -23 C ANISOU 2879 CE1 PHE C 40 7631 3925 6578 397 -366 -138 C ANISOU 2880 CE2 PHE C 40 7257 3685 6258 496 -327 -10 C ANISOU 2881 CZ PHE C 40 7375 3800 6344 425 -350 -65 C ANISOU 2882 N LYS C 41 7022 2786 5982 742 -342 -50 N ANISOU 2883 CA LYS C 41 7129 2860 6083 859 -329 -32 C ANISOU 2884 C LYS C 41 6836 2725 5832 895 -335 58 C ANISOU 2885 O LYS C 41 6922 2934 5932 981 -328 67 O ANISOU 2886 CB LYS C 41 7555 3022 6470 891 -309 -22 C ANISOU 2887 CG LYS C 41 8002 3263 6874 850 -289 -134 C ANISOU 2888 CD LYS C 41 8225 3529 7077 928 -278 -237 C ANISOU 2889 CE LYS C 41 8388 3479 7195 886 -251 -373 C ANISOU 2890 NZ LYS C 41 8365 3507 7174 727 -267 -440 N ANISOU 2891 N LYS C 42 6534 2440 5548 826 -346 116 N ANISOU 2892 CA LYS C 42 6308 2390 5362 841 -350 181 C ANISOU 2893 C LYS C 42 6016 2239 5112 749 -350 165 C ANISOU 2894 O LYS C 42 5970 2156 5065 671 -357 171 O ANISOU 2895 CB LYS C 42 6382 2396 5423 850 -354 260 C ANISOU 2896 CG LYS C 42 6617 2447 5615 959 -333 294 C ANISOU 2897 CD LYS C 42 6776 2533 5760 980 -324 400 C ANISOU 2898 CE LYS C 42 7082 2611 6021 1104 -283 447 C ANISOU 2899 NZ LYS C 42 7309 2771 6235 1137 -262 580 N ANISOU 2900 N ILE C 43 5910 2289 5043 764 -334 149 N ANISOU 2901 CA ILE C 43 5736 2209 4911 687 -313 136 C ANISOU 2902 C ILE C 43 5581 2244 4810 680 -294 140 C ANISOU 2903 O ILE C 43 5602 2361 4836 748 -295 145 O ANISOU 2904 CB ILE C 43 5809 2256 4973 689 -293 107 C ANISOU 2905 CG1 ILE C 43 5931 2247 5046 677 -313 83 C ANISOU 2906 CG2 ILE C 43 5706 2223 4914 632 -251 116 C ANISOU 2907 CD1 ILE C 43 5971 2330 5073 688 -296 54 C ANISOU 2908 N GLU C 44 5450 2172 4719 591 -271 128 N ANISOU 2909 CA GLU C 44 5374 2276 4704 540 -241 106 C ANISOU 2910 C GLU C 44 5333 2180 4696 471 -182 85 C ANISOU 2911 O GLU C 44 5234 1961 4582 439 -170 85 O ANISOU 2912 CB GLU C 44 5357 2377 4705 490 -256 96 C ANISOU 2913 CG GLU C 44 5389 2454 4700 574 -304 149 C ANISOU 2914 CD GLU C 44 5380 2620 4705 540 -320 155 C ANISOU 2915 OE1 GLU C 44 5311 2647 4679 437 -296 93 O ANISOU 2916 OE2 GLU C 44 5410 2692 4704 622 -348 222 O ANISOU 2917 N THR C 45 5363 2300 4770 454 -137 77 N ANISOU 2918 CA THR C 45 5456 2312 4895 402 -63 80 C ANISOU 2919 C THR C 45 5470 2456 4973 355 -6 70 C ANISOU 2920 O THR C 45 5366 2536 4885 372 -33 58 O ANISOU 2921 CB THR C 45 5507 2246 4897 481 -64 126 C ANISOU 2922 OG1 THR C 45 5672 2340 5088 455 17 157 O ANISOU 2923 CG2 THR C 45 5523 2344 4891 568 -92 140 C ANISOU 2924 N ASP C 46 5582 2471 5121 296 81 82 N ANISOU 2925 CA ASP C 46 5710 2687 5316 231 155 83 C ANISOU 2926 C ASP C 46 5791 2659 5390 286 220 169 C ANISOU 2927 O ASP C 46 5883 2775 5536 234 304 197 O ANISOU 2928 CB ASP C 46 5830 2798 5505 76 228 9 C ANISOU 2929 CG ASP C 46 5949 2667 5620 41 295 5 C ANISOU 2930 OD1 ASP C 46 5838 2418 5450 141 277 68 O ANISOU 2931 OD2 ASP C 46 6206 2878 5934 -87 373 -67 O ANISOU 2932 N LEU C 47 5830 2608 5362 389 182 213 N ANISOU 2933 CA LEU C 47 5993 2718 5507 462 236 301 C ANISOU 2934 C LEU C 47 5893 2743 5355 577 168 320 C ANISOU 2935 O LEU C 47 5912 2830 5344 605 83 266 O ANISOU 2936 CB LEU C 47 6164 2723 5642 485 255 324 C ANISOU 2937 CG LEU C 47 6391 2797 5909 387 325 289 C ANISOU 2938 CD1 LEU C 47 6477 2743 5954 446 357 336 C ANISOU 2939 CD2 LEU C 47 6660 3025 6254 302 442 305 C ANISOU 2940 N SER C 48 5857 2736 5305 648 216 399 N ANISOU 2941 CA SER C 48 5770 2786 5166 756 165 408 C ANISOU 2942 C SER C 48 5664 2617 4999 802 129 402 C ANISOU 2943 O SER C 48 5839 2692 5178 791 184 453 O ANISOU 2944 CB SER C 48 5837 2984 5256 806 238 498 C ANISOU 2945 OG SER C 48 5896 3126 5376 747 271 498 O ANISOU 2946 N SER C 49 5505 2516 4784 850 46 338 N ANISOU 2947 CA SER C 49 5414 2393 4639 868 11 318 C ANISOU 2948 C SER C 49 5402 2518 4572 933 -39 262 C ANISOU 2949 O SER C 49 5398 2568 4560 961 -72 207 O ANISOU 2950 CB SER C 49 5368 2194 4585 798 -39 259 C ANISOU 2951 OG SER C 49 5305 2119 4474 800 -76 234 O ANISOU 2952 N LYS C 50 5373 2558 4504 956 -42 268 N ANISOU 2953 CA LYS C 50 5398 2733 4476 993 -89 189 C ANISOU 2954 C LYS C 50 5384 2656 4428 935 -131 133 C ANISOU 2955 O LYS C 50 5288 2565 4335 928 -103 199 O ANISOU 2956 CB LYS C 50 5420 3023 4490 1084 -43 252 C ANISOU 2957 CG LYS C 50 5442 3260 4458 1116 -88 147 C ANISOU 2958 CD LYS C 50 5444 3589 4450 1218 -43 215 C ANISOU 2959 CE LYS C 50 5480 3877 4432 1235 -90 80 C ANISOU 2960 NZ LYS C 50 5519 3808 4455 1207 -142 -73 N ANISOU 2961 N ILE C 51 5424 2623 4436 893 -192 15 N ANISOU 2962 CA ILE C 51 5477 2605 4460 816 -231 -45 C ANISOU 2963 C ILE C 51 5625 2911 4562 808 -257 -161 C ANISOU 2964 O ILE C 51 5600 2882 4522 832 -271 -248 O ANISOU 2965 CB ILE C 51 5536 2401 4526 756 -263 -78 C ANISOU 2966 CG1 ILE C 51 5480 2245 4517 755 -238 12 C ANISOU 2967 CG2 ILE C 51 5565 2350 4529 667 -297 -131 C ANISOU 2968 CD1 ILE C 51 5520 2100 4565 719 -268 -5 C ANISOU 2969 N THR C 52 5720 3154 4636 770 -264 -175 N ANISOU 2970 CA THR C 52 5908 3547 4784 739 -286 -303 C ANISOU 2971 C THR C 52 6131 3740 4990 617 -315 -371 C ANISOU 2972 O THR C 52 6030 3723 4896 607 -307 -291 O ANISOU 2973 CB THR C 52 5845 3869 4712 831 -255 -248 C ANISOU 2974 OG1 THR C 52 5802 3842 4692 936 -218 -158 O ANISOU 2975 CG2 THR C 52 5928 4239 4755 802 -278 -398 C ANISOU 2976 N TYR C 53 6561 4039 5399 525 -341 -521 N ANISOU 2977 CA TYR C 53 6955 4411 5780 387 -361 -598 C ANISOU 2978 C TYR C 53 7243 5116 6045 361 -364 -675 C ANISOU 2979 O TYR C 53 7401 5436 6181 364 -365 -802 O ANISOU 2980 CB TYR C 53 7248 4389 6060 288 -369 -727 C ANISOU 2981 CG TYR C 53 7287 4049 6117 301 -367 -644 C ANISOU 2982 CD1 TYR C 53 7195 3861 6042 421 -358 -560 C ANISOU 2983 CD2 TYR C 53 7405 3939 6236 189 -370 -648 C ANISOU 2984 CE1 TYR C 53 7250 3634 6113 436 -357 -487 C ANISOU 2985 CE2 TYR C 53 7505 3741 6351 212 -366 -561 C ANISOU 2986 CZ TYR C 53 7434 3610 6295 339 -361 -483 C ANISOU 2987 OH TYR C 53 7610 3552 6485 365 -357 -399 O ANISOU 2988 N GLU C 54 7491 5567 6296 341 -365 -600 N ANISOU 2989 CA GLU C 54 7851 6390 6634 329 -367 -655 C ANISOU 2990 C GLU C 54 8014 6590 6790 145 -390 -773 C ANISOU 2991 O GLU C 54 7819 6038 6608 42 -398 -792 O ANISOU 2992 CB GLU C 54 7877 6677 6665 478 -336 -469 C ANISOU 2993 CG GLU C 54 8102 6846 6903 635 -300 -358 C ANISOU 2994 CD GLU C 54 8341 7292 7148 788 -248 -165 C ANISOU 2995 OE1 GLU C 54 8749 7576 7570 798 -230 -60 O ANISOU 2996 OE2 GLU C 54 8570 7790 7368 906 -216 -116 O ANISOU 2997 N ASP C 55 8589 7630 7347 106 -396 -846 N ANISOU 2998 CA ASP C 55 9256 8424 8011 -87 -414 -979 C ANISOU 2999 C ASP C 55 9552 8379 8328 -182 -420 -910 C ANISOU 3000 O ASP C 55 9879 8381 8662 -331 -421 -1016 O ANISOU 3001 CB ASP C 55 9427 9223 8165 -73 -417 -989 C ANISOU 3002 CG ASP C 55 9639 9834 8354 -27 -415 -1109 C ANISOU 3003 OD1 ASP C 55 10139 10269 8848 -168 -423 -1329 O ANISOU 3004 OD2 ASP C 55 9577 10148 8280 152 -398 -982 O ANISOU 3005 N THR C 56 9743 8639 8528 -91 -415 -733 N ANISOU 3006 CA THR C 56 10114 8747 8917 -178 -422 -671 C ANISOU 3007 C THR C 56 10235 8508 9056 -55 -411 -516 C ANISOU 3008 O THR C 56 10794 8736 9630 -126 -417 -493 O ANISOU 3009 CB THR C 56 10091 9105 8891 -206 -428 -620 C ANISOU 3010 OG1 THR C 56 10443 9856 9230 -329 -438 -777 O ANISOU 3011 CG2 THR C 56 10087 8881 8905 -309 -436 -568 C ANISOU 3012 N GLY C 57 9769 8123 8589 122 -388 -411 N ANISOU 3013 CA GLY C 57 9282 7334 8124 223 -370 -281 C ANISOU 3014 C GLY C 57 8932 6789 7780 298 -359 -293 C ANISOU 3015 O GLY C 57 8815 6779 7648 292 -365 -395 O ANISOU 3016 N VAL C 58 8394 5988 7267 361 -344 -196 N ANISOU 3017 CA VAL C 58 8024 5449 6911 435 -331 -186 C ANISOU 3018 C VAL C 58 7721 5222 6626 566 -283 -52 C ANISOU 3019 O VAL C 58 8053 5507 6972 583 -262 33 O ANISOU 3020 CB VAL C 58 7961 5032 6864 385 -348 -193 C ANISOU 3021 CG1 VAL C 58 7906 4849 6825 468 -334 -177 C ANISOU 3022 CG2 VAL C 58 8039 4987 6924 259 -376 -307 C ANISOU 3023 N LYS C 59 7336 4950 6240 657 -258 -38 N ANISOU 3024 CA LYS C 59 7033 4702 5958 777 -195 95 C ANISOU 3025 C LYS C 59 6793 4211 5754 794 -178 126 C ANISOU 3026 O LYS C 59 6702 4049 5664 777 -205 54 O ANISOU 3027 CB LYS C 59 7079 5088 5982 874 -167 120 C ANISOU 3028 CG LYS C 59 7061 5123 5985 1010 -84 282 C ANISOU 3029 CD LYS C 59 7318 5762 6217 1122 -51 332 C ANISOU 3030 CE LYS C 59 7380 5962 6267 1114 -87 226 C ANISOU 3031 NZ LYS C 59 7603 6616 6466 1231 -53 281 N ANISOU 3032 N ILE C 60 6531 3829 5524 825 -127 227 N ANISOU 3033 CA ILE C 60 6359 3461 5394 825 -101 256 C ANISOU 3034 C ILE C 60 6310 3460 5372 915 -10 374 C ANISOU 3035 O ILE C 60 6127 3293 5187 958 44 453 O ANISOU 3036 CB ILE C 60 6377 3267 5434 746 -119 240 C ANISOU 3037 CG1 ILE C 60 6413 3245 5445 664 -196 150 C ANISOU 3038 CG2 ILE C 60 6344 3093 5449 736 -90 258 C ANISOU 3039 CD1 ILE C 60 6490 3164 5539 597 -214 149 C ANISOU 3040 N GLU C 61 6239 3413 5322 950 13 392 N ANISOU 3041 CA GLU C 61 6355 3551 5469 1023 110 513 C ANISOU 3042 C GLU C 61 6228 3243 5398 964 134 507 C ANISOU 3043 O GLU C 61 6143 3128 5316 914 69 419 O ANISOU 3044 CB GLU C 61 6555 4020 5647 1117 123 549 C ANISOU 3045 CG GLU C 61 6713 4436 5752 1170 99 543 C ANISOU 3046 CD GLU C 61 6895 4947 5909 1261 106 561 C ANISOU 3047 OE1 GLU C 61 7127 5200 6164 1287 127 581 O ANISOU 3048 OE2 GLU C 61 7065 5393 6037 1308 93 557 O ANISOU 3049 N THR C 62 6201 3097 5414 968 232 595 N ANISOU 3050 CA THR C 62 6219 2978 5493 891 266 579 C ANISOU 3051 C THR C 62 6481 3222 5798 928 390 700 C ANISOU 3052 O THR C 62 6670 3439 5970 1019 465 810 O ANISOU 3053 CB THR C 62 6063 2626 5361 795 266 522 C ANISOU 3054 OG1 THR C 62 6084 2536 5383 826 354 591 O ANISOU 3055 CG2 THR C 62 5907 2475 5168 753 155 424 C ANISOU 3056 N ASP C 63 6714 3426 6086 859 415 684 N ANISOU 3057 CA ASP C 63 7081 3751 6509 856 542 789 C ANISOU 3058 C ASP C 63 7132 3618 6626 710 585 722 C ANISOU 3059 O ASP C 63 7019 3562 6529 632 506 615 O ANISOU 3060 CB ASP C 63 7227 4122 6662 907 537 834 C ANISOU 3061 CG ASP C 63 7343 4467 6713 1047 504 887 C ANISOU 3062 OD1 ASP C 63 7556 4680 6877 1100 479 888 O ANISOU 3063 OD2 ASP C 63 7654 4986 7027 1101 506 926 O ANISOU 3064 N SER C 64 7374 3648 6906 679 715 781 N ANISOU 3065 CA SER C 64 7573 3673 7171 524 771 696 C ANISOU 3066 C SER C 64 8110 3984 7759 501 954 794 C ANISOU 3067 O SER C 64 8098 3928 7720 630 1034 942 O ANISOU 3068 CB SER C 64 7547 3554 7120 481 708 584 C ANISOU 3069 OG SER C 64 7455 3340 6983 579 752 650 O ANISOU 3070 N SER C 65 8501 4236 8223 335 1024 708 N ANISOU 3071 CA SER C 65 8803 4268 8584 275 1214 773 C ANISOU 3072 C SER C 65 8983 4181 8778 186 1272 657 C ANISOU 3073 O SER C 65 8669 3948 8456 109 1165 501 O ANISOU 3074 CB SER C 65 9023 4561 8889 134 1273 763 C ANISOU 3075 OG SER C 65 8943 4624 8845 -21 1182 581 O ANISOU 3076 N LYS C 66 9500 4380 9314 206 1450 739 N ANISOU 3077 CA LYS C 66 9653 4246 9477 136 1530 628 C ANISOU 3078 C LYS C 66 9693 4299 9593 -109 1525 417 C ANISOU 3079 O LYS C 66 9434 4048 9324 -175 1462 255 O ANISOU 3080 CB LYS C 66 10149 4370 9984 209 1750 769 C ANISOU 3081 CG LYS C 66 10396 4272 10237 156 1860 656 C ANISOU 3082 CD LYS C 66 10710 4188 10551 270 2089 816 C ANISOU 3083 CE LYS C 66 11078 4352 11002 168 2271 908 C ANISOU 3084 NZ LYS C 66 11131 4292 11150 -124 2321 684 N ANISOU 3085 N SER C 67 9857 4517 9834 -241 1586 422 N ANISOU 3086 CA SER C 67 10041 4773 10101 -487 1595 228 C ANISOU 3087 C SER C 67 10042 5108 10076 -525 1397 71 C ANISOU 3088 O SER C 67 10002 5104 10079 -693 1396 -117 O ANISOU 3089 CB SER C 67 10060 4894 10197 -593 1664 288 C ANISOU 3090 OG SER C 67 9593 4754 9692 -465 1534 399 O ANISOU 3091 N ASP C 68 10277 5594 10243 -369 1238 149 N ANISOU 3092 CA ASP C 68 10365 5968 10300 -380 1062 33 C ANISOU 3093 C ASP C 68 10370 5846 10259 -352 1035 -47 C ANISOU 3094 O ASP C 68 10102 5494 9919 -191 1003 46 O ANISOU 3095 CB ASP C 68 10536 6383 10412 -223 922 135 C ANISOU 3096 CG ASP C 68 10858 6968 10699 -215 754 41 C ANISOU 3097 OD1 ASP C 68 11821 7973 11685 -326 737 -95 O ANISOU 3098 OD2 ASP C 68 10728 7000 10519 -94 648 107 O ANISOU 3099 N LYS C 69 10505 6002 10436 -512 1049 -227 N ANISOU 3100 CA LYS C 69 10546 5955 10438 -496 1028 -318 C ANISOU 3101 C LYS C 69 10030 5753 9873 -448 843 -358 C ANISOU 3102 O LYS C 69 9498 5208 9295 -404 796 -402 O ANISOU 3103 CB LYS C 69 10904 6177 10864 -691 1150 -502 C ANISOU 3104 CG LYS C 69 11164 6345 11086 -677 1146 -612 C ANISOU 3105 CD LYS C 69 11766 6804 11753 -874 1277 -817 C ANISOU 3106 CE LYS C 69 11976 6949 11919 -843 1269 -929 C ANISOU 3107 NZ LYS C 69 12477 7315 12484 -1042 1403 -1158 N ANISOU 3108 N GLU C 70 9819 5820 9671 -445 746 -331 N ANISOU 3109 CA GLU C 70 9459 5736 9265 -389 587 -349 C ANISOU 3110 C GLU C 70 8821 5102 8556 -210 501 -200 C ANISOU 3111 O GLU C 70 8975 5470 8684 -159 390 -183 O ANISOU 3112 CB GLU C 70 9982 6585 9843 -494 542 -427 C ANISOU 3113 CG GLU C 70 10636 7311 10575 -697 621 -601 C ANISOU 3114 CD GLU C 70 11162 7872 11085 -742 599 -727 C ANISOU 3115 OE1 GLU C 70 11377 8055 11227 -612 517 -667 O ANISOU 3116 OE2 GLU C 70 11473 8259 11458 -917 666 -894 O ANISOU 3117 N ARG C 71 8299 4352 7999 -111 559 -97 N ANISOU 3118 CA ARG C 71 7730 3810 7364 43 489 24 C ANISOU 3119 C ARG C 71 7453 3599 7022 107 374 9 C ANISOU 3120 O ARG C 71 7637 3695 7192 92 391 -33 O ANISOU 3121 CB ARG C 71 7809 3681 7421 138 585 138 C ANISOU 3122 CG ARG C 71 7874 3629 7546 95 724 193 C ANISOU 3123 CD ARG C 71 7912 3470 7556 216 829 329 C ANISOU 3124 NE ARG C 71 7743 3111 7362 237 879 298 N ANISOU 3125 CZ ARG C 71 7941 3036 7592 212 1038 307 C ANISOU 3126 NH1 ARG C 71 7980 2925 7598 255 1074 276 N ANISOU 3127 NH2 ARG C 71 8025 2988 7738 148 1168 351 N ANISOU 3128 N TYR C 72 6867 3156 6397 178 268 46 N ANISOU 3129 CA TYR C 72 6647 2977 6117 229 170 44 C ANISOU 3130 C TYR C 72 6049 2469 5477 313 85 92 C ANISOU 3131 O TYR C 72 5953 2456 5399 327 82 105 O ANISOU 3132 CB TYR C 72 6850 3298 6335 153 120 -43 C ANISOU 3133 CG TYR C 72 7098 3745 6608 128 70 -69 C ANISOU 3134 CD1 TYR C 72 7452 4178 7024 61 125 -100 C ANISOU 3135 CD2 TYR C 72 7358 4119 6829 183 -25 -50 C ANISOU 3136 CE1 TYR C 72 7518 4474 7112 53 79 -118 C ANISOU 3137 CE2 TYR C 72 7568 4522 7056 191 -65 -57 C ANISOU 3138 CZ TYR C 72 7866 4940 7415 131 -16 -93 C ANISOU 3139 OH TYR C 72 8613 5923 8176 152 -55 -96 O ANISOU 3140 N LEU C 73 5802 2202 5172 365 23 112 N ANISOU 3141 CA LEU C 73 5600 2046 4923 430 -53 134 C ANISOU 3142 C LEU C 73 5433 1879 4723 413 -119 116 C ANISOU 3143 O LEU C 73 5375 1775 4645 404 -112 122 O ANISOU 3144 CB LEU C 73 5632 2054 4919 503 -38 185 C ANISOU 3145 CG LEU C 73 5588 2046 4824 552 -110 178 C ANISOU 3146 CD1 LEU C 73 5612 2135 4860 586 -124 167 C ANISOU 3147 CD2 LEU C 73 5634 2119 4832 604 -100 207 C ANISOU 3148 N TYR C 74 5292 1802 4579 416 -173 104 N ANISOU 3149 CA TYR C 74 5231 1749 4491 405 -227 108 C ANISOU 3150 C TYR C 74 4989 1453 4204 462 -276 133 C ANISOU 3151 O TYR C 74 4987 1477 4203 511 -284 134 O ANISOU 3152 CB TYR C 74 5233 1886 4528 365 -233 83 C ANISOU 3153 CG TYR C 74 5241 1939 4510 370 -284 111 C ANISOU 3154 CD1 TYR C 74 5240 1889 4482 343 -297 124 C ANISOU 3155 CD2 TYR C 74 5265 2080 4537 410 -313 138 C ANISOU 3156 CE1 TYR C 74 5277 1978 4499 346 -337 165 C ANISOU 3157 CE2 TYR C 74 5302 2164 4549 428 -348 188 C ANISOU 3158 CZ TYR C 74 5307 2105 4531 390 -359 204 C ANISOU 3159 OH TYR C 74 5373 2227 4575 407 -387 269 O ANISOU 3160 N ILE C 75 5010 1399 4185 450 -302 146 N ANISOU 3161 CA ILE C 75 5083 1378 4215 477 -334 153 C ANISOU 3162 C ILE C 75 5140 1402 4254 449 -362 189 C ANISOU 3163 O ILE C 75 5089 1388 4204 397 -364 198 O ANISOU 3164 CB ILE C 75 5083 1347 4186 467 -328 131 C ANISOU 3165 CG1 ILE C 75 5038 1369 4161 502 -288 123 C ANISOU 3166 CG2 ILE C 75 5181 1347 4243 474 -353 104 C ANISOU 3167 CD1 ILE C 75 5042 1412 4139 510 -277 117 C ANISOU 3168 N TYR C 76 5474 1668 4571 493 -377 218 N ANISOU 3169 CA TYR C 76 5596 1758 4678 477 -392 278 C ANISOU 3170 C TYR C 76 5920 1897 4965 523 -389 308 C ANISOU 3171 O TYR C 76 5867 1782 4903 591 -379 280 O ANISOU 3172 CB TYR C 76 5516 1853 4628 500 -395 319 C ANISOU 3173 CG TYR C 76 5533 1931 4654 590 -390 336 C ANISOU 3174 CD1 TYR C 76 5451 1915 4596 612 -377 283 C ANISOU 3175 CD2 TYR C 76 5623 2002 4723 667 -391 419 C ANISOU 3176 CE1 TYR C 76 5483 2037 4637 700 -373 300 C ANISOU 3177 CE2 TYR C 76 5682 2138 4785 773 -384 445 C ANISOU 3178 CZ TYR C 76 5599 2155 4729 787 -378 379 C ANISOU 3179 OH TYR C 76 5620 2289 4751 896 -371 406 O ANISOU 3180 N GLN C 77 6258 2143 5284 486 -389 365 N ANISOU 3181 CA GLN C 77 6890 2547 5882 521 -368 402 C ANISOU 3182 C GLN C 77 7186 2863 6176 557 -358 530 C ANISOU 3183 O GLN C 77 7128 2969 6135 508 -375 571 O ANISOU 3184 CB GLN C 77 7145 2627 6112 420 -359 348 C ANISOU 3185 CG GLN C 77 7295 2797 6257 392 -366 227 C ANISOU 3186 CD GLN C 77 7321 3050 6309 364 -387 201 C ANISOU 3187 OE1 GLN C 77 7453 3277 6457 417 -386 166 O ANISOU 3188 NE2 GLN C 77 7401 3213 6395 286 -397 224 N ANISOU 3189 N ASN C 78 7829 3346 6795 657 -326 596 N ANISOU 3190 CA ASN C 78 8211 3744 7170 723 -304 744 C ANISOU 3191 C ASN C 78 8635 3876 7567 658 -263 797 C ANISOU 3192 O ASN C 78 8886 3829 7790 666 -223 757 O ANISOU 3193 CB ASN C 78 8410 3976 7360 894 -281 809 C ANISOU 3194 CG ASN C 78 8345 4245 7331 933 -318 760 C ANISOU 3195 OD1 ASN C 78 8242 4320 7260 833 -352 685 O ANISOU 3196 ND2 ASN C 78 8444 4438 7425 1078 -303 806 N ANISOU 3197 N ILE C 79 8800 4136 7740 589 -268 882 N ANISOU 3198 CA ILE C 79 9130 4225 8054 500 -225 942 C ANISOU 3199 C ILE C 79 9392 4590 8317 545 -203 1129 C ANISOU 3200 O ILE C 79 9032 4505 7968 653 -223 1202 O ANISOU 3201 CB ILE C 79 9206 4354 8141 324 -258 833 C ANISOU 3202 CG1 ILE C 79 9005 4508 7967 292 -308 850 C ANISOU 3203 CG2 ILE C 79 9084 4172 8016 291 -276 663 C ANISOU 3204 CD1 ILE C 79 8998 4586 7968 149 -335 764 C ANISOU 3205 N LYS C 80 9561 4546 8475 456 -156 1205 N ANISOU 3206 CA LYS C 80 9742 4806 8657 475 -124 1397 C ANISOU 3207 C LYS C 80 9596 4541 8516 286 -106 1391 C ANISOU 3208 O LYS C 80 9635 4213 8541 218 -38 1398 O ANISOU 3209 CB LYS C 80 10303 5161 9192 639 -43 1575 C ANISOU 3210 CG LYS C 80 10523 5602 9408 842 -60 1618 C ANISOU 3211 CD LYS C 80 11149 6075 10004 1028 27 1830 C ANISOU 3212 CE LYS C 80 11275 6511 10127 1234 7 1881 C ANISOU 3213 NZ LYS C 80 11867 6983 10686 1441 100 2111 N ANISOU 3214 N GLU C 81 9292 4562 8234 197 -163 1368 N ANISOU 3215 CA GLU C 81 9403 4654 8354 17 -157 1356 C ANISOU 3216 C GLU C 81 9005 4635 7971 0 -192 1445 C ANISOU 3217 O GLU C 81 8740 4668 7714 107 -232 1467 O ANISOU 3218 CB GLU C 81 9456 4712 8412 -98 -200 1147 C ANISOU 3219 CG GLU C 81 9802 4722 8741 -100 -168 1034 C ANISOU 3220 CD GLU C 81 9831 4823 8773 -192 -211 837 C ANISOU 3221 OE1 GLU C 81 9430 4723 8387 -239 -265 795 O ANISOU 3222 OE2 GLU C 81 10153 4910 9081 -211 -186 728 O ANISOU 3223 N ASN C 82 8827 4459 7801 -149 -174 1483 N ANISOU 3224 CA ASN C 82 8547 4535 7534 -186 -201 1562 C ANISOU 3225 C ASN C 82 8118 4288 7115 -311 -256 1400 C ANISOU 3226 O ASN C 82 8154 4175 7154 -456 -236 1342 O ANISOU 3227 CB ASN C 82 8888 4768 7877 -247 -129 1759 C ANISOU 3228 CG ASN C 82 8812 5085 7813 -287 -153 1851 C ANISOU 3229 OD1 ASN C 82 8540 5166 7548 -264 -224 1759 O ANISOU 3230 ND2 ASN C 82 9204 5414 8210 -344 -87 2036 N ANISOU 3231 N TRP C 83 7775 4270 6778 -252 -317 1324 N ANISOU 3232 CA TRP C 83 7441 4125 6449 -330 -361 1186 C ANISOU 3233 C TRP C 83 7383 4408 6398 -372 -377 1247 C ANISOU 3234 O TRP C 83 6985 4252 6001 -365 -415 1149 O ANISOU 3235 CB TRP C 83 7294 4064 6304 -235 -401 1049 C ANISOU 3236 CG TRP C 83 7215 3715 6219 -200 -393 963 C ANISOU 3237 CD1 TRP C 83 7362 3542 6356 -236 -355 972 C ANISOU 3238 CD2 TRP C 83 6934 3470 5943 -124 -419 844 C ANISOU 3239 NE1 TRP C 83 7229 3276 6219 -178 -363 865 N ANISOU 3240 CE2 TRP C 83 7020 3284 6020 -110 -401 795 C ANISOU 3241 CE3 TRP C 83 6676 3436 5697 -70 -445 773 C ANISOU 3242 CZ2 TRP C 83 6867 3109 5870 -42 -415 693 C ANISOU 3243 CZ3 TRP C 83 6589 3290 5616 -12 -450 673 C ANISOU 3244 CH2 TRP C 83 6627 3088 5646 2 -438 641 C ANISOU 3245 N SER C 84 7470 4504 6487 -411 -340 1414 N ANISOU 3246 CA SER C 84 7458 4839 6482 -447 -351 1493 C ANISOU 3247 C SER C 84 7588 5083 6614 -588 -364 1417 C ANISOU 3248 O SER C 84 7374 5213 6401 -591 -392 1405 O ANISOU 3249 CB SER C 84 7610 4955 6637 -451 -297 1711 C ANISOU 3250 OG SER C 84 7553 4857 6573 -299 -284 1798 O ANISOU 3251 N MSE C 85 8053 5285 7082 -703 -339 1360 N ANISOU 3252 CA MSE C 85 8272 5634 7305 -850 -346 1288 C ANISOU 3253 C MSE C 85 8194 5683 7216 -807 -393 1111 C ANISOU 3254 O MSE C 85 8592 6188 7615 -911 -399 1035 O ANISOU 3255 CB MSE C 85 8721 5767 7764 -1012 -289 1299 C ANISOU 3256 CG MSE C 85 8930 5616 7964 -986 -276 1189 C ANISOU 3257 SE MSE C 85 9224 5631 8245 -775 -256 1287 SE ANISOU 3258 CE MSE C 85 9528 5766 8560 -837 -165 1547 C ANISOU 3259 N TYR C 86 8031 5527 7046 -655 -421 1050 N ANISOU 3260 CA TYR C 86 7802 5384 6807 -599 -449 904 C ANISOU 3261 C TYR C 86 7512 5379 6513 -491 -473 885 C ANISOU 3262 O TYR C 86 7689 5644 6695 -440 -474 960 O ANISOU 3263 CB TYR C 86 7960 5248 6963 -540 -445 831 C ANISOU 3264 CG TYR C 86 8381 5383 7385 -647 -414 833 C ANISOU 3265 CD1 TYR C 86 8550 5597 7554 -788 -406 774 C ANISOU 3266 CD2 TYR C 86 8731 5433 7735 -610 -385 891 C ANISOU 3267 CE1 TYR C 86 8850 5627 7857 -907 -369 751 C ANISOU 3268 CE2 TYR C 86 9139 5541 8141 -706 -343 882 C ANISOU 3269 CZ TYR C 86 9075 5504 8081 -865 -333 802 C ANISOU 3270 OH TYR C 86 9565 5686 8571 -978 -283 767 O ANISOU 3271 N AASN C 87 8063 5201 6253 -518 -667 995 N ANISOU 3272 N BASN C 87 7980 5117 6170 -519 -668 995 N ANISOU 3273 CA AASN C 87 7864 5298 6134 -431 -616 941 C ANISOU 3274 CA BASN C 87 7721 5160 5992 -435 -616 942 C ANISOU 3275 C AASN C 87 7668 5039 5983 -310 -580 811 C ANISOU 3276 C BASN C 87 7590 4967 5907 -312 -580 812 C ANISOU 3277 O AASN C 87 7467 4979 5835 -219 -545 750 O ANISOU 3278 O BASN C 87 7404 4926 5773 -222 -545 752 O ANISOU 3279 CB AASN C 87 7905 5661 6225 -493 -604 978 C ANISOU 3280 CB BASN C 87 7646 5390 5965 -504 -607 980 C ANISOU 3281 CG AASN C 87 8088 5971 6382 -621 -632 1121 C ANISOU 3282 CG BASN C 87 7405 5448 5794 -402 -555 914 C ANISOU 3283 OD1AASN C 87 8267 5963 6499 -670 -666 1198 O ANISOU 3284 OD1BASN C 87 7307 5480 5698 -353 -539 918 O ANISOU 3285 ND2AASN C 87 8055 6260 6397 -673 -619 1167 N ANISOU 3286 ND2BASN C 87 7369 5521 5810 -365 -531 851 N ANISOU 3287 N ASN C 88 7588 4753 5882 -310 -591 770 N ANISOU 3288 CA ASN C 88 7455 4571 5796 -201 -554 665 C ANISOU 3289 C ASN C 88 7398 4243 5688 -191 -571 634 C ANISOU 3290 O ASN C 88 7665 4349 5875 -272 -616 679 O ANISOU 3291 CB ASN C 88 7423 4763 5836 -179 -522 624 C ANISOU 3292 CG ASN C 88 7732 5105 6124 -272 -548 665 C ANISOU 3293 OD1 ASN C 88 8046 5512 6413 -380 -579 748 O ANISOU 3294 ND2 ASN C 88 7865 5185 6271 -235 -537 612 N ANISOU 3295 N PHE C 89 7194 3991 5527 -89 -535 556 N ANISOU 3296 CA PHE C 89 7145 3737 5437 -56 -538 519 C ANISOU 3297 C PHE C 89 6968 3669 5295 -64 -524 494 C ANISOU 3298 O PHE C 89 6841 3754 5245 -46 -494 482 O ANISOU 3299 CB PHE C 89 7232 3744 5563 56 -502 464 C ANISOU 3300 CG PHE C 89 7201 3637 5514 90 -509 482 C ANISOU 3301 CD1 PHE C 89 7183 3775 5536 82 -507 502 C ANISOU 3302 CD2 PHE C 89 7316 3538 5563 138 -520 479 C ANISOU 3303 CE1 PHE C 89 7270 3813 5606 119 -517 524 C ANISOU 3304 CE2 PHE C 89 7315 3484 5547 181 -528 502 C ANISOU 3305 CZ PHE C 89 7318 3651 5597 168 -527 528 C ANISOU 3306 N TYR C 90 6984 3542 5244 -84 -546 483 N ANISOU 3307 CA TYR C 90 6758 3422 5042 -85 -537 464 C ANISOU 3308 C TYR C 90 6665 3148 4903 -15 -528 418 C ANISOU 3309 O TYR C 90 6875 3162 5007 -46 -570 415 O ANISOU 3310 CB TYR C 90 6902 3642 5144 -213 -588 512 C ANISOU 3311 CG TYR C 90 6853 3812 5146 -221 -577 511 C ANISOU 3312 CD1 TYR C 90 6721 3922 5113 -169 -531 512 C ANISOU 3313 CD2 TYR C 90 6878 3814 5115 -279 -615 509 C ANISOU 3314 CE1 TYR C 90 6672 4088 5111 -162 -519 518 C ANISOU 3315 CE2 TYR C 90 6877 4047 5166 -282 -607 517 C ANISOU 3316 CZ TYR C 90 6783 4195 5174 -218 -556 526 C ANISOU 3317 OH TYR C 90 6889 4540 5332 -201 -544 538 O ANISOU 3318 N ILE C 91 6213 2754 4526 82 -475 385 N ANISOU 3319 CA ILE C 91 6099 2514 4385 162 -453 353 C ANISOU 3320 C ILE C 91 5870 2374 4161 177 -443 347 C ANISOU 3321 O ILE C 91 5638 2318 4011 189 -417 356 O ANISOU 3322 CB ILE C 91 6008 2430 4385 252 -401 336 C ANISOU 3323 CG1 ILE C 91 6024 2404 4403 237 -415 346 C ANISOU 3324 CG2 ILE C 91 6032 2354 4393 336 -372 319 C ANISOU 3325 CD1 ILE C 91 5919 2332 4393 308 -374 327 C ANISOU 3326 N GLU C 92 5861 2244 4053 184 -465 329 N ANISOU 3327 CA GLU C 92 5786 2259 3968 206 -458 324 C ANISOU 3328 C GLU C 92 5698 2109 3888 321 -409 310 C ANISOU 3329 O GLU C 92 5742 1995 3841 354 -420 284 O ANISOU 3330 CB GLU C 92 5963 2392 4028 114 -529 315 C ANISOU 3331 CG GLU C 92 5955 2530 4013 123 -531 315 C ANISOU 3332 CD GLU C 92 6123 2691 4076 16 -609 301 C ANISOU 3333 OE1 GLU C 92 6278 2687 4151 -77 -668 290 O ANISOU 3334 OE2 GLU C 92 6106 2832 4060 20 -614 306 O ANISOU 3335 N ILE C 93 5482 2018 3781 386 -352 330 N ANISOU 3336 CA ILE C 93 5312 1811 3640 484 -300 335 C ANISOU 3337 C ILE C 93 5394 2028 3782 537 -260 368 C ANISOU 3338 O ILE C 93 5186 1946 3637 518 -258 384 O ANISOU 3339 CB ILE C 93 5345 1810 3770 509 -267 336 C ANISOU 3340 CG1 ILE C 93 5340 1772 3805 595 -216 350 C ANISOU 3341 CG2 ILE C 93 5253 1837 3795 490 -250 345 C ANISOU 3342 CD1 ILE C 93 5285 1698 3846 607 -193 350 C ANISOU 3343 N GLN C 94 5466 2080 3831 612 -227 382 N ANISOU 3344 CA GLN C 94 5538 2268 3954 673 -186 429 C ANISOU 3345 C GLN C 94 5554 2259 4056 749 -121 468 C ANISOU 3346 O GLN C 94 5558 2187 4019 778 -111 458 O ANISOU 3347 CB GLN C 94 5671 2447 3963 687 -213 426 C ANISOU 3348 CG GLN C 94 5667 2584 4005 756 -171 487 C ANISOU 3349 CD GLN C 94 5819 2812 4031 772 -201 481 C ANISOU 3350 OE1 GLN C 94 5790 2916 4023 830 -174 536 O ANISOU 3351 NE2 GLN C 94 5905 2808 3979 724 -261 415 N ANISOU 3352 N ASN C 95 5608 2380 4231 781 -77 516 N ANISOU 3353 CA ASN C 95 5678 2431 4402 834 -18 566 C ANISOU 3354 C ASN C 95 5908 2745 4624 904 19 638 C ANISOU 3355 O ASN C 95 5922 2831 4668 922 25 670 O ANISOU 3356 CB ASN C 95 5592 2325 4461 818 2 570 C ANISOU 3357 CG ASN C 95 5566 2267 4549 849 55 624 C ANISOU 3358 OD1 ASN C 95 5564 2278 4523 884 81 663 O ANISOU 3359 ND2 ASN C 95 5561 2225 4667 834 69 623 N ANISOU 3360 N LYS C 96 6182 3024 4856 953 47 669 N ANISOU 3361 CA LYS C 96 6498 3438 5151 1025 84 745 C ANISOU 3362 C LYS C 96 6606 3558 5413 1058 149 841 C ANISOU 3363 O LYS C 96 6803 3834 5622 1111 180 921 O ANISOU 3364 CB LYS C 96 6777 3734 5303 1072 86 733 C ANISOU 3365 CG LYS C 96 6931 3851 5287 1043 16 638 C ANISOU 3366 CD LYS C 96 7083 4096 5376 1030 -19 636 C ANISOU 3367 CE LYS C 96 7365 4338 5492 983 -96 544 C ANISOU 3368 NZ LYS C 96 7560 4665 5640 965 -132 550 N ANISOU 3369 N ASN C 97 6574 3447 5496 1022 166 838 N ANISOU 3370 CA ASN C 97 6857 3718 5932 1033 220 926 C ANISOU 3371 C ASN C 97 6938 3755 6088 1026 215 933 C ANISOU 3372 O ASN C 97 7237 4028 6362 994 172 853 O ANISOU 3373 CB ASN C 97 6840 3643 6021 987 232 917 C ANISOU 3374 CG ASN C 97 6857 3724 5987 1016 250 932 C ANISOU 3375 OD1 ASN C 97 6795 3665 5787 1031 217 865 O ANISOU 3376 ND2 ASN C 97 6864 3779 6104 1024 303 1023 N ANISOU 3377 N LYS C 98 7056 3868 6300 1064 263 1035 N ANISOU 3378 CA LYS C 98 6980 3728 6297 1079 265 1049 C ANISOU 3379 C LYS C 98 6650 3266 6070 1014 246 977 C ANISOU 3380 O LYS C 98 6699 3250 6156 1021 232 940 O ANISOU 3381 CB LYS C 98 7313 4062 6700 1138 320 1188 C ANISOU 3382 CG LYS C 98 7404 4309 6687 1213 339 1267 C ANISOU 3383 CD LYS C 98 7504 4503 6678 1250 300 1219 C ANISOU 3384 CE LYS C 98 7703 4870 6769 1321 312 1291 C ANISOU 3385 NZ LYS C 98 7919 5154 6885 1308 308 1265 N ANISOU 3386 N SER C 99 6405 2999 5867 958 247 958 N ANISOU 3387 CA SER C 99 6311 2807 5863 890 224 885 C ANISOU 3388 C SER C 99 6013 2533 5474 858 171 768 C ANISOU 3389 O SER C 99 5935 2531 5276 871 155 751 O ANISOU 3390 CB SER C 99 6373 2866 6022 844 247 929 C ANISOU 3391 OG SER C 99 6706 3179 6451 859 297 1051 O ANISOU 3392 N SER C 100 5818 2269 5335 814 143 689 N ANISOU 3393 CA SER C 100 5582 2062 5025 780 95 591 C ANISOU 3394 C SER C 100 5432 1928 4876 737 85 574 C ANISOU 3395 O SER C 100 5419 1906 4951 723 112 623 O ANISOU 3396 CB SER C 100 5589 2016 5078 765 71 515 C ANISOU 3397 OG SER C 100 5614 1949 5226 727 77 504 O ANISOU 3398 N GLN C 101 5308 1837 4655 717 47 514 N ANISOU 3399 CA GLN C 101 5201 1742 4532 691 32 494 C ANISOU 3400 C GLN C 101 5109 1641 4452 644 -9 413 C ANISOU 3401 O GLN C 101 5058 1584 4408 638 -23 373 O ANISOU 3402 CB GLN C 101 5200 1764 4385 715 18 496 C ANISOU 3403 CG GLN C 101 5237 1831 4369 771 49 560 C ANISOU 3404 CD GLN C 101 5231 1857 4444 803 102 637 C ANISOU 3405 OE1 GLN C 101 5222 1851 4540 778 114 647 O ANISOU 3406 NE2 GLN C 101 5258 1929 4419 858 131 697 N ANISOU 3407 N LYS C 102 5041 1589 4383 620 -27 391 N ANISOU 3408 CA LYS C 102 5005 1567 4346 580 -69 321 C ANISOU 3409 C LYS C 102 4986 1561 4231 581 -93 318 C ANISOU 3410 O LYS C 102 4989 1569 4231 608 -76 356 O ANISOU 3411 CB LYS C 102 5015 1578 4489 544 -72 290 C ANISOU 3412 CG LYS C 102 5075 1580 4634 543 -56 281 C ANISOU 3413 CD LYS C 102 5117 1601 4795 495 -74 227 C ANISOU 3414 CE LYS C 102 5118 1633 4897 459 -63 271 C ANISOU 3415 NZ LYS C 102 5159 1661 5053 396 -93 210 N ANISOU 3416 N ILE C 103 4991 1571 4149 559 -131 282 N ANISOU 3417 CA ILE C 103 5031 1594 4092 556 -160 282 C ANISOU 3418 C ILE C 103 5062 1675 4139 519 -195 241 C ANISOU 3419 O ILE C 103 4999 1658 4127 497 -200 203 O ANISOU 3420 CB ILE C 103 5046 1560 3970 555 -180 295 C ANISOU 3421 CG1 ILE C 103 5031 1592 3929 512 -203 273 C ANISOU 3422 CG2 ILE C 103 5097 1580 3989 598 -150 329 C ANISOU 3423 CD1 ILE C 103 5072 1603 3848 488 -231 288 C ANISOU 3424 N ASN C 104 5188 1790 4207 523 -219 250 N ANISOU 3425 CA ASN C 104 5271 1931 4284 494 -254 225 C ANISOU 3426 C ASN C 104 5353 1945 4242 502 -282 259 C ANISOU 3427 O ASN C 104 5285 1781 4105 535 -273 285 O ANISOU 3428 CB ASN C 104 5369 2111 4498 493 -254 200 C ANISOU 3429 CG ASN C 104 5507 2250 4662 533 -240 237 C ANISOU 3430 OD1 ASN C 104 5659 2381 4736 562 -258 262 O ANISOU 3431 ND2 ASN C 104 5528 2306 4800 536 -210 243 N ANISOU 3432 N LEU C 105 5457 2092 4310 476 -316 257 N ANISOU 3433 CA LEU C 105 5603 2151 4337 477 -347 298 C ANISOU 3434 C LEU C 105 5786 2388 4534 503 -365 310 C ANISOU 3435 O LEU C 105 5889 2624 4732 499 -363 280 O ANISOU 3436 CB LEU C 105 5635 2193 4299 413 -373 310 C ANISOU 3437 CG LEU C 105 5613 2145 4255 385 -363 305 C ANISOU 3438 CD1 LEU C 105 5713 2266 4280 314 -396 335 C ANISOU 3439 CD2 LEU C 105 5716 2109 4305 421 -352 314 C ANISOU 3440 N SER C 106 5992 2483 4637 532 -386 354 N ANISOU 3441 CA SER C 106 6063 2598 4704 570 -406 381 C ANISOU 3442 C SER C 106 6353 2756 4857 556 -443 437 C ANISOU 3443 O SER C 106 6334 2559 4742 553 -450 449 O ANISOU 3444 CB SER C 106 6066 2598 4745 654 -384 386 C ANISOU 3445 OG SER C 106 5846 2502 4664 649 -351 348 O ANISOU 3446 N ILE C 107 6611 3104 5107 540 -470 469 N ANISOU 3447 CA ILE C 107 6964 3343 5341 520 -507 540 C ANISOU 3448 C ILE C 107 7395 3858 5775 578 -524 582 C ANISOU 3449 O ILE C 107 7347 4026 5807 569 -524 562 O ANISOU 3450 CB ILE C 107 6923 3368 5279 418 -523 558 C ANISOU 3451 CG1 ILE C 107 6911 3323 5277 365 -507 517 C ANISOU 3452 CG2 ILE C 107 7055 3378 5294 384 -563 650 C ANISOU 3453 CD1 ILE C 107 7029 3202 5302 369 -517 527 C ANISOU 3454 N GLN C 108 7875 4163 6160 644 -541 637 N ANISOU 3455 CA GLN C 108 8122 4479 6398 715 -558 691 C ANISOU 3456 C GLN C 108 8508 4760 6672 675 -596 784 C ANISOU 3457 O GLN C 108 8645 4640 6699 655 -614 819 O ANISOU 3458 CB GLN C 108 8415 4669 6670 841 -545 694 C ANISOU 3459 CG GLN C 108 8965 5323 7222 931 -560 753 C ANISOU 3460 CD GLN C 108 9409 5702 7652 1071 -543 756 C ANISOU 3461 OE1 GLN C 108 10012 6183 8239 1103 -517 712 O ANISOU 3462 NE2 GLN C 108 9282 5681 7529 1164 -555 811 N ANISOU 3463 N SER C 109 8701 5156 6892 662 -611 826 N ANISOU 3464 CA SER C 109 9124 5529 7223 620 -645 931 C ANISOU 3465 C SER C 109 9086 5575 7166 712 -662 1005 C ANISOU 3466 O SER C 109 8701 5418 6872 770 -653 964 O ANISOU 3467 CB SER C 109 9009 5612 7143 510 -645 929 C ANISOU 3468 OG SER C 109 9269 5854 7319 464 -674 1047 O ANISOU 3469 N LYS C 110 9504 5802 7468 720 -692 1120 N ANISOU 3470 CA LYS C 110 9997 6344 7921 811 -712 1217 C ANISOU 3471 C LYS C 110 10192 6565 8154 958 -699 1180 C ANISOU 3472 O LYS C 110 10242 6811 8231 1037 -708 1223 O ANISOU 3473 CB LYS C 110 9959 6649 7934 767 -720 1247 C ANISOU 3474 CG LYS C 110 10058 6776 7997 632 -729 1300 C ANISOU 3475 CD LYS C 110 10513 6959 8325 599 -758 1445 C ANISOU 3476 CE LYS C 110 10739 7245 8530 452 -765 1507 C ANISOU 3477 NZ LYS C 110 10811 7282 8647 362 -747 1403 N ANISOU 3478 N ASN C 111 10782 6988 8748 996 -677 1103 N ANISOU 3479 CA ASN C 111 10919 7152 8920 1138 -658 1073 C ANISOU 3480 C ASN C 111 10688 7300 8847 1153 -641 1015 C ANISOU 3481 O ASN C 111 10627 7338 8831 1269 -631 1013 O ANISOU 3482 CB ASN C 111 11147 7222 9040 1271 -681 1177 C ANISOU 3483 CG ASN C 111 11559 7210 9290 1263 -704 1223 C ANISOU 3484 OD1 ASN C 111 11646 7081 9334 1279 -692 1155 O ANISOU 3485 ND2 ASN C 111 11356 6885 8994 1238 -740 1340 N ANISOU 3486 N MSE C 112 10328 7153 8570 1039 -641 965 N ANISOU 3487 CA MSE C 112 10196 7350 8583 1043 -634 898 C ANISOU 3488 C MSE C 112 9364 6638 7836 920 -622 801 C ANISOU 3489 O MSE C 112 9739 7141 8331 910 -603 716 O ANISOU 3490 CB MSE C 112 10700 8087 9088 1088 -666 965 C ANISOU 3491 CG MSE C 112 11067 8525 9398 1005 -690 1011 C ANISOU 3492 SE MSE C 112 11771 9523 10081 1088 -731 1116 SE ANISOU 3493 CE MSE C 112 11604 9033 9787 1245 -735 1254 C ANISOU 3494 N PHE C 113 8695 5928 7108 830 -632 818 N ANISOU 3495 CA PHE C 113 8250 5602 6730 731 -622 730 C ANISOU 3496 C PHE C 113 8019 5198 6524 696 -590 666 C ANISOU 3497 O PHE C 113 7618 4561 6035 681 -586 703 O ANISOU 3498 CB PHE C 113 8373 5767 6777 660 -640 784 C ANISOU 3499 CG PHE C 113 8586 6189 6964 691 -669 849 C ANISOU 3500 CD1 PHE C 113 8554 6448 7018 706 -681 779 C ANISOU 3501 CD2 PHE C 113 9009 6513 7274 706 -689 985 C ANISOU 3502 CE1 PHE C 113 8626 6735 7058 739 -711 839 C ANISOU 3503 CE2 PHE C 113 9167 6877 7405 742 -715 1058 C ANISOU 3504 CZ PHE C 113 8968 6994 7287 762 -726 983 C ANISOU 3505 N GLU C 114 7843 5147 6469 678 -570 569 N ANISOU 3506 CA GLU C 114 7761 4941 6425 649 -538 511 C ANISOU 3507 C GLU C 114 7687 4949 6386 564 -533 447 C ANISOU 3508 O GLU C 114 7494 4955 6235 542 -549 407 O ANISOU 3509 CB GLU C 114 7900 5144 6679 693 -516 464 C ANISOU 3510 CG GLU C 114 8348 5534 7097 795 -513 524 C ANISOU 3511 CD GLU C 114 8714 5623 7341 838 -501 567 C ANISOU 3512 OE1 GLU C 114 8638 5406 7212 774 -496 552 O ANISOU 3513 OE2 GLU C 114 9310 6150 7892 939 -499 611 O ANISOU 3514 N PHE C 115 7691 4807 6364 526 -512 434 N ANISOU 3515 CA PHE C 115 7458 4646 6160 462 -503 378 C ANISOU 3516 C PHE C 115 7377 4492 6153 460 -469 317 C ANISOU 3517 O PHE C 115 7260 4225 6018 489 -452 339 O ANISOU 3518 CB PHE C 115 7522 4657 6123 410 -514 436 C ANISOU 3519 CG PHE C 115 7642 4866 6174 404 -545 511 C ANISOU 3520 CD1 PHE C 115 7742 4874 6216 451 -564 588 C ANISOU 3521 CD2 PHE C 115 7586 5004 6112 364 -553 506 C ANISOU 3522 CE1 PHE C 115 7687 4902 6097 450 -592 670 C ANISOU 3523 CE2 PHE C 115 7599 5122 6062 361 -579 586 C ANISOU 3524 CZ PHE C 115 7599 5017 6006 400 -598 673 C ANISOU 3525 N ARG C 116 7151 4376 6005 432 -460 240 N ANISOU 3526 CA ARG C 116 7204 4373 6137 428 -429 187 C ANISOU 3527 C ARG C 116 6773 3987 5704 395 -422 142 C ANISOU 3528 O ARG C 116 6558 3893 5450 378 -441 134 O ANISOU 3529 CB ARG C 116 7511 4767 6568 438 -428 129 C ANISOU 3530 CG ARG C 116 8098 5372 7179 478 -434 171 C ANISOU 3531 CD ARG C 116 8835 5967 7898 519 -404 223 C ANISOU 3532 NE ARG C 116 9571 6663 8723 507 -369 194 N ANISOU 3533 CZ ARG C 116 10099 7099 9252 543 -336 230 C ANISOU 3534 NH1 ARG C 116 10371 7301 9439 601 -335 284 N ANISOU 3535 NH2 ARG C 116 9939 6919 9177 528 -304 213 N ANISOU 3536 N LEU C 117 6571 3706 5546 395 -392 116 N ANISOU 3537 CA LEU C 117 6343 3520 5320 382 -381 76 C ANISOU 3538 C LEU C 117 6326 3640 5352 385 -396 -8 C ANISOU 3539 O LEU C 117 6432 3754 5540 389 -402 -58 O ANISOU 3540 CB LEU C 117 6225 3292 5253 396 -346 67 C ANISOU 3541 CG LEU C 117 6184 3129 5149 397 -333 136 C ANISOU 3542 CD1 LEU C 117 6068 2947 5077 415 -299 129 C ANISOU 3543 CD2 LEU C 117 6070 3032 4928 364 -354 182 C ANISOU 3544 N LYS C 118 6315 3748 5288 381 -404 -24 N ANISOU 3545 CA LYS C 118 6347 3922 5338 396 -420 -114 C ANISOU 3546 C LYS C 118 6170 3693 5228 421 -401 -203 C ANISOU 3547 O LYS C 118 5971 3476 5010 439 -376 -194 O ANISOU 3548 CB LYS C 118 6515 4262 5418 393 -431 -91 C ANISOU 3549 CG LYS C 118 6769 4683 5671 424 -446 -195 C ANISOU 3550 CD LYS C 118 6975 5097 5789 429 -449 -160 C ANISOU 3551 CE LYS C 118 7112 5411 5912 477 -462 -277 C ANISOU 3552 NZ LYS C 118 7250 5591 6071 478 -500 -344 N ANISOU 3553 N GLU C 119 6308 3811 5442 423 -417 -288 N ANISOU 3554 CA GLU C 119 6326 3743 5526 444 -406 -376 C ANISOU 3555 C GLU C 119 6402 3910 5541 493 -399 -431 C ANISOU 3556 O GLU C 119 6420 4100 5492 504 -419 -457 O ANISOU 3557 CB GLU C 119 6494 3911 5771 422 -441 -470 C ANISOU 3558 CG GLU C 119 6768 4050 6120 433 -437 -562 C ANISOU 3559 CD GLU C 119 6920 4020 6352 422 -400 -498 C ANISOU 3560 OE1 GLU C 119 6986 4072 6409 410 -376 -389 O ANISOU 3561 OE2 GLU C 119 7121 4089 6617 427 -396 -556 O ANISOU 3562 N GLY C 120 6441 3851 5601 529 -367 -440 N ANISOU 3563 CA GLY C 120 6394 3895 5504 594 -356 -492 C ANISOU 3564 C GLY C 120 6254 3896 5287 597 -337 -400 C ANISOU 3565 O GLY C 120 6210 3959 5206 655 -321 -427 O ANISOU 3566 N SER C 121 6243 3895 5249 537 -341 -293 N ANISOU 3567 CA SER C 121 6285 4052 5223 520 -330 -201 C ANISOU 3568 C SER C 121 6403 4088 5364 541 -299 -167 C ANISOU 3569 O SER C 121 6251 3762 5273 552 -286 -179 O ANISOU 3570 CB SER C 121 6299 4058 5194 450 -349 -102 C ANISOU 3571 OG SER C 121 6296 4159 5164 438 -378 -119 O ANISOU 3572 N GLU C 122 6657 4490 5574 546 -288 -119 N ANISOU 3573 CA GLU C 122 6964 4759 5899 568 -262 -81 C ANISOU 3574 C GLU C 122 6727 4466 5631 490 -271 22 C ANISOU 3575 O GLU C 122 6949 4760 5798 423 -295 81 O ANISOU 3576 CB GLU C 122 7461 5467 6375 627 -245 -91 C ANISOU 3577 CG GLU C 122 7996 6033 6927 727 -234 -209 C ANISOU 3578 CD GLU C 122 8497 6750 7405 811 -211 -221 C ANISOU 3579 OE1 GLU C 122 8589 6996 7478 779 -204 -128 O ANISOU 3580 OE2 GLU C 122 9049 7318 7956 910 -203 -327 O ANISOU 3581 N VAL C 123 6439 4036 5372 502 -255 43 N ANISOU 3582 CA VAL C 123 6406 3932 5301 441 -265 124 C ANISOU 3583 C VAL C 123 6431 4023 5332 470 -247 152 C ANISOU 3584 O VAL C 123 6394 3983 5344 551 -219 113 O ANISOU 3585 CB VAL C 123 6297 3612 5211 433 -265 126 C ANISOU 3586 CG1 VAL C 123 6161 3449 5073 409 -286 104 C ANISOU 3587 CG2 VAL C 123 6229 3439 5220 497 -233 90 C ANISOU 3588 N PHE C 124 6533 4177 5381 404 -267 222 N ANISOU 3589 CA PHE C 124 6628 4379 5478 421 -257 256 C ANISOU 3590 C PHE C 124 6399 4001 5228 404 -262 289 C ANISOU 3591 O PHE C 124 6116 3603 4891 334 -290 313 O ANISOU 3592 CB PHE C 124 6900 4875 5711 350 -282 308 C ANISOU 3593 CG PHE C 124 7155 5300 5977 374 -275 280 C ANISOU 3594 CD1 PHE C 124 7373 5626 6238 485 -242 221 C ANISOU 3595 CD2 PHE C 124 7461 5633 6243 299 -302 306 C ANISOU 3596 CE1 PHE C 124 7597 6008 6457 519 -236 182 C ANISOU 3597 CE2 PHE C 124 7691 6036 6474 328 -294 280 C ANISOU 3598 CZ PHE C 124 7570 6040 6389 439 -262 212 C ANISOU 3599 N LEU C 125 6311 3917 5177 477 -233 289 N ANISOU 3600 CA LEU C 125 6326 3824 5169 477 -232 321 C ANISOU 3601 C LEU C 125 6247 3914 5079 488 -235 363 C ANISOU 3602 O LEU C 125 6262 4020 5145 577 -204 362 O ANISOU 3603 CB LEU C 125 6425 3765 5326 557 -193 301 C ANISOU 3604 CG LEU C 125 6614 3799 5541 547 -190 264 C ANISOU 3605 CD1 LEU C 125 6618 3847 5598 574 -183 207 C ANISOU 3606 CD2 LEU C 125 6756 3793 5725 591 -159 278 C ANISOU 3607 N GLU C 126 6105 3803 4867 398 -277 399 N ANISOU 3608 CA GLU C 126 5998 3872 4745 390 -291 440 C ANISOU 3609 C GLU C 126 6069 3831 4787 428 -285 451 C ANISOU 3610 O GLU C 126 5974 3599 4620 368 -315 447 O ANISOU 3611 CB GLU C 126 5929 3904 4614 255 -351 472 C ANISOU 3612 CG GLU C 126 5841 4018 4517 237 -373 512 C ANISOU 3613 CD GLU C 126 5763 4026 4379 84 -441 545 C ANISOU 3614 OE1 GLU C 126 5704 3843 4279 -11 -473 543 O ANISOU 3615 OE2 GLU C 126 5725 4178 4339 58 -465 577 O ANISOU 3616 N GLY C 127 6160 3977 4930 536 -243 466 N ANISOU 3617 CA GLY C 127 6305 4060 5051 583 -231 491 C ANISOU 3618 C GLY C 127 6497 4433 5186 536 -273 525 C ANISOU 3619 O GLY C 127 6656 4723 5321 441 -318 527 O ANISOU 3620 N LYS C 128 6705 4666 5377 600 -260 556 N ANISOU 3621 CA LYS C 128 6769 4915 5385 561 -304 584 C ANISOU 3622 C LYS C 128 6514 4944 5193 588 -302 618 C ANISOU 3623 O LYS C 128 6377 5000 5028 497 -354 631 O ANISOU 3624 CB LYS C 128 7040 5164 5621 640 -285 613 C ANISOU 3625 CG LYS C 128 7335 5668 5851 606 -335 636 C ANISOU 3626 CD LYS C 128 7655 5992 6129 696 -314 670 C ANISOU 3627 CE LYS C 128 7815 6385 6221 661 -371 687 C ANISOU 3628 NZ LYS C 128 7900 6495 6259 760 -348 725 N ANISOU 3629 N ASN C 129 6488 4938 5251 713 -243 632 N ANISOU 3630 CA ASN C 129 6520 5239 5341 776 -231 663 C ANISOU 3631 C ASN C 129 6399 5107 5283 819 -199 629 C ANISOU 3632 O ASN C 129 6426 5379 5346 856 -195 645 O ANISOU 3633 CB ASN C 129 6570 5362 5422 924 -190 717 C ANISOU 3634 CG ASN C 129 6696 5567 5483 904 -221 758 C ANISOU 3635 OD1 ASN C 129 6809 5530 5576 963 -195 777 O ANISOU 3636 ND2 ASN C 129 6623 5740 5375 814 -279 771 N ANISOU 3637 N ILE C 130 6333 4784 5227 816 -178 580 N ANISOU 3638 CA ILE C 130 6294 4736 5241 867 -151 536 C ANISOU 3639 C ILE C 130 6192 4496 5117 765 -172 485 C ANISOU 3640 O ILE C 130 6314 4398 5214 718 -178 470 O ANISOU 3641 CB ILE C 130 6362 4631 5365 1007 -96 523 C ANISOU 3642 CG1 ILE C 130 6595 4970 5618 1124 -71 586 C ANISOU 3643 CG2 ILE C 130 6311 4559 5355 1065 -75 459 C ANISOU 3644 CD1 ILE C 130 6643 5327 5682 1186 -72 607 C ANISOU 3645 N ILE C 131 6068 4525 5006 745 -178 464 N ANISOU 3646 CA ILE C 131 5993 4356 4915 667 -194 423 C ANISOU 3647 C ILE C 131 5883 4218 4853 771 -157 361 C ANISOU 3648 O ILE C 131 5774 4296 4771 862 -135 357 O ANISOU 3649 CB ILE C 131 5999 4558 4885 542 -237 455 C ANISOU 3650 CG1 ILE C 131 6101 4538 4965 473 -251 422 C ANISOU 3651 CG2 ILE C 131 5974 4865 4894 590 -226 479 C ANISOU 3652 CD1 ILE C 131 6118 4723 4949 345 -292 467 C ANISOU 3653 N TYR C 132 5850 3956 4828 762 -151 310 N ANISOU 3654 CA TYR C 132 5868 3921 4883 846 -127 236 C ANISOU 3655 C TYR C 132 5770 3700 4770 769 -147 193 C ANISOU 3656 O TYR C 132 5739 3584 4706 672 -172 225 O ANISOU 3657 CB TYR C 132 5902 3770 4969 956 -91 215 C ANISOU 3658 CG TYR C 132 5890 3506 4973 914 -89 227 C ANISOU 3659 CD1 TYR C 132 5850 3442 4902 860 -98 293 C ANISOU 3660 CD2 TYR C 132 5926 3347 5051 922 -81 167 C ANISOU 3661 CE1 TYR C 132 5892 3283 4956 834 -92 305 C ANISOU 3662 CE2 TYR C 132 5888 3116 5038 883 -77 186 C ANISOU 3663 CZ TYR C 132 5893 3112 5011 844 -79 257 C ANISOU 3664 OH TYR C 132 5765 2821 4905 817 -70 277 O ANISOU 3665 N SER C 133 5793 3715 4812 821 -138 117 N ANISOU 3666 CA SER C 133 5827 3663 4836 762 -158 72 C ANISOU 3667 C SER C 133 5887 3485 4950 804 -146 9 C ANISOU 3668 O SER C 133 5939 3460 5044 894 -120 -16 O ANISOU 3669 CB SER C 133 5868 3908 4850 775 -166 32 C ANISOU 3670 OG SER C 133 5898 3980 4902 900 -141 -41 O ANISOU 3671 N ASP C 134 5845 3326 4910 735 -165 -6 N ANISOU 3672 CA ASP C 134 5989 3270 5116 752 -159 -59 C ANISOU 3673 C ASP C 134 6070 3362 5184 695 -189 -104 C ANISOU 3674 O ASP C 134 5924 3353 4978 647 -210 -77 O ANISOU 3675 CB ASP C 134 6013 3136 5173 735 -143 4 C ANISOU 3676 CG ASP C 134 6153 3083 5397 755 -129 -27 C ANISOU 3677 OD1 ASP C 134 6207 3100 5484 779 -138 -112 O ANISOU 3678 OD2 ASP C 134 6280 3105 5556 745 -111 33 O ANISOU 3679 N LYS C 135 6180 3337 5351 696 -195 -166 N ANISOU 3680 CA LYS C 135 6260 3449 5422 648 -227 -210 C ANISOU 3681 C LYS C 135 6320 3377 5527 591 -233 -177 C ANISOU 3682 O LYS C 135 6313 3237 5578 596 -211 -145 O ANISOU 3683 CB LYS C 135 6418 3609 5601 693 -240 -330 C ANISOU 3684 CG LYS C 135 6551 3902 5679 767 -234 -378 C ANISOU 3685 CD LYS C 135 6695 4035 5827 821 -252 -514 C ANISOU 3686 CE LYS C 135 6833 4354 5900 915 -240 -563 C ANISOU 3687 NZ LYS C 135 6988 4484 6042 977 -262 -714 N ANISOU 3688 N ILE C 136 6385 3506 5566 543 -262 -180 N ANISOU 3689 CA ILE C 136 6470 3512 5688 499 -272 -153 C ANISOU 3690 C ILE C 136 6765 3736 6078 499 -280 -231 C ANISOU 3691 O ILE C 136 6714 3754 6024 504 -307 -318 O ANISOU 3692 CB ILE C 136 6380 3525 5530 462 -301 -124 C ANISOU 3693 CG1 ILE C 136 6311 3506 5370 448 -298 -47 C ANISOU 3694 CG2 ILE C 136 6381 3467 5567 434 -311 -96 C ANISOU 3695 CD1 ILE C 136 6280 3556 5266 409 -328 -5 C ANISOU 3696 N LYS C 137 7081 3919 6475 492 -259 -201 N ANISOU 3697 CA LYS C 137 7536 4286 7035 472 -268 -260 C ANISOU 3698 C LYS C 137 7766 4518 7330 419 -276 -218 C ANISOU 3699 O LYS C 137 8325 5044 7897 418 -248 -128 O ANISOU 3700 CB LYS C 137 7778 4382 7334 505 -234 -243 C ANISOU 3701 CG LYS C 137 8041 4651 7540 576 -222 -278 C ANISOU 3702 CD LYS C 137 8293 4755 7846 621 -188 -249 C ANISOU 3703 CE LYS C 137 8358 4849 7852 709 -175 -279 C ANISOU 3704 NZ LYS C 137 8240 4896 7643 724 -164 -218 N ANISOU 3705 N GLU C 138 7909 4716 7516 380 -316 -287 N ANISOU 3706 CA GLU C 138 7882 4734 7559 333 -328 -252 C ANISOU 3707 C GLU C 138 7470 4397 7066 352 -318 -166 C ANISOU 3708 O GLU C 138 7548 4480 7184 344 -303 -97 O ANISOU 3709 CB GLU C 138 8424 5168 8227 302 -303 -209 C ANISOU 3710 CG GLU C 138 8850 5484 8735 273 -321 -296 C ANISOU 3711 CD GLU C 138 9315 5833 9334 228 -298 -239 C ANISOU 3712 OE1 GLU C 138 9635 6185 9684 227 -261 -129 O ANISOU 3713 OE2 GLU C 138 9647 6044 9738 194 -318 -306 O ANISOU 3714 N GLY C 139 7044 4029 6524 378 -328 -170 N ANISOU 3715 CA GLY C 139 6687 3713 6075 391 -327 -95 C ANISOU 3716 C GLY C 139 6468 3396 5819 413 -290 -14 C ANISOU 3717 O GLY C 139 6210 3130 5497 424 -290 45 O ANISOU 3718 N OCS C 140 6342 3192 5722 427 -260 -15 N ANISOU 3719 CA OCS C 140 6299 3074 5642 451 -227 55 C ANISOU 3720 CB OCS C 140 6692 3401 6135 457 -193 90 C ANISOU 3721 SG OCS C 140 7132 3876 6629 449 -189 135 S ANISOU 3722 C OCS C 140 5927 2693 5219 471 -216 51 C ANISOU 3723 O OCS C 140 5797 2592 5108 479 -222 -7 O ANISOU 3724 OD1 OCS C 140 7229 3969 6877 411 -185 112 O ANISOU 3725 OD2 OCS C 140 7432 4134 6891 487 -154 208 O ANISOU 3726 OD3 OCS C 140 7269 4089 6717 440 -227 111 O ANISOU 3727 N ILE C 141 5677 2411 4899 485 -201 111 N ANISOU 3728 CA ILE C 141 5558 2305 4737 505 -189 122 C ANISOU 3729 C ILE C 141 5466 2140 4691 538 -151 165 C ANISOU 3730 O ILE C 141 5335 1965 4558 543 -137 211 O ANISOU 3731 CB ILE C 141 5592 2375 4654 483 -210 158 C ANISOU 3732 CG1 ILE C 141 5640 2495 4652 446 -247 140 C ANISOU 3733 CG2 ILE C 141 5589 2424 4624 500 -200 171 C ANISOU 3734 CD1 ILE C 141 5733 2604 4637 407 -272 185 C ANISOU 3735 N GLU C 142 5386 2055 4650 571 -132 155 N ANISOU 3736 CA GLU C 142 5403 2008 4710 608 -94 210 C ANISOU 3737 C GLU C 142 5263 1916 4485 633 -87 257 C ANISOU 3738 O GLU C 142 5268 1995 4455 647 -97 239 O ANISOU 3739 CB GLU C 142 5587 2134 4984 639 -77 182 C ANISOU 3740 CG GLU C 142 5758 2237 5203 678 -35 257 C ANISOU 3741 CD GLU C 142 6002 2385 5532 713 -20 239 C ANISOU 3742 OE1 GLU C 142 6109 2477 5653 713 -43 152 O ANISOU 3743 OE2 GLU C 142 6265 2582 5840 745 14 313 O ANISOU 3744 N VAL C 143 5176 1803 4363 641 -72 315 N ANISOU 3745 CA VAL C 143 5164 1836 4267 662 -71 356 C ANISOU 3746 C VAL C 143 5195 1850 4359 720 -28 409 C ANISOU 3747 O VAL C 143 5205 1810 4415 736 1 454 O ANISOU 3748 CB VAL C 143 5166 1815 4176 646 -84 377 C ANISOU 3749 CG1 VAL C 143 5203 1899 4119 660 -92 406 C ANISOU 3750 CG2 VAL C 143 5143 1777 4097 594 -125 337 C ANISOU 3751 N PRO C 144 5264 1971 4436 760 -21 415 N ANISOU 3752 CA PRO C 144 5346 2024 4577 825 19 476 C ANISOU 3753 C PRO C 144 5398 2111 4580 856 40 555 C ANISOU 3754 O PRO C 144 5379 2164 4457 840 16 554 O ANISOU 3755 CB PRO C 144 5363 2113 4592 872 15 458 C ANISOU 3756 CG PRO C 144 5308 2176 4454 824 -27 410 C ANISOU 3757 CD PRO C 144 5241 2049 4370 751 -50 373 C ANISOU 3758 N GLY C 145 5529 2187 4784 900 84 625 N ANISOU 3759 CA GLY C 145 5598 2305 4812 943 111 710 C ANISOU 3760 C GLY C 145 5636 2473 4744 971 90 716 C ANISOU 3761 O GLY C 145 5628 2519 4743 993 77 698 O ANISOU 3762 N GLU C 146 5720 2619 4730 972 82 737 N ANISOU 3763 CA GLU C 146 5884 2913 4786 985 53 739 C ANISOU 3764 C GLU C 146 5949 3022 4795 917 -4 660 C ANISOU 3765 O GLU C 146 6076 3270 4842 907 -37 657 O ANISOU 3766 CB GLU C 146 5982 3101 4917 1065 80 815 C ANISOU 3767 CG GLU C 146 6126 3222 5107 1133 137 917 C ANISOU 3768 CD GLU C 146 6262 3445 5266 1222 163 1003 C ANISOU 3769 OE1 GLU C 146 6587 3755 5632 1280 211 1104 O ANISOU 3770 OE2 GLU C 146 6247 3530 5227 1236 135 978 O ANISOU 3771 N PHE C 147 6023 3015 4910 864 -17 602 N ANISOU 3772 CA PHE C 147 6090 3136 4928 796 -68 543 C ANISOU 3773 C PHE C 147 6186 3247 4894 742 -115 524 C ANISOU 3774 O PHE C 147 6138 3107 4797 744 -112 519 O ANISOU 3775 CB PHE C 147 6153 3109 5036 748 -77 487 C ANISOU 3776 CG PHE C 147 6158 3184 4997 679 -125 443 C ANISOU 3777 CD1 PHE C 147 6237 3399 5103 692 -129 441 C ANISOU 3778 CD2 PHE C 147 6331 3299 5096 607 -164 413 C ANISOU 3779 CE1 PHE C 147 6236 3493 5068 625 -168 414 C ANISOU 3780 CE2 PHE C 147 6283 3319 5012 535 -206 390 C ANISOU 3781 CZ PHE C 147 6239 3432 5004 540 -207 394 C ANISOU 3782 N GLU C 148 6302 3479 4957 693 -160 509 N ANISOU 3783 CA GLU C 148 6394 3574 4925 622 -217 484 C ANISOU 3784 C GLU C 148 6349 3624 4874 534 -264 464 C ANISOU 3785 O GLU C 148 6450 3905 5002 538 -270 488 O ANISOU 3786 CB GLU C 148 6563 3840 5028 661 -222 515 C ANISOU 3787 CG GLU C 148 6711 3979 5036 584 -292 475 C ANISOU 3788 CD GLU C 148 6905 4286 5152 621 -305 494 C ANISOU 3789 OE1 GLU C 148 7325 4803 5629 716 -254 553 O ANISOU 3790 OE2 GLU C 148 6868 4239 4994 554 -369 450 O ANISOU 3791 N GLY C 149 6338 3507 4832 459 -295 429 N ANISOU 3792 CA GLY C 149 6298 3568 4792 370 -335 425 C ANISOU 3793 C GLY C 149 6193 3330 4654 296 -364 400 C ANISOU 3794 O GLY C 149 6217 3173 4610 291 -377 378 O ANISOU 3795 N LYS C 150 6078 3318 4586 253 -371 406 N ANISOU 3796 CA LYS C 150 6111 3265 4590 179 -401 399 C ANISOU 3797 C LYS C 150 6012 3208 4579 222 -364 387 C ANISOU 3798 O LYS C 150 5880 3252 4512 251 -342 392 O ANISOU 3799 CB LYS C 150 6200 3478 4637 61 -456 431 C ANISOU 3800 CG LYS C 150 6328 3602 4684 8 -502 434 C ANISOU 3801 CD LYS C 150 6413 3837 4747 -125 -561 472 C ANISOU 3802 CE LYS C 150 6643 4079 4899 -182 -614 465 C ANISOU 3803 NZ LYS C 150 6634 4233 4933 -83 -577 467 N ANISOU 3804 N ILE C 151 6096 3140 4656 229 -360 367 N ANISOU 3805 CA ILE C 151 6026 3102 4659 263 -334 345 C ANISOU 3806 C ILE C 151 6246 3331 4839 186 -371 361 C ANISOU 3807 O ILE C 151 6254 3185 4781 151 -398 371 O ANISOU 3808 CB ILE C 151 5907 2845 4585 335 -300 317 C ANISOU 3809 CG1 ILE C 151 5816 2746 4536 406 -262 321 C ANISOU 3810 CG2 ILE C 151 5851 2825 4601 357 -284 284 C ANISOU 3811 CD1 ILE C 151 5773 2588 4548 464 -226 309 C ANISOU 3812 N TYR C 152 8198 7356 4018 900 -1496 1579 N ANISOU 3813 CA TYR C 152 8355 7654 4424 911 -1437 1456 C ANISOU 3814 C TYR C 152 8340 7421 4456 865 -1377 1468 C ANISOU 3815 O TYR C 152 8618 7430 4622 914 -1431 1551 O ANISOU 3816 CB TYR C 152 8646 8075 4822 1074 -1526 1408 C ANISOU 3817 CG TYR C 152 8780 8364 5202 1102 -1486 1289 C ANISOU 3818 CD1 TYR C 152 8902 8320 5413 1103 -1443 1274 C ANISOU 3819 CD2 TYR C 152 8964 8862 5518 1125 -1500 1195 C ANISOU 3820 CE1 TYR C 152 8781 8342 5507 1127 -1409 1169 C ANISOU 3821 CE2 TYR C 152 8760 8804 5525 1138 -1467 1092 C ANISOU 3822 CZ TYR C 152 8717 8592 5569 1143 -1421 1079 C ANISOU 3823 OH TYR C 152 9077 9097 6128 1151 -1389 980 O ANISOU 3824 N VAL C 153 8095 7285 4365 773 -1271 1383 N ANISOU 3825 CA VAL C 153 8223 7253 4558 720 -1208 1383 C ANISOU 3826 C VAL C 153 7953 7147 4527 723 -1146 1254 C ANISOU 3827 O VAL C 153 7840 7205 4481 646 -1074 1183 O ANISOU 3828 CB VAL C 153 8279 7238 4500 568 -1129 1442 C ANISOU 3829 CG1 VAL C 153 8254 7094 4561 505 -1060 1432 C ANISOU 3830 CG2 VAL C 153 8819 7599 4784 542 -1190 1578 C ANISOU 3831 N ASN C 154 8088 7211 4772 814 -1177 1226 N ANISOU 3832 CA ASN C 154 8144 7404 5044 818 -1127 1113 C ANISOU 3833 C ASN C 154 7924 7116 4874 702 -1025 1097 C ANISOU 3834 O ASN C 154 7925 6933 4762 642 -1007 1179 O ANISOU 3835 CB ASN C 154 8488 7702 5474 953 -1191 1092 C ANISOU 3836 CG ASN C 154 8716 8081 5918 956 -1147 980 C ANISOU 3837 OD1 ASN C 154 8952 8426 6237 857 -1069 917 O ANISOU 3838 ND2 ASN C 154 8952 8314 6234 1076 -1198 954 N ANISOU 3839 N PHE C 155 7675 7020 4782 664 -961 994 N ANISOU 3840 CA PHE C 155 7816 7123 4983 572 -867 968 C ANISOU 3841 C PHE C 155 7274 6396 4492 589 -865 994 C ANISOU 3842 O PHE C 155 7042 6092 4265 508 -801 1010 O ANISOU 3843 CB PHE C 155 7916 7395 5218 539 -810 851 C ANISOU 3844 CG PHE C 155 8475 8109 5713 497 -793 811 C ANISOU 3845 CD1 PHE C 155 9041 8668 6148 434 -754 854 C ANISOU 3846 CD2 PHE C 155 8969 8756 6276 506 -808 720 C ANISOU 3847 CE1 PHE C 155 9093 8852 6130 401 -737 808 C ANISOU 3848 CE2 PHE C 155 9092 8990 6319 460 -794 677 C ANISOU 3849 CZ PHE C 155 9141 9020 6233 415 -759 718 C ANISOU 3850 N ASN C 156 7046 6103 4299 697 -936 994 N ANISOU 3851 CA ASN C 156 6998 5862 4284 718 -938 1012 C ANISOU 3852 C ASN C 156 7086 5691 4178 683 -967 1132 C ANISOU 3853 O ASN C 156 7309 5708 4381 679 -972 1162 O ANISOU 3854 CB ASN C 156 7217 6096 4595 852 -1001 965 C ANISOU 3855 CG ASN C 156 7547 6387 4810 976 -1104 1015 C ANISOU 3856 OD1 ASN C 156 8017 6779 5114 958 -1136 1096 O ANISOU 3857 ND2 ASN C 156 7833 6727 5177 1109 -1160 968 N ANISOU 3858 N SER C 157 7273 5881 4208 649 -987 1201 N ANISOU 3859 CA SER C 157 7537 5901 4261 593 -1016 1324 C ANISOU 3860 C SER C 157 7441 5857 4136 430 -922 1350 C ANISOU 3861 O SER C 157 7638 5912 4153 343 -930 1453 O ANISOU 3862 CB SER C 157 7596 5912 4147 656 -1103 1394 C ANISOU 3863 OG SER C 157 7641 5920 4219 822 -1192 1369 O ANISOU 3864 N LEU C 158 7288 5918 4153 392 -838 1255 N ANISOU 3865 CA LEU C 158 7248 5974 4116 264 -744 1258 C ANISOU 3866 C LEU C 158 7283 5964 4291 239 -697 1216 C ANISOU 3867 O LEU C 158 7501 6232 4664 314 -699 1129 O ANISOU 3868 CB LEU C 158 7062 6047 3989 260 -694 1179 C ANISOU 3869 CG LEU C 158 7264 6313 4059 288 -743 1209 C ANISOU 3870 CD1 LEU C 158 7182 6459 3995 252 -679 1139 C ANISOU 3871 CD2 LEU C 158 7594 6488 4175 232 -781 1342 C ANISOU 3872 N ILE C 159 7521 6119 4469 128 -658 1279 N ANISOU 3873 CA ILE C 159 7424 5972 4491 98 -620 1247 C ANISOU 3874 C ILE C 159 7695 6374 4774 -31 -531 1260 C ANISOU 3875 O ILE C 159 8009 6745 4957 -118 -511 1328 O ANISOU 3876 CB ILE C 159 7583 5826 4556 113 -694 1315 C ANISOU 3877 CG1 ILE C 159 7635 5816 4737 101 -666 1270 C ANISOU 3878 CG2 ILE C 159 7917 5985 4656 4 -721 1446 C ANISOU 3879 CD1 ILE C 159 7769 5628 4764 124 -740 1324 C ANISOU 3880 N ASN C 160 7594 6335 4833 -39 -480 1193 N ANISOU 3881 CA ASN C 160 7804 6692 5091 -140 -396 1190 C ANISOU 3882 C ASN C 160 8111 6813 5372 -219 -411 1249 C ANISOU 3883 O ASN C 160 8076 6719 5461 -180 -412 1196 O ANISOU 3884 CB ASN C 160 7421 6506 4892 -81 -337 1068 C ANISOU 3885 CG ASN C 160 7303 6565 4838 -156 -253 1052 C ANISOU 3886 OD1 ASN C 160 7636 6909 5300 -147 -229 1001 O ANISOU 3887 ND2 ASN C 160 7346 6768 4793 -226 -209 1091 N ANISOU 3888 N GLU C 161 8512 7116 5598 -338 -425 1362 N ANISOU 3889 CA GLU C 161 9119 7507 6122 -441 -451 1436 C ANISOU 3890 C GLU C 161 8849 7311 6026 -459 -402 1371 C ANISOU 3891 O GLU C 161 9177 7421 6366 -434 -445 1366 O ANISOU 3892 CB GLU C 161 9664 8067 6478 -610 -437 1553 C ANISOU 3893 CG GLU C 161 10026 8179 6697 -753 -472 1648 C ANISOU 3894 CD GLU C 161 10113 8350 6908 -837 -421 1619 C ANISOU 3895 OE1 GLU C 161 9484 7991 6493 -779 -351 1521 O ANISOU 3896 OE2 GLU C 161 10562 8583 7224 -967 -454 1698 O ANISOU 3897 N GLU C 162 8675 7439 5978 -489 -316 1319 N ANISOU 3898 CA GLU C 162 8509 7374 5971 -508 -267 1261 C ANISOU 3899 C GLU C 162 8065 6812 5663 -383 -297 1175 C ANISOU 3900 O GLU C 162 8149 6731 5763 -409 -322 1183 O ANISOU 3901 CB GLU C 162 8680 7900 6254 -508 -178 1201 C ANISOU 3902 CG GLU C 162 9196 8604 6658 -635 -134 1276 C ANISOU 3903 CD GLU C 162 9815 9190 7197 -813 -130 1370 C ANISOU 3904 OE1 GLU C 162 10252 9802 7536 -935 -94 1437 O ANISOU 3905 OE2 GLU C 162 10609 9796 8021 -837 -162 1375 O ANISOU 3906 N SER C 163 7467 6308 5156 -257 -294 1091 N ANISOU 3907 CA SER C 163 7091 5867 4909 -148 -317 1006 C ANISOU 3908 C SER C 163 6989 5518 4731 -78 -403 1030 C ANISOU 3909 O SER C 163 6873 5329 4707 0 -428 972 O ANISOU 3910 CB SER C 163 7069 6034 4988 -61 -285 911 C ANISOU 3911 OG SER C 163 7273 6259 5097 -24 -311 928 O ANISOU 3912 N ASN C 164 7331 5746 4901 -99 -448 1114 N ANISOU 3913 CA ASN C 164 7488 5669 4960 -15 -537 1143 C ANISOU 3914 C ASN C 164 7304 5602 4886 122 -554 1055 C ANISOU 3915 O ASN C 164 7502 5679 5090 224 -615 1034 O ANISOU 3916 CB ASN C 164 7469 5395 4912 -19 -579 1160 C ANISOU 3917 CG ASN C 164 7814 5473 5115 76 -677 1198 C ANISOU 3918 OD1 ASN C 164 8026 5546 5136 45 -722 1288 O ANISOU 3919 ND2 ASN C 164 8024 5611 5407 198 -714 1131 N ANISOU 3920 N VAL C 165 6864 5402 4521 122 -501 1003 N ANISOU 3921 CA VAL C 165 6786 5450 4534 223 -514 919 C ANISOU 3922 C VAL C 165 6948 5660 4581 248 -547 953 C ANISOU 3923 O VAL C 165 6935 5684 4460 175 -523 1011 O ANISOU 3924 CB VAL C 165 6522 5382 4411 210 -442 828 C ANISOU 3925 CG1 VAL C 165 6467 5446 4419 287 -458 746 C ANISOU 3926 CG2 VAL C 165 6484 5306 4487 189 -413 794 C ANISOU 3927 N VAL C 166 7084 5820 4742 349 -602 914 N ANISOU 3928 CA VAL C 166 7778 6575 5335 383 -641 939 C ANISOU 3929 C VAL C 166 7617 6636 5241 367 -590 860 C ANISOU 3930 O VAL C 166 7575 6674 5327 366 -549 779 O ANISOU 3931 CB VAL C 166 8098 6832 5639 502 -731 940 C ANISOU 3932 CG1 VAL C 166 8496 6964 5923 527 -789 1021 C ANISOU 3933 CG2 VAL C 166 8230 7082 5940 571 -733 838 C ANISOU 3934 N LEU C 167 7838 6936 5355 357 -599 884 N ANISOU 3935 CA LEU C 167 7903 7179 5441 340 -555 811 C ANISOU 3936 C LEU C 167 7852 7218 5497 396 -579 716 C ANISOU 3937 O LEU C 167 7896 7353 5593 373 -534 637 O ANISOU 3938 CB LEU C 167 7921 7250 5303 321 -570 862 C ANISOU 3939 CG LEU C 167 7795 7288 5160 303 -528 789 C ANISOU 3940 CD1 LEU C 167 7750 7299 5122 245 -440 770 C ANISOU 3941 CD2 LEU C 167 8263 7808 5480 304 -564 830 C ANISOU 3942 N ASP C 168 7681 7025 5349 467 -650 722 N ANISOU 3943 CA ASP C 168 7480 6947 5248 504 -674 636 C ANISOU 3944 C ASP C 168 7228 6657 5137 518 -658 591 C ANISOU 3945 O ASP C 168 7329 6810 5313 576 -702 559 O ANISOU 3946 CB ASP C 168 7734 7265 5464 579 -758 655 C ANISOU 3947 CG ASP C 168 8085 7482 5798 662 -817 721 C ANISOU 3948 OD1 ASP C 168 8476 7710 6192 646 -792 756 O ANISOU 3949 OD2 ASP C 168 8377 7835 6068 746 -890 731 O ANISOU 3950 N SER C 169 6855 6218 4801 465 -593 584 N ANISOU 3951 CA SER C 169 6792 6113 4862 469 -575 544 C ANISOU 3952 C SER C 169 6618 5947 4726 405 -500 504 C ANISOU 3953 O SER C 169 6279 5674 4329 374 -469 482 O ANISOU 3954 CB SER C 169 6911 6076 4973 502 -602 608 C ANISOU 3955 OG SER C 169 6735 5863 4913 507 -584 566 O ANISOU 3956 N ASN C 170 6848 6111 5047 396 -476 492 N ANISOU 3957 CA ASN C 170 6988 6259 5231 349 -411 457 C ANISOU 3958 C ASN C 170 7254 6423 5540 328 -392 500 C ANISOU 3959 O ASN C 170 6904 5972 5164 346 -430 556 O ANISOU 3960 CB ASN C 170 6951 6281 5263 349 -404 364 C ANISOU 3961 CG ASN C 170 6955 6279 5364 376 -439 336 C ANISOU 3962 OD1 ASN C 170 7063 6312 5531 384 -436 357 O ANISOU 3963 ND2 ASN C 170 6988 6404 5407 388 -475 290 N ANISOU 3964 N MSE C 171 7302 6491 5644 293 -338 469 N ANISOU 3965 CA MSE C 171 7361 6480 5744 257 -315 505 C ANISOU 3966 C MSE C 171 7015 6045 5481 284 -346 486 C ANISOU 3967 O MSE C 171 6861 5794 5335 257 -345 526 O ANISOU 3968 CB MSE C 171 7608 6807 6032 227 -253 469 C ANISOU 3969 CG MSE C 171 8219 7520 6560 204 -215 492 C ANISOU 3970 SE MSE C 171 9371 8646 7637 119 -203 614 SE ANISOU 3971 CE MSE C 171 10131 9415 8242 131 -237 664 C ANISOU 3972 N LEU C 172 6955 6027 5475 328 -373 424 N ANISOU 3973 CA LEU C 172 7171 6196 5770 360 -400 397 C ANISOU 3974 C LEU C 172 7792 6707 6338 408 -453 452 C ANISOU 3975 O LEU C 172 8095 6928 6682 435 -471 445 O ANISOU 3976 CB LEU C 172 7258 6393 5911 385 -418 322 C ANISOU 3977 CG LEU C 172 7121 6310 5811 341 -379 259 C ANISOU 3978 CD1 LEU C 172 7038 6316 5765 342 -404 193 C ANISOU 3979 CD2 LEU C 172 7175 6301 5931 314 -344 254 C ANISOU 3980 N SER C 173 7524 6426 5966 424 -481 506 N ANISOU 3981 CA SER C 173 7625 6396 5984 482 -542 562 C ANISOU 3982 C SER C 173 7728 6303 6040 446 -541 617 C ANISOU 3983 O SER C 173 7659 6086 5925 508 -593 635 O ANISOU 3984 CB SER C 173 7781 6565 6020 491 -569 617 C ANISOU 3985 OG SER C 173 7267 6040 5437 403 -524 667 O ANISOU 3986 N ASN C 174 7731 6306 6044 349 -485 640 N ANISOU 3987 CA ASN C 174 7629 6035 5889 289 -484 695 C ANISOU 3988 C ASN C 174 7076 5542 5449 229 -428 654 C ANISOU 3989 O ASN C 174 6989 5541 5367 150 -377 673 O ANISOU 3990 CB ASN C 174 7746 6087 5860 207 -481 790 C ANISOU 3991 CG ASN C 174 8107 6347 6081 260 -545 846 C ANISOU 3992 OD1 ASN C 174 8668 6689 6498 240 -591 921 O ANISOU 3993 ND2 ASN C 174 8205 6587 6202 325 -555 812 N ANISOU 3994 N ILE C 175 7035 5462 5493 273 -440 599 N ANISOU 3995 CA ILE C 175 6651 5118 5210 224 -396 560 C ANISOU 3996 C ILE C 175 6939 5209 5440 181 -416 603 C ANISOU 3997 O ILE C 175 6928 5037 5376 243 -469 605 O ANISOU 3998 CB ILE C 175 6564 5129 5247 283 -393 469 C ANISOU 3999 CG1 ILE C 175 6195 4928 4907 306 -380 428 C ANISOU 4000 CG2 ILE C 175 6558 5142 5331 234 -354 435 C ANISOU 4001 CD1 ILE C 175 5855 4686 4564 248 -327 434 C ANISOU 4002 N VAL C 176 6673 4963 5176 77 -376 635 N ANISOU 4003 CA VAL C 176 6903 5012 5336 6 -393 681 C ANISOU 4004 C VAL C 176 7221 5378 5772 -20 -362 627 C ANISOU 4005 O VAL C 176 7258 5270 5762 -81 -377 652 O ANISOU 4006 CB VAL C 176 7160 5252 5480 -115 -379 773 C ANISOU 4007 CG1 VAL C 176 7103 5095 5274 -94 -420 835 C ANISOU 4008 CG2 VAL C 176 7050 5406 5459 -176 -308 763 C ANISOU 4009 N SER C 177 6690 5032 5376 20 -326 556 N ANISOU 4010 CA SER C 177 6532 4922 5323 -1 -300 508 C ANISOU 4011 C SER C 177 6179 4742 5085 48 -270 434 C ANISOU 4012 O SER C 177 5715 4383 4617 77 -258 425 O ANISOU 4013 CB SER C 177 6675 5103 5459 -113 -269 552 C ANISOU 4014 OG SER C 177 6782 5261 5665 -130 -248 506 O ANISOU 4015 N TRP C 178 6709 5281 5697 51 -263 382 N ANISOU 4016 CA TRP C 178 6392 5090 5467 80 -240 317 C ANISOU 4017 C TRP C 178 6181 4879 5324 43 -225 292 C ANISOU 4018 O TRP C 178 5871 4458 5000 18 -242 305 O ANISOU 4019 CB TRP C 178 6523 5233 5617 151 -266 265 C ANISOU 4020 CG TRP C 178 7097 5723 6210 183 -297 238 C ANISOU 4021 CD1 TRP C 178 7402 5887 6451 209 -332 266 C ANISOU 4022 CD2 TRP C 178 7348 6015 6536 190 -293 175 C ANISOU 4023 NE1 TRP C 178 7384 5834 6469 248 -351 218 N ANISOU 4024 CE2 TRP C 178 7472 6046 6648 230 -324 163 C ANISOU 4025 CE3 TRP C 178 7561 6323 6809 168 -270 129 C ANISOU 4026 CZ2 TRP C 178 7828 6435 7064 247 -326 103 C ANISOU 4027 CZ3 TRP C 178 7762 6541 7061 171 -276 78 C ANISOU 4028 CH2 TRP C 178 7705 6424 7005 209 -300 64 C ANISOU 4029 N GLY C 179 5682 4486 4881 43 -197 254 N ANISOU 4030 CA GLY C 179 5235 4047 4493 11 -186 232 C ANISOU 4031 C GLY C 179 5201 4096 4499 34 -170 182 C ANISOU 4032 O GLY C 179 4805 3748 4075 69 -164 166 O ANISOU 4033 N ILE C 180 5006 3897 4352 12 -167 159 N ANISOU 4034 CA ILE C 180 4900 3832 4264 30 -160 116 C ANISOU 4035 C ILE C 180 5005 4003 4402 7 -142 131 C ANISOU 4036 O ILE C 180 4550 3540 3976 -41 -142 155 O ANISOU 4037 CB ILE C 180 4842 3722 4225 28 -180 67 C ANISOU 4038 CG1 ILE C 180 5280 4146 4637 54 -199 48 C ANISOU 4039 CG2 ILE C 180 4828 3717 4205 31 -179 32 C ANISOU 4040 CD1 ILE C 180 5345 4207 4722 45 -215 0 C ANISOU 4041 N THR C 181 4929 3992 4307 48 -130 114 N ANISOU 4042 CA THR C 181 4943 4098 4349 53 -116 119 C ANISOU 4043 C THR C 181 5290 4381 4697 66 -135 75 C ANISOU 4044 O THR C 181 5119 4121 4479 85 -152 39 O ANISOU 4045 CB THR C 181 5353 4622 4726 112 -96 121 C ANISOU 4046 OG1 THR C 181 5746 5087 5114 82 -77 168 O ANISOU 4047 CG2 THR C 181 6003 5392 5404 141 -86 117 C ANISOU 4048 N PHE C 182 4720 3858 4172 45 -134 81 N ANISOU 4049 CA PHE C 182 5161 4234 4605 50 -155 47 C ANISOU 4050 C PHE C 182 5013 4189 4477 81 -153 53 C ANISOU 4051 O PHE C 182 5055 4333 4581 37 -142 84 O ANISOU 4052 CB PHE C 182 5656 4662 5139 -17 -166 44 C ANISOU 4053 CG PHE C 182 6173 5123 5648 -30 -185 14 C ANISOU 4054 CD1 PHE C 182 6362 5226 5768 -10 -204 -19 C ANISOU 4055 CD2 PHE C 182 6669 5648 6192 -74 -188 23 C ANISOU 4056 CE1 PHE C 182 6768 5573 6151 -35 -224 -40 C ANISOU 4057 CE2 PHE C 182 6799 5729 6307 -90 -207 0 C ANISOU 4058 CZ PHE C 182 7086 5929 6522 -71 -225 -30 C ANISOU 4059 N ILE C 183 4924 4073 4320 160 -165 24 N ANISOU 4060 CA ILE C 183 4763 4004 4164 216 -171 22 C ANISOU 4061 C ILE C 183 4634 3746 4002 201 -205 0 C ANISOU 4062 O ILE C 183 4670 3617 3941 217 -229 -29 O ANISOU 4063 CB ILE C 183 5178 4462 4507 333 -169 2 C ANISOU 4064 CG1 ILE C 183 5544 4979 4904 338 -132 26 C ANISOU 4065 CG2 ILE C 183 5181 4560 4507 413 -183 -5 C ANISOU 4066 CD1 ILE C 183 5853 5355 5141 460 -124 1 C ANISOU 4067 N PRO C 184 4399 3575 3835 152 -209 16 N ANISOU 4068 CA PRO C 184 4334 3397 3736 129 -240 0 C ANISOU 4069 C PRO C 184 4253 3276 3567 226 -271 -17 C ANISOU 4070 O PRO C 184 4075 3207 3382 319 -265 -16 O ANISOU 4071 CB PRO C 184 4310 3475 3807 53 -234 23 C ANISOU 4072 CG PRO C 184 4381 3685 3953 20 -201 56 C ANISOU 4073 CD PRO C 184 4514 3872 4050 105 -187 54 C ANISOU 4074 N SER C 185 4710 3575 3947 206 -307 -33 N ANISOU 4075 CA SER C 185 5344 4118 4468 294 -349 -46 C ANISOU 4076 C SER C 185 5426 4377 4628 328 -354 -27 C ANISOU 4077 O SER C 185 5357 4479 4690 260 -326 -3 O ANISOU 4078 CB SER C 185 5694 4244 4701 237 -387 -61 C ANISOU 4079 OG SER C 185 5286 3876 4368 137 -384 -49 O ANISOU 4080 N ASP C 186 5925 4823 5031 433 -395 -36 N ANISOU 4081 CA ASP C 186 6124 5200 5290 482 -410 -20 C ANISOU 4082 C ASP C 186 5527 4610 4754 362 -418 -2 C ANISOU 4083 O ASP C 186 5628 4900 4941 361 -420 16 O ANISOU 4084 CB ASP C 186 6485 5468 5509 639 -462 -39 C ANISOU 4085 CG ASP C 186 7056 6081 6028 780 -452 -64 C ANISOU 4086 OD1 ASP C 186 7083 6239 6144 746 -401 -60 O ANISOU 4087 OD2 ASP C 186 6961 5872 5790 926 -498 -87 O ANISOU 4088 N GLU C 187 5105 3997 4282 262 -422 -10 N ANISOU 4089 CA GLU C 187 5035 3927 4259 149 -426 0 C ANISOU 4090 C GLU C 187 4951 4056 4334 80 -385 17 C ANISOU 4091 O GLU C 187 5506 4692 4948 82 -350 22 O ANISOU 4092 CB GLU C 187 4928 3623 4078 57 -430 -17 C ANISOU 4093 CG GLU C 187 5304 3767 4269 94 -479 -28 C ANISOU 4094 CD GLU C 187 5403 3705 4290 -13 -481 -43 C ANISOU 4095 OE1 GLU C 187 5530 3867 4467 -114 -471 -44 O ANISOU 4096 OE2 GLU C 187 6525 4673 5291 3 -496 -57 O ANISOU 4097 N GLU C 188 4722 3903 4159 12 -394 29 N ANISOU 4098 CA GLU C 188 5000 4353 4561 -65 -363 48 C ANISOU 4099 C GLU C 188 4127 3384 3708 -157 -333 36 C ANISOU 4100 O GLU C 188 4703 4036 4344 -183 -304 50 O ANISOU 4101 CB GLU C 188 5345 4806 4947 -117 -384 62 C ANISOU 4102 CG GLU C 188 6139 5749 5738 -18 -415 76 C ANISOU 4103 CD GLU C 188 6609 6378 6265 -74 -436 94 C ANISOU 4104 OE1 GLU C 188 6971 6719 6661 -200 -424 94 O ANISOU 4105 OE2 GLU C 188 7396 7314 7055 13 -465 105 O ANISOU 4106 N HIS C 189 3963 3065 3490 -203 -344 13 N ANISOU 4107 CA HIS C 189 4292 3317 3833 -272 -320 -5 C ANISOU 4108 C HIS C 189 4648 3556 4126 -240 -316 -25 C ANISOU 4109 O HIS C 189 4799 3601 4192 -240 -338 -41 O ANISOU 4110 CB HIS C 189 4407 3384 3937 -351 -330 -25 C ANISOU 4111 CG HIS C 189 4605 3676 4190 -408 -334 -12 C ANISOU 4112 ND1 HIS C 189 5013 4224 4636 -390 -346 18 N ANISOU 4113 CD2 HIS C 189 4577 3626 4179 -485 -326 -28 C ANISOU 4114 CE1 HIS C 189 4370 3639 4030 -472 -347 23 C ANISOU 4115 NE2 HIS C 189 4292 3444 3931 -528 -337 -6 N ANISOU 4116 N ASN C 190 4014 2939 3524 -224 -289 -23 N ANISOU 4117 CA ASN C 190 4280 3116 3737 -202 -285 -41 C ANISOU 4118 C ASN C 190 4355 3174 3847 -250 -266 -59 C ANISOU 4119 O ASN C 190 4060 2923 3611 -272 -250 -47 O ANISOU 4120 CB ASN C 190 4224 3085 3665 -125 -277 -29 C ANISOU 4121 CG ASN C 190 4048 2908 3430 -50 -302 -23 C ANISOU 4122 OD1 ASN C 190 4533 3269 3808 -12 -324 -39 O ANISOU 4123 ND2 ASN C 190 4286 3271 3721 -32 -305 -3 N ANISOU 4124 N ILE C 191 4350 3101 3791 -266 -271 -87 N ANISOU 4125 CA ILE C 191 4560 3316 4027 -292 -256 -111 C ANISOU 4126 C ILE C 191 4996 3727 4418 -275 -257 -125 C ANISOU 4127 O ILE C 191 4454 3130 3796 -288 -275 -133 O ANISOU 4128 CB ILE C 191 4672 3429 4138 -350 -261 -141 C ANISOU 4129 CG1 ILE C 191 4613 3388 4109 -376 -265 -128 C ANISOU 4130 CG2 ILE C 191 5331 4115 4824 -353 -247 -173 C ANISOU 4131 CD1 ILE C 191 4781 3558 4267 -431 -269 -160 C ANISOU 4132 N VAL C 192 4698 3458 4158 -250 -242 -126 N ANISOU 4133 CA VAL C 192 4762 3524 4189 -238 -243 -141 C ANISOU 4134 C VAL C 192 5127 3941 4603 -233 -234 -162 C ANISOU 4135 O VAL C 192 5074 3883 4593 -216 -226 -152 O ANISOU 4136 CB VAL C 192 4758 3505 4163 -186 -240 -116 C ANISOU 4137 CG1 VAL C 192 4860 3551 4198 -167 -254 -105 C ANISOU 4138 CG2 VAL C 192 4741 3523 4205 -153 -223 -86 C ANISOU 4139 N ILE C 193 5110 3973 4567 -250 -238 -194 N ANISOU 4140 CA ILE C 193 5665 4602 5163 -225 -233 -222 C ANISOU 4141 C ILE C 193 5688 4669 5176 -192 -238 -221 C ANISOU 4142 O ILE C 193 6003 5011 5443 -229 -246 -230 O ANISOU 4143 CB ILE C 193 5937 4958 5436 -271 -234 -267 C ANISOU 4144 CG1 ILE C 193 5764 4741 5264 -309 -231 -268 C ANISOU 4145 CG2 ILE C 193 6143 5264 5684 -220 -230 -304 C ANISOU 4146 CD1 ILE C 193 5783 4851 5275 -360 -229 -312 C ANISOU 4147 N ILE C 194 6027 5001 5545 -128 -236 -209 N ANISOU 4148 CA ILE C 194 5802 4824 5311 -88 -243 -207 C ANISOU 4149 C ILE C 194 6358 5476 5900 -43 -250 -245 C ANISOU 4150 O ILE C 194 6395 5458 5950 12 -253 -243 O ANISOU 4151 CB ILE C 194 5947 4892 5447 -45 -241 -160 C ANISOU 4152 CG1 ILE C 194 5808 4693 5281 -72 -232 -129 C ANISOU 4153 CG2 ILE C 194 6160 5158 5646 -3 -252 -157 C ANISOU 4154 CD1 ILE C 194 6072 4920 5537 -39 -225 -83 C ANISOU 4155 N LYS C 195 6818 6079 6361 -69 -255 -282 N ANISOU 4156 CA LYS C 195 7037 6440 6616 -15 -261 -327 C ANISOU 4157 C LYS C 195 7202 6631 6785 72 -277 -316 C ANISOU 4158 O LYS C 195 6395 5821 5991 164 -288 -331 O ANISOU 4159 CB LYS C 195 7623 7218 7204 -85 -260 -367 C ANISOU 4160 CG LYS C 195 8429 8021 7993 -179 -249 -381 C ANISOU 4161 CD LYS C 195 8753 8540 8301 -268 -250 -414 C ANISOU 4162 CE LYS C 195 8870 8904 8478 -210 -249 -467 C ANISOU 4163 NZ LYS C 195 9062 9323 8653 -318 -249 -495 N ANISOU 4164 N LYS C 196 7123 6560 6678 48 -283 -289 N ANISOU 4165 CA LYS C 196 7108 6584 6660 124 -302 -277 C ANISOU 4166 C LYS C 196 7229 6619 6733 100 -303 -231 C ANISOU 4167 O LYS C 196 7443 6794 6912 23 -294 -224 O ANISOU 4168 CB LYS C 196 6892 6609 6470 128 -315 -323 C ANISOU 4169 CG LYS C 196 7345 7150 6924 212 -340 -317 C ANISOU 4170 CD LYS C 196 7638 7729 7253 210 -353 -365 C ANISOU 4171 CE LYS C 196 7808 8001 7397 66 -347 -373 C ANISOU 4172 NZ LYS C 196 8431 8937 8055 47 -361 -417 N ANISOU 4173 N ILE C 197 7345 6695 6836 175 -317 -202 N ANISOU 4174 CA ILE C 197 7226 6517 6670 169 -318 -161 C ANISOU 4175 C ILE C 197 7519 6902 6957 242 -346 -160 C ANISOU 4176 O ILE C 197 7115 6442 6550 326 -362 -145 O ANISOU 4177 CB ILE C 197 7359 6478 6779 175 -304 -110 C ANISOU 4178 CG1 ILE C 197 7385 6439 6819 113 -281 -113 C ANISOU 4179 CG2 ILE C 197 7429 6522 6799 175 -303 -72 C ANISOU 4180 CD1 ILE C 197 7836 6770 7255 109 -266 -65 C ANISOU 4181 N SER C 198 7899 7413 7323 209 -357 -176 N ANISOU 4182 CA SER C 198 8135 7769 7556 275 -387 -177 C ANISOU 4183 C SER C 198 8513 8126 7871 246 -393 -148 C ANISOU 4184 O SER C 198 8620 8169 7936 167 -376 -146 O ANISOU 4185 CB SER C 198 8208 8081 7677 271 -401 -231 C ANISOU 4186 OG SER C 198 9088 9036 8538 147 -392 -253 O ANISOU 4187 N LEU C 199 8552 8207 7892 321 -420 -127 N ANISOU 4188 CA LEU C 199 8137 7786 7412 305 -429 -100 C ANISOU 4189 C LEU C 199 8314 8184 7594 282 -457 -135 C ANISOU 4190 O LEU C 199 7702 7722 7021 358 -486 -149 O ANISOU 4191 CB LEU C 199 8150 7701 7390 395 -446 -47 C ANISOU 4192 CG LEU C 199 7839 7186 7065 407 -424 -6 C ANISOU 4193 CD1 LEU C 199 8255 7496 7410 458 -442 55 C ANISOU 4194 CD2 LEU C 199 7670 6938 6891 320 -383 -5 C ANISOU 4195 N LEU C 200 8746 8634 7974 179 -452 -152 N ANISOU 4196 CA LEU C 200 9360 9453 8574 124 -480 -185 C ANISOU 4197 C LEU C 200 9837 9950 8990 155 -505 -158 C ANISOU 4198 O LEU C 200 10217 10173 9330 205 -496 -116 O ANISOU 4199 CB LEU C 200 9819 9873 8971 -15 -470 -213 C ANISOU 4200 CG LEU C 200 10301 10326 9494 -61 -447 -236 C ANISOU 4201 CD1 LEU C 200 10073 10093 9183 -209 -453 -264 C ANISOU 4202 CD2 LEU C 200 10567 10791 9872 0 -452 -259 C ANISOU 4203 N SER C 201 9725 10050 8868 115 -537 -183 N ANISOU 4204 CA SER C 201 9098 9473 8180 135 -567 -163 C ANISOU 4205 C SER C 201 8596 9201 7654 35 -598 -202 C ANISOU 4206 O SER C 201 7668 8437 6782 -21 -599 -239 O ANISOU 4207 CB SER C 201 9070 9492 8196 281 -590 -131 C ANISOU 4208 OG SER C 201 8857 9322 7917 301 -620 -106 O TER 4209 SER C 201 ANISOU 4210 N ASP D 33 8728 11608 8300 49 -988 -556 N ANISOU 4211 CA ASP D 33 8563 10855 7973 9 -905 -596 C ANISOU 4212 C ASP D 33 8408 10442 7627 200 -770 -346 C ANISOU 4213 O ASP D 33 8646 10698 7930 303 -690 -154 O ANISOU 4214 CB ASP D 33 8495 10415 8095 -174 -859 -669 C ANISOU 4215 CG ASP D 33 8705 10806 8563 -386 -983 -912 C ANISOU 4216 OD1 ASP D 33 8892 11422 8768 -397 -1123 -1064 O ANISOU 4217 OD2 ASP D 33 8635 10455 8689 -537 -939 -947 O ANISOU 4218 N LYS D 34 8285 10081 7292 246 -744 -357 N ANISOU 4219 CA LYS D 34 8201 9730 7071 401 -626 -136 C ANISOU 4220 C LYS D 34 8033 8981 6875 312 -544 -164 C ANISOU 4221 O LYS D 34 7970 8726 6769 192 -574 -328 O ANISOU 4222 CB LYS D 34 8327 10040 7012 524 -643 -83 C ANISOU 4223 CG LYS D 34 8530 9979 7132 673 -521 163 C ANISOU 4224 CD LYS D 34 8752 10437 7205 803 -523 260 C ANISOU 4225 CE LYS D 34 8930 10346 7376 934 -397 530 C ANISOU 4226 NZ LYS D 34 9217 10923 7546 1072 -384 667 N ANISOU 4227 N ILE D 35 7841 8534 6709 384 -443 -11 N ANISOU 4228 CA ILE D 35 7682 7877 6512 327 -369 -27 C ANISOU 4229 C ILE D 35 7477 7426 6180 424 -315 83 C ANISOU 4230 O ILE D 35 7440 7472 6150 573 -272 255 O ANISOU 4231 CB ILE D 35 7765 7856 6693 357 -299 40 C ANISOU 4232 CG1 ILE D 35 7844 8240 6953 265 -342 -25 C ANISOU 4233 CG2 ILE D 35 7733 7361 6595 316 -233 12 C ANISOU 4234 CD1 ILE D 35 7881 8195 7057 69 -395 -201 C ANISOU 4235 N LEU D 36 6992 6651 5612 338 -314 0 N ANISOU 4236 CA LEU D 36 7096 6530 5638 404 -266 107 C ANISOU 4237 C LEU D 36 7193 6233 5762 418 -197 156 C ANISOU 4238 O LEU D 36 6734 5623 5320 347 -189 64 O ANISOU 4239 CB LEU D 36 6968 6313 5419 315 -297 -4 C ANISOU 4240 CG LEU D 36 7079 6800 5475 314 -372 -100 C ANISOU 4241 CD1 LEU D 36 7108 6720 5400 279 -376 -174 C ANISOU 4242 CD2 LEU D 36 7221 7335 5602 470 -377 54 C ANISOU 4243 N ASP D 37 7546 6444 6134 519 -146 304 N ANISOU 4244 CA ASP D 37 8050 6567 6675 535 -96 319 C ANISOU 4245 C ASP D 37 8079 6325 6643 416 -114 221 C ANISOU 4246 O ASP D 37 8352 6591 6906 401 -119 274 O ANISOU 4247 CB ASP D 37 8715 7154 7440 671 -39 507 C ANISOU 4248 CG ASP D 37 9292 7313 8080 685 -1 483 C ANISOU 4249 OD1 ASP D 37 10009 7841 8727 602 -21 322 O ANISOU 4250 OD2 ASP D 37 9890 7785 8809 783 48 624 O ANISOU 4251 N LEU D 38 7840 5900 6370 346 -117 97 N ANISOU 4252 CA LEU D 38 7658 5502 6134 243 -136 13 C ANISOU 4253 C LEU D 38 7699 5243 6213 264 -121 41 C ANISOU 4254 O LEU D 38 8231 5583 6720 255 -122 -44 O ANISOU 4255 CB LEU D 38 7516 5349 5951 170 -142 -103 C ANISOU 4256 CG LEU D 38 7501 5606 5964 119 -163 -144 C ANISOU 4257 CD1 LEU D 38 7532 5581 6003 26 -158 -228 C ANISOU 4258 CD2 LEU D 38 7498 5753 5945 93 -202 -150 C ANISOU 4259 N SER D 39 7337 4875 5928 298 -110 166 N ANISOU 4260 CA SER D 39 7220 4490 5920 297 -102 213 C ANISOU 4261 C SER D 39 6806 4120 5527 236 -111 284 C ANISOU 4262 O SER D 39 6502 4015 5262 291 -84 431 O ANISOU 4263 CB SER D 39 7355 4576 6200 414 -56 345 C ANISOU 4264 OG SER D 39 7856 4785 6860 393 -53 376 O ANISOU 4265 N PHE D 40 6616 3782 5305 138 -145 188 N ANISOU 4266 CA PHE D 40 6372 3604 5075 87 -148 248 C ANISOU 4267 C PHE D 40 6188 3217 5049 34 -160 299 C ANISOU 4268 O PHE D 40 6105 2907 5024 2 -192 208 O ANISOU 4269 CB PHE D 40 6427 3691 4989 13 -176 112 C ANISOU 4270 CG PHE D 40 6616 4062 5067 26 -176 34 C ANISOU 4271 CD1 PHE D 40 6703 4404 5122 72 -167 78 C ANISOU 4272 CD2 PHE D 40 6561 3949 4955 -6 -187 -81 C ANISOU 4273 CE1 PHE D 40 6817 4689 5172 63 -186 -20 C ANISOU 4274 CE2 PHE D 40 6705 4261 5059 -14 -188 -141 C ANISOU 4275 CZ PHE D 40 6765 4552 5111 10 -195 -124 C ANISOU 4276 N LYS D 41 6063 3211 5001 30 -135 441 N ANISOU 4277 CA LYS D 41 6032 3059 5153 -37 -145 515 C ANISOU 4278 C LYS D 41 5889 2996 4886 -98 -168 435 C ANISOU 4279 O LYS D 41 5615 2862 4425 -72 -161 358 O ANISOU 4280 CB LYS D 41 6225 3342 5563 15 -82 769 C ANISOU 4281 CG LYS D 41 6455 3428 5961 77 -54 850 C ANISOU 4282 CD LYS D 41 6521 3582 6285 141 24 1147 C ANISOU 4283 CE LYS D 41 6485 3947 6118 261 88 1316 C ANISOU 4284 NZ LYS D 41 6637 4217 6530 350 181 1647 N ANISOU 4285 N LYS D 42 5983 3014 5106 -177 -195 453 N ANISOU 4286 CA LYS D 42 5945 3046 4951 -217 -212 379 C ANISOU 4287 C LYS D 42 5864 3077 5012 -241 -191 522 C ANISOU 4288 O LYS D 42 5965 3158 5354 -266 -182 668 O ANISOU 4289 CB LYS D 42 6043 2970 5004 -283 -284 207 C ANISOU 4290 CG LYS D 42 6336 3096 5511 -351 -343 199 C ANISOU 4291 CD LYS D 42 6490 3111 5591 -388 -421 3 C ANISOU 4292 CE LYS D 42 6143 2859 5115 -417 -453 -66 C ANISOU 4293 NZ LYS D 42 6122 2758 5008 -428 -528 -242 N ANISOU 4294 N ILE D 43 5648 2982 4664 -229 -175 484 N ANISOU 4295 CA ILE D 43 5544 3019 4654 -231 -147 602 C ANISOU 4296 C ILE D 43 5378 2816 4387 -267 -179 479 C ANISOU 4297 O ILE D 43 5293 2778 4123 -216 -149 395 O ANISOU 4298 CB ILE D 43 5590 3316 4621 -118 -62 713 C ANISOU 4299 CG1 ILE D 43 5741 3558 4841 -52 -21 857 C ANISOU 4300 CG2 ILE D 43 5583 3476 4713 -102 -19 843 C ANISOU 4301 CD1 ILE D 43 5878 3646 5293 -99 -11 1056 C ANISOU 4302 N GLU D 44 5276 2639 4419 -353 -243 466 N ANISOU 4303 CA GLU D 44 5169 2535 4240 -376 -276 383 C ANISOU 4304 C GLU D 44 5111 2651 4285 -363 -243 508 C ANISOU 4305 O GLU D 44 5067 2689 4468 -406 -252 640 O ANISOU 4306 CB GLU D 44 5231 2483 4372 -461 -379 286 C ANISOU 4307 CG GLU D 44 5249 2344 4260 -456 -410 139 C ANISOU 4308 CD GLU D 44 5386 2397 4442 -517 -515 16 C ANISOU 4309 OE1 GLU D 44 5564 2637 4784 -584 -580 38 O ANISOU 4310 OE2 GLU D 44 5417 2333 4337 -491 -536 -110 O ANISOU 4311 N THR D 45 5031 2627 4068 -302 -199 474 N ANISOU 4312 CA THR D 45 5088 2854 4205 -263 -157 584 C ANISOU 4313 C THR D 45 5076 2821 4140 -267 -186 522 C ANISOU 4314 O THR D 45 4955 2601 3856 -225 -158 423 O ANISOU 4315 CB THR D 45 5178 3059 4193 -143 -52 622 C ANISOU 4316 OG1 THR D 45 5367 3324 4422 -120 -23 707 O ANISOU 4317 CG2 THR D 45 5231 3296 4327 -79 4 737 C ANISOU 4318 N ASP D 46 5146 3002 4373 -321 -244 592 N ANISOU 4319 CA ASP D 46 5320 3229 4520 -313 -277 571 C ANISOU 4320 C ASP D 46 5311 3073 4338 -319 -315 431 C ANISOU 4321 O ASP D 46 5194 2947 4118 -253 -269 424 O ANISOU 4322 CB ASP D 46 5551 3562 4723 -200 -178 653 C ANISOU 4323 CG ASP D 46 5742 3972 5096 -173 -138 816 C ANISOU 4324 OD1 ASP D 46 6060 4368 5593 -254 -185 887 O ANISOU 4325 OD2 ASP D 46 6355 4686 5702 -68 -59 884 O ANISOU 4326 N LEU D 47 5245 2900 4261 -390 -390 334 N ANISOU 4327 CA LEU D 47 5326 2886 4186 -385 -425 211 C ANISOU 4328 C LEU D 47 5536 2994 4427 -456 -512 105 C ANISOU 4329 O LEU D 47 5278 2716 4339 -515 -542 138 O ANISOU 4330 CB LEU D 47 5271 2719 3973 -318 -330 179 C ANISOU 4331 CG LEU D 47 5176 2528 3853 -312 -280 158 C ANISOU 4332 CD1 LEU D 47 5146 2397 3802 -353 -333 76 C ANISOU 4333 CD2 LEU D 47 5145 2438 3716 -253 -196 123 C ANISOU 4334 N SER D 48 5795 3204 4543 -440 -550 -11 N ANISOU 4335 CA SER D 48 6119 3409 4865 -477 -622 -142 C ANISOU 4336 C SER D 48 6119 3309 4684 -413 -556 -195 C ANISOU 4337 O SER D 48 6308 3555 4751 -357 -500 -168 O ANISOU 4338 CB SER D 48 6367 3743 5123 -509 -747 -258 C ANISOU 4339 OG SER D 48 6748 4259 5318 -433 -740 -276 O ANISOU 4340 N SER D 49 6298 3349 4879 -420 -554 -248 N ANISOU 4341 CA SER D 49 6122 3115 4560 -362 -494 -286 C ANISOU 4342 C SER D 49 6482 3379 4879 -344 -543 -417 C ANISOU 4343 O SER D 49 6028 2850 4539 -386 -621 -486 O ANISOU 4344 CB SER D 49 6081 3042 4551 -351 -417 -207 C ANISOU 4345 OG SER D 49 5789 2685 4401 -379 -434 -171 O ANISOU 4346 N LYS D 50 6799 3704 5052 -278 -495 -454 N ANISOU 4347 CA LYS D 50 7287 4122 5474 -227 -516 -573 C ANISOU 4348 C LYS D 50 7162 3996 5301 -178 -428 -526 C ANISOU 4349 O LYS D 50 7283 4222 5341 -150 -370 -480 O ANISOU 4350 CB LYS D 50 7796 4738 5831 -170 -560 -680 C ANISOU 4351 CG LYS D 50 8461 5457 6532 -212 -672 -762 C ANISOU 4352 CD LYS D 50 8820 5980 6702 -127 -718 -880 C ANISOU 4353 CE LYS D 50 9364 6628 7278 -168 -852 -990 C ANISOU 4354 NZ LYS D 50 9476 6869 7485 -228 -852 -836 N ANISOU 4355 N ILE D 51 6873 3603 5098 -173 -417 -517 N ANISOU 4356 CA ILE D 51 6664 3431 4865 -125 -349 -474 C ANISOU 4357 C ILE D 51 7060 3768 5211 -43 -351 -568 C ANISOU 4358 O ILE D 51 6942 3501 5171 -32 -392 -632 O ANISOU 4359 CB ILE D 51 6534 3295 4852 -148 -324 -370 C ANISOU 4360 CG1 ILE D 51 6304 3131 4656 -208 -320 -296 C ANISOU 4361 CG2 ILE D 51 6369 3223 4662 -97 -270 -336 C ANISOU 4362 CD1 ILE D 51 6233 3110 4671 -207 -291 -192 C ANISOU 4363 N THR D 52 7043 3870 5089 18 -300 -574 N ANISOU 4364 CA THR D 52 7300 4114 5278 123 -285 -658 C ANISOU 4365 C THR D 52 7535 4444 5550 167 -214 -576 C ANISOU 4366 O THR D 52 7500 4563 5519 137 -171 -497 O ANISOU 4367 CB THR D 52 7297 4231 5116 183 -286 -728 C ANISOU 4368 OG1 THR D 52 7137 4029 4936 132 -366 -794 O ANISOU 4369 CG2 THR D 52 7550 4491 5270 317 -269 -838 C ANISOU 4370 N TYR D 53 8119 4937 6191 238 -206 -595 N ANISOU 4371 CA TYR D 53 8422 5356 6544 296 -147 -512 C ANISOU 4372 C TYR D 53 9557 6596 7590 415 -98 -560 C ANISOU 4373 O TYR D 53 10318 7242 8329 522 -94 -645 O ANISOU 4374 CB TYR D 53 8303 5106 6557 329 -151 -465 C ANISOU 4375 CG TYR D 53 7687 4435 6039 231 -184 -387 C ANISOU 4376 CD1 TYR D 53 7385 4308 5739 167 -175 -300 C ANISOU 4377 CD2 TYR D 53 7628 4159 6084 203 -224 -410 C ANISOU 4378 CE1 TYR D 53 7249 4156 5672 103 -194 -227 C ANISOU 4379 CE2 TYR D 53 7347 3867 5911 123 -241 -310 C ANISOU 4380 CZ TYR D 53 7220 3940 5749 84 -221 -214 C ANISOU 4381 OH TYR D 53 6806 3549 5420 28 -227 -114 O ANISOU 4382 N GLU D 54 10742 7998 8742 399 -55 -501 N ANISOU 4383 CA GLU D 54 11473 8894 9407 513 9 -503 C ANISOU 4384 C GLU D 54 11494 9123 9553 521 61 -387 C ANISOU 4385 O GLU D 54 11900 9574 10067 419 38 -323 O ANISOU 4386 CB GLU D 54 12004 9551 9847 495 29 -490 C ANISOU 4387 CG GLU D 54 12375 9784 10092 491 -35 -605 C ANISOU 4388 CD GLU D 54 12620 10194 10241 497 -11 -563 C ANISOU 4389 OE1 GLU D 54 12768 10544 10446 498 68 -430 O ANISOU 4390 OE2 GLU D 54 12927 10445 10442 499 -72 -653 O ANISOU 4391 N ASP D 55 11819 9603 9862 650 127 -370 N ANISOU 4392 CA ASP D 55 11682 9714 9865 664 173 -257 C ANISOU 4393 C ASP D 55 11109 9341 9401 531 185 -169 C ANISOU 4394 O ASP D 55 10729 9147 9182 469 183 -98 O ANISOU 4395 CB ASP D 55 12057 10226 10206 849 251 -249 C ANISOU 4396 CG ASP D 55 12161 10100 10245 991 245 -348 C ANISOU 4397 OD1 ASP D 55 11822 9498 9913 931 179 -405 O ANISOU 4398 OD2 ASP D 55 12350 10375 10401 1164 313 -360 O ANISOU 4399 N THR D 56 11197 9396 9419 490 196 -176 N ANISOU 4400 CA THR D 56 10853 9190 9211 367 220 -84 C ANISOU 4401 C THR D 56 10429 8630 8862 212 147 -116 C ANISOU 4402 O THR D 56 10350 8640 8948 95 152 -67 O ANISOU 4403 CB THR D 56 11366 9741 9631 406 272 -45 C ANISOU 4404 OG1 THR D 56 11819 9966 9915 405 211 -148 O ANISOU 4405 CG2 THR D 56 11619 10189 9796 581 355 -9 C ANISOU 4406 N GLY D 57 9850 7837 8176 215 84 -199 N ANISOU 4407 CA GLY D 57 9015 6899 7387 99 25 -225 C ANISOU 4408 C GLY D 57 8590 6239 6839 98 -19 -285 C ANISOU 4409 O GLY D 57 8766 6335 6903 159 -14 -321 O ANISOU 4410 N VAL D 58 7401 4976 5681 33 -66 -296 N ANISOU 4411 CA VAL D 58 7013 4398 5230 15 -107 -328 C ANISOU 4412 C VAL D 58 6644 3993 4834 -43 -103 -329 C ANISOU 4413 O VAL D 58 6614 4019 4878 -112 -87 -304 O ANISOU 4414 CB VAL D 58 7128 4504 5396 -17 -139 -305 C ANISOU 4415 CG1 VAL D 58 7268 4480 5514 -44 -173 -309 C ANISOU 4416 CG2 VAL D 58 7232 4678 5540 60 -134 -266 C ANISOU 4417 N LYS D 59 6385 3646 4482 -8 -120 -364 N ANISOU 4418 CA LYS D 59 6215 3477 4280 -40 -116 -343 C ANISOU 4419 C LYS D 59 5932 3075 4004 -92 -171 -360 C ANISOU 4420 O LYS D 59 5783 2828 3840 -79 -222 -410 O ANISOU 4421 CB LYS D 59 6475 3805 4423 45 -102 -364 C ANISOU 4422 CG LYS D 59 6623 4011 4528 41 -93 -316 C ANISOU 4423 CD LYS D 59 6933 4467 4699 154 -73 -326 C ANISOU 4424 CE LYS D 59 7388 4858 5023 225 -147 -486 C ANISOU 4425 NZ LYS D 59 7830 5485 5296 357 -129 -520 N ANISOU 4426 N ILE D 60 5526 2675 3652 -151 -155 -312 N ANISOU 4427 CA ILE D 60 5434 2513 3581 -190 -192 -304 C ANISOU 4428 C ILE D 60 5517 2626 3637 -188 -186 -266 C ANISOU 4429 O ILE D 60 5231 2386 3388 -191 -127 -209 O ANISOU 4430 CB ILE D 60 5323 2409 3544 -230 -174 -286 C ANISOU 4431 CG1 ILE D 60 5399 2527 3636 -211 -179 -303 C ANISOU 4432 CG2 ILE D 60 5239 2288 3485 -252 -196 -258 C ANISOU 4433 CD1 ILE D 60 5397 2600 3679 -233 -171 -308 C ANISOU 4434 N GLU D 61 5686 2781 3765 -181 -247 -295 N ANISOU 4435 CA GLU D 61 5892 3067 3937 -165 -258 -256 C ANISOU 4436 C GLU D 61 5763 2915 3879 -211 -307 -239 C ANISOU 4437 O GLU D 61 5872 2957 4036 -245 -365 -288 O ANISOU 4438 CB GLU D 61 6515 3771 4440 -104 -307 -330 C ANISOU 4439 CG GLU D 61 7077 4403 4922 -33 -252 -337 C ANISOU 4440 CD GLU D 61 7797 5224 5489 55 -299 -436 C ANISOU 4441 OE1 GLU D 61 8211 5644 5869 46 -394 -526 O ANISOU 4442 OE2 GLU D 61 8726 6249 6340 136 -244 -431 O ANISOU 4443 N THR D 62 5571 2784 3720 -207 -276 -151 N ANISOU 4444 CA THR D 62 5439 2676 3667 -238 -314 -112 C ANISOU 4445 C THR D 62 5447 2834 3655 -199 -325 -46 C ANISOU 4446 O THR D 62 5344 2804 3488 -141 -278 1 O ANISOU 4447 CB THR D 62 5368 2547 3680 -254 -253 -60 C ANISOU 4448 OG1 THR D 62 5316 2483 3638 -222 -169 -10 O ANISOU 4449 CG2 THR D 62 5329 2427 3650 -276 -248 -110 C ANISOU 4450 N ASP D 63 5492 2953 3776 -227 -387 -25 N ANISOU 4451 CA ASP D 63 5690 3342 3981 -191 -416 47 C ANISOU 4452 C ASP D 63 5621 3294 4053 -209 -393 143 C ANISOU 4453 O ASP D 63 5582 3243 4116 -274 -449 118 O ANISOU 4454 CB ASP D 63 5973 3755 4217 -207 -549 -63 C ANISOU 4455 CG ASP D 63 6349 4400 4596 -166 -604 1 C ANISOU 4456 OD1 ASP D 63 6517 4643 4811 -115 -523 161 O ANISOU 4457 OD2 ASP D 63 6747 4938 4956 -180 -730 -117 O ANISOU 4458 N SER D 64 5816 3521 4275 -144 -301 265 N ANISOU 4459 CA SER D 64 5786 3514 4364 -130 -256 356 C ANISOU 4460 C SER D 64 6266 4132 4885 -40 -201 500 C ANISOU 4461 O SER D 64 6341 4263 4899 15 -175 549 O ANISOU 4462 CB SER D 64 5640 3180 4228 -129 -168 326 C ANISOU 4463 OG SER D 64 5510 2933 4055 -92 -88 320 O ANISOU 4464 N SER D 65 6888 4824 5621 -10 -169 590 N ANISOU 4465 CA SER D 65 7522 5590 6321 93 -104 746 C ANISOU 4466 C SER D 65 8231 6114 7091 165 35 784 C ANISOU 4467 O SER D 65 8583 6351 7453 140 58 707 O ANISOU 4468 CB SER D 65 7615 5961 6516 91 -183 828 C ANISOU 4469 OG SER D 65 7433 5766 6438 49 -182 820 O ANISOU 4470 N LYS D 66 8615 6485 7523 265 130 904 N ANISOU 4471 CA LYS D 66 9147 6814 8144 345 267 926 C ANISOU 4472 C LYS D 66 9229 6965 8299 402 297 955 C ANISOU 4473 O LYS D 66 9670 7225 8767 449 383 884 O ANISOU 4474 CB LYS D 66 9656 7327 8741 451 362 1096 C ANISOU 4475 CG LYS D 66 10010 7438 9240 542 511 1123 C ANISOU 4476 CD LYS D 66 10333 7742 9700 647 620 1326 C ANISOU 4477 CE LYS D 66 10487 8233 9883 755 610 1551 C ANISOU 4478 NZ LYS D 66 10924 8666 10468 879 735 1785 N ANISOU 4479 N SER D 67 9593 7616 8702 402 224 1052 N ANISOU 4480 CA SER D 67 9626 7785 8832 463 256 1120 C ANISOU 4481 C SER D 67 9193 7293 8363 397 236 999 C ANISOU 4482 O SER D 67 9226 7316 8430 483 322 1007 O ANISOU 4483 CB SER D 67 9767 8283 9064 463 171 1264 C ANISOU 4484 OG SER D 67 10480 9106 9736 319 18 1181 O ANISOU 4485 N ASP D 68 8787 6869 7889 263 130 900 N ANISOU 4486 CA ASP D 68 8853 6907 7936 208 114 823 C ANISOU 4487 C ASP D 68 8324 6132 7296 243 193 685 C ANISOU 4488 O ASP D 68 8393 6041 7278 177 162 575 O ANISOU 4489 CB ASP D 68 9050 7140 8128 65 -15 768 C ANISOU 4490 CG ASP D 68 9602 7944 8818 6 -120 859 C ANISOU 4491 OD1 ASP D 68 10144 8678 9459 79 -92 989 O ANISOU 4492 OD2 ASP D 68 9988 8337 9224 -109 -233 790 O ANISOU 4493 N LYS D 69 8308 6119 7288 351 288 681 N ANISOU 4494 CA LYS D 69 8455 6071 7338 394 350 518 C ANISOU 4495 C LYS D 69 8291 5979 7094 354 315 452 C ANISOU 4496 O LYS D 69 8784 6388 7490 396 351 309 O ANISOU 4497 CB LYS D 69 8901 6478 7822 553 471 517 C ANISOU 4498 CG LYS D 69 9416 6783 8256 606 528 305 C ANISOU 4499 CD LYS D 69 9739 7025 8632 774 648 273 C ANISOU 4500 CE LYS D 69 9988 7536 8883 907 705 375 C ANISOU 4501 NZ LYS D 69 10217 7930 8977 914 684 296 N ANISOU 4502 N GLU D 70 7612 5466 6474 274 243 557 N ANISOU 4503 CA GLU D 70 7489 5426 6320 240 219 549 C ANISOU 4504 C GLU D 70 7002 4817 5796 111 126 479 C ANISOU 4505 O GLU D 70 7317 5180 6103 78 102 487 O ANISOU 4506 CB GLU D 70 7629 5823 6617 236 213 737 C ANISOU 4507 CG GLU D 70 8000 6374 7040 379 314 837 C ANISOU 4508 CD GLU D 70 8338 6745 7235 524 412 754 C ANISOU 4509 OE1 GLU D 70 8404 6724 7167 505 394 625 O ANISOU 4510 OE2 GLU D 70 9100 7641 8016 667 505 809 O ANISOU 4511 N ARG D 71 6548 4225 5323 58 85 428 N ANISOU 4512 CA ARG D 71 6494 4067 5224 -41 6 357 C ANISOU 4513 C ARG D 71 6403 3888 5028 -38 23 241 C ANISOU 4514 O ARG D 71 6319 3746 4883 22 82 156 O ANISOU 4515 CB ARG D 71 6655 4142 5362 -58 -11 336 C ANISOU 4516 CG ARG D 71 7087 4433 5755 1 70 276 C ANISOU 4517 CD ARG D 71 7331 4631 6009 -1 71 313 C ANISOU 4518 NE ARG D 71 7710 4847 6413 39 157 271 N ANISOU 4519 CZ ARG D 71 7955 5057 6746 114 234 356 C ANISOU 4520 NH1 ARG D 71 8424 5681 7263 170 235 495 N ANISOU 4521 NH2 ARG D 71 8163 5079 7024 135 310 306 N ANISOU 4522 N TYR D 72 5978 3451 4596 -105 -35 227 N ANISOU 4523 CA TYR D 72 5977 3423 4507 -94 -27 142 C ANISOU 4524 C TYR D 72 5594 3010 4145 -160 -90 151 C ANISOU 4525 O TYR D 72 5378 2824 4040 -204 -130 237 O ANISOU 4526 CB TYR D 72 6518 4121 5032 -4 32 182 C ANISOU 4527 CG TYR D 72 6788 4477 5212 37 42 130 C ANISOU 4528 CD1 TYR D 72 6940 4672 5395 4 7 196 C ANISOU 4529 CD2 TYR D 72 7233 4993 5551 128 87 21 C ANISOU 4530 CE1 TYR D 72 7397 5263 5772 64 20 181 C ANISOU 4531 CE2 TYR D 72 7342 5252 5563 183 86 -28 C ANISOU 4532 CZ TYR D 72 7700 5681 5947 154 55 67 C ANISOU 4533 OH TYR D 72 7992 6167 6144 224 55 46 O ANISOU 4534 N LEU D 73 5408 2759 3876 -169 -99 55 N ANISOU 4535 CA LEU D 73 5324 2644 3809 -203 -142 60 C ANISOU 4536 C LEU D 73 5475 2882 3894 -155 -120 33 C ANISOU 4537 O LEU D 73 5626 3049 3965 -134 -102 -71 O ANISOU 4538 CB LEU D 73 5154 2349 3605 -249 -183 -16 C ANISOU 4539 CG LEU D 73 5058 2204 3517 -262 -217 -32 C ANISOU 4540 CD1 LEU D 73 5098 2213 3688 -294 -260 37 C ANISOU 4541 CD2 LEU D 73 5001 2069 3390 -273 -235 -121 C ANISOU 4542 N TYR D 74 5520 2997 4001 -138 -123 132 N ANISOU 4543 CA TYR D 74 5482 3100 3907 -74 -104 143 C ANISOU 4544 C TYR D 74 5549 3097 4034 -89 -130 183 C ANISOU 4545 O TYR D 74 5542 3019 4167 -114 -138 289 O ANISOU 4546 CB TYR D 74 5495 3328 3940 6 -53 272 C ANISOU 4547 CG TYR D 74 5696 3747 4080 98 -32 322 C ANISOU 4548 CD1 TYR D 74 5729 3871 3972 129 -51 168 C ANISOU 4549 CD2 TYR D 74 5739 3946 4229 158 9 535 C ANISOU 4550 CE1 TYR D 74 5881 4284 4059 224 -43 210 C ANISOU 4551 CE2 TYR D 74 5932 4395 4359 266 36 611 C ANISOU 4552 CZ TYR D 74 5988 4565 4242 304 4 440 C ANISOU 4553 OH TYR D 74 6468 5351 4649 420 17 508 O ANISOU 4554 N ILE D 75 6656 3255 5063 -712 -449 -535 N ANISOU 4555 CA ILE D 75 6809 3272 5241 -734 -442 -574 C ANISOU 4556 C ILE D 75 6817 3266 5269 -678 -411 -526 C ANISOU 4557 O ILE D 75 7049 3532 5447 -613 -402 -530 O ANISOU 4558 CB ILE D 75 6827 3217 5179 -729 -447 -665 C ANISOU 4559 CG1 ILE D 75 6786 3192 5077 -663 -428 -669 C ANISOU 4560 CG2 ILE D 75 6864 3303 5191 -771 -479 -707 C ANISOU 4561 CD1 ILE D 75 6827 3191 5060 -651 -424 -728 C ANISOU 4562 N TYR D 76 6810 3220 5356 -701 -399 -476 N ANISOU 4563 CA TYR D 76 6728 3151 5297 -640 -365 -416 C ANISOU 4564 C TYR D 76 6889 3176 5523 -663 -350 -419 C ANISOU 4565 O TYR D 76 6806 2987 5476 -728 -371 -473 O ANISOU 4566 CB TYR D 76 6653 3226 5291 -614 -351 -296 C ANISOU 4567 CG TYR D 76 6660 3233 5444 -690 -354 -223 C ANISOU 4568 CD1 TYR D 76 6681 3249 5500 -772 -392 -254 C ANISOU 4569 CD2 TYR D 76 6655 3223 5560 -683 -323 -123 C ANISOU 4570 CE1 TYR D 76 6722 3281 5706 -851 -407 -194 C ANISOU 4571 CE2 TYR D 76 6779 3332 5858 -762 -330 -48 C ANISOU 4572 CZ TYR D 76 6749 3294 5876 -850 -377 -88 C ANISOU 4573 OH TYR D 76 6859 3387 6189 -936 -396 -17 O ANISOU 4574 N GLN D 77 6896 3197 5548 -602 -315 -363 N ANISOU 4575 CA GLN D 77 7202 3386 5923 -607 -292 -348 C ANISOU 4576 C GLN D 77 7120 3404 5916 -548 -252 -219 C ANISOU 4577 O GLN D 77 7006 3398 5733 -463 -238 -202 O ANISOU 4578 CB GLN D 77 7339 3427 5966 -571 -286 -438 C ANISOU 4579 CG GLN D 77 7629 3600 6312 -559 -258 -423 C ANISOU 4580 CD GLN D 77 7804 3707 6399 -516 -248 -500 C ANISOU 4581 OE1 GLN D 77 8065 4002 6571 -503 -262 -560 O ANISOU 4582 NE2 GLN D 77 8089 3898 6721 -493 -220 -487 N ANISOU 4583 N ASN D 78 7285 3542 6233 -590 -238 -127 N ANISOU 4584 CA ASN D 78 7347 3714 6387 -529 -191 20 C ANISOU 4585 C ASN D 78 7500 3783 6516 -472 -159 7 C ANISOU 4586 O ASN D 78 7692 3793 6742 -517 -164 -51 O ANISOU 4587 CB ASN D 78 7291 3661 6540 -595 -183 145 C ANISOU 4588 CG ASN D 78 7174 3671 6466 -642 -209 187 C ANISOU 4589 OD1 ASN D 78 7115 3526 6498 -744 -250 152 O ANISOU 4590 ND2 ASN D 78 7044 3755 6269 -560 -189 257 N ANISOU 4591 N ILE D 79 7599 4024 6551 -365 -130 54 N ANISOU 4592 CA ILE D 79 7743 4124 6667 -300 -101 48 C ANISOU 4593 C ILE D 79 7963 4536 6933 -195 -53 193 C ANISOU 4594 O ILE D 79 8193 4924 7226 -175 -40 306 O ANISOU 4595 CB ILE D 79 7533 3892 6302 -267 -129 -90 C ANISOU 4596 CG1 ILE D 79 7440 3988 6121 -188 -150 -98 C ANISOU 4597 CG2 ILE D 79 7522 3726 6247 -354 -167 -213 C ANISOU 4598 CD1 ILE D 79 7403 3928 5976 -160 -185 -223 C ANISOU 4599 N LYS D 80 8147 4714 7089 -122 -26 197 N ANISOU 4600 CA LYS D 80 8267 5028 7231 -2 18 322 C ANISOU 4601 C LYS D 80 8389 5144 7247 70 14 237 C ANISOU 4602 O LYS D 80 8542 5209 7448 82 49 267 O ANISOU 4603 CB LYS D 80 8454 5200 7602 -8 79 494 C ANISOU 4604 CG LYS D 80 8528 5287 7832 -87 83 604 C ANISOU 4605 CD LYS D 80 8662 5421 8188 -87 144 797 C ANISOU 4606 CE LYS D 80 8814 5313 8420 -139 152 757 C ANISOU 4607 NZ LYS D 80 8943 5437 8793 -139 208 956 N ANISOU 4608 N GLU D 81 8359 5204 7089 116 -33 128 N ANISOU 4609 CA GLU D 81 8542 5390 7192 174 -52 37 C ANISOU 4610 C GLU D 81 8471 5540 7035 290 -91 1 C ANISOU 4611 O GLU D 81 7793 4997 6336 323 -107 25 O ANISOU 4612 CB GLU D 81 8704 5360 7308 82 -91 -103 C ANISOU 4613 CG GLU D 81 8862 5303 7529 -12 -64 -99 C ANISOU 4614 CD GLU D 81 9159 5445 7771 -85 -97 -227 C ANISOU 4615 OE1 GLU D 81 9551 5888 8094 -73 -138 -309 O ANISOU 4616 OE2 GLU D 81 9246 5366 7892 -148 -84 -244 O ANISOU 4617 N ASN D 82 8796 5900 7315 354 -111 -64 N ANISOU 4618 CA ASN D 82 8742 6042 7190 470 -165 -130 C ANISOU 4619 C ASN D 82 8828 6028 7239 419 -240 -293 C ANISOU 4620 O ASN D 82 8929 6004 7360 372 -241 -341 O ANISOU 4621 CB ASN D 82 8750 6203 7199 592 -137 -71 C ANISOU 4622 CG ASN D 82 8654 6323 7030 723 -206 -158 C ANISOU 4623 OD1 ASN D 82 8698 6379 7028 721 -280 -274 O ANISOU 4624 ND2 ASN D 82 8866 6703 7233 843 -188 -110 N ANISOU 4625 N TRP D 83 8878 6143 7246 437 -301 -367 N ANISOU 4626 CA TRP D 83 8802 5984 7162 392 -376 -506 C ANISOU 4627 C TRP D 83 8802 6146 7132 508 -459 -606 C ANISOU 4628 O TRP D 83 9112 6410 7453 486 -533 -718 O ANISOU 4629 CB TRP D 83 8740 5842 7091 311 -384 -516 C ANISOU 4630 CG TRP D 83 8592 5518 6976 187 -331 -465 C ANISOU 4631 CD1 TRP D 83 8462 5335 6884 157 -262 -364 C ANISOU 4632 CD2 TRP D 83 8474 5276 6859 88 -347 -510 C ANISOU 4633 NE1 TRP D 83 8492 5201 6935 44 -246 -368 N ANISOU 4634 CE2 TRP D 83 8379 5056 6793 3 -294 -452 C ANISOU 4635 CE3 TRP D 83 8503 5287 6874 68 -404 -594 C ANISOU 4636 CZ2 TRP D 83 8269 4825 6682 -93 -298 -483 C ANISOU 4637 CZ3 TRP D 83 8439 5105 6815 -29 -398 -606 C ANISOU 4638 CH2 TRP D 83 8487 5050 6876 -106 -347 -554 C ANISOU 4639 N SER D 84 8685 6217 6988 635 -451 -568 N ANISOU 4640 CA SER D 84 8647 6359 6913 767 -539 -675 C ANISOU 4641 C SER D 84 8280 5951 6601 759 -608 -790 C ANISOU 4642 O SER D 84 8124 5961 6428 879 -678 -871 O ANISOU 4643 CB SER D 84 8926 6891 7135 922 -505 -586 C ANISOU 4644 OG SER D 84 9390 7424 7570 936 -448 -470 O ANISOU 4645 N MSE D 85 8107 5575 6499 628 -592 -799 N ANISOU 4646 CA MSE D 85 8104 5543 6574 614 -652 -887 C ANISOU 4647 C MSE D 85 7796 5054 6348 491 -691 -951 C ANISOU 4648 O MSE D 85 7777 4977 6423 444 -717 -987 O ANISOU 4649 CB MSE D 85 8325 5749 6815 605 -578 -800 C ANISOU 4650 CG MSE D 85 8500 5727 7004 484 -488 -712 C ANISOU 4651 SE MSE D 85 8953 6170 7390 483 -381 -559 SE ANISOU 4652 CE MSE D 85 9137 6612 7544 656 -351 -475 C ANISOU 4653 N TYR D 86 7670 4859 6194 446 -692 -955 N ANISOU 4654 CA TYR D 86 7559 4593 6158 338 -718 -996 C ANISOU 4655 C TYR D 86 7827 4893 6439 377 -812 -1098 C ANISOU 4656 O TYR D 86 7922 5106 6447 468 -826 -1110 O ANISOU 4657 CB TYR D 86 7395 4302 5954 241 -627 -901 C ANISOU 4658 CG TYR D 86 7128 3978 5680 207 -543 -816 C ANISOU 4659 CD1 TYR D 86 6993 3787 5618 170 -542 -826 C ANISOU 4660 CD2 TYR D 86 7068 3929 5555 219 -468 -723 C ANISOU 4661 CE1 TYR D 86 7007 3750 5619 153 -467 -755 C ANISOU 4662 CE2 TYR D 86 7078 3871 5570 194 -397 -653 C ANISOU 4663 CZ TYR D 86 7085 3817 5628 166 -396 -675 C ANISOU 4664 OH TYR D 86 7246 3910 5786 154 -327 -613 O ANISOU 4665 N ASN D 87 8049 5013 6780 310 -871 -1162 N ANISOU 4666 CA ASN D 87 8562 5529 7336 343 -969 -1268 C ANISOU 4667 C ASN D 87 8843 5687 7628 258 -945 -1235 C ANISOU 4668 O ASN D 87 9498 6376 8207 303 -958 -1253 O ANISOU 4669 CB ASN D 87 8728 5683 7671 345 -1079 -1375 C ANISOU 4670 CG ASN D 87 9117 6217 8058 441 -1124 -1429 C ANISOU 4671 OD1 ASN D 87 9497 6714 8302 517 -1069 -1380 O ANISOU 4672 ND2 ASN D 87 9380 6481 8484 440 -1227 -1526 N ANISOU 4673 N ASN D 88 8751 5472 7631 147 -910 -1185 N ANISOU 4674 CA ASN D 88 8665 5287 7564 74 -889 -1151 C ANISOU 4675 C ASN D 88 8299 4868 7111 1 -778 -1040 C ANISOU 4676 O ASN D 88 7938 4500 6729 -18 -720 -989 O ANISOU 4677 CB ASN D 88 8994 5533 8087 14 -943 -1175 C ANISOU 4678 CG ASN D 88 9668 6232 8879 77 -1071 -1301 C ANISOU 4679 OD1 ASN D 88 10365 7022 9489 179 -1121 -1382 O ANISOU 4680 ND2 ASN D 88 9871 6362 9290 24 -1128 -1317 N ANISOU 4681 N PHE D 89 7984 4515 6752 -33 -755 -1013 N ANISOU 4682 CA PHE D 89 7881 4365 6572 -100 -669 -930 C ANISOU 4683 C PHE D 89 7349 3755 6130 -173 -659 -903 C ANISOU 4684 O PHE D 89 7414 3806 6277 -173 -708 -930 O ANISOU 4685 CB PHE D 89 8072 4607 6654 -75 -654 -913 C ANISOU 4686 CG PHE D 89 8436 4939 6943 -137 -579 -839 C ANISOU 4687 CD1 PHE D 89 8527 4961 7048 -210 -553 -814 C ANISOU 4688 CD2 PHE D 89 8506 5060 6941 -117 -539 -794 C ANISOU 4689 CE1 PHE D 89 8688 5100 7143 -261 -499 -767 C ANISOU 4690 CE2 PHE D 89 8651 5166 7045 -179 -485 -736 C ANISOU 4691 CZ PHE D 89 8730 5171 7130 -251 -470 -734 C ANISOU 4692 N TYR D 90 6866 3232 5637 -223 -595 -846 N ANISOU 4693 CA TYR D 90 6587 2915 5438 -275 -574 -802 C ANISOU 4694 C TYR D 90 6369 2677 5116 -316 -511 -756 C ANISOU 4695 O TYR D 90 6493 2788 5143 -322 -466 -745 O ANISOU 4696 CB TYR D 90 6498 2824 5430 -282 -557 -778 C ANISOU 4697 CG TYR D 90 6309 2630 5347 -320 -531 -714 C ANISOU 4698 CD1 TYR D 90 6189 2512 5389 -334 -578 -702 C ANISOU 4699 CD2 TYR D 90 6138 2460 5124 -333 -460 -659 C ANISOU 4700 CE1 TYR D 90 6104 2447 5424 -362 -547 -617 C ANISOU 4701 CE2 TYR D 90 6124 2476 5202 -350 -430 -586 C ANISOU 4702 CZ TYR D 90 6123 2494 5375 -366 -469 -554 C ANISOU 4703 OH TYR D 90 5994 2418 5358 -378 -431 -456 O ANISOU 4704 N ILE D 91 6163 2473 4946 -340 -513 -732 N ANISOU 4705 CA ILE D 91 6118 2431 4811 -372 -464 -696 C ANISOU 4706 C ILE D 91 5980 2312 4755 -389 -440 -637 C ANISOU 4707 O ILE D 91 5994 2337 4887 -388 -470 -616 O ANISOU 4708 CB ILE D 91 6159 2494 4790 -371 -484 -711 C ANISOU 4709 CG1 ILE D 91 6237 2586 4794 -344 -499 -745 C ANISOU 4710 CG2 ILE D 91 6175 2528 4728 -405 -443 -679 C ANISOU 4711 CD1 ILE D 91 6251 2645 4758 -333 -518 -749 C ANISOU 4712 N GLU D 92 5924 2266 4641 -396 -386 -607 N ANISOU 4713 CA GLU D 92 5895 2292 4667 -395 -350 -537 C ANISOU 4714 C GLU D 92 5845 2276 4503 -404 -329 -535 C ANISOU 4715 O GLU D 92 5810 2233 4340 -406 -305 -569 O ANISOU 4716 CB GLU D 92 5996 2406 4770 -377 -308 -511 C ANISOU 4717 CG GLU D 92 6058 2559 4903 -358 -265 -419 C ANISOU 4718 CD GLU D 92 6160 2696 5011 -326 -222 -386 C ANISOU 4719 OE1 GLU D 92 6275 2750 5063 -321 -224 -442 O ANISOU 4720 OE2 GLU D 92 6207 2843 5139 -301 -183 -292 O ANISOU 4721 N ILE D 93 5739 2208 4455 -407 -344 -501 N ANISOU 4722 CA ILE D 93 5755 2271 4366 -413 -332 -502 C ANISOU 4723 C ILE D 93 5777 2387 4454 -395 -304 -413 C ANISOU 4724 O ILE D 93 5767 2386 4607 -388 -310 -348 O ANISOU 4725 CB ILE D 93 5715 2200 4297 -426 -376 -548 C ANISOU 4726 CG1 ILE D 93 5723 2258 4190 -440 -369 -558 C ANISOU 4727 CG2 ILE D 93 5677 2150 4399 -412 -415 -527 C ANISOU 4728 CD1 ILE D 93 5689 2218 4133 -446 -406 -588 C ANISOU 4729 N GLN D 94 5807 2493 4367 -386 -277 -410 N ANISOU 4730 CA GLN D 94 5822 2632 4414 -355 -242 -322 C ANISOU 4731 C GLN D 94 5818 2686 4305 -360 -252 -345 C ANISOU 4732 O GLN D 94 5805 2673 4153 -372 -261 -421 O ANISOU 4733 CB GLN D 94 5927 2829 4466 -311 -191 -289 C ANISOU 4734 CG GLN D 94 6005 3074 4578 -259 -146 -179 C ANISOU 4735 CD GLN D 94 6126 3314 4635 -194 -94 -145 C ANISOU 4736 OE1 GLN D 94 6173 3307 4601 -187 -94 -217 O ANISOU 4737 NE2 GLN D 94 6186 3551 4728 -133 -47 -32 N ANISOU 4738 N ASN D 95 5762 2677 4334 -350 -254 -276 N ANISOU 4739 CA ASN D 95 5784 2777 4275 -347 -260 -278 C ANISOU 4740 C ASN D 95 5863 3023 4344 -295 -210 -190 C ANISOU 4741 O ASN D 95 5879 3087 4503 -265 -179 -76 O ANISOU 4742 CB ASN D 95 5717 2671 4301 -354 -291 -255 C ANISOU 4743 CG ASN D 95 5714 2762 4217 -346 -294 -248 C ANISOU 4744 OD1 ASN D 95 5719 2853 4092 -348 -284 -281 O ANISOU 4745 ND2 ASN D 95 5719 2749 4300 -335 -314 -217 N ANISOU 4746 N LYS D 96 5948 3206 4273 -279 -204 -238 N ANISOU 4747 CA LYS D 96 6029 3477 4319 -211 -158 -162 C ANISOU 4748 C LYS D 96 6085 3649 4381 -192 -155 -101 C ANISOU 4749 O LYS D 96 6206 3945 4512 -125 -110 -2 O ANISOU 4750 CB LYS D 96 6097 3606 4218 -184 -161 -258 C ANISOU 4751 CG LYS D 96 6103 3506 4218 -189 -157 -309 C ANISOU 4752 CD LYS D 96 6195 3650 4154 -147 -162 -407 C ANISOU 4753 CE LYS D 96 6265 3948 4166 -41 -116 -342 C ANISOU 4754 NZ LYS D 96 6381 4103 4123 12 -133 -464 N ANISOU 4755 N ASN D 97 6079 3563 4373 -240 -198 -147 N ANISOU 4756 CA ASN D 97 6102 3696 4400 -219 -194 -88 C ANISOU 4757 C ASN D 97 6154 3727 4642 -195 -170 40 C ANISOU 4758 O ASN D 97 6158 3603 4775 -214 -176 55 O ANISOU 4759 CB ASN D 97 6054 3597 4281 -269 -246 -174 C ANISOU 4760 CG ASN D 97 6047 3615 4127 -300 -278 -291 C ANISOU 4761 OD1 ASN D 97 5977 3435 4030 -332 -294 -368 O ANISOU 4762 ND2 ASN D 97 6095 3801 4094 -293 -293 -306 N ANISOU 4763 N LYS D 98 6214 3916 4728 -153 -147 131 N ANISOU 4764 CA LYS D 98 6240 3920 4954 -128 -128 259 C ANISOU 4765 C LYS D 98 6203 3723 4962 -165 -184 196 C ANISOU 4766 O LYS D 98 6130 3548 5071 -160 -196 249 O ANISOU 4767 CB LYS D 98 6317 4204 5050 -57 -76 395 C ANISOU 4768 CG LYS D 98 6422 4513 5122 9 -13 484 C ANISOU 4769 CD LYS D 98 6460 4777 5187 91 40 632 C ANISOU 4770 CE LYS D 98 6573 5130 5255 179 106 727 C ANISOU 4771 NZ LYS D 98 6632 5432 5342 270 162 883 N ANISOU 4772 N SER D 99 6170 3681 4771 -195 -222 85 N ANISOU 4773 CA SER D 99 6137 3532 4752 -214 -272 23 C ANISOU 4774 C SER D 99 6031 3262 4650 -258 -311 -76 C ANISOU 4775 O SER D 99 5918 3140 4469 -286 -304 -123 O ANISOU 4776 CB SER D 99 6240 3731 4711 -221 -289 -20 C ANISOU 4777 OG SER D 99 6371 4027 4838 -173 -254 73 O ANISOU 4778 N SER D 100 5937 3049 4633 -252 -354 -110 N ANISOU 4779 CA SER D 100 5904 2880 4608 -276 -396 -202 C ANISOU 4780 C SER D 100 5845 2841 4385 -306 -412 -287 C ANISOU 4781 O SER D 100 5830 2918 4284 -303 -413 -284 O ANISOU 4782 CB SER D 100 5911 2783 4734 -241 -445 -223 C ANISOU 4783 OG SER D 100 5930 2854 4683 -209 -460 -233 O ANISOU 4784 N GLN D 101 5848 2766 4361 -336 -425 -351 N ANISOU 4785 CA GLN D 101 5876 2803 4272 -366 -440 -416 C ANISOU 4786 C GLN D 101 5933 2782 4358 -340 -482 -466 C ANISOU 4787 O GLN D 101 5972 2752 4502 -303 -505 -469 O ANISOU 4788 CB GLN D 101 5858 2759 4204 -408 -422 -450 C ANISOU 4789 CG GLN D 101 5869 2854 4181 -413 -386 -415 C ANISOU 4790 CD GLN D 101 5877 2992 4105 -418 -384 -406 C ANISOU 4791 OE1 GLN D 101 5872 3019 4071 -427 -406 -416 O ANISOU 4792 NE2 GLN D 101 5921 3129 4106 -407 -357 -387 N ANISOU 4793 N LYS D 102 5997 2871 4340 -351 -494 -503 N ANISOU 4794 CA LYS D 102 6122 2959 4471 -309 -529 -547 C ANISOU 4795 C LYS D 102 6182 3006 4479 -342 -522 -574 C ANISOU 4796 O LYS D 102 6243 3116 4485 -392 -502 -558 O ANISOU 4797 CB LYS D 102 6226 3145 4543 -256 -548 -536 C ANISOU 4798 CG LYS D 102 6367 3281 4750 -212 -558 -510 C ANISOU 4799 CD LYS D 102 6483 3474 4831 -145 -578 -506 C ANISOU 4800 CE LYS D 102 6530 3663 4784 -173 -552 -460 C ANISOU 4801 NZ LYS D 102 6574 3796 4796 -98 -568 -445 N ANISOU 4802 N ILE D 103 6323 3079 4653 -315 -542 -614 N ANISOU 4803 CA ILE D 103 6466 3208 4760 -335 -532 -630 C ANISOU 4804 C ILE D 103 6658 3414 4954 -261 -565 -663 C ANISOU 4805 O ILE D 103 6609 3356 4942 -197 -604 -697 O ANISOU 4806 CB ILE D 103 6500 3156 4822 -376 -512 -642 C ANISOU 4807 CG1 ILE D 103 6481 3066 4890 -340 -537 -672 C ANISOU 4808 CG2 ILE D 103 6582 3249 4889 -426 -482 -616 C ANISOU 4809 CD1 ILE D 103 6477 2998 4917 -373 -513 -673 C ANISOU 4810 N ASN D 104 6940 3721 5203 -263 -552 -655 N ANISOU 4811 CA ASN D 104 7247 4074 5499 -180 -576 -678 C ANISOU 4812 C ASN D 104 7535 4357 5779 -205 -546 -654 C ANISOU 4813 O ASN D 104 7732 4555 5970 -274 -511 -607 O ANISOU 4814 CB ASN D 104 7432 4387 5638 -109 -590 -658 C ANISOU 4815 CG ASN D 104 7673 4724 5850 -156 -552 -576 C ANISOU 4816 OD1 ASN D 104 7798 4877 5980 -181 -525 -533 O ANISOU 4817 ND2 ASN D 104 7583 4691 5745 -166 -552 -550 N ANISOU 4818 N LEU D 105 7671 4485 5926 -145 -565 -691 N ANISOU 4819 CA LEU D 105 7896 4708 6152 -153 -536 -664 C ANISOU 4820 C LEU D 105 7603 4559 5826 -86 -523 -607 C ANISOU 4821 O LEU D 105 7434 4497 5624 0 -551 -618 O ANISOU 4822 CB LEU D 105 8240 4994 6531 -116 -562 -726 C ANISOU 4823 CG LEU D 105 8543 5176 6892 -173 -570 -763 C ANISOU 4824 CD1 LEU D 105 8752 5344 7148 -148 -587 -802 C ANISOU 4825 CD2 LEU D 105 8578 5150 6917 -266 -522 -720 C ANISOU 4826 N SER D 106 7471 4434 5712 -117 -481 -541 N ANISOU 4827 CA SER D 106 7358 4471 5596 -57 -456 -455 C ANISOU 4828 C SER D 106 7161 4253 5433 -53 -423 -417 C ANISOU 4829 O SER D 106 6889 3857 5204 -143 -398 -405 O ANISOU 4830 CB SER D 106 7311 4485 5576 -116 -430 -368 C ANISOU 4831 OG SER D 106 7578 4626 5897 -235 -408 -354 O ANISOU 4832 N ILE D 107 7032 3946 5306 -147 -352 213 N ANISOU 4833 CA ILE D 107 7199 4048 5429 -122 -342 185 C ANISOU 4834 C ILE D 107 7244 4113 5495 -145 -364 213 C ANISOU 4835 O ILE D 107 7118 4095 5463 -141 -362 238 O ANISOU 4836 CB ILE D 107 7159 4052 5439 -65 -300 155 C ANISOU 4837 CG1 ILE D 107 7107 4010 5375 -55 -282 140 C ANISOU 4838 CG2 ILE D 107 7212 4053 5447 -28 -286 129 C ANISOU 4839 CD1 ILE D 107 7139 3953 5298 -54 -285 122 C ANISOU 4840 N GLN D 108 7568 4329 5720 -168 -387 208 N ANISOU 4841 CA GLN D 108 7752 4523 5907 -205 -415 238 C ANISOU 4842 C GLN D 108 7761 4458 5874 -166 -402 208 C ANISOU 4843 O GLN D 108 7721 4277 5708 -147 -404 178 O ANISOU 4844 CB GLN D 108 8115 4808 6163 -289 -469 272 C ANISOU 4845 CG GLN D 108 8505 5229 6550 -351 -508 317 C ANISOU 4846 CD GLN D 108 9163 5811 7088 -454 -569 359 C ANISOU 4847 OE1 GLN D 108 9708 6389 7618 -524 -610 406 O ANISOU 4848 NE2 GLN D 108 9468 6020 7304 -470 -580 346 N ANISOU 4849 N SER D 109 7453 4245 5664 -147 -389 218 N ANISOU 4850 CA SER D 109 7452 4193 5640 -111 -377 194 C ANISOU 4851 C SER D 109 7694 4343 5784 -172 -424 219 C ANISOU 4852 O SER D 109 7904 4562 5967 -248 -465 261 O ANISOU 4853 CB SER D 109 7109 3978 5431 -68 -345 194 C ANISOU 4854 OG SER D 109 6960 3943 5363 -103 -364 241 O ANISOU 4855 N LYS D 110 7999 4563 6030 -144 -420 197 N ANISOU 4856 CA LYS D 110 8345 4791 6255 -206 -470 219 C ANISOU 4857 C LYS D 110 8310 4900 6322 -271 -495 275 C ANISOU 4858 O LYS D 110 8521 5051 6443 -355 -547 313 O ANISOU 4859 CB LYS D 110 8628 4941 6441 -149 -457 180 C ANISOU 4860 CG LYS D 110 9067 5214 6716 -213 -513 199 C ANISOU 4861 CD LYS D 110 9412 5405 6940 -145 -502 158 C ANISOU 4862 CE LYS D 110 9761 5558 7097 -218 -566 179 C ANISOU 4863 NZ LYS D 110 9836 5464 7033 -139 -554 138 N ANISOU 4864 N ASN D 111 8327 5105 6512 -234 -461 286 N ANISOU 4865 CA ASN D 111 8091 5030 6374 -274 -478 342 C ANISOU 4866 C ASN D 111 7600 4633 5901 -337 -508 394 C ANISOU 4867 O ASN D 111 7347 4548 5733 -364 -521 450 O ANISOU 4868 CB ASN D 111 8247 5325 6680 -195 -430 330 C ANISOU 4869 CG ASN D 111 8470 5716 6999 -212 -441 384 C ANISOU 4870 OD1 ASN D 111 8822 6171 7454 -147 -407 380 O ANISOU 4871 ND2 ASN D 111 8872 6151 7360 -298 -490 440 N ANISOU 4872 N AMSE D 112 7470 4404 5687 -355 -518 378 N ANISOU 4873 N BMSE D 112 7508 4442 5724 -357 -519 380 N ANISOU 4874 CA AMSE D 112 7383 4386 5601 -414 -546 422 C ANISOU 4875 CA BMSE D 112 7391 4404 5614 -417 -547 426 C ANISOU 4876 C AMSE D 112 7106 4279 5468 -351 -507 429 C ANISOU 4877 C BMSE D 112 7168 4347 5532 -352 -508 431 C ANISOU 4878 O AMSE D 112 6975 4257 5369 -382 -524 473 O ANISOU 4879 O BMSE D 112 7116 4407 5515 -382 -524 476 O ANISOU 4880 CB AMSE D 112 7399 4462 5580 -523 -606 495 C ANISOU 4881 CB BMSE D 112 7358 4454 5562 -519 -603 501 C ANISOU 4882 CG AMSE D 112 7675 4527 5670 -600 -656 492 C ANISOU 4883 CG BMSE D 112 7455 4395 5525 -579 -643 501 C ANISOU 4884 SE AMSE D 112 7828 4383 5628 -573 -653 420 SE ANISOU 4885 SE BMSE D 112 7484 4419 5421 -761 -740 594 SE ANISOU 4886 CE AMSE D 112 8180 4474 5778 -586 -683 392 C ANISOU 4887 CE BMSE D 112 7294 4627 5457 -763 -730 682 C ANISOU 4888 N PHE D 113 7067 4254 5500 -263 -458 386 N ANISOU 4889 CA PHE D 113 6908 4207 5441 -200 -424 385 C ANISOU 4890 C PHE D 113 6787 4010 5278 -190 -413 354 C ANISOU 4891 O PHE D 113 6507 3610 4940 -171 -397 305 O ANISOU 4892 CB PHE D 113 7050 4368 5649 -124 -384 353 C ANISOU 4893 CG PHE D 113 7276 4710 5944 -112 -386 388 C ANISOU 4894 CD1 PHE D 113 7321 4775 5964 -174 -421 424 C ANISOU 4895 CD2 PHE D 113 7397 4897 6139 -38 -353 379 C ANISOU 4896 CE1 PHE D 113 7415 4991 6125 -162 -421 459 C ANISOU 4897 CE2 PHE D 113 7350 4954 6150 -17 -352 409 C ANISOU 4898 CZ PHE D 113 7375 5027 6166 -77 -384 450 C ANISOU 4899 N GLU D 114 6773 4078 5289 -202 -422 386 N ANISOU 4900 CA GLU D 114 6866 4115 5350 -196 -414 363 C ANISOU 4901 C GLU D 114 6629 3907 5170 -123 -374 338 C ANISOU 4902 O GLU D 114 6482 3856 5086 -82 -364 360 O ANISOU 4903 CB GLU D 114 7058 4374 5531 -247 -446 413 C ANISOU 4904 CG GLU D 114 7329 4582 5712 -338 -493 438 C ANISOU 4905 CD GLU D 114 7791 4853 6057 -352 -495 388 C ANISOU 4906 OE1 GLU D 114 7762 4774 6035 -292 -457 339 O ANISOU 4907 OE2 GLU D 114 8578 5538 6734 -423 -535 401 O ANISOU 4908 N PHE D 115 6725 3915 5228 -108 -354 294 N ANISOU 4909 CA PHE D 115 6695 3893 5228 -59 -325 272 C ANISOU 4910 C PHE D 115 6899 4073 5396 -74 -329 271 C ANISOU 4911 O PHE D 115 6780 3887 5222 -103 -335 253 O ANISOU 4912 CB PHE D 115 6651 3796 5176 -32 -297 227 C ANISOU 4913 CG PHE D 115 6636 3798 5194 -12 -290 224 C ANISOU 4914 CD1 PHE D 115 6696 3835 5230 -39 -309 233 C ANISOU 4915 CD2 PHE D 115 6615 3808 5217 28 -268 215 C ANISOU 4916 CE1 PHE D 115 6578 3731 5140 -21 -303 230 C ANISOU 4917 CE2 PHE D 115 6512 3723 5147 47 -261 213 C ANISOU 4918 CZ PHE D 115 6520 3716 5140 23 -277 220 C ANISOU 4919 N ARG D 116 7101 4324 5621 -47 -327 290 N ANISOU 4920 CA ARG D 116 7329 4530 5815 -57 -332 292 C ANISOU 4921 C ARG D 116 7371 4552 5849 -14 -316 282 C ANISOU 4922 O ARG D 116 7238 4428 5735 24 -305 280 O ANISOU 4923 CB ARG D 116 7516 4786 6006 -82 -360 339 C ANISOU 4924 CG ARG D 116 7620 4858 6074 -147 -384 344 C ANISOU 4925 CD ARG D 116 7773 5083 6222 -195 -419 396 C ANISOU 4926 NE ARG D 116 7821 5253 6321 -194 -432 444 N ANISOU 4927 CZ ARG D 116 8005 5461 6488 -259 -464 475 C ANISOU 4928 NH1 ARG D 116 8362 5700 6762 -325 -487 459 N ANISOU 4929 NH2 ARG D 116 8106 5696 6641 -260 -476 524 N ANISOU 4930 N LEU D 117 7465 4601 5899 -28 -318 273 N ANISOU 4931 CA LEU D 117 7512 4598 5906 -5 -311 264 C ANISOU 4932 C LEU D 117 7423 4524 5810 53 -314 289 C ANISOU 4933 O LEU D 117 7431 4595 5829 78 -325 324 O ANISOU 4934 CB LEU D 117 7525 4577 5872 -33 -321 265 C ANISOU 4935 CG LEU D 117 7614 4640 5947 -80 -315 239 C ANISOU 4936 CD1 LEU D 117 7748 4740 6032 -104 -324 241 C ANISOU 4937 CD2 LEU D 117 7518 4526 5848 -83 -295 210 C ANISOU 4938 N LYS D 118 7638 4685 5997 77 -304 274 N ANISOU 4939 CA LYS D 118 8121 5151 6446 144 -306 292 C ANISOU 4940 C LYS D 118 8456 5410 6684 170 -319 303 C ANISOU 4941 O LYS D 118 7884 4750 6050 130 -324 285 O ANISOU 4942 CB LYS D 118 8679 5654 6988 152 -296 270 C ANISOU 4943 CG LYS D 118 9287 6221 7540 226 -298 286 C ANISOU 4944 CD LYS D 118 9939 6812 8171 224 -291 265 C ANISOU 4945 CE LYS D 118 10441 7252 8597 304 -295 280 C ANISOU 4946 NZ LYS D 118 10818 7567 8951 292 -291 261 N ANISOU 4947 N GLU D 119 9091 6084 7298 241 -325 337 N ANISOU 4948 CA GLU D 119 10097 7015 8197 286 -337 352 C ANISOU 4949 C GLU D 119 10552 7294 8523 298 -344 330 C ANISOU 4950 O GLU D 119 11247 7950 9187 343 -339 328 O ANISOU 4951 CB GLU D 119 10259 7279 8363 378 -338 398 C ANISOU 4952 CG GLU D 119 10852 7805 8836 444 -350 418 C ANISOU 4953 CD GLU D 119 10933 7888 8915 390 -361 419 C ANISOU 4954 OE1 GLU D 119 10975 7980 9046 299 -360 403 O ANISOU 4955 OE2 GLU D 119 11327 8228 9210 445 -371 436 O ANISOU 4956 N GLY D 120 10645 7278 8533 250 -357 316 N ANISOU 4957 CA GLY D 120 10620 7072 8363 237 -372 300 C ANISOU 4958 C GLY D 120 10303 6743 8074 133 -371 274 C ANISOU 4959 O GLY D 120 10750 7064 8406 83 -390 267 O ANISOU 4960 N SER D 121 9481 6054 7394 100 -350 263 N ANISOU 4961 CA SER D 121 8653 5250 6603 19 -343 242 C ANISOU 4962 C SER D 121 8034 4595 5933 -43 -355 239 C ANISOU 4963 O SER D 121 8012 4588 5914 -33 -359 247 O ANISOU 4964 CB SER D 121 8554 5289 6645 10 -320 232 C ANISOU 4965 OG SER D 121 8665 5472 6814 16 -317 240 O ANISOU 4966 N GLU D 122 7497 4030 5354 -113 -361 232 N ANISOU 4967 CA GLU D 122 7490 3996 5290 -181 -374 234 C ANISOU 4968 C GLU D 122 7086 3734 4992 -223 -351 223 C ANISOU 4969 O GLU D 122 6877 3612 4854 -229 -332 215 O ANISOU 4970 CB GLU D 122 7817 4210 5486 -241 -400 242 C ANISOU 4971 CG GLU D 122 8266 4608 5842 -320 -423 252 C ANISOU 4972 CD GLU D 122 8554 4765 6023 -290 -445 259 C ANISOU 4973 OE1 GLU D 122 9184 5358 6653 -199 -441 259 O ANISOU 4974 OE2 GLU D 122 8291 4443 5670 -356 -468 268 O ANISOU 4975 N VAL D 123 6875 3540 4780 -244 -353 224 N ANISOU 4976 CA VAL D 123 6721 3500 4694 -276 -333 215 C ANISOU 4977 C VAL D 123 6689 3439 4584 -341 -350 225 C ANISOU 4978 O VAL D 123 6891 3531 4698 -346 -374 234 O ANISOU 4979 CB VAL D 123 6583 3417 4634 -237 -319 206 C ANISOU 4980 CG1 VAL D 123 6459 3326 4581 -186 -307 201 C ANISOU 4981 CG2 VAL D 123 6628 3403 4641 -225 -337 217 C ANISOU 4982 N PHE D 124 6532 3383 4449 -388 -337 225 N ANISOU 4983 CA PHE D 124 6580 3432 4430 -456 -352 240 C ANISOU 4984 C PHE D 124 6523 3477 4430 -446 -329 231 C ANISOU 4985 O PHE D 124 6462 3505 4446 -405 -301 216 O ANISOU 4986 CB PHE D 124 6608 3496 4407 -530 -364 261 C ANISOU 4987 CG PHE D 124 6661 3423 4380 -542 -390 269 C ANISOU 4988 CD1 PHE D 124 6599 3362 4372 -485 -376 257 C ANISOU 4989 CD2 PHE D 124 6882 3500 4451 -606 -432 289 C ANISOU 4990 CE1 PHE D 124 6721 3360 4408 -491 -400 264 C ANISOU 4991 CE2 PHE D 124 6912 3383 4377 -610 -460 295 C ANISOU 4992 CZ PHE D 124 6861 3345 4386 -550 -443 283 C ANISOU 4993 N LEU D 125 6621 3543 4477 -481 -343 238 N ANISOU 4994 CA LEU D 125 6669 3667 4555 -475 -326 231 C ANISOU 4995 C LEU D 125 6918 4001 4763 -544 -329 252 C ANISOU 4996 O LEU D 125 7065 4082 4827 -610 -359 272 O ANISOU 4997 CB LEU D 125 6613 3517 4477 -457 -340 226 C ANISOU 4998 CG LEU D 125 6538 3385 4441 -395 -342 217 C ANISOU 4999 CD1 LEU D 125 6620 3370 4477 -383 -362 227 C ANISOU 5000 CD2 LEU D 125 6541 3359 4444 -381 -348 216 C ANISOU 5001 N GLU D 126 7130 4356 5019 -528 -299 250 N ANISOU 5002 CA GLU D 126 7530 4879 5389 -586 -297 275 C ANISOU 5003 C GLU D 126 7720 5076 5565 -575 -290 269 C ANISOU 5004 O GLU D 126 7635 5064 5512 -515 -260 254 O ANISOU 5005 CB GLU D 126 7661 5193 5567 -568 -267 286 C ANISOU 5006 CG GLU D 126 7767 5469 5648 -626 -263 322 C ANISOU 5007 CD GLU D 126 7885 5803 5810 -600 -231 341 C ANISOU 5008 OE1 GLU D 126 8019 5941 5993 -534 -211 321 O ANISOU 5009 OE2 GLU D 126 8140 6235 6050 -645 -226 379 O ANISOU 5010 N GLY D 127 8036 5302 5817 -631 -320 280 N ANISOU 5011 CA GLY D 127 8350 5613 6110 -631 -319 276 C ANISOU 5012 C GLY D 127 8508 5934 6250 -676 -308 303 C ANISOU 5013 O GLY D 127 8544 6105 6298 -704 -300 327 O ANISOU 5014 N LYS D 128 9181 6607 6893 -685 -309 304 N ANISOU 5015 CA LYS D 128 9577 7173 7271 -724 -298 334 C ANISOU 5016 C LYS D 128 9653 7275 7288 -841 -333 376 C ANISOU 5017 O LYS D 128 9725 7536 7365 -882 -325 413 O ANISOU 5018 CB LYS D 128 9935 7508 7602 -708 -294 324 C ANISOU 5019 CG LYS D 128 10163 7700 7855 -604 -265 287 C ANISOU 5020 CD LYS D 128 10389 7899 8040 -595 -264 280 C ANISOU 5021 CE LYS D 128 10630 8321 8256 -615 -247 310 C ANISOU 5022 NZ LYS D 128 10710 8572 8356 -540 -206 314 N ANISOU 5023 N ASN D 129 9743 7176 7311 -894 -375 376 N ANISOU 5024 CA ASN D 129 9869 7274 7344 -1012 -418 416 C ANISOU 5025 C ASN D 129 9875 7063 7285 -1025 -453 406 C ANISOU 5026 O ASN D 129 10399 7508 7699 -1121 -497 436 O ANISOU 5027 CB ASN D 129 9945 7322 7343 -1081 -442 435 C ANISOU 5028 CG ASN D 129 9864 7462 7309 -1072 -410 451 C ANISOU 5029 OD1 ASN D 129 9800 7611 7272 -1100 -395 485 O ANISOU 5030 ND2 ASN D 129 9730 7286 7180 -1028 -398 429 N ANISOU 5031 N ILE D 130 9623 6713 7086 -930 -437 368 N ANISOU 5032 CA ILE D 130 9262 6157 6661 -922 -467 360 C ANISOU 5033 C ILE D 130 9119 6044 6603 -850 -441 340 C ANISOU 5034 O ILE D 130 8827 5859 6419 -779 -402 319 O ANISOU 5035 CB ILE D 130 9204 5925 6557 -880 -482 341 C ANISOU 5036 CG1 ILE D 130 9004 5681 6261 -955 -510 361 C ANISOU 5037 CG2 ILE D 130 9296 5829 6579 -846 -507 334 C ANISOU 5038 CD1 ILE D 130 9012 5528 6217 -913 -526 346 C ANISOU 5039 N ILE D 131 9112 5922 6529 -871 -468 347 N ANISOU 5040 CA ILE D 131 8978 5794 6457 -812 -450 332 C ANISOU 5041 C ILE D 131 8952 5568 6376 -753 -469 315 C ANISOU 5042 O ILE D 131 8977 5427 6262 -791 -509 328 O ANISOU 5043 CB ILE D 131 9061 5934 6503 -887 -465 360 C ANISOU 5044 CG1 ILE D 131 8948 6043 6425 -954 -452 390 C ANISOU 5045 CG2 ILE D 131 8994 5884 6508 -823 -445 343 C ANISOU 5046 CD1 ILE D 131 8840 6124 6455 -873 -398 372 C ANISOU 5047 N TYR D 132 8829 5462 6351 -660 -442 290 N ANISOU 5048 CA TYR D 132 8667 5152 6150 -593 -455 281 C ANISOU 5049 C TYR D 132 8774 5236 6275 -551 -450 276 C ANISOU 5050 O TYR D 132 8607 5182 6227 -510 -419 262 O ANISOU 5051 CB TYR D 132 8347 4870 5916 -523 -434 265 C ANISOU 5052 CG TYR D 132 8138 4679 5694 -553 -438 268 C ANISOU 5053 CD1 TYR D 132 7894 4559 5488 -600 -422 269 C ANISOU 5054 CD2 TYR D 132 8036 4473 5531 -531 -457 272 C ANISOU 5055 CE1 TYR D 132 8044 4724 5620 -626 -424 272 C ANISOU 5056 CE2 TYR D 132 8064 4514 5543 -561 -461 274 C ANISOU 5057 CZ TYR D 132 8101 4669 5622 -611 -445 273 C ANISOU 5058 OH TYR D 132 8325 4907 5828 -639 -448 276 O ANISOU 5059 N SER D 133 9007 5306 6373 -562 -483 286 N ANISOU 5060 CA SER D 133 9065 5313 6422 -519 -483 283 C ANISOU 5061 C SER D 133 9237 5420 6604 -411 -477 274 C ANISOU 5062 O SER D 133 9140 5154 6367 -379 -504 282 O ANISOU 5063 CB SER D 133 9490 5579 6672 -583 -525 301 C ANISOU 5064 OG SER D 133 9518 5694 6690 -696 -534 320 O ANISOU 5065 N ASP D 134 9072 5391 6592 -355 -443 261 N ANISOU 5066 CA ASP D 134 9167 5470 6712 -263 -438 262 C ANISOU 5067 C ASP D 134 9064 5398 6667 -199 -424 259 C ANISOU 5068 O ASP D 134 8624 5044 6310 -217 -405 249 O ANISOU 5069 CB ASP D 134 9288 5704 6938 -255 -421 259 C ANISOU 5070 CG ASP D 134 9509 5889 7099 -305 -436 263 C ANISOU 5071 OD1 ASP D 134 10110 6378 7574 -350 -461 270 O ANISOU 5072 OD2 ASP D 134 9669 6126 7328 -303 -425 261 O ANISOU 5073 N LYS D 135 9231 5501 6784 -116 -431 271 N ANISOU 5074 CA LYS D 135 9144 5443 6737 -39 -420 275 C ANISOU 5075 C LYS D 135 8732 5184 6462 0 -401 284 C ANISOU 5076 O LYS D 135 8623 5090 6344 18 -407 298 O ANISOU 5077 CB LYS D 135 9311 5452 6744 37 -441 290 C ANISOU 5078 CG LYS D 135 9316 5491 6774 136 -429 300 C ANISOU 5079 CD LYS D 135 9577 5588 6852 230 -449 316 C ANISOU 5080 CE LYS D 135 9725 5788 7021 340 -434 331 C ANISOU 5081 NZ LYS D 135 10015 5913 7111 451 -452 347 N ANISOU 5082 N ILE D 136 9002 5562 6848 6 -381 278 N ANISOU 5083 CA ILE D 136 8870 5564 6829 27 -370 290 C ANISOU 5084 C ILE D 136 9007 5722 6942 114 -376 322 C ANISOU 5085 O ILE D 136 8668 5365 6577 175 -373 330 O ANISOU 5086 CB ILE D 136 8742 5524 6807 12 -351 277 C ANISOU 5087 CG1 ILE D 136 8858 5643 6943 -57 -341 250 C ANISOU 5088 CG2 ILE D 136 8727 5628 6884 26 -348 296 C ANISOU 5089 CD1 ILE D 136 8917 5776 7087 -63 -323 236 C ANISOU 5090 N LYS D 137 9425 6185 7362 121 -385 343 N ANISOU 5091 CA LYS D 137 9948 6766 7867 205 -390 382 C ANISOU 5092 C LYS D 137 9704 6701 7749 186 -387 409 C ANISOU 5093 O LYS D 137 10003 7030 8095 112 -391 400 O ANISOU 5094 CB LYS D 137 10339 7066 8142 232 -406 393 C ANISOU 5095 CG LYS D 137 10678 7416 8503 156 -413 386 C ANISOU 5096 CD LYS D 137 11005 7647 8708 186 -430 397 C ANISOU 5097 CE LYS D 137 11101 7754 8825 110 -437 390 C ANISOU 5098 NZ LYS D 137 11285 7879 9020 19 -433 352 N ANISOU 5099 N GLU D 138 9593 6705 7678 250 -384 445 N ANISOU 5100 CA GLU D 138 9393 6682 7585 224 -388 481 C ANISOU 5101 C GLU D 138 9052 6342 7318 136 -385 451 C ANISOU 5102 O GLU D 138 9763 7141 8086 79 -396 469 O ANISOU 5103 CB GLU D 138 9751 7109 7939 206 -404 513 C ANISOU 5104 CG GLU D 138 10091 7461 8199 307 -407 547 C ANISOU 5105 CD GLU D 138 10299 7753 8406 294 -423 584 C ANISOU 5106 OE1 GLU D 138 9946 7439 8111 197 -434 582 O ANISOU 5107 OE2 GLU D 138 10808 8282 8844 386 -424 615 O ANISOU 5108 N GLY D 139 8185 5371 6434 127 -371 408 N ANISOU 5109 CA GLY D 139 7665 4844 5968 63 -364 378 C ANISOU 5110 C GLY D 139 7284 4420 5578 -9 -369 356 C ANISOU 5111 O GLY D 139 7178 4314 5502 -55 -366 338 O ANISOU 5112 N OCS D 140 7130 4218 5367 -11 -377 357 N ANISOU 5113 CA OCS D 140 6860 3911 5081 -73 -382 340 C ANISOU 5114 CB OCS D 140 7014 4114 5226 -83 -401 373 C ANISOU 5115 SG OCS D 140 7232 4449 5504 -121 -419 410 S ANISOU 5116 C OCS D 140 6754 3702 4910 -87 -375 309 C ANISOU 5117 O OCS D 140 6485 3372 4581 -52 -377 312 O ANISOU 5118 OD1 OCS D 140 7188 4347 5446 -187 -423 384 O ANISOU 5119 OD2 OCS D 140 6876 4162 5195 -84 -413 427 O ANISOU 5120 OD3 OCS D 140 7046 4335 5305 -112 -438 455 O ANISOU 5121 N ILE D 141 6500 3427 4657 -139 -368 283 N ANISOU 5122 CA ILE D 141 6523 3386 4626 -168 -363 261 C ANISOU 5123 C ILE D 141 6650 3498 4720 -193 -377 270 C ANISOU 5124 O ILE D 141 6519 3397 4610 -217 -381 272 O ANISOU 5125 CB ILE D 141 6490 3367 4615 -196 -345 233 C ANISOU 5126 CG1 ILE D 141 6430 3331 4596 -171 -331 225 C ANISOU 5127 CG2 ILE D 141 6527 3373 4600 -232 -341 220 C ANISOU 5128 CD1 ILE D 141 6457 3385 4640 -185 -311 201 C ANISOU 5129 N GLU D 142 6866 3652 4867 -188 -388 277 N ANISOU 5130 CA GLU D 142 7000 3769 4965 -209 -401 286 C ANISOU 5131 C GLU D 142 7137 3878 5073 -264 -395 263 C ANISOU 5132 O GLU D 142 7271 3955 5147 -283 -398 257 O ANISOU 5133 CB GLU D 142 7200 3910 5091 -169 -417 307 C ANISOU 5134 CG GLU D 142 7343 4034 5193 -187 -431 318 C ANISOU 5135 CD GLU D 142 7500 4124 5260 -135 -448 340 C ANISOU 5136 OE1 GLU D 142 7545 4127 5262 -78 -448 346 O ANISOU 5137 OE2 GLU D 142 7757 4363 5477 -145 -460 350 O ANISOU 5138 N VAL D 143 7264 4042 5229 -291 -390 254 N ANISOU 5139 CA VAL D 143 7303 4075 5239 -331 -381 236 C ANISOU 5140 C VAL D 143 7261 3991 5143 -354 -397 247 C ANISOU 5141 O VAL D 143 7236 3970 5121 -354 -410 259 O ANISOU 5142 CB VAL D 143 7336 4137 5294 -337 -370 222 C ANISOU 5143 CG1 VAL D 143 7449 4253 5367 -362 -359 206 C ANISOU 5144 CG2 VAL D 143 7280 4111 5280 -311 -355 211 C ANISOU 5145 N PRO D 144 7313 4003 5136 -381 -401 245 N ANISOU 5146 CA PRO D 144 7325 3963 5084 -404 -419 255 C ANISOU 5147 C PRO D 144 7192 3857 4956 -431 -416 249 C ANISOU 5148 O PRO D 144 6999 3712 4792 -438 -398 234 O ANISOU 5149 CB PRO D 144 7415 4009 5105 -446 -424 254 C ANISOU 5150 CG PRO D 144 7426 4038 5139 -433 -414 249 C ANISOU 5151 CD PRO D 144 7350 4045 5158 -400 -391 237 C ANISOU 5152 N GLY D 145 7141 3767 4865 -440 -434 262 N ANISOU 5153 CA GLY D 145 7181 3819 4897 -468 -435 258 C ANISOU 5154 C GLY D 145 7211 3869 4899 -507 -421 244 C ANISOU 5155 O GLY D 145 7115 3756 4763 -533 -425 248 O ANISOU 5156 N GLU D 146 7219 3912 4917 -509 -407 231 N ANISOU 5157 CA GLU D 146 7368 4108 5040 -531 -390 221 C ANISOU 5158 C GLU D 146 7175 3983 4870 -524 -369 216 C ANISOU 5159 O GLU D 146 7248 4124 4923 -546 -356 218 O ANISOU 5160 CB GLU D 146 7497 4214 5114 -577 -405 233 C ANISOU 5161 CG GLU D 146 7688 4345 5282 -582 -425 240 C ANISOU 5162 CD GLU D 146 7732 4357 5265 -626 -440 251 C ANISOU 5163 OE1 GLU D 146 7843 4515 5352 -654 -429 248 O ANISOU 5164 OE2 GLU D 146 7985 4541 5487 -627 -464 265 O ANISOU 5165 N PHE D 147 7087 3891 4825 -494 -366 213 N ANISOU 5166 CA PHE D 147 6980 3850 4744 -486 -348 209 C ANISOU 5167 C PHE D 147 6980 3918 4752 -452 -320 194 C ANISOU 5168 O PHE D 147 6778 3676 4547 -418 -318 181 O ANISOU 5169 CB PHE D 147 7040 3883 4846 -457 -351 209 C ANISOU 5170 CG PHE D 147 7077 3987 4911 -449 -333 206 C ANISOU 5171 CD1 PHE D 147 7216 4152 5021 -494 -338 220 C ANISOU 5172 CD2 PHE D 147 7072 4017 4947 -405 -313 191 C ANISOU 5173 CE1 PHE D 147 7251 4263 5081 -494 -323 222 C ANISOU 5174 CE2 PHE D 147 7131 4147 5031 -395 -295 190 C ANISOU 5175 CZ PHE D 147 7168 4226 5052 -440 -299 206 C ANISOU 5176 N GLU D 148 6882 3922 4650 -460 -300 199 N ANISOU 5177 CA GLU D 148 6872 3995 4634 -412 -269 188 C ANISOU 5178 C GLU D 148 6918 4158 4712 -416 -253 200 C ANISOU 5179 O GLU D 148 7000 4335 4783 -464 -253 223 O ANISOU 5180 CB GLU D 148 6873 4039 4582 -415 -260 191 C ANISOU 5181 CG GLU D 148 6938 4186 4617 -346 -226 181 C ANISOU 5182 CD GLU D 148 7010 4317 4629 -337 -213 187 C ANISOU 5183 OE1 GLU D 148 7207 4495 4816 -396 -232 199 O ANISOU 5184 OE2 GLU D 148 6986 4358 4561 -264 -184 180 O ANISOU 5185 N GLY D 149 6889 4126 4720 -375 -242 189 N ANISOU 5186 CA GLY D 149 6933 4284 4796 -381 -228 202 C ANISOU 5187 C GLY D 149 6956 4299 4856 -324 -214 186 C ANISOU 5188 O GLY D 149 7015 4310 4898 -263 -203 164 O ANISOU 5189 N LYS D 150 6927 4301 4864 -351 -219 198 N ANISOU 5190 CA LYS D 150 6896 4280 4874 -305 -206 186 C ANISOU 5191 C LYS D 150 6750 4035 4756 -329 -230 186 C ANISOU 5192 O LYS D 150 6709 3950 4693 -386 -254 202 O ANISOU 5193 CB LYS D 150 7057 4610 5049 -311 -185 207 C ANISOU 5194 CG LYS D 150 7265 4954 5224 -287 -160 218 C ANISOU 5195 CD LYS D 150 7404 5299 5382 -303 -142 251 C ANISOU 5196 CE LYS D 150 7564 5624 5508 -272 -116 269 C ANISOU 5197 NZ LYS D 150 7766 5796 5670 -154 -85 240 N ANISOU 5198 N ILE D 151 6616 3858 4656 -282 -224 170 N ANISOU 5199 CA ILE D 151 6566 3732 4633 -288 -243 172 C ANISOU 5200 C ILE D 151 6558 3780 4666 -262 -226 168 C ANISOU 5201 O ILE D 151 6611 3868 4732 -213 -205 154 O ANISOU 5202 CB ILE D 151 6499 3568 4572 -265 -257 163 C ANISOU 5203 CG1 ILE D 151 6536 3557 4568 -293 -274 169 C ANISOU 5204 CG2 ILE D 151 6537 3557 4640 -258 -272 170 C ANISOU 5205 CD1 ILE D 151 6565 3514 4602 -281 -293 171 C ANISOU 5206 N TYR D 152 6523 3739 4634 -296 -239 182 N ANISOU 5207 CA TYR D 152 6524 3791 4671 -282 -227 183 C ANISOU 5208 C TYR D 152 6490 3665 4661 -256 -239 176 C ANISOU 5209 O TYR D 152 6543 3631 4682 -276 -263 185 O ANISOU 5210 CB TYR D 152 6527 3858 4644 -347 -236 208 C ANISOU 5211 CG TYR D 152 6560 4028 4663 -370 -221 223 C ANISOU 5212 CD1 TYR D 152 6538 4138 4674 -319 -187 219 C ANISOU 5213 CD2 TYR D 152 6703 4169 4752 -434 -239 242 C ANISOU 5214 CE1 TYR D 152 6588 4336 4707 -326 -170 237 C ANISOU 5215 CE2 TYR D 152 6697 4310 4735 -454 -225 261 C ANISOU 5216 CZ TYR D 152 6707 4470 4783 -396 -188 260 C ANISOU 5217 OH TYR D 152 6844 4773 4906 -401 -171 283 O ANISOU 5218 N VAL D 153 6466 3661 4684 -206 -223 162 N ANISOU 5219 CA VAL D 153 6573 3707 4822 -178 -231 159 C ANISOU 5220 C VAL D 153 6582 3770 4869 -156 -215 153 C ANISOU 5221 O VAL D 153 6591 3838 4895 -126 -193 142 O ANISOU 5222 CB VAL D 153 6526 3618 4789 -147 -235 150 C ANISOU 5223 CG1 VAL D 153 6605 3666 4905 -121 -244 155 C ANISOU 5224 CG2 VAL D 153 6527 3575 4754 -170 -252 157 C ANISOU 5225 N ASN D 154 6703 3861 4991 -166 -225 162 N ANISOU 5226 CA ASN D 154 6712 3917 5037 -148 -211 159 C ANISOU 5227 C ASN D 154 6508 3679 4878 -98 -209 148 C ANISOU 5228 O ASN D 154 6244 3352 4610 -88 -225 154 O ANISOU 5229 CB ASN D 154 7061 4243 5349 -189 -227 175 C ANISOU 5230 CG ASN D 154 7297 4536 5620 -178 -214 174 C ANISOU 5231 OD1 ASN D 154 7424 4718 5803 -133 -192 160 O ANISOU 5232 ND2 ASN D 154 7609 4821 5886 -223 -231 190 N ANISOU 5233 N PHE D 155 6503 3723 4910 -65 -189 136 N ANISOU 5234 CA PHE D 155 6784 3974 5225 -28 -190 129 C ANISOU 5235 C PHE D 155 6853 4006 5315 -20 -203 140 C ANISOU 5236 O PHE D 155 7015 4151 5503 2 -210 144 O ANISOU 5237 CB PHE D 155 6875 4107 5332 6 -169 114 C ANISOU 5238 CG PHE D 155 7234 4474 5648 25 -158 101 C ANISOU 5239 CD1 PHE D 155 7399 4567 5777 23 -173 98 C ANISOU 5240 CD2 PHE D 155 7406 4726 5806 49 -133 95 C ANISOU 5241 CE1 PHE D 155 7456 4604 5769 45 -165 85 C ANISOU 5242 CE2 PHE D 155 7437 4755 5777 83 -121 84 C ANISOU 5243 CZ PHE D 155 7578 4796 5868 82 -138 77 C ANISOU 5244 N ASN D 156 6935 4073 5373 -39 -209 149 N ANISOU 5245 CA ASN D 156 7103 4191 5541 -15 -220 159 C ANISOU 5246 C ASN D 156 7006 4036 5407 -7 -240 173 C ANISOU 5247 O ASN D 156 7015 4002 5397 25 -250 186 O ANISOU 5248 CB ASN D 156 7331 4397 5735 -31 -224 163 C ANISOU 5249 CG ASN D 156 7575 4591 5894 -83 -241 173 C ANISOU 5250 OD1 ASN D 156 7841 4906 6154 -121 -237 173 O ANISOU 5251 ND2 ASN D 156 7697 4608 5937 -83 -263 184 N ANISOU 5252 N SER D 157 6985 4016 5369 -30 -244 173 N ANISOU 5253 CA SER D 157 7050 4038 5401 -22 -262 189 C ANISOU 5254 C SER D 157 7049 4080 5453 3 -264 199 C ANISOU 5255 O SER D 157 7141 4167 5533 23 -278 220 O ANISOU 5256 CB SER D 157 7006 3978 5314 -63 -267 187 C ANISOU 5257 OG SER D 157 7009 3953 5261 -101 -271 185 O ANISOU 5258 N LEU D 158 7222 4295 5672 0 -253 187 N ANISOU 5259 CA LEU D 158 7243 4348 5728 7 -262 200 C ANISOU 5260 C LEU D 158 7328 4465 5854 43 -261 214 C ANISOU 5261 O LEU D 158 7269 4403 5807 57 -247 200 O ANISOU 5262 CB LEU D 158 7418 4518 5899 -11 -255 180 C ANISOU 5263 CG LEU D 158 7619 4693 6053 -35 -252 167 C ANISOU 5264 CD1 LEU D 158 7942 4990 6344 -39 -251 152 C ANISOU 5265 CD2 LEU D 158 7734 4795 6146 -54 -271 185 C ANISOU 5266 N ILE D 159 7288 4470 5832 57 -276 246 N ANISOU 5267 CA ILE D 159 7504 4735 6086 96 -274 265 C ANISOU 5268 C ILE D 159 7736 5052 6352 84 -293 303 C ANISOU 5269 O ILE D 159 7988 5318 6590 51 -309 319 O ANISOU 5270 CB ILE D 159 7634 4842 6179 149 -273 277 C ANISOU 5271 CG1 ILE D 159 7650 4900 6221 203 -268 293 C ANISOU 5272 CG2 ILE D 159 7606 4827 6117 160 -288 304 C ANISOU 5273 CD1 ILE D 159 7931 5128 6433 267 -268 303 C ANISOU 5274 N ASN D 160 8031 5408 6691 104 -292 319 N ANISOU 5275 CA ASN D 160 8271 5752 6964 87 -312 365 C ANISOU 5276 C ASN D 160 8499 6072 7207 154 -310 405 C ANISOU 5277 O ASN D 160 9119 6685 7832 211 -294 397 O ANISOU 5278 CB ASN D 160 8562 6055 7283 60 -316 362 C ANISOU 5279 CG ASN D 160 8652 6255 7395 22 -345 417 C ANISOU 5280 OD1 ASN D 160 9032 6719 7777 13 -361 460 O ANISOU 5281 ND2 ASN D 160 9014 6622 7769 -6 -353 420 N ANISOU 5282 N GLU D 161 8626 6282 7329 154 -326 448 N ANISOU 5283 CA GLU D 161 8791 6545 7493 234 -323 491 C ANISOU 5284 C GLU D 161 8674 6547 7427 270 -320 524 C ANISOU 5285 O GLU D 161 7949 5814 6684 355 -302 522 O ANISOU 5286 CB GLU D 161 9088 6941 7786 216 -344 538 C ANISOU 5287 CG GLU D 161 9396 7369 8082 312 -339 589 C ANISOU 5288 CD GLU D 161 9734 7823 8418 298 -359 639 C ANISOU 5289 OE1 GLU D 161 9732 7794 8420 204 -378 633 O ANISOU 5290 OE2 GLU D 161 9616 7822 8285 387 -354 687 O ANISOU 5291 N GLU D 162 8783 6752 7585 201 -339 554 N ANISOU 5292 CA GLU D 162 8970 7076 7825 219 -341 594 C ANISOU 5293 C GLU D 162 8638 6662 7500 263 -317 552 C ANISOU 5294 O GLU D 162 8260 6350 7129 346 -303 572 O ANISOU 5295 CB GLU D 162 9225 7406 8106 111 -375 629 C ANISOU 5296 CG GLU D 162 9684 7974 8558 61 -404 684 C ANISOU 5297 CD GLU D 162 10071 8571 8975 139 -400 753 C ANISOU 5298 OE1 GLU D 162 10190 8855 9141 157 -403 803 O ANISOU 5299 OE2 GLU D 162 10094 8594 8968 191 -392 757 O ANISOU 5300 N SER D 163 8606 6493 7459 211 -314 498 N ANISOU 5301 CA SER D 163 8318 6134 7180 243 -292 460 C ANISOU 5302 C SER D 163 8255 5959 7067 308 -270 422 C ANISOU 5303 O SER D 163 7792 5455 6602 350 -254 403 O ANISOU 5304 CB SER D 163 8452 6178 7314 173 -296 421 C ANISOU 5305 OG SER D 163 8416 6027 7232 142 -295 383 O ANISOU 5306 N ASN D 164 8672 6317 7435 307 -273 413 N ANISOU 5307 CA ASN D 164 8926 6447 7618 352 -260 382 C ANISOU 5308 C ASN D 164 8749 6164 7438 316 -248 331 C ANISOU 5309 O ASN D 164 9162 6504 7813 352 -238 313 O ANISOU 5310 CB ASN D 164 9259 6799 7910 452 -253 407 C ANISOU 5311 CG ASN D 164 9947 7327 8487 494 -249 380 C ANISOU 5312 OD1 ASN D 164 10275 7549 8778 442 -252 347 O ANISOU 5313 ND2 ASN D 164 10167 7525 8638 589 -245 397 N ANISOU 5314 N VAL D 165 8769 6178 7489 248 -251 312 N ANISOU 5315 CA VAL D 165 8536 5875 7256 220 -238 270 C ANISOU 5316 C VAL D 165 8465 5741 7148 177 -238 245 C ANISOU 5317 O VAL D 165 8056 5348 6736 144 -251 254 O ANISOU 5318 CB VAL D 165 8805 6184 7575 196 -238 268 C ANISOU 5319 CG1 VAL D 165 8915 6234 7679 178 -223 226 C ANISOU 5320 CG2 VAL D 165 8768 6220 7578 236 -237 294 C ANISOU 5321 N VAL D 166 8265 5478 6916 173 -227 218 N ANISOU 5322 CA VAL D 166 8100 5273 6716 134 -225 198 C ANISOU 5323 C VAL D 166 8033 5223 6672 110 -215 177 C ANISOU 5324 O VAL D 166 7763 4971 6433 123 -206 168 O ANISOU 5325 CB VAL D 166 8134 5250 6698 129 -221 186 C ANISOU 5326 CG1 VAL D 166 8231 5333 6764 83 -218 171 C ANISOU 5327 CG2 VAL D 166 8246 5304 6748 161 -234 204 C ANISOU 5328 N LEU D 167 7959 5134 6571 81 -218 169 N ANISOU 5329 CA LEU D 167 7988 5156 6589 71 -212 150 C ANISOU 5330 C LEU D 167 7868 5053 6474 87 -188 128 C ANISOU 5331 O LEU D 167 7984 5166 6589 102 -182 116 O ANISOU 5332 CB LEU D 167 8125 5265 6679 46 -218 146 C ANISOU 5333 CG LEU D 167 8201 5309 6710 47 -213 127 C ANISOU 5334 CD1 LEU D 167 8186 5256 6678 36 -235 138 C ANISOU 5335 CD2 LEU D 167 8274 5358 6730 30 -214 121 C ANISOU 5336 N ASP D 168 8017 5218 6617 79 -179 126 N ANISOU 5337 CA ASP D 168 8155 5401 6763 87 -159 113 C ANISOU 5338 C ASP D 168 7843 5096 6481 97 -158 118 C ANISOU 5339 O ASP D 168 7454 4743 6090 87 -148 117 O ANISOU 5340 CB ASP D 168 8118 5399 6693 58 -153 113 C ANISOU 5341 CG ASP D 168 8417 5663 6963 22 -170 129 C ANISOU 5342 OD1 ASP D 168 8604 5796 7150 33 -184 138 O ANISOU 5343 OD2 ASP D 168 9112 6388 7625 -14 -170 135 O ANISOU 5344 N SER D 169 8050 5277 6711 116 -169 128 N ANISOU 5345 CA SER D 169 8260 5485 6941 135 -168 134 C ANISOU 5346 C SER D 169 8217 5477 6939 156 -154 122 C ANISOU 5347 O SER D 169 8064 5325 6800 166 -156 119 O ANISOU 5348 CB SER D 169 8308 5508 6990 158 -183 154 C ANISOU 5349 OG SER D 169 8477 5668 7166 186 -181 159 O ANISOU 5350 N ASN D 170 8658 5940 7389 158 -143 117 N ANISOU 5351 CA ASN D 170 9032 6350 7798 182 -128 106 C ANISOU 5352 C ASN D 170 8779 6081 7579 208 -135 114 C ANISOU 5353 O ASN D 170 8577 5853 7368 214 -144 127 O ANISOU 5354 CB ASN D 170 9571 6938 8336 171 -115 103 C ANISOU 5355 CG ASN D 170 10286 7703 9021 146 -107 102 C ANISOU 5356 OD1 ASN D 170 11209 8611 9922 142 -110 100 O ANISOU 5357 ND2 ASN D 170 10282 7772 9016 127 -98 109 N ANISOU 5358 N MSE D 171 8526 5839 7352 226 -131 108 N ANISOU 5359 CA MSE D 171 8590 5907 7451 245 -138 120 C ANISOU 5360 C MSE D 171 8323 5651 7203 263 -129 120 C ANISOU 5361 O MSE D 171 8806 6129 7695 283 -136 136 O ANISOU 5362 CB MSE D 171 8917 6228 7781 250 -139 113 C ANISOU 5363 CG MSE D 171 9300 6572 8114 230 -150 109 C ANISOU 5364 SE MSE D 171 10623 7894 9428 197 -177 140 SE ANISOU 5365 CE MSE D 171 9692 7005 8537 191 -199 175 C ANISOU 5366 N LEU D 172 8044 5391 6922 259 -114 104 N ANISOU 5367 CA LEU D 172 7775 5131 6663 265 -107 104 C ANISOU 5368 C LEU D 172 7697 5001 6538 253 -121 118 C ANISOU 5369 O LEU D 172 7596 4873 6426 267 -124 122 O ANISOU 5370 CB LEU D 172 7805 5215 6691 253 -91 93 C ANISOU 5371 CG LEU D 172 7718 5164 6625 283 -75 78 C ANISOU 5372 CD1 LEU D 172 7724 5250 6630 286 -56 74 C ANISOU 5373 CD2 LEU D 172 7717 5143 6658 310 -77 77 C ANISOU 5374 N SER D 173 7706 4979 6503 230 -132 123 N ANISOU 5375 CA SER D 173 7668 4863 6390 220 -149 135 C ANISOU 5376 C SER D 173 7904 5051 6611 271 -157 147 C ANISOU 5377 O SER D 173 8231 5301 6866 277 -167 153 O ANISOU 5378 CB SER D 173 7506 4676 6188 197 -160 140 C ANISOU 5379 OG SER D 173 7315 4536 6002 155 -152 132 O ANISOU 5380 N ASN D 174 8183 5378 6945 307 -153 155 N ANISOU 5381 CA ASN D 174 8660 5846 7414 363 -158 174 C ANISOU 5382 C ASN D 174 8414 5680 7251 385 -148 179 C ANISOU 5383 O ASN D 174 8184 5515 7068 383 -151 192 O ANISOU 5384 CB ASN D 174 9235 6421 7961 389 -169 196 C ANISOU 5385 CG ASN D 174 9912 7001 8539 374 -182 195 C ANISOU 5386 OD1 ASN D 174 10364 7383 8935 337 -186 181 O ANISOU 5387 ND2 ASN D 174 10390 7479 8988 400 -191 214 N ANISOU 5388 N ILE D 175 8120 5378 6967 398 -140 170 N ANISOU 5389 CA ILE D 175 7561 4886 6478 419 -133 175 C ANISOU 5390 C ILE D 175 7433 4760 6329 482 -136 199 C ANISOU 5391 O ILE D 175 7744 4991 6570 508 -137 196 O ANISOU 5392 CB ILE D 175 7585 4911 6528 401 -120 152 C ANISOU 5393 CG1 ILE D 175 7620 4960 6573 357 -114 132 C ANISOU 5394 CG2 ILE D 175 7499 4881 6503 425 -114 158 C ANISOU 5395 CD1 ILE D 175 7640 5014 6622 346 -117 133 C ANISOU 5396 N VAL D 176 6971 4388 5914 504 -139 227 N ANISOU 5397 CA VAL D 176 7008 4462 5934 575 -139 258 C ANISOU 5398 C VAL D 176 6955 4491 5948 592 -132 270 C ANISOU 5399 O VAL D 176 6824 4408 5808 658 -130 298 O ANISOU 5400 CB VAL D 176 7122 4650 6045 595 -149 295 C ANISOU 5401 CG1 VAL D 176 7162 4594 6003 593 -156 284 C ANISOU 5402 CG2 VAL D 176 7032 4664 6034 536 -158 311 C ANISOU 5403 N SER D 177 6773 4324 5824 540 -130 250 N ANISOU 5404 CA SER D 177 6857 4473 5963 549 -126 260 C ANISOU 5405 C SER D 177 6593 4191 5734 493 -125 233 C ANISOU 5406 O SER D 177 6363 3938 5497 448 -131 221 O ANISOU 5407 CB SER D 177 7247 4994 6392 564 -136 310 C ANISOU 5408 OG SER D 177 7789 5602 6984 564 -135 322 O ANISOU 5409 N TRP D 178 6330 3933 5499 506 -116 224 N ANISOU 5410 CA TRP D 178 6232 3819 5424 469 -114 201 C ANISOU 5411 C TRP D 178 5996 3640 5229 484 -115 219 C ANISOU 5412 O TRP D 178 5686 3372 4929 530 -110 239 O ANISOU 5413 CB TRP D 178 6385 3905 5557 466 -98 162 C ANISOU 5414 CG TRP D 178 6757 4262 5929 500 -87 157 C ANISOU 5415 CD1 TRP D 178 6896 4369 6027 534 -87 166 C ANISOU 5416 CD2 TRP D 178 6700 4214 5903 506 -77 144 C ANISOU 5417 NE1 TRP D 178 7161 4612 6289 555 -79 158 N ANISOU 5418 CE2 TRP D 178 6963 4451 6145 538 -72 145 C ANISOU 5419 CE3 TRP D 178 6920 4446 6149 491 -74 131 C ANISOU 5420 CZ2 TRP D 178 7007 4496 6210 550 -62 135 C ANISOU 5421 CZ3 TRP D 178 7038 4568 6288 508 -63 121 C ANISOU 5422 CH2 TRP D 178 6990 4510 6236 534 -57 123 C ANISOU 5423 N GLY D 179 5782 3419 5025 449 -122 211 N ANISOU 5424 CA GLY D 179 5533 3221 4811 453 -127 229 C ANISOU 5425 C GLY D 179 5453 3080 4713 424 -130 205 C ANISOU 5426 O GLY D 179 5357 2912 4574 405 -131 179 O ANISOU 5427 N ILE D 180 5380 3036 4666 429 -132 214 N ANISOU 5428 CA ILE D 180 5482 3073 4739 410 -137 194 C ANISOU 5429 C ILE D 180 5598 3240 4863 375 -163 233 C ANISOU 5430 O ILE D 180 5518 3267 4838 392 -162 267 O ANISOU 5431 CB ILE D 180 5423 2987 4698 454 -109 158 C ANISOU 5432 CG1 ILE D 180 5586 3075 4816 448 -111 133 C ANISOU 5433 CG2 ILE D 180 5364 2996 4695 488 -98 174 C ANISOU 5434 CD1 ILE D 180 5593 3076 4841 491 -83 102 C ANISOU 5435 N THR D 181 5761 3325 4958 326 -189 232 N ANISOU 5436 CA THR D 181 6050 3650 5235 274 -222 274 C ANISOU 5437 C THR D 181 6340 3849 5484 277 -224 249 C ANISOU 5438 O THR D 181 6187 3568 5259 294 -217 207 O ANISOU 5439 CB THR D 181 6061 3638 5175 193 -266 308 C ANISOU 5440 OG1 THR D 181 6110 3792 5273 198 -261 335 O ANISOU 5441 CG2 THR D 181 6115 3732 5203 119 -308 360 C ANISOU 5442 N PHE D 182 6626 4213 5814 269 -231 278 N ANISOU 5443 CA PHE D 182 7075 4588 6227 269 -235 261 C ANISOU 5444 C PHE D 182 7066 4569 6153 181 -286 309 C ANISOU 5445 O PHE D 182 6764 4415 5909 145 -302 365 O ANISOU 5446 CB PHE D 182 7314 4915 6563 330 -201 254 C ANISOU 5447 CG PHE D 182 7878 5418 7100 333 -205 240 C ANISOU 5448 CD1 PHE D 182 8241 5635 7381 352 -200 195 C ANISOU 5449 CD2 PHE D 182 8148 5784 7422 322 -212 275 C ANISOU 5450 CE1 PHE D 182 8298 5631 7404 361 -204 182 C ANISOU 5451 CE2 PHE D 182 8193 5768 7440 322 -217 262 C ANISOU 5452 CZ PHE D 182 8273 5691 7433 341 -213 215 C ANISOU 5453 N ILE D 183 7351 4674 6300 145 -315 289 N ANISOU 5454 CA ILE D 183 7335 4596 6179 47 -372 330 C ANISOU 5455 C ILE D 183 7146 4308 5940 66 -373 307 C ANISOU 5456 O ILE D 183 7265 4249 5952 107 -367 258 O ANISOU 5457 CB ILE D 183 7768 4867 6456 -13 -414 330 C ANISOU 5458 CG1 ILE D 183 8031 5245 6782 -30 -411 355 C ANISOU 5459 CG2 ILE D 183 7863 4858 6405 -126 -483 374 C ANISOU 5460 CD1 ILE D 183 8499 5564 7100 -94 -452 359 C ANISOU 5461 N PRO D 184 6878 4161 5746 47 -378 343 N ANISOU 5462 CA PRO D 184 6827 4028 5657 65 -378 323 C ANISOU 5463 C PRO D 184 6878 3856 5504 -4 -434 324 C ANISOU 5464 O PRO D 184 6838 3744 5353 -93 -484 357 O ANISOU 5465 CB PRO D 184 6778 4181 5729 43 -379 376 C ANISOU 5466 CG PRO D 184 6838 4442 5913 56 -360 410 C ANISOU 5467 CD PRO D 184 6864 4381 5855 15 -382 407 C ANISOU 5468 N SER D 185 6996 3854 5562 36 -427 290 N ANISOU 5469 CA SER D 185 7230 3844 5577 -13 -479 286 C ANISOU 5470 C SER D 185 7261 3920 5572 -143 -541 358 C ANISOU 5471 O SER D 185 6818 3715 5278 -184 -539 411 O ANISOU 5472 CB SER D 185 7262 3761 5564 78 -450 232 C ANISOU 5473 OG SER D 185 7198 3851 5642 92 -429 246 O ANISOU 5474 N ASP D 186 7615 4043 5711 -205 -597 362 N ANISOU 5475 CA ASP D 186 7876 4331 5912 -344 -664 434 C ANISOU 5476 C ASP D 186 7578 4203 5762 -320 -639 449 C ANISOU 5477 O ASP D 186 7657 4401 5859 -424 -681 519 O ANISOU 5478 CB ASP D 186 8484 4608 6216 -426 -740 436 C ANISOU 5479 CG ASP D 186 8931 4871 6486 -471 -778 433 C ANISOU 5480 OD1 ASP D 186 8991 5076 6674 -440 -744 430 O ANISOU 5481 OD2 ASP D 186 9641 5286 6919 -541 -846 436 O ANISOU 5482 N GLU D 187 7340 3984 5625 -185 -571 387 N ANISOU 5483 CA GLU D 187 7489 4280 5909 -152 -544 395 C ANISOU 5484 C GLU D 187 7414 4520 6041 -174 -527 453 C ANISOU 5485 O GLU D 187 7100 4319 5807 -159 -508 461 O ANISOU 5486 CB GLU D 187 7388 4145 5873 -9 -477 321 C ANISOU 5487 CG GLU D 187 7572 4041 5853 36 -488 266 C ANISOU 5488 CD GLU D 187 7468 3936 5815 174 -423 203 C ANISOU 5489 OE1 GLU D 187 7110 3786 5658 224 -374 200 O ANISOU 5490 OE2 GLU D 187 7878 4138 6064 234 -424 158 O ANISOU 5491 N GLU D 188 7611 4855 6314 -200 -532 492 N ANISOU 5492 CA GLU D 188 7790 5339 6669 -211 -518 555 C ANISOU 5493 C GLU D 188 7487 5174 6539 -79 -442 516 C ANISOU 5494 O GLU D 188 7308 5159 6448 -70 -429 546 O ANISOU 5495 CB GLU D 188 8326 5974 7230 -259 -539 602 C ANISOU 5496 CG GLU D 188 8798 6777 7870 -263 -525 675 C ANISOU 5497 CD GLU D 188 9191 7289 8287 -313 -547 728 C ANISOU 5498 OE1 GLU D 188 9420 7327 8399 -353 -576 707 O ANISOU 5499 OE2 GLU D 188 9948 8330 9173 -308 -535 793 O ANISOU 5500 N HIS D 189 7258 4872 6345 19 -396 453 N ANISOU 5501 CA HIS D 189 7067 4790 6294 133 -332 419 C ANISOU 5502 C HIS D 189 6928 4487 6112 203 -301 344 C ANISOU 5503 O HIS D 189 6808 4221 5925 234 -295 300 O ANISOU 5504 CB HIS D 189 7111 4930 6433 187 -303 417 C ANISOU 5505 CG HIS D 189 7384 5303 6827 293 -245 390 C ANISOU 5506 ND1 HIS D 189 7189 5279 6714 317 -231 427 N ANISOU 5507 CD2 HIS D 189 7376 5246 6857 377 -203 337 C ANISOU 5508 CE1 HIS D 189 7409 5521 7002 412 -184 392 C ANISOU 5509 NE2 HIS D 189 7676 5661 7246 442 -168 339 N ANISOU 5510 N ASN D 190 6505 4104 5728 232 -280 334 N ANISOU 5511 CA ASN D 190 6505 3983 5695 294 -251 272 C ANISOU 5512 C ASN D 190 6313 3899 5627 379 -198 249 C ANISOU 5513 O ASN D 190 6223 3959 5626 389 -189 283 O ANISOU 5514 CB ASN D 190 6619 4012 5721 254 -274 272 C ANISOU 5515 CG ASN D 190 6706 3942 5644 168 -332 289 C ANISOU 5516 OD1 ASN D 190 7053 4097 5860 186 -339 248 O ANISOU 5517 ND2 ASN D 190 6795 4107 5726 78 -375 351 N ANISOU 5518 N ILE D 191 6143 3646 5445 441 -167 195 N ANISOU 5519 CA ILE D 191 6287 3862 5678 508 -124 173 C ANISOU 5520 C ILE D 191 6249 3748 5602 540 -105 131 C ANISOU 5521 O ILE D 191 6248 3641 5522 551 -107 102 O ANISOU 5522 CB ILE D 191 6475 4075 5915 549 -103 160 C ANISOU 5523 CG1 ILE D 191 6671 4348 6142 518 -123 202 C ANISOU 5524 CG2 ILE D 191 6501 4157 6011 605 -66 141 C ANISOU 5525 CD1 ILE D 191 6757 4456 6273 558 -103 191 C ANISOU 5526 N VAL D 192 6013 3572 5417 560 -85 129 N ANISOU 5527 CA VAL D 192 5864 3382 5243 584 -67 97 C ANISOU 5528 C VAL D 192 5883 3469 5329 619 -39 90 C ANISOU 5529 O VAL D 192 5576 3225 5070 625 -38 113 O ANISOU 5530 CB VAL D 192 5993 3479 5324 551 -84 104 C ANISOU 5531 CG1 VAL D 192 5939 3319 5166 513 -116 107 C ANISOU 5532 CG2 VAL D 192 5865 3439 5246 530 -93 141 C ANISOU 5533 N ILE D 193 5980 3549 5414 642 -19 62 N ANISOU 5534 CA ILE D 193 6050 3660 5520 659 0 57 C ANISOU 5535 C ILE D 193 6078 3681 5520 648 3 49 C ANISOU 5536 O ILE D 193 5642 3232 5052 656 11 31 O ANISOU 5537 CB ILE D 193 6075 3699 5559 683 17 40 C ANISOU 5538 CG1 ILE D 193 6083 3709 5591 694 14 45 C ANISOU 5539 CG2 ILE D 193 5895 3547 5394 683 28 41 C ANISOU 5540 CD1 ILE D 193 6113 3772 5659 695 9 69 C ANISOU 5541 N ILE D 194 6338 3952 5787 637 -1 64 N ANISOU 5542 CA ILE D 194 6594 4200 6017 623 0 59 C ANISOU 5543 C ILE D 194 6779 4394 6200 624 9 57 C ANISOU 5544 O ILE D 194 6420 4019 5835 630 4 70 O ANISOU 5545 CB ILE D 194 7001 4602 6415 609 -15 79 C ANISOU 5546 CG1 ILE D 194 7176 4769 6581 591 -33 91 C ANISOU 5547 CG2 ILE D 194 7139 4725 6522 593 -13 73 C ANISOU 5548 CD1 ILE D 194 7321 4933 6721 571 -50 118 C ANISOU 5549 N LYS D 195 7002 4642 6415 619 21 43 N ANISOU 5550 CA LYS D 195 7427 5080 6827 601 23 48 C ANISOU 5551 C LYS D 195 7311 4944 6668 569 15 55 C ANISOU 5552 O LYS D 195 7208 4800 6526 550 4 65 O ANISOU 5553 CB LYS D 195 7769 5488 7178 601 38 41 C ANISOU 5554 CG LYS D 195 8520 6256 7961 630 47 34 C ANISOU 5555 CD LYS D 195 9033 6855 8481 634 61 34 C ANISOU 5556 CE LYS D 195 9523 7359 8999 664 70 28 C ANISOU 5557 NZ LYS D 195 9809 7748 9291 674 85 32 N ANISOU 5558 N LYS D 196 6912 4557 6262 564 16 50 N ANISOU 5559 CA LYS D 196 6718 4351 6028 531 8 57 C ANISOU 5560 C LYS D 196 6559 4196 5863 533 9 51 C ANISOU 5561 O LYS D 196 6081 3747 5393 554 19 40 O ANISOU 5562 CB LYS D 196 6882 4574 6177 498 12 63 C ANISOU 5563 CG LYS D 196 7184 4875 6428 449 0 76 C ANISOU 5564 CD LYS D 196 7482 5262 6715 406 2 91 C ANISOU 5565 CE LYS D 196 7799 5586 6974 341 -14 110 C ANISOU 5566 NZ LYS D 196 7977 5881 7143 290 -16 135 N ANISOU 5567 N ILE D 197 6389 3986 5665 515 -2 59 N ANISOU 5568 CA ILE D 197 6531 4124 5792 508 -5 56 C ANISOU 5569 C ILE D 197 6690 4282 5911 471 -11 64 C ANISOU 5570 O ILE D 197 6420 3957 5607 457 -25 75 O ANISOU 5571 CB ILE D 197 6540 4093 5807 519 -17 64 C ANISOU 5572 CG1 ILE D 197 6499 4056 5796 541 -17 62 C ANISOU 5573 CG2 ILE D 197 6571 4113 5813 503 -23 63 C ANISOU 5574 CD1 ILE D 197 6526 4073 5830 538 -34 81 C ANISOU 5575 N SER D 198 6794 4445 6006 458 -1 61 N ANISOU 5576 CA SER D 198 7285 4952 6458 412 -9 73 C ANISOU 5577 C SER D 198 7353 5051 6514 411 -3 69 C ANISOU 5578 O SER D 198 7466 5182 6637 449 8 56 O ANISOU 5579 CB SER D 198 7422 5165 6590 381 -6 85 C ANISOU 5580 OG SER D 198 7648 5496 6850 414 16 80 O ANISOU 5581 N LEU D 199 7322 5006 6443 367 -16 81 N ANISOU 5582 CA LEU D 199 7311 5027 6414 359 -12 80 C ANISOU 5583 C LEU D 199 7211 5047 6305 327 -5 97 C ANISOU 5584 O LEU D 199 6679 4524 5748 274 -19 116 O ANISOU 5585 CB LEU D 199 7609 5239 6670 328 -33 87 C ANISOU 5586 CG LEU D 199 7808 5350 6878 358 -42 81 C ANISOU 5587 CD1 LEU D 199 7782 5263 6809 338 -59 89 C ANISOU 5588 CD2 LEU D 199 8028 5583 7134 398 -32 68 C ANISOU 5589 N LEU D 200 7319 5247 6420 363 16 93 N ANISOU 5590 CA LEU D 200 7634 5718 6733 343 27 116 C ANISOU 5591 C LEU D 200 8284 6411 7351 319 25 127 C ANISOU 5592 O LEU D 200 8216 6258 7265 340 23 109 O ANISOU 5593 CB LEU D 200 7613 5793 6732 418 56 109 C ANISOU 5594 CG LEU D 200 7551 5700 6703 446 59 98 C ANISOU 5595 CD1 LEU D 200 7704 5977 6862 514 87 99 C ANISOU 5596 CD2 LEU D 200 7667 5805 6830 378 39 116 C ANISOU 5597 N SER D 201 9047 7316 8104 268 24 161 N ANISOU 5598 CA SER D 201 9656 8002 8685 237 23 179 C ANISOU 5599 C SER D 201 10024 8583 9066 282 53 200 C ANISOU 5600 O SER D 201 10118 8820 9180 258 56 230 O ANISOU 5601 CB SER D 201 9824 8153 8811 128 -9 210 C ANISOU 5602 OG SER D 201 10119 8529 9079 93 -11 230 O ANISOU 5603 N GLU D 202 10370 8952 9393 352 75 186 N ANISOU 5604 CA GLU D 202 10662 9441 9680 422 107 204 C ANISOU 5605 C GLU D 202 10246 9088 9226 426 114 215 C ANISOU 5606 O GLU D 202 10348 9377 9314 489 142 237 O ANISOU 5607 CB GLU D 202 10917 9632 9920 541 132 169 C ANISOU 5608 CG GLU D 202 11065 9726 10107 538 126 159 C ANISOU 5609 CD GLU D 202 11328 9907 10343 647 145 125 C ANISOU 5610 OE1 GLU D 202 11272 9815 10219 729 161 108 O ANISOU 5611 OE2 GLU D 202 11552 10091 10599 647 142 117 O TER 5612 GLU D 202 HETATM 5613 CL CL A 401 -58.666 -9.256 15.787 1.00 50.06 CL HETATM 5614 CL CL A 402 -47.647 -29.867 26.550 1.00 54.95 CL HETATM 5615 CL CL A 403 -43.757 -35.568 27.670 1.00 59.46 CL HETATM 5616 CL CL A 404 -55.497 -2.076 22.888 1.00 59.13 CL HETATM 5617 C1 EDO A 405 13.927 -39.934 29.733 1.00 52.07 C HETATM 5618 O1 EDO A 405 15.045 -39.121 30.038 1.00 48.15 O HETATM 5619 C2 EDO A 405 13.253 -40.489 30.936 1.00 53.45 C HETATM 5620 O2 EDO A 405 12.112 -41.268 30.627 1.00 57.83 O HETATM 5641 O HOH A 501 -50.895 -16.805 10.588 1.00 33.71 O HETATM 5642 O HOH A 502 -40.651 -14.534 16.632 1.00 37.51 O HETATM 5643 O HOH A 503 -61.399 -18.058 20.878 1.00 40.75 O HETATM 5644 O HOH A 504 -61.548 -8.979 16.968 1.00 37.05 O HETATM 5645 O HOH A 505 -57.542 -9.487 36.425 1.00 46.96 O HETATM 5646 O HOH A 506 -43.563 -17.179 30.760 1.00 39.40 O HETATM 5647 O HOH A 507 -55.642 -5.907 37.596 1.00 48.72 O HETATM 5648 O HOH A 508 -30.788 -19.555 15.502 1.00 47.15 O HETATM 5649 O HOH A 509 -56.754 -26.981 37.168 1.00 59.39 O HETATM 5650 O HOH A 510 -54.050 -17.811 9.527 1.00 43.04 O HETATM 5651 O HOH A 511 -40.564 -16.368 10.227 1.00 53.08 O HETATM 5652 O HOH A 512 -41.416 -9.718 31.651 1.00 61.79 O HETATM 5653 O HOH A 513 -63.028 -21.984 22.456 1.00 48.96 O HETATM 5654 O HOH A 514 -59.062 -18.197 16.628 1.00 39.82 O HETATM 5655 O AHOH A 515 -47.174 -33.442 31.460 0.50 36.61 O HETATM 5656 O BHOH A 515 -46.531 -35.726 30.450 0.50 38.00 O HETATM 5657 O HOH A 516 -49.981 -5.457 8.169 1.00 38.30 O HETATM 5658 O HOH A 517 -50.297 -27.354 34.291 1.00 44.74 O HETATM 5659 O HOH A 518 -52.127 -32.264 22.071 1.00 58.75 O HETATM 5660 O HOH A 519 -61.446 -27.635 25.860 1.00 47.49 O HETATM 5661 O AHOH A 520 -65.315 -21.191 22.554 0.50 35.78 O HETATM 5662 O BHOH A 520 -66.643 -22.113 23.075 0.50 29.87 O HETATM 5663 O HOH A 521 -49.297 -6.597 19.587 1.00 40.12 O HETATM 5664 O HOH A 522 -61.884 -17.635 41.109 1.00 36.58 O HETATM 5665 O HOH A 523 13.843 -38.411 22.832 1.00 31.15 O HETATM 5666 O HOH A 524 -65.293 -2.674 20.332 1.00 44.62 O HETATM 5667 O HOH A 525 -21.224 -16.023 18.757 1.00 42.98 O HETATM 5668 O HOH A 526 -29.160 -11.834 22.558 1.00 58.50 O HETATM 5669 O HOH A 527 3.025 -36.870 28.812 1.00 33.31 O HETATM 5670 O HOH A 528 -31.731 -20.807 32.766 1.00 48.22 O HETATM 5671 O HOH A 529 -43.367 -7.756 32.118 1.00 44.63 O HETATM 5672 O HOH A 530 7.441 -39.978 29.666 1.00 44.32 O HETATM 5673 O HOH A 531 -57.988 -7.657 12.710 1.00 41.74 O HETATM 5674 O HOH A 532 14.662 -33.825 26.403 1.00 46.40 O HETATM 5675 O HOH A 533 -31.780 -26.254 19.767 1.00 36.27 O HETATM 5676 O HOH A 534 -53.376 -27.188 22.235 1.00 58.01 O HETATM 5677 O HOH A 535 -40.709 -14.326 28.113 1.00 34.16 O HETATM 5678 O HOH A 536 -36.108 -13.990 14.959 1.00 55.47 O HETATM 5679 O HOH A 537 -56.660 -10.849 43.029 1.00 45.78 O HETATM 5680 O HOH A 538 -10.006 -22.239 26.618 1.00 29.39 O HETATM 5681 O HOH A 539 -23.080 -14.551 30.817 1.00 64.23 O HETATM 5682 O HOH A 540 -30.864 -24.805 14.165 1.00 42.55 O HETATM 5683 O HOH A 541 -46.406 -4.615 11.264 1.00 44.49 O HETATM 5684 O HOH A 542 -3.873 -23.315 12.398 1.00 39.01 O HETATM 5685 O HOH A 543 -39.565 -0.796 16.571 1.00 43.98 O HETATM 5686 O HOH A 544 -38.540 -4.092 21.833 1.00 47.78 O HETATM 5687 O HOH A 545 -35.511 -25.860 10.474 1.00 60.96 O HETATM 5688 O HOH A 546 -64.716 -23.136 36.509 1.00 48.94 O HETATM 5689 O HOH A 547 -52.779 -25.607 41.005 1.00 39.47 O HETATM 5690 O HOH A 548 -27.614 -19.133 19.907 1.00 33.31 O HETATM 5691 O HOH A 549 -47.166 -31.965 24.877 1.00 44.19 O HETATM 5692 O HOH A 550 5.499 -39.259 35.259 1.00 46.90 O HETATM 5693 O AHOH A 551 -44.947 -6.251 22.562 0.50 22.12 O HETATM 5694 O BHOH A 551 -46.091 -7.206 21.391 0.50 28.28 O HETATM 5695 O HOH A 552 -58.371 -7.505 5.683 1.00 42.10 O HETATM 5696 O HOH A 553 12.914 -26.428 26.754 1.00 43.93 O HETATM 5697 O HOH A 554 -63.705 -14.963 37.663 1.00 56.56 O HETATM 5698 O HOH A 555 -41.448 -23.752 31.818 1.00 30.05 O HETATM 5699 O HOH A 556 -33.237 -16.790 30.035 1.00 35.81 O HETATM 5700 O HOH A 557 -60.995 -15.273 45.349 1.00 50.24 O HETATM 5701 O HOH A 558 -49.746 -30.304 34.440 1.00 48.52 O HETATM 5702 O HOH A 559 -58.324 -17.172 19.034 1.00 55.35 O HETATM 5703 O HOH A 560 -49.884 -29.804 9.919 1.00 56.27 O HETATM 5704 O HOH A 561 -41.451 -23.717 35.477 1.00 38.81 O HETATM 5705 O HOH A 562 -42.003 -4.999 14.309 1.00 35.80 O HETATM 5706 O HOH A 563 -48.411 -24.462 29.935 1.00 36.62 O HETATM 5707 O HOH A 564 16.402 -29.804 32.613 1.00 41.11 O HETATM 5708 O HOH A 565 -32.611 -19.356 12.914 1.00 47.63 O HETATM 5709 O HOH A 566 -65.427 -9.869 28.443 1.00 46.52 O HETATM 5710 O HOH A 567 -54.939 -25.060 39.519 1.00 50.81 O HETATM 5711 O HOH A 568 12.705 -28.248 24.486 1.00 44.41 O HETATM 5712 O HOH A 569 -38.115 -28.009 10.745 1.00 45.96 O HETATM 5713 O HOH A 570 -34.796 -29.837 11.838 1.00 60.49 O HETATM 5714 O HOH A 571 -32.344 -23.292 12.916 1.00 51.35 O HETATM 5715 O HOH A 572 -0.750 -21.783 11.558 1.00 49.85 O HETATM 5716 O HOH A 573 -40.768 -36.992 22.027 1.00 49.89 O HETATM 5717 O HOH A 574 -68.432 -16.735 35.386 1.00 56.79 O HETATM 5718 O HOH A 575 -39.106 -8.609 32.460 1.00 46.97 O HETATM 5719 O HOH A 576 -35.497 -3.769 18.344 1.00 53.58 O HETATM 5720 O HOH A 577 -22.868 -30.656 7.104 1.00 49.55 O HETATM 5721 O HOH A 578 -31.024 -17.511 14.113 1.00 41.16 O HETATM 5722 O HOH A 579 -31.733 -10.274 24.434 1.00 54.69 O HETATM 5723 O HOH A 580 -46.390 -7.640 44.726 1.00 57.17 O HETATM 5724 O HOH A 581 -57.034 -7.125 16.452 1.00 38.19 O HETATM 5725 O HOH A 582 -66.365 -13.563 27.668 1.00 51.51 O CONECT 437 441 CONECT 441 437 442 CONECT 442 441 443 445 CONECT 443 442 444 449 CONECT 444 443 CONECT 445 442 446 CONECT 446 445 447 CONECT 447 446 448 CONECT 448 447 CONECT 449 443 CONECT 671 677 CONECT 677 671 678 CONECT 678 677 679 681 CONECT 679 678 680 685 CONECT 680 679 CONECT 681 678 682 CONECT 682 681 683 CONECT 683 682 684 CONECT 684 683 CONECT 685 679 CONECT 907 909 CONECT 909 907 910 CONECT 910 909 911 913 CONECT 911 910 912 CONECT 912 911 915 916 917 CONECT 913 910 914 918 CONECT 914 913 CONECT 915 912 CONECT 916 912 CONECT 917 912 CONECT 918 913 CONECT 1149 1155 CONECT 1155 1149 1156 CONECT 1156 1155 1157 1159 CONECT 1157 1156 1158 1163 CONECT 1158 1157 CONECT 1159 1156 1160 CONECT 1160 1159 1161 CONECT 1161 1160 1162 CONECT 1162 1161 CONECT 1163 1157 CONECT 1841 1845 CONECT 1845 1841 1846 CONECT 1846 1845 1847 1849 CONECT 1847 1846 1848 1853 CONECT 1848 1847 CONECT 1849 1846 1850 CONECT 1850 1849 1851 CONECT 1851 1850 1852 CONECT 1852 1851 CONECT 1853 1847 CONECT 2066 2072 CONECT 2072 2066 2073 CONECT 2073 2072 2074 2076 CONECT 2074 2073 2075 2080 CONECT 2075 2074 CONECT 2076 2073 2077 CONECT 2077 2076 2078 CONECT 2078 2077 2079 CONECT 2079 2078 CONECT 2080 2074 CONECT 2313 2315 CONECT 2315 2313 2316 CONECT 2316 2315 2317 2319 CONECT 2317 2316 2318 CONECT 2318 2317 2321 2322 2323 CONECT 2319 2316 2320 2324 CONECT 2320 2319 CONECT 2321 2318 CONECT 2322 2318 CONECT 2323 2318 CONECT 2324 2319 CONECT 2555 2561 CONECT 2561 2555 2562 CONECT 2562 2561 2563 2565 CONECT 2563 2562 2564 2569 CONECT 2564 2563 CONECT 2565 2562 2566 CONECT 2566 2565 2567 CONECT 2567 2566 2568 CONECT 2568 2567 CONECT 2569 2563 CONECT 3247 3251 CONECT 3251 3247 3252 CONECT 3252 3251 3253 3255 CONECT 3253 3252 3254 3259 CONECT 3254 3253 CONECT 3255 3252 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 CONECT 3259 3253 CONECT 3480 3486 CONECT 3486 3480 3487 CONECT 3487 3486 3488 3490 CONECT 3488 3487 3489 3494 CONECT 3489 3488 CONECT 3490 3487 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 CONECT 3494 3488 CONECT 3716 3718 CONECT 3718 3716 3719 CONECT 3719 3718 3720 3722 CONECT 3720 3719 3721 CONECT 3721 3720 3724 3725 3726 CONECT 3722 3719 3723 3727 CONECT 3723 3722 CONECT 3724 3721 CONECT 3725 3721 CONECT 3726 3721 CONECT 3727 3722 CONECT 3958 3964 CONECT 3964 3958 3965 CONECT 3965 3964 3966 3968 CONECT 3966 3965 3967 3972 CONECT 3967 3966 CONECT 3968 3965 3969 CONECT 3969 3968 3970 CONECT 3970 3969 3971 CONECT 3971 3970 CONECT 3972 3966 CONECT 4641 4645 CONECT 4645 4641 4646 CONECT 4646 4645 4647 4649 CONECT 4647 4646 4648 4653 CONECT 4648 4647 CONECT 4649 4646 4650 CONECT 4650 4649 4651 CONECT 4651 4650 4652 CONECT 4652 4651 CONECT 4653 4647 CONECT 4866 4872 4873 CONECT 4872 4866 4874 CONECT 4873 4866 4875 CONECT 4874 4872 4876 4880 CONECT 4875 4873 4877 4881 CONECT 4876 4874 4878 4888 CONECT 4877 4875 4879 4888 CONECT 4878 4876 CONECT 4879 4877 CONECT 4880 4874 4882 CONECT 4881 4875 4883 CONECT 4882 4880 4884 CONECT 4883 4881 4885 CONECT 4884 4882 4886 CONECT 4885 4883 4887 CONECT 4886 4884 CONECT 4887 4885 CONECT 4888 4876 4877 CONECT 5110 5112 CONECT 5112 5110 5113 CONECT 5113 5112 5114 5116 CONECT 5114 5113 5115 CONECT 5115 5114 5118 5119 5120 CONECT 5116 5113 5117 5121 CONECT 5117 5116 CONECT 5118 5115 CONECT 5119 5115 CONECT 5120 5115 CONECT 5121 5116 CONECT 5352 5358 CONECT 5358 5352 5359 CONECT 5359 5358 5360 5362 CONECT 5360 5359 5361 5366 CONECT 5361 5360 CONECT 5362 5359 5363 CONECT 5363 5362 5364 CONECT 5364 5363 5365 CONECT 5365 5364 CONECT 5366 5360 CONECT 5617 5618 5619 CONECT 5618 5617 CONECT 5619 5617 5620 CONECT 5620 5619 CONECT 5626 5627 5628 CONECT 5627 5626 CONECT 5628 5626 5629 5630 CONECT 5629 5628 CONECT 5630 5628 5631 CONECT 5631 5630 MASTER 527 0 36 4 88 0 0 6 5885 4 182 56 END